Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 24-JAN-11 3QGB TITLE CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD-1 FBEA 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*AP*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 3QGB 1 JRNL REVDAT 1 23-MAR-11 3QGB 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. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21358 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1089 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) : 28.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.73 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.03000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : -1.03000 REMARK 3 B13 (A**2) : 2.05900 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 : 10.653 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 3QGB 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 RCSB063608. 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 : 21358 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 43.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 15.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.17400 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 14.80 REMARK 200 R MERGE FOR SHELL (I) : 0.90300 REMARK 200 R SYM FOR SHELL (I) : 0.90300 REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100 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 (%): 55.07 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 33.63167 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 67.26333 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 50.44750 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 84.07917 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 16.81583 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: 2490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 N3 G B 2 C4 0.072 REMARK 500 G B 2 C5 G B 2 N7 -0.046 REMARK 500 G B 2 C8 G B 2 N9 -0.046 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 ARG A 180 170.39 -58.25 REMARK 500 ARG A 182 38.86 -86.53 REMARK 500 ASP A 312 -155.08 -120.71 REMARK 500 ARG A 441 -2.49 76.01 REMARK 500 ASP A 477 13.30 -153.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 577 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH A 660 DISTANCE = 5.28 ANGSTROMS REMARK 525 HOH A 685 DISTANCE = 5.15 ANGSTROMS 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: 3QGC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD REMARK 900 -1 FBEA A7U MUTANT DBREF 3QGB A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3QGB B 1 9 PDB 3QGB 3QGB 1 9 SEQADV 3QGB GLY A 163 UNP Q09312 EXPRESSION TAG SEQADV 3QGB 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 A U A FORMUL 3 HOH *298(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 VAL A 211 1 12 HELIX 5 5 THR A 216 GLY A 229 1 14 HELIX 6 6 ARG A 230 THR A 239 1 10 HELIX 7 7 PHE A 242 ALA A 256 1 15 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 ASP A 321 1 10 HELIX 13 13 ALA A 324 ILE A 335 1 12 HELIX 14 14 PRO A 336 THR A 349 1 14 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 SER A 447 1 6 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 PHE A 495 1 8 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 CRYST1 96.809 96.809 100.895 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 0.010330 0.005964 0.000000 0.00000 SCALE2 0.000000 0.011928 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009911 0.00000 ATOM 1 N LEU A 168 -6.403 13.902 -21.955 1.00 45.23 N ANISOU 1 N LEU A 168 6459 4935 5793 154 -2758 -2129 N ATOM 2 CA LEU A 168 -7.000 14.885 -22.856 1.00 51.00 C ANISOU 2 CA LEU A 168 7152 5830 6395 119 -2709 -2079 C ATOM 3 C LEU A 168 -8.287 14.374 -23.506 1.00 52.72 C ANISOU 3 C LEU A 168 7364 6096 6570 54 -2830 -2042 C ATOM 4 O LEU A 168 -8.360 13.220 -23.926 1.00 54.69 O ANISOU 4 O LEU A 168 7638 6309 6834 63 -2948 -2135 O ATOM 5 CB LEU A 168 -6.005 15.314 -23.939 1.00 48.54 C ANISOU 5 CB LEU A 168 6824 5648 5972 189 -2642 -2202 C ATOM 6 CG LEU A 168 -4.914 16.301 -23.522 1.00 47.83 C ANISOU 6 CG LEU A 168 6723 5570 5881 242 -2487 -2204 C ATOM 7 CD1 LEU A 168 -4.095 16.755 -24.718 1.00 53.19 C ANISOU 7 CD1 LEU A 168 7382 6392 6434 304 -2423 -2317 C ATOM 8 CD2 LEU A 168 -5.526 17.493 -22.821 1.00 44.49 C ANISOU 8 CD2 LEU A 168 6280 5163 5461 187 -2386 -2036 C ATOM 9 N PRO A 169 -9.306 15.245 -23.588 1.00 45.26 N ANISOU 9 N PRO A 169 6383 5240 5573 -11 -2800 -1903 N ATOM 10 CA PRO A 169 -10.587 14.950 -24.233 1.00 45.51 C ANISOU 10 CA PRO A 169 6393 5339 5562 -66 -2887 -1831 C ATOM 11 C PRO A 169 -10.385 14.617 -25.702 1.00 43.71 C ANISOU 11 C PRO A 169 6155 5240 5214 -32 -2936 -1953 C ATOM 12 O PRO A 169 -9.623 15.292 -26.391 1.00 43.49 O ANISOU 12 O PRO A 169 6105 5316 5103 30 -2833 -1998 O ATOM 13 CB PRO A 169 -11.354 16.270 -24.107 1.00 42.14 C ANISOU 13 CB PRO A 169 5908 4994 5110 -85 -2750 -1620 C ATOM 14 CG PRO A 169 -10.720 16.972 -22.980 1.00 45.61 C ANISOU 14 CG PRO A 169 6355 5350 5624 -68 -2629 -1565 C ATOM 15 CD PRO A 169 -9.275 16.608 -23.040 1.00 45.80 C ANISOU 15 CD PRO A 169 6415 5338 5648 -2 -2626 -1750 C ATOM 16 N THR A 170 -11.075 13.592 -26.180 1.00 48.83 N ANISOU 16 N THR A 170 6819 5881 5851 -74 -3088 -2003 N ATOM 17 CA THR A 170 -10.909 13.150 -27.558 1.00 56.82 C ANISOU 17 CA THR A 170 7829 7007 6755 -48 -3147 -2126 C ATOM 18 C THR A 170 -11.311 14.218 -28.591 1.00 57.19 C ANISOU 18 C THR A 170 7813 7239 6676 -34 -3047 -2032 C ATOM 19 O THR A 170 -10.768 14.250 -29.694 1.00 60.99 O ANISOU 19 O THR A 170 8288 7830 7057 12 -3034 -2137 O ATOM 20 CB THR A 170 -11.650 11.817 -27.814 1.00 62.50 C ANISOU 20 CB THR A 170 8576 7665 7506 -87 -3305 -2167 C ATOM 21 OG1 THR A 170 -11.386 11.366 -29.148 1.00 60.74 O ANISOU 21 OG1 THR A 170 8355 7547 7179 -59 -3358 -2298 O ATOM 22 CG2 THR A 170 -13.147 11.985 -27.614 1.00 65.56 C ANISOU 22 CG2 THR A 170 8936 8077 7898 -177 -3357 -2004 C ATOM 23 N TRP A 171 -12.239 15.101 -28.235 1.00 49.83 N ANISOU 23 N TRP A 171 6836 6343 5753 -71 -2971 -1833 N ATOM 24 CA TRP A 171 -12.638 16.173 -29.147 1.00 45.22 C ANISOU 24 CA TRP A 171 6192 5931 5058 -55 -2866 -1728 C ATOM 25 C TRP A 171 -11.511 17.162 -29.441 1.00 47.76 C ANISOU 25 C TRP A 171 6497 6327 5322 24 -2707 -1763 C ATOM 26 O TRP A 171 -11.568 17.915 -30.412 1.00 51.29 O ANISOU 26 O TRP A 171 6903 6926 5660 52 -2629 -1727 O ATOM 27 CB TRP A 171 -13.862 16.924 -28.620 1.00 40.24 C ANISOU 27 CB TRP A 171 5516 5313 4458 -110 -2814 -1502 C ATOM 28 CG TRP A 171 -13.647 17.672 -27.327 1.00 43.01 C ANISOU 28 CG TRP A 171 5868 5570 4905 -108 -2698 -1393 C ATOM 29 CD1 TRP A 171 -14.038 17.278 -26.080 1.00 40.03 C ANISOU 29 CD1 TRP A 171 5517 5041 4651 -158 -2744 -1335 C ATOM 30 CD2 TRP A 171 -13.016 18.952 -27.162 1.00 45.07 C ANISOU 30 CD2 TRP A 171 6102 5882 5142 -57 -2514 -1326 C ATOM 31 NE1 TRP A 171 -13.686 18.225 -25.152 1.00 40.60 N ANISOU 31 NE1 TRP A 171 5581 5068 4779 -143 -2602 -1237 N ATOM 32 CE2 TRP A 171 -13.054 19.261 -25.788 1.00 42.47 C ANISOU 32 CE2 TRP A 171 5785 5426 4926 -80 -2459 -1230 C ATOM 33 CE3 TRP A 171 -12.415 19.862 -28.040 1.00 45.51 C ANISOU 33 CE3 TRP A 171 6125 6078 5091 5 -2390 -1340 C ATOM 34 CZ2 TRP A 171 -12.515 20.440 -25.270 1.00 41.12 C ANISOU 34 CZ2 TRP A 171 5596 5264 4764 -45 -2285 -1149 C ATOM 35 CZ3 TRP A 171 -11.878 21.029 -27.524 1.00 41.75 C ANISOU 35 CZ3 TRP A 171 5631 5609 4624 42 -2218 -1259 C ATOM 36 CH2 TRP A 171 -11.935 21.309 -26.153 1.00 36.24 C ANISOU 36 CH2 TRP A 171 4947 4784 4040 16 -2166 -1165 C ATOM 37 N SER A 172 -10.484 17.160 -28.602 1.00 47.75 N ANISOU 37 N SER A 172 6529 6221 5394 60 -2659 -1832 N ATOM 38 CA SER A 172 -9.389 18.104 -28.765 1.00 49.23 C ANISOU 38 CA SER A 172 6703 6468 5535 132 -2505 -1862 C ATOM 39 C SER A 172 -8.169 17.464 -29.419 1.00 57.76 C ANISOU 39 C SER A 172 7817 7558 6573 192 -2544 -2082 C ATOM 40 O SER A 172 -7.194 18.147 -29.719 1.00 57.11 O ANISOU 40 O SER A 172 7723 7535 6440 256 -2427 -2132 O ATOM 41 CB SER A 172 -9.002 18.686 -27.413 1.00 36.11 C ANISOU 41 CB SER A 172 5049 4696 3974 135 -2404 -1783 C ATOM 42 OG SER A 172 -8.386 17.696 -26.618 1.00 34.05 O ANISOU 42 OG SER A 172 4845 4281 3812 133 -2496 -1905 O ATOM 43 N LEU A 173 -8.225 16.153 -29.636 1.00 64.10 N ANISOU 43 N LEU A 173 8659 8299 7396 172 -2708 -2213 N ATOM 44 CA LEU A 173 -7.109 15.429 -30.242 1.00 65.97 C ANISOU 44 CA LEU A 173 8933 8535 7600 226 -2758 -2428 C ATOM 45 C LEU A 173 -7.318 15.233 -31.737 1.00 70.99 C ANISOU 45 C LEU A 173 9552 9315 8106 236 -2802 -2498 C ATOM 46 O LEU A 173 -8.451 15.088 -32.199 1.00 73.43 O ANISOU 46 O LEU A 173 9841 9682 8378 183 -2868 -2415 O ATOM 47 CB LEU A 173 -6.927 14.064 -29.578 1.00 57.97 C ANISOU 47 CB LEU A 173 7976 7357 6694 208 -2901 -2539 C ATOM 48 CG LEU A 173 -6.456 14.050 -28.127 1.00 53.72 C ANISOU 48 CG LEU A 173 7458 6656 6298 220 -2855 -2497 C ATOM 49 CD1 LEU A 173 -6.341 12.619 -27.628 1.00 52.19 C ANISOU 49 CD1 LEU A 173 7306 6302 6220 227 -2973 -2570 C ATOM 50 CD2 LEU A 173 -5.133 14.783 -27.992 1.00 47.88 C ANISOU 50 CD2 LEU A 173 6712 5933 5547 295 -2717 -2554 C ATOM 51 N ASP A 174 -6.225 15.219 -32.494 1.00 68.73 N ANISOU 51 N ASP A 174 9275 9088 7752 302 -2767 -2650 N ATOM 52 CA ASP A 174 -6.318 14.970 -33.930 1.00 74.76 C ANISOU 52 CA ASP A 174 10029 9984 8392 313 -2811 -2734 C ATOM 53 C ASP A 174 -6.218 13.478 -34.267 1.00 82.42 C ANISOU 53 C ASP A 174 11051 10888 9377 298 -2985 -2906 C ATOM 54 O ASP A 174 -6.397 12.619 -33.400 1.00 75.81 O ANISOU 54 O ASP A 174 10242 9897 8663 277 -3063 -2905 O ATOM 55 CB ASP A 174 -5.288 15.798 -34.716 1.00 74.17 C ANISOU 55 CB ASP A 174 9934 10028 8220 389 -2678 -2800 C ATOM 56 CG ASP A 174 -3.851 15.442 -34.372 1.00 80.71 C ANISOU 56 CG ASP A 174 10800 10774 9093 452 -2659 -2969 C ATOM 57 OD1 ASP A 174 -2.942 16.197 -34.782 1.00 83.93 O ANISOU 57 OD1 ASP A 174 11191 11260 9440 514 -2535 -3012 O ATOM 58 OD2 ASP A 174 -3.621 14.416 -33.697 1.00 82.54 O ANISOU 58 OD2 ASP A 174 11069 10860 9433 448 -2752 -3041 O ATOM 59 N SER A 175 -5.935 13.180 -35.532 1.00 95.71 N ANISOU 59 N SER A 175 12736 12676 10954 323 -3017 -3027 N ATOM 60 CA SER A 175 -5.897 11.804 -36.010 1.00103.89 C ANISOU 60 CA SER A 175 13806 13654 12014 324 -3146 -3157 C ATOM 61 C SER A 175 -4.749 11.024 -35.385 1.00104.51 C ANISOU 61 C SER A 175 13918 13583 12209 389 -3148 -3278 C ATOM 62 O SER A 175 -4.936 9.916 -34.880 1.00106.80 O ANISOU 62 O SER A 175 14240 13740 12598 374 -3252 -3309 O ATOM 63 CB SER A 175 -5.770 11.784 -37.531 1.00110.21 C ANISOU 63 CB SER A 175 14599 14609 12667 341 -3161 -3256 C ATOM 64 OG SER A 175 -6.631 12.746 -38.115 1.00114.16 O ANISOU 64 OG SER A 175 15054 15262 13060 305 -3115 -3124 O ATOM 65 N ASN A 176 -3.560 11.613 -35.419 1.00100.23 N ANISOU 65 N ASN A 176 13365 13065 11652 463 -3031 -3341 N ATOM 66 CA ASN A 176 -2.362 10.963 -34.896 1.00 98.03 C ANISOU 66 CA ASN A 176 13108 12664 11476 533 -3024 -3454 C ATOM 67 C ASN A 176 -2.236 11.024 -33.372 1.00 86.79 C ANISOU 67 C ASN A 176 11691 11090 10196 531 -2995 -3367 C ATOM 68 O ASN A 176 -1.195 10.678 -32.818 1.00 77.53 O ANISOU 68 O ASN A 176 10527 9823 9109 592 -2970 -3438 O ATOM 69 CB ASN A 176 -1.100 11.521 -35.568 1.00102.45 C ANISOU 69 CB ASN A 176 13650 13312 11966 615 -2912 -3560 C ATOM 70 CG ASN A 176 -1.187 13.017 -35.835 1.00103.55 C ANISOU 70 CG ASN A 176 13753 13589 12002 611 -2777 -3467 C ATOM 71 OD1 ASN A 176 -2.079 13.482 -36.547 1.00105.80 O ANISOU 71 OD1 ASN A 176 14024 13997 12177 563 -2788 -3403 O ATOM 72 ND2 ASN A 176 -0.247 13.774 -35.278 1.00 99.25 N ANISOU 72 ND2 ASN A 176 13194 13028 11489 664 -2649 -3459 N ATOM 73 N GLY A 177 -3.299 11.466 -32.705 1.00 87.61 N ANISOU 73 N GLY A 177 11788 11175 10324 460 -3000 -3210 N ATOM 74 CA GLY A 177 -3.353 11.451 -31.253 1.00 85.84 C ANISOU 74 CA GLY A 177 11574 10805 10236 446 -2986 -3117 C ATOM 75 C GLY A 177 -2.729 12.658 -30.575 1.00 83.13 C ANISOU 75 C GLY A 177 11208 10472 9906 475 -2833 -3046 C ATOM 76 O GLY A 177 -2.464 12.640 -29.372 1.00 78.73 O ANISOU 76 O GLY A 177 10660 9790 9465 480 -2807 -2993 O ATOM 77 N GLU A 178 -2.492 13.711 -31.347 1.00 81.82 N ANISOU 77 N GLU A 178 11013 10456 9619 494 -2730 -3044 N ATOM 78 CA GLU A 178 -1.933 14.939 -30.800 1.00 79.89 C ANISOU 78 CA GLU A 178 10747 10236 9371 519 -2576 -2976 C ATOM 79 C GLU A 178 -2.991 16.021 -30.613 1.00 76.08 C ANISOU 79 C GLU A 178 10243 9830 8834 451 -2525 -2808 C ATOM 80 O GLU A 178 -3.916 16.146 -31.413 1.00 81.67 O ANISOU 80 O GLU A 178 10929 10642 9459 415 -2558 -2748 O ATOM 81 CB GLU A 178 -0.810 15.461 -31.695 1.00 87.66 C ANISOU 81 CB GLU A 178 11714 11332 10262 595 -2477 -3086 C ATOM 82 CG GLU A 178 0.571 14.970 -31.303 1.00 95.12 C ANISOU 82 CG GLU A 178 12663 12185 11292 674 -2451 -3200 C ATOM 83 CD GLU A 178 1.661 15.531 -32.193 1.00102.36 C ANISOU 83 CD GLU A 178 13557 13216 12118 747 -2348 -3301 C ATOM 84 OE1 GLU A 178 1.774 15.078 -33.352 1.00106.39 O ANISOU 84 OE1 GLU A 178 14070 13807 12547 767 -2398 -3411 O ATOM 85 OE2 GLU A 178 2.410 16.418 -31.732 1.00102.71 O ANISOU 85 OE2 GLU A 178 13582 13270 12174 784 -2216 -3269 O ATOM 86 N MET A 179 -2.847 16.798 -29.546 1.00 69.39 N ANISOU 86 N MET A 179 9391 8927 8050 446 -2426 -2705 N ATOM 87 CA MET A 179 -3.707 17.947 -29.317 1.00 64.59 C ANISOU 87 CA MET A 179 8736 8381 7424 415 -2317 -2495 C ATOM 88 C MET A 179 -3.723 18.823 -30.571 1.00 61.94 C ANISOU 88 C MET A 179 8356 8230 6948 448 -2220 -2471 C ATOM 89 O MET A 179 -2.670 19.139 -31.126 1.00 62.03 O ANISOU 89 O MET A 179 8366 8305 6899 512 -2146 -2578 O ATOM 90 CB MET A 179 -3.200 18.749 -28.112 1.00 61.14 C ANISOU 90 CB MET A 179 8298 7868 7066 426 -2191 -2413 C ATOM 91 CG MET A 179 -4.246 19.652 -27.474 1.00 60.76 C ANISOU 91 CG MET A 179 8216 7824 7046 376 -2112 -2188 C ATOM 92 SD MET A 179 -3.574 20.882 -26.329 1.00 50.28 S ANISOU 92 SD MET A 179 6879 6450 5775 398 -1925 -2086 S ATOM 93 CE MET A 179 -3.015 22.142 -27.477 1.00 60.09 C ANISOU 93 CE MET A 179 8075 7883 6874 464 -1757 -2081 C ATOM 94 N ARG A 180 -4.917 19.197 -31.023 1.00 59.25 N ANISOU 94 N ARG A 180 7980 7976 6557 404 -2224 -2332 N ATOM 95 CA ARG A 180 -5.071 20.030 -32.218 1.00 63.04 C ANISOU 95 CA ARG A 180 8416 8633 6903 429 -2139 -2293 C ATOM 96 C ARG A 180 -4.333 21.359 -32.065 1.00 69.03 C ANISOU 96 C ARG A 180 9149 9450 7631 481 -1945 -2236 C ATOM 97 O ARG A 180 -3.872 21.695 -30.975 1.00 68.02 O ANISOU 97 O ARG A 180 9031 9225 7588 488 -1876 -2201 O ATOM 98 CB ARG A 180 -6.552 20.275 -32.516 1.00 61.56 C ANISOU 98 CB ARG A 180 8193 8513 6684 368 -2169 -2126 C ATOM 99 CG ARG A 180 -7.321 19.034 -32.949 1.00 63.46 C ANISOU 99 CG ARG A 180 8454 8733 6926 318 -2355 -2185 C ATOM 100 CD ARG A 180 -8.818 19.219 -32.747 1.00 69.49 C ANISOU 100 CD ARG A 180 9186 9511 7705 246 -2390 -1999 C ATOM 101 NE ARG A 180 -9.258 20.564 -33.112 1.00 78.89 N ANISOU 101 NE ARG A 180 10320 10831 8824 255 -2246 -1837 N ATOM 102 CZ ARG A 180 -10.456 21.065 -32.820 1.00 83.71 C ANISOU 102 CZ ARG A 180 10893 11461 9450 204 -2228 -1646 C ATOM 103 NH1 ARG A 180 -11.337 20.329 -32.155 1.00 87.63 N ANISOU 103 NH1 ARG A 180 11404 11858 10033 138 -2345 -1594 N ATOM 104 NH2 ARG A 180 -10.774 22.302 -33.189 1.00 80.30 N ANISOU 104 NH2 ARG A 180 10410 11149 8950 218 -2092 -1506 N ATOM 105 N SER A 181 -4.230 22.120 -33.150 1.00 76.05 N ANISOU 105 N SER A 181 10003 10496 8397 515 -1857 -2225 N ATOM 106 CA SER A 181 -3.421 23.338 -33.131 1.00 83.45 C ANISOU 106 CA SER A 181 10917 11495 9293 570 -1675 -2194 C ATOM 107 C SER A 181 -4.229 24.636 -33.143 1.00 82.74 C ANISOU 107 C SER A 181 10778 11497 9163 553 -1544 -1983 C ATOM 108 O SER A 181 -3.853 25.611 -32.492 1.00 83.75 O ANISOU 108 O SER A 181 10893 11612 9315 572 -1400 -1899 O ATOM 109 CB SER A 181 -2.404 23.328 -34.276 1.00 87.85 C ANISOU 109 CB SER A 181 11478 12156 9745 635 -1646 -2359 C ATOM 110 OG SER A 181 -1.277 22.538 -33.941 1.00 84.77 O ANISOU 110 OG SER A 181 11130 11668 9409 670 -1696 -2539 O ATOM 111 N ARG A 182 -5.329 24.651 -33.886 1.00 78.93 N ANISOU 111 N ARG A 182 10266 11106 8616 517 -1594 -1897 N ATOM 112 CA ARG A 182 -6.185 25.830 -33.942 1.00 74.84 C ANISOU 112 CA ARG A 182 9698 10676 8059 500 -1480 -1692 C ATOM 113 C ARG A 182 -7.200 25.813 -32.805 1.00 61.21 C ANISOU 113 C ARG A 182 7968 8845 6442 435 -1508 -1532 C ATOM 114 O ARG A 182 -8.359 26.190 -32.981 1.00 61.16 O ANISOU 114 O ARG A 182 7926 8897 6416 395 -1507 -1377 O ATOM 115 CB ARG A 182 -6.904 25.910 -35.290 1.00 86.69 C ANISOU 115 CB ARG A 182 11168 12333 9439 492 -1515 -1667 C ATOM 116 CG ARG A 182 -6.009 26.305 -36.458 1.00 95.95 C ANISOU 116 CG ARG A 182 12334 13637 10487 556 -1444 -1780 C ATOM 117 CD ARG A 182 -6.812 26.448 -37.747 1.00105.26 C ANISOU 117 CD ARG A 182 13479 14971 11546 543 -1475 -1736 C ATOM 118 NE ARG A 182 -8.035 27.228 -37.557 1.00110.90 N ANISOU 118 NE ARG A 182 14148 15730 12259 502 -1425 -1514 N ATOM 119 CZ ARG A 182 -9.243 26.698 -37.377 1.00112.87 C ANISOU 119 CZ ARG A 182 14387 15950 12548 437 -1539 -1425 C ATOM 120 NH1 ARG A 182 -9.395 25.380 -37.364 1.00113.51 N ANISOU 120 NH1 ARG A 182 14503 15955 12671 404 -1710 -1538 N ATOM 121 NH2 ARG A 182 -10.300 27.484 -37.211 1.00112.06 N ANISOU 121 NH2 ARG A 182 14240 15894 12445 405 -1481 -1222 N ATOM 122 N LEU A 183 -6.749 25.369 -31.637 1.00 56.78 N ANISOU 122 N LEU A 183 7444 8131 5999 426 -1532 -1571 N ATOM 123 CA LEU A 183 -7.602 25.247 -30.462 1.00 53.70 C ANISOU 123 CA LEU A 183 7057 7623 5722 364 -1565 -1437 C ATOM 124 C LEU A 183 -7.799 26.602 -29.782 1.00 49.48 C ANISOU 124 C LEU A 183 6493 7101 5209 364 -1391 -1254 C ATOM 125 O LEU A 183 -6.841 27.336 -29.554 1.00 47.28 O ANISOU 125 O LEU A 183 6215 6828 4919 412 -1258 -1277 O ATOM 126 CB LEU A 183 -6.988 24.249 -29.485 1.00 51.91 C ANISOU 126 CB LEU A 183 6885 7227 5611 356 -1657 -1555 C ATOM 127 CG LEU A 183 -7.979 23.306 -28.811 1.00 63.37 C ANISOU 127 CG LEU A 183 8355 8564 7157 284 -1805 -1510 C ATOM 128 CD1 LEU A 183 -9.171 23.045 -29.720 1.00 67.18 C ANISOU 128 CD1 LEU A 183 8809 9143 7573 244 -1893 -1449 C ATOM 129 CD2 LEU A 183 -7.293 22.001 -28.443 1.00 69.62 C ANISOU 129 CD2 LEU A 183 9205 9230 8019 287 -1940 -1691 C ATOM 130 N SER A 184 -9.047 26.937 -29.472 1.00 44.14 N ANISOU 130 N SER A 184 5786 6426 4558 310 -1389 -1073 N ATOM 131 CA SER A 184 -9.340 28.225 -28.851 1.00 41.41 C ANISOU 131 CA SER A 184 5411 6094 4231 306 -1224 -890 C ATOM 132 C SER A 184 -9.583 28.080 -27.353 1.00 37.19 C ANISOU 132 C SER A 184 4899 5396 3835 260 -1230 -812 C ATOM 133 O SER A 184 -10.041 27.039 -26.884 1.00 38.62 O ANISOU 133 O SER A 184 5107 5474 4093 213 -1375 -843 O ATOM 134 CB SER A 184 -10.539 28.905 -29.525 1.00 38.25 C ANISOU 134 CB SER A 184 4956 5818 3760 283 -1190 -722 C ATOM 135 OG SER A 184 -11.771 28.372 -29.067 1.00 41.32 O ANISOU 135 OG SER A 184 5337 6145 4217 213 -1297 -621 O ATOM 136 N LEU A 185 -9.268 29.134 -26.610 1.00 28.50 N ANISOU 136 N LEU A 185 3792 4274 2765 273 -1069 -712 N ATOM 137 CA LEU A 185 -9.482 29.152 -25.174 1.00 29.11 C ANISOU 137 CA LEU A 185 3890 4203 2969 229 -1053 -625 C ATOM 138 C LEU A 185 -10.949 28.899 -24.838 1.00 33.40 C ANISOU 138 C LEU A 185 4415 4712 3563 157 -1131 -477 C ATOM 139 O LEU A 185 -11.260 28.155 -23.907 1.00 36.69 O ANISOU 139 O LEU A 185 4862 4993 4087 109 -1225 -476 O ATOM 140 CB LEU A 185 -9.035 30.486 -24.585 1.00 26.33 C ANISOU 140 CB LEU A 185 3525 3858 2621 253 -851 -519 C ATOM 141 CG LEU A 185 -9.239 30.664 -23.081 1.00 27.84 C ANISOU 141 CG LEU A 185 3737 3903 2938 207 -811 -415 C ATOM 142 CD1 LEU A 185 -8.404 29.670 -22.284 1.00 25.04 C ANISOU 142 CD1 LEU A 185 3438 3402 2673 204 -905 -564 C ATOM 143 CD2 LEU A 185 -8.913 32.098 -22.653 1.00 29.25 C ANISOU 143 CD2 LEU A 185 3898 4112 3105 229 -600 -295 C ATOM 144 N SER A 186 -11.850 29.522 -25.595 1.00 31.92 N ANISOU 144 N SER A 186 4177 4651 3301 150 -1091 -352 N ATOM 145 CA SER A 186 -13.276 29.416 -25.301 1.00 33.64 C ANISOU 145 CA SER A 186 4370 4848 3563 83 -1149 -196 C ATOM 146 C SER A 186 -13.795 28.004 -25.509 1.00 33.03 C ANISOU 146 C SER A 186 4314 4723 3514 41 -1357 -287 C ATOM 147 O SER A 186 -14.631 27.539 -24.745 1.00 42.03 O ANISOU 147 O SER A 186 5461 5765 4742 -21 -1434 -210 O ATOM 148 CB SER A 186 -14.090 30.419 -26.117 1.00 33.54 C ANISOU 148 CB SER A 186 4297 4989 3460 89 -1059 -44 C ATOM 149 OG SER A 186 -14.054 31.696 -25.506 1.00 35.34 O ANISOU 149 OG SER A 186 4505 5219 3705 100 -875 102 O ATOM 150 N GLU A 187 -13.294 27.320 -26.533 1.00 32.95 N ANISOU 150 N GLU A 187 4315 4777 3427 73 -1447 -451 N ATOM 151 CA GLU A 187 -13.627 25.911 -26.723 1.00 41.71 C ANISOU 151 CA GLU A 187 5454 5832 4564 37 -1645 -561 C ATOM 152 C GLU A 187 -13.367 25.129 -25.445 1.00 34.86 C ANISOU 152 C GLU A 187 4638 4779 3829 5 -1717 -610 C ATOM 153 O GLU A 187 -14.221 24.386 -24.974 1.00 41.98 O ANISOU 153 O GLU A 187 5550 5599 4800 -57 -1835 -572 O ATOM 154 CB GLU A 187 -12.796 25.301 -27.847 1.00 50.41 C ANISOU 154 CB GLU A 187 6572 7007 5576 86 -1712 -758 C ATOM 155 CG GLU A 187 -13.194 25.730 -29.236 1.00 62.61 C ANISOU 155 CG GLU A 187 8071 8730 6986 106 -1693 -733 C ATOM 156 CD GLU A 187 -12.547 24.872 -30.304 1.00 76.56 C ANISOU 156 CD GLU A 187 9861 10551 8676 138 -1796 -933 C ATOM 157 OE1 GLU A 187 -12.144 25.424 -31.350 1.00 88.15 O ANISOU 157 OE1 GLU A 187 11306 12156 10030 186 -1726 -968 O ATOM 158 OE2 GLU A 187 -12.438 23.645 -30.093 1.00 74.38 O ANISOU 158 OE2 GLU A 187 9628 10179 8454 115 -1944 -1057 O ATOM 159 N VAL A 188 -12.171 25.304 -24.896 1.00 33.93 N ANISOU 159 N VAL A 188 4552 4597 3744 47 -1645 -697 N ATOM 160 CA VAL A 188 -11.760 24.603 -23.690 1.00 35.13 C ANISOU 160 CA VAL A 188 4756 4575 4017 24 -1704 -755 C ATOM 161 C VAL A 188 -12.609 25.026 -22.491 1.00 35.89 C ANISOU 161 C VAL A 188 4845 4578 4212 -36 -1659 -573 C ATOM 162 O VAL A 188 -13.010 24.187 -21.690 1.00 38.29 O ANISOU 162 O VAL A 188 5181 4753 4613 -88 -1769 -577 O ATOM 163 CB VAL A 188 -10.257 24.838 -23.390 1.00 41.75 C ANISOU 163 CB VAL A 188 5623 5377 4862 85 -1618 -878 C ATOM 164 CG1 VAL A 188 -9.847 24.162 -22.094 1.00 34.30 C ANISOU 164 CG1 VAL A 188 4732 4253 4046 60 -1675 -928 C ATOM 165 CG2 VAL A 188 -9.409 24.328 -24.534 1.00 47.27 C ANISOU 165 CG2 VAL A 188 6332 6157 5471 142 -1671 -1067 C ATOM 166 N LEU A 189 -12.889 26.319 -22.368 1.00 27.31 N ANISOU 166 N LEU A 189 3719 3555 3101 -29 -1497 -414 N ATOM 167 CA LEU A 189 -13.646 26.812 -21.212 1.00 27.74 C ANISOU 167 CA LEU A 189 3768 3523 3250 -83 -1437 -237 C ATOM 168 C LEU A 189 -15.107 26.359 -21.234 1.00 29.12 C ANISOU 168 C LEU A 189 3921 3693 3451 -152 -1545 -127 C ATOM 169 O LEU A 189 -15.703 26.111 -20.180 1.00 29.55 O ANISOU 169 O LEU A 189 3992 3627 3610 -210 -1578 -44 O ATOM 170 CB LEU A 189 -13.569 28.339 -21.104 1.00 25.68 C ANISOU 170 CB LEU A 189 3469 3334 2953 -57 -1230 -93 C ATOM 171 CG LEU A 189 -12.213 28.944 -20.739 1.00 27.16 C ANISOU 171 CG LEU A 189 3679 3502 3137 -3 -1100 -163 C ATOM 172 CD1 LEU A 189 -12.264 30.458 -20.841 1.00 24.36 C ANISOU 172 CD1 LEU A 189 3283 3241 2730 22 -899 -17 C ATOM 173 CD2 LEU A 189 -11.791 28.513 -19.333 1.00 27.56 C ANISOU 173 CD2 LEU A 189 3781 3375 3315 -33 -1121 -189 C ATOM 174 N ASP A 190 -15.672 26.255 -22.438 1.00 32.95 N ANISOU 174 N ASP A 190 4369 4308 3841 -146 -1598 -128 N ATOM 175 CA ASP A 190 -17.071 25.870 -22.628 1.00 37.05 C ANISOU 175 CA ASP A 190 4861 4846 4369 -208 -1698 -25 C ATOM 176 C ASP A 190 -17.301 24.369 -22.418 1.00 42.14 C ANISOU 176 C ASP A 190 5550 5387 5076 -253 -1898 -139 C ATOM 177 O ASP A 190 -18.373 23.949 -21.971 1.00 35.51 O ANISOU 177 O ASP A 190 4705 4491 4297 -319 -1981 -48 O ATOM 178 CB ASP A 190 -17.544 26.261 -24.035 1.00 34.78 C ANISOU 178 CB ASP A 190 4521 4741 3954 -185 -1688 6 C ATOM 179 CG ASP A 190 -17.646 27.772 -24.228 1.00 43.76 C ANISOU 179 CG ASP A 190 5609 5984 5036 -154 -1496 158 C ATOM 180 OD1 ASP A 190 -17.844 28.214 -25.382 1.00 47.23 O ANISOU 180 OD1 ASP A 190 6007 6577 5364 -125 -1467 177 O ATOM 181 OD2 ASP A 190 -17.527 28.521 -23.233 1.00 46.38 O ANISOU 181 OD2 ASP A 190 5944 6247 5434 -159 -1373 260 O ATOM 182 N SER A 191 -16.279 23.577 -22.738 1.00 45.97 N ANISOU 182 N SER A 191 6077 5847 5544 -216 -1973 -338 N ATOM 183 CA SER A 191 -16.376 22.115 -22.781 1.00 42.77 C ANISOU 183 CA SER A 191 5714 5363 5174 -247 -2166 -472 C ATOM 184 C SER A 191 -16.559 21.457 -21.412 1.00 48.73 C ANISOU 184 C SER A 191 6514 5933 6068 -301 -2235 -459 C ATOM 185 O SER A 191 -17.143 20.378 -21.310 1.00 54.20 O ANISOU 185 O SER A 191 7230 6560 6803 -351 -2391 -499 O ATOM 186 CB SER A 191 -15.125 21.533 -23.441 1.00 33.41 C ANISOU 186 CB SER A 191 4563 4196 3937 -186 -2209 -689 C ATOM 187 OG SER A 191 -13.998 21.713 -22.599 1.00 33.84 O ANISOU 187 OG SER A 191 4653 4154 4050 -151 -2136 -752 O ATOM 188 N GLY A 192 -16.041 22.094 -20.367 1.00 40.59 N ANISOU 188 N GLY A 192 5497 4819 5105 -292 -2119 -406 N ATOM 189 CA GLY A 192 -16.081 21.520 -19.034 1.00 36.23 C ANISOU 189 CA GLY A 192 4992 4090 4683 -339 -2173 -401 C ATOM 190 C GLY A 192 -14.861 20.653 -18.781 1.00 43.45 C ANISOU 190 C GLY A 192 5966 4911 5632 -305 -2243 -599 C ATOM 191 O GLY A 192 -14.741 20.014 -17.739 1.00 40.80 O ANISOU 191 O GLY A 192 5677 4423 5401 -339 -2307 -627 O ATOM 192 N ASP A 193 -13.944 20.640 -19.740 1.00 42.99 N ANISOU 192 N ASP A 193 5907 4943 5486 -239 -2230 -736 N ATOM 193 CA ASP A 193 -12.799 19.739 -19.685 1.00 38.71 C ANISOU 193 CA ASP A 193 5418 4327 4965 -202 -2308 -938 C ATOM 194 C ASP A 193 -11.507 20.419 -19.244 1.00 39.70 C ANISOU 194 C ASP A 193 5555 4431 5098 -143 -2174 -985 C ATOM 195 O ASP A 193 -10.424 19.865 -19.427 1.00 42.09 O ANISOU 195 O ASP A 193 5891 4708 5395 -97 -2213 -1156 O ATOM 196 CB ASP A 193 -12.597 19.066 -21.047 1.00 36.21 C ANISOU 196 CB ASP A 193 5097 4110 4549 -169 -2405 -1084 C ATOM 197 CG ASP A 193 -13.693 18.052 -21.366 1.00 47.13 C ANISOU 197 CG ASP A 193 6486 5480 5940 -230 -2574 -1084 C ATOM 198 OD1 ASP A 193 -13.930 17.783 -22.564 1.00 48.91 O ANISOU 198 OD1 ASP A 193 6692 5821 6072 -218 -2631 -1139 O ATOM 199 OD2 ASP A 193 -14.323 17.528 -20.419 1.00 51.20 O ANISOU 199 OD2 ASP A 193 7027 5871 6557 -292 -2648 -1027 O ATOM 200 N LEU A 194 -11.614 21.611 -18.665 1.00 30.43 N ANISOU 200 N LEU A 194 3526 4029 4006 -87 -938 347 N ATOM 201 CA LEU A 194 -10.414 22.376 -18.309 1.00 34.86 C ANISOU 201 CA LEU A 194 4103 4585 4558 -80 -867 302 C ATOM 202 C LEU A 194 -9.479 21.607 -17.375 1.00 27.70 C ANISOU 202 C LEU A 194 3197 3665 3663 -108 -891 264 C ATOM 203 O LEU A 194 -8.272 21.594 -17.573 1.00 29.10 O ANISOU 203 O LEU A 194 3399 3830 3830 -99 -876 212 O ATOM 204 CB LEU A 194 -10.778 23.740 -17.709 1.00 25.36 C ANISOU 204 CB LEU A 194 2883 3396 3356 -75 -777 328 C ATOM 205 CG LEU A 194 -9.594 24.576 -17.220 1.00 28.17 C ANISOU 205 CG LEU A 194 3252 3747 3705 -70 -701 285 C ATOM 206 CD1 LEU A 194 -9.768 26.050 -17.569 1.00 23.14 C ANISOU 206 CD1 LEU A 194 2619 3120 3055 -42 -614 297 C ATOM 207 CD2 LEU A 194 -9.381 24.390 -15.721 1.00 32.64 C ANISOU 207 CD2 LEU A 194 3798 4314 4290 -104 -691 285 C ATOM 208 N MET A 195 -10.040 20.969 -16.360 1.00 25.86 N ANISOU 208 N MET A 195 2937 3437 3450 -141 -928 292 N ATOM 209 CA MET A 195 -9.226 20.226 -15.408 1.00 25.35 C ANISOU 209 CA MET A 195 2872 3361 3398 -170 -953 261 C ATOM 210 C MET A 195 -8.334 19.187 -16.085 1.00 25.91 C ANISOU 210 C MET A 195 2969 3413 3461 -166 -1015 213 C ATOM 211 O MET A 195 -7.235 18.914 -15.618 1.00 37.85 O ANISOU 211 O MET A 195 4493 4913 4975 -176 -1012 168 O ATOM 212 CB MET A 195 -10.108 19.572 -14.346 1.00 22.38 C ANISOU 212 CB MET A 195 2463 2994 3046 -206 -996 303 C ATOM 213 CG MET A 195 -10.781 20.582 -13.422 1.00 24.45 C ANISOU 213 CG MET A 195 2698 3274 3316 -214 -928 343 C ATOM 214 SD MET A 195 -9.576 21.570 -12.511 1.00 31.51 S ANISOU 214 SD MET A 195 3599 4164 4207 -215 -836 302 S ATOM 215 CE MET A 195 -8.838 20.297 -11.488 1.00 27.74 C ANISOU 215 CE MET A 195 3119 3674 3747 -254 -896 272 C ATOM 216 N LYS A 196 -8.797 18.625 -17.193 1.00 27.17 N ANISOU 216 N LYS A 196 3139 3569 3613 -151 -1072 222 N ATOM 217 CA LYS A 196 -7.997 17.658 -17.935 1.00 32.30 C ANISOU 217 CA LYS A 196 3816 4201 4255 -144 -1132 177 C ATOM 218 C LYS A 196 -6.841 18.330 -18.670 1.00 30.02 C ANISOU 218 C LYS A 196 3559 3904 3944 -113 -1079 126 C ATOM 219 O LYS A 196 -5.772 17.753 -18.804 1.00 33.74 O ANISOU 219 O LYS A 196 4050 4359 4410 -113 -1101 76 O ATOM 220 CB LYS A 196 -8.871 16.870 -18.913 1.00 37.98 C ANISOU 220 CB LYS A 196 4538 4920 4971 -136 -1208 203 C ATOM 221 CG LYS A 196 -9.981 16.079 -18.248 1.00 45.50 C ANISOU 221 CG LYS A 196 5462 5880 5946 -168 -1270 252 C ATOM 222 CD LYS A 196 -10.722 15.200 -19.254 1.00 53.52 C ANISOU 222 CD LYS A 196 6484 6893 6959 -161 -1352 273 C ATOM 223 CE LYS A 196 -12.016 14.619 -18.674 1.00 54.69 C ANISOU 223 CE LYS A 196 6599 7052 7127 -189 -1404 331 C ATOM 224 NZ LYS A 196 -13.107 15.641 -18.533 1.00 55.09 N ANISOU 224 NZ LYS A 196 6626 7124 7181 -183 -1351 385 N ATOM 225 N PHE A 197 -7.067 19.549 -19.149 1.00 28.34 N ANISOU 225 N PHE A 197 3349 3701 3718 -87 -1008 139 N ATOM 226 CA PHE A 197 -6.030 20.331 -19.811 1.00 25.35 C ANISOU 226 CA PHE A 197 2998 3316 3318 -58 -950 94 C ATOM 227 C PHE A 197 -4.987 20.827 -18.825 1.00 33.14 C ANISOU 227 C PHE A 197 3985 4299 4308 -69 -891 60 C ATOM 228 O PHE A 197 -3.792 20.749 -19.084 1.00 27.37 O ANISOU 228 O PHE A 197 3278 3555 3567 -60 -880 8 O ATOM 229 CB PHE A 197 -6.651 21.534 -20.524 1.00 26.47 C ANISOU 229 CB PHE A 197 3141 3471 3446 -29 -890 122 C ATOM 230 CG PHE A 197 -7.197 21.214 -21.881 1.00 29.31 C ANISOU 230 CG PHE A 197 3515 3830 3792 -5 -934 134 C ATOM 231 CD1 PHE A 197 -6.423 21.403 -23.015 1.00 30.69 C ANISOU 231 CD1 PHE A 197 3722 3996 3944 25 -923 95 C ATOM 232 CD2 PHE A 197 -8.473 20.703 -22.025 1.00 30.44 C ANISOU 232 CD2 PHE A 197 3640 3981 3945 -14 -989 184 C ATOM 233 CE1 PHE A 197 -6.916 21.096 -24.264 1.00 33.06 C ANISOU 233 CE1 PHE A 197 4036 4294 4231 47 -965 105 C ATOM 234 CE2 PHE A 197 -8.972 20.392 -23.281 1.00 29.15 C ANISOU 234 CE2 PHE A 197 3491 3816 3769 7 -1032 195 C ATOM 235 CZ PHE A 197 -8.193 20.590 -24.397 1.00 29.97 C ANISOU 235 CZ PHE A 197 3627 3910 3850 38 -1020 155 C ATOM 236 N ALA A 198 -5.453 21.338 -17.690 1.00 31.79 N ANISOU 236 N ALA A 198 3787 4138 4152 -90 -852 91 N ATOM 237 CA ALA A 198 -4.578 21.969 -16.713 1.00 28.54 C ANISOU 237 CA ALA A 198 3374 3725 3744 -100 -788 65 C ATOM 238 C ALA A 198 -3.560 21.024 -16.077 1.00 31.62 C ANISOU 238 C ALA A 198 3771 4100 4144 -123 -827 21 C ATOM 239 O ALA A 198 -2.550 21.487 -15.555 1.00 30.04 O ANISOU 239 O ALA A 198 3579 3894 3942 -125 -777 -14 O ATOM 240 CB ALA A 198 -5.404 22.674 -15.632 1.00 23.17 C ANISOU 240 CB ALA A 198 2664 3061 3079 -117 -743 110 C ATOM 241 N VAL A 199 -3.812 19.714 -16.110 1.00 29.39 N ANISOU 241 N VAL A 199 3485 3810 3871 -140 -915 24 N ATOM 242 CA VAL A 199 -2.887 18.760 -15.480 1.00 27.45 C ANISOU 242 CA VAL A 199 3245 3550 3636 -164 -956 -15 C ATOM 243 C VAL A 199 -2.057 17.964 -16.488 1.00 30.15 C ANISOU 243 C VAL A 199 3615 3874 3964 -147 -1006 -62 C ATOM 244 O VAL A 199 -1.278 17.088 -16.109 1.00 35.10 O ANISOU 244 O VAL A 199 4250 4488 4599 -164 -1047 -97 O ATOM 245 CB VAL A 199 -3.597 17.779 -14.526 1.00 32.03 C ANISOU 245 CB VAL A 199 3799 4131 4239 -201 -1020 16 C ATOM 246 CG1 VAL A 199 -4.338 18.541 -13.444 1.00 28.84 C ANISOU 246 CG1 VAL A 199 3365 3744 3848 -219 -969 59 C ATOM 247 CG2 VAL A 199 -4.539 16.828 -15.302 1.00 21.73 C ANISOU 247 CG2 VAL A 199 2492 2827 2936 -200 -1104 45 C ATOM 248 N ASP A 200 -2.248 18.267 -17.766 1.00 28.79 N ANISOU 248 N ASP A 200 3462 3704 3774 -115 -1003 -62 N ATOM 249 CA ASP A 200 -1.413 17.743 -18.840 1.00 31.26 C ANISOU 249 CA ASP A 200 3805 4003 4070 -93 -1035 -108 C ATOM 250 C ASP A 200 -0.415 18.839 -19.222 1.00 31.86 C ANISOU 250 C ASP A 200 3901 4078 4128 -66 -953 -145 C ATOM 251 O ASP A 200 -0.759 20.016 -19.213 1.00 35.41 O ANISOU 251 O ASP A 200 4344 4539 4570 -54 -882 -123 O ATOM 252 CB ASP A 200 -2.296 17.392 -20.043 1.00 34.17 C ANISOU 252 CB ASP A 200 4181 4375 4429 -73 -1084 -82 C ATOM 253 CG ASP A 200 -1.496 16.910 -21.247 1.00 43.04 C ANISOU 253 CG ASP A 200 5337 5484 5533 -47 -1116 -127 C ATOM 254 OD1 ASP A 200 -1.006 15.755 -21.230 1.00 42.64 O ANISOU 254 OD1 ASP A 200 5294 5419 5487 -59 -1183 -155 O ATOM 255 OD2 ASP A 200 -1.377 17.687 -22.220 1.00 40.54 O ANISOU 255 OD2 ASP A 200 5037 5170 5195 -15 -1073 -135 O ATOM 256 N LYS A 201 0.812 18.469 -19.568 1.00 35.00 N ANISOU 256 N LYS A 201 4323 4461 4516 -57 -961 -201 N ATOM 257 CA LYS A 201 1.839 19.472 -19.855 1.00 36.54 C ANISOU 257 CA LYS A 201 4537 4655 4694 -35 -884 -238 C ATOM 258 C LYS A 201 1.499 20.312 -21.090 1.00 36.19 C ANISOU 258 C LYS A 201 4507 4618 4628 2 -847 -227 C ATOM 259 O LYS A 201 1.467 21.542 -21.028 1.00 39.69 O ANISOU 259 O LYS A 201 4948 5071 5063 14 -769 -217 O ATOM 260 CB LYS A 201 3.209 18.813 -20.014 1.00 42.81 C ANISOU 260 CB LYS A 201 5352 5431 5482 -32 -906 -300 C ATOM 261 CG LYS A 201 4.327 19.769 -20.414 1.00 46.29 C ANISOU 261 CG LYS A 201 5814 5869 5905 -8 -831 -341 C ATOM 262 CD LYS A 201 5.650 19.021 -20.529 1.00 51.72 C ANISOU 262 CD LYS A 201 6521 6541 6589 -7 -860 -401 C ATOM 263 CE LYS A 201 6.664 19.780 -21.377 1.00 53.61 C ANISOU 263 CE LYS A 201 6786 6777 6804 25 -803 -442 C ATOM 264 NZ LYS A 201 7.164 21.018 -20.726 1.00 44.06 N ANISOU 264 NZ LYS A 201 5572 5574 5594 24 -711 -448 N ATOM 265 N THR A 202 1.242 19.645 -22.208 1.00 31.78 N ANISOU 265 N THR A 202 3963 4055 4058 19 -905 -229 N ATOM 266 CA THR A 202 0.829 20.329 -23.428 1.00 35.59 C ANISOU 266 CA THR A 202 4459 4544 4519 53 -880 -217 C ATOM 267 C THR A 202 -0.443 21.143 -23.207 1.00 38.71 C ANISOU 267 C THR A 202 4832 4957 4920 52 -846 -157 C ATOM 268 O THR A 202 -0.541 22.285 -23.646 1.00 44.26 O ANISOU 268 O THR A 202 5540 5668 5609 74 -780 -148 O ATOM 269 CB THR A 202 0.577 19.339 -24.571 1.00 41.91 C ANISOU 269 CB THR A 202 5276 5337 5309 67 -959 -222 C ATOM 270 OG1 THR A 202 1.718 18.487 -24.728 1.00 44.48 O ANISOU 270 OG1 THR A 202 5622 5647 5632 67 -996 -276 O ATOM 271 CG2 THR A 202 0.319 20.087 -25.873 1.00 46.51 C ANISOU 271 CG2 THR A 202 5878 5927 5869 104 -928 -215 C ATOM 272 N GLY A 203 -1.412 20.549 -22.521 1.00 35.99 N ANISOU 272 N GLY A 203 4463 4617 4596 25 -893 -116 N ATOM 273 CA GLY A 203 -2.655 21.232 -22.223 1.00 37.49 C ANISOU 273 CA GLY A 203 4629 4824 4794 21 -866 -58 C ATOM 274 C GLY A 203 -2.428 22.494 -21.412 1.00 37.63 C ANISOU 274 C GLY A 203 4635 4850 4813 19 -773 -54 C ATOM 275 O GLY A 203 -2.873 23.577 -21.796 1.00 36.62 O ANISOU 275 O GLY A 203 4507 4733 4676 39 -715 -31 O ATOM 276 N CYS A 204 -1.730 22.357 -20.286 1.00 31.40 N ANISOU 276 N CYS A 204 3838 4055 4037 -5 -759 -76 N ATOM 277 CA CYS A 204 -1.492 23.489 -19.394 1.00 31.46 C ANISOU 277 CA CYS A 204 3835 4071 4049 -10 -674 -72 C ATOM 278 C CYS A 204 -0.613 24.545 -20.055 1.00 35.41 C ANISOU 278 C CYS A 204 4358 4568 4526 20 -601 -106 C ATOM 279 O CYS A 204 -0.746 25.736 -19.780 1.00 33.13 O ANISOU 279 O CYS A 204 4064 4289 4234 27 -526 -91 O ATOM 280 CB CYS A 204 -0.865 23.031 -18.079 1.00 26.41 C ANISOU 280 CB CYS A 204 3184 3424 3427 -43 -680 -92 C ATOM 281 SG CYS A 204 -1.002 24.265 -16.759 1.00 35.78 S ANISOU 281 SG CYS A 204 4349 4622 4624 -58 -591 -69 S ATOM 282 N GLN A 205 0.279 24.096 -20.930 1.00 36.19 N ANISOU 282 N GLN A 205 4485 4655 4611 37 -625 -151 N ATOM 283 CA GLN A 205 1.148 24.993 -21.675 1.00 42.40 C ANISOU 283 CA GLN A 205 5295 5439 5375 67 -563 -185 C ATOM 284 C GLN A 205 0.310 25.857 -22.611 1.00 49.37 C ANISOU 284 C GLN A 205 6181 6334 6243 94 -532 -151 C ATOM 285 O GLN A 205 0.555 27.058 -22.755 1.00 49.22 O ANISOU 285 O GLN A 205 6168 6321 6212 112 -455 -154 O ATOM 286 CB GLN A 205 2.170 24.177 -22.466 1.00 53.32 C ANISOU 286 CB GLN A 205 6706 6809 6746 79 -606 -237 C ATOM 287 CG GLN A 205 3.178 24.986 -23.246 1.00 68.74 C ANISOU 287 CG GLN A 205 8684 8758 8675 109 -548 -277 C ATOM 288 CD GLN A 205 4.391 24.155 -23.635 1.00 81.33 C ANISOU 288 CD GLN A 205 10302 10338 10263 113 -584 -334 C ATOM 289 OE1 GLN A 205 4.859 24.203 -24.779 1.00 82.98 O ANISOU 289 OE1 GLN A 205 10534 10542 10450 141 -584 -360 O ATOM 290 NE2 GLN A 205 4.903 23.379 -22.682 1.00 81.05 N ANISOU 290 NE2 GLN A 205 10258 10293 10245 85 -616 -354 N ATOM 291 N PHE A 206 -0.691 25.242 -23.239 1.00 41.70 N ANISOU 291 N PHE A 206 5205 5366 5272 98 -592 -119 N ATOM 292 CA PHE A 206 -1.601 25.973 -24.113 1.00 31.60 C ANISOU 292 CA PHE A 206 3928 4099 3982 122 -570 -83 C ATOM 293 C PHE A 206 -2.409 27.001 -23.324 1.00 34.62 C ANISOU 293 C PHE A 206 4286 4496 4374 115 -510 -38 C ATOM 294 O PHE A 206 -2.549 28.157 -23.745 1.00 30.44 O ANISOU 294 O PHE A 206 3760 3973 3831 137 -445 -28 O ATOM 295 CB PHE A 206 -2.547 25.015 -24.839 1.00 26.33 C ANISOU 295 CB PHE A 206 3258 3431 3315 124 -652 -56 C ATOM 296 CG PHE A 206 -3.753 25.694 -25.431 1.00 31.76 C ANISOU 296 CG PHE A 206 3937 4132 3997 140 -635 -6 C ATOM 297 CD1 PHE A 206 -3.643 26.455 -26.582 1.00 31.30 C ANISOU 297 CD1 PHE A 206 3901 4077 3917 174 -599 -13 C ATOM 298 CD2 PHE A 206 -4.996 25.585 -24.821 1.00 33.24 C ANISOU 298 CD2 PHE A 206 4096 4331 4204 122 -655 49 C ATOM 299 CE1 PHE A 206 -4.747 27.080 -27.125 1.00 32.13 C ANISOU 299 CE1 PHE A 206 3997 4193 4017 189 -584 34 C ATOM 300 CE2 PHE A 206 -6.105 26.212 -25.353 1.00 32.28 C ANISOU 300 CE2 PHE A 206 3965 4221 4077 137 -640 95 C ATOM 301 CZ PHE A 206 -5.981 26.959 -26.511 1.00 34.90 C ANISOU 301 CZ PHE A 206 4319 4555 4387 171 -604 87 C ATOM 302 N LEU A 207 -2.941 26.574 -22.180 1.00 30.33 N ANISOU 302 N LEU A 207 3715 3955 3853 83 -532 -12 N ATOM 303 CA LEU A 207 -3.745 27.454 -21.339 1.00 31.19 C ANISOU 303 CA LEU A 207 3798 4079 3974 74 -481 32 C ATOM 304 C LEU A 207 -2.943 28.652 -20.856 1.00 29.23 C ANISOU 304 C LEU A 207 3556 3831 3719 80 -389 10 C ATOM 305 O LEU A 207 -3.456 29.763 -20.790 1.00 28.25 O ANISOU 305 O LEU A 207 3424 3718 3592 91 -327 38 O ATOM 306 CB LEU A 207 -4.318 26.700 -20.141 1.00 27.88 C ANISOU 306 CB LEU A 207 3351 3663 3580 37 -523 58 C ATOM 307 CG LEU A 207 -5.439 25.732 -20.482 1.00 29.07 C ANISOU 307 CG LEU A 207 3489 3818 3740 29 -604 96 C ATOM 308 CD1 LEU A 207 -6.027 25.136 -19.220 1.00 35.40 C ANISOU 308 CD1 LEU A 207 4260 4623 4566 -8 -636 126 C ATOM 309 CD2 LEU A 207 -6.499 26.447 -21.285 1.00 27.66 C ANISOU 309 CD2 LEU A 207 3306 3651 3552 52 -584 139 C ATOM 310 N GLU A 208 -1.678 28.425 -20.523 1.00 25.88 N ANISOU 310 N GLU A 208 3146 3395 3294 73 -381 -41 N ATOM 311 CA GLU A 208 -0.860 29.498 -19.978 1.00 37.49 C ANISOU 311 CA GLU A 208 4621 4865 4759 76 -297 -63 C ATOM 312 C GLU A 208 -0.508 30.549 -21.019 1.00 38.95 C ANISOU 312 C GLU A 208 4828 5051 4920 112 -238 -77 C ATOM 313 O GLU A 208 -0.395 31.730 -20.694 1.00 44.17 O ANISOU 313 O GLU A 208 5488 5718 5578 119 -161 -71 O ATOM 314 CB GLU A 208 0.401 28.949 -19.315 1.00 46.57 C ANISOU 314 CB GLU A 208 5779 6001 5915 58 -305 -113 C ATOM 315 CG GLU A 208 0.159 28.411 -17.923 1.00 51.87 C ANISOU 315 CG GLU A 208 6425 6672 6610 21 -328 -98 C ATOM 316 CD GLU A 208 1.387 27.765 -17.344 1.00 69.22 C ANISOU 316 CD GLU A 208 8631 8856 8814 4 -344 -147 C ATOM 317 OE1 GLU A 208 1.295 26.593 -16.929 1.00 80.83 O ANISOU 317 OE1 GLU A 208 10093 10321 10299 -20 -414 -149 O ATOM 318 OE2 GLU A 208 2.450 28.419 -17.316 1.00 74.94 O ANISOU 318 OE2 GLU A 208 9371 9574 9528 13 -288 -185 O ATOM 319 N LYS A 209 -0.338 30.126 -22.267 1.00 29.91 N ANISOU 319 N LYS A 209 3704 3901 3759 134 -275 -94 N ATOM 320 CA LYS A 209 -0.101 31.081 -23.334 1.00 33.35 C ANISOU 320 CA LYS A 209 4160 4339 4171 168 -224 -103 C ATOM 321 C LYS A 209 -1.400 31.845 -23.584 1.00 32.96 C ANISOU 321 C LYS A 209 4097 4305 4122 179 -200 -48 C ATOM 322 O LYS A 209 -1.402 33.075 -23.698 1.00 29.22 O ANISOU 322 O LYS A 209 3626 3837 3638 196 -126 -40 O ATOM 323 CB LYS A 209 0.359 30.376 -24.609 1.00 42.04 C ANISOU 323 CB LYS A 209 5287 5431 5255 188 -273 -134 C ATOM 324 CG LYS A 209 1.165 31.263 -25.557 1.00 59.56 C ANISOU 324 CG LYS A 209 7534 7649 7449 220 -216 -165 C ATOM 325 CD LYS A 209 2.548 31.566 -24.980 1.00 75.12 C ANISOU 325 CD LYS A 209 9514 9610 9417 214 -171 -214 C ATOM 326 CE LYS A 209 3.521 32.089 -26.039 1.00 82.84 C ANISOU 326 CE LYS A 209 10522 10584 10369 244 -134 -254 C ATOM 327 NZ LYS A 209 3.363 33.546 -26.338 1.00 82.08 N ANISOU 327 NZ LYS A 209 10430 10497 10260 265 -53 -239 N ATOM 328 N ALA A 210 -2.503 31.104 -23.635 1.00 22.22 N ANISOU 328 N ALA A 210 2720 2949 2773 169 -262 -9 N ATOM 329 CA ALA A 210 -3.810 31.673 -23.940 1.00 25.05 C ANISOU 329 CA ALA A 210 3065 3322 3132 179 -250 45 C ATOM 330 C ALA A 210 -4.283 32.702 -22.911 1.00 24.61 C ANISOU 330 C ALA A 210 2987 3277 3087 170 -183 77 C ATOM 331 O ALA A 210 -4.950 33.676 -23.269 1.00 28.54 O ANISOU 331 O ALA A 210 3480 3784 3578 188 -138 107 O ATOM 332 CB ALA A 210 -4.837 30.568 -24.092 1.00 23.29 C ANISOU 332 CB ALA A 210 2827 3101 2921 167 -335 79 C ATOM 333 N VAL A 211 -3.941 32.489 -21.643 1.00 26.56 N ANISOU 333 N VAL A 211 3219 3521 3351 141 -177 69 N ATOM 334 CA VAL A 211 -4.381 33.403 -20.586 1.00 32.89 C ANISOU 334 CA VAL A 211 4000 4334 4165 130 -116 98 C ATOM 335 C VAL A 211 -3.506 34.653 -20.455 1.00 32.84 C ANISOU 335 C VAL A 211 4007 4325 4145 144 -27 72 C ATOM 336 O VAL A 211 -3.842 35.568 -19.711 1.00 35.53 O ANISOU 336 O VAL A 211 4333 4674 4493 140 31 95 O ATOM 337 CB VAL A 211 -4.537 32.704 -19.204 1.00 35.71 C ANISOU 337 CB VAL A 211 4332 4691 4546 93 -145 108 C ATOM 338 CG1 VAL A 211 -5.381 31.450 -19.334 1.00 41.18 C ANISOU 338 CG1 VAL A 211 5011 5385 5250 78 -235 134 C ATOM 339 CG2 VAL A 211 -3.187 32.390 -18.593 1.00 37.81 C ANISOU 339 CG2 VAL A 211 4610 4944 4814 78 -139 56 C ATOM 340 N LYS A 212 -2.393 34.688 -21.180 1.00 39.67 N ANISOU 340 N LYS A 212 4900 5180 4993 161 -17 24 N ATOM 341 CA LYS A 212 -1.543 35.876 -21.218 1.00 35.27 C ANISOU 341 CA LYS A 212 4358 4620 4422 177 66 -2 C ATOM 342 C LYS A 212 -2.105 36.894 -22.198 1.00 35.18 C ANISOU 342 C LYS A 212 4356 4617 4394 208 108 21 C ATOM 343 O LYS A 212 -1.814 38.080 -22.102 1.00 36.52 O ANISOU 343 O LYS A 212 4531 4789 4555 221 183 18 O ATOM 344 CB LYS A 212 -0.115 35.516 -21.632 1.00 39.47 C ANISOU 344 CB LYS A 212 4918 5138 4942 183 61 -63 C ATOM 345 CG LYS A 212 0.682 34.797 -20.564 1.00 48.24 C ANISOU 345 CG LYS A 212 6022 6239 6067 153 40 -92 C ATOM 346 CD LYS A 212 2.156 34.679 -20.939 1.00 57.28 C ANISOU 346 CD LYS A 212 7194 7371 7199 162 50 -153 C ATOM 347 CE LYS A 212 2.883 36.011 -20.781 1.00 65.22 C ANISOU 347 CE LYS A 212 8211 8377 8194 174 141 -170 C ATOM 348 NZ LYS A 212 4.370 35.858 -20.826 1.00 68.00 N ANISOU 348 NZ LYS A 212 8582 8716 8537 175 153 -228 N ATOM 349 N GLY A 213 -2.911 36.424 -23.146 1.00 29.99 N ANISOU 349 N GLY A 213 3700 3964 3732 221 58 45 N ATOM 350 CA GLY A 213 -3.441 37.288 -24.182 1.00 29.24 C ANISOU 350 CA GLY A 213 3613 3875 3620 252 90 65 C ATOM 351 C GLY A 213 -4.620 38.120 -23.719 1.00 36.27 C ANISOU 351 C GLY A 213 4480 4780 4520 251 127 120 C ATOM 352 O GLY A 213 -4.959 38.131 -22.534 1.00 37.32 O ANISOU 352 O GLY A 213 4590 4918 4672 228 137 139 O ATOM 353 N SER A 214 -5.239 38.835 -24.653 1.00 34.80 N ANISOU 353 N SER A 214 4301 4601 4321 278 150 144 N ATOM 354 CA SER A 214 -6.455 39.566 -24.349 1.00 33.77 C ANISOU 354 CA SER A 214 4148 4485 4199 280 179 198 C ATOM 355 C SER A 214 -7.510 38.566 -23.936 1.00 36.45 C ANISOU 355 C SER A 214 4462 4830 4558 259 109 236 C ATOM 356 O SER A 214 -7.572 37.459 -24.467 1.00 48.90 O ANISOU 356 O SER A 214 6043 6401 6135 255 36 229 O ATOM 357 CB SER A 214 -6.931 40.350 -25.565 1.00 34.60 C ANISOU 357 CB SER A 214 4267 4595 4286 313 204 215 C ATOM 358 OG SER A 214 -5.888 41.177 -26.049 1.00 39.17 O ANISOU 358 OG SER A 214 4872 5167 4845 333 262 177 O ATOM 359 N LEU A 215 -8.323 38.945 -22.966 1.00 28.02 N ANISOU 359 N LEU A 215 3366 3772 3507 244 131 275 N ATOM 360 CA LEU A 215 -9.372 38.072 -22.465 1.00 24.05 C ANISOU 360 CA LEU A 215 2836 3277 3024 222 71 315 C ATOM 361 C LEU A 215 -10.639 38.888 -22.360 1.00 27.20 C ANISOU 361 C LEU A 215 3214 3692 3429 230 102 371 C ATOM 362 O LEU A 215 -10.615 40.019 -21.868 1.00 22.74 O ANISOU 362 O LEU A 215 2645 3132 2863 236 176 379 O ATOM 363 CB LEU A 215 -9.012 37.532 -21.077 1.00 25.26 C ANISOU 363 CB LEU A 215 2972 3428 3196 188 60 305 C ATOM 364 CG LEU A 215 -7.803 36.602 -20.943 1.00 26.34 C ANISOU 364 CG LEU A 215 3126 3550 3333 174 23 252 C ATOM 365 CD1 LEU A 215 -7.598 36.236 -19.501 1.00 21.64 C ANISOU 365 CD1 LEU A 215 2512 2954 2757 141 22 249 C ATOM 366 CD2 LEU A 215 -8.000 35.349 -21.770 1.00 30.97 C ANISOU 366 CD2 LEU A 215 3718 4131 3917 174 -65 248 C ATOM 367 N THR A 216 -11.744 38.319 -22.822 1.00 23.41 N ANISOU 367 N THR A 216 2720 3220 2955 231 47 411 N ATOM 368 CA THR A 216 -13.015 38.992 -22.700 1.00 22.62 C ANISOU 368 CA THR A 216 2598 3136 2863 237 71 466 C ATOM 369 C THR A 216 -13.504 38.776 -21.290 1.00 27.99 C ANISOU 369 C THR A 216 3246 3823 3565 207 69 492 C ATOM 370 O THR A 216 -13.019 37.888 -20.580 1.00 27.04 O ANISOU 370 O THR A 216 3121 3697 3456 181 32 472 O ATOM 371 CB THR A 216 -14.060 38.437 -23.686 1.00 35.51 C ANISOU 371 CB THR A 216 4226 4773 4495 247 9 502 C ATOM 372 OG1 THR A 216 -14.391 37.090 -23.330 1.00 32.53 O ANISOU 372 OG1 THR A 216 3834 4395 4133 221 -72 510 O ATOM 373 CG2 THR A 216 -13.526 38.470 -25.114 1.00 33.52 C ANISOU 373 CG2 THR A 216 4006 4512 4219 275 0 473 C ATOM 374 N SER A 217 -14.471 39.590 -20.896 1.00 22.64 N ANISOU 374 N SER A 217 2547 3160 2895 211 109 538 N ATOM 375 CA SER A 217 -15.034 39.534 -19.568 1.00 22.60 C ANISOU 375 CA SER A 217 2510 3164 2911 185 116 567 C ATOM 376 C SER A 217 -15.543 38.144 -19.222 1.00 25.02 C ANISOU 376 C SER A 217 2798 3473 3235 158 30 584 C ATOM 377 O SER A 217 -15.365 37.676 -18.092 1.00 25.13 O ANISOU 377 O SER A 217 2797 3487 3264 129 20 580 O ATOM 378 CB SER A 217 -16.176 40.532 -19.466 1.00 22.73 C ANISOU 378 CB SER A 217 2507 3198 2932 198 161 619 C ATOM 379 OG SER A 217 -16.852 40.368 -18.243 1.00 32.25 O ANISOU 379 OG SER A 217 3681 4415 4159 173 159 652 O ATOM 380 N TYR A 218 -16.183 37.488 -20.189 1.00 28.55 N ANISOU 380 N TYR A 218 3246 3921 3679 166 -31 603 N ATOM 381 CA TYR A 218 -16.731 36.156 -19.953 1.00 25.05 C ANISOU 381 CA TYR A 218 2786 3480 3252 141 -116 621 C ATOM 382 C TYR A 218 -15.648 35.081 -19.823 1.00 24.01 C ANISOU 382 C TYR A 218 2670 3332 3120 123 -165 572 C ATOM 383 O TYR A 218 -15.761 34.183 -18.988 1.00 22.88 O ANISOU 383 O TYR A 218 2510 3190 2994 94 -211 577 O ATOM 384 CB TYR A 218 -17.747 35.750 -21.022 1.00 24.89 C ANISOU 384 CB TYR A 218 2763 3465 3230 154 -170 656 C ATOM 385 CG TYR A 218 -18.502 34.504 -20.620 1.00 23.55 C ANISOU 385 CG TYR A 218 2569 3300 3079 127 -252 685 C ATOM 386 CD1 TYR A 218 -19.142 34.437 -19.393 1.00 27.84 C ANISOU 386 CD1 TYR A 218 3079 3855 3642 101 -248 719 C ATOM 387 CD2 TYR A 218 -18.556 33.389 -21.447 1.00 27.72 C ANISOU 387 CD2 TYR A 218 3107 3820 3604 125 -333 679 C ATOM 388 CE1 TYR A 218 -19.829 33.313 -19.000 1.00 25.23 C ANISOU 388 CE1 TYR A 218 2727 3530 3330 75 -321 746 C ATOM 389 CE2 TYR A 218 -19.248 32.250 -21.064 1.00 23.62 C ANISOU 389 CE2 TYR A 218 2567 3304 3102 99 -408 706 C ATOM 390 CZ TYR A 218 -19.886 32.223 -19.834 1.00 33.29 C ANISOU 390 CZ TYR A 218 3758 4542 4348 74 -402 740 C ATOM 391 OH TYR A 218 -20.574 31.105 -19.414 1.00 32.48 O ANISOU 391 OH TYR A 218 3633 4444 4263 47 -476 768 O ATOM 392 N GLN A 219 -14.607 35.170 -20.643 1.00 22.77 N ANISOU 392 N GLN A 219 2546 3161 2944 142 -156 524 N ATOM 393 CA GLN A 219 -13.490 34.241 -20.517 1.00 26.43 C ANISOU 393 CA GLN A 219 3026 3610 3407 127 -195 474 C ATOM 394 C GLN A 219 -12.887 34.317 -19.119 1.00 22.75 C ANISOU 394 C GLN A 219 2550 3142 2953 102 -164 457 C ATOM 395 O GLN A 219 -12.622 33.290 -18.508 1.00 29.02 O ANISOU 395 O GLN A 219 3336 3930 3759 75 -215 445 O ATOM 396 CB GLN A 219 -12.425 34.500 -21.585 1.00 27.92 C ANISOU 396 CB GLN A 219 3252 3786 3572 153 -178 426 C ATOM 397 CG GLN A 219 -12.855 34.094 -22.987 1.00 26.96 C ANISOU 397 CG GLN A 219 3144 3661 3437 175 -227 434 C ATOM 398 CD GLN A 219 -11.879 34.549 -24.050 1.00 29.77 C ANISOU 398 CD GLN A 219 3536 4007 3769 203 -198 390 C ATOM 399 OE1 GLN A 219 -11.346 35.651 -23.985 1.00 35.64 O ANISOU 399 OE1 GLN A 219 4289 4750 4502 218 -122 374 O ATOM 400 NE2 GLN A 219 -11.643 33.701 -25.036 1.00 30.09 N ANISOU 400 NE2 GLN A 219 3595 4038 3799 212 -259 370 N ATOM 401 N LYS A 220 -12.691 35.530 -18.612 1.00 25.97 N ANISOU 401 N LYS A 220 2956 3555 3358 109 -81 458 N ATOM 402 CA LYS A 220 -12.203 35.714 -17.246 1.00 27.75 C ANISOU 402 CA LYS A 220 3170 3779 3595 86 -45 446 C ATOM 403 C LYS A 220 -13.142 35.067 -16.239 1.00 27.02 C ANISOU 403 C LYS A 220 3042 3697 3525 56 -84 487 C ATOM 404 O LYS A 220 -12.698 34.427 -15.284 1.00 27.15 O ANISOU 404 O LYS A 220 3052 3710 3554 28 -105 471 O ATOM 405 CB LYS A 220 -12.078 37.196 -16.893 1.00 22.31 C ANISOU 405 CB LYS A 220 2482 3096 2900 100 50 449 C ATOM 406 CG LYS A 220 -11.032 37.948 -17.666 1.00 23.25 C ANISOU 406 CG LYS A 220 2633 3204 2996 127 100 406 C ATOM 407 CD LYS A 220 -10.856 39.362 -17.116 1.00 25.97 C ANISOU 407 CD LYS A 220 2978 3554 3338 136 193 409 C ATOM 408 CE LYS A 220 -10.139 40.261 -18.126 1.00 35.38 C ANISOU 408 CE LYS A 220 4199 4737 4505 168 244 379 C ATOM 409 NZ LYS A 220 -9.442 41.401 -17.466 1.00 38.37 N ANISOU 409 NZ LYS A 220 4586 5115 4880 172 328 360 N ATOM 410 N PHE A 221 -14.440 35.253 -16.460 1.00 23.14 N ANISOU 410 N PHE A 221 2531 3221 3039 62 -93 540 N ATOM 411 CA PHE A 221 -15.470 34.778 -15.549 1.00 22.43 C ANISOU 411 CA PHE A 221 2407 3144 2971 36 -124 586 C ATOM 412 C PHE A 221 -15.383 33.260 -15.437 1.00 24.57 C ANISOU 412 C PHE A 221 2674 3409 3254 10 -215 577 C ATOM 413 O PHE A 221 -15.420 32.704 -14.343 1.00 22.70 O ANISOU 413 O PHE A 221 2419 3174 3033 -20 -235 583 O ATOM 414 CB PHE A 221 -16.847 35.200 -16.071 1.00 23.54 C ANISOU 414 CB PHE A 221 2530 3301 3114 52 -124 642 C ATOM 415 CG PHE A 221 -17.977 34.928 -15.116 1.00 22.78 C ANISOU 415 CG PHE A 221 2395 3221 3038 28 -142 694 C ATOM 416 CD1 PHE A 221 -18.297 35.841 -14.119 1.00 24.48 C ANISOU 416 CD1 PHE A 221 2592 3448 3261 23 -77 716 C ATOM 417 CD2 PHE A 221 -18.731 33.765 -15.225 1.00 22.94 C ANISOU 417 CD2 PHE A 221 2400 3245 3071 11 -225 721 C ATOM 418 CE1 PHE A 221 -19.342 35.596 -13.241 1.00 32.12 C ANISOU 418 CE1 PHE A 221 3525 4432 4248 2 -93 764 C ATOM 419 CE2 PHE A 221 -19.774 33.511 -14.350 1.00 25.70 C ANISOU 419 CE2 PHE A 221 2713 3610 3440 -11 -243 770 C ATOM 420 CZ PHE A 221 -20.084 34.429 -13.357 1.00 22.98 C ANISOU 420 CZ PHE A 221 2350 3278 3102 -16 -176 791 C ATOM 421 N GLN A 222 -15.259 32.595 -16.578 1.00 23.58 N ANISOU 421 N GLN A 222 2567 3274 3117 23 -269 563 N ATOM 422 CA GLN A 222 -15.116 31.143 -16.613 1.00 24.27 C ANISOU 422 CA GLN A 222 2654 3352 3213 1 -358 551 C ATOM 423 C GLN A 222 -13.822 30.671 -15.948 1.00 24.09 C ANISOU 423 C GLN A 222 2645 3315 3192 -17 -361 498 C ATOM 424 O GLN A 222 -13.829 29.700 -15.204 1.00 24.77 O ANISOU 424 O GLN A 222 2718 3399 3294 -47 -412 499 O ATOM 425 CB GLN A 222 -15.152 30.647 -18.052 1.00 22.84 C ANISOU 425 CB GLN A 222 2496 3165 3019 23 -408 542 C ATOM 426 CG GLN A 222 -16.488 30.821 -18.757 1.00 23.03 C ANISOU 426 CG GLN A 222 2505 3201 3043 37 -426 595 C ATOM 427 CD GLN A 222 -16.384 30.471 -20.225 1.00 34.39 C ANISOU 427 CD GLN A 222 3970 4632 4466 61 -466 581 C ATOM 428 OE1 GLN A 222 -15.715 31.168 -20.985 1.00 28.75 O ANISOU 428 OE1 GLN A 222 3282 3911 3732 88 -423 551 O ATOM 429 NE2 GLN A 222 -17.035 29.384 -20.631 1.00 33.30 N ANISOU 429 NE2 GLN A 222 3826 4493 4334 52 -549 602 N ATOM 430 N LEU A 223 -12.711 31.346 -16.231 1.00 23.71 N ANISOU 430 N LEU A 223 2623 3257 3128 1 -307 453 N ATOM 431 CA LEU A 223 -11.438 30.975 -15.632 1.00 21.98 C ANISOU 431 CA LEU A 223 2418 3023 2910 -15 -305 402 C ATOM 432 C LEU A 223 -11.520 31.121 -14.121 1.00 24.06 C ANISOU 432 C LEU A 223 2657 3293 3191 -44 -278 415 C ATOM 433 O LEU A 223 -11.020 30.273 -13.384 1.00 24.17 O ANISOU 433 O LEU A 223 2667 3300 3216 -71 -315 395 O ATOM 434 CB LEU A 223 -10.303 31.838 -16.173 1.00 21.84 C ANISOU 434 CB LEU A 223 2430 2995 2871 10 -243 356 C ATOM 435 CG LEU A 223 -9.807 31.508 -17.582 1.00 31.67 C ANISOU 435 CG LEU A 223 3705 4231 4099 35 -274 326 C ATOM 436 CD1 LEU A 223 -9.142 32.730 -18.203 1.00 32.01 C ANISOU 436 CD1 LEU A 223 3772 4271 4121 66 -197 301 C ATOM 437 CD2 LEU A 223 -8.858 30.319 -17.577 1.00 21.83 C ANISOU 437 CD2 LEU A 223 2474 2968 2854 20 -334 281 C ATOM 438 N PHE A 224 -12.166 32.189 -13.665 1.00 23.21 N ANISOU 438 N PHE A 224 2533 3199 3085 -38 -215 449 N ATOM 439 CA PHE A 224 -12.313 32.432 -12.239 1.00 23.40 C ANISOU 439 CA PHE A 224 2534 3231 3125 -63 -184 464 C ATOM 440 C PHE A 224 -13.102 31.313 -11.562 1.00 24.54 C ANISOU 440 C PHE A 224 2651 3382 3290 -95 -255 496 C ATOM 441 O PHE A 224 -12.743 30.866 -10.478 1.00 29.21 O ANISOU 441 O PHE A 224 3233 3972 3895 -124 -264 486 O ATOM 442 CB PHE A 224 -12.987 33.776 -11.978 1.00 21.77 C ANISOU 442 CB PHE A 224 2315 3040 2917 -49 -106 499 C ATOM 443 CG PHE A 224 -12.165 34.968 -12.394 1.00 22.35 C ANISOU 443 CG PHE A 224 2414 3107 2972 -21 -28 467 C ATOM 444 CD1 PHE A 224 -10.788 34.903 -12.436 1.00 21.83 C ANISOU 444 CD1 PHE A 224 2373 3024 2897 -21 -15 410 C ATOM 445 CD2 PHE A 224 -12.781 36.172 -12.710 1.00 23.61 C ANISOU 445 CD2 PHE A 224 2570 3278 3125 3 33 496 C ATOM 446 CE1 PHE A 224 -10.036 36.002 -12.810 1.00 22.85 C ANISOU 446 CE1 PHE A 224 2525 3148 3009 3 56 382 C ATOM 447 CE2 PHE A 224 -12.039 37.273 -13.081 1.00 21.62 C ANISOU 447 CE2 PHE A 224 2341 3019 2855 27 104 468 C ATOM 448 CZ PHE A 224 -10.668 37.187 -13.133 1.00 25.27 C ANISOU 448 CZ PHE A 224 2828 3465 3308 27 116 411 C ATOM 449 N GLU A 225 -14.175 30.858 -12.198 1.00 22.07 N ANISOU 449 N GLU A 225 2326 3078 2981 -91 -305 536 N ATOM 450 CA GLU A 225 -14.988 29.812 -11.601 1.00 28.23 C ANISOU 450 CA GLU A 225 3079 3865 3780 -121 -373 570 C ATOM 451 C GLU A 225 -14.292 28.451 -11.661 1.00 29.26 C ANISOU 451 C GLU A 225 3221 3980 3915 -140 -450 535 C ATOM 452 O GLU A 225 -14.416 27.647 -10.738 1.00 28.20 O ANISOU 452 O GLU A 225 3070 3848 3798 -172 -491 543 O ATOM 453 CB GLU A 225 -16.367 29.724 -12.273 1.00 42.51 C ANISOU 453 CB GLU A 225 4871 5689 5592 -110 -406 624 C ATOM 454 CG GLU A 225 -16.983 31.064 -12.654 1.00 66.25 C ANISOU 454 CG GLU A 225 7874 8707 8589 -82 -335 652 C ATOM 455 CD GLU A 225 -17.266 31.971 -11.463 1.00 80.64 C ANISOU 455 CD GLU A 225 9675 10543 10421 -91 -266 674 C ATOM 456 OE1 GLU A 225 -17.989 31.532 -10.540 1.00 83.28 O ANISOU 456 OE1 GLU A 225 9980 10889 10773 -117 -290 709 O ATOM 457 OE2 GLU A 225 -16.781 33.130 -11.463 1.00 83.34 O ANISOU 457 OE2 GLU A 225 10029 10883 10751 -72 -187 657 O ATOM 458 N GLN A 226 -13.557 28.195 -12.739 1.00 22.13 N ANISOU 458 N GLN A 226 2349 3063 2997 -120 -471 496 N ATOM 459 CA GLN A 226 -13.044 26.850 -12.983 1.00 24.55 C ANISOU 459 CA GLN A 226 2666 3355 3306 -135 -552 468 C ATOM 460 C GLN A 226 -11.687 26.586 -12.353 1.00 23.87 C ANISOU 460 C GLN A 226 2595 3253 3220 -149 -543 413 C ATOM 461 O GLN A 226 -11.344 25.442 -12.066 1.00 27.36 O ANISOU 461 O GLN A 226 3038 3685 3671 -172 -607 396 O ATOM 462 CB GLN A 226 -12.997 26.544 -14.483 1.00 23.56 C ANISOU 462 CB GLN A 226 2565 3222 3165 -108 -590 455 C ATOM 463 CG GLN A 226 -14.373 26.535 -15.136 1.00 23.18 C ANISOU 463 CG GLN A 226 2502 3187 3119 -98 -618 510 C ATOM 464 CD GLN A 226 -14.327 26.130 -16.597 1.00 27.75 C ANISOU 464 CD GLN A 226 3105 3758 3682 -73 -662 497 C ATOM 465 OE1 GLN A 226 -13.596 25.214 -16.975 1.00 22.94 O ANISOU 465 OE1 GLN A 226 2515 3133 3069 -77 -715 459 O ATOM 466 NE2 GLN A 226 -15.128 26.797 -17.423 1.00 26.49 N ANISOU 466 NE2 GLN A 226 2944 3608 3514 -48 -642 529 N ATOM 467 N VAL A 227 -10.916 27.639 -12.129 1.00 23.12 N ANISOU 467 N VAL A 227 2514 3156 3116 -137 -463 387 N ATOM 468 CA VAL A 227 -9.558 27.462 -11.638 1.00 21.48 C ANISOU 468 CA VAL A 227 2322 2933 2906 -147 -450 332 C ATOM 469 C VAL A 227 -9.437 27.920 -10.198 1.00 24.50 C ANISOU 469 C VAL A 227 2688 3321 3302 -171 -402 338 C ATOM 470 O VAL A 227 -8.711 27.318 -9.412 1.00 21.88 O ANISOU 470 O VAL A 227 2355 2979 2978 -195 -421 311 O ATOM 471 CB VAL A 227 -8.541 28.198 -12.532 1.00 28.95 C ANISOU 471 CB VAL A 227 3301 3869 3830 -115 -401 288 C ATOM 472 CG1 VAL A 227 -7.128 28.125 -11.943 1.00 21.14 C ANISOU 472 CG1 VAL A 227 2328 2865 2840 -126 -380 233 C ATOM 473 CG2 VAL A 227 -8.577 27.608 -13.920 1.00 21.55 C ANISOU 473 CG2 VAL A 227 2383 2925 2881 -94 -455 278 C ATOM 474 N ILE A 228 -10.158 28.976 -9.840 1.00 21.34 N ANISOU 474 N ILE A 228 2271 2936 2902 -163 -341 375 N ATOM 475 CA ILE A 228 -10.109 29.461 -8.468 1.00 22.60 C ANISOU 475 CA ILE A 228 2413 3101 3073 -185 -293 383 C ATOM 476 C ILE A 228 -11.480 29.682 -7.842 1.00 25.53 C ANISOU 476 C ILE A 228 2751 3493 3457 -196 -289 445 C ATOM 477 O ILE A 228 -11.609 30.440 -6.889 1.00 23.49 O ANISOU 477 O ILE A 228 2478 3242 3204 -204 -231 458 O ATOM 478 CB ILE A 228 -9.314 30.766 -8.381 1.00 25.42 C ANISOU 478 CB ILE A 228 2787 3455 3417 -166 -201 356 C ATOM 479 CG1 ILE A 228 -10.059 31.887 -9.105 1.00 23.44 C ANISOU 479 CG1 ILE A 228 2536 3216 3154 -134 -150 387 C ATOM 480 CG2 ILE A 228 -7.925 30.571 -8.953 1.00 22.51 C ANISOU 480 CG2 ILE A 228 2450 3067 3034 -155 -203 295 C ATOM 481 CD1 ILE A 228 -9.578 33.268 -8.730 1.00 22.55 C ANISOU 481 CD1 ILE A 228 2431 3105 3033 -120 -55 375 C ATOM 482 N GLY A 229 -12.499 29.015 -8.371 1.00 27.86 N ANISOU 482 N GLY A 229 3032 3796 3758 -197 -350 481 N ATOM 483 CA GLY A 229 -13.850 29.189 -7.872 1.00 26.78 C ANISOU 483 CA GLY A 229 2862 3679 3633 -206 -349 542 C ATOM 484 C GLY A 229 -14.284 28.111 -6.898 1.00 30.22 C ANISOU 484 C GLY A 229 3273 4119 4090 -244 -410 563 C ATOM 485 O GLY A 229 -15.037 28.383 -5.966 1.00 32.69 O ANISOU 485 O GLY A 229 3558 4447 4415 -260 -389 601 O ATOM 486 N ARG A 230 -13.820 26.883 -7.115 1.00 24.63 N ANISOU 486 N ARG A 230 2535 3573 3251 162 -99 378 N ATOM 487 CA ARG A 230 -14.161 25.779 -6.220 1.00 30.23 C ANISOU 487 CA ARG A 230 3197 4277 4011 106 -117 404 C ATOM 488 C ARG A 230 -12.955 25.208 -5.486 1.00 29.80 C ANISOU 488 C ARG A 230 3184 4157 3981 57 -123 392 C ATOM 489 O ARG A 230 -11.919 24.932 -6.085 1.00 34.49 O ANISOU 489 O ARG A 230 3813 4709 4584 41 -150 349 O ATOM 490 CB ARG A 230 -14.919 24.684 -6.962 1.00 35.49 C ANISOU 490 CB ARG A 230 3788 4972 4725 74 -174 397 C ATOM 491 CG ARG A 230 -16.410 24.987 -7.064 1.00 50.58 C ANISOU 491 CG ARG A 230 5640 6954 6625 105 -161 433 C ATOM 492 CD ARG A 230 -17.077 24.207 -8.176 1.00 52.29 C ANISOU 492 CD ARG A 230 5793 7201 6875 90 -216 415 C ATOM 493 NE ARG A 230 -16.596 24.622 -9.489 1.00 53.25 N ANISOU 493 NE ARG A 230 5941 7317 6974 120 -232 369 N ATOM 494 CZ ARG A 230 -15.610 24.019 -10.141 1.00 56.96 C ANISOU 494 CZ ARG A 230 6433 7743 7467 91 -273 322 C ATOM 495 NH1 ARG A 230 -15.000 22.976 -9.595 1.00 62.28 N ANISOU 495 NH1 ARG A 230 7105 8372 8187 32 -301 315 N ATOM 496 NH2 ARG A 230 -15.237 24.458 -11.336 1.00 53.52 N ANISOU 496 NH2 ARG A 230 6019 7309 7009 121 -285 282 N ATOM 497 N LYS A 231 -13.120 25.034 -4.178 1.00 33.28 N ANISOU 497 N LYS A 231 3621 4592 4433 33 -98 432 N ATOM 498 CA LYS A 231 -12.049 24.618 -3.288 1.00 34.50 C ANISOU 498 CA LYS A 231 3816 4686 4606 -10 -95 429 C ATOM 499 C LYS A 231 -11.283 23.405 -3.788 1.00 27.80 C ANISOU 499 C LYS A 231 2960 3794 3810 -66 -156 390 C ATOM 500 O LYS A 231 -10.057 23.422 -3.843 1.00 29.59 O ANISOU 500 O LYS A 231 3242 3968 4033 -77 -159 359 O ATOM 501 CB LYS A 231 -12.602 24.338 -1.889 1.00 34.59 C ANISOU 501 CB LYS A 231 3802 4708 4634 -37 -72 480 C ATOM 502 CG LYS A 231 -11.543 23.974 -0.856 1.00 34.90 C ANISOU 502 CG LYS A 231 3885 4687 4690 -82 -64 482 C ATOM 503 CD LYS A 231 -12.090 24.149 0.547 1.00 34.45 C ANISOU 503 CD LYS A 231 3816 4646 4628 -89 -22 536 C ATOM 504 CE LYS A 231 -11.133 23.601 1.576 1.00 41.54 C ANISOU 504 CE LYS A 231 4746 5486 5552 -142 -22 540 C ATOM 505 NZ LYS A 231 -11.727 23.650 2.942 1.00 43.23 N ANISOU 505 NZ LYS A 231 4941 5719 5765 -156 14 593 N ATOM 506 N ASP A 232 -11.995 22.352 -4.161 1.00 24.19 N ANISOU 506 N ASP A 232 2432 3358 3400 -100 -204 390 N ATOM 507 CA ASP A 232 -11.311 21.096 -4.478 1.00 25.49 C ANISOU 507 CA ASP A 232 2585 3479 3619 -158 -263 357 C ATOM 508 C ASP A 232 -10.513 21.147 -5.787 1.00 24.24 C ANISOU 508 C ASP A 232 2457 3300 3454 -143 -293 299 C ATOM 509 O ASP A 232 -9.391 20.640 -5.845 1.00 30.73 O ANISOU 509 O ASP A 232 3312 4069 4297 -175 -317 265 O ATOM 510 CB ASP A 232 -12.267 19.890 -4.422 1.00 25.76 C ANISOU 510 CB ASP A 232 2539 3539 3709 -204 -310 375 C ATOM 511 CG ASP A 232 -13.539 20.097 -5.246 1.00 42.17 C ANISOU 511 CG ASP A 232 4561 5684 5777 -171 -318 385 C ATOM 512 OD1 ASP A 232 -13.641 21.104 -5.978 1.00 43.80 O ANISOU 512 OD1 ASP A 232 4791 5915 5938 -113 -293 372 O ATOM 513 OD2 ASP A 232 -14.442 19.241 -5.160 1.00 42.99 O ANISOU 513 OD2 ASP A 232 4597 5816 5920 -203 -350 407 O ATOM 514 N ASP A 233 -11.069 21.767 -6.827 1.00 21.17 N ANISOU 514 N ASP A 233 2055 2954 3035 -96 -291 286 N ATOM 515 CA ASP A 233 -10.328 21.904 -8.084 1.00 22.47 C ANISOU 515 CA ASP A 233 2248 3103 3187 -79 -317 232 C ATOM 516 C ASP A 233 -9.160 22.886 -7.928 1.00 28.13 C ANISOU 516 C ASP A 233 3049 3783 3857 -50 -277 215 C ATOM 517 O ASP A 233 -8.086 22.691 -8.501 1.00 21.63 O ANISOU 517 O ASP A 233 2261 2921 3036 -61 -301 171 O ATOM 518 CB ASP A 233 -11.245 22.314 -9.236 1.00 27.45 C ANISOU 518 CB ASP A 233 2843 3790 3798 -37 -326 225 C ATOM 519 CG ASP A 233 -12.020 21.139 -9.811 1.00 40.52 C ANISOU 519 CG ASP A 233 4422 5468 5505 -72 -384 219 C ATOM 520 OD1 ASP A 233 -11.654 19.978 -9.531 1.00 40.48 O ANISOU 520 OD1 ASP A 233 4399 5428 5552 -129 -425 209 O ATOM 521 OD2 ASP A 233 -12.994 21.375 -10.556 1.00 47.50 O ANISOU 521 OD2 ASP A 233 5265 6404 6378 -43 -390 225 O ATOM 522 N PHE A 234 -9.372 23.931 -7.135 1.00 25.68 N ANISOU 522 N PHE A 234 2770 3485 3503 -15 -219 251 N ATOM 523 CA PHE A 234 -8.296 24.842 -6.771 1.00 19.35 C ANISOU 523 CA PHE A 234 2048 2646 2657 8 -178 243 C ATOM 524 C PHE A 234 -7.127 24.110 -6.090 1.00 22.65 C ANISOU 524 C PHE A 234 2500 3000 3108 -45 -192 230 C ATOM 525 O PHE A 234 -5.969 24.310 -6.453 1.00 19.61 O ANISOU 525 O PHE A 234 2168 2576 2707 -44 -196 194 O ATOM 526 CB PHE A 234 -8.832 25.955 -5.874 1.00 18.24 C ANISOU 526 CB PHE A 234 1928 2530 2471 49 -115 290 C ATOM 527 CG PHE A 234 -7.762 26.793 -5.233 1.00 24.91 C ANISOU 527 CG PHE A 234 2856 3333 3277 64 -72 290 C ATOM 528 CD1 PHE A 234 -7.088 27.762 -5.960 1.00 21.72 C ANISOU 528 CD1 PHE A 234 2508 2921 2823 106 -57 262 C ATOM 529 CD2 PHE A 234 -7.435 26.617 -3.897 1.00 24.97 C ANISOU 529 CD2 PHE A 234 2882 3309 3295 34 -47 319 C ATOM 530 CE1 PHE A 234 -6.105 28.542 -5.371 1.00 17.26 C ANISOU 530 CE1 PHE A 234 2019 2317 2220 119 -18 264 C ATOM 531 CE2 PHE A 234 -6.452 27.395 -3.303 1.00 20.48 C ANISOU 531 CE2 PHE A 234 2389 2702 2690 47 -7 320 C ATOM 532 CZ PHE A 234 -5.792 28.360 -4.044 1.00 18.23 C ANISOU 532 CZ PHE A 234 2162 2410 2356 90 7 293 C ATOM 533 N LEU A 235 -7.430 23.252 -5.119 1.00 21.03 N ANISOU 533 N LEU A 235 2260 2785 2947 -92 -201 259 N ATOM 534 CA LEU A 235 -6.388 22.474 -4.452 1.00 25.46 C ANISOU 534 CA LEU A 235 2847 3286 3543 -146 -217 248 C ATOM 535 C LEU A 235 -5.703 21.498 -5.403 1.00 22.62 C ANISOU 535 C LEU A 235 2477 2896 3222 -179 -279 195 C ATOM 536 O LEU A 235 -4.483 21.360 -5.385 1.00 23.29 O ANISOU 536 O LEU A 235 2610 2930 3308 -196 -286 166 O ATOM 537 CB LEU A 235 -6.936 21.733 -3.224 1.00 23.39 C ANISOU 537 CB LEU A 235 2545 3022 3320 -192 -217 292 C ATOM 538 CG LEU A 235 -7.336 22.669 -2.078 1.00 29.19 C ANISOU 538 CG LEU A 235 3301 3773 4016 -166 -152 341 C ATOM 539 CD1 LEU A 235 -7.730 21.897 -0.830 1.00 29.02 C ANISOU 539 CD1 LEU A 235 3245 3747 4035 -216 -153 382 C ATOM 540 CD2 LEU A 235 -6.214 23.654 -1.766 1.00 24.43 C ANISOU 540 CD2 LEU A 235 2784 3133 3367 -140 -109 332 C ATOM 541 N LYS A 236 -6.490 20.831 -6.236 1.00 23.41 N ANISOU 541 N LYS A 236 2514 3029 3351 -187 -323 184 N ATOM 542 CA LYS A 236 -5.954 19.842 -7.163 1.00 22.32 C ANISOU 542 CA LYS A 236 2361 2867 3254 -218 -385 134 C ATOM 543 C LYS A 236 -4.983 20.480 -8.148 1.00 25.89 C ANISOU 543 C LYS A 236 2866 3303 3667 -185 -384 86 C ATOM 544 O LYS A 236 -3.933 19.918 -8.454 1.00 33.29 O ANISOU 544 O LYS A 236 3826 4197 4624 -212 -415 46 O ATOM 545 CB LYS A 236 -7.096 19.142 -7.902 1.00 25.65 C ANISOU 545 CB LYS A 236 2706 3333 3708 -226 -429 134 C ATOM 546 CG LYS A 236 -6.673 17.983 -8.792 1.00 36.52 C ANISOU 546 CG LYS A 236 4057 4686 5132 -263 -498 85 C ATOM 547 CD LYS A 236 -7.883 17.108 -9.128 1.00 52.95 C ANISOU 547 CD LYS A 236 6057 6806 7255 -284 -540 99 C ATOM 548 CE LYS A 236 -7.495 15.833 -9.874 1.00 63.54 C ANISOU 548 CE LYS A 236 7372 8121 8651 -328 -612 54 C ATOM 549 NZ LYS A 236 -7.041 16.102 -11.270 1.00 68.72 N ANISOU 549 NZ LYS A 236 8043 8782 9285 -297 -632 0 N ATOM 550 N LEU A 237 -5.327 21.665 -8.634 1.00 28.98 N ANISOU 550 N LEU A 237 3276 3732 4002 -127 -349 91 N ATOM 551 CA LEU A 237 -4.448 22.392 -9.542 1.00 22.39 C ANISOU 551 CA LEU A 237 2494 2888 3126 -93 -344 50 C ATOM 552 C LEU A 237 -3.225 22.967 -8.815 1.00 23.10 C ANISOU 552 C LEU A 237 2661 2929 3187 -92 -307 49 C ATOM 553 O LEU A 237 -2.110 22.914 -9.327 1.00 23.52 O ANISOU 553 O LEU A 237 2754 2949 3233 -98 -324 7 O ATOM 554 CB LEU A 237 -5.226 23.502 -10.251 1.00 22.61 C ANISOU 554 CB LEU A 237 2519 2969 3103 -32 -317 58 C ATOM 555 CG LEU A 237 -6.352 23.029 -11.182 1.00 27.68 C ANISOU 555 CG LEU A 237 3089 3661 3767 -27 -354 53 C ATOM 556 CD1 LEU A 237 -6.849 24.182 -12.038 1.00 26.77 C ANISOU 556 CD1 LEU A 237 2982 3592 3598 34 -331 51 C ATOM 557 CD2 LEU A 237 -5.886 21.895 -12.065 1.00 24.59 C ANISOU 557 CD2 LEU A 237 2673 3250 3421 -65 -419 4 C ATOM 558 N SER A 238 -3.443 23.501 -7.615 1.00 20.36 N ANISOU 558 N SER A 238 2334 2580 2823 -86 -259 95 N ATOM 559 CA SER A 238 -2.367 24.104 -6.828 1.00 23.67 C ANISOU 559 CA SER A 238 2827 2955 3213 -84 -220 100 C ATOM 560 C SER A 238 -1.277 23.108 -6.456 1.00 24.81 C ANISOU 560 C SER A 238 2986 3040 3399 -140 -251 77 C ATOM 561 O SER A 238 -0.097 23.452 -6.439 1.00 25.60 O ANISOU 561 O SER A 238 3148 3102 3478 -139 -240 55 O ATOM 562 CB SER A 238 -2.924 24.767 -5.566 1.00 17.39 C ANISOU 562 CB SER A 238 2041 2170 2395 -70 -164 156 C ATOM 563 OG SER A 238 -3.638 25.944 -5.906 1.00 25.25 O ANISOU 563 OG SER A 238 3044 3212 3338 -10 -128 173 O ATOM 564 N THR A 239 -1.686 21.880 -6.157 1.00 22.03 N ANISOU 564 N THR A 239 2579 2682 3109 -190 -289 83 N ATOM 565 CA THR A 239 -0.766 20.809 -5.795 1.00 19.66 C ANISOU 565 CA THR A 239 2286 2327 2857 -246 -324 62 C ATOM 566 C THR A 239 -0.269 20.056 -7.033 1.00 29.42 C ANISOU 566 C THR A 239 3506 3552 4119 -260 -383 4 C ATOM 567 O THR A 239 0.399 19.024 -6.920 1.00 29.69 O ANISOU 567 O THR A 239 3536 3545 4200 -307 -423 -20 O ATOM 568 CB THR A 239 -1.421 19.799 -4.808 1.00 20.04 C ANISOU 568 CB THR A 239 2283 2371 2962 -297 -340 97 C ATOM 569 OG1 THR A 239 -2.617 19.254 -5.379 1.00 27.37 O ANISOU 569 OG1 THR A 239 3138 3344 3917 -299 -374 103 O ATOM 570 CG2 THR A 239 -1.778 20.481 -3.482 1.00 23.43 C ANISOU 570 CG2 THR A 239 2731 2805 3367 -289 -282 153 C ATOM 571 N ASN A 240 -0.585 20.572 -8.215 1.00 21.40 N ANISOU 571 N ASN A 240 2483 2575 3074 -218 -390 -20 N ATOM 572 CA ASN A 240 -0.218 19.873 -9.432 1.00 17.05 C ANISOU 572 CA ASN A 240 1913 2020 2546 -229 -446 -75 C ATOM 573 C ASN A 240 0.999 20.466 -10.089 1.00 22.68 C ANISOU 573 C ASN A 240 2687 2711 3219 -207 -440 -117 C ATOM 574 O ASN A 240 1.127 21.693 -10.206 1.00 22.31 O ANISOU 574 O ASN A 240 2684 2681 3112 -161 -397 -109 O ATOM 575 CB ASN A 240 -1.356 19.863 -10.447 1.00 21.68 C ANISOU 575 CB ASN A 240 2442 2663 3132 -205 -468 -80 C ATOM 576 CG ASN A 240 -0.977 19.136 -11.720 1.00 25.49 C ANISOU 576 CG ASN A 240 2904 3142 3638 -216 -527 -137 C ATOM 577 OD1 ASN A 240 -0.651 19.761 -12.731 1.00 26.16 O ANISOU 577 OD1 ASN A 240 3011 3243 3684 -180 -526 -169 O ATOM 578 ND2 ASN A 240 -0.990 17.802 -11.670 1.00 22.87 N ANISOU 578 ND2 ASN A 240 2530 2788 3369 -266 -579 -151 N ATOM 579 N ILE A 241 1.872 19.577 -10.547 1.00 19.24 N ANISOU 579 N ILE A 241 2253 2241 2817 -240 -487 -163 N ATOM 580 CA ILE A 241 3.140 19.954 -11.155 1.00 22.86 C ANISOU 580 CA ILE A 241 2767 2675 3245 -227 -489 -207 C ATOM 581 C ILE A 241 2.963 21.010 -12.250 1.00 23.84 C ANISOU 581 C ILE A 241 2906 2843 3311 -172 -474 -224 C ATOM 582 O ILE A 241 3.741 21.963 -12.324 1.00 22.60 O ANISOU 582 O ILE A 241 2809 2677 3102 -144 -441 -231 O ATOM 583 CB ILE A 241 3.914 18.704 -11.666 1.00 21.51 C ANISOU 583 CB ILE A 241 2581 2469 3124 -269 -550 -259 C ATOM 584 CG1 ILE A 241 5.255 19.099 -12.281 1.00 28.65 C ANISOU 584 CG1 ILE A 241 3541 3350 3994 -256 -551 -305 C ATOM 585 CG2 ILE A 241 3.070 17.886 -12.661 1.00 16.98 C ANISOU 585 CG2 ILE A 241 1936 1927 2587 -276 -604 -282 C ATOM 586 CD1 ILE A 241 6.125 17.905 -12.670 1.00 32.92 C ANISOU 586 CD1 ILE A 241 4073 3853 4583 -297 -608 -355 C ATOM 587 N PHE A 242 1.927 20.857 -13.071 1.00 24.41 N ANISOU 587 N PHE A 242 2923 2961 3392 -157 -496 -227 N ATOM 588 CA PHE A 242 1.634 21.825 -14.133 1.00 23.09 C ANISOU 588 CA PHE A 242 2763 2839 3173 -105 -485 -241 C ATOM 589 C PHE A 242 0.585 22.855 -13.735 1.00 28.02 C ANISOU 589 C PHE A 242 3384 3504 3760 -64 -435 -190 C ATOM 590 O PHE A 242 0.718 24.038 -14.046 1.00 34.09 O ANISOU 590 O PHE A 242 4193 4291 4469 -19 -401 -187 O ATOM 591 CB PHE A 242 1.176 21.119 -15.403 1.00 18.56 C ANISOU 591 CB PHE A 242 2133 2293 2625 -109 -540 -279 C ATOM 592 CG PHE A 242 2.092 20.022 -15.848 1.00 26.86 C ANISOU 592 CG PHE A 242 3181 3309 3718 -148 -593 -331 C ATOM 593 CD1 PHE A 242 3.448 20.272 -16.044 1.00 30.20 C ANISOU 593 CD1 PHE A 242 3661 3699 4116 -147 -590 -366 C ATOM 594 CD2 PHE A 242 1.604 18.747 -16.081 1.00 29.59 C ANISOU 594 CD2 PHE A 242 3465 3653 4126 -185 -646 -345 C ATOM 595 CE1 PHE A 242 4.299 19.267 -16.455 1.00 29.04 C ANISOU 595 CE1 PHE A 242 3509 3519 4006 -182 -639 -415 C ATOM 596 CE2 PHE A 242 2.450 17.735 -16.495 1.00 33.82 C ANISOU 596 CE2 PHE A 242 3997 4154 4699 -220 -697 -394 C ATOM 597 CZ PHE A 242 3.802 17.993 -16.681 1.00 32.45 C ANISOU 597 CZ PHE A 242 3881 3949 4501 -217 -693 -429 C ATOM 598 N GLY A 243 -0.457 22.407 -13.046 1.00 24.52 N ANISOU 598 N GLY A 243 2892 3075 3350 -80 -433 -151 N ATOM 599 CA GLY A 243 -1.584 23.270 -12.735 1.00 21.59 C ANISOU 599 CA GLY A 243 2507 2748 2948 -42 -392 -104 C ATOM 600 C GLY A 243 -1.265 24.486 -11.883 1.00 22.46 C ANISOU 600 C GLY A 243 2679 2849 3005 -11 -329 -71 C ATOM 601 O GLY A 243 -1.951 25.508 -11.967 1.00 23.21 O ANISOU 601 O GLY A 243 2780 2982 3057 35 -293 -46 O ATOM 602 N ASN A 244 -0.224 24.384 -11.063 1.00 16.27 N ANISOU 602 N ASN A 244 1944 2015 2225 -36 -315 -71 N ATOM 603 CA ASN A 244 0.082 25.451 -10.120 1.00 16.92 C ANISOU 603 CA ASN A 244 2084 2083 2260 -12 -256 -37 C ATOM 604 C ASN A 244 0.418 26.761 -10.831 1.00 20.00 C ANISOU 604 C ASN A 244 2526 2491 2583 42 -228 -49 C ATOM 605 O ASN A 244 0.156 27.838 -10.305 1.00 30.37 O ANISOU 605 O ASN A 244 3871 3817 3851 78 -179 -15 O ATOM 606 CB ASN A 244 1.168 25.023 -9.119 1.00 16.05 C ANISOU 606 CB ASN A 244 2016 1914 2170 -53 -249 -36 C ATOM 607 CG ASN A 244 2.575 25.127 -9.686 1.00 18.31 C ANISOU 607 CG ASN A 244 2356 2164 2436 -57 -262 -82 C ATOM 608 OD1 ASN A 244 3.204 26.178 -9.617 1.00 19.48 O ANISOU 608 OD1 ASN A 244 2567 2305 2531 -26 -226 -79 O ATOM 609 ND2 ASN A 244 3.077 24.032 -10.232 1.00 14.91 N ANISOU 609 ND2 ASN A 244 1901 1713 2050 -94 -315 -123 N ATOM 610 N TYR A 245 0.967 26.658 -12.036 1.00 14.70 N ANISOU 610 N TYR A 245 1859 1823 1904 47 -262 -98 N ATOM 611 CA TYR A 245 1.280 27.834 -12.845 1.00 19.67 C ANISOU 611 CA TYR A 245 2531 2472 2469 96 -244 -113 C ATOM 612 C TYR A 245 0.009 28.523 -13.355 1.00 22.36 C ANISOU 612 C TYR A 245 2838 2871 2785 141 -230 -92 C ATOM 613 O TYR A 245 -0.069 29.753 -13.378 1.00 22.86 O ANISOU 613 O TYR A 245 2941 2951 2793 187 -191 -75 O ATOM 614 CB TYR A 245 2.165 27.457 -14.035 1.00 20.06 C ANISOU 614 CB TYR A 245 2589 2514 2521 87 -287 -172 C ATOM 615 CG TYR A 245 3.571 27.017 -13.676 1.00 26.08 C ANISOU 615 CG TYR A 245 3395 3220 3293 52 -297 -197 C ATOM 616 CD1 TYR A 245 4.591 27.941 -13.533 1.00 24.69 C ANISOU 616 CD1 TYR A 245 3294 3023 3066 70 -266 -200 C ATOM 617 CD2 TYR A 245 3.883 25.673 -13.514 1.00 28.50 C ANISOU 617 CD2 TYR A 245 3671 3497 3662 0 -338 -218 C ATOM 618 CE1 TYR A 245 5.881 27.539 -13.225 1.00 27.36 C ANISOU 618 CE1 TYR A 245 3671 3311 3412 38 -275 -223 C ATOM 619 CE2 TYR A 245 5.167 25.267 -13.204 1.00 27.80 C ANISOU 619 CE2 TYR A 245 3622 3358 3583 -31 -348 -242 C ATOM 620 CZ TYR A 245 6.161 26.206 -13.058 1.00 30.09 C ANISOU 620 CZ TYR A 245 3984 3628 3820 -12 -315 -244 C ATOM 621 OH TYR A 245 7.443 25.814 -12.746 1.00 34.65 O ANISOU 621 OH TYR A 245 4602 4158 4407 -42 -324 -266 O ATOM 622 N LEU A 246 -0.971 27.725 -13.778 1.00 17.41 N ANISOU 622 N LEU A 246 2140 2275 2201 128 -264 -93 N ATOM 623 CA LEU A 246 -2.265 28.243 -14.213 1.00 19.21 C ANISOU 623 CA LEU A 246 2328 2559 2413 167 -254 -71 C ATOM 624 C LEU A 246 -2.988 28.927 -13.055 1.00 27.18 C ANISOU 624 C LEU A 246 3344 3580 3404 188 -202 -15 C ATOM 625 O LEU A 246 -3.608 29.979 -13.238 1.00 25.94 O ANISOU 625 O LEU A 246 3196 3458 3203 237 -171 6 O ATOM 626 CB LEU A 246 -3.135 27.124 -14.791 1.00 18.90 C ANISOU 626 CB LEU A 246 2208 2546 2428 141 -303 -82 C ATOM 627 CG LEU A 246 -4.452 27.585 -15.422 1.00 27.88 C ANISOU 627 CG LEU A 246 3299 3744 3550 179 -299 -65 C ATOM 628 CD1 LEU A 246 -4.213 28.622 -16.508 1.00 16.29 C ANISOU 628 CD1 LEU A 246 1863 2299 2026 226 -293 -88 C ATOM 629 CD2 LEU A 246 -5.260 26.403 -15.958 1.00 25.32 C ANISOU 629 CD2 LEU A 246 2897 3442 3282 149 -350 -75 C ATOM 630 N VAL A 247 -2.902 28.339 -11.865 1.00 15.66 N ANISOU 630 N VAL A 247 1882 2091 1978 151 -192 11 N ATOM 631 CA VAL A 247 -3.490 28.956 -10.682 1.00 15.75 C ANISOU 631 CA VAL A 247 1903 2110 1972 169 -141 63 C ATOM 632 C VAL A 247 -2.860 30.310 -10.338 1.00 20.63 C ANISOU 632 C VAL A 247 2598 2713 2525 209 -91 75 C ATOM 633 O VAL A 247 -3.567 31.281 -10.052 1.00 21.33 O ANISOU 633 O VAL A 247 2696 2833 2577 253 -51 107 O ATOM 634 CB VAL A 247 -3.373 28.059 -9.447 1.00 18.37 C ANISOU 634 CB VAL A 247 2221 2407 2350 118 -141 86 C ATOM 635 CG1 VAL A 247 -3.784 28.840 -8.212 1.00 18.25 C ANISOU 635 CG1 VAL A 247 2229 2397 2308 138 -84 138 C ATOM 636 CG2 VAL A 247 -4.232 26.817 -9.609 1.00 18.76 C ANISOU 636 CG2 VAL A 247 2191 2477 2462 81 -185 88 C ATOM 637 N GLN A 248 -1.531 30.367 -10.350 1.00 15.54 N ANISOU 637 N GLN A 248 2012 2024 1868 195 -93 48 N ATOM 638 CA GLN A 248 -0.824 31.618 -10.083 1.00 19.85 C ANISOU 638 CA GLN A 248 2636 2554 2353 230 -50 55 C ATOM 639 C GLN A 248 -1.219 32.669 -11.111 1.00 23.44 C ANISOU 639 C GLN A 248 3100 3050 2758 286 -43 47 C ATOM 640 O GLN A 248 -1.424 33.835 -10.793 1.00 27.13 O ANISOU 640 O GLN A 248 3605 3528 3174 329 0 73 O ATOM 641 CB GLN A 248 0.685 31.396 -10.116 1.00 15.08 C ANISOU 641 CB GLN A 248 2086 1898 1747 202 -62 22 C ATOM 642 CG GLN A 248 1.215 30.548 -8.963 1.00 19.25 C ANISOU 642 CG GLN A 248 2619 2379 2317 150 -61 34 C ATOM 643 CD GLN A 248 2.710 30.287 -9.084 1.00 22.61 C ANISOU 643 CD GLN A 248 3096 2755 2741 123 -77 -1 C ATOM 644 OE1 GLN A 248 3.529 31.194 -8.941 1.00 22.12 O ANISOU 644 OE1 GLN A 248 3102 2673 2630 143 -47 -1 O ATOM 645 NE2 GLN A 248 3.067 29.043 -9.354 1.00 17.22 N ANISOU 645 NE2 GLN A 248 2378 2052 2112 76 -124 -32 N ATOM 646 N SER A 249 -1.347 32.230 -12.351 1.00 20.22 N ANISOU 646 N SER A 249 2656 2665 2363 284 -86 10 N ATOM 647 CA SER A 249 -1.676 33.119 -13.450 1.00 22.41 C ANISOU 647 CA SER A 249 2938 2981 2597 332 -87 -2 C ATOM 648 C SER A 249 -3.124 33.631 -13.374 1.00 21.90 C ANISOU 648 C SER A 249 2833 2967 2522 370 -65 35 C ATOM 649 O SER A 249 -3.400 34.788 -13.684 1.00 27.67 O ANISOU 649 O SER A 249 3590 3722 3202 420 -39 45 O ATOM 650 CB SER A 249 -1.424 32.390 -14.765 1.00 17.57 C ANISOU 650 CB SER A 249 2293 2378 2006 314 -142 -52 C ATOM 651 OG SER A 249 -1.393 33.297 -15.835 1.00 40.54 O ANISOU 651 OG SER A 249 5222 5315 4867 355 -142 -70 O ATOM 652 N VAL A 250 -4.046 32.770 -12.955 1.00 18.49 N ANISOU 652 N VAL A 250 2335 2551 2138 346 -77 55 N ATOM 653 CA VAL A 250 -5.448 33.170 -12.829 1.00 18.41 C ANISOU 653 CA VAL A 250 2282 2591 2122 379 -57 91 C ATOM 654 C VAL A 250 -5.664 34.075 -11.619 1.00 18.75 C ANISOU 654 C VAL A 250 2362 2629 2132 407 0 137 C ATOM 655 O VAL A 250 -6.505 34.973 -11.645 1.00 23.66 O ANISOU 655 O VAL A 250 2981 3289 2721 455 28 162 O ATOM 656 CB VAL A 250 -6.392 31.951 -12.790 1.00 16.58 C ANISOU 656 CB VAL A 250 1966 2381 1951 344 -90 99 C ATOM 657 CG1 VAL A 250 -7.804 32.366 -12.404 1.00 19.39 C ANISOU 657 CG1 VAL A 250 2281 2786 2301 376 -63 143 C ATOM 658 CG2 VAL A 250 -6.398 31.272 -14.130 1.00 16.68 C ANISOU 658 CG2 VAL A 250 1941 2410 1988 330 -144 56 C ATOM 659 N ILE A 251 -4.884 33.859 -10.566 1.00 20.95 N ANISOU 659 N ILE A 251 2679 2862 2420 377 18 147 N ATOM 660 CA ILE A 251 -4.909 34.761 -9.415 1.00 17.47 C ANISOU 660 CA ILE A 251 2283 2411 1944 403 74 187 C ATOM 661 C ILE A 251 -4.433 36.155 -9.812 1.00 20.82 C ANISOU 661 C ILE A 251 2775 2835 2301 454 101 181 C ATOM 662 O ILE A 251 -4.958 37.156 -9.335 1.00 24.00 O ANISOU 662 O ILE A 251 3199 3256 2665 498 143 213 O ATOM 663 CB ILE A 251 -4.028 34.235 -8.264 1.00 22.50 C ANISOU 663 CB ILE A 251 2951 2994 2603 357 85 195 C ATOM 664 CG1 ILE A 251 -4.659 32.987 -7.638 1.00 15.73 C ANISOU 664 CG1 ILE A 251 2027 2141 1809 310 65 212 C ATOM 665 CG2 ILE A 251 -3.772 35.330 -7.223 1.00 17.61 C ANISOU 665 CG2 ILE A 251 2395 2358 1936 387 142 228 C ATOM 666 CD1 ILE A 251 -3.777 32.325 -6.609 1.00 19.23 C ANISOU 666 CD1 ILE A 251 2495 2530 2281 259 68 216 C ATOM 667 N GLY A 252 -3.438 36.218 -10.690 1.00 18.25 N ANISOU 667 N GLY A 252 2485 2489 1960 449 77 141 N ATOM 668 CA GLY A 252 -2.938 37.494 -11.153 1.00 15.00 C ANISOU 668 CA GLY A 252 2138 2078 1485 495 98 134 C ATOM 669 C GLY A 252 -4.020 38.232 -11.910 1.00 26.64 C ANISOU 669 C GLY A 252 3584 3606 2932 546 101 142 C ATOM 670 O GLY A 252 -4.238 39.437 -11.721 1.00 26.14 O ANISOU 670 O GLY A 252 3560 3554 2818 595 138 164 O ATOM 671 N ILE A 253 -4.710 37.501 -12.775 1.00 20.59 N ANISOU 671 N ILE A 253 2750 2874 2201 536 62 125 N ATOM 672 CA ILE A 253 -5.750 38.093 -13.588 1.00 16.02 C ANISOU 672 CA ILE A 253 2138 2348 1600 581 61 131 C ATOM 673 C ILE A 253 -6.900 38.562 -12.706 1.00 22.18 C ANISOU 673 C ILE A 253 2898 3157 2374 611 100 179 C ATOM 674 O ILE A 253 -7.440 39.657 -12.900 1.00 22.64 O ANISOU 674 O ILE A 253 2971 3242 2388 665 125 196 O ATOM 675 CB ILE A 253 -6.229 37.110 -14.665 1.00 20.05 C ANISOU 675 CB ILE A 253 2579 2887 2154 558 9 102 C ATOM 676 CG1 ILE A 253 -5.079 36.815 -15.641 1.00 16.71 C ANISOU 676 CG1 ILE A 253 2182 2441 1728 536 -28 51 C ATOM 677 CG2 ILE A 253 -7.432 37.670 -15.408 1.00 16.68 C ANISOU 677 CG2 ILE A 253 2112 2517 1709 602 9 113 C ATOM 678 CD1 ILE A 253 -5.271 35.521 -16.453 1.00 17.81 C ANISOU 678 CD1 ILE A 253 2255 2591 1922 496 -83 19 C ATOM 679 N SER A 254 -7.250 37.743 -11.718 1.00 22.59 N ANISOU 679 N SER A 254 2915 3201 2469 577 106 202 N ATOM 680 CA SER A 254 -8.291 38.095 -10.756 1.00 23.97 C ANISOU 680 CA SER A 254 3067 3400 2639 601 144 249 C ATOM 681 C SER A 254 -7.995 39.408 -10.042 1.00 26.91 C ANISOU 681 C SER A 254 3511 3758 2954 644 195 273 C ATOM 682 O SER A 254 -8.876 40.246 -9.876 1.00 28.47 O ANISOU 682 O SER A 254 3704 3991 3124 692 225 300 O ATOM 683 CB SER A 254 -8.457 36.998 -9.710 1.00 17.54 C ANISOU 683 CB SER A 254 2215 2571 1877 550 142 268 C ATOM 684 OG SER A 254 -9.536 37.306 -8.850 1.00 27.23 O ANISOU 684 OG SER A 254 3415 3830 3101 573 176 313 O ATOM 685 N LEU A 255 -6.750 39.566 -9.609 1.00 26.56 N ANISOU 685 N LEU A 255 3533 3662 2895 627 206 262 N ATOM 686 CA LEU A 255 -6.326 40.752 -8.884 1.00 27.67 C ANISOU 686 CA LEU A 255 3748 3783 2984 662 253 283 C ATOM 687 C LEU A 255 -6.332 41.952 -9.806 1.00 31.08 C ANISOU 687 C LEU A 255 4215 4234 3360 717 258 272 C ATOM 688 O LEU A 255 -6.492 43.085 -9.361 1.00 37.78 O ANISOU 688 O LEU A 255 5108 5086 4162 763 297 296 O ATOM 689 CB LEU A 255 -4.927 40.550 -8.297 1.00 24.05 C ANISOU 689 CB LEU A 255 3349 3263 2524 625 258 271 C ATOM 690 CG LEU A 255 -4.859 39.555 -7.138 1.00 25.03 C ANISOU 690 CG LEU A 255 3451 3362 2696 574 263 289 C ATOM 691 CD1 LEU A 255 -3.416 39.220 -6.765 1.00 33.32 C ANISOU 691 CD1 LEU A 255 4556 4353 3751 533 258 271 C ATOM 692 CD2 LEU A 255 -5.624 40.075 -5.940 1.00 21.67 C ANISOU 692 CD2 LEU A 255 3026 2951 2258 599 311 337 C ATOM 693 N ALA A 256 -6.163 41.691 -11.098 1.00 24.56 N ANISOU 693 N ALA A 256 3371 3421 2539 712 217 236 N ATOM 694 CA ALA A 256 -6.095 42.752 -12.090 1.00 25.80 C ANISOU 694 CA ALA A 256 3561 3597 2646 759 215 222 C ATOM 695 C ALA A 256 -7.454 43.070 -12.685 1.00 32.84 C ANISOU 695 C ALA A 256 4397 4546 3533 799 212 235 C ATOM 696 O ALA A 256 -7.533 43.822 -13.649 1.00 34.92 O ANISOU 696 O ALA A 256 4676 4831 3762 835 203 222 O ATOM 697 CB ALA A 256 -5.105 42.393 -13.207 1.00 15.61 C ANISOU 697 CB ALA A 256 2285 2290 1357 733 172 175 C ATOM 698 N THR A 257 -8.519 42.503 -12.125 1.00 27.99 N ANISOU 698 N THR A 257 3721 3960 2955 793 218 261 N ATOM 699 CA THR A 257 -9.852 42.710 -12.685 1.00 26.76 C ANISOU 699 CA THR A 257 3506 3861 2800 828 214 274 C ATOM 700 C THR A 257 -10.807 43.304 -11.661 1.00 30.69 C ANISOU 700 C THR A 257 3996 4381 3283 864 259 319 C ATOM 701 O THR A 257 -11.442 42.583 -10.896 1.00 30.57 O ANISOU 701 O THR A 257 3932 4377 3305 842 265 342 O ATOM 702 CB THR A 257 -10.432 41.400 -13.262 1.00 27.08 C ANISOU 702 CB THR A 257 3463 3927 2899 787 170 259 C ATOM 703 OG1 THR A 257 -9.493 40.837 -14.184 1.00 26.25 O ANISOU 703 OG1 THR A 257 3367 3799 2807 753 129 215 O ATOM 704 CG2 THR A 257 -11.747 41.655 -13.994 1.00 22.26 C ANISOU 704 CG2 THR A 257 2795 3376 2285 824 162 269 C ATOM 705 N ASN A 258 -10.907 44.627 -11.657 1.00 43.36 N ANISOU 705 N ASN A 258 5649 5994 4833 921 289 332 N ATOM 706 CA ASN A 258 -11.709 45.335 -10.663 1.00 47.25 C ANISOU 706 CA ASN A 258 6144 6504 5304 962 335 374 C ATOM 707 C ASN A 258 -13.198 45.392 -10.983 1.00 40.24 C ANISOU 707 C ASN A 258 5187 5679 4425 994 334 393 C ATOM 708 O ASN A 258 -13.792 46.464 -11.018 1.00 47.76 O ANISOU 708 O ASN A 258 6154 6656 5337 1052 359 410 O ATOM 709 CB ASN A 258 -11.162 46.746 -10.450 1.00 56.62 C ANISOU 709 CB ASN A 258 7417 7669 6428 1010 368 380 C ATOM 710 CG ASN A 258 -9.890 46.755 -9.625 1.00 72.91 C ANISOU 710 CG ASN A 258 9548 9673 8482 981 385 378 C ATOM 711 OD1 ASN A 258 -8.793 46.926 -10.160 1.00 78.09 O ANISOU 711 OD1 ASN A 258 10255 10296 9120 969 368 350 O ATOM 712 ND2 ASN A 258 -10.028 46.559 -8.313 1.00 76.60 N ANISOU 712 ND2 ASN A 258 10016 10127 8962 969 417 407 N ATOM 713 N ASP A 259 -13.799 44.230 -11.200 1.00 30.75 N ANISOU 713 N ASP A 259 3908 4501 3275 957 306 391 N ATOM 714 CA ASP A 259 -15.226 44.147 -11.473 1.00 24.55 C ANISOU 714 CA ASP A 259 3049 3775 2502 981 303 410 C ATOM 715 C ASP A 259 -15.987 43.934 -10.173 1.00 28.56 C ANISOU 715 C ASP A 259 3527 4300 3026 980 336 451 C ATOM 716 O ASP A 259 -15.398 43.988 -9.096 1.00 33.92 O ANISOU 716 O ASP A 259 4246 4942 3700 966 363 464 O ATOM 717 CB ASP A 259 -15.531 43.050 -12.503 1.00 33.77 C ANISOU 717 CB ASP A 259 4149 4965 3716 943 251 386 C ATOM 718 CG ASP A 259 -15.333 41.635 -11.952 1.00 49.84 C ANISOU 718 CG ASP A 259 6145 6982 5809 876 231 385 C ATOM 719 OD1 ASP A 259 -14.637 41.455 -10.927 1.00 48.71 O ANISOU 719 OD1 ASP A 259 6037 6797 5671 850 251 393 O ATOM 720 OD2 ASP A 259 -15.871 40.689 -12.568 1.00 56.79 O ANISOU 720 OD2 ASP A 259 6959 7888 6732 847 193 375 O ATOM 721 N ASP A 260 -17.290 43.694 -10.271 1.00 35.67 N ANISOU 721 N ASP A 260 4354 5254 3943 994 333 472 N ATOM 722 CA ASP A 260 -18.124 43.553 -9.081 1.00 46.08 C ANISOU 722 CA ASP A 260 5638 6596 5273 997 366 513 C ATOM 723 C ASP A 260 -17.808 42.321 -8.234 1.00 47.26 C ANISOU 723 C ASP A 260 5762 6721 5472 930 357 519 C ATOM 724 O ASP A 260 -18.040 42.318 -7.029 1.00 51.76 O ANISOU 724 O ASP A 260 6332 7292 6044 927 389 550 O ATOM 725 CB ASP A 260 -19.603 43.538 -9.456 1.00 52.83 C ANISOU 725 CB ASP A 260 6417 7519 6136 1026 362 533 C ATOM 726 CG ASP A 260 -20.499 43.770 -8.263 1.00 62.75 C ANISOU 726 CG ASP A 260 7650 8806 7387 1048 403 576 C ATOM 727 OD1 ASP A 260 -20.307 44.799 -7.578 1.00 65.25 O ANISOU 727 OD1 ASP A 260 8021 9109 7660 1089 445 591 O ATOM 728 OD2 ASP A 260 -21.388 42.927 -8.008 1.00 71.78 O ANISOU 728 OD2 ASP A 260 8719 9987 8568 1023 393 596 O ATOM 729 N GLY A 261 -17.291 41.273 -8.863 1.00 48.67 N ANISOU 729 N GLY A 261 5920 6882 5692 877 311 490 N ATOM 730 CA GLY A 261 -17.032 40.032 -8.155 1.00 50.56 C ANISOU 730 CA GLY A 261 6130 7098 5981 811 297 494 C ATOM 731 C GLY A 261 -15.638 39.947 -7.566 1.00 41.99 C ANISOU 731 C GLY A 261 5114 5947 4894 780 304 480 C ATOM 732 O GLY A 261 -15.244 38.909 -7.039 1.00 45.83 O ANISOU 732 O GLY A 261 5584 6407 5422 722 289 479 O ATOM 733 N TYR A 262 -14.893 41.043 -7.658 1.00 33.01 N ANISOU 733 N TYR A 262 4053 4782 3706 817 327 469 N ATOM 734 CA TYR A 262 -13.514 41.084 -7.186 1.00 29.30 C ANISOU 734 CA TYR A 262 3654 4250 3228 791 335 455 C ATOM 735 C TYR A 262 -13.450 40.614 -5.741 1.00 32.47 C ANISOU 735 C TYR A 262 4054 4632 3651 758 361 484 C ATOM 736 O TYR A 262 -12.778 39.641 -5.418 1.00 41.41 O ANISOU 736 O TYR A 262 5183 5729 4821 700 341 473 O ATOM 737 CB TYR A 262 -12.973 42.513 -7.311 1.00 24.11 C ANISOU 737 CB TYR A 262 3077 3576 2507 845 365 451 C ATOM 738 CG TYR A 262 -11.560 42.732 -6.818 1.00 33.54 C ANISOU 738 CG TYR A 262 4352 4708 3684 825 378 438 C ATOM 739 CD1 TYR A 262 -10.491 42.784 -7.708 1.00 38.46 C ANISOU 739 CD1 TYR A 262 5017 5299 4296 814 351 400 C ATOM 740 CD2 TYR A 262 -11.296 42.919 -5.466 1.00 41.34 C ANISOU 740 CD2 TYR A 262 5373 5669 4664 819 417 466 C ATOM 741 CE1 TYR A 262 -9.193 42.997 -7.265 1.00 37.87 C ANISOU 741 CE1 TYR A 262 5016 5168 4204 796 362 389 C ATOM 742 CE2 TYR A 262 -10.003 43.139 -5.013 1.00 48.91 C ANISOU 742 CE2 TYR A 262 6406 6571 5606 801 429 455 C ATOM 743 CZ TYR A 262 -8.955 43.172 -5.915 1.00 46.71 C ANISOU 743 CZ TYR A 262 6168 6262 5318 789 401 418 C ATOM 744 OH TYR A 262 -7.672 43.390 -5.462 1.00 48.24 O ANISOU 744 OH TYR A 262 6435 6400 5494 771 413 409 O ATOM 745 N THR A 263 -14.184 41.307 -4.884 1.00 36.66 N ANISOU 745 N THR A 263 4585 5189 4157 796 404 521 N ATOM 746 CA THR A 263 -14.158 41.064 -3.451 1.00 32.21 C ANISOU 746 CA THR A 263 4024 4609 3603 773 436 552 C ATOM 747 C THR A 263 -14.461 39.612 -3.097 1.00 35.93 C ANISOU 747 C THR A 263 4428 5086 4139 709 407 559 C ATOM 748 O THR A 263 -13.653 38.949 -2.451 1.00 38.04 O ANISOU 748 O THR A 263 4713 5309 4431 658 403 556 O ATOM 749 CB THR A 263 -15.132 42.012 -2.711 1.00 37.36 C ANISOU 749 CB THR A 263 4673 5301 4220 829 484 590 C ATOM 750 OG1 THR A 263 -14.634 43.355 -2.777 1.00 43.49 O ANISOU 750 OG1 THR A 263 5528 6059 4938 883 514 585 O ATOM 751 CG2 THR A 263 -15.277 41.612 -1.249 1.00 33.11 C ANISOU 751 CG2 THR A 263 4124 4756 3699 801 513 624 C ATOM 752 N LYS A 264 -15.623 39.122 -3.517 1.00 40.60 N ANISOU 752 N LYS A 264 4940 5731 4755 710 387 569 N ATOM 753 CA LYS A 264 -15.999 37.740 -3.253 1.00 47.45 C ANISOU 753 CA LYS A 264 5738 6607 5682 649 356 577 C ATOM 754 C LYS A 264 -14.884 36.802 -3.691 1.00 48.45 C ANISOU 754 C LYS A 264 5880 6683 5845 591 314 540 C ATOM 755 O LYS A 264 -14.536 35.858 -2.991 1.00 51.48 O ANISOU 755 O LYS A 264 6251 7041 6269 535 302 546 O ATOM 756 CB LYS A 264 -17.304 37.386 -3.971 1.00 56.84 C ANISOU 756 CB LYS A 264 6846 7860 6890 661 332 585 C ATOM 757 CG LYS A 264 -18.497 38.226 -3.536 1.00 69.02 C ANISOU 757 CG LYS A 264 8366 9459 8401 717 372 622 C ATOM 758 CD LYS A 264 -19.800 37.708 -4.134 1.00 78.48 C ANISOU 758 CD LYS A 264 9475 10720 9624 719 347 633 C ATOM 759 CE LYS A 264 -21.007 38.491 -3.618 1.00 78.76 C ANISOU 759 CE LYS A 264 9484 10813 9629 773 387 672 C ATOM 760 NZ LYS A 264 -21.083 38.484 -2.128 1.00 76.75 N ANISOU 760 NZ LYS A 264 9234 10554 9372 761 426 707 N ATOM 761 N ARG A 265 -14.313 37.097 -4.851 1.00 41.39 N ANISOU 761 N ARG A 265 5016 5775 4936 606 291 503 N ATOM 762 CA ARG A 265 -13.283 36.265 -5.449 1.00 34.37 C ANISOU 762 CA ARG A 265 4139 4843 4078 557 247 463 C ATOM 763 C ARG A 265 -12.032 36.170 -4.564 1.00 34.54 C ANISOU 763 C ARG A 265 4223 4802 4099 525 263 459 C ATOM 764 O ARG A 265 -11.500 35.082 -4.335 1.00 30.81 O ANISOU 764 O ARG A 265 3737 4298 3672 465 234 448 O ATOM 765 CB ARG A 265 -12.939 36.819 -6.834 1.00 34.46 C ANISOU 765 CB ARG A 265 4176 4857 4062 589 227 426 C ATOM 766 CG ARG A 265 -12.823 35.783 -7.928 1.00 32.23 C ANISOU 766 CG ARG A 265 3849 4575 3820 551 168 390 C ATOM 767 CD ARG A 265 -13.039 36.398 -9.317 1.00 29.03 C ANISOU 767 CD ARG A 265 3445 4198 3387 593 151 365 C ATOM 768 NE ARG A 265 -12.243 37.607 -9.521 1.00 26.80 N ANISOU 768 NE ARG A 265 3242 3893 3049 634 177 352 N ATOM 769 CZ ARG A 265 -12.733 38.771 -9.938 1.00 24.03 C ANISOU 769 CZ ARG A 265 2908 3573 2649 695 200 360 C ATOM 770 NH1 ARG A 265 -14.025 38.898 -10.231 1.00 19.95 N ANISOU 770 NH1 ARG A 265 2334 3112 2134 724 201 380 N ATOM 771 NH2 ARG A 265 -11.922 39.809 -10.085 1.00 25.98 N ANISOU 771 NH2 ARG A 265 3230 3794 2847 727 220 349 N ATOM 772 N GLN A 266 -11.571 37.306 -4.055 1.00 34.49 N ANISOU 772 N GLN A 266 4286 4776 4042 563 307 470 N ATOM 773 CA GLN A 266 -10.369 37.325 -3.217 1.00 30.44 C ANISOU 773 CA GLN A 266 3837 4204 3524 536 325 468 C ATOM 774 C GLN A 266 -10.611 36.778 -1.810 1.00 29.85 C ANISOU 774 C GLN A 266 3743 4123 3477 501 346 504 C ATOM 775 O GLN A 266 -9.728 36.159 -1.222 1.00 29.18 O ANISOU 775 O GLN A 266 3680 3990 3415 452 340 498 O ATOM 776 CB GLN A 266 -9.779 38.734 -3.138 1.00 29.66 C ANISOU 776 CB GLN A 266 3821 4086 3360 588 364 467 C ATOM 777 CG GLN A 266 -8.629 38.980 -4.083 1.00 44.34 C ANISOU 777 CG GLN A 266 5735 5910 5201 588 342 425 C ATOM 778 CD GLN A 266 -8.998 38.774 -5.546 1.00 63.02 C ANISOU 778 CD GLN A 266 8062 8308 7576 598 300 395 C ATOM 779 OE1 GLN A 266 -9.827 39.500 -6.114 1.00 58.63 O ANISOU 779 OE1 GLN A 266 7489 7795 6991 649 308 402 O ATOM 780 NE2 GLN A 266 -8.365 37.785 -6.172 1.00 70.89 N ANISOU 780 NE2 GLN A 266 9043 9282 8610 551 254 361 N ATOM 781 N GLU A 267 -11.798 37.015 -1.265 1.00 34.55 N ANISOU 781 N GLU A 267 4295 4766 4067 526 371 540 N ATOM 782 CA GLU A 267 -12.165 36.438 0.025 1.00 43.25 C ANISOU 782 CA GLU A 267 5368 5871 5196 491 389 576 C ATOM 783 C GLU A 267 -12.156 34.916 -0.076 1.00 39.57 C ANISOU 783 C GLU A 267 4842 5396 4796 421 340 567 C ATOM 784 O GLU A 267 -11.631 34.227 0.797 1.00 41.21 O ANISOU 784 O GLU A 267 5056 5568 5033 371 338 576 O ATOM 785 CB GLU A 267 -13.561 36.912 0.451 1.00 53.83 C ANISOU 785 CB GLU A 267 6661 7273 6519 532 419 615 C ATOM 786 CG GLU A 267 -13.954 36.531 1.878 1.00 60.98 C ANISOU 786 CG GLU A 267 7542 8184 7442 505 445 655 C ATOM 787 CD GLU A 267 -13.270 37.401 2.930 1.00 71.90 C ANISOU 787 CD GLU A 267 9000 9533 8786 523 496 671 C ATOM 788 OE1 GLU A 267 -12.805 38.510 2.581 1.00 75.08 O ANISOU 788 OE1 GLU A 267 9466 9921 9138 572 518 657 O ATOM 789 OE2 GLU A 267 -13.202 36.976 4.106 1.00 72.19 O ANISOU 789 OE2 GLU A 267 9032 9557 8840 487 513 697 O ATOM 790 N LYS A 268 -12.748 34.411 -1.156 1.00 30.36 N ANISOU 790 N LYS A 268 3621 4261 3652 420 299 549 N ATOM 791 CA LYS A 268 -12.855 32.984 -1.429 1.00 31.00 C ANISOU 791 CA LYS A 268 3642 4340 3796 358 247 538 C ATOM 792 C LYS A 268 -11.477 32.352 -1.461 1.00 35.09 C ANISOU 792 C LYS A 268 4202 4792 4338 310 221 506 C ATOM 793 O LYS A 268 -11.249 31.287 -0.889 1.00 41.85 O ANISOU 793 O LYS A 268 5034 5625 5242 250 199 511 O ATOM 794 CB LYS A 268 -13.509 32.792 -2.785 1.00 30.89 C ANISOU 794 CB LYS A 268 3581 4366 3792 375 209 516 C ATOM 795 CG LYS A 268 -14.402 31.589 -2.915 1.00 40.17 C ANISOU 795 CG LYS A 268 4669 5573 5021 334 169 526 C ATOM 796 CD LYS A 268 -15.122 31.663 -4.248 1.00 41.81 C ANISOU 796 CD LYS A 268 4835 5824 5225 363 140 508 C ATOM 797 CE LYS A 268 -16.164 30.590 -4.397 1.00 41.88 C ANISOU 797 CE LYS A 268 4756 5874 5283 329 103 523 C ATOM 798 NZ LYS A 268 -16.845 30.749 -5.707 1.00 46.63 N ANISOU 798 NZ LYS A 268 5323 6518 5879 360 78 506 N ATOM 799 N LEU A 269 -10.556 33.028 -2.134 1.00 29.51 N ANISOU 799 N LEU A 269 3558 4057 3598 335 223 474 N ATOM 800 CA LEU A 269 -9.203 32.530 -2.287 1.00 33.60 C ANISOU 800 CA LEU A 269 4120 4515 4133 294 199 440 C ATOM 801 C LEU A 269 -8.533 32.453 -0.921 1.00 29.42 C ANISOU 801 C LEU A 269 3629 3942 3607 264 229 462 C ATOM 802 O LEU A 269 -7.850 31.482 -0.601 1.00 27.31 O ANISOU 802 O LEU A 269 3360 3634 3381 207 203 451 O ATOM 803 CB LEU A 269 -8.423 33.454 -3.221 1.00 36.18 C ANISOU 803 CB LEU A 269 4509 4826 4414 335 203 406 C ATOM 804 CG LEU A 269 -7.292 32.815 -4.017 1.00 47.93 C ANISOU 804 CG LEU A 269 6017 6271 5922 300 159 358 C ATOM 805 CD1 LEU A 269 -7.815 31.618 -4.769 1.00 49.66 C ANISOU 805 CD1 LEU A 269 6161 6510 6195 265 104 340 C ATOM 806 CD2 LEU A 269 -6.687 33.831 -4.974 1.00 53.33 C ANISOU 806 CD2 LEU A 269 6757 6951 6555 345 164 329 C ATOM 807 N LYS A 270 -8.753 33.479 -0.110 1.00 25.29 N ANISOU 807 N LYS A 270 3141 3428 3041 303 283 493 N ATOM 808 CA LYS A 270 -8.179 33.525 1.227 1.00 29.92 C ANISOU 808 CA LYS A 270 3766 3977 3625 279 316 517 C ATOM 809 C LYS A 270 -8.727 32.399 2.091 1.00 33.68 C ANISOU 809 C LYS A 270 4181 4462 4155 225 303 544 C ATOM 810 O LYS A 270 -7.992 31.799 2.881 1.00 32.99 O ANISOU 810 O LYS A 270 4111 4329 4093 176 301 548 O ATOM 811 CB LYS A 270 -8.435 34.884 1.881 1.00 24.66 C ANISOU 811 CB LYS A 270 3145 3325 2899 337 376 546 C ATOM 812 CG LYS A 270 -7.972 34.981 3.326 1.00 31.61 C ANISOU 812 CG LYS A 270 4062 4172 3775 315 414 575 C ATOM 813 CD LYS A 270 -9.067 34.595 4.310 1.00 33.65 C ANISOU 813 CD LYS A 270 4261 4470 4055 302 431 618 C ATOM 814 CE LYS A 270 -10.165 35.649 4.361 1.00 34.77 C ANISOU 814 CE LYS A 270 4391 4667 4152 369 469 644 C ATOM 815 NZ LYS A 270 -11.253 35.286 5.332 1.00 30.82 N ANISOU 815 NZ LYS A 270 3830 4209 3671 357 486 686 N ATOM 816 N ASN A 271 -10.018 32.115 1.933 1.00 31.79 N ANISOU 816 N ASN A 271 3868 4279 3931 233 294 564 N ATOM 817 CA ASN A 271 -10.667 31.051 2.696 1.00 29.23 C ANISOU 817 CA ASN A 271 3480 3971 3657 183 279 592 C ATOM 818 C ASN A 271 -10.186 29.665 2.317 1.00 24.53 C ANISOU 818 C ASN A 271 2854 3344 3123 117 220 566 C ATOM 819 O ASN A 271 -10.003 28.817 3.189 1.00 30.19 O ANISOU 819 O ASN A 271 3554 4039 3879 62 211 583 O ATOM 820 CB ASN A 271 -12.195 31.132 2.569 1.00 29.84 C ANISOU 820 CB ASN A 271 3485 4120 3733 211 283 620 C ATOM 821 CG ASN A 271 -12.786 32.236 3.422 1.00 31.51 C ANISOU 821 CG ASN A 271 3714 4361 3896 260 343 658 C ATOM 822 OD1 ASN A 271 -12.163 32.673 4.382 1.00 34.19 O ANISOU 822 OD1 ASN A 271 4106 4669 4215 259 380 671 O ATOM 823 ND2 ASN A 271 -13.980 32.705 3.067 1.00 32.93 N ANISOU 823 ND2 ASN A 271 3851 4603 4056 306 354 674 N ATOM 824 N PHE A 272 -9.995 29.433 1.018 1.00 26.65 N ANISOU 824 N PHE A 272 3114 3612 3399 122 179 526 N ATOM 825 CA PHE A 272 -9.518 28.137 0.541 1.00 28.83 C ANISOU 825 CA PHE A 272 3362 3859 3732 63 121 497 C ATOM 826 C PHE A 272 -8.129 27.850 1.099 1.00 32.09 C ANISOU 826 C PHE A 272 3834 4203 4157 24 120 482 C ATOM 827 O PHE A 272 -7.859 26.771 1.627 1.00 34.32 O ANISOU 827 O PHE A 272 4094 4458 4489 -36 93 485 O ATOM 828 CB PHE A 272 -9.448 28.098 -0.987 1.00 25.35 C ANISOU 828 CB PHE A 272 2913 3429 3291 83 82 453 C ATOM 829 CG PHE A 272 -10.786 28.213 -1.671 1.00 27.51 C ANISOU 829 CG PHE A 272 3124 3769 3561 115 73 464 C ATOM 830 CD1 PHE A 272 -11.964 27.977 -0.977 1.00 23.09 C ANISOU 830 CD1 PHE A 272 2505 3253 3014 109 84 508 C ATOM 831 CD2 PHE A 272 -10.852 28.509 -3.028 1.00 22.35 C ANISOU 831 CD2 PHE A 272 2468 3133 2892 147 50 430 C ATOM 832 CE1 PHE A 272 -13.179 28.061 -1.612 1.00 28.16 C ANISOU 832 CE1 PHE A 272 3090 3956 3654 137 75 518 C ATOM 833 CE2 PHE A 272 -12.062 28.592 -3.674 1.00 23.34 C ANISOU 833 CE2 PHE A 272 2535 3318 3015 175 41 440 C ATOM 834 CZ PHE A 272 -13.231 28.369 -2.966 1.00 33.73 C ANISOU 834 CZ PHE A 272 3794 4677 4344 170 53 484 C ATOM 835 N ILE A 273 -7.253 28.836 0.967 1.00 29.28 N ANISOU 835 N ILE A 273 3553 3820 3753 59 150 465 N ATOM 836 CA ILE A 273 -5.867 28.704 1.373 1.00 26.07 C ANISOU 836 CA ILE A 273 3208 3348 3349 29 152 448 C ATOM 837 C ILE A 273 -5.745 28.606 2.892 1.00 27.03 C ANISOU 837 C ILE A 273 3343 3449 3478 -1 185 487 C ATOM 838 O ILE A 273 -5.062 27.725 3.413 1.00 27.81 O ANISOU 838 O ILE A 273 3445 3504 3617 -57 164 483 O ATOM 839 CB ILE A 273 -5.034 29.877 0.834 1.00 26.06 C ANISOU 839 CB ILE A 273 3283 3328 3289 77 177 424 C ATOM 840 CG1 ILE A 273 -4.893 29.764 -0.695 1.00 25.35 C ANISOU 840 CG1 ILE A 273 3183 3248 3200 92 135 378 C ATOM 841 CG2 ILE A 273 -3.680 29.916 1.505 1.00 29.19 C ANISOU 841 CG2 ILE A 273 3749 3662 3681 50 191 417 C ATOM 842 CD1 ILE A 273 -4.464 31.046 -1.396 1.00 24.37 C ANISOU 842 CD1 ILE A 273 3120 3128 3014 151 159 360 C ATOM 843 N SER A 274 -6.411 29.504 3.605 1.00 22.77 N ANISOU 843 N SER A 274 2810 2939 2900 38 236 525 N ATOM 844 CA SER A 274 -6.370 29.463 5.058 1.00 31.40 C ANISOU 844 CA SER A 274 3915 4019 3998 13 270 564 C ATOM 845 C SER A 274 -6.725 28.074 5.565 1.00 34.83 C ANISOU 845 C SER A 274 4285 4452 4498 -55 233 578 C ATOM 846 O SER A 274 -6.061 27.543 6.447 1.00 38.54 O ANISOU 846 O SER A 274 4772 4879 4993 -103 234 587 O ATOM 847 CB SER A 274 -7.324 30.492 5.661 1.00 33.05 C ANISOU 847 CB SER A 274 4121 4274 4162 64 323 604 C ATOM 848 OG SER A 274 -6.830 31.801 5.479 1.00 36.47 O ANISOU 848 OG SER A 274 4626 4697 4534 120 362 595 O ATOM 849 N SER A 275 -7.766 27.484 4.989 1.00 31.86 N ANISOU 849 N SER A 275 3835 4122 4150 -58 201 581 N ATOM 850 CA SER A 275 -8.277 26.209 5.467 1.00 24.05 C ANISOU 850 CA SER A 275 2778 3140 3220 -119 166 599 C ATOM 851 C SER A 275 -7.307 25.067 5.221 1.00 27.15 C ANISOU 851 C SER A 275 3175 3478 3665 -180 114 567 C ATOM 852 O SER A 275 -7.386 24.038 5.885 1.00 32.07 O ANISOU 852 O SER A 275 3761 4087 4337 -239 90 583 O ATOM 853 CB SER A 275 -9.645 25.895 4.833 1.00 22.38 C ANISOU 853 CB SER A 275 2487 2993 3024 -106 142 609 C ATOM 854 OG SER A 275 -9.504 25.446 3.490 1.00 27.29 O ANISOU 854 OG SER A 275 3092 3613 3664 -107 92 566 O ATOM 855 N GLN A 276 -6.397 25.241 4.268 1.00 28.21 N ANISOU 855 N GLN A 276 3351 3580 3788 -167 96 521 N ATOM 856 CA GLN A 276 -5.426 24.191 3.952 1.00 27.15 C ANISOU 856 CA GLN A 276 3222 3393 3700 -220 46 486 C ATOM 857 C GLN A 276 -3.977 24.675 4.049 1.00 28.61 C ANISOU 857 C GLN A 276 3491 3519 3860 -218 64 461 C ATOM 858 O GLN A 276 -3.082 24.096 3.438 1.00 29.87 O ANISOU 858 O GLN A 276 3667 3640 4044 -243 25 421 O ATOM 859 CB GLN A 276 -5.693 23.626 2.557 1.00 31.65 C ANISOU 859 CB GLN A 276 3751 3981 4294 -218 -9 447 C ATOM 860 CG GLN A 276 -6.953 22.796 2.467 1.00 43.50 C ANISOU 860 CG GLN A 276 5166 5528 5836 -240 -41 467 C ATOM 861 CD GLN A 276 -6.927 21.613 3.409 1.00 52.12 C ANISOU 861 CD GLN A 276 6224 6596 6985 -311 -67 488 C ATOM 862 OE1 GLN A 276 -5.907 20.942 3.546 1.00 55.41 O ANISOU 862 OE1 GLN A 276 6665 6956 7432 -354 -93 466 O ATOM 863 NE2 GLN A 276 -8.052 21.350 4.066 1.00 57.38 N ANISOU 863 NE2 GLN A 276 6834 7305 7665 -323 -60 532 N ATOM 864 N MET A 277 -3.756 25.722 4.835 1.00 26.01 N ANISOU 864 N MET A 277 2614 3862 3408 111 -265 613 N ATOM 865 CA MET A 277 -2.478 26.428 4.875 1.00 25.17 C ANISOU 865 CA MET A 277 2558 3748 3259 133 -238 526 C ATOM 866 C MET A 277 -1.244 25.531 5.035 1.00 27.58 C ANISOU 866 C MET A 277 2884 4009 3588 118 -259 499 C ATOM 867 O MET A 277 -0.290 25.628 4.256 1.00 28.30 O ANISOU 867 O MET A 277 3024 4043 3686 125 -261 427 O ATOM 868 CB MET A 277 -2.499 27.480 5.985 1.00 29.43 C ANISOU 868 CB MET A 277 3085 4374 3724 160 -196 522 C ATOM 869 CG MET A 277 -1.298 28.433 5.974 1.00 32.02 C ANISOU 869 CG MET A 277 3465 4696 4005 185 -168 431 C ATOM 870 SD MET A 277 -1.170 29.306 4.399 1.00 43.46 S ANISOU 870 SD MET A 277 4968 6082 5462 199 -163 361 S ATOM 871 CE MET A 277 -0.136 30.703 4.841 1.00 33.55 C ANISOU 871 CE MET A 277 3753 4857 4138 230 -127 281 C ATOM 872 N THR A 278 -1.262 24.668 6.043 1.00 28.81 N ANISOU 872 N THR A 278 3000 4194 3754 98 -275 558 N ATOM 873 CA THR A 278 -0.095 23.847 6.369 1.00 24.19 C ANISOU 873 CA THR A 278 2429 3575 3186 85 -294 538 C ATOM 874 C THR A 278 0.251 22.899 5.243 1.00 26.07 C ANISOU 874 C THR A 278 2693 3718 3494 68 -340 516 C ATOM 875 O THR A 278 1.402 22.808 4.819 1.00 30.77 O ANISOU 875 O THR A 278 3332 4267 4094 76 -342 449 O ATOM 876 CB THR A 278 -0.330 23.002 7.619 1.00 24.59 C ANISOU 876 CB THR A 278 2426 3676 3242 62 -310 619 C ATOM 877 OG1 THR A 278 -0.482 23.861 8.755 1.00 30.44 O ANISOU 877 OG1 THR A 278 3144 4512 3911 83 -268 631 O ATOM 878 CG2 THR A 278 0.843 22.063 7.843 1.00 24.39 C ANISOU 878 CG2 THR A 278 2416 3607 3245 46 -336 601 C ATOM 879 N ASP A 279 -0.757 22.189 4.759 1.00 27.29 N ANISOU 879 N ASP A 279 2819 3847 3704 46 -378 573 N ATOM 880 CA ASP A 279 -0.541 21.216 3.707 1.00 29.83 C ANISOU 880 CA ASP A 279 3160 4079 4096 30 -430 556 C ATOM 881 C ASP A 279 -0.089 21.881 2.415 1.00 29.03 C ANISOU 881 C ASP A 279 3113 3931 3988 54 -418 469 C ATOM 882 O ASP A 279 0.710 21.321 1.664 1.00 33.70 O ANISOU 882 O ASP A 279 3738 4455 4612 54 -446 418 O ATOM 883 CB ASP A 279 -1.795 20.366 3.497 1.00 42.33 C ANISOU 883 CB ASP A 279 4697 5647 5740 0 -476 640 C ATOM 884 CG ASP A 279 -1.955 19.299 4.573 1.00 57.53 C ANISOU 884 CG ASP A 279 6573 7592 7694 -32 -510 723 C ATOM 885 OD1 ASP A 279 -0.924 18.793 5.065 1.00 61.57 O ANISOU 885 OD1 ASP A 279 7097 8090 8208 -37 -519 705 O ATOM 886 OD2 ASP A 279 -3.107 18.971 4.929 1.00 63.51 O ANISOU 886 OD2 ASP A 279 7278 8381 8471 -53 -527 811 O ATOM 887 N MET A 280 -0.581 23.086 2.164 1.00 27.37 N ANISOU 887 N MET A 280 2910 3757 3732 75 -376 451 N ATOM 888 CA MET A 280 -0.168 23.812 0.975 1.00 27.37 C ANISOU 888 CA MET A 280 2958 3720 3720 96 -363 373 C ATOM 889 C MET A 280 1.284 24.284 1.076 1.00 27.24 C ANISOU 889 C MET A 280 2987 3699 3664 115 -337 295 C ATOM 890 O MET A 280 2.028 24.204 0.104 1.00 29.28 O ANISOU 890 O MET A 280 3284 3905 3936 124 -348 233 O ATOM 891 CB MET A 280 -1.126 24.967 0.670 1.00 21.94 C ANISOU 891 CB MET A 280 2265 3072 2999 111 -330 381 C ATOM 892 CG MET A 280 -2.421 24.502 0.030 1.00 20.55 C ANISOU 892 CG MET A 280 2059 2879 2872 95 -362 437 C ATOM 893 SD MET A 280 -3.518 25.855 -0.450 1.00 34.24 S ANISOU 893 SD MET A 280 3787 4653 4570 115 -325 443 S ATOM 894 CE MET A 280 -2.835 26.371 -2.027 1.00 25.81 C ANISOU 894 CE MET A 280 2777 3526 3502 131 -326 353 C ATOM 895 N CYS A 281 1.690 24.755 2.253 1.00 26.51 N ANISOU 895 N CYS A 281 2887 3663 3524 123 -304 300 N ATOM 896 CA CYS A 281 3.066 25.221 2.440 1.00 23.36 C ANISOU 896 CA CYS A 281 2528 3262 3087 140 -280 230 C ATOM 897 C CYS A 281 4.060 24.073 2.285 1.00 27.98 C ANISOU 897 C CYS A 281 3127 3791 3714 129 -315 210 C ATOM 898 O CYS A 281 5.129 24.249 1.706 1.00 24.77 O ANISOU 898 O CYS A 281 2762 3351 3300 142 -310 142 O ATOM 899 CB CYS A 281 3.253 25.872 3.813 1.00 16.21 C ANISOU 899 CB CYS A 281 1606 2430 2123 150 -244 243 C ATOM 900 SG CYS A 281 2.347 27.416 4.067 1.00 25.41 S ANISOU 900 SG CYS A 281 2763 3664 3228 173 -202 247 S ATOM 901 N LEU A 282 3.697 22.900 2.801 1.00 18.53 N ANISOU 901 N LEU A 282 1894 2586 2562 104 -352 273 N ATOM 902 CA LEU A 282 4.581 21.741 2.755 1.00 22.11 C ANISOU 902 CA LEU A 282 2356 2986 3060 92 -391 261 C ATOM 903 C LEU A 282 4.618 21.106 1.372 1.00 23.03 C ANISOU 903 C LEU A 282 2496 3025 3231 92 -434 228 C ATOM 904 O LEU A 282 5.500 20.309 1.072 1.00 30.51 O ANISOU 904 O LEU A 282 3461 3922 4210 91 -465 196 O ATOM 905 CB LEU A 282 4.177 20.700 3.811 1.00 17.88 C ANISOU 905 CB LEU A 282 1771 2468 2555 63 -421 344 C ATOM 906 CG LEU A 282 4.282 21.141 5.279 1.00 15.31 C ANISOU 906 CG LEU A 282 1419 2223 2175 64 -384 378 C ATOM 907 CD1 LEU A 282 3.485 20.204 6.191 1.00 12.54 C ANISOU 907 CD1 LEU A 282 1009 1900 1854 32 -414 477 C ATOM 908 CD2 LEU A 282 5.737 21.234 5.741 1.00 11.72 C ANISOU 908 CD2 LEU A 282 993 1768 1691 76 -366 323 C ATOM 909 N ASP A 283 3.661 21.465 0.524 1.00 27.01 N ANISOU 909 N ASP A 283 2997 3521 3743 94 -437 234 N ATOM 910 CA ASP A 283 3.567 20.850 -0.792 1.00 20.46 C ANISOU 910 CA ASP A 283 2184 2623 2965 94 -482 207 C ATOM 911 C ASP A 283 4.591 21.458 -1.734 1.00 22.94 C ANISOU 911 C ASP A 283 2550 2916 3252 122 -463 115 C ATOM 912 O ASP A 283 4.870 22.657 -1.700 1.00 27.71 O ANISOU 912 O ASP A 283 3173 3558 3798 140 -412 82 O ATOM 913 CB ASP A 283 2.154 20.983 -1.370 1.00 20.86 C ANISOU 913 CB ASP A 283 2212 2676 3037 85 -494 250 C ATOM 914 CG ASP A 283 1.996 20.279 -2.708 1.00 27.78 C ANISOU 914 CG ASP A 283 3104 3484 3969 86 -547 224 C ATOM 915 OD1 ASP A 283 2.134 20.945 -3.762 1.00 28.89 O ANISOU 915 OD1 ASP A 283 3274 3612 4089 107 -532 167 O ATOM 916 OD2 ASP A 283 1.741 19.054 -2.705 1.00 32.53 O ANISOU 916 OD2 ASP A 283 3685 4041 4633 65 -606 260 O ATOM 917 N LYS A 284 5.138 20.602 -2.581 1.00 27.71 N ANISOU 917 N LYS A 284 3173 3457 3898 126 -507 77 N ATOM 918 CA LYS A 284 6.227 20.941 -3.482 1.00 25.19 C ANISOU 918 CA LYS A 284 2899 3115 3557 153 -497 -8 C ATOM 919 C LYS A 284 5.820 21.991 -4.523 1.00 30.71 C ANISOU 919 C LYS A 284 3616 3826 4225 169 -472 -40 C ATOM 920 O LYS A 284 6.647 22.788 -4.967 1.00 32.63 O ANISOU 920 O LYS A 284 3892 4080 4425 190 -440 -99 O ATOM 921 CB LYS A 284 6.713 19.651 -4.163 1.00 32.67 C ANISOU 921 CB LYS A 284 3855 3994 4563 155 -561 -34 C ATOM 922 CG LYS A 284 7.939 19.799 -5.042 1.00 51.17 C ANISOU 922 CG LYS A 284 6241 6315 6888 184 -557 -120 C ATOM 923 CD LYS A 284 8.311 18.467 -5.687 1.00 58.39 C ANISOU 923 CD LYS A 284 7162 7163 7862 190 -626 -144 C ATOM 924 CE LYS A 284 9.512 18.616 -6.619 1.00 65.22 C ANISOU 924 CE LYS A 284 8064 8011 8703 223 -623 -230 C ATOM 925 NZ LYS A 284 9.936 17.312 -7.225 1.00 67.44 N ANISOU 925 NZ LYS A 284 8352 8230 9041 235 -692 -260 N ATOM 926 N PHE A 285 4.548 21.990 -4.914 1.00 26.48 N ANISOU 926 N PHE A 285 3058 3290 3712 159 -487 2 N ATOM 927 CA PHE A 285 4.070 22.930 -5.924 1.00 18.64 C ANISOU 927 CA PHE A 285 2080 2310 2695 172 -467 -21 C ATOM 928 C PHE A 285 3.177 24.030 -5.359 1.00 21.54 C ANISOU 928 C PHE A 285 2428 2734 3023 168 -422 21 C ATOM 929 O PHE A 285 3.298 25.186 -5.755 1.00 21.38 O ANISOU 929 O PHE A 285 2426 2739 2957 183 -384 -11 O ATOM 930 CB PHE A 285 3.353 22.196 -7.054 1.00 17.57 C ANISOU 930 CB PHE A 285 1937 2127 2610 171 -519 -17 C ATOM 931 CG PHE A 285 4.117 21.023 -7.579 1.00 23.87 C ANISOU 931 CG PHE A 285 2751 2867 3452 177 -573 -56 C ATOM 932 CD1 PHE A 285 5.335 21.204 -8.214 1.00 23.50 C ANISOU 932 CD1 PHE A 285 2741 2808 3379 204 -565 -132 C ATOM 933 CD2 PHE A 285 3.624 19.739 -7.434 1.00 28.24 C ANISOU 933 CD2 PHE A 285 3281 3377 4072 159 -634 -15 C ATOM 934 CE1 PHE A 285 6.050 20.124 -8.692 1.00 23.14 C ANISOU 934 CE1 PHE A 285 2710 2712 3372 215 -615 -171 C ATOM 935 CE2 PHE A 285 4.334 18.650 -7.915 1.00 30.36 C ANISOU 935 CE2 PHE A 285 3564 3589 4383 168 -689 -54 C ATOM 936 CZ PHE A 285 5.552 18.844 -8.541 1.00 25.45 C ANISOU 936 CZ PHE A 285 2980 2958 3732 198 -679 -134 C ATOM 937 N ALA A 286 2.287 23.683 -4.434 1.00 22.02 N ANISOU 937 N ALA A 286 2448 2816 3102 147 -428 93 N ATOM 938 CA ALA A 286 1.353 24.674 -3.903 1.00 19.50 C ANISOU 938 CA ALA A 286 2107 2555 2748 147 -389 135 C ATOM 939 C ALA A 286 2.052 25.737 -3.037 1.00 22.85 C ANISOU 939 C ALA A 286 2546 3030 3107 160 -336 111 C ATOM 940 O ALA A 286 1.480 26.793 -2.757 1.00 23.59 O ANISOU 940 O ALA A 286 2632 3169 3161 168 -301 125 O ATOM 941 CB ALA A 286 0.215 24.006 -3.142 1.00 16.58 C ANISOU 941 CB ALA A 286 1687 2201 2412 123 -410 222 C ATOM 942 N CYS A 287 3.291 25.477 -2.631 1.00 16.75 N ANISOU 942 N CYS A 287 1795 2247 2323 165 -333 72 N ATOM 943 CA CYS A 287 4.046 26.500 -1.899 1.00 22.06 C ANISOU 943 CA CYS A 287 2485 2963 2936 179 -287 42 C ATOM 944 C CYS A 287 4.282 27.746 -2.768 1.00 17.53 C ANISOU 944 C CYS A 287 1944 2394 2323 198 -260 -10 C ATOM 945 O CYS A 287 4.408 28.858 -2.264 1.00 27.48 O ANISOU 945 O CYS A 287 3211 3696 3535 209 -225 -21 O ATOM 946 CB CYS A 287 5.371 25.944 -1.348 1.00 19.24 C ANISOU 946 CB CYS A 287 2143 2591 2576 180 -291 11 C ATOM 947 SG CYS A 287 6.534 25.408 -2.606 1.00 27.75 S ANISOU 947 SG CYS A 287 3262 3605 3677 191 -317 -62 S ATOM 948 N TYR A 288 4.332 27.558 -4.079 1.00 17.68 N ANISOU 948 N TYR A 288 1981 2372 2364 202 -281 -41 N ATOM 949 CA TYR A 288 4.512 28.686 -4.985 1.00 21.68 C ANISOU 949 CA TYR A 288 2515 2885 2838 217 -260 -83 C ATOM 950 C TYR A 288 3.227 29.511 -5.065 1.00 22.39 C ANISOU 950 C TYR A 288 2585 3006 2917 216 -244 -43 C ATOM 951 O TYR A 288 3.268 30.725 -5.237 1.00 22.84 O ANISOU 951 O TYR A 288 2655 3087 2934 227 -217 -62 O ATOM 952 CB TYR A 288 4.947 28.209 -6.378 1.00 18.96 C ANISOU 952 CB TYR A 288 2193 2494 2517 224 -287 -127 C ATOM 953 CG TYR A 288 6.287 27.511 -6.365 1.00 21.97 C ANISOU 953 CG TYR A 288 2595 2847 2903 230 -300 -172 C ATOM 954 CD1 TYR A 288 7.469 28.234 -6.251 1.00 21.34 C ANISOU 954 CD1 TYR A 288 2545 2783 2781 242 -273 -220 C ATOM 955 CD2 TYR A 288 6.369 26.125 -6.440 1.00 22.27 C ANISOU 955 CD2 TYR A 288 2625 2845 2993 224 -343 -165 C ATOM 956 CE1 TYR A 288 8.703 27.590 -6.217 1.00 18.61 C ANISOU 956 CE1 TYR A 288 2217 2414 2440 249 -284 -260 C ATOM 957 CE2 TYR A 288 7.583 25.476 -6.418 1.00 16.38 C ANISOU 957 CE2 TYR A 288 1897 2073 2254 231 -357 -206 C ATOM 958 CZ TYR A 288 8.748 26.210 -6.306 1.00 20.49 C ANISOU 958 CZ TYR A 288 2445 2611 2728 245 -325 -253 C ATOM 959 OH TYR A 288 9.954 25.555 -6.284 1.00 28.55 O ANISOU 959 OH TYR A 288 3483 3610 3757 254 -338 -293 O ATOM 960 N VAL A 289 2.090 28.837 -4.925 1.00 20.85 N ANISOU 960 N VAL A 289 2355 2809 2759 203 -265 15 N ATOM 961 CA VAL A 289 0.797 29.499 -4.913 1.00 24.20 C ANISOU 961 CA VAL A 289 2753 3264 3176 203 -252 61 C ATOM 962 C VAL A 289 0.666 30.361 -3.662 1.00 22.44 C ANISOU 962 C VAL A 289 2518 3099 2908 209 -217 80 C ATOM 963 O VAL A 289 0.171 31.483 -3.727 1.00 18.82 O ANISOU 963 O VAL A 289 2059 2671 2420 221 -193 83 O ATOM 964 CB VAL A 289 -0.360 28.478 -4.996 1.00 23.13 C ANISOU 964 CB VAL A 289 2580 3114 3095 185 -286 124 C ATOM 965 CG1 VAL A 289 -1.699 29.164 -4.776 1.00 15.86 C ANISOU 965 CG1 VAL A 289 1628 2235 2165 185 -269 178 C ATOM 966 CG2 VAL A 289 -0.337 27.767 -6.338 1.00 11.29 C ANISOU 966 CG2 VAL A 289 1093 1559 1639 183 -325 100 C ATOM 967 N ILE A 290 1.129 29.837 -2.532 1.00 20.04 N ANISOU 967 N ILE A 290 2203 2810 2599 204 -216 93 N ATOM 968 CA ILE A 290 1.165 30.612 -1.294 1.00 16.51 C ANISOU 968 CA ILE A 290 1747 2422 2105 214 -184 103 C ATOM 969 C ILE A 290 2.063 31.834 -1.442 1.00 15.23 C ANISOU 969 C ILE A 290 1623 2268 1896 232 -159 40 C ATOM 970 O ILE A 290 1.672 32.947 -1.105 1.00 27.78 O ANISOU 970 O ILE A 290 3209 3896 3449 245 -137 42 O ATOM 971 CB ILE A 290 1.698 29.780 -0.108 1.00 17.97 C ANISOU 971 CB ILE A 290 1916 2620 2292 205 -189 121 C ATOM 972 CG1 ILE A 290 0.825 28.543 0.136 1.00 17.03 C ANISOU 972 CG1 ILE A 290 1754 2494 2222 184 -220 191 C ATOM 973 CG2 ILE A 290 1.805 30.653 1.147 1.00 14.01 C ANISOU 973 CG2 ILE A 290 1405 2183 1734 220 -158 123 C ATOM 974 CD1 ILE A 290 -0.606 28.859 0.443 1.00 25.50 C ANISOU 974 CD1 ILE A 290 2786 3611 3292 183 -213 256 C ATOM 975 N GLN A 291 3.270 31.629 -1.946 1.00 17.76 N ANISOU 975 N GLN A 291 1978 2551 2218 232 -165 -14 N ATOM 976 CA GLN A 291 4.228 32.727 -2.043 1.00 19.84 C ANISOU 976 CA GLN A 291 2277 2823 2440 246 -144 -70 C ATOM 977 C GLN A 291 3.725 33.786 -3.014 1.00 23.98 C ANISOU 977 C GLN A 291 2812 3347 2954 253 -138 -81 C ATOM 978 O GLN A 291 3.862 34.984 -2.782 1.00 26.49 O ANISOU 978 O GLN A 291 3140 3690 3235 264 -120 -99 O ATOM 979 CB GLN A 291 5.600 32.207 -2.466 1.00 10.18 C ANISOU 979 CB GLN A 291 1084 1561 1223 245 -154 -122 C ATOM 980 CG GLN A 291 6.297 31.374 -1.405 1.00 15.12 C ANISOU 980 CG GLN A 291 1703 2190 1852 240 -157 -118 C ATOM 981 CD GLN A 291 7.456 30.569 -1.960 1.00 21.82 C ANISOU 981 CD GLN A 291 2575 2994 2721 239 -173 -159 C ATOM 982 OE1 GLN A 291 7.357 29.356 -2.125 1.00 28.44 O ANISOU 982 OE1 GLN A 291 3402 3802 3604 229 -200 -141 O ATOM 983 NE2 GLN A 291 8.555 31.240 -2.253 1.00 16.07 N ANISOU 983 NE2 GLN A 291 1880 2262 1964 249 -160 -213 N ATOM 984 N SER A 292 3.125 33.326 -4.098 1.00 21.78 N ANISOU 984 N SER A 292 2529 3039 2709 247 -155 -67 N ATOM 985 CA SER A 292 2.544 34.213 -5.086 1.00 23.76 C ANISOU 985 CA SER A 292 2785 3289 2955 253 -151 -69 C ATOM 986 C SER A 292 1.443 35.070 -4.453 1.00 26.95 C ANISOU 986 C SER A 292 3163 3737 3341 260 -134 -28 C ATOM 987 O SER A 292 1.425 36.293 -4.603 1.00 27.74 O ANISOU 987 O SER A 292 3273 3853 3414 270 -120 -43 O ATOM 988 CB SER A 292 1.978 33.378 -6.226 1.00 30.95 C ANISOU 988 CB SER A 292 3688 4164 3909 245 -176 -55 C ATOM 989 OG SER A 292 1.900 34.142 -7.399 1.00 45.59 O ANISOU 989 OG SER A 292 5557 6009 5755 252 -174 -75 O ATOM 990 N SER A 293 0.539 34.423 -3.724 1.00 19.96 N ANISOU 990 N SER A 293 2241 2870 2472 254 -138 25 N ATOM 991 CA SER A 293 -0.574 35.126 -3.092 1.00 23.48 C ANISOU 991 CA SER A 293 2657 3362 2901 264 -124 69 C ATOM 992 C SER A 293 -0.117 36.136 -2.031 1.00 23.42 C ANISOU 992 C SER A 293 2657 3397 2845 281 -103 47 C ATOM 993 O SER A 293 -0.700 37.203 -1.892 1.00 28.22 O ANISOU 993 O SER A 293 3257 4034 3431 296 -91 54 O ATOM 994 CB SER A 293 -1.561 34.126 -2.483 1.00 23.44 C ANISOU 994 CB SER A 293 2608 3374 2923 254 -134 135 C ATOM 995 OG SER A 293 -1.999 33.194 -3.459 1.00 26.88 O ANISOU 995 OG SER A 293 3038 3768 3409 238 -160 153 O ATOM 996 N LEU A 294 0.926 35.790 -1.287 1.00 17.36 N ANISOU 996 N LEU A 294 1902 2632 2063 279 -101 19 N ATOM 997 CA LEU A 294 1.420 36.647 -0.223 1.00 17.65 C ANISOU 997 CA LEU A 294 1943 2708 2054 295 -86 -4 C ATOM 998 C LEU A 294 1.926 37.998 -0.753 1.00 23.02 C ANISOU 998 C LEU A 294 2655 3381 2712 305 -81 -51 C ATOM 999 O LEU A 294 1.712 39.033 -0.121 1.00 23.45 O ANISOU 999 O LEU A 294 2702 3470 2736 322 -73 -57 O ATOM 1000 CB LEU A 294 2.529 35.932 0.558 1.00 14.75 C ANISOU 1000 CB LEU A 294 1585 2339 1679 289 -87 -26 C ATOM 1001 CG LEU A 294 2.136 34.808 1.528 1.00 20.37 C ANISOU 1001 CG LEU A 294 2260 3075 2403 281 -91 24 C ATOM 1002 CD1 LEU A 294 3.378 34.001 1.999 1.00 9.60 C ANISOU 1002 CD1 LEU A 294 911 1695 1042 272 -95 -2 C ATOM 1003 CD2 LEU A 294 1.367 35.395 2.715 1.00 12.84 C ANISOU 1003 CD2 LEU A 294 1273 2192 1414 298 -77 56 C ATOM 1004 N GLN A 295 2.590 37.996 -1.906 1.00 20.05 N ANISOU 1004 N GLN A 295 2308 2959 2350 296 -88 -84 N ATOM 1005 CA GLN A 295 3.140 39.246 -2.425 1.00 27.90 C ANISOU 1005 CA GLN A 295 3329 3946 3326 303 -86 -124 C ATOM 1006 C GLN A 295 2.194 39.988 -3.374 1.00 26.00 C ANISOU 1006 C GLN A 295 3080 3701 3097 307 -87 -103 C ATOM 1007 O GLN A 295 2.330 41.195 -3.568 1.00 25.52 O ANISOU 1007 O GLN A 295 3029 3644 3022 315 -86 -121 O ATOM 1008 CB GLN A 295 4.533 39.042 -3.055 1.00 22.03 C ANISOU 1008 CB GLN A 295 2621 3167 2583 294 -92 -173 C ATOM 1009 CG GLN A 295 4.565 38.261 -4.353 1.00 28.14 C ANISOU 1009 CG GLN A 295 3404 3901 3388 283 -103 -173 C ATOM 1010 CD GLN A 295 5.992 38.007 -4.854 1.00 36.93 C ANISOU 1010 CD GLN A 295 4547 4986 4497 279 -108 -221 C ATOM 1011 OE1 GLN A 295 6.191 37.555 -5.979 1.00 40.15 O ANISOU 1011 OE1 GLN A 295 4965 5365 4924 275 -118 -231 O ATOM 1012 NE2 GLN A 295 6.984 38.303 -4.016 1.00 31.14 N ANISOU 1012 NE2 GLN A 295 3810 4255 3767 278 -110 -229 N ATOM 1013 N ASN A 296 1.232 39.270 -3.948 1.00 21.07 N ANISOU 1013 N ASN A 296 2437 3067 2503 300 -92 -63 N ATOM 1014 CA ASN A 296 0.330 39.872 -4.928 1.00 22.84 C ANISOU 1014 CA ASN A 296 2652 3286 2741 303 -92 -41 C ATOM 1015 C ASN A 296 -1.030 40.321 -4.390 1.00 26.62 C ANISOU 1015 C ASN A 296 3095 3801 3218 316 -85 7 C ATOM 1016 O ASN A 296 -1.549 41.360 -4.807 1.00 23.21 O ANISOU 1016 O ASN A 296 2659 3375 2783 327 -81 14 O ATOM 1017 CB ASN A 296 0.154 38.953 -6.136 1.00 25.72 C ANISOU 1017 CB ASN A 296 3019 3614 3139 290 -105 -33 C ATOM 1018 CG ASN A 296 1.448 38.764 -6.904 1.00 35.11 C ANISOU 1018 CG ASN A 296 4243 4771 4327 284 -113 -84 C ATOM 1019 OD1 ASN A 296 2.242 39.695 -7.042 1.00 30.32 O ANISOU 1019 OD1 ASN A 296 3658 4165 3698 288 -108 -117 O ATOM 1020 ND2 ASN A 296 1.669 37.557 -7.407 1.00 43.37 N ANISOU 1020 ND2 ASN A 296 5292 5789 5399 274 -127 -88 N ATOM 1021 N MET A 297 -1.603 39.537 -3.476 1.00 22.09 N ANISOU 1021 N MET A 297 2494 3253 2647 316 -83 43 N ATOM 1022 CA MET A 297 -2.911 39.846 -2.914 1.00 19.49 C ANISOU 1022 CA MET A 297 2126 2964 2314 330 -75 94 C ATOM 1023 C MET A 297 -2.902 41.194 -2.220 1.00 21.74 C ANISOU 1023 C MET A 297 2411 3284 2565 354 -66 76 C ATOM 1024 O MET A 297 -1.843 41.695 -1.851 1.00 26.85 O ANISOU 1024 O MET A 297 3083 3929 3191 358 -67 28 O ATOM 1025 CB MET A 297 -3.346 38.765 -1.918 1.00 21.88 C ANISOU 1025 CB MET A 297 2397 3295 2621 326 -75 136 C ATOM 1026 CG MET A 297 -4.056 37.582 -2.555 1.00 25.72 C ANISOU 1026 CG MET A 297 2863 3757 3152 306 -89 180 C ATOM 1027 SD MET A 297 -4.402 36.241 -1.389 1.00 49.77 S ANISOU 1027 SD MET A 297 5870 6832 6209 295 -95 233 S ATOM 1028 CE MET A 297 -5.289 37.103 -0.104 1.00 83.18 C ANISOU 1028 CE MET A 297 10063 11142 10398 323 -75 269 C ATOM 1029 N ASP A 298 -4.081 41.786 -2.055 1.00 27.05 N ANISOU 1029 N ASP A 298 3054 3988 3237 372 -59 114 N ATOM 1030 CA ASP A 298 -4.197 42.987 -1.240 1.00 28.96 C ANISOU 1030 CA ASP A 298 3287 4267 3449 400 -54 100 C ATOM 1031 C ASP A 298 -3.602 42.682 0.131 1.00 29.19 C ANISOU 1031 C ASP A 298 3312 4333 3446 407 -52 83 C ATOM 1032 O ASP A 298 -3.795 41.593 0.675 1.00 29.51 O ANISOU 1032 O ASP A 298 3334 4392 3488 398 -50 114 O ATOM 1033 CB ASP A 298 -5.659 43.429 -1.113 1.00 27.32 C ANISOU 1033 CB ASP A 298 3040 4095 3246 422 -47 151 C ATOM 1034 CG ASP A 298 -6.221 43.983 -2.413 1.00 29.52 C ANISOU 1034 CG ASP A 298 3322 4341 3553 419 -48 164 C ATOM 1035 OD1 ASP A 298 -5.436 44.361 -3.302 1.00 31.11 O ANISOU 1035 OD1 ASP A 298 3556 4500 3765 407 -54 127 O ATOM 1036 OD2 ASP A 298 -7.456 44.046 -2.543 1.00 30.66 O ANISOU 1036 OD2 ASP A 298 3434 4504 3709 430 -42 213 O ATOM 1037 N LEU A 299 -2.866 43.634 0.682 1.00 25.07 N ANISOU 1037 N LEU A 299 2805 3822 2899 422 -56 35 N ATOM 1038 CA LEU A 299 -2.137 43.386 1.914 1.00 25.52 C ANISOU 1038 CA LEU A 299 2861 3911 2924 428 -56 10 C ATOM 1039 C LEU A 299 -3.029 42.898 3.051 1.00 29.00 C ANISOU 1039 C LEU A 299 3257 4416 3344 444 -47 56 C ATOM 1040 O LEU A 299 -2.654 42.000 3.801 1.00 28.96 O ANISOU 1040 O LEU A 299 3245 4432 3328 436 -44 64 O ATOM 1041 CB LEU A 299 -1.358 44.625 2.348 1.00 28.87 C ANISOU 1041 CB LEU A 299 3301 4340 3327 444 -64 -47 C ATOM 1042 CG LEU A 299 -0.445 44.322 3.532 1.00 32.64 C ANISOU 1042 CG LEU A 299 3782 4847 3773 447 -66 -79 C ATOM 1043 CD1 LEU A 299 0.503 43.190 3.158 1.00 25.56 C ANISOU 1043 CD1 LEU A 299 2913 3912 2889 417 -64 -88 C ATOM 1044 CD2 LEU A 299 0.303 45.566 3.956 1.00 30.28 C ANISOU 1044 CD2 LEU A 299 3495 4552 3458 462 -79 -137 C ATOM 1045 N SER A 300 -4.213 43.479 3.173 1.00 28.96 N ANISOU 1045 N SER A 300 3220 4446 3337 468 -42 90 N ATOM 1046 CA SER A 300 -5.122 43.074 4.239 1.00 32.62 C ANISOU 1046 CA SER A 300 3637 4980 3779 487 -34 138 C ATOM 1047 C SER A 300 -5.496 41.605 4.139 1.00 26.39 C ANISOU 1047 C SER A 300 2829 4188 3011 460 -30 195 C ATOM 1048 O SER A 300 -5.603 40.917 5.147 1.00 31.71 O ANISOU 1048 O SER A 300 3473 4910 3665 462 -26 223 O ATOM 1049 CB SER A 300 -6.376 43.941 4.233 1.00 40.03 C ANISOU 1049 CB SER A 300 4542 5952 4716 518 -29 168 C ATOM 1050 OG SER A 300 -6.021 45.295 4.455 1.00 54.50 O ANISOU 1050 OG SER A 300 6386 7788 6533 544 -37 114 O ATOM 1051 N LEU A 301 -5.695 41.125 2.918 1.00 22.73 N ANISOU 1051 N LEU A 301 2379 3668 2589 435 -34 213 N ATOM 1052 CA LEU A 301 -5.999 39.717 2.714 1.00 24.28 C ANISOU 1052 CA LEU A 301 2558 3850 2816 407 -37 262 C ATOM 1053 C LEU A 301 -4.759 38.836 2.879 1.00 21.64 C ANISOU 1053 C LEU A 301 2250 3487 2487 383 -44 231 C ATOM 1054 O LEU A 301 -4.840 37.756 3.453 1.00 24.00 O ANISOU 1054 O LEU A 301 2524 3802 2793 369 -47 269 O ATOM 1055 CB LEU A 301 -6.646 39.493 1.346 1.00 35.14 C ANISOU 1055 CB LEU A 301 3937 5177 4237 390 -43 287 C ATOM 1056 CG LEU A 301 -8.130 39.867 1.242 1.00 46.61 C ANISOU 1056 CG LEU A 301 5349 6663 5696 407 -37 345 C ATOM 1057 CD1 LEU A 301 -8.735 39.184 0.039 1.00 53.15 C ANISOU 1057 CD1 LEU A 301 6174 7445 6575 382 -47 380 C ATOM 1058 CD2 LEU A 301 -8.890 39.480 2.503 1.00 48.25 C ANISOU 1058 CD2 LEU A 301 5505 6945 5882 421 -30 400 C ATOM 1059 N ALA A 302 -3.623 39.300 2.367 1.00 17.58 N ANISOU 1059 N ALA A 302 1782 2928 1969 379 -48 167 N ATOM 1060 CA ALA A 302 -2.355 38.585 2.521 1.00 16.36 C ANISOU 1060 CA ALA A 302 1654 2745 1816 360 -53 131 C ATOM 1061 C ALA A 302 -2.051 38.359 3.999 1.00 21.56 C ANISOU 1061 C ALA A 302 2292 3461 2440 371 -47 135 C ATOM 1062 O ALA A 302 -1.550 37.308 4.388 1.00 27.05 O ANISOU 1062 O ALA A 302 2983 4151 3145 353 -51 146 O ATOM 1063 CB ALA A 302 -1.224 39.358 1.866 1.00 14.01 C ANISOU 1063 CB ALA A 302 1405 2405 1513 359 -56 62 C ATOM 1064 N CYS A 303 -2.363 39.356 4.817 1.00 25.14 N ANISOU 1064 N CYS A 303 2730 3970 2853 400 -40 126 N ATOM 1065 CA CYS A 303 -2.181 39.253 6.262 1.00 24.46 C ANISOU 1065 CA CYS A 303 2618 3950 2727 415 -34 130 C ATOM 1066 C CYS A 303 -3.011 38.123 6.875 1.00 23.67 C ANISOU 1066 C CYS A 303 2467 3892 2634 406 -31 206 C ATOM 1067 O CYS A 303 -2.559 37.454 7.796 1.00 26.60 O ANISOU 1067 O CYS A 303 2823 4295 2989 401 -30 216 O ATOM 1068 CB CYS A 303 -2.477 40.596 6.941 1.00 21.30 C ANISOU 1068 CB CYS A 303 2205 3602 2285 453 -32 104 C ATOM 1069 SG CYS A 303 -1.187 41.862 6.598 1.00 31.59 S ANISOU 1069 SG CYS A 303 3562 4864 3579 459 -42 11 S ATOM 1070 N LYS A 304 -4.215 37.902 6.355 1.00 25.24 N ANISOU 1070 N LYS A 304 2639 4092 2859 403 -32 263 N ATOM 1071 CA LYS A 304 -5.050 36.798 6.822 1.00 24.70 C ANISOU 1071 CA LYS A 304 2520 4059 2805 390 -34 343 C ATOM 1072 C LYS A 304 -4.429 35.428 6.527 1.00 30.62 C ANISOU 1072 C LYS A 304 3280 4759 3598 351 -48 356 C ATOM 1073 O LYS A 304 -4.627 34.486 7.289 1.00 34.66 O ANISOU 1073 O LYS A 304 3753 5304 4112 338 -52 409 O ATOM 1074 CB LYS A 304 -6.448 36.878 6.201 1.00 30.42 C ANISOU 1074 CB LYS A 304 3216 4787 3554 392 -34 399 C ATOM 1075 CG LYS A 304 -7.219 38.148 6.531 1.00 42.73 C ANISOU 1075 CG LYS A 304 4758 6401 5076 433 -21 396 C ATOM 1076 CD LYS A 304 -8.166 37.951 7.705 1.00 50.52 C ANISOU 1076 CD LYS A 304 5681 7481 6032 452 -13 460 C ATOM 1077 CE LYS A 304 -8.972 39.220 7.990 1.00 52.63 C ANISOU 1077 CE LYS A 304 5930 7803 6266 497 -3 455 C ATOM 1078 NZ LYS A 304 -9.638 39.764 6.770 1.00 50.99 N ANISOU 1078 NZ LYS A 304 5736 7545 6092 498 -4 459 N ATOM 1079 N LEU A 305 -3.694 35.311 5.421 1.00 23.31 N ANISOU 1079 N LEU A 305 2401 3753 2704 334 -57 312 N ATOM 1080 CA LEU A 305 -3.037 34.048 5.093 1.00 23.34 C ANISOU 1080 CA LEU A 305 2414 3704 2749 302 -74 316 C ATOM 1081 C LEU A 305 -1.981 33.716 6.137 1.00 22.11 C ANISOU 1081 C LEU A 305 2263 3571 2567 301 -71 294 C ATOM 1082 O LEU A 305 -1.893 32.588 6.607 1.00 22.94 O ANISOU 1082 O LEU A 305 2344 3680 2693 281 -83 334 O ATOM 1083 CB LEU A 305 -2.394 34.093 3.702 1.00 19.76 C ANISOU 1083 CB LEU A 305 2011 3169 2328 290 -84 264 C ATOM 1084 CG LEU A 305 -3.333 34.300 2.518 1.00 27.68 C ANISOU 1084 CG LEU A 305 3013 4142 3363 287 -90 284 C ATOM 1085 CD1 LEU A 305 -2.568 34.208 1.207 1.00 33.63 C ANISOU 1085 CD1 LEU A 305 3812 4820 4145 275 -102 232 C ATOM 1086 CD2 LEU A 305 -4.456 33.274 2.560 1.00 23.63 C ANISOU 1086 CD2 LEU A 305 2451 3637 2888 269 -106 364 C ATOM 1087 N VAL A 306 -1.176 34.710 6.487 1.00 20.90 N ANISOU 1087 N VAL A 306 2139 3433 2371 323 -58 231 N ATOM 1088 CA VAL A 306 -0.176 34.564 7.538 1.00 25.57 C ANISOU 1088 CA VAL A 306 2732 4052 2929 326 -53 205 C ATOM 1089 C VAL A 306 -0.838 34.142 8.852 1.00 32.50 C ANISOU 1089 C VAL A 306 3553 5014 3782 331 -48 267 C ATOM 1090 O VAL A 306 -0.314 33.319 9.604 1.00 32.63 O ANISOU 1090 O VAL A 306 3554 5048 3797 318 -52 284 O ATOM 1091 CB VAL A 306 0.558 35.892 7.767 1.00 23.33 C ANISOU 1091 CB VAL A 306 2482 3782 2602 352 -42 132 C ATOM 1092 CG1 VAL A 306 1.525 35.771 8.931 1.00 24.89 C ANISOU 1092 CG1 VAL A 306 2676 4016 2763 357 -37 107 C ATOM 1093 CG2 VAL A 306 1.273 36.332 6.487 1.00 16.72 C ANISOU 1093 CG2 VAL A 306 1698 2867 1787 344 -48 75 C ATOM 1094 N GLN A 307 -2.005 34.713 9.115 1.00 36.19 N ANISOU 1094 N GLN A 307 3986 5537 4229 351 -41 303 N ATOM 1095 CA GLN A 307 -2.740 34.439 10.338 1.00 38.74 C ANISOU 1095 CA GLN A 307 4249 5950 4521 361 -35 364 C ATOM 1096 C GLN A 307 -3.145 32.960 10.400 1.00 37.35 C ANISOU 1096 C GLN A 307 4036 5767 4389 325 -50 443 C ATOM 1097 O GLN A 307 -3.357 32.401 11.472 1.00 37.07 O ANISOU 1097 O GLN A 307 3953 5798 4334 322 -50 494 O ATOM 1098 CB GLN A 307 -3.957 35.358 10.393 1.00 40.85 C ANISOU 1098 CB GLN A 307 4489 6268 4763 391 -26 385 C ATOM 1099 CG GLN A 307 -4.893 35.131 11.550 1.00 57.07 C ANISOU 1099 CG GLN A 307 6476 8424 6785 405 -20 455 C ATOM 1100 CD GLN A 307 -6.178 35.930 11.407 1.00 68.66 C ANISOU 1100 CD GLN A 307 7916 9932 8238 434 -12 482 C ATOM 1101 OE1 GLN A 307 -6.160 37.098 11.003 1.00 64.58 O ANISOU 1101 OE1 GLN A 307 7429 9401 7707 461 -7 427 O ATOM 1102 NE2 GLN A 307 -7.302 35.303 11.736 1.00 77.02 N ANISOU 1102 NE2 GLN A 307 8917 11044 9305 428 -13 570 N ATOM 1103 N ALA A 308 -3.216 32.324 9.237 1.00 27.87 N ANISOU 1103 N ALA A 308 2855 4485 3249 299 -67 452 N ATOM 1104 CA ALA A 308 -3.634 30.934 9.148 1.00 20.34 C ANISOU 1104 CA ALA A 308 1868 3512 2348 263 -91 525 C ATOM 1105 C ALA A 308 -2.480 29.957 9.375 1.00 28.16 C ANISOU 1105 C ALA A 308 2873 4464 3361 238 -106 511 C ATOM 1106 O ALA A 308 -2.677 28.745 9.328 1.00 34.56 O ANISOU 1106 O ALA A 308 3660 5252 4221 206 -132 567 O ATOM 1107 CB ALA A 308 -4.286 30.675 7.803 1.00 16.42 C ANISOU 1107 CB ALA A 308 1383 2948 1910 247 -107 540 C ATOM 1108 N LEU A 309 -1.276 30.473 9.605 1.00 25.08 N ANISOU 1108 N LEU A 309 2524 4066 2938 252 -93 437 N ATOM 1109 CA LEU A 309 -0.144 29.603 9.918 1.00 30.97 C ANISOU 1109 CA LEU A 309 3283 4784 3701 232 -105 423 C ATOM 1110 C LEU A 309 -0.377 28.909 11.251 1.00 28.91 C ANISOU 1110 C LEU A 309 2965 4598 3423 221 -109 491 C ATOM 1111 O LEU A 309 -0.987 29.486 12.142 1.00 32.26 O ANISOU 1111 O LEU A 309 3352 5108 3796 242 -91 516 O ATOM 1112 CB LEU A 309 1.166 30.395 9.949 1.00 26.26 C ANISOU 1112 CB LEU A 309 2737 4170 3069 251 -89 333 C ATOM 1113 CG LEU A 309 1.700 30.760 8.569 1.00 25.55 C ANISOU 1113 CG LEU A 309 2705 3996 3007 251 -92 269 C ATOM 1114 CD1 LEU A 309 2.826 31.773 8.661 1.00 26.56 C ANISOU 1114 CD1 LEU A 309 2877 4121 3094 272 -75 186 C ATOM 1115 CD2 LEU A 309 2.138 29.506 7.843 1.00 23.55 C ANISOU 1115 CD2 LEU A 309 2464 3668 2818 222 -120 278 C ATOM 1116 N PRO A 310 0.093 27.657 11.379 1.00 31.89 N ANISOU 1116 N PRO A 310 3332 4941 3842 189 -134 524 N ATOM 1117 CA PRO A 310 -0.019 26.877 12.623 1.00 30.26 C ANISOU 1117 CA PRO A 310 3071 4802 3625 173 -142 593 C ATOM 1118 C PRO A 310 0.876 27.461 13.703 1.00 43.35 C ANISOU 1118 C PRO A 310 4733 6521 5217 195 -117 550 C ATOM 1119 O PRO A 310 1.879 28.098 13.379 1.00 46.37 O ANISOU 1119 O PRO A 310 5169 6868 5583 211 -104 466 O ATOM 1120 CB PRO A 310 0.500 25.485 12.242 1.00 26.82 C ANISOU 1120 CB PRO A 310 2640 4292 3259 134 -180 618 C ATOM 1121 CG PRO A 310 0.780 25.518 10.780 1.00 32.42 C ANISOU 1121 CG PRO A 310 3403 4900 4015 133 -192 562 C ATOM 1122 CD PRO A 310 0.816 26.938 10.318 1.00 30.46 C ANISOU 1122 CD PRO A 310 3193 4658 3723 168 -159 491 C ATOM 1123 N ARG A 311 0.525 27.241 14.966 1.00 51.05 N ANISOU 1123 N ARG A 311 5652 7590 6153 194 -113 608 N ATOM 1124 CA ARG A 311 1.297 27.786 16.078 1.00 50.76 C ANISOU 1124 CA ARG A 311 5612 7623 6050 215 -92 570 C ATOM 1125 C ARG A 311 1.916 26.671 16.910 1.00 45.27 C ANISOU 1125 C ARG A 311 4889 6947 5367 185 -108 615 C ATOM 1126 O ARG A 311 2.392 26.907 18.017 1.00 47.53 O ANISOU 1126 O ARG A 311 5155 7308 5597 197 -94 606 O ATOM 1127 CB ARG A 311 0.410 28.653 16.973 1.00 51.70 C ANISOU 1127 CB ARG A 311 5687 7856 6100 247 -70 590 C ATOM 1128 CG ARG A 311 -0.504 29.590 16.215 1.00 54.43 C ANISOU 1128 CG ARG A 311 6046 8193 6443 272 -60 572 C ATOM 1129 CD ARG A 311 0.272 30.353 15.178 1.00 51.97 C ANISOU 1129 CD ARG A 311 5808 7794 6144 285 -54 477 C ATOM 1130 NE ARG A 311 -0.588 31.170 14.328 1.00 48.22 N ANISOU 1130 NE ARG A 311 5347 7300 5674 304 -48 464 N ATOM 1131 CZ ARG A 311 -0.997 32.393 14.641 1.00 43.76 C ANISOU 1131 CZ ARG A 311 4780 6791 5057 343 -31 432 C ATOM 1132 NH1 ARG A 311 -0.638 32.934 15.800 1.00 42.94 N ANISOU 1132 NH1 ARG A 311 4657 6767 4889 367 -19 407 N ATOM 1133 NH2 ARG A 311 -1.765 33.071 13.798 1.00 42.48 N ANISOU 1133 NH2 ARG A 311 4630 6603 4906 356 -29 425 N ATOM 1134 N ASP A 312 1.903 25.457 16.378 1.00 40.99 N ANISOU 1134 N ASP A 312 4343 6336 4897 147 -141 662 N ATOM 1135 CA ASP A 312 2.361 24.303 17.132 1.00 41.29 C ANISOU 1135 CA ASP A 312 4347 6387 4954 114 -165 717 C ATOM 1136 C ASP A 312 3.519 23.604 16.438 1.00 42.67 C ANISOU 1136 C ASP A 312 4571 6456 5184 95 -187 675 C ATOM 1137 O ASP A 312 4.242 24.223 15.664 1.00 46.54 O ANISOU 1137 O ASP A 312 5122 6887 5676 115 -173 588 O ATOM 1138 CB ASP A 312 1.205 23.329 17.379 1.00 50.47 C ANISOU 1138 CB ASP A 312 5444 7578 6152 81 -194 833 C ATOM 1139 CG ASP A 312 0.554 22.840 16.091 1.00 58.66 C ANISOU 1139 CG ASP A 312 6498 8524 7267 62 -223 852 C ATOM 1140 OD1 ASP A 312 1.191 22.923 15.019 1.00 59.16 O ANISOU 1140 OD1 ASP A 312 6621 8490 7366 66 -228 781 O ATOM 1141 OD2 ASP A 312 -0.597 22.355 16.157 1.00 59.06 O ANISOU 1141 OD2 ASP A 312 6497 8601 7341 42 -242 939 O ATOM 1142 N ALA A 313 3.687 22.314 16.717 1.00 39.73 N ANISOU 1142 N ALA A 313 4171 6064 4860 57 -223 738 N ATOM 1143 CA ALA A 313 4.794 21.539 16.167 1.00 41.29 C ANISOU 1143 CA ALA A 313 4408 6167 5112 40 -249 704 C ATOM 1144 C ALA A 313 4.878 21.623 14.646 1.00 38.32 C ANISOU 1144 C ALA A 313 4088 5685 4788 46 -260 646 C ATOM 1145 O ALA A 313 5.963 21.517 14.073 1.00 43.10 O ANISOU 1145 O ALA A 313 4743 6221 5414 50 -265 580 O ATOM 1146 CB ALA A 313 4.696 20.088 16.609 1.00 44.60 C ANISOU 1146 CB ALA A 313 4784 6577 5586 -5 -296 793 C ATOM 1147 N ARG A 314 3.731 21.805 13.999 1.00 43.23 N ANISOU 1147 N ARG A 314 5042 5290 6094 142 -349 563 N ATOM 1148 CA ARG A 314 3.676 21.927 12.545 1.00 38.07 C ANISOU 1148 CA ARG A 314 4379 4619 5469 105 -390 523 C ATOM 1149 C ARG A 314 4.476 23.140 12.063 1.00 37.28 C ANISOU 1149 C ARG A 314 4326 4521 5316 129 -370 435 C ATOM 1150 O ARG A 314 4.996 23.147 10.949 1.00 39.70 O ANISOU 1150 O ARG A 314 4646 4803 5635 100 -412 369 O ATOM 1151 CB ARG A 314 2.223 22.007 12.061 1.00 35.26 C ANISOU 1151 CB ARG A 314 3960 4282 5153 92 -381 603 C ATOM 1152 CG ARG A 314 1.361 20.788 12.439 1.00 35.45 C ANISOU 1152 CG ARG A 314 3933 4303 5235 64 -404 693 C ATOM 1153 CD ARG A 314 -0.093 20.944 11.989 1.00 32.04 C ANISOU 1153 CD ARG A 314 3440 3894 4840 53 -391 772 C ATOM 1154 NE ARG A 314 -0.838 21.860 12.850 1.00 29.55 N ANISOU 1154 NE ARG A 314 3115 3625 4489 102 -317 828 N ATOM 1155 CZ ARG A 314 -2.007 22.404 12.531 1.00 39.58 C ANISOU 1155 CZ ARG A 314 4344 4923 5771 107 -290 884 C ATOM 1156 NH1 ARG A 314 -2.570 22.131 11.363 1.00 47.28 N ANISOU 1156 NH1 ARG A 314 5284 5886 6796 67 -330 892 N ATOM 1157 NH2 ARG A 314 -2.608 23.231 13.376 1.00 38.77 N ANISOU 1157 NH2 ARG A 314 4235 4862 5632 154 -223 932 N ATOM 1158 N LEU A 315 4.584 24.157 12.912 1.00 25.28 N ANISOU 1158 N LEU A 315 2834 3032 3739 182 -305 433 N ATOM 1159 CA LEU A 315 5.356 25.348 12.569 1.00 24.25 C ANISOU 1159 CA LEU A 315 2752 2907 3556 209 -282 351 C ATOM 1160 C LEU A 315 6.853 25.052 12.476 1.00 24.57 C ANISOU 1160 C LEU A 315 2847 2914 3575 200 -317 255 C ATOM 1161 O LEU A 315 7.533 25.534 11.568 1.00 30.98 O ANISOU 1161 O LEU A 315 3688 3711 4374 190 -337 177 O ATOM 1162 CB LEU A 315 5.089 26.484 13.561 1.00 23.95 C ANISOU 1162 CB LEU A 315 2728 2910 3461 269 -204 376 C ATOM 1163 CG LEU A 315 5.620 27.844 13.107 1.00 24.80 C ANISOU 1163 CG LEU A 315 2877 3028 3518 296 -174 304 C ATOM 1164 CD1 LEU A 315 5.141 28.132 11.694 1.00 24.03 C ANISOU 1164 CD1 LEU A 315 2755 2923 3451 265 -201 291 C ATOM 1165 CD2 LEU A 315 5.220 28.960 14.059 1.00 19.16 C ANISOU 1165 CD2 LEU A 315 2171 2356 2753 355 -97 336 C ATOM 1166 N ILE A 316 7.366 24.263 13.413 1.00 29.37 N ANISOU 1166 N ILE A 316 3469 3510 4179 204 -325 262 N ATOM 1167 CA ILE A 316 8.750 23.806 13.334 1.00 33.19 C ANISOU 1167 CA ILE A 316 4001 3960 4650 191 -365 176 C ATOM 1168 C ILE A 316 8.940 23.096 11.998 1.00 33.68 C ANISOU 1168 C ILE A 316 4050 3987 4762 134 -437 138 C ATOM 1169 O ILE A 316 9.860 23.407 11.237 1.00 35.51 O ANISOU 1169 O ILE A 316 4317 4198 4977 124 -462 51 O ATOM 1170 CB ILE A 316 9.100 22.824 14.471 1.00 36.08 C ANISOU 1170 CB ILE A 316 4373 4317 5019 196 -372 201 C ATOM 1171 CG1 ILE A 316 8.965 23.489 15.838 1.00 38.76 C ANISOU 1171 CG1 ILE A 316 4728 4692 5308 253 -302 236 C ATOM 1172 CG2 ILE A 316 10.504 22.280 14.296 1.00 32.51 C ANISOU 1172 CG2 ILE A 316 3968 3828 4558 178 -419 112 C ATOM 1173 CD1 ILE A 316 9.112 22.515 16.990 1.00 38.11 C ANISOU 1173 CD1 ILE A 316 4645 4605 5232 258 -305 276 C ATOM 1174 N ALA A 317 8.048 22.150 11.714 1.00 21.77 N ANISOU 1174 N ALA A 317 2487 2470 3313 98 -470 206 N ATOM 1175 CA ALA A 317 8.110 21.371 10.478 1.00 27.93 C ANISOU 1175 CA ALA A 317 3249 3217 4147 42 -541 181 C ATOM 1176 C ALA A 317 8.101 22.265 9.245 1.00 29.44 C ANISOU 1176 C ALA A 317 3445 3409 4332 34 -544 132 C ATOM 1177 O ALA A 317 8.791 21.988 8.265 1.00 34.09 O ANISOU 1177 O ALA A 317 4050 3969 4936 1 -596 63 O ATOM 1178 CB ALA A 317 6.960 20.376 10.412 1.00 24.47 C ANISOU 1178 CB ALA A 317 2747 2776 3773 10 -565 273 C ATOM 1179 N ILE A 318 7.311 23.330 9.299 1.00 20.25 N ANISOU 1179 N ILE A 318 2267 2280 3147 65 -490 167 N ATOM 1180 CA ILE A 318 7.257 24.288 8.205 1.00 22.50 C ANISOU 1180 CA ILE A 318 2558 2570 3421 62 -486 124 C ATOM 1181 C ILE A 318 8.608 24.983 8.028 1.00 25.87 C ANISOU 1181 C ILE A 318 3049 2986 3796 79 -483 18 C ATOM 1182 O ILE A 318 9.107 25.091 6.915 1.00 23.32 O ANISOU 1182 O ILE A 318 2738 2641 3480 53 -521 -47 O ATOM 1183 CB ILE A 318 6.122 25.321 8.409 1.00 19.62 C ANISOU 1183 CB ILE A 318 2166 2247 3040 96 -424 186 C ATOM 1184 CG1 ILE A 318 4.789 24.729 7.942 1.00 24.81 C ANISOU 1184 CG1 ILE A 318 2758 2910 3760 65 -443 270 C ATOM 1185 CG2 ILE A 318 6.397 26.591 7.640 1.00 19.58 C ANISOU 1185 CG2 ILE A 318 2188 2251 2999 112 -403 125 C ATOM 1186 CD1 ILE A 318 3.595 25.600 8.228 1.00 26.31 C ANISOU 1186 CD1 ILE A 318 2916 3141 3938 96 -383 341 C ATOM 1187 N CYS A 319 9.199 25.427 9.135 1.00 23.13 N ANISOU 1187 N CYS A 319 2741 2652 3397 122 -440 2 N ATOM 1188 CA CYS A 319 10.471 26.147 9.087 1.00 22.87 C ANISOU 1188 CA CYS A 319 2769 2611 3309 143 -431 -96 C ATOM 1189 C CYS A 319 11.645 25.325 8.539 1.00 31.08 C ANISOU 1189 C CYS A 319 3838 3609 4363 106 -497 -174 C ATOM 1190 O CYS A 319 12.542 25.882 7.904 1.00 25.84 O ANISOU 1190 O CYS A 319 3213 2932 3671 105 -507 -260 O ATOM 1191 CB CYS A 319 10.826 26.708 10.466 1.00 21.24 C ANISOU 1191 CB CYS A 319 2596 2428 3047 197 -372 -91 C ATOM 1192 SG CYS A 319 9.842 28.145 10.972 1.00 32.41 S ANISOU 1192 SG CYS A 319 3999 3893 4423 250 -287 -37 S ATOM 1193 N VAL A 320 11.637 24.011 8.775 1.00 28.45 N ANISOU 1193 N VAL A 320 3485 3254 4072 76 -541 -145 N ATOM 1194 CA VAL A 320 12.740 23.156 8.338 1.00 22.98 C ANISOU 1194 CA VAL A 320 2817 2521 3393 42 -604 -217 C ATOM 1195 C VAL A 320 12.441 22.394 7.051 1.00 21.75 C ANISOU 1195 C VAL A 320 2627 2339 3297 -14 -670 -219 C ATOM 1196 O VAL A 320 13.259 21.603 6.592 1.00 25.51 O ANISOU 1196 O VAL A 320 3119 2782 3792 -46 -728 -274 O ATOM 1197 CB VAL A 320 13.181 22.154 9.429 1.00 26.05 C ANISOU 1197 CB VAL A 320 3216 2897 3784 45 -615 -199 C ATOM 1198 CG1 VAL A 320 13.382 22.869 10.758 1.00 28.29 C ANISOU 1198 CG1 VAL A 320 3530 3210 4011 102 -548 -189 C ATOM 1199 CG2 VAL A 320 12.163 21.013 9.561 1.00 24.24 C ANISOU 1199 CG2 VAL A 320 2930 2664 3617 15 -642 -108 C ATOM 1200 N ASP A 321 11.278 22.640 6.462 1.00 24.81 N ANISOU 1200 N ASP A 321 2968 2742 3715 -24 -662 -162 N ATOM 1201 CA ASP A 321 10.910 21.975 5.210 1.00 23.69 C ANISOU 1201 CA ASP A 321 2791 2578 3631 -76 -723 -162 C ATOM 1202 C ASP A 321 11.639 22.605 4.022 1.00 22.45 C ANISOU 1202 C ASP A 321 2664 2408 3459 -89 -745 -253 C ATOM 1203 O ASP A 321 11.835 23.816 3.983 1.00 26.83 O ANISOU 1203 O ASP A 321 3247 2982 3967 -57 -701 -287 O ATOM 1204 CB ASP A 321 9.398 22.053 4.982 1.00 30.09 C ANISOU 1204 CB ASP A 321 3541 3411 4479 -82 -706 -70 C ATOM 1205 CG ASP A 321 8.945 21.240 3.776 1.00 36.57 C ANISOU 1205 CG ASP A 321 4322 4208 5365 -136 -770 -60 C ATOM 1206 OD1 ASP A 321 8.998 19.993 3.858 1.00 35.92 O ANISOU 1206 OD1 ASP A 321 4221 4102 5326 -169 -818 -41 O ATOM 1207 OD2 ASP A 321 8.537 21.849 2.753 1.00 30.71 O ANISOU 1207 OD2 ASP A 321 3565 3472 4631 -146 -772 -72 O ATOM 1208 N GLN A 322 12.025 21.783 3.051 1.00 24.46 N ANISOU 1208 N GLN A 322 2912 2629 3753 -136 -814 -292 N ATOM 1209 CA GLN A 322 12.693 22.279 1.850 1.00 29.93 C ANISOU 1209 CA GLN A 322 3629 3306 4435 -153 -841 -378 C ATOM 1210 C GLN A 322 11.813 23.183 0.977 1.00 30.67 C ANISOU 1210 C GLN A 322 3697 3421 4535 -152 -820 -358 C ATOM 1211 O GLN A 322 12.334 24.018 0.248 1.00 30.81 O ANISOU 1211 O GLN A 322 3744 3439 4525 -148 -816 -425 O ATOM 1212 CB GLN A 322 13.251 21.123 1.017 1.00 36.40 C ANISOU 1212 CB GLN A 322 4443 4086 5299 -204 -922 -420 C ATOM 1213 CG GLN A 322 12.217 20.065 0.667 1.00 53.75 C ANISOU 1213 CG GLN A 322 6580 6274 7567 -243 -962 -344 C ATOM 1214 CD GLN A 322 12.755 19.003 -0.287 1.00 58.53 C ANISOU 1214 CD GLN A 322 7187 6841 8209 -270 -1024 -374 C ATOM 1215 OE1 GLN A 322 13.532 19.299 -1.197 1.00 54.20 O ANISOU 1215 OE1 GLN A 322 6674 6284 7636 -236 -1015 -419 O ATOM 1216 NE2 GLN A 322 12.341 17.758 -0.077 1.00 59.10 N ANISOU 1216 NE2 GLN A 322 7224 6897 8335 -304 -1068 -326 N ATOM 1217 N ASN A 323 10.493 23.020 1.052 1.00 29.15 N ANISOU 1217 N ASN A 323 3450 3246 4378 -155 -806 -266 N ATOM 1218 CA ASN A 323 9.568 23.878 0.306 1.00 20.95 C ANISOU 1218 CA ASN A 323 2385 2229 3345 -152 -782 -240 C ATOM 1219 C ASN A 323 9.016 25.026 1.147 1.00 23.66 C ANISOU 1219 C ASN A 323 2733 2613 3643 -100 -702 -199 C ATOM 1220 O ASN A 323 9.126 26.194 0.772 1.00 25.75 O ANISOU 1220 O ASN A 323 3021 2894 3871 -77 -669 -235 O ATOM 1221 CB ASN A 323 8.401 23.060 -0.241 1.00 19.13 C ANISOU 1221 CB ASN A 323 2090 1995 3183 -189 -816 -166 C ATOM 1222 CG ASN A 323 8.854 21.798 -0.930 1.00 28.81 C ANISOU 1222 CG ASN A 323 3307 3182 4459 -240 -895 -195 C ATOM 1223 OD1 ASN A 323 9.725 21.839 -1.799 1.00 22.90 O ANISOU 1223 OD1 ASN A 323 2586 2411 3704 -259 -933 -277 O ATOM 1224 ND2 ASN A 323 8.269 20.659 -0.542 1.00 25.54 N ANISOU 1224 ND2 ASN A 323 2853 2759 4093 -262 -921 -128 N ATOM 1225 N ALA A 324 8.416 24.676 2.281 1.00 20.73 N ANISOU 1225 N ALA A 324 2341 2258 3276 -81 -673 -123 N ATOM 1226 CA ALA A 324 7.736 25.643 3.139 1.00 17.24 C ANISOU 1226 CA ALA A 324 1896 1856 2798 -32 -598 -70 C ATOM 1227 C ALA A 324 8.639 26.727 3.732 1.00 24.64 C ANISOU 1227 C ALA A 324 2892 2807 3664 14 -550 -131 C ATOM 1228 O ALA A 324 8.170 27.833 4.017 1.00 28.47 O ANISOU 1228 O ALA A 324 3381 3324 4115 51 -491 -110 O ATOM 1229 CB ALA A 324 7.002 24.927 4.251 1.00 21.23 C ANISOU 1229 CB ALA A 324 2368 2374 3324 -24 -581 20 C ATOM 1230 N ASN A 325 9.920 26.420 3.936 1.00 20.35 N ANISOU 1230 N ASN A 325 2394 2239 3097 11 -573 -204 N ATOM 1231 CA ASN A 325 10.823 27.419 4.501 1.00 21.50 C ANISOU 1231 CA ASN A 325 2597 2396 3176 54 -529 -264 C ATOM 1232 C ASN A 325 10.783 28.689 3.647 1.00 21.10 C ANISOU 1232 C ASN A 325 2560 2358 3098 66 -505 -305 C ATOM 1233 O ASN A 325 10.878 29.799 4.161 1.00 22.87 O ANISOU 1233 O ASN A 325 2812 2608 3271 110 -448 -315 O ATOM 1234 CB ASN A 325 12.259 26.876 4.678 1.00 18.12 C ANISOU 1234 CB ASN A 325 2217 1937 2730 45 -564 -345 C ATOM 1235 CG ASN A 325 13.086 26.928 3.398 1.00 20.37 C ANISOU 1235 CG ASN A 325 2525 2195 3020 13 -613 -434 C ATOM 1236 OD1 ASN A 325 13.153 25.955 2.645 1.00 24.45 O ANISOU 1236 OD1 ASN A 325 3022 2685 3585 -33 -676 -444 O ATOM 1237 ND2 ASN A 325 13.719 28.066 3.146 1.00 15.04 N ANISOU 1237 ND2 ASN A 325 1892 1528 2295 37 -585 -501 N ATOM 1238 N HIS A 326 10.593 28.516 2.343 1.00 15.44 N ANISOU 1238 N HIS A 326 1824 1626 2418 27 -549 -324 N ATOM 1239 CA HIS A 326 10.482 29.654 1.441 1.00 20.40 C ANISOU 1239 CA HIS A 326 2461 2265 3025 35 -531 -359 C ATOM 1240 C HIS A 326 9.182 30.461 1.633 1.00 18.65 C ANISOU 1240 C HIS A 326 2205 2081 2801 62 -477 -283 C ATOM 1241 O HIS A 326 9.126 31.637 1.289 1.00 21.62 O ANISOU 1241 O HIS A 326 2598 2474 3143 85 -441 -307 O ATOM 1242 CB HIS A 326 10.661 29.207 -0.014 1.00 19.13 C ANISOU 1242 CB HIS A 326 2289 2076 2904 -15 -596 -403 C ATOM 1243 CG HIS A 326 11.992 28.584 -0.286 1.00 22.03 C ANISOU 1243 CG HIS A 326 2694 2409 3268 -39 -646 -487 C ATOM 1244 ND1 HIS A 326 13.155 29.322 -0.361 1.00 19.62 N ANISOU 1244 ND1 HIS A 326 2445 2098 2911 -21 -635 -576 N ATOM 1245 CD2 HIS A 326 12.353 27.293 -0.484 1.00 17.09 C ANISOU 1245 CD2 HIS A 326 2058 1752 2684 -79 -708 -496 C ATOM 1246 CE1 HIS A 326 14.171 28.513 -0.595 1.00 17.17 C ANISOU 1246 CE1 HIS A 326 2153 1761 2609 -39 -680 -624 C ATOM 1247 NE2 HIS A 326 13.711 27.277 -0.677 1.00 20.15 N ANISOU 1247 NE2 HIS A 326 2495 2118 3044 -82 -732 -588 N ATOM 1248 N VAL A 327 8.149 29.832 2.188 1.00 18.41 N ANISOU 1248 N VAL A 327 2127 2062 2805 59 -470 -191 N ATOM 1249 CA VAL A 327 6.908 30.543 2.514 1.00 17.60 C ANISOU 1249 CA VAL A 327 1991 1997 2698 87 -417 -114 C ATOM 1250 C VAL A 327 7.151 31.519 3.664 1.00 18.09 C ANISOU 1250 C VAL A 327 2088 2087 2697 144 -347 -114 C ATOM 1251 O VAL A 327 6.742 32.678 3.604 1.00 19.67 O ANISOU 1251 O VAL A 327 2293 2315 2867 175 -300 -109 O ATOM 1252 CB VAL A 327 5.759 29.579 2.906 1.00 19.89 C ANISOU 1252 CB VAL A 327 2222 2294 3041 70 -426 -13 C ATOM 1253 CG1 VAL A 327 4.545 30.373 3.385 1.00 17.38 C ANISOU 1253 CG1 VAL A 327 1873 2017 2712 105 -365 64 C ATOM 1254 CG2 VAL A 327 5.387 28.643 1.742 1.00 16.47 C ANISOU 1254 CG2 VAL A 327 1750 1836 2674 14 -493 -6 C ATOM 1255 N ILE A 328 7.822 31.037 4.709 1.00 16.69 N ANISOU 1255 N ILE A 328 1936 1905 2502 159 -343 -122 N ATOM 1256 CA ILE A 328 8.142 31.871 5.861 1.00 18.83 C ANISOU 1256 CA ILE A 328 2242 2200 2713 213 -280 -126 C ATOM 1257 C ILE A 328 9.040 33.040 5.465 1.00 20.57 C ANISOU 1257 C ILE A 328 2515 2420 2881 235 -260 -214 C ATOM 1258 O ILE A 328 8.840 34.169 5.916 1.00 22.03 O ANISOU 1258 O ILE A 328 2715 2634 3021 279 -201 -208 O ATOM 1259 CB ILE A 328 8.829 31.058 6.983 1.00 23.98 C ANISOU 1259 CB ILE A 328 2913 2840 3356 221 -286 -127 C ATOM 1260 CG1 ILE A 328 7.910 29.930 7.466 1.00 23.28 C ANISOU 1260 CG1 ILE A 328 2773 2754 3318 202 -301 -35 C ATOM 1261 CG2 ILE A 328 9.197 31.970 8.147 1.00 20.72 C ANISOU 1261 CG2 ILE A 328 2539 2454 2880 279 -221 -136 C ATOM 1262 CD1 ILE A 328 6.514 30.403 7.803 1.00 23.09 C ANISOU 1262 CD1 ILE A 328 2704 2767 3301 224 -254 56 C ATOM 1263 N GLN A 329 10.029 32.764 4.618 1.00 17.75 N ANISOU 1263 N GLN A 329 2185 2030 2528 204 -309 -296 N ATOM 1264 CA GLN A 329 10.936 33.802 4.146 1.00 24.39 C ANISOU 1264 CA GLN A 329 3076 2868 3322 220 -296 -384 C ATOM 1265 C GLN A 329 10.187 34.841 3.319 1.00 18.43 C ANISOU 1265 C GLN A 329 2307 2134 2564 226 -272 -373 C ATOM 1266 O GLN A 329 10.497 36.021 3.378 1.00 22.84 O ANISOU 1266 O GLN A 329 2898 2707 3073 260 -230 -411 O ATOM 1267 CB GLN A 329 12.089 33.206 3.327 1.00 21.94 C ANISOU 1267 CB GLN A 329 2795 2520 3023 181 -359 -470 C ATOM 1268 CG GLN A 329 13.013 32.299 4.117 1.00 20.05 C ANISOU 1268 CG GLN A 329 2579 2259 2778 177 -381 -496 C ATOM 1269 CD GLN A 329 14.341 32.074 3.411 1.00 24.00 C ANISOU 1269 CD GLN A 329 3122 2727 3271 152 -429 -598 C ATOM 1270 OE1 GLN A 329 15.170 32.981 3.327 1.00 21.54 O ANISOU 1270 OE1 GLN A 329 2857 2417 2911 174 -408 -668 O ATOM 1271 NE2 GLN A 329 14.545 30.868 2.895 1.00 16.60 N ANISOU 1271 NE2 GLN A 329 2168 1760 2381 106 -494 -605 N ATOM 1272 N LYS A 330 9.210 34.390 2.542 1.00 16.96 N ANISOU 1272 N LYS A 330 2069 1945 2429 193 -300 -323 N ATOM 1273 CA LYS A 330 8.371 35.296 1.773 1.00 17.74 C ANISOU 1273 CA LYS A 330 2148 2064 2530 198 -278 -304 C ATOM 1274 C LYS A 330 7.528 36.181 2.693 1.00 23.82 C ANISOU 1274 C LYS A 330 2907 2874 3270 248 -207 -240 C ATOM 1275 O LYS A 330 7.426 37.398 2.479 1.00 21.26 O ANISOU 1275 O LYS A 330 2600 2570 2909 276 -167 -259 O ATOM 1276 CB LYS A 330 7.457 34.513 0.834 1.00 19.45 C ANISOU 1276 CB LYS A 330 2308 2270 2812 153 -324 -257 C ATOM 1277 CG LYS A 330 6.516 35.392 0.041 1.00 19.94 C ANISOU 1277 CG LYS A 330 2345 2353 2879 157 -303 -232 C ATOM 1278 CD LYS A 330 7.292 36.284 -0.901 1.00 27.13 C ANISOU 1278 CD LYS A 330 3296 3253 3759 156 -308 -320 C ATOM 1279 CE LYS A 330 7.934 35.464 -2.004 1.00 32.11 C ANISOU 1279 CE LYS A 330 3929 3847 4425 105 -380 -377 C ATOM 1280 NZ LYS A 330 8.787 36.318 -2.881 1.00 30.94 N ANISOU 1280 NZ LYS A 330 3824 3688 4245 104 -385 -467 N ATOM 1281 N VAL A 331 6.932 35.571 3.715 1.00 18.57 N ANISOU 1281 N VAL A 331 2214 2223 2619 259 -191 -166 N ATOM 1282 CA VAL A 331 6.157 36.315 4.704 1.00 15.63 C ANISOU 1282 CA VAL A 331 1832 1890 2218 307 -123 -103 C ATOM 1283 C VAL A 331 7.001 37.440 5.285 1.00 19.22 C ANISOU 1283 C VAL A 331 2343 2357 2604 354 -76 -160 C ATOM 1284 O VAL A 331 6.606 38.598 5.286 1.00 20.57 O ANISOU 1284 O VAL A 331 2519 2553 2742 387 -28 -154 O ATOM 1285 CB VAL A 331 5.726 35.403 5.864 1.00 22.31 C ANISOU 1285 CB VAL A 331 2651 2743 3081 313 -116 -30 C ATOM 1286 CG1 VAL A 331 5.327 36.236 7.075 1.00 21.36 C ANISOU 1286 CG1 VAL A 331 2538 2662 2917 370 -44 13 C ATOM 1287 CG2 VAL A 331 4.601 34.472 5.426 1.00 16.48 C ANISOU 1287 CG2 VAL A 331 1849 2002 2409 275 -149 47 C ATOM 1288 N VAL A 332 8.179 37.077 5.772 1.00 22.10 N ANISOU 1288 N VAL A 332 2749 2701 2946 356 -89 -217 N ATOM 1289 CA VAL A 332 9.119 38.033 6.336 1.00 27.03 C ANISOU 1289 CA VAL A 332 3431 3334 3507 398 -50 -279 C ATOM 1290 C VAL A 332 9.448 39.171 5.366 1.00 29.25 C ANISOU 1290 C VAL A 332 3739 3613 3760 402 -41 -344 C ATOM 1291 O VAL A 332 9.635 40.322 5.771 1.00 23.63 O ANISOU 1291 O VAL A 332 3058 2923 2998 445 10 -365 O ATOM 1292 CB VAL A 332 10.418 37.323 6.727 1.00 26.73 C ANISOU 1292 CB VAL A 332 3432 3266 3457 388 -81 -342 C ATOM 1293 CG1 VAL A 332 11.482 38.330 7.077 1.00 23.40 C ANISOU 1293 CG1 VAL A 332 3072 2848 2972 425 -47 -418 C ATOM 1294 CG2 VAL A 332 10.160 36.366 7.876 1.00 19.39 C ANISOU 1294 CG2 VAL A 332 2483 2341 2544 394 -78 -280 C ATOM 1295 N ALA A 333 9.521 38.840 4.083 1.00 16.56 N ANISOU 1295 N ALA A 333 2121 1983 2188 357 -92 -376 N ATOM 1296 CA ALA A 333 9.850 39.828 3.067 1.00 20.02 C ANISOU 1296 CA ALA A 333 2584 2418 2605 356 -90 -438 C ATOM 1297 C ALA A 333 8.707 40.789 2.737 1.00 14.19 C ANISOU 1297 C ALA A 333 1819 1710 1864 375 -51 -389 C ATOM 1298 O ALA A 333 8.956 41.952 2.484 1.00 19.80 O ANISOU 1298 O ALA A 333 2559 2431 2534 400 -19 -430 O ATOM 1299 CB ALA A 333 10.362 39.144 1.788 1.00 13.55 C ANISOU 1299 CB ALA A 333 1764 1563 1822 302 -160 -492 C ATOM 1300 N VAL A 334 7.464 40.320 2.737 1.00 23.62 N ANISOU 1300 N VAL A 334 2957 2918 3101 364 -52 -302 N ATOM 1301 CA VAL A 334 6.377 41.142 2.196 1.00 25.29 C ANISOU 1301 CA VAL A 334 3139 3154 3317 374 -25 -260 C ATOM 1302 C VAL A 334 5.227 41.480 3.152 1.00 25.54 C ANISOU 1302 C VAL A 334 3138 3224 3342 411 30 -169 C ATOM 1303 O VAL A 334 4.301 42.197 2.778 1.00 22.26 O ANISOU 1303 O VAL A 334 2699 2832 2929 423 56 -132 O ATOM 1304 CB VAL A 334 5.781 40.526 0.897 1.00 25.90 C ANISOU 1304 CB VAL A 334 3174 3214 3452 323 -79 -246 C ATOM 1305 CG1 VAL A 334 6.873 40.302 -0.142 1.00 23.87 C ANISOU 1305 CG1 VAL A 334 2948 2922 3200 287 -131 -337 C ATOM 1306 CG2 VAL A 334 5.038 39.225 1.196 1.00 15.06 C ANISOU 1306 CG2 VAL A 334 1749 1837 2135 296 -108 -170 C ATOM 1307 N ILE A 335 5.273 40.963 4.372 1.00 23.48 N ANISOU 1307 N ILE A 335 2875 2971 3074 430 47 -133 N ATOM 1308 CA ILE A 335 4.219 41.244 5.345 1.00 19.67 C ANISOU 1308 CA ILE A 335 2363 2526 2585 466 99 -46 C ATOM 1309 C ILE A 335 4.782 42.024 6.531 1.00 23.35 C ANISOU 1309 C ILE A 335 2871 3011 2989 520 154 -65 C ATOM 1310 O ILE A 335 5.853 41.688 7.051 1.00 24.59 O ANISOU 1310 O ILE A 335 3067 3151 3126 524 145 -114 O ATOM 1311 CB ILE A 335 3.579 39.947 5.854 1.00 16.92 C ANISOU 1311 CB ILE A 335 1968 2175 2285 444 76 30 C ATOM 1312 CG1 ILE A 335 3.099 39.091 4.680 1.00 19.12 C ANISOU 1312 CG1 ILE A 335 2206 2432 2627 388 16 44 C ATOM 1313 CG2 ILE A 335 2.422 40.251 6.785 1.00 19.08 C ANISOU 1313 CG2 ILE A 335 2207 2489 2554 479 129 121 C ATOM 1314 CD1 ILE A 335 2.014 39.750 3.862 1.00 16.33 C ANISOU 1314 CD1 ILE A 335 1817 2097 2289 386 29 80 C ATOM 1315 N PRO A 336 4.070 43.076 6.956 1.00 22.71 N ANISOU 1315 N PRO A 336 2785 2966 2878 563 213 -27 N ATOM 1316 CA PRO A 336 4.531 43.857 8.110 1.00 18.49 C ANISOU 1316 CA PRO A 336 2289 2452 2284 618 268 -41 C ATOM 1317 C PRO A 336 4.707 42.973 9.341 1.00 24.43 C ANISOU 1317 C PRO A 336 3038 3206 3039 627 272 -6 C ATOM 1318 O PRO A 336 3.976 41.995 9.511 1.00 21.96 O ANISOU 1318 O PRO A 336 2680 2894 2772 605 252 62 O ATOM 1319 CB PRO A 336 3.409 44.882 8.320 1.00 18.96 C ANISOU 1319 CB PRO A 336 2325 2552 2326 655 324 17 C ATOM 1320 CG PRO A 336 2.780 45.037 6.955 1.00 23.96 C ANISOU 1320 CG PRO A 336 2931 3179 2994 622 297 20 C ATOM 1321 CD PRO A 336 2.889 43.674 6.300 1.00 22.79 C ANISOU 1321 CD PRO A 336 2757 2998 2904 564 229 20 C ATOM 1322 N LEU A 337 5.669 43.335 10.185 1.00 25.57 N ANISOU 1322 N LEU A 337 3230 3351 3135 661 297 -52 N ATOM 1323 CA LEU A 337 6.098 42.505 11.304 1.00 23.07 C ANISOU 1323 CA LEU A 337 2920 3030 2815 669 296 -37 C ATOM 1324 C LEU A 337 4.949 42.131 12.244 1.00 25.69 C ANISOU 1324 C LEU A 337 3205 3392 3163 686 325 67 C ATOM 1325 O LEU A 337 4.872 40.996 12.736 1.00 26.81 O ANISOU 1325 O LEU A 337 3327 3525 3336 668 301 105 O ATOM 1326 CB LEU A 337 7.230 43.208 12.072 1.00 19.22 C ANISOU 1326 CB LEU A 337 2493 2544 2265 710 329 -103 C ATOM 1327 CG LEU A 337 7.613 42.681 13.461 1.00 24.38 C ANISOU 1327 CG LEU A 337 3159 3204 2901 736 346 -84 C ATOM 1328 CD1 LEU A 337 8.026 41.207 13.413 1.00 20.88 C ANISOU 1328 CD1 LEU A 337 2705 2728 2500 692 288 -85 C ATOM 1329 CD2 LEU A 337 8.713 43.528 14.088 1.00 20.34 C ANISOU 1329 CD2 LEU A 337 2708 2695 2326 778 380 -154 C ATOM 1330 N LYS A 338 4.049 43.079 12.478 1.00 24.67 N ANISOU 1330 N LYS A 338 3059 3298 3015 722 376 113 N ATOM 1331 CA LYS A 338 2.988 42.890 13.460 1.00 25.40 C ANISOU 1331 CA LYS A 338 3112 3425 3115 746 412 209 C ATOM 1332 C LYS A 338 2.257 41.557 13.232 1.00 27.39 C ANISOU 1332 C LYS A 338 3310 3666 3433 701 369 274 C ATOM 1333 O LYS A 338 1.935 40.844 14.178 1.00 26.46 O ANISOU 1333 O LYS A 338 3170 3557 3325 707 376 332 O ATOM 1334 CB LYS A 338 2.025 44.092 13.450 1.00 23.04 C ANISOU 1334 CB LYS A 338 2796 3164 2793 782 465 248 C ATOM 1335 CG LYS A 338 0.915 44.044 14.500 1.00 24.59 C ANISOU 1335 CG LYS A 338 2953 3399 2991 813 508 345 C ATOM 1336 CD LYS A 338 1.471 43.694 15.871 1.00 25.61 C ANISOU 1336 CD LYS A 338 3103 3534 3093 843 530 351 C ATOM 1337 CE LYS A 338 0.375 43.542 16.906 1.00 24.58 C ANISOU 1337 CE LYS A 338 2930 3440 2967 870 569 450 C ATOM 1338 NZ LYS A 338 0.910 42.808 18.093 1.00 27.82 N ANISOU 1338 NZ LYS A 338 3355 3849 3368 883 573 461 N ATOM 1339 N ASN A 339 2.052 41.204 11.969 1.00 29.43 N ANISOU 1339 N ASN A 339 3547 3902 3733 654 321 261 N ATOM 1340 CA ASN A 339 1.330 39.988 11.619 1.00 24.37 C ANISOU 1340 CA ASN A 339 2854 3249 3156 608 278 320 C ATOM 1341 C ASN A 339 2.084 38.688 11.856 1.00 25.97 C ANISOU 1341 C ASN A 339 3064 3419 3384 576 230 302 C ATOM 1342 O ASN A 339 1.471 37.637 12.043 1.00 32.03 O ANISOU 1342 O ASN A 339 3790 4183 4197 551 206 365 O ATOM 1343 CB ASN A 339 0.884 40.051 10.164 1.00 20.54 C ANISOU 1343 CB ASN A 339 2345 2751 2708 569 242 309 C ATOM 1344 CG ASN A 339 -0.054 41.192 9.909 1.00 22.92 C ANISOU 1344 CG ASN A 339 2629 3085 2993 597 286 341 C ATOM 1345 OD1 ASN A 339 0.351 42.229 9.395 1.00 33.61 O ANISOU 1345 OD1 ASN A 339 4016 4441 4313 612 302 284 O ATOM 1346 ND2 ASN A 339 -1.307 41.025 10.296 1.00 22.00 N ANISOU 1346 ND2 ASN A 339 2462 2997 2900 604 308 433 N ATOM 1347 N TRP A 340 3.409 38.746 11.841 1.00 26.23 N ANISOU 1347 N TRP A 340 3150 3427 3388 577 214 216 N ATOM 1348 CA TRP A 340 4.189 37.523 11.997 1.00 27.77 C ANISOU 1348 CA TRP A 340 3355 3589 3606 546 165 192 C ATOM 1349 C TRP A 340 5.105 37.551 13.217 1.00 28.36 C ANISOU 1349 C TRP A 340 3473 3666 3636 581 191 164 C ATOM 1350 O TRP A 340 6.060 36.789 13.309 1.00 29.27 O ANISOU 1350 O TRP A 340 3613 3751 3756 562 154 119 O ATOM 1351 CB TRP A 340 4.954 37.169 10.712 1.00 20.56 C ANISOU 1351 CB TRP A 340 2459 2636 2716 499 104 116 C ATOM 1352 CG TRP A 340 5.828 38.249 10.138 1.00 20.18 C ANISOU 1352 CG TRP A 340 2461 2582 2625 513 114 26 C ATOM 1353 CD1 TRP A 340 5.477 39.168 9.195 1.00 23.33 C ANISOU 1353 CD1 TRP A 340 2858 2989 3018 513 123 8 C ATOM 1354 CD2 TRP A 340 7.215 38.487 10.434 1.00 18.84 C ANISOU 1354 CD2 TRP A 340 2352 2395 2412 528 114 -60 C ATOM 1355 NE1 TRP A 340 6.552 39.980 8.895 1.00 22.22 N ANISOU 1355 NE1 TRP A 340 2773 2838 2834 527 130 -83 N ATOM 1356 CE2 TRP A 340 7.633 39.580 9.641 1.00 21.09 C ANISOU 1356 CE2 TRP A 340 2668 2680 2667 536 124 -126 C ATOM 1357 CE3 TRP A 340 8.146 37.882 11.290 1.00 21.85 C ANISOU 1357 CE3 TRP A 340 2763 2762 2777 534 105 -88 C ATOM 1358 CZ2 TRP A 340 8.936 40.090 9.684 1.00 23.39 C ANISOU 1358 CZ2 TRP A 340 3019 2956 2913 550 127 -218 C ATOM 1359 CZ3 TRP A 340 9.446 38.391 11.338 1.00 23.45 C ANISOU 1359 CZ3 TRP A 340 3026 2951 2934 550 108 -180 C ATOM 1360 CH2 TRP A 340 9.825 39.485 10.540 1.00 25.24 C ANISOU 1360 CH2 TRP A 340 3281 3177 3132 557 119 -243 C ATOM 1361 N GLU A 341 4.787 38.425 14.160 1.00 24.40 N ANISOU 1361 N GLU A 341 2980 3200 3092 634 254 193 N ATOM 1362 CA GLU A 341 5.521 38.493 15.404 1.00 26.54 C ANISOU 1362 CA GLU A 341 3287 3478 3319 673 284 177 C ATOM 1363 C GLU A 341 5.427 37.168 16.166 1.00 27.00 C ANISOU 1363 C GLU A 341 3323 3527 3409 657 262 227 C ATOM 1364 O GLU A 341 6.348 36.793 16.886 1.00 29.54 O ANISOU 1364 O GLU A 341 3679 3836 3709 667 258 193 O ATOM 1365 CB GLU A 341 4.983 39.638 16.250 1.00 32.60 C ANISOU 1365 CB GLU A 341 4057 4288 4040 732 357 212 C ATOM 1366 CG GLU A 341 5.978 40.199 17.234 1.00 47.96 C ANISOU 1366 CG GLU A 341 6056 6240 5925 777 393 162 C ATOM 1367 CD GLU A 341 5.414 41.378 18.008 1.00 55.63 C ANISOU 1367 CD GLU A 341 7030 7255 6852 836 463 196 C ATOM 1368 OE1 GLU A 341 4.189 41.635 17.908 1.00 54.48 O ANISOU 1368 OE1 GLU A 341 6840 7137 6724 841 485 268 O ATOM 1369 OE2 GLU A 341 6.201 42.044 18.711 1.00 54.25 O ANISOU 1369 OE2 GLU A 341 6901 7088 6625 877 497 150 O ATOM 1370 N PHE A 342 4.323 36.449 15.999 1.00 25.07 N ANISOU 1370 N PHE A 342 3021 3288 3215 630 246 308 N ATOM 1371 CA PHE A 342 4.160 35.172 16.686 1.00 26.98 C ANISOU 1371 CA PHE A 342 3239 3522 3491 613 224 360 C ATOM 1372 C PHE A 342 5.237 34.171 16.257 1.00 28.95 C ANISOU 1372 C PHE A 342 3512 3727 3762 571 160 298 C ATOM 1373 O PHE A 342 5.624 33.299 17.026 1.00 35.96 O ANISOU 1373 O PHE A 342 4405 4603 4655 568 147 309 O ATOM 1374 CB PHE A 342 2.747 34.599 16.487 1.00 18.86 C ANISOU 1374 CB PHE A 342 2142 2507 2515 589 216 457 C ATOM 1375 CG PHE A 342 2.460 34.123 15.082 1.00 23.25 C ANISOU 1375 CG PHE A 342 2672 3038 3125 534 160 447 C ATOM 1376 CD1 PHE A 342 2.695 32.803 14.720 1.00 23.11 C ANISOU 1376 CD1 PHE A 342 2639 2986 3157 485 98 447 C ATOM 1377 CD2 PHE A 342 1.919 34.982 14.133 1.00 23.78 C ANISOU 1377 CD2 PHE A 342 2727 3116 3193 532 169 441 C ATOM 1378 CE1 PHE A 342 2.421 32.356 13.438 1.00 25.14 C ANISOU 1378 CE1 PHE A 342 2870 3219 3462 435 47 439 C ATOM 1379 CE2 PHE A 342 1.642 34.537 12.844 1.00 22.77 C ANISOU 1379 CE2 PHE A 342 2573 2965 3114 482 118 432 C ATOM 1380 CZ PHE A 342 1.900 33.226 12.498 1.00 24.60 C ANISOU 1380 CZ PHE A 342 2790 3163 3394 434 56 431 C ATOM 1381 N ILE A 343 5.730 34.319 15.033 1.00 31.24 N ANISOU 1381 N ILE A 343 3818 3991 4063 540 122 230 N ATOM 1382 CA ILE A 343 6.776 33.445 14.513 1.00 28.37 C ANISOU 1382 CA ILE A 343 3478 3584 3718 500 60 164 C ATOM 1383 C ILE A 343 8.103 33.720 15.210 1.00 27.05 C ANISOU 1383 C ILE A 343 3371 3407 3498 529 73 91 C ATOM 1384 O ILE A 343 8.830 32.805 15.592 1.00 23.36 O ANISOU 1384 O ILE A 343 2920 2917 3040 514 42 70 O ATOM 1385 CB ILE A 343 6.950 33.646 12.997 1.00 25.02 C ANISOU 1385 CB ILE A 343 3054 3137 3314 462 19 109 C ATOM 1386 CG1 ILE A 343 5.679 33.208 12.260 1.00 23.98 C ANISOU 1386 CG1 ILE A 343 2861 3010 3241 428 -2 180 C ATOM 1387 CG2 ILE A 343 8.163 32.893 12.508 1.00 25.80 C ANISOU 1387 CG2 ILE A 343 3185 3193 3424 427 -40 31 C ATOM 1388 CD1 ILE A 343 5.762 33.334 10.754 1.00 27.79 C ANISOU 1388 CD1 ILE A 343 3339 3470 3748 389 -45 133 C ATOM 1389 N VAL A 344 8.413 34.997 15.372 1.00 22.70 N ANISOU 1389 N VAL A 344 2855 2876 2894 571 120 51 N ATOM 1390 CA VAL A 344 9.607 35.389 16.096 1.00 27.46 C ANISOU 1390 CA VAL A 344 3515 3475 3442 604 140 -15 C ATOM 1391 C VAL A 344 9.603 34.789 17.493 1.00 35.12 C ANISOU 1391 C VAL A 344 4483 4456 4403 628 161 32 C ATOM 1392 O VAL A 344 10.568 34.149 17.910 1.00 38.03 O ANISOU 1392 O VAL A 344 4882 4803 4765 623 137 -9 O ATOM 1393 CB VAL A 344 9.693 36.906 16.211 1.00 25.23 C ANISOU 1393 CB VAL A 344 3262 3219 3104 651 197 -46 C ATOM 1394 CG1 VAL A 344 10.846 37.300 17.109 1.00 36.08 C ANISOU 1394 CG1 VAL A 344 4693 4593 4423 690 223 -106 C ATOM 1395 CG2 VAL A 344 9.840 37.521 14.834 1.00 18.79 C ANISOU 1395 CG2 VAL A 344 2456 2391 2294 628 176 -101 C ATOM 1396 N ASP A 345 8.507 34.986 18.216 1.00 37.91 N ANISOU 1396 N ASP A 345 4801 4845 4758 655 205 119 N ATOM 1397 CA ASP A 345 8.425 34.514 19.591 1.00 35.19 C ANISOU 1397 CA ASP A 345 4453 4515 4402 683 230 169 C ATOM 1398 C ASP A 345 8.348 32.996 19.671 1.00 35.49 C ANISOU 1398 C ASP A 345 4464 4528 4491 641 179 205 C ATOM 1399 O ASP A 345 8.825 32.399 20.629 1.00 34.49 O ANISOU 1399 O ASP A 345 4353 4398 4355 653 180 210 O ATOM 1400 CB ASP A 345 7.262 35.182 20.324 1.00 44.24 C ANISOU 1400 CB ASP A 345 5568 5707 5533 724 292 253 C ATOM 1401 CG ASP A 345 7.596 36.605 20.764 1.00 58.23 C ANISOU 1401 CG ASP A 345 7378 7505 7240 779 351 215 C ATOM 1402 OD1 ASP A 345 7.026 37.565 20.201 1.00 48.66 O ANISOU 1402 OD1 ASP A 345 6157 6312 6019 790 375 219 O ATOM 1403 OD2 ASP A 345 8.450 36.763 21.665 1.00 71.08 O ANISOU 1403 OD2 ASP A 345 9047 9134 8825 812 372 179 O ATOM 1404 N PHE A 346 7.755 32.380 18.655 1.00 33.56 N ANISOU 1404 N PHE A 346 4180 4268 4303 592 134 229 N ATOM 1405 CA PHE A 346 7.729 30.927 18.552 1.00 28.04 C ANISOU 1405 CA PHE A 346 3456 3541 3657 546 79 255 C ATOM 1406 C PHE A 346 9.146 30.373 18.441 1.00 30.21 C ANISOU 1406 C PHE A 346 3778 3778 3923 528 35 169 C ATOM 1407 O PHE A 346 9.512 29.432 19.139 1.00 32.89 O ANISOU 1407 O PHE A 346 4121 4103 4272 522 17 180 O ATOM 1408 CB PHE A 346 6.919 30.496 17.329 1.00 21.67 C ANISOU 1408 CB PHE A 346 2603 2722 2909 496 37 284 C ATOM 1409 CG PHE A 346 6.824 29.002 17.153 1.00 29.03 C ANISOU 1409 CG PHE A 346 3505 3625 3899 447 -23 313 C ATOM 1410 CD1 PHE A 346 5.783 28.283 17.732 1.00 28.89 C ANISOU 1410 CD1 PHE A 346 3438 3622 3917 441 -17 411 C ATOM 1411 CD2 PHE A 346 7.769 28.316 16.400 1.00 31.72 C ANISOU 1411 CD2 PHE A 346 3868 3924 4260 407 -85 243 C ATOM 1412 CE1 PHE A 346 5.688 26.911 17.568 1.00 29.46 C ANISOU 1412 CE1 PHE A 346 3483 3667 4044 396 -71 439 C ATOM 1413 CE2 PHE A 346 7.682 26.946 16.227 1.00 33.88 C ANISOU 1413 CE2 PHE A 346 4116 4171 4588 362 -140 269 C ATOM 1414 CZ PHE A 346 6.639 26.239 16.811 1.00 34.30 C ANISOU 1414 CZ PHE A 346 4119 4237 4676 356 -134 368 C ATOM 1415 N VAL A 347 9.925 30.960 17.539 1.00 23.76 N ANISOU 1415 N VAL A 347 2996 2944 3089 520 18 82 N ATOM 1416 CA VAL A 347 11.286 30.520 17.258 1.00 21.48 C ANISOU 1416 CA VAL A 347 2752 2618 2792 500 -25 -8 C ATOM 1417 C VAL A 347 12.241 30.805 18.409 1.00 25.29 C ANISOU 1417 C VAL A 347 3284 3106 3219 544 7 -47 C ATOM 1418 O VAL A 347 13.244 30.120 18.572 1.00 31.27 O ANISOU 1418 O VAL A 347 4071 3836 3975 531 -27 -97 O ATOM 1419 CB VAL A 347 11.817 31.192 15.977 1.00 26.65 C ANISOU 1419 CB VAL A 347 3431 3257 3439 482 -47 -89 C ATOM 1420 CG1 VAL A 347 13.317 31.025 15.864 1.00 25.73 C ANISOU 1420 CG1 VAL A 347 3369 3109 3298 476 -77 -189 C ATOM 1421 CG2 VAL A 347 11.112 30.622 14.740 1.00 23.24 C ANISOU 1421 CG2 VAL A 347 2954 2809 3069 429 -96 -65 C ATOM 1422 N ALA A 348 11.922 31.810 19.218 1.00 26.84 N ANISOU 1422 N ALA A 348 3488 3339 3371 597 73 -23 N ATOM 1423 CA ALA A 348 12.803 32.184 20.319 1.00 27.27 C ANISOU 1423 CA ALA A 348 3590 3401 3370 642 108 -60 C ATOM 1424 C ALA A 348 12.678 31.251 21.515 1.00 33.05 C ANISOU 1424 C ALA A 348 4311 4137 4111 652 112 -3 C ATOM 1425 O ALA A 348 13.561 31.221 22.362 1.00 36.31 O ANISOU 1425 O ALA A 348 4762 4546 4487 678 124 -40 O ATOM 1426 CB ALA A 348 12.569 33.632 20.755 1.00 18.46 C ANISOU 1426 CB ALA A 348 2490 2322 2201 697 177 -60 C ATOM 1427 N THR A 349 11.591 30.493 21.601 1.00 36.42 N ANISOU 1427 N THR A 349 4683 4571 4584 631 102 87 N ATOM 1428 CA THR A 349 11.472 29.544 22.701 1.00 40.79 C ANISOU 1428 CA THR A 349 5224 5126 5149 637 103 142 C ATOM 1429 C THR A 349 12.592 28.500 22.594 1.00 42.58 C ANISOU 1429 C THR A 349 5478 5311 5389 605 45 83 C ATOM 1430 O THR A 349 12.782 27.880 21.547 1.00 39.21 O ANISOU 1430 O THR A 349 5043 4852 5002 556 -13 54 O ATOM 1431 CB THR A 349 10.097 28.870 22.751 1.00 44.15 C ANISOU 1431 CB THR A 349 5584 5565 5625 616 99 248 C ATOM 1432 OG1 THR A 349 10.020 27.859 21.744 1.00 57.83 O ANISOU 1432 OG1 THR A 349 7292 7264 7417 556 32 246 O ATOM 1433 CG2 THR A 349 8.998 29.890 22.526 1.00 30.19 C ANISOU 1433 CG2 THR A 349 3787 3834 3851 637 145 297 C ATOM 1434 N PRO A 350 13.344 28.320 23.690 1.00 41.26 N ANISOU 1434 N PRO A 350 4742 6077 4860 929 -647 136 N ATOM 1435 CA PRO A 350 14.583 27.540 23.775 1.00 39.86 C ANISOU 1435 CA PRO A 350 4551 5865 4731 931 -670 92 C ATOM 1436 C PRO A 350 14.578 26.250 22.951 1.00 36.14 C ANISOU 1436 C PRO A 350 4081 5346 4306 878 -663 129 C ATOM 1437 O PRO A 350 15.485 26.035 22.142 1.00 30.36 O ANISOU 1437 O PRO A 350 3346 4558 3633 838 -660 71 O ATOM 1438 CB PRO A 350 14.676 27.219 25.265 1.00 43.30 C ANISOU 1438 CB PRO A 350 4972 6356 5125 1007 -703 118 C ATOM 1439 CG PRO A 350 14.027 28.379 25.925 1.00 34.55 C ANISOU 1439 CG PRO A 350 3867 5304 3957 1049 -700 121 C ATOM 1440 CD PRO A 350 12.931 28.837 25.007 1.00 34.08 C ANISOU 1440 CD PRO A 350 3825 5237 3885 1001 -664 158 C ATOM 1441 N GLU A 351 13.574 25.404 23.150 1.00 33.31 N ANISOU 1441 N GLU A 351 3725 5010 3923 878 -662 223 N ATOM 1442 CA GLU A 351 13.526 24.129 22.441 1.00 39.46 C ANISOU 1442 CA GLU A 351 4504 5745 4744 831 -659 262 C ATOM 1443 C GLU A 351 13.329 24.315 20.931 1.00 39.00 C ANISOU 1443 C GLU A 351 4459 5634 4725 755 -625 245 C ATOM 1444 O GLU A 351 13.920 23.592 20.126 1.00 39.54 O ANISOU 1444 O GLU A 351 4526 5649 4850 711 -624 223 O ATOM 1445 CB GLU A 351 12.452 23.209 23.037 1.00 45.60 C ANISOU 1445 CB GLU A 351 5280 6561 5483 849 -666 369 C ATOM 1446 CG GLU A 351 12.405 21.801 22.428 1.00 55.78 C ANISOU 1446 CG GLU A 351 6569 7808 6816 806 -667 414 C ATOM 1447 CD GLU A 351 13.767 21.114 22.380 1.00 64.55 C ANISOU 1447 CD GLU A 351 7667 8875 7983 805 -690 356 C ATOM 1448 OE1 GLU A 351 14.647 21.456 23.204 1.00 74.02 O ANISOU 1448 OE1 GLU A 351 8856 10092 9177 853 -714 303 O ATOM 1449 OE2 GLU A 351 13.956 20.225 21.519 1.00 57.71 O ANISOU 1449 OE2 GLU A 351 6801 7958 7167 755 -686 362 O ATOM 1450 N HIS A 352 12.511 25.291 20.551 1.00 32.15 N ANISOU 1450 N HIS A 352 3605 4782 3827 740 -599 254 N ATOM 1451 CA HIS A 352 12.272 25.569 19.138 1.00 35.01 C ANISOU 1451 CA HIS A 352 3982 5099 4222 670 -566 238 C ATOM 1452 C HIS A 352 13.513 26.151 18.473 1.00 31.75 C ANISOU 1452 C HIS A 352 3567 4638 3860 645 -562 135 C ATOM 1453 O HIS A 352 13.899 25.740 17.383 1.00 37.23 O ANISOU 1453 O HIS A 352 4263 5277 4605 588 -549 112 O ATOM 1454 CB HIS A 352 11.091 26.528 18.956 1.00 40.73 C ANISOU 1454 CB HIS A 352 4721 5854 4899 665 -541 272 C ATOM 1455 CG HIS A 352 9.784 25.988 19.449 1.00 42.00 C ANISOU 1455 CG HIS A 352 4885 6060 5013 682 -539 374 C ATOM 1456 ND1 HIS A 352 8.740 26.805 19.831 1.00 43.88 N ANISOU 1456 ND1 HIS A 352 5131 6348 5192 705 -528 411 N ATOM 1457 CD2 HIS A 352 9.350 24.717 19.623 1.00 41.99 C ANISOU 1457 CD2 HIS A 352 4879 6061 5014 678 -548 448 C ATOM 1458 CE1 HIS A 352 7.720 26.060 20.217 1.00 44.07 C ANISOU 1458 CE1 HIS A 352 5155 6404 5184 714 -529 503 C ATOM 1459 NE2 HIS A 352 8.065 24.790 20.102 1.00 49.16 N ANISOU 1459 NE2 HIS A 352 5792 7021 5865 698 -541 527 N ATOM 1460 N LEU A 353 14.134 27.115 19.135 1.00 32.61 N ANISOU 1460 N LEU A 353 3670 4768 3951 687 -575 74 N ATOM 1461 CA LEU A 353 15.331 27.744 18.606 1.00 30.51 C ANISOU 1461 CA LEU A 353 3402 4462 3731 667 -572 -26 C ATOM 1462 C LEU A 353 16.361 26.668 18.275 1.00 31.82 C ANISOU 1462 C LEU A 353 3555 4580 3955 646 -587 -55 C ATOM 1463 O LEU A 353 17.033 26.726 17.243 1.00 31.40 O ANISOU 1463 O LEU A 353 3502 4475 3952 595 -573 -111 O ATOM 1464 CB LEU A 353 15.899 28.745 19.619 1.00 25.01 C ANISOU 1464 CB LEU A 353 2697 3800 3006 728 -591 -81 C ATOM 1465 CG LEU A 353 17.077 29.603 19.155 1.00 25.59 C ANISOU 1465 CG LEU A 353 2768 3838 3118 712 -588 -187 C ATOM 1466 CD1 LEU A 353 16.631 30.688 18.186 1.00 25.09 C ANISOU 1466 CD1 LEU A 353 2721 3757 3054 668 -555 -208 C ATOM 1467 CD2 LEU A 353 17.793 30.209 20.340 1.00 25.67 C ANISOU 1467 CD2 LEU A 353 2764 3882 3107 779 -616 -237 C ATOM 1468 N ARG A 354 16.453 25.669 19.146 1.00 35.16 N ANISOU 1468 N ARG A 354 3966 5024 4370 684 -615 -15 N ATOM 1469 CA ARG A 354 17.454 24.617 19.015 1.00 33.03 C ANISOU 1469 CA ARG A 354 3682 4714 4152 674 -634 -42 C ATOM 1470 C ARG A 354 17.246 23.770 17.758 1.00 35.97 C ANISOU 1470 C ARG A 354 4061 5035 4571 604 -615 -19 C ATOM 1471 O ARG A 354 18.196 23.486 17.031 1.00 43.06 O ANISOU 1471 O ARG A 354 4952 5883 5524 569 -614 -78 O ATOM 1472 CB ARG A 354 17.451 23.729 20.259 1.00 36.34 C ANISOU 1472 CB ARG A 354 4090 5171 4548 732 -668 6 C ATOM 1473 CG ARG A 354 18.498 22.636 20.242 1.00 46.64 C ANISOU 1473 CG ARG A 354 5380 6438 5905 729 -692 -21 C ATOM 1474 CD ARG A 354 18.260 21.625 21.355 1.00 59.43 C ANISOU 1474 CD ARG A 354 6991 8092 7499 778 -722 46 C ATOM 1475 NE ARG A 354 17.098 20.778 21.094 1.00 70.91 N ANISOU 1475 NE ARG A 354 8453 9550 8941 754 -712 143 N ATOM 1476 CZ ARG A 354 17.058 19.822 20.168 1.00 81.49 C ANISOU 1476 CZ ARG A 354 9795 10842 10326 700 -704 164 C ATOM 1477 NH1 ARG A 354 18.115 19.593 19.394 1.00 82.69 N ANISOU 1477 NH1 ARG A 354 9941 10939 10539 665 -705 94 N ATOM 1478 NH2 ARG A 354 15.957 19.100 20.006 1.00 83.82 N ANISOU 1478 NH2 ARG A 354 10098 11146 10606 682 -695 254 N ATOM 1479 N GLN A 355 16.003 23.370 17.506 1.00 26.33 N ANISOU 1479 N GLN A 355 2851 3827 3326 585 -599 67 N ATOM 1480 CA GLN A 355 15.684 22.537 16.347 1.00 29.00 C ANISOU 1480 CA GLN A 355 3195 4119 3703 520 -581 96 C ATOM 1481 C GLN A 355 15.787 23.291 15.024 1.00 30.39 C ANISOU 1481 C GLN A 355 3383 4255 3909 459 -548 46 C ATOM 1482 O GLN A 355 16.308 22.779 14.037 1.00 38.54 O ANISOU 1482 O GLN A 355 4414 5236 4995 409 -540 16 O ATOM 1483 CB GLN A 355 14.272 21.972 16.463 1.00 32.75 C ANISOU 1483 CB GLN A 355 3680 4623 4143 517 -572 202 C ATOM 1484 CG GLN A 355 14.016 21.117 17.687 1.00 41.68 C ANISOU 1484 CG GLN A 355 4800 5793 5243 571 -602 266 C ATOM 1485 CD GLN A 355 12.622 20.522 17.664 1.00 46.84 C ANISOU 1485 CD GLN A 355 5462 6469 5867 560 -591 370 C ATOM 1486 OE1 GLN A 355 12.165 20.030 16.627 1.00 46.87 O ANISOU 1486 OE1 GLN A 355 5474 6437 5898 503 -572 397 O ATOM 1487 NE2 GLN A 355 11.932 20.574 18.801 1.00 42.57 N ANISOU 1487 NE2 GLN A 355 4920 5988 5268 613 -604 428 N ATOM 1488 N ILE A 356 15.270 24.507 14.997 1.00 25.99 N ANISOU 1488 N ILE A 356 2837 3722 3315 464 -529 37 N ATOM 1489 CA ILE A 356 15.249 25.258 13.753 1.00 24.72 C ANISOU 1489 CA ILE A 356 2689 3526 3177 406 -496 -3 C ATOM 1490 C ILE A 356 16.661 25.709 13.336 1.00 28.76 C ANISOU 1490 C ILE A 356 3193 3999 3736 391 -499 -108 C ATOM 1491 O ILE A 356 17.044 25.588 12.169 1.00 26.03 O ANISOU 1491 O ILE A 356 2849 3604 3436 333 -481 -143 O ATOM 1492 CB ILE A 356 14.293 26.443 13.861 1.00 19.12 C ANISOU 1492 CB ILE A 356 1995 2853 2415 416 -477 17 C ATOM 1493 CG1 ILE A 356 12.877 25.934 14.120 1.00 22.53 C ANISOU 1493 CG1 ILE A 356 2435 3321 2806 423 -471 121 C ATOM 1494 CG2 ILE A 356 14.320 27.271 12.594 1.00 23.10 C ANISOU 1494 CG2 ILE A 356 2512 3320 2942 358 -444 -28 C ATOM 1495 CD1 ILE A 356 11.914 27.016 14.579 1.00 24.73 C ANISOU 1495 CD1 ILE A 356 2725 3649 3023 451 -460 148 C ATOM 1496 N CYS A 357 17.435 26.211 14.294 1.00 27.15 N ANISOU 1496 N CYS A 357 2978 3818 3521 444 -522 -157 N ATOM 1497 CA CYS A 357 18.779 26.706 13.999 1.00 21.01 C ANISOU 1497 CA CYS A 357 2191 3007 2785 434 -526 -258 C ATOM 1498 C CYS A 357 19.716 25.577 13.623 1.00 23.11 C ANISOU 1498 C CYS A 357 2443 3230 3108 412 -539 -284 C ATOM 1499 O CYS A 357 20.669 25.779 12.878 1.00 27.45 O ANISOU 1499 O CYS A 357 2987 3738 3704 377 -532 -359 O ATOM 1500 CB CYS A 357 19.352 27.480 15.188 1.00 19.21 C ANISOU 1500 CB CYS A 357 1954 2816 2529 500 -549 -302 C ATOM 1501 SG CYS A 357 18.542 29.064 15.500 1.00 31.84 S ANISOU 1501 SG CYS A 357 3569 4458 4071 522 -533 -300 S ATOM 1502 N SER A 358 19.434 24.382 14.125 1.00 26.45 N ANISOU 1502 N SER A 358 2859 3662 3528 431 -559 -223 N ATOM 1503 CA SER A 358 20.308 23.244 13.881 1.00 31.22 C ANISOU 1503 CA SER A 358 3449 4229 4185 416 -577 -245 C ATOM 1504 C SER A 358 19.919 22.513 12.608 1.00 29.10 C ANISOU 1504 C SER A 358 3187 3916 3953 348 -555 -217 C ATOM 1505 O SER A 358 20.293 21.363 12.400 1.00 33.80 O ANISOU 1505 O SER A 358 3772 4483 4585 334 -568 -209 O ATOM 1506 CB SER A 358 20.301 22.294 15.080 1.00 34.89 C ANISOU 1506 CB SER A 358 3902 4723 4632 472 -612 -198 C ATOM 1507 OG SER A 358 20.817 22.968 16.220 1.00 41.26 O ANISOU 1507 OG SER A 358 4701 5567 5410 535 -634 -234 O ATOM 1508 N ASP A 359 19.181 23.197 11.746 1.00 29.87 N ANISOU 1508 N ASP A 359 3302 4008 4040 306 -521 -205 N ATOM 1509 CA ASP A 359 18.705 22.586 10.517 1.00 25.73 C ANISOU 1509 CA ASP A 359 2785 3446 3546 241 -498 -176 C ATOM 1510 C ASP A 359 19.168 23.357 9.283 1.00 23.69 C ANISOU 1510 C ASP A 359 2533 3148 3320 185 -469 -245 C ATOM 1511 O ASP A 359 19.251 24.583 9.283 1.00 26.91 O ANISOU 1511 O ASP A 359 2947 3567 3709 189 -456 -285 O ATOM 1512 CB ASP A 359 17.183 22.475 10.538 1.00 22.10 C ANISOU 1512 CB ASP A 359 2341 3015 3042 237 -483 -80 C ATOM 1513 CG ASP A 359 16.633 21.836 9.288 1.00 31.29 C ANISOU 1513 CG ASP A 359 3513 4141 4236 172 -459 -47 C ATOM 1514 OD1 ASP A 359 16.614 20.584 9.211 1.00 36.64 O ANISOU 1514 OD1 ASP A 359 4183 4801 4938 162 -473 -10 O ATOM 1515 OD2 ASP A 359 16.213 22.593 8.386 1.00 23.38 O ANISOU 1515 OD2 ASP A 359 2525 3127 3231 130 -428 -57 O ATOM 1516 N LYS A 360 19.469 22.599 8.242 1.00 25.14 N ANISOU 1516 N LYS A 360 2714 3285 3554 131 -459 -257 N ATOM 1517 CA LYS A 360 19.923 23.110 6.964 1.00 26.43 C ANISOU 1517 CA LYS A 360 2882 3407 3754 71 -432 -317 C ATOM 1518 C LYS A 360 19.048 24.253 6.440 1.00 26.31 C ANISOU 1518 C LYS A 360 2887 3404 3706 48 -399 -303 C ATOM 1519 O LYS A 360 19.554 25.251 5.936 1.00 21.54 O ANISOU 1519 O LYS A 360 2287 2786 3112 27 -382 -368 O ATOM 1520 CB LYS A 360 19.912 21.950 5.972 1.00 32.25 C ANISOU 1520 CB LYS A 360 3616 4102 4537 20 -426 -299 C ATOM 1521 CG LYS A 360 20.303 22.302 4.569 1.00 41.52 C ANISOU 1521 CG LYS A 360 4793 5232 5750 -47 -396 -354 C ATOM 1522 CD LYS A 360 19.728 21.283 3.590 1.00 47.34 C ANISOU 1522 CD LYS A 360 5534 5939 6513 -97 -384 -307 C ATOM 1523 CE LYS A 360 20.019 19.860 4.015 1.00 49.45 C ANISOU 1523 CE LYS A 360 5786 6197 6807 -80 -414 -280 C ATOM 1524 NZ LYS A 360 19.856 18.927 2.864 1.00 58.00 N ANISOU 1524 NZ LYS A 360 6868 7238 7930 -137 -402 -265 N ATOM 1525 N TYR A 361 17.732 24.108 6.555 1.00 23.41 N ANISOU 1525 N TYR A 361 2532 3062 3299 51 -390 -218 N ATOM 1526 CA TYR A 361 16.828 25.133 6.042 1.00 22.45 C ANISOU 1526 CA TYR A 361 2431 2953 3146 28 -359 -200 C ATOM 1527 C TYR A 361 16.436 26.121 7.124 1.00 22.95 C ANISOU 1527 C TYR A 361 2500 3067 3153 84 -367 -190 C ATOM 1528 O TYR A 361 16.284 27.309 6.858 1.00 22.51 O ANISOU 1528 O TYR A 361 2456 3016 3079 76 -348 -218 O ATOM 1529 CB TYR A 361 15.589 24.505 5.401 1.00 22.49 C ANISOU 1529 CB TYR A 361 2449 2955 3142 -7 -341 -118 C ATOM 1530 CG TYR A 361 15.915 23.581 4.239 1.00 24.71 C ANISOU 1530 CG TYR A 361 2726 3185 3479 -66 -331 -129 C ATOM 1531 CD1 TYR A 361 16.532 24.064 3.095 1.00 26.15 C ANISOU 1531 CD1 TYR A 361 2911 3328 3698 -119 -309 -195 C ATOM 1532 CD2 TYR A 361 15.596 22.230 4.290 1.00 24.28 C ANISOU 1532 CD2 TYR A 361 2664 3123 3439 -69 -345 -72 C ATOM 1533 CE1 TYR A 361 16.827 23.224 2.039 1.00 31.26 C ANISOU 1533 CE1 TYR A 361 3553 3930 4393 -171 -300 -206 C ATOM 1534 CE2 TYR A 361 15.882 21.384 3.239 1.00 17.66 C ANISOU 1534 CE2 TYR A 361 1821 2238 2650 -122 -337 -83 C ATOM 1535 CZ TYR A 361 16.498 21.887 2.120 1.00 25.29 C ANISOU 1535 CZ TYR A 361 2789 3168 3652 -172 -315 -150 C ATOM 1536 OH TYR A 361 16.791 21.056 1.080 1.00 30.69 O ANISOU 1536 OH TYR A 361 3468 3808 4385 -223 -307 -162 O ATOM 1537 N GLY A 362 16.295 25.626 8.349 1.00 26.09 N ANISOU 1537 N GLY A 362 2888 3500 3523 142 -395 -151 N ATOM 1538 CA GLY A 362 15.892 26.457 9.468 1.00 22.57 C ANISOU 1538 CA GLY A 362 2445 3107 3022 201 -405 -137 C ATOM 1539 C GLY A 362 16.870 27.575 9.781 1.00 21.63 C ANISOU 1539 C GLY A 362 2322 2990 2906 223 -411 -224 C ATOM 1540 O GLY A 362 16.459 28.667 10.149 1.00 28.55 O ANISOU 1540 O GLY A 362 3207 3896 3742 246 -404 -227 O ATOM 1541 N CYS A 363 18.164 27.313 9.622 1.00 20.59 N ANISOU 1541 N CYS A 363 2175 2825 2822 215 -423 -295 N ATOM 1542 CA CYS A 363 19.178 28.312 9.935 1.00 18.41 C ANISOU 1542 CA CYS A 363 1893 2549 2553 236 -430 -381 C ATOM 1543 C CYS A 363 19.138 29.497 8.960 1.00 17.72 C ANISOU 1543 C CYS A 363 1821 2441 2472 191 -398 -425 C ATOM 1544 O CYS A 363 19.477 30.610 9.336 1.00 27.18 O ANISOU 1544 O CYS A 363 3019 3653 3653 215 -400 -473 O ATOM 1545 CB CYS A 363 20.578 27.682 10.004 1.00 22.55 C ANISOU 1545 CB CYS A 363 2397 3044 3128 239 -452 -446 C ATOM 1546 SG CYS A 363 21.297 27.141 8.417 1.00 34.98 S ANISOU 1546 SG CYS A 363 3968 4550 4773 158 -431 -494 S ATOM 1547 N ARG A 364 18.718 29.256 7.719 1.00 18.21 N ANISOU 1547 N ARG A 364 1894 2470 2556 128 -370 -407 N ATOM 1548 CA ARG A 364 18.517 30.336 6.750 1.00 17.73 C ANISOU 1548 CA ARG A 364 1849 2390 2496 83 -339 -436 C ATOM 1549 C ARG A 364 17.266 31.135 7.081 1.00 17.67 C ANISOU 1549 C ARG A 364 1859 2422 2431 103 -327 -382 C ATOM 1550 O ARG A 364 17.243 32.358 6.950 1.00 19.40 O ANISOU 1550 O ARG A 364 2090 2647 2636 101 -314 -416 O ATOM 1551 CB ARG A 364 18.418 29.804 5.320 1.00 16.92 C ANISOU 1551 CB ARG A 364 1753 2243 2435 10 -312 -432 C ATOM 1552 CG ARG A 364 18.010 30.877 4.292 1.00 27.76 C ANISOU 1552 CG ARG A 364 3145 3600 3803 -38 -278 -449 C ATOM 1553 CD ARG A 364 18.964 32.103 4.307 1.00 17.48 C ANISOU 1553 CD ARG A 364 1841 2288 2511 -34 -276 -537 C ATOM 1554 NE ARG A 364 20.317 31.718 3.905 1.00 24.28 N ANISOU 1554 NE ARG A 364 2686 3112 3429 -56 -282 -611 N ATOM 1555 CZ ARG A 364 21.379 32.520 3.899 1.00 27.83 C ANISOU 1555 CZ ARG A 364 3127 3547 3898 -56 -284 -694 C ATOM 1556 NH1 ARG A 364 21.281 33.794 4.280 1.00 24.84 N ANISOU 1556 NH1 ARG A 364 2758 3188 3491 -34 -281 -718 N ATOM 1557 NH2 ARG A 364 22.556 32.037 3.509 1.00 27.87 N ANISOU 1557 NH2 ARG A 364 3116 3519 3956 -78 -289 -756 N ATOM 1558 N VAL A 365 16.228 30.439 7.523 1.00 17.22 N ANISOU 1558 N VAL A 365 1805 2394 2341 122 -333 -296 N ATOM 1559 CA VAL A 365 14.998 31.107 7.939 1.00 17.82 C ANISOU 1559 CA VAL A 365 1897 2513 2360 146 -324 -240 C ATOM 1560 C VAL A 365 15.280 32.044 9.107 1.00 19.09 C ANISOU 1560 C VAL A 365 2054 2715 2486 209 -344 -271 C ATOM 1561 O VAL A 365 14.812 33.175 9.139 1.00 18.87 O ANISOU 1561 O VAL A 365 2039 2705 2427 217 -332 -277 O ATOM 1562 CB VAL A 365 13.920 30.087 8.357 1.00 19.74 C ANISOU 1562 CB VAL A 365 2140 2784 2575 162 -331 -142 C ATOM 1563 CG1 VAL A 365 12.729 30.792 8.967 1.00 17.11 C ANISOU 1563 CG1 VAL A 365 1820 2502 2179 196 -327 -88 C ATOM 1564 CG2 VAL A 365 13.492 29.265 7.168 1.00 20.75 C ANISOU 1564 CG2 VAL A 365 2275 2875 2733 99 -310 -108 C ATOM 1565 N VAL A 366 16.050 31.567 10.076 1.00 22.09 N ANISOU 1565 N VAL A 366 2415 3108 2871 256 -375 -291 N ATOM 1566 CA VAL A 366 16.332 32.376 11.247 1.00 17.78 C ANISOU 1566 CA VAL A 366 1863 2601 2292 319 -396 -319 C ATOM 1567 C VAL A 366 17.191 33.577 10.861 1.00 22.13 C ANISOU 1567 C VAL A 366 2416 3129 2863 305 -387 -410 C ATOM 1568 O VAL A 366 17.035 34.656 11.419 1.00 22.43 O ANISOU 1568 O VAL A 366 2459 3196 2867 339 -390 -428 O ATOM 1569 CB VAL A 366 16.977 31.547 12.361 1.00 19.44 C ANISOU 1569 CB VAL A 366 2053 2831 2503 372 -431 -320 C ATOM 1570 CG1 VAL A 366 17.666 32.440 13.362 1.00 20.67 C ANISOU 1570 CG1 VAL A 366 2199 3013 2641 428 -452 -378 C ATOM 1571 CG2 VAL A 366 15.917 30.713 13.063 1.00 18.80 C ANISOU 1571 CG2 VAL A 366 1972 2790 2382 403 -442 -224 C ATOM 1572 N GLN A 367 18.075 33.407 9.884 1.00 19.45 N ANISOU 1572 N GLN A 367 2074 2739 2579 254 -376 -466 N ATOM 1573 CA GLN A 367 18.911 34.520 9.467 1.00 21.64 C ANISOU 1573 CA GLN A 367 2352 2992 2878 236 -367 -551 C ATOM 1574 C GLN A 367 18.100 35.575 8.709 1.00 24.89 C ANISOU 1574 C GLN A 367 2786 3400 3270 202 -336 -541 C ATOM 1575 O GLN A 367 18.275 36.783 8.914 1.00 23.07 O ANISOU 1575 O GLN A 367 2562 3179 3026 218 -334 -585 O ATOM 1576 CB GLN A 367 20.110 34.048 8.636 1.00 26.37 C ANISOU 1576 CB GLN A 367 2940 3539 3542 191 -363 -616 C ATOM 1577 CG GLN A 367 21.019 35.205 8.233 1.00 38.10 C ANISOU 1577 CG GLN A 367 4425 5000 5051 173 -354 -706 C ATOM 1578 CD GLN A 367 22.295 34.781 7.520 1.00 38.45 C ANISOU 1578 CD GLN A 367 4456 4998 5158 133 -352 -775 C ATOM 1579 OE1 GLN A 367 22.806 33.687 7.724 1.00 36.95 O ANISOU 1579 OE1 GLN A 367 4249 4799 4992 140 -370 -774 O ATOM 1580 NE2 GLN A 367 22.817 35.665 6.679 1.00 45.11 N ANISOU 1580 NE2 GLN A 367 5304 5809 6026 91 -331 -837 N ATOM 1581 N THR A 368 17.224 35.116 7.822 1.00 17.03 N ANISOU 1581 N THR A 368 1805 2391 2276 156 -313 -485 N ATOM 1582 CA THR A 368 16.339 36.022 7.102 1.00 21.81 C ANISOU 1582 CA THR A 368 2433 2995 2860 125 -284 -467 C ATOM 1583 C THR A 368 15.486 36.833 8.076 1.00 25.72 C ANISOU 1583 C THR A 368 2936 3542 3294 179 -293 -433 C ATOM 1584 O THR A 368 15.232 38.024 7.863 1.00 21.04 O ANISOU 1584 O THR A 368 2357 2952 2684 175 -280 -455 O ATOM 1585 CB THR A 368 15.432 35.247 6.146 1.00 24.01 C ANISOU 1585 CB THR A 368 2722 3256 3143 74 -261 -401 C ATOM 1586 OG1 THR A 368 16.251 34.534 5.213 1.00 23.33 O ANISOU 1586 OG1 THR A 368 2628 3121 3115 23 -253 -437 O ATOM 1587 CG2 THR A 368 14.484 36.185 5.392 1.00 16.28 C ANISOU 1587 CG2 THR A 368 1768 2276 2142 42 -232 -381 C ATOM 1588 N ILE A 369 15.059 36.189 9.156 1.00 22.47 N ANISOU 1588 N ILE A 369 2515 3173 2850 232 -315 -381 N ATOM 1589 CA ILE A 369 14.274 36.875 10.173 1.00 23.83 C ANISOU 1589 CA ILE A 369 2692 3399 2963 289 -326 -348 C ATOM 1590 C ILE A 369 15.100 37.947 10.873 1.00 25.50 C ANISOU 1590 C ILE A 369 2897 3622 3169 330 -342 -422 C ATOM 1591 O ILE A 369 14.630 39.061 11.078 1.00 28.60 O ANISOU 1591 O ILE A 369 3301 4036 3529 347 -338 -427 O ATOM 1592 CB ILE A 369 13.728 35.891 11.222 1.00 22.00 C ANISOU 1592 CB ILE A 369 2449 3211 2698 338 -348 -277 C ATOM 1593 CG1 ILE A 369 12.578 35.076 10.624 1.00 22.00 C ANISOU 1593 CG1 ILE A 369 2460 3210 2689 304 -330 -192 C ATOM 1594 CG2 ILE A 369 13.274 36.648 12.480 1.00 17.60 C ANISOU 1594 CG2 ILE A 369 1891 2712 2083 408 -366 -264 C ATOM 1595 CD1 ILE A 369 12.145 33.899 11.491 1.00 25.32 C ANISOU 1595 CD1 ILE A 369 2869 3664 3088 341 -351 -123 C ATOM 1596 N ILE A 370 16.334 37.602 11.238 1.00 24.01 N ANISOU 1596 N ILE A 370 2690 3419 3015 345 -363 -479 N ATOM 1597 CA ILE A 370 17.211 38.540 11.929 1.00 21.50 C ANISOU 1597 CA ILE A 370 2363 3111 2696 384 -380 -552 C ATOM 1598 C ILE A 370 17.504 39.752 11.054 1.00 22.80 C ANISOU 1598 C ILE A 370 2540 3242 2879 344 -358 -612 C ATOM 1599 O ILE A 370 17.512 40.890 11.534 1.00 18.32 O ANISOU 1599 O ILE A 370 1977 2695 2288 374 -364 -644 O ATOM 1600 CB ILE A 370 18.527 37.886 12.362 1.00 20.56 C ANISOU 1600 CB ILE A 370 2220 2976 2614 402 -405 -605 C ATOM 1601 CG1 ILE A 370 18.283 36.919 13.520 1.00 20.69 C ANISOU 1601 CG1 ILE A 370 2224 3035 2603 459 -433 -552 C ATOM 1602 CG2 ILE A 370 19.554 38.949 12.780 1.00 18.57 C ANISOU 1602 CG2 ILE A 370 1961 2722 2373 427 -418 -694 C ATOM 1603 CD1 ILE A 370 19.382 35.863 13.661 1.00 19.66 C ANISOU 1603 CD1 ILE A 370 2072 2881 2516 460 -452 -582 C ATOM 1604 N GLU A 371 17.724 39.492 9.769 1.00 18.83 N ANISOU 1604 N GLU A 371 2044 2691 2418 274 -334 -626 N ATOM 1605 CA GLU A 371 18.028 40.536 8.796 1.00 24.91 C ANISOU 1605 CA GLU A 371 2828 3425 3212 227 -310 -680 C ATOM 1606 C GLU A 371 16.876 41.517 8.704 1.00 28.37 C ANISOU 1606 C GLU A 371 3288 3885 3605 230 -295 -644 C ATOM 1607 O GLU A 371 17.073 42.730 8.669 1.00 28.34 O ANISOU 1607 O GLU A 371 3292 3879 3597 232 -291 -690 O ATOM 1608 CB GLU A 371 18.331 39.913 7.424 1.00 22.86 C ANISOU 1608 CB GLU A 371 2572 3113 3002 152 -285 -688 C ATOM 1609 CG GLU A 371 19.690 39.219 7.375 1.00 31.23 C ANISOU 1609 CG GLU A 371 3609 4143 4113 143 -299 -747 C ATOM 1610 CD GLU A 371 19.943 38.467 6.076 1.00 42.94 C ANISOU 1610 CD GLU A 371 5094 5579 5644 73 -276 -750 C ATOM 1611 OE1 GLU A 371 21.123 38.375 5.665 1.00 45.16 O ANISOU 1611 OE1 GLU A 371 5362 5826 5972 48 -277 -819 O ATOM 1612 OE2 GLU A 371 18.968 37.969 5.471 1.00 41.08 O ANISOU 1612 OE2 GLU A 371 4870 5340 5397 42 -258 -685 O ATOM 1613 N LYS A 372 15.665 40.978 8.701 1.00 29.37 N ANISOU 1613 N LYS A 372 3424 4035 3699 231 -287 -560 N ATOM 1614 CA LYS A 372 14.474 41.796 8.646 1.00 22.72 C ANISOU 1614 CA LYS A 372 2602 3218 2812 235 -274 -518 C ATOM 1615 C LYS A 372 14.310 42.621 9.921 1.00 25.93 C ANISOU 1615 C LYS A 372 3005 3674 3173 307 -297 -526 C ATOM 1616 O LYS A 372 13.808 43.737 9.868 1.00 24.01 O ANISOU 1616 O LYS A 372 2777 3441 2904 312 -289 -532 O ATOM 1617 CB LYS A 372 13.245 40.921 8.417 1.00 26.09 C ANISOU 1617 CB LYS A 372 3038 3661 3215 223 -262 -425 C ATOM 1618 CG LYS A 372 11.956 41.707 8.233 1.00 37.35 C ANISOU 1618 CG LYS A 372 4485 5110 4596 221 -246 -378 C ATOM 1619 CD LYS A 372 12.098 42.788 7.167 1.00 41.84 C ANISOU 1619 CD LYS A 372 5072 5641 5184 172 -221 -424 C ATOM 1620 CE LYS A 372 12.357 42.211 5.776 1.00 41.67 C ANISOU 1620 CE LYS A 372 5056 5566 5211 96 -195 -430 C ATOM 1621 NZ LYS A 372 12.105 43.234 4.703 1.00 38.57 N ANISOU 1621 NZ LYS A 372 4685 5144 4825 47 -168 -452 N ATOM 1622 N LEU A 373 14.741 42.073 11.056 1.00 21.21 N ANISOU 1622 N LEU A 373 2387 3105 2565 362 -327 -526 N ATOM 1623 CA LEU A 373 14.621 42.762 12.342 1.00 21.13 C ANISOU 1623 CA LEU A 373 2372 3146 2512 435 -351 -533 C ATOM 1624 C LEU A 373 15.792 43.705 12.616 1.00 26.62 C ANISOU 1624 C LEU A 373 3058 3826 3229 451 -364 -627 C ATOM 1625 O LEU A 373 15.953 44.197 13.732 1.00 33.72 O ANISOU 1625 O LEU A 373 3948 4763 4099 513 -389 -646 O ATOM 1626 CB LEU A 373 14.509 41.755 13.498 1.00 17.76 C ANISOU 1626 CB LEU A 373 1927 2762 2060 490 -378 -489 C ATOM 1627 CG LEU A 373 13.321 40.786 13.477 1.00 22.04 C ANISOU 1627 CG LEU A 373 2473 3326 2573 486 -370 -391 C ATOM 1628 CD1 LEU A 373 13.349 39.858 14.687 1.00 19.18 C ANISOU 1628 CD1 LEU A 373 2093 3006 2188 544 -399 -354 C ATOM 1629 CD2 LEU A 373 12.000 41.542 13.392 1.00 24.30 C ANISOU 1629 CD2 LEU A 373 2780 3642 2812 490 -355 -343 C ATOM 1630 N THR A 374 16.606 43.956 11.600 1.00 25.11 N ANISOU 1630 N THR A 374 2871 3582 3089 395 -348 -685 N ATOM 1631 CA THR A 374 17.794 44.775 11.774 1.00 22.75 C ANISOU 1631 CA THR A 374 2563 3265 2817 404 -359 -776 C ATOM 1632 C THR A 374 17.532 46.177 11.262 1.00 26.08 C ANISOU 1632 C THR A 374 3004 3674 3232 384 -342 -806 C ATOM 1633 O THR A 374 17.011 46.362 10.162 1.00 27.18 O ANISOU 1633 O THR A 374 3162 3786 3380 328 -314 -787 O ATOM 1634 CB THR A 374 19.008 44.170 11.035 1.00 22.20 C ANISOU 1634 CB THR A 374 2481 3143 2810 358 -354 -830 C ATOM 1635 OG1 THR A 374 19.319 42.897 11.606 1.00 25.99 O ANISOU 1635 OG1 THR A 374 2942 3636 3297 382 -373 -807 O ATOM 1636 CG2 THR A 374 20.221 45.071 11.159 1.00 21.90 C ANISOU 1636 CG2 THR A 374 2433 3085 2801 364 -363 -925 C ATOM 1637 N ALA A 375 17.898 47.163 12.070 1.00 21.76 N ANISOU 1637 N ALA A 375 2451 3147 2669 431 -361 -854 N ATOM 1638 CA ALA A 375 17.676 48.553 11.718 1.00 20.61 C ANISOU 1638 CA ALA A 375 2324 2993 2516 420 -350 -885 C ATOM 1639 C ALA A 375 18.793 49.004 10.797 1.00 26.88 C ANISOU 1639 C ALA A 375 3117 3730 3366 366 -337 -963 C ATOM 1640 O ALA A 375 19.681 49.770 11.200 1.00 30.57 O ANISOU 1640 O ALA A 375 3575 4191 3848 387 -352 -1034 O ATOM 1641 CB ALA A 375 17.639 49.406 12.969 1.00 27.26 C ANISOU 1641 CB ALA A 375 3159 3879 3319 493 -378 -906 C ATOM 1642 N ASP A 376 18.756 48.502 9.568 1.00 21.53 N ANISOU 1642 N ASP A 376 2449 3011 2721 297 -309 -949 N ATOM 1643 CA ASP A 376 19.750 48.855 8.563 1.00 26.40 C ANISOU 1643 CA ASP A 376 3066 3574 3392 239 -293 -1017 C ATOM 1644 C ASP A 376 19.152 49.808 7.532 1.00 24.56 C ANISOU 1644 C ASP A 376 2860 3316 3157 189 -264 -1013 C ATOM 1645 O ASP A 376 18.047 50.313 7.719 1.00 29.86 O ANISOU 1645 O ASP A 376 3547 4014 3784 208 -261 -966 O ATOM 1646 CB ASP A 376 20.347 47.599 7.902 1.00 28.90 C ANISOU 1646 CB ASP A 376 3371 3859 3752 196 -284 -1016 C ATOM 1647 CG ASP A 376 19.284 46.665 7.315 1.00 36.06 C ANISOU 1647 CG ASP A 376 4288 4768 4644 166 -265 -932 C ATOM 1648 OD1 ASP A 376 18.165 47.119 6.994 1.00 38.34 O ANISOU 1648 OD1 ASP A 376 4598 5067 4901 156 -250 -884 O ATOM 1649 OD2 ASP A 376 19.575 45.461 7.166 1.00 40.65 O ANISOU 1649 OD2 ASP A 376 4857 5340 5248 153 -267 -916 O ATOM 1650 N SER A 377 19.880 50.054 6.450 1.00 28.82 N ANISOU 1650 N SER A 377 3402 3804 3743 127 -244 -1062 N ATOM 1651 CA SER A 377 19.444 51.019 5.453 1.00 34.34 C ANISOU 1651 CA SER A 377 4126 4477 4445 79 -217 -1065 C ATOM 1652 C SER A 377 18.206 50.539 4.697 1.00 33.83 C ANISOU 1652 C SER A 377 4081 4414 4359 44 -193 -986 C ATOM 1653 O SER A 377 17.545 51.324 4.034 1.00 39.64 O ANISOU 1653 O SER A 377 4840 5139 5084 15 -173 -972 O ATOM 1654 CB SER A 377 20.582 51.351 4.481 1.00 35.41 C ANISOU 1654 CB SER A 377 4258 4558 4636 19 -201 -1138 C ATOM 1655 OG SER A 377 21.071 50.177 3.859 1.00 43.71 O ANISOU 1655 OG SER A 377 5298 5586 5724 -20 -191 -1135 O ATOM 1656 N MET A 378 17.893 49.252 4.807 1.00 29.06 N ANISOU 1656 N MET A 378 3468 3823 3751 48 -195 -934 N ATOM 1657 CA MET A 378 16.688 48.705 4.185 1.00 32.31 C ANISOU 1657 CA MET A 378 3896 4240 4142 20 -174 -854 C ATOM 1658 C MET A 378 15.420 48.974 4.996 1.00 33.61 C ANISOU 1658 C MET A 378 4070 4455 4245 72 -184 -791 C ATOM 1659 O MET A 378 14.313 48.838 4.482 1.00 34.59 O ANISOU 1659 O MET A 378 4212 4585 4346 50 -166 -729 O ATOM 1660 CB MET A 378 16.827 47.199 3.941 1.00 28.62 C ANISOU 1660 CB MET A 378 3414 3764 3695 1 -173 -822 C ATOM 1661 CG MET A 378 17.609 46.856 2.682 1.00 42.66 C ANISOU 1661 CG MET A 378 5191 5488 5528 -71 -150 -860 C ATOM 1662 SD MET A 378 17.060 47.823 1.254 1.00154.79 S ANISOU 1662 SD MET A 378 19423 19656 19736 -140 -113 -860 S ATOM 1663 CE MET A 378 15.292 47.500 1.214 1.00 33.03 C ANISOU 1663 CE MET A 378 4021 4267 4262 -132 -102 -755 C ATOM 1664 N ASN A 379 15.576 49.348 6.261 1.00 23.95 N ANISOU 1664 N ASN A 379 2835 3269 2995 140 -213 -806 N ATOM 1665 CA ASN A 379 14.411 49.624 7.100 1.00 21.91 C ANISOU 1665 CA ASN A 379 2584 3063 2677 192 -224 -749 C ATOM 1666 C ASN A 379 14.185 51.091 7.429 1.00 23.62 C ANISOU 1666 C ASN A 379 2814 3292 2869 218 -230 -779 C ATOM 1667 O ASN A 379 13.414 51.402 8.333 1.00 29.08 O ANISOU 1667 O ASN A 379 3507 4031 3512 273 -245 -745 O ATOM 1668 CB ASN A 379 14.474 48.815 8.392 1.00 21.86 C ANISOU 1668 CB ASN A 379 2557 3102 2649 257 -254 -726 C ATOM 1669 CG ASN A 379 14.017 47.400 8.193 1.00 26.66 C ANISOU 1669 CG ASN A 379 3159 3714 3256 242 -247 -660 C ATOM 1670 OD1 ASN A 379 14.498 46.474 8.848 1.00 32.14 O ANISOU 1670 OD1 ASN A 379 3832 4421 3958 270 -266 -656 O ATOM 1671 ND2 ASN A 379 13.098 47.215 7.255 1.00 21.45 N ANISOU 1671 ND2 ASN A 379 2518 3042 2592 196 -221 -608 N ATOM 1672 N VAL A 380 14.840 51.993 6.702 1.00 27.86 N ANISOU 1672 N VAL A 380 3359 3786 3439 179 -218 -841 N ATOM 1673 CA VAL A 380 14.697 53.423 6.986 1.00 26.34 C ANISOU 1673 CA VAL A 380 3178 3601 3227 202 -224 -874 C ATOM 1674 C VAL A 380 13.294 53.924 6.685 1.00 28.20 C ANISOU 1674 C VAL A 380 3440 3855 3421 198 -210 -814 C ATOM 1675 O VAL A 380 12.908 54.990 7.149 1.00 33.60 O ANISOU 1675 O VAL A 380 4133 4559 4076 231 -220 -825 O ATOM 1676 CB VAL A 380 15.714 54.295 6.208 1.00 26.70 C ANISOU 1676 CB VAL A 380 3229 3595 3320 157 -214 -953 C ATOM 1677 CG1 VAL A 380 17.115 54.082 6.742 1.00 29.90 C ANISOU 1677 CG1 VAL A 380 3609 3991 3760 175 -233 -1023 C ATOM 1678 CG2 VAL A 380 15.643 54.016 4.710 1.00 26.18 C ANISOU 1678 CG2 VAL A 380 3178 3482 3286 75 -179 -942 C ATOM 1679 N ASP A 381 12.535 53.151 5.910 1.00 24.17 N ANISOU 1679 N ASP A 381 2939 3337 2907 158 -188 -753 N ATOM 1680 CA ASP A 381 11.175 53.528 5.547 1.00 23.76 C ANISOU 1680 CA ASP A 381 2910 3301 2817 150 -173 -693 C ATOM 1681 C ASP A 381 10.163 53.313 6.676 1.00 31.38 C ANISOU 1681 C ASP A 381 3871 4329 3724 216 -191 -633 C ATOM 1682 O ASP A 381 9.022 53.756 6.572 1.00 31.37 O ANISOU 1682 O ASP A 381 3887 4347 3685 221 -183 -587 O ATOM 1683 CB ASP A 381 10.714 52.783 4.284 1.00 20.97 C ANISOU 1683 CB ASP A 381 2569 2917 2482 82 -141 -649 C ATOM 1684 CG ASP A 381 10.690 51.272 4.464 1.00 28.70 C ANISOU 1684 CG ASP A 381 3531 3908 3466 83 -144 -604 C ATOM 1685 OD1 ASP A 381 11.760 50.685 4.698 1.00 35.26 O ANISOU 1685 OD1 ASP A 381 4342 4725 4330 86 -155 -644 O ATOM 1686 OD2 ASP A 381 9.604 50.667 4.359 1.00 30.31 O ANISOU 1686 OD2 ASP A 381 3742 4133 3641 82 -135 -531 O ATOM 1687 N LEU A 382 10.568 52.633 7.744 1.00 31.14 N ANISOU 1687 N LEU A 382 3816 4329 3685 266 -216 -632 N ATOM 1688 CA LEU A 382 9.630 52.328 8.829 1.00 26.38 C ANISOU 1688 CA LEU A 382 3207 3788 3027 329 -233 -573 C ATOM 1689 C LEU A 382 9.298 53.568 9.647 1.00 29.47 C ANISOU 1689 C LEU A 382 3604 4214 3380 383 -251 -593 C ATOM 1690 O LEU A 382 10.155 54.419 9.865 1.00 29.61 O ANISOU 1690 O LEU A 382 3618 4216 3416 395 -263 -664 O ATOM 1691 CB LEU A 382 10.202 51.261 9.773 1.00 19.46 C ANISOU 1691 CB LEU A 382 2304 2936 2153 369 -256 -568 C ATOM 1692 CG LEU A 382 10.547 49.890 9.181 1.00 25.20 C ANISOU 1692 CG LEU A 382 3022 3637 2915 326 -244 -546 C ATOM 1693 CD1 LEU A 382 11.145 48.988 10.236 1.00 21.80 C ANISOU 1693 CD1 LEU A 382 2565 3232 2484 374 -271 -547 C ATOM 1694 CD2 LEU A 382 9.315 49.255 8.591 1.00 20.26 C ANISOU 1694 CD2 LEU A 382 2410 3019 2268 298 -223 -463 C ATOM 1695 N THR A 383 8.056 53.651 10.115 1.00 25.56 N ANISOU 1695 N THR A 383 3116 3765 2831 417 -253 -531 N ATOM 1696 CA THR A 383 7.678 54.618 11.140 1.00 22.77 C ANISOU 1696 CA THR A 383 2761 3456 2434 482 -276 -541 C ATOM 1697 C THR A 383 8.403 54.280 12.438 1.00 32.80 C ANISOU 1697 C THR A 383 4005 4761 3697 545 -307 -567 C ATOM 1698 O THR A 383 8.876 53.151 12.619 1.00 32.06 O ANISOU 1698 O THR A 383 3894 4666 3620 544 -311 -554 O ATOM 1699 CB THR A 383 6.154 54.591 11.432 1.00 28.06 C ANISOU 1699 CB THR A 383 3441 4176 3045 507 -272 -462 C ATOM 1700 OG1 THR A 383 5.777 53.294 11.927 1.00 32.81 O ANISOU 1700 OG1 THR A 383 4027 4810 3628 526 -276 -400 O ATOM 1701 CG2 THR A 383 5.348 54.919 10.178 1.00 20.51 C ANISOU 1701 CG2 THR A 383 2512 3189 2092 448 -242 -433 C ATOM 1702 N SER A 384 8.477 55.256 13.341 1.00 31.26 N ANISOU 1702 N SER A 384 3806 4596 3476 602 -330 -602 N ATOM 1703 CA SER A 384 9.106 55.067 14.647 1.00 30.55 C ANISOU 1703 CA SER A 384 3692 4543 3374 668 -362 -628 C ATOM 1704 C SER A 384 8.389 53.993 15.435 1.00 32.87 C ANISOU 1704 C SER A 384 3972 4891 3627 707 -371 -554 C ATOM 1705 O SER A 384 9.018 53.208 16.149 1.00 34.01 O ANISOU 1705 O SER A 384 4095 5051 3777 736 -389 -559 O ATOM 1706 CB SER A 384 9.081 56.368 15.445 1.00 34.42 C ANISOU 1706 CB SER A 384 4181 5060 3835 723 -384 -671 C ATOM 1707 OG SER A 384 9.866 57.357 14.806 1.00 43.75 O ANISOU 1707 OG SER A 384 5374 6192 5058 690 -379 -744 O ATOM 1708 N ALA A 385 7.065 53.965 15.306 1.00 24.14 N ANISOU 1708 N ALA A 385 2879 3813 2479 707 -359 -485 N ATOM 1709 CA ALA A 385 6.268 52.967 15.996 1.00 30.31 C ANISOU 1709 CA ALA A 385 3650 4647 3220 741 -365 -408 C ATOM 1710 C ALA A 385 6.670 51.584 15.501 1.00 27.21 C ANISOU 1710 C ALA A 385 3249 4226 2862 700 -354 -382 C ATOM 1711 O ALA A 385 6.871 50.659 16.295 1.00 29.83 O ANISOU 1711 O ALA A 385 3562 4587 3185 734 -370 -359 O ATOM 1712 CB ALA A 385 4.788 53.211 15.769 1.00 28.77 C ANISOU 1712 CB ALA A 385 3472 4480 2979 739 -350 -341 C ATOM 1713 N ALA A 386 6.802 51.453 14.183 1.00 17.96 N ANISOU 1713 N ALA A 386 2092 2998 1732 627 -327 -387 N ATOM 1714 CA ALA A 386 7.259 50.198 13.587 1.00 20.88 C ANISOU 1714 CA ALA A 386 2456 3335 2143 582 -315 -371 C ATOM 1715 C ALA A 386 8.682 49.850 14.024 1.00 23.28 C ANISOU 1715 C ALA A 386 2739 3621 2485 596 -335 -433 C ATOM 1716 O ALA A 386 8.986 48.689 14.286 1.00 27.23 O ANISOU 1716 O ALA A 386 3224 4126 2997 599 -342 -409 O ATOM 1717 CB ALA A 386 7.159 50.246 12.053 1.00 16.88 C ANISOU 1717 CB ALA A 386 1969 2771 1673 500 -282 -371 C ATOM 1718 N GLN A 387 9.554 50.852 14.099 1.00 22.25 N ANISOU 1718 N GLN A 387 2608 3471 2375 603 -344 -512 N ATOM 1719 CA GLN A 387 10.928 50.604 14.545 1.00 22.58 C ANISOU 1719 CA GLN A 387 2630 3498 2453 619 -363 -576 C ATOM 1720 C GLN A 387 10.943 50.015 15.952 1.00 24.03 C ANISOU 1720 C GLN A 387 2791 3737 2602 691 -393 -553 C ATOM 1721 O GLN A 387 11.721 49.110 16.243 1.00 27.17 O ANISOU 1721 O GLN A 387 3170 4128 3023 697 -405 -564 O ATOM 1722 CB GLN A 387 11.781 51.879 14.501 1.00 22.00 C ANISOU 1722 CB GLN A 387 2558 3399 2402 621 -370 -663 C ATOM 1723 CG GLN A 387 12.212 52.337 13.103 1.00 22.08 C ANISOU 1723 CG GLN A 387 2585 3344 2461 545 -343 -703 C ATOM 1724 CD GLN A 387 13.286 51.450 12.473 1.00 30.74 C ANISOU 1724 CD GLN A 387 3670 4394 3614 499 -336 -733 C ATOM 1725 OE1 GLN A 387 13.669 50.421 13.032 1.00 31.53 O ANISOU 1725 OE1 GLN A 387 3751 4508 3719 521 -350 -720 O ATOM 1726 NE2 GLN A 387 13.772 51.852 11.301 1.00 26.81 N ANISOU 1726 NE2 GLN A 387 3185 3841 3161 435 -314 -774 N ATOM 1727 N ASN A 388 10.080 50.531 16.821 1.00 23.31 N ANISOU 1727 N ASN A 388 2701 3702 2455 747 -406 -523 N ATOM 1728 CA ASN A 388 10.023 50.078 18.206 1.00 22.01 C ANISOU 1728 CA ASN A 388 2516 3596 2251 819 -435 -501 C ATOM 1729 C ASN A 388 9.556 48.640 18.264 1.00 27.99 C ANISOU 1729 C ASN A 388 3266 4368 3000 812 -430 -425 C ATOM 1730 O ASN A 388 10.049 47.834 19.057 1.00 31.52 O ANISOU 1730 O ASN A 388 3694 4837 3447 847 -451 -420 O ATOM 1731 CB ASN A 388 9.068 50.949 19.029 1.00 38.08 C ANISOU 1731 CB ASN A 388 4555 5688 4224 876 -446 -478 C ATOM 1732 CG ASN A 388 9.634 52.330 19.311 1.00 53.40 C ANISOU 1732 CG ASN A 388 6497 7624 6168 901 -459 -557 C ATOM 1733 OD1 ASN A 388 10.839 52.489 19.523 1.00 59.50 O ANISOU 1733 OD1 ASN A 388 7258 8375 6976 908 -474 -627 O ATOM 1734 ND2 ASN A 388 8.763 53.338 19.319 1.00 54.65 N ANISOU 1734 ND2 ASN A 388 6670 7803 6291 914 -456 -547 N ATOM 1735 N LEU A 389 8.586 48.325 17.416 1.00 21.85 N ANISOU 1735 N LEU A 389 2505 3581 2217 767 -404 -365 N ATOM 1736 CA LEU A 389 8.103 46.966 17.312 1.00 25.08 C ANISOU 1736 CA LEU A 389 2909 3997 2622 751 -397 -292 C ATOM 1737 C LEU A 389 9.259 46.070 16.877 1.00 23.66 C ANISOU 1737 C LEU A 389 2718 3770 2501 717 -398 -325 C ATOM 1738 O LEU A 389 9.487 45.020 17.459 1.00 31.14 O ANISOU 1738 O LEU A 389 3649 4734 3448 739 -412 -298 O ATOM 1739 CB LEU A 389 6.948 46.896 16.317 1.00 27.23 C ANISOU 1739 CB LEU A 389 3202 4258 2885 701 -367 -232 C ATOM 1740 CG LEU A 389 6.076 45.646 16.407 1.00 25.36 C ANISOU 1740 CG LEU A 389 2961 4046 2627 698 -361 -142 C ATOM 1741 CD1 LEU A 389 5.606 45.470 17.829 1.00 26.98 C ANISOU 1741 CD1 LEU A 389 3152 4323 2777 773 -386 -103 C ATOM 1742 CD2 LEU A 389 4.897 45.773 15.474 1.00 21.78 C ANISOU 1742 CD2 LEU A 389 2529 3586 2161 654 -333 -88 C ATOM 1743 N ARG A 390 10.005 46.504 15.866 1.00 26.92 N ANISOU 1743 N ARG A 390 3139 4124 2964 663 -383 -384 N ATOM 1744 CA ARG A 390 11.128 45.718 15.353 1.00 26.11 C ANISOU 1744 CA ARG A 390 3027 3973 2919 626 -381 -421 C ATOM 1745 C ARG A 390 12.188 45.518 16.431 1.00 28.38 C ANISOU 1745 C ARG A 390 3292 4279 3214 679 -413 -468 C ATOM 1746 O ARG A 390 12.714 44.414 16.612 1.00 29.35 O ANISOU 1746 O ARG A 390 3399 4394 3358 679 -423 -459 O ATOM 1747 CB ARG A 390 11.744 46.399 14.125 1.00 19.58 C ANISOU 1747 CB ARG A 390 2213 3085 2141 563 -360 -483 C ATOM 1748 CG ARG A 390 12.887 45.635 13.483 1.00 19.38 C ANISOU 1748 CG ARG A 390 2178 3009 2177 519 -356 -523 C ATOM 1749 CD ARG A 390 13.826 46.584 12.741 1.00 25.64 C ANISOU 1749 CD ARG A 390 2976 3752 3013 481 -346 -608 C ATOM 1750 NE ARG A 390 14.055 47.789 13.534 1.00 27.07 N ANISOU 1750 NE ARG A 390 3156 3958 3172 531 -364 -656 N ATOM 1751 CZ ARG A 390 14.906 47.856 14.549 1.00 29.57 C ANISOU 1751 CZ ARG A 390 3453 4294 3490 583 -393 -702 C ATOM 1752 NH1 ARG A 390 15.619 46.791 14.879 1.00 30.71 N ANISOU 1752 NH1 ARG A 390 3578 4435 3657 591 -407 -706 N ATOM 1753 NH2 ARG A 390 15.041 48.980 15.233 1.00 30.52 N ANISOU 1753 NH2 ARG A 390 3572 4435 3588 626 -409 -744 N ATOM 1754 N GLU A 391 12.494 46.588 17.154 1.00 29.00 N ANISOU 1754 N GLU A 391 3366 4379 3274 725 -431 -518 N ATOM 1755 CA GLU A 391 13.522 46.527 18.183 1.00 27.38 C ANISOU 1755 CA GLU A 391 3139 4189 3074 777 -462 -568 C ATOM 1756 C GLU A 391 13.181 45.527 19.278 1.00 32.08 C ANISOU 1756 C GLU A 391 3719 4837 3635 831 -483 -510 C ATOM 1757 O GLU A 391 14.053 44.799 19.755 1.00 38.37 O ANISOU 1757 O GLU A 391 4496 5630 4451 849 -502 -531 O ATOM 1758 CB GLU A 391 13.776 47.906 18.788 1.00 28.47 C ANISOU 1758 CB GLU A 391 3276 4346 3194 820 -477 -627 C ATOM 1759 CG GLU A 391 15.063 47.972 19.585 1.00 39.83 C ANISOU 1759 CG GLU A 391 4694 5786 4653 860 -505 -698 C ATOM 1760 CD GLU A 391 16.228 47.309 18.859 1.00 46.43 C ANISOU 1760 CD GLU A 391 5522 6565 5554 811 -499 -743 C ATOM 1761 OE1 GLU A 391 16.799 46.337 19.408 1.00 42.20 O ANISOU 1761 OE1 GLU A 391 4968 6037 5028 834 -517 -740 O ATOM 1762 OE2 GLU A 391 16.561 47.758 17.739 1.00 40.07 O ANISOU 1762 OE2 GLU A 391 4729 5708 4789 751 -477 -780 O ATOM 1763 N ARG A 392 11.913 45.482 19.673 1.00 34.93 N ANISOU 1763 N ARG A 392 4085 5244 3940 856 -480 -436 N ATOM 1764 CA ARG A 392 11.513 44.576 20.740 1.00 41.27 C ANISOU 1764 CA ARG A 392 4874 6100 4706 907 -500 -377 C ATOM 1765 C ARG A 392 11.539 43.127 20.281 1.00 36.05 C ANISOU 1765 C ARG A 392 4209 5416 4072 870 -492 -329 C ATOM 1766 O ARG A 392 11.913 42.235 21.043 1.00 35.92 O ANISOU 1766 O ARG A 392 4176 5420 4053 904 -513 -313 O ATOM 1767 CB ARG A 392 10.129 44.921 21.285 1.00 47.27 C ANISOU 1767 CB ARG A 392 5641 6920 5400 943 -498 -310 C ATOM 1768 CG ARG A 392 10.118 46.017 22.338 1.00 58.67 C ANISOU 1768 CG ARG A 392 7079 8410 6802 1010 -520 -345 C ATOM 1769 CD ARG A 392 8.938 45.814 23.282 1.00 69.94 C ANISOU 1769 CD ARG A 392 8502 9909 8161 1063 -529 -269 C ATOM 1770 NE ARG A 392 7.819 45.148 22.613 1.00 72.60 N ANISOU 1770 NE ARG A 392 8853 10246 8487 1023 -504 -186 N ATOM 1771 CZ ARG A 392 6.711 45.761 22.206 1.00 69.62 C ANISOU 1771 CZ ARG A 392 8492 9882 8079 1009 -486 -151 C ATOM 1772 NH1 ARG A 392 6.555 47.064 22.406 1.00 70.23 N ANISOU 1772 NH1 ARG A 392 8576 9974 8135 1033 -489 -191 N ATOM 1773 NH2 ARG A 392 5.754 45.067 21.605 1.00 63.05 N ANISOU 1773 NH2 ARG A 392 7669 9048 7239 972 -464 -77 N ATOM 1774 N ALA A 393 11.129 42.894 19.039 1.00 27.32 N ANISOU 1774 N ALA A 393 3119 4270 2992 802 -463 -305 N ATOM 1775 CA ALA A 393 11.183 41.555 18.481 1.00 28.56 C ANISOU 1775 CA ALA A 393 3274 4399 3180 761 -454 -265 C ATOM 1776 C ALA A 393 12.642 41.106 18.362 1.00 25.46 C ANISOU 1776 C ALA A 393 2866 3964 2843 749 -466 -331 C ATOM 1777 O ALA A 393 12.977 39.959 18.651 1.00 29.98 O ANISOU 1777 O ALA A 393 3425 4536 3429 756 -479 -309 O ATOM 1778 CB ALA A 393 10.500 41.519 17.139 1.00 28.77 C ANISOU 1778 CB ALA A 393 3320 4388 3223 691 -420 -234 C ATOM 1779 N LEU A 394 13.505 42.024 17.943 1.00 21.47 N ANISOU 1779 N LEU A 394 2363 3425 2370 732 -463 -414 N ATOM 1780 CA LEU A 394 14.928 41.737 17.848 1.00 27.59 C ANISOU 1780 CA LEU A 394 3124 4162 3197 722 -475 -485 C ATOM 1781 C LEU A 394 15.485 41.391 19.222 1.00 33.97 C ANISOU 1781 C LEU A 394 3910 5010 3987 793 -511 -497 C ATOM 1782 O LEU A 394 16.259 40.442 19.367 1.00 34.96 O ANISOU 1782 O LEU A 394 4020 5119 4143 794 -524 -507 O ATOM 1783 CB LEU A 394 15.684 42.933 17.268 1.00 23.37 C ANISOU 1783 CB LEU A 394 2595 3590 2693 697 -466 -572 C ATOM 1784 CG LEU A 394 17.193 42.774 17.096 1.00 27.99 C ANISOU 1784 CG LEU A 394 3166 4134 3335 684 -476 -653 C ATOM 1785 CD1 LEU A 394 17.498 41.639 16.133 1.00 25.38 C ANISOU 1785 CD1 LEU A 394 2833 3757 3051 624 -461 -639 C ATOM 1786 CD2 LEU A 394 17.824 44.066 16.605 1.00 26.94 C ANISOU 1786 CD2 LEU A 394 3040 3971 3226 663 -468 -734 C ATOM 1787 N GLN A 395 15.091 42.162 20.231 1.00 31.33 N ANISOU 1787 N GLN A 395 3573 4727 3603 854 -527 -495 N ATOM 1788 CA GLN A 395 15.583 41.936 21.584 1.00 33.64 C ANISOU 1788 CA GLN A 395 3846 5062 3874 926 -561 -507 C ATOM 1789 C GLN A 395 15.159 40.570 22.095 1.00 33.91 C ANISOU 1789 C GLN A 395 3871 5123 3890 944 -571 -431 C ATOM 1790 O GLN A 395 15.964 39.842 22.669 1.00 40.81 O ANISOU 1790 O GLN A 395 4728 5998 4781 969 -594 -447 O ATOM 1791 CB GLN A 395 15.099 43.024 22.535 1.00 43.78 C ANISOU 1791 CB GLN A 395 5130 6400 5103 987 -575 -513 C ATOM 1792 CG GLN A 395 16.138 44.063 22.878 1.00 53.82 C ANISOU 1792 CG GLN A 395 6394 7663 6391 1012 -590 -608 C ATOM 1793 CD GLN A 395 15.572 45.170 23.750 1.00 66.25 C ANISOU 1793 CD GLN A 395 7970 9290 7912 1070 -603 -612 C ATOM 1794 OE1 GLN A 395 14.669 45.899 23.339 1.00 61.99 O ANISOU 1794 OE1 GLN A 395 7448 8757 7349 1054 -584 -589 O ATOM 1795 NE2 GLN A 395 16.105 45.302 24.962 1.00 74.64 N ANISOU 1795 NE2 GLN A 395 9014 10391 8954 1137 -634 -642 N ATOM 1796 N ARG A 396 13.899 40.218 21.872 1.00 29.01 N ANISOU 1796 N ARG A 396 3262 4522 3237 930 -555 -348 N ATOM 1797 CA ARG A 396 13.402 38.921 22.303 1.00 35.90 C ANISOU 1797 CA ARG A 396 4127 5420 4094 943 -563 -269 C ATOM 1798 C ARG A 396 14.166 37.775 21.632 1.00 36.37 C ANISOU 1798 C ARG A 396 4181 5427 4211 898 -561 -277 C ATOM 1799 O ARG A 396 14.543 36.810 22.294 1.00 35.07 O ANISOU 1799 O ARG A 396 4001 5275 4049 926 -583 -259 O ATOM 1800 CB ARG A 396 11.889 38.799 22.069 1.00 42.10 C ANISOU 1800 CB ARG A 396 4927 6233 4837 930 -543 -180 C ATOM 1801 CG ARG A 396 11.071 39.873 22.818 1.00 57.02 C ANISOU 1801 CG ARG A 396 6821 8179 6664 980 -547 -168 C ATOM 1802 CD ARG A 396 9.585 39.520 22.966 1.00 55.77 C ANISOU 1802 CD ARG A 396 6671 8064 6456 985 -535 -70 C ATOM 1803 NE ARG A 396 8.906 39.405 21.679 1.00 52.66 N ANISOU 1803 NE ARG A 396 6296 7633 6082 916 -503 -38 N ATOM 1804 CZ ARG A 396 8.407 40.432 21.000 1.00 49.68 C ANISOU 1804 CZ ARG A 396 5935 7243 5697 890 -482 -53 C ATOM 1805 NH1 ARG A 396 8.504 41.666 21.483 1.00 54.98 N ANISOU 1805 NH1 ARG A 396 6608 7938 6345 927 -490 -100 N ATOM 1806 NH2 ARG A 396 7.812 40.225 19.834 1.00 43.15 N ANISOU 1806 NH2 ARG A 396 5124 6382 4889 826 -452 -21 N ATOM 1807 N LEU A 397 14.406 37.886 20.328 1.00 31.96 N ANISOU 1807 N LEU A 397 3633 4810 3699 829 -535 -305 N ATOM 1808 CA LEU A 397 15.075 36.810 19.596 1.00 25.08 C ANISOU 1808 CA LEU A 397 2757 3888 2884 782 -532 -312 C ATOM 1809 C LEU A 397 16.558 36.713 19.948 1.00 24.35 C ANISOU 1809 C LEU A 397 2646 3774 2830 800 -555 -392 C ATOM 1810 O LEU A 397 17.096 35.619 20.088 1.00 36.86 O ANISOU 1810 O LEU A 397 4219 5346 4441 800 -569 -385 O ATOM 1811 CB LEU A 397 14.896 36.974 18.082 1.00 19.97 C ANISOU 1811 CB LEU A 397 2127 3187 2274 702 -497 -320 C ATOM 1812 CG LEU A 397 15.657 35.937 17.246 1.00 22.49 C ANISOU 1812 CG LEU A 397 2441 3452 2654 651 -492 -336 C ATOM 1813 CD1 LEU A 397 15.227 34.519 17.627 1.00 26.47 C ANISOU 1813 CD1 LEU A 397 2936 3971 3150 662 -504 -260 C ATOM 1814 CD2 LEU A 397 15.488 36.174 15.741 1.00 19.87 C ANISOU 1814 CD2 LEU A 397 2125 3068 2357 573 -458 -347 C ATOM 1815 N MET A 398 17.213 37.860 20.091 1.00 31.49 N ANISOU 1815 N MET A 398 3549 4675 3739 815 -559 -469 N ATOM 1816 CA MET A 398 18.620 37.898 20.453 1.00 28.06 C ANISOU 1816 CA MET A 398 3097 4223 3340 834 -581 -550 C ATOM 1817 C MET A 398 18.872 37.370 21.860 1.00 29.77 C ANISOU 1817 C MET A 398 3296 4487 3529 907 -617 -535 C ATOM 1818 O MET A 398 19.929 36.813 22.140 1.00 34.11 O ANISOU 1818 O MET A 398 3829 5020 4111 919 -636 -576 O ATOM 1819 CB MET A 398 19.164 39.315 20.331 1.00 24.02 C ANISOU 1819 CB MET A 398 2589 3701 2836 836 -578 -631 C ATOM 1820 CG MET A 398 19.412 39.792 18.907 1.00 27.77 C ANISOU 1820 CG MET A 398 3077 4117 3356 761 -547 -671 C ATOM 1821 SD MET A 398 20.511 38.739 17.922 1.00 32.00 S ANISOU 1821 SD MET A 398 3604 4588 3967 701 -540 -707 S ATOM 1822 CE MET A 398 19.303 37.852 16.958 1.00 21.44 C ANISOU 1822 CE MET A 398 2283 3236 2626 645 -512 -614 C ATOM 1823 N THR A 399 17.902 37.547 22.748 1.00 31.77 N ANISOU 1823 N THR A 399 3551 4799 3721 957 -625 -478 N ATOM 1824 CA THR A 399 18.041 37.047 24.108 1.00 35.47 C ANISOU 1824 CA THR A 399 4003 5317 4156 1027 -658 -457 C ATOM 1825 C THR A 399 18.173 35.529 24.102 1.00 39.83 C ANISOU 1825 C THR A 399 4547 5857 4730 1016 -666 -410 C ATOM 1826 O THR A 399 19.046 34.967 24.763 1.00 43.99 O ANISOU 1826 O THR A 399 5057 6386 5271 1049 -693 -436 O ATOM 1827 CB THR A 399 16.844 37.433 24.982 1.00 41.10 C ANISOU 1827 CB THR A 399 4721 6098 4799 1077 -662 -394 C ATOM 1828 OG1 THR A 399 16.859 38.844 25.209 1.00 43.74 O ANISOU 1828 OG1 THR A 399 5059 6449 5112 1101 -661 -445 O ATOM 1829 CG2 THR A 399 16.899 36.711 26.318 1.00 37.61 C ANISOU 1829 CG2 THR A 399 4261 5706 4322 1145 -694 -359 C ATOM 1830 N SER A 400 17.302 34.869 23.349 1.00 29.36 N ANISOU 1830 N SER A 400 3233 4516 3406 970 -644 -341 N ATOM 1831 CA SER A 400 17.344 33.419 23.265 1.00 28.85 C ANISOU 1831 CA SER A 400 3162 4437 3363 955 -651 -292 C ATOM 1832 C SER A 400 18.631 32.959 22.599 1.00 29.61 C ANISOU 1832 C SER A 400 3250 4473 3527 918 -654 -359 C ATOM 1833 O SER A 400 19.189 31.926 22.959 1.00 33.95 O ANISOU 1833 O SER A 400 3786 5016 4097 932 -675 -353 O ATOM 1834 CB SER A 400 16.145 32.895 22.484 1.00 29.56 C ANISOU 1834 CB SER A 400 3267 4519 3444 908 -624 -210 C ATOM 1835 OG SER A 400 14.950 33.443 22.993 1.00 45.71 O ANISOU 1835 OG SER A 400 5322 6619 5428 938 -618 -154 O ATOM 1836 N VAL A 401 19.097 33.728 21.622 1.00 27.74 N ANISOU 1836 N VAL A 401 3020 4192 3326 871 -634 -424 N ATOM 1837 CA VAL A 401 20.297 33.359 20.885 1.00 24.46 C ANISOU 1837 CA VAL A 401 2597 3719 2977 831 -633 -490 C ATOM 1838 C VAL A 401 21.533 33.477 21.765 1.00 25.90 C ANISOU 1838 C VAL A 401 2759 3909 3172 880 -665 -560 C ATOM 1839 O VAL A 401 22.424 32.625 21.715 1.00 25.26 O ANISOU 1839 O VAL A 401 2666 3801 3132 874 -680 -586 O ATOM 1840 CB VAL A 401 20.444 34.197 19.616 1.00 25.08 C ANISOU 1840 CB VAL A 401 2689 3753 3089 768 -602 -539 C ATOM 1841 CG1 VAL A 401 21.847 34.109 19.063 1.00 19.88 C ANISOU 1841 CG1 VAL A 401 2019 3043 2493 739 -606 -626 C ATOM 1842 CG2 VAL A 401 19.421 33.747 18.587 1.00 19.86 C ANISOU 1842 CG2 VAL A 401 2044 3071 2430 710 -572 -472 C ATOM 1843 N THR A 402 21.569 34.513 22.595 1.00 25.53 N ANISOU 1843 N THR A 402 2710 3901 3089 931 -677 -591 N ATOM 1844 CA THR A 402 22.703 34.731 23.485 1.00 25.78 C ANISOU 1844 CA THR A 402 2723 3944 3129 982 -708 -659 C ATOM 1845 C THR A 402 22.745 33.735 24.647 1.00 33.93 C ANISOU 1845 C THR A 402 3741 5014 4137 1040 -740 -616 C ATOM 1846 O THR A 402 23.827 33.342 25.096 1.00 38.78 O ANISOU 1846 O THR A 402 4338 5619 4778 1064 -765 -665 O ATOM 1847 CB THR A 402 22.721 36.155 24.034 1.00 33.61 C ANISOU 1847 CB THR A 402 3716 4965 4089 1020 -712 -706 C ATOM 1848 OG1 THR A 402 21.445 36.451 24.610 1.00 50.35 O ANISOU 1848 OG1 THR A 402 5846 7139 6146 1053 -709 -635 O ATOM 1849 CG2 THR A 402 23.005 37.144 22.923 1.00 26.29 C ANISOU 1849 CG2 THR A 402 2800 3994 3196 965 -685 -766 C ATOM 1850 N ASN A 403 21.575 33.317 25.121 1.00 30.01 N ANISOU 1850 N ASN A 403 3252 4560 3592 1062 -740 -526 N ATOM 1851 CA ASN A 403 21.488 32.318 26.188 1.00 31.78 C ANISOU 1851 CA ASN A 403 3462 4821 3790 1113 -768 -474 C ATOM 1852 C ASN A 403 21.911 30.900 25.781 1.00 36.01 C ANISOU 1852 C ASN A 403 3993 5320 4371 1083 -775 -452 C ATOM 1853 O ASN A 403 22.253 30.083 26.635 1.00 41.45 O ANISOU 1853 O ASN A 403 4669 6028 5054 1125 -803 -435 O ATOM 1854 CB ASN A 403 20.080 32.283 26.782 1.00 37.53 C ANISOU 1854 CB ASN A 403 4200 5607 4453 1142 -765 -381 C ATOM 1855 CG ASN A 403 19.744 33.541 27.542 1.00 46.72 C ANISOU 1855 CG ASN A 403 5365 6821 5567 1192 -769 -400 C ATOM 1856 OD1 ASN A 403 20.581 34.431 27.693 1.00 52.42 O ANISOU 1856 OD1 ASN A 403 6081 7535 6302 1208 -777 -482 O ATOM 1857 ND2 ASN A 403 18.512 33.628 28.022 1.00 45.35 N ANISOU 1857 ND2 ASN A 403 5198 6697 5334 1216 -764 -324 N ATOM 1858 N ARG A 404 21.884 30.605 24.487 1.00 33.02 N ANISOU 1858 N ARG A 404 3624 4887 4036 1011 -749 -454 N ATOM 1859 CA ARG A 404 22.292 29.288 24.010 1.00 34.25 C ANISOU 1859 CA ARG A 404 3774 5003 4238 979 -754 -438 C ATOM 1860 C ARG A 404 23.405 29.383 22.984 1.00 29.02 C ANISOU 1860 C ARG A 404 3107 4277 3641 927 -744 -521 C ATOM 1861 O ARG A 404 23.642 28.440 22.230 1.00 34.06 O ANISOU 1861 O ARG A 404 3745 4873 4324 883 -739 -512 O ATOM 1862 CB ARG A 404 21.101 28.539 23.403 1.00 46.72 C ANISOU 1862 CB ARG A 404 5367 6577 5807 939 -733 -345 C ATOM 1863 CG ARG A 404 20.140 27.967 24.432 1.00 62.31 C ANISOU 1863 CG ARG A 404 7341 8609 7726 987 -748 -253 C ATOM 1864 CD ARG A 404 18.896 27.371 23.772 1.00 74.88 C ANISOU 1864 CD ARG A 404 8947 10196 9307 944 -724 -163 C ATOM 1865 NE ARG A 404 19.104 26.005 23.288 1.00 79.92 N ANISOU 1865 NE ARG A 404 9582 10796 9988 910 -728 -133 N ATOM 1866 CZ ARG A 404 18.867 24.910 24.008 1.00 74.59 C ANISOU 1866 CZ ARG A 404 8899 10142 9299 939 -750 -70 C ATOM 1867 NH1 ARG A 404 18.417 25.015 25.251 1.00 74.51 N ANISOU 1867 NH1 ARG A 404 8885 10194 9233 1003 -769 -29 N ATOM 1868 NH2 ARG A 404 19.082 23.709 23.486 1.00 68.95 N ANISOU 1868 NH2 ARG A 404 8182 9387 8627 905 -754 -47 N ATOM 1869 N CYS A 405 24.095 30.517 22.962 1.00 29.94 N ANISOU 1869 N CYS A 405 2492 4642 4243 224 -393 -218 N ATOM 1870 CA CYS A 405 25.025 30.800 21.876 1.00 30.72 C ANISOU 1870 CA CYS A 405 2692 4647 4332 247 -387 -255 C ATOM 1871 C CYS A 405 26.192 29.820 21.798 1.00 28.52 C ANISOU 1871 C CYS A 405 2439 4350 4045 244 -374 -209 C ATOM 1872 O CYS A 405 26.705 29.546 20.715 1.00 30.92 O ANISOU 1872 O CYS A 405 2833 4554 4361 259 -390 -216 O ATOM 1873 CB CYS A 405 25.508 32.255 21.912 1.00 30.05 C ANISOU 1873 CB CYS A 405 2621 4588 4206 262 -347 -335 C ATOM 1874 SG CYS A 405 26.418 32.759 23.365 1.00 55.81 S ANISOU 1874 SG CYS A 405 5799 7993 7412 252 -279 -343 S ATOM 1875 N GLN A 406 26.607 29.297 22.946 1.00 29.21 N ANISOU 1875 N GLN A 406 2450 4536 4114 226 -345 -162 N ATOM 1876 CA GLN A 406 27.641 28.270 22.990 1.00 35.39 C ANISOU 1876 CA GLN A 406 3247 5310 4892 221 -334 -111 C ATOM 1877 C GLN A 406 27.254 27.103 22.077 1.00 30.79 C ANISOU 1877 C GLN A 406 2715 4624 4359 220 -388 -62 C ATOM 1878 O GLN A 406 28.022 26.676 21.219 1.00 33.60 O ANISOU 1878 O GLN A 406 3148 4898 4720 231 -395 -59 O ATOM 1879 CB GLN A 406 27.823 27.779 24.432 1.00 47.14 C ANISOU 1879 CB GLN A 406 4630 6922 6359 197 -305 -58 C ATOM 1880 CG GLN A 406 28.604 26.476 24.574 1.00 63.33 C ANISOU 1880 CG GLN A 406 6681 8966 8415 187 -304 12 C ATOM 1881 CD GLN A 406 30.106 26.677 24.699 1.00 73.36 C ANISOU 1881 CD GLN A 406 7976 10255 9642 196 -257 -6 C ATOM 1882 OE1 GLN A 406 30.577 27.580 25.398 1.00 74.45 O ANISOU 1882 OE1 GLN A 406 8078 10473 9737 198 -210 -45 O ATOM 1883 NE2 GLN A 406 30.868 25.817 24.032 1.00 76.23 N ANISOU 1883 NE2 GLN A 406 8401 10546 10017 200 -268 24 N ATOM 1884 N GLU A 407 26.043 26.604 22.265 1.00 23.56 N ANISOU 1884 N GLU A 407 1757 3715 3481 206 -426 -26 N ATOM 1885 CA GLU A 407 25.535 25.479 21.498 1.00 26.32 C ANISOU 1885 CA GLU A 407 2145 3975 3882 204 -479 23 C ATOM 1886 C GLU A 407 25.371 25.829 20.016 1.00 28.49 C ANISOU 1886 C GLU A 407 2525 4123 4179 227 -512 -24 C ATOM 1887 O GLU A 407 25.608 25.000 19.146 1.00 29.03 O ANISOU 1887 O GLU A 407 2656 4101 4275 233 -541 2 O ATOM 1888 CB GLU A 407 24.204 25.018 22.096 1.00 29.10 C ANISOU 1888 CB GLU A 407 2421 4370 4267 184 -510 65 C ATOM 1889 CG GLU A 407 23.463 23.982 21.271 1.00 48.53 C ANISOU 1889 CG GLU A 407 4918 6736 6784 182 -569 108 C ATOM 1890 CD GLU A 407 22.122 23.605 21.883 1.00 62.23 C ANISOU 1890 CD GLU A 407 6577 8517 8551 163 -598 146 C ATOM 1891 OE1 GLU A 407 21.729 24.221 22.900 1.00 59.74 O ANISOU 1891 OE1 GLU A 407 6183 8303 8212 152 -573 135 O ATOM 1892 OE2 GLU A 407 21.465 22.690 21.345 1.00 72.07 O ANISOU 1892 OE2 GLU A 407 7841 9697 9845 158 -646 187 O ATOM 1893 N LEU A 408 24.974 27.063 19.732 1.00 24.62 N ANISOU 1893 N LEU A 408 2054 3625 3676 241 -506 -93 N ATOM 1894 CA LEU A 408 24.728 27.471 18.354 1.00 23.78 C ANISOU 1894 CA LEU A 408 2044 3402 3590 263 -538 -140 C ATOM 1895 C LEU A 408 26.024 27.675 17.581 1.00 29.28 C ANISOU 1895 C LEU A 408 2826 4038 4263 282 -516 -170 C ATOM 1896 O LEU A 408 26.129 27.293 16.417 1.00 31.57 O ANISOU 1896 O LEU A 408 3199 4220 4577 295 -548 -173 O ATOM 1897 CB LEU A 408 23.872 28.742 18.311 1.00 21.73 C ANISOU 1897 CB LEU A 408 1777 3155 3325 272 -539 -204 C ATOM 1898 CG LEU A 408 22.492 28.550 18.947 1.00 21.56 C ANISOU 1898 CG LEU A 408 1678 3183 3331 254 -567 -177 C ATOM 1899 CD1 LEU A 408 21.749 29.863 19.070 1.00 21.24 C ANISOU 1899 CD1 LEU A 408 1620 3171 3279 261 -561 -243 C ATOM 1900 CD2 LEU A 408 21.677 27.521 18.165 1.00 21.41 C ANISOU 1900 CD2 LEU A 408 1692 3076 3368 252 -626 -135 C ATOM 1901 N ALA A 409 27.005 28.284 18.236 1.00 23.98 N ANISOU 1901 N ALA A 409 2132 3436 3542 283 -462 -195 N ATOM 1902 CA ALA A 409 28.299 28.543 17.616 1.00 21.08 C ANISOU 1902 CA ALA A 409 1840 3023 3148 299 -436 -226 C ATOM 1903 C ALA A 409 29.006 27.260 17.188 1.00 20.78 C ANISOU 1903 C ALA A 409 1840 2930 3127 297 -451 -171 C ATOM 1904 O ALA A 409 29.701 27.248 16.179 1.00 23.77 O ANISOU 1904 O ALA A 409 2304 3223 3504 313 -455 -192 O ATOM 1905 CB ALA A 409 29.182 29.341 18.556 1.00 25.09 C ANISOU 1905 CB ALA A 409 2303 3628 3602 298 -375 -255 C ATOM 1906 N THR A 410 28.816 26.182 17.946 1.00 20.86 N ANISOU 1906 N THR A 410 1784 2989 3153 276 -459 -99 N ATOM 1907 CA THR A 410 29.531 24.929 17.698 1.00 23.61 C ANISOU 1907 CA THR A 410 2157 3298 3515 271 -470 -43 C ATOM 1908 C THR A 410 28.779 23.988 16.745 1.00 28.78 C ANISOU 1908 C THR A 410 2856 3852 4226 272 -531 -9 C ATOM 1909 O THR A 410 29.293 22.937 16.357 1.00 27.15 O ANISOU 1909 O THR A 410 2681 3597 4039 271 -547 35 O ATOM 1910 CB THR A 410 29.814 24.177 19.008 1.00 24.10 C ANISOU 1910 CB THR A 410 2127 3465 3566 247 -446 20 C ATOM 1911 OG1 THR A 410 28.589 23.999 19.728 1.00 32.62 O ANISOU 1911 OG1 THR A 410 3126 4599 4667 230 -466 51 O ATOM 1912 CG2 THR A 410 30.785 24.955 19.869 1.00 22.89 C ANISOU 1912 CG2 THR A 410 1938 3403 3355 247 -384 -10 C ATOM 1913 N ASN A 411 27.566 24.379 16.375 1.00 24.54 N ANISOU 1913 N ASN A 411 2321 3284 3716 276 -565 -30 N ATOM 1914 CA ASN A 411 26.713 23.575 15.515 1.00 21.96 C ANISOU 1914 CA ASN A 411 2032 2868 3445 277 -624 -1 C ATOM 1915 C ASN A 411 27.004 23.759 14.028 1.00 20.61 C ANISOU 1915 C ASN A 411 1972 2572 3285 302 -647 -42 C ATOM 1916 O ASN A 411 27.344 24.846 13.588 1.00 22.58 O ANISOU 1916 O ASN A 411 2269 2803 3508 319 -627 -107 O ATOM 1917 CB ASN A 411 25.254 23.909 15.780 1.00 22.82 C ANISOU 1917 CB ASN A 411 2093 2999 3579 270 -651 -6 C ATOM 1918 CG ASN A 411 24.324 23.118 14.908 1.00 24.96 C ANISOU 1918 CG ASN A 411 2399 3179 3906 272 -712 21 C ATOM 1919 OD1 ASN A 411 24.085 21.934 15.148 1.00 27.91 O ANISOU 1919 OD1 ASN A 411 2740 3552 4311 257 -736 87 O ATOM 1920 ND2 ASN A 411 23.793 23.760 13.882 1.00 20.97 N ANISOU 1920 ND2 ASN A 411 1959 2593 3415 291 -738 -31 N ATOM 1921 N GLU A 412 26.847 22.687 13.262 1.00 25.10 N ANISOU 1921 N GLU A 412 2583 3058 3897 303 -691 -3 N ATOM 1922 CA GLU A 412 27.151 22.685 11.830 1.00 27.49 C ANISOU 1922 CA GLU A 412 2992 3241 4214 326 -716 -33 C ATOM 1923 C GLU A 412 26.370 23.711 11.005 1.00 25.96 C ANISOU 1923 C GLU A 412 2846 2990 4026 344 -737 -97 C ATOM 1924 O GLU A 412 26.845 24.156 9.960 1.00 26.14 O ANISOU 1924 O GLU A 412 2956 2935 4042 365 -740 -142 O ATOM 1925 CB GLU A 412 26.903 21.292 11.251 1.00 31.64 C ANISOU 1925 CB GLU A 412 3540 3694 4790 322 -765 25 C ATOM 1926 CG GLU A 412 25.485 20.808 11.463 1.00 37.88 C ANISOU 1926 CG GLU A 412 4280 4488 5626 309 -807 60 C ATOM 1927 CD GLU A 412 25.272 19.383 10.994 1.00 39.32 C ANISOU 1927 CD GLU A 412 4476 4605 5857 303 -853 122 C ATOM 1928 OE1 GLU A 412 25.968 18.970 10.043 1.00 39.67 O ANISOU 1928 OE1 GLU A 412 4597 4567 5910 317 -866 118 O ATOM 1929 OE2 GLU A 412 24.393 18.689 11.559 1.00 33.28 O ANISOU 1929 OE2 GLU A 412 3647 3872 5125 285 -877 173 O ATOM 1930 N TYR A 413 25.166 24.066 11.442 1.00 20.40 N ANISOU 1930 N TYR A 413 2090 2324 3339 336 -752 -101 N ATOM 1931 CA TYR A 413 24.372 25.035 10.689 1.00 20.64 C ANISOU 1931 CA TYR A 413 2164 2303 3377 353 -773 -161 C ATOM 1932 C TYR A 413 24.260 26.378 11.397 1.00 22.93 C ANISOU 1932 C TYR A 413 2413 2672 3628 354 -734 -213 C ATOM 1933 O TYR A 413 24.358 27.430 10.766 1.00 23.55 O ANISOU 1933 O TYR A 413 2547 2714 3689 373 -726 -278 O ATOM 1934 CB TYR A 413 22.972 24.490 10.371 1.00 21.52 C ANISOU 1934 CB TYR A 413 2262 2372 3541 349 -829 -135 C ATOM 1935 CG TYR A 413 22.988 23.282 9.465 1.00 22.94 C ANISOU 1935 CG TYR A 413 2494 2457 3764 353 -873 -94 C ATOM 1936 CD1 TYR A 413 23.471 23.377 8.167 1.00 20.40 C ANISOU 1936 CD1 TYR A 413 2273 2031 3446 375 -889 -127 C ATOM 1937 CD2 TYR A 413 22.517 22.048 9.903 1.00 29.72 C ANISOU 1937 CD2 TYR A 413 3302 3331 4660 333 -900 -22 C ATOM 1938 CE1 TYR A 413 23.487 22.286 7.329 1.00 20.44 C ANISOU 1938 CE1 TYR A 413 2326 1949 3490 380 -930 -91 C ATOM 1939 CE2 TYR A 413 22.528 20.936 9.067 1.00 28.28 C ANISOU 1939 CE2 TYR A 413 3166 3060 4518 337 -941 15 C ATOM 1940 CZ TYR A 413 23.011 21.069 7.777 1.00 29.42 C ANISOU 1940 CZ TYR A 413 3411 3102 4666 361 -956 -21 C ATOM 1941 OH TYR A 413 23.046 19.992 6.924 1.00 27.46 O ANISOU 1941 OH TYR A 413 3210 2766 4457 366 -997 12 O ATOM 1942 N ALA A 414 24.070 26.332 12.709 1.00 21.62 N ANISOU 1942 N ALA A 414 2151 2617 3448 333 -709 -185 N ATOM 1943 CA ALA A 414 23.799 27.532 13.491 1.00 20.93 C ANISOU 1943 CA ALA A 414 2010 2613 3328 331 -676 -230 C ATOM 1944 C ALA A 414 25.013 28.454 13.625 1.00 22.28 C ANISOU 1944 C ALA A 414 2205 2814 3446 342 -622 -279 C ATOM 1945 O ALA A 414 24.861 29.635 13.936 1.00 21.31 O ANISOU 1945 O ALA A 414 2065 2735 3297 347 -597 -333 O ATOM 1946 CB ALA A 414 23.242 27.165 14.851 1.00 20.76 C ANISOU 1946 CB ALA A 414 1879 2702 3308 305 -667 -184 C ATOM 1947 N ASN A 415 26.213 27.930 13.375 1.00 21.43 N ANISOU 1947 N ASN A 415 2137 2682 3323 345 -604 -262 N ATOM 1948 CA ASN A 415 27.396 28.789 13.359 1.00 19.69 C ANISOU 1948 CA ASN A 415 1949 2477 3055 357 -556 -311 C ATOM 1949 C ASN A 415 27.271 29.910 12.322 1.00 19.46 C ANISOU 1949 C ASN A 415 1999 2375 3021 381 -562 -385 C ATOM 1950 O ASN A 415 27.822 30.990 12.503 1.00 22.75 O ANISOU 1950 O ASN A 415 2422 2825 3399 390 -522 -438 O ATOM 1951 CB ASN A 415 28.691 27.978 13.162 1.00 24.02 C ANISOU 1951 CB ASN A 415 2533 3002 3591 358 -539 -280 C ATOM 1952 CG ASN A 415 28.915 27.561 11.718 1.00 21.26 C ANISOU 1952 CG ASN A 415 2287 2524 3266 376 -575 -287 C ATOM 1953 OD1 ASN A 415 29.409 28.346 10.901 1.00 20.47 O ANISOU 1953 OD1 ASN A 415 2260 2369 3148 396 -565 -343 O ATOM 1954 ND2 ASN A 415 28.558 26.315 11.396 1.00 19.55 N ANISOU 1954 ND2 ASN A 415 2076 2261 3092 369 -616 -229 N ATOM 1955 N TYR A 416 26.520 29.666 11.253 1.00 20.01 N ANISOU 1955 N TYR A 416 2126 2347 3130 392 -613 -388 N ATOM 1956 CA TYR A 416 26.308 30.687 10.224 1.00 21.18 C ANISOU 1956 CA TYR A 416 2350 2422 3277 415 -624 -456 C ATOM 1957 C TYR A 416 25.507 31.884 10.734 1.00 25.64 C ANISOU 1957 C TYR A 416 2869 3042 3829 415 -613 -503 C ATOM 1958 O TYR A 416 25.701 33.017 10.293 1.00 29.27 O ANISOU 1958 O TYR A 416 3372 3480 4267 432 -597 -567 O ATOM 1959 CB TYR A 416 25.627 30.079 8.998 1.00 19.35 C ANISOU 1959 CB TYR A 416 2185 2075 3091 426 -683 -445 C ATOM 1960 CG TYR A 416 26.556 29.197 8.188 1.00 22.34 C ANISOU 1960 CG TYR A 416 2634 2379 3477 433 -692 -420 C ATOM 1961 CD1 TYR A 416 27.543 29.751 7.385 1.00 19.91 C ANISOU 1961 CD1 TYR A 416 2407 2016 3142 452 -672 -465 C ATOM 1962 CD2 TYR A 416 26.453 27.813 8.241 1.00 20.77 C ANISOU 1962 CD2 TYR A 416 2417 2164 3310 421 -720 -352 C ATOM 1963 CE1 TYR A 416 28.396 28.947 6.643 1.00 24.98 C ANISOU 1963 CE1 TYR A 416 3111 2590 3790 459 -681 -443 C ATOM 1964 CE2 TYR A 416 27.292 27.006 7.516 1.00 28.25 C ANISOU 1964 CE2 TYR A 416 3426 3044 4265 427 -729 -330 C ATOM 1965 CZ TYR A 416 28.262 27.573 6.713 1.00 30.38 C ANISOU 1965 CZ TYR A 416 3776 3260 4506 447 -709 -376 C ATOM 1966 OH TYR A 416 29.098 26.756 5.992 1.00 29.84 O ANISOU 1966 OH TYR A 416 3767 3125 4445 453 -719 -355 O ATOM 1967 N ILE A 417 24.599 31.616 11.659 1.00 22.55 N ANISOU 1967 N ILE A 417 2391 2722 3453 396 -622 -471 N ATOM 1968 CA ILE A 417 23.788 32.655 12.262 1.00 22.60 C ANISOU 1968 CA ILE A 417 2345 2792 3451 394 -612 -510 C ATOM 1969 C ILE A 417 24.637 33.508 13.195 1.00 21.13 C ANISOU 1969 C ILE A 417 2114 2700 3213 391 -552 -541 C ATOM 1970 O ILE A 417 24.579 34.736 13.152 1.00 21.59 O ANISOU 1970 O ILE A 417 2182 2770 3250 402 -533 -603 O ATOM 1971 CB ILE A 417 22.615 32.024 13.046 1.00 23.26 C ANISOU 1971 CB ILE A 417 2344 2930 3565 373 -639 -462 C ATOM 1972 CG1 ILE A 417 21.668 31.318 12.076 1.00 20.22 C ANISOU 1972 CG1 ILE A 417 2003 2448 3232 377 -701 -440 C ATOM 1973 CG2 ILE A 417 21.870 33.077 13.851 1.00 20.21 C ANISOU 1973 CG2 ILE A 417 1889 2625 3164 367 -623 -500 C ATOM 1974 CD1 ILE A 417 20.715 30.408 12.761 1.00 22.14 C ANISOU 1974 CD1 ILE A 417 2171 2734 3508 356 -728 -380 C ATOM 1975 N ILE A 418 25.432 32.845 14.026 1.00 19.65 N ANISOU 1975 N ILE A 418 1881 2579 3007 376 -521 -496 N ATOM 1976 CA ILE A 418 26.297 33.531 14.965 1.00 19.56 C ANISOU 1976 CA ILE A 418 1824 2661 2946 372 -463 -519 C ATOM 1977 C ILE A 418 27.325 34.375 14.210 1.00 23.63 C ANISOU 1977 C ILE A 418 2420 3126 3432 394 -436 -578 C ATOM 1978 O ILE A 418 27.618 35.500 14.609 1.00 22.20 O ANISOU 1978 O ILE A 418 2223 2995 3217 400 -398 -630 O ATOM 1979 CB ILE A 418 27.005 32.532 15.909 1.00 24.18 C ANISOU 1979 CB ILE A 418 2350 3318 3519 353 -439 -456 C ATOM 1980 CG1 ILE A 418 25.976 31.708 16.696 1.00 20.33 C ANISOU 1980 CG1 ILE A 418 1779 2885 3060 331 -464 -396 C ATOM 1981 CG2 ILE A 418 27.968 33.249 16.842 1.00 19.52 C ANISOU 1981 CG2 ILE A 418 1717 2822 2876 351 -377 -482 C ATOM 1982 CD1 ILE A 418 24.987 32.559 17.469 1.00 24.08 C ANISOU 1982 CD1 ILE A 418 2181 3436 3531 324 -460 -423 C ATOM 1983 N GLN A 419 27.869 33.832 13.123 1.00 21.47 N ANISOU 1983 N GLN A 419 2234 2753 3171 406 -455 -570 N ATOM 1984 CA GLN A 419 28.773 34.606 12.275 1.00 19.90 C ANISOU 1984 CA GLN A 419 2119 2495 2947 428 -434 -626 C ATOM 1985 C GLN A 419 28.064 35.807 11.691 1.00 21.68 C ANISOU 1985 C GLN A 419 2378 2683 3176 444 -447 -692 C ATOM 1986 O GLN A 419 28.635 36.886 11.628 1.00 19.97 O ANISOU 1986 O GLN A 419 2184 2476 2927 456 -413 -748 O ATOM 1987 CB GLN A 419 29.332 33.775 11.129 1.00 18.58 C ANISOU 1987 CB GLN A 419 2040 2222 2797 438 -460 -605 C ATOM 1988 CG GLN A 419 30.390 32.769 11.527 1.00 20.46 C ANISOU 1988 CG GLN A 419 2266 2485 3022 428 -439 -555 C ATOM 1989 CD GLN A 419 30.964 32.069 10.311 1.00 24.24 C ANISOU 1989 CD GLN A 419 2838 2854 3517 440 -464 -543 C ATOM 1990 OE1 GLN A 419 31.566 32.701 9.445 1.00 26.34 O ANISOU 1990 OE1 GLN A 419 3182 3058 3767 459 -454 -591 O ATOM 1991 NE2 GLN A 419 30.764 30.763 10.232 1.00 19.68 N ANISOU 1991 NE2 GLN A 419 2254 2252 2972 430 -496 -480 N ATOM 1992 N HIS A 420 26.824 35.630 11.249 1.00 19.97 N ANISOU 1992 N HIS A 420 2166 2421 2999 444 -496 -685 N ATOM 1993 CA HIS A 420 26.110 36.768 10.691 1.00 20.01 C ANISOU 1993 CA HIS A 420 2203 2390 3010 459 -510 -747 C ATOM 1994 C HIS A 420 25.928 37.868 11.725 1.00 27.10 C ANISOU 1994 C HIS A 420 3029 3389 3880 454 -472 -786 C ATOM 1995 O HIS A 420 26.106 39.043 11.425 1.00 23.01 O ANISOU 1995 O HIS A 420 2541 2859 3341 469 -454 -849 O ATOM 1996 CB HIS A 420 24.752 36.381 10.133 1.00 26.73 C ANISOU 1996 CB HIS A 420 3064 3184 3910 460 -569 -732 C ATOM 1997 CG HIS A 420 23.964 37.560 9.663 1.00 31.58 C ANISOU 1997 CG HIS A 420 3702 3769 4529 474 -582 -795 C ATOM 1998 ND1 HIS A 420 22.966 38.139 10.418 1.00 31.42 N ANISOU 1998 ND1 HIS A 420 3609 3815 4513 465 -585 -810 N ATOM 1999 CD2 HIS A 420 24.065 38.304 8.537 1.00 29.15 C ANISOU 1999 CD2 HIS A 420 3481 3375 4220 497 -593 -847 C ATOM 2000 CE1 HIS A 420 22.472 39.174 9.767 1.00 32.50 C ANISOU 2000 CE1 HIS A 420 3788 3907 4654 482 -597 -869 C ATOM 2001 NE2 HIS A 420 23.122 39.297 8.624 1.00 35.24 N ANISOU 2001 NE2 HIS A 420 4232 4161 4997 501 -602 -892 N ATOM 2002 N ILE A 421 25.572 37.483 12.945 1.00 23.83 N ANISOU 2002 N ILE A 421 2517 3075 3464 433 -462 -748 N ATOM 2003 CA ILE A 421 25.378 38.459 14.010 1.00 20.57 C ANISOU 2003 CA ILE A 421 2027 2765 3025 426 -426 -781 C ATOM 2004 C ILE A 421 26.676 39.171 14.342 1.00 19.20 C ANISOU 2004 C ILE A 421 1860 2633 2803 432 -369 -817 C ATOM 2005 O ILE A 421 26.717 40.397 14.426 1.00 19.10 O ANISOU 2005 O ILE A 421 1847 2642 2769 442 -345 -879 O ATOM 2006 CB ILE A 421 24.816 37.815 15.295 1.00 20.20 C ANISOU 2006 CB ILE A 421 1871 2820 2983 400 -424 -729 C ATOM 2007 CG1 ILE A 421 23.442 37.187 15.011 1.00 22.86 C ANISOU 2007 CG1 ILE A 421 2197 3121 3369 394 -481 -696 C ATOM 2008 CG2 ILE A 421 24.736 38.855 16.403 1.00 19.45 C ANISOU 2008 CG2 ILE A 421 1697 2835 2856 395 -384 -766 C ATOM 2009 CD1 ILE A 421 22.816 36.454 16.189 1.00 21.61 C ANISOU 2009 CD1 ILE A 421 1935 3055 3221 368 -485 -639 C ATOM 2010 N VAL A 422 27.736 38.393 14.534 1.00 21.87 N ANISOU 2010 N VAL A 422 2203 2982 3125 427 -346 -779 N ATOM 2011 CA VAL A 422 29.034 38.946 14.896 1.00 21.09 C ANISOU 2011 CA VAL A 422 2108 2926 2980 432 -290 -807 C ATOM 2012 C VAL A 422 29.592 39.893 13.819 1.00 24.31 C ANISOU 2012 C VAL A 422 2609 3252 3374 456 -282 -872 C ATOM 2013 O VAL A 422 30.254 40.878 14.130 1.00 20.82 O ANISOU 2013 O VAL A 422 2163 2852 2898 463 -239 -920 O ATOM 2014 CB VAL A 422 30.048 37.818 15.225 1.00 22.08 C ANISOU 2014 CB VAL A 422 2225 3070 3093 421 -273 -750 C ATOM 2015 CG1 VAL A 422 31.482 38.330 15.176 1.00 18.24 C ANISOU 2015 CG1 VAL A 422 1775 2591 2564 432 -223 -783 C ATOM 2016 CG2 VAL A 422 29.745 37.218 16.586 1.00 19.81 C ANISOU 2016 CG2 VAL A 422 1829 2894 2804 397 -261 -698 C ATOM 2017 N SER A 423 29.297 39.613 12.556 1.00 24.56 N ANISOU 2017 N SER A 423 2726 3171 3435 469 -325 -874 N ATOM 2018 CA SER A 423 29.908 40.370 11.474 1.00 30.07 C ANISOU 2018 CA SER A 423 3518 3787 4120 491 -318 -928 C ATOM 2019 C SER A 423 29.068 41.556 11.008 1.00 28.87 C ANISOU 2019 C SER A 423 3388 3604 3977 505 -333 -989 C ATOM 2020 O SER A 423 29.482 42.314 10.126 1.00 35.67 O ANISOU 2020 O SER A 423 4325 4399 4828 524 -328 -1039 O ATOM 2021 CB SER A 423 30.234 39.449 10.302 1.00 32.48 C ANISOU 2021 CB SER A 423 3910 3983 4447 500 -351 -900 C ATOM 2022 OG SER A 423 29.051 38.897 9.781 1.00 47.77 O ANISOU 2022 OG SER A 423 5857 5865 6428 499 -407 -875 O ATOM 2023 N ASN A 424 27.899 41.730 11.614 1.00 26.08 N ANISOU 2023 N ASN A 424 2966 3300 3642 495 -352 -986 N ATOM 2024 CA ASN A 424 27.002 42.804 11.220 1.00 23.09 C ANISOU 2024 CA ASN A 424 2602 2895 3275 506 -370 -1041 C ATOM 2025 C ASN A 424 27.107 44.029 12.141 1.00 24.30 C ANISOU 2025 C ASN A 424 2696 3141 3397 505 -326 -1091 C ATOM 2026 O ASN A 424 26.737 43.963 13.307 1.00 25.38 O ANISOU 2026 O ASN A 424 2738 3377 3528 488 -312 -1073 O ATOM 2027 CB ASN A 424 25.564 42.293 11.158 1.00 30.32 C ANISOU 2027 CB ASN A 424 3491 3795 4234 499 -423 -1012 C ATOM 2028 CG ASN A 424 24.655 43.200 10.350 1.00 34.09 C ANISOU 2028 CG ASN A 424 4012 4209 4732 515 -454 -1065 C ATOM 2029 OD1 ASN A 424 24.886 44.402 10.242 1.00 34.29 O ANISOU 2029 OD1 ASN A 424 4055 4238 4736 527 -430 -1126 O ATOM 2030 ND2 ASN A 424 23.609 42.625 9.785 1.00 42.51 N ANISOU 2030 ND2 ASN A 424 5096 5217 5839 514 -507 -1041 N ATOM 2031 N ASP A 425 27.623 45.135 11.606 1.00 24.63 N ANISOU 2031 N ASP A 425 2791 3149 3418 523 -305 -1154 N ATOM 2032 CA ASP A 425 27.793 46.373 12.365 1.00 25.91 C ANISOU 2032 CA ASP A 425 2904 3388 3551 525 -263 -1208 C ATOM 2033 C ASP A 425 26.480 46.905 12.924 1.00 30.97 C ANISOU 2033 C ASP A 425 3479 4079 4210 518 -282 -1225 C ATOM 2034 O ASP A 425 26.455 47.506 13.997 1.00 29.01 O ANISOU 2034 O ASP A 425 3151 3929 3940 510 -249 -1244 O ATOM 2035 CB ASP A 425 28.458 47.445 11.507 1.00 26.66 C ANISOU 2035 CB ASP A 425 3081 3422 3628 547 -245 -1272 C ATOM 2036 CG ASP A 425 29.956 47.234 11.369 1.00 33.10 C ANISOU 2036 CG ASP A 425 3936 4228 4411 551 -205 -1268 C ATOM 2037 OD1 ASP A 425 30.509 46.350 12.069 1.00 31.70 O ANISOU 2037 OD1 ASP A 425 3717 4107 4223 536 -187 -1219 O ATOM 2038 OD2 ASP A 425 30.582 47.957 10.563 1.00 35.04 O ANISOU 2038 OD2 ASP A 425 4257 4414 4644 569 -192 -1314 O ATOM 2039 N ASP A 426 25.389 46.672 12.202 1.00 20.63 N ANISOU 2039 N ASP A 426 2199 2700 2938 522 -335 -1218 N ATOM 2040 CA ASP A 426 24.085 47.113 12.672 1.00 24.47 C ANISOU 2040 CA ASP A 426 2625 3228 3445 516 -358 -1232 C ATOM 2041 C ASP A 426 23.583 46.269 13.828 1.00 26.18 C ANISOU 2041 C ASP A 426 2742 3536 3669 491 -360 -1176 C ATOM 2042 O ASP A 426 22.504 46.523 14.355 1.00 22.91 O ANISOU 2042 O ASP A 426 2267 3168 3271 483 -377 -1182 O ATOM 2043 CB ASP A 426 23.082 47.127 11.523 1.00 25.70 C ANISOU 2043 CB ASP A 426 2845 3279 3640 528 -414 -1243 C ATOM 2044 CG ASP A 426 23.384 48.219 10.519 1.00 28.39 C ANISOU 2044 CG ASP A 426 3270 3544 3974 552 -411 -1309 C ATOM 2045 OD1 ASP A 426 23.463 47.910 9.314 1.00 29.45 O ANISOU 2045 OD1 ASP A 426 3494 3572 4124 565 -440 -1306 O ATOM 2046 OD2 ASP A 426 23.577 49.383 10.944 1.00 26.46 O ANISOU 2046 OD2 ASP A 426 3001 3347 3706 557 -378 -1362 O ATOM 2047 N LEU A 427 24.377 45.276 14.225 1.00 23.79 N ANISOU 2047 N LEU A 427 2423 3261 3354 480 -342 -1123 N ATOM 2048 CA LEU A 427 24.029 44.402 15.341 1.00 23.58 C ANISOU 2048 CA LEU A 427 2304 3323 3331 456 -341 -1065 C ATOM 2049 C LEU A 427 25.142 44.432 16.379 1.00 23.22 C ANISOU 2049 C LEU A 427 2205 3374 3244 447 -283 -1057 C ATOM 2050 O LEU A 427 25.292 43.499 17.173 1.00 29.06 O ANISOU 2050 O LEU A 427 2886 4176 3981 429 -275 -999 O ATOM 2051 CB LEU A 427 23.777 42.958 14.858 1.00 19.07 C ANISOU 2051 CB LEU A 427 1758 2693 2792 449 -382 -996 C ATOM 2052 CG LEU A 427 22.461 42.706 14.093 1.00 22.49 C ANISOU 2052 CG LEU A 427 2219 3052 3272 452 -442 -989 C ATOM 2053 CD1 LEU A 427 22.408 41.312 13.476 1.00 20.60 C ANISOU 2053 CD1 LEU A 427 2020 2744 3064 448 -480 -926 C ATOM 2054 CD2 LEU A 427 21.253 42.905 14.980 1.00 20.50 C ANISOU 2054 CD2 LEU A 427 1877 2877 3034 438 -455 -986 C ATOM 2055 N ALA A 428 25.914 45.514 16.376 1.00 23.41 N ANISOU 2055 N ALA A 428 2249 3412 3236 460 -243 -1115 N ATOM 2056 CA ALA A 428 27.112 45.608 17.215 1.00 25.15 C ANISOU 2056 CA ALA A 428 2431 3711 3414 455 -186 -1114 C ATOM 2057 C ALA A 428 26.858 45.267 18.687 1.00 30.50 C ANISOU 2057 C ALA A 428 2991 4517 4080 432 -166 -1079 C ATOM 2058 O ALA A 428 27.678 44.602 19.326 1.00 29.57 O ANISOU 2058 O ALA A 428 2842 4452 3942 421 -137 -1039 O ATOM 2059 CB ALA A 428 27.742 46.979 17.089 1.00 31.38 C ANISOU 2059 CB ALA A 428 3246 4504 4174 471 -149 -1189 C ATOM 2060 N VAL A 429 25.717 45.697 19.215 1.00 22.94 N ANISOU 2060 N VAL A 429 1971 3609 3138 425 -182 -1092 N ATOM 2061 CA VAL A 429 25.425 45.486 20.629 1.00 33.14 C ANISOU 2061 CA VAL A 429 3149 5026 4417 404 -162 -1065 C ATOM 2062 C VAL A 429 25.278 44.000 20.961 1.00 32.12 C ANISOU 2062 C VAL A 429 2989 4912 4305 385 -182 -981 C ATOM 2063 O VAL A 429 25.665 43.554 22.041 1.00 40.30 O ANISOU 2063 O VAL A 429 3950 6042 5319 369 -153 -945 O ATOM 2064 CB VAL A 429 24.178 46.282 21.089 1.00 32.45 C ANISOU 2064 CB VAL A 429 3001 4986 4342 401 -178 -1099 C ATOM 2065 CG1 VAL A 429 22.929 45.677 20.506 1.00 33.10 C ANISOU 2065 CG1 VAL A 429 3100 5006 4471 397 -238 -1070 C ATOM 2066 CG2 VAL A 429 24.087 46.294 22.584 1.00 31.23 C ANISOU 2066 CG2 VAL A 429 2730 4970 4166 382 -147 -1083 C ATOM 2067 N TYR A 430 24.742 43.231 20.023 1.00 28.95 N ANISOU 2067 N TYR A 430 2644 4414 3940 388 -231 -949 N ATOM 2068 CA TYR A 430 24.595 41.788 20.204 1.00 27.71 C ANISOU 2068 CA TYR A 430 2468 4258 3804 371 -254 -870 C ATOM 2069 C TYR A 430 25.885 41.041 19.863 1.00 27.47 C ANISOU 2069 C TYR A 430 2489 4191 3759 374 -235 -838 C ATOM 2070 O TYR A 430 26.157 39.969 20.403 1.00 27.12 O ANISOU 2070 O TYR A 430 2407 4184 3715 358 -233 -775 O ATOM 2071 CB TYR A 430 23.390 41.266 19.405 1.00 31.12 C ANISOU 2071 CB TYR A 430 2931 4607 4284 371 -316 -849 C ATOM 2072 CG TYR A 430 22.125 41.998 19.793 1.00 35.05 C ANISOU 2072 CG TYR A 430 3376 5146 4797 368 -334 -880 C ATOM 2073 CD1 TYR A 430 21.452 41.691 20.976 1.00 35.72 C ANISOU 2073 CD1 TYR A 430 3356 5334 4883 346 -332 -847 C ATOM 2074 CD2 TYR A 430 21.637 43.037 19.013 1.00 26.84 C ANISOU 2074 CD2 TYR A 430 2386 4044 3765 386 -350 -944 C ATOM 2075 CE1 TYR A 430 20.300 42.385 21.351 1.00 34.54 C ANISOU 2075 CE1 TYR A 430 3154 5223 4744 343 -347 -877 C ATOM 2076 CE2 TYR A 430 20.496 43.735 19.380 1.00 31.14 C ANISOU 2076 CE2 TYR A 430 2881 4628 4323 383 -366 -975 C ATOM 2077 CZ TYR A 430 19.832 43.408 20.550 1.00 35.76 C ANISOU 2077 CZ TYR A 430 3363 5315 4910 361 -364 -942 C ATOM 2078 OH TYR A 430 18.701 44.114 20.907 1.00 43.80 O ANISOU 2078 OH TYR A 430 4331 6372 5940 358 -379 -975 O ATOM 2079 N ARG A 431 26.688 41.624 18.980 1.00 26.91 N ANISOU 2079 N ARG A 431 2502 4049 3674 394 -222 -883 N ATOM 2080 CA ARG A 431 28.031 41.116 18.732 1.00 26.74 C ANISOU 2080 CA ARG A 431 2526 4003 3630 398 -196 -864 C ATOM 2081 C ARG A 431 28.874 41.115 20.004 1.00 28.89 C ANISOU 2081 C ARG A 431 2721 4392 3862 386 -143 -851 C ATOM 2082 O ARG A 431 29.535 40.131 20.320 1.00 33.03 O ANISOU 2082 O ARG A 431 3233 4935 4380 376 -132 -798 O ATOM 2083 CB ARG A 431 28.723 41.954 17.663 1.00 28.68 C ANISOU 2083 CB ARG A 431 2869 4165 3864 422 -186 -925 C ATOM 2084 CG ARG A 431 30.228 42.012 17.809 1.00 19.73 C ANISOU 2084 CG ARG A 431 1756 3049 2691 427 -137 -932 C ATOM 2085 CD ARG A 431 30.850 42.403 16.511 1.00 22.55 C ANISOU 2085 CD ARG A 431 2224 3297 3046 449 -141 -971 C ATOM 2086 NE ARG A 431 30.708 43.827 16.269 1.00 29.34 N ANISOU 2086 NE ARG A 431 3103 4150 3894 464 -127 -1046 N ATOM 2087 CZ ARG A 431 30.561 44.380 15.071 1.00 25.26 C ANISOU 2087 CZ ARG A 431 2674 3533 3391 483 -150 -1088 C ATOM 2088 NH1 ARG A 431 30.509 43.627 13.977 1.00 22.64 N ANISOU 2088 NH1 ARG A 431 2420 3098 3085 489 -188 -1062 N ATOM 2089 NH2 ARG A 431 30.449 45.695 14.975 1.00 24.86 N ANISOU 2089 NH2 ARG A 431 2632 3487 3328 495 -134 -1155 N ATOM 2090 N GLU A 432 28.850 42.230 20.725 1.00 27.04 N ANISOU 2090 N GLU A 432 2435 4236 3602 387 -109 -902 N ATOM 2091 CA GLU A 432 29.597 42.344 21.970 1.00 28.31 C ANISOU 2091 CA GLU A 432 2519 4514 3724 377 -56 -895 C ATOM 2092 C GLU A 432 29.087 41.359 23.006 1.00 33.73 C ANISOU 2092 C GLU A 432 3114 5282 4419 353 -64 -827 C ATOM 2093 O GLU A 432 29.872 40.706 23.686 1.00 30.42 O ANISOU 2093 O GLU A 432 2659 4920 3980 342 -36 -787 O ATOM 2094 CB GLU A 432 29.527 43.767 22.507 1.00 28.91 C ANISOU 2094 CB GLU A 432 2555 4654 3775 384 -23 -965 C ATOM 2095 CG GLU A 432 30.008 44.788 21.489 1.00 40.38 C ANISOU 2095 CG GLU A 432 4097 6026 5220 407 -15 -1034 C ATOM 2096 CD GLU A 432 30.259 46.147 22.097 1.00 49.08 C ANISOU 2096 CD GLU A 432 5160 7198 6291 414 27 -1101 C ATOM 2097 OE1 GLU A 432 29.935 46.335 23.293 1.00 55.42 O ANISOU 2097 OE1 GLU A 432 5865 8113 7081 401 47 -1097 O ATOM 2098 OE2 GLU A 432 30.779 47.024 21.375 1.00 45.98 O ANISOU 2098 OE2 GLU A 432 4834 6749 5887 433 41 -1158 O ATOM 2099 N CYS A 433 27.769 41.231 23.102 1.00 30.87 N ANISOU 2099 N CYS A 433 2716 4925 4090 344 -103 -814 N ATOM 2100 CA CYS A 433 27.178 40.288 24.038 1.00 33.52 C ANISOU 2100 CA CYS A 433 2966 5334 4437 320 -115 -748 C ATOM 2101 C CYS A 433 27.657 38.856 23.786 1.00 37.03 C ANISOU 2101 C CYS A 433 3436 5738 4895 312 -130 -675 C ATOM 2102 O CYS A 433 28.082 38.162 24.707 1.00 36.23 O ANISOU 2102 O CYS A 433 3273 5714 4778 296 -108 -625 O ATOM 2103 CB CYS A 433 25.653 40.360 23.970 1.00 40.53 C ANISOU 2103 CB CYS A 433 3826 6213 5361 314 -160 -747 C ATOM 2104 SG CYS A 433 24.822 39.381 25.245 1.00112.25 S ANISOU 2104 SG CYS A 433 12792 15401 14456 285 -171 -673 S ATOM 2105 N ILE A 434 27.590 38.423 22.534 1.00 33.42 N ANISOU 2105 N ILE A 434 3070 5160 4466 323 -167 -668 N ATOM 2106 CA ILE A 434 27.992 37.073 22.162 1.00 32.50 C ANISOU 2106 CA ILE A 434 2987 4994 4368 317 -187 -602 C ATOM 2107 C ILE A 434 29.452 36.782 22.496 1.00 30.74 C ANISOU 2107 C ILE A 434 2770 4802 4109 317 -142 -588 C ATOM 2108 O ILE A 434 29.780 35.749 23.074 1.00 34.48 O ANISOU 2108 O ILE A 434 3204 5316 4582 302 -137 -526 O ATOM 2109 CB ILE A 434 27.753 36.845 20.662 1.00 31.94 C ANISOU 2109 CB ILE A 434 3022 4784 4332 333 -232 -611 C ATOM 2110 CG1 ILE A 434 26.310 36.406 20.434 1.00 28.56 C ANISOU 2110 CG1 ILE A 434 2577 4324 3949 325 -287 -585 C ATOM 2111 CG2 ILE A 434 28.733 35.823 20.106 1.00 24.94 C ANISOU 2111 CG2 ILE A 434 2193 3836 3447 335 -234 -569 C ATOM 2112 CD1 ILE A 434 25.874 36.503 18.998 1.00 35.63 C ANISOU 2112 CD1 ILE A 434 3570 5091 4876 343 -331 -610 C ATOM 2113 N ILE A 435 30.322 37.707 22.127 1.00 22.62 N ANISOU 2113 N ILE A 435 1790 3754 3051 335 -109 -648 N ATOM 2114 CA ILE A 435 31.741 37.554 22.372 1.00 31.93 C ANISOU 2114 CA ILE A 435 2980 4956 4194 337 -65 -643 C ATOM 2115 C ILE A 435 32.056 37.266 23.843 1.00 42.36 C ANISOU 2115 C ILE A 435 4197 6409 5487 318 -27 -609 C ATOM 2116 O ILE A 435 32.734 36.283 24.151 1.00 42.23 O ANISOU 2116 O ILE A 435 4171 6411 5466 309 -18 -555 O ATOM 2117 CB ILE A 435 32.517 38.789 21.891 1.00 30.08 C ANISOU 2117 CB ILE A 435 2802 4696 3930 358 -32 -721 C ATOM 2118 CG1 ILE A 435 32.393 38.925 20.372 1.00 24.28 C ANISOU 2118 CG1 ILE A 435 2179 3826 3221 377 -68 -748 C ATOM 2119 CG2 ILE A 435 33.974 38.686 22.309 1.00 32.72 C ANISOU 2119 CG2 ILE A 435 3137 5072 4225 359 19 -718 C ATOM 2120 CD1 ILE A 435 33.072 40.162 19.785 1.00 25.20 C ANISOU 2120 CD1 ILE A 435 2357 3907 3312 398 -39 -824 C ATOM 2121 N GLU A 436 31.559 38.101 24.753 1.00 46.78 N ANISOU 2121 N GLU A 436 4680 7062 6030 313 -7 -639 N ATOM 2122 CA GLU A 436 31.817 37.866 26.175 1.00 55.28 C ANISOU 2122 CA GLU A 436 5655 8268 7080 295 29 -607 C ATOM 2123 C GLU A 436 30.958 36.762 26.799 1.00 54.96 C ANISOU 2123 C GLU A 436 5546 8270 7067 273 0 -532 C ATOM 2124 O GLU A 436 31.315 36.216 27.839 1.00 61.58 O ANISOU 2124 O GLU A 436 6313 9199 7887 257 24 -489 O ATOM 2125 CB GLU A 436 31.760 39.158 27.003 1.00 57.74 C ANISOU 2125 CB GLU A 436 5905 8673 7359 298 69 -667 C ATOM 2126 CG GLU A 436 30.785 40.213 26.530 1.00 69.82 C ANISOU 2126 CG GLU A 436 7451 10170 8906 309 47 -727 C ATOM 2127 CD GLU A 436 31.035 41.562 27.198 1.00 85.16 C ANISOU 2127 CD GLU A 436 9351 12193 10814 316 92 -795 C ATOM 2128 OE1 GLU A 436 30.300 42.532 26.902 1.00 88.37 O ANISOU 2128 OE1 GLU A 436 9765 12581 11229 325 79 -849 O ATOM 2129 OE2 GLU A 436 31.973 41.650 28.023 1.00 89.20 O ANISOU 2129 OE2 GLU A 436 9820 12785 11288 312 140 -794 O ATOM 2130 N LYS A 437 29.855 36.411 26.147 1.00 45.63 N ANISOU 2130 N LYS A 437 4389 7020 5928 271 -53 -517 N ATOM 2131 CA LYS A 437 28.955 35.390 26.677 1.00 46.14 C ANISOU 2131 CA LYS A 437 4391 7119 6022 249 -85 -447 C ATOM 2132 C LYS A 437 29.465 33.974 26.457 1.00 45.90 C ANISOU 2132 C LYS A 437 4384 7048 6007 241 -100 -375 C ATOM 2133 O LYS A 437 29.338 33.122 27.337 1.00 47.62 O ANISOU 2133 O LYS A 437 4531 7337 6227 221 -98 -312 O ATOM 2134 CB LYS A 437 27.555 35.513 26.069 1.00 52.95 C ANISOU 2134 CB LYS A 437 5269 7923 6927 251 -137 -457 C ATOM 2135 CG LYS A 437 26.599 34.387 26.469 1.00 57.44 C ANISOU 2135 CG LYS A 437 5784 8512 7531 229 -174 -384 C ATOM 2136 CD LYS A 437 26.280 34.426 27.960 1.00 61.04 C ANISOU 2136 CD LYS A 437 6120 9107 7966 209 -148 -361 C ATOM 2137 CE LYS A 437 25.095 33.535 28.313 1.00 63.17 C ANISOU 2137 CE LYS A 437 6334 9395 8273 189 -189 -300 C ATOM 2138 NZ LYS A 437 25.384 32.096 28.084 1.00 67.67 N ANISOU 2138 NZ LYS A 437 6923 9922 8866 179 -211 -223 N ATOM 2139 N CYS A 438 30.025 33.702 25.285 1.00 42.00 N ANISOU 2139 N CYS A 438 3990 6444 5526 256 -116 -381 N ATOM 2140 CA CYS A 438 30.465 32.342 25.014 1.00 43.21 C ANISOU 2140 CA CYS A 438 4168 6554 5697 248 -134 -313 C ATOM 2141 C CYS A 438 31.855 32.219 24.399 1.00 38.75 C ANISOU 2141 C CYS A 438 3678 5933 5111 262 -111 -325 C ATOM 2142 O CYS A 438 32.463 31.153 24.473 1.00 45.22 O ANISOU 2142 O CYS A 438 4502 6747 5935 254 -112 -269 O ATOM 2143 CB CYS A 438 29.439 31.596 24.162 1.00 43.45 C ANISOU 2143 CB CYS A 438 4236 6492 5781 247 -196 -281 C ATOM 2144 SG CYS A 438 29.588 31.913 22.413 1.00 53.73 S ANISOU 2144 SG CYS A 438 5671 7639 7104 273 -226 -328 S ATOM 2145 N LEU A 439 32.362 33.289 23.795 1.00 32.65 N ANISOU 2145 N LEU A 439 2965 5122 4318 283 -91 -396 N ATOM 2146 CA LEU A 439 33.680 33.213 23.159 1.00 30.56 C ANISOU 2146 CA LEU A 439 2776 4803 4034 296 -69 -410 C ATOM 2147 C LEU A 439 34.801 33.478 24.156 1.00 27.88 C ANISOU 2147 C LEU A 439 2388 4561 3645 293 -10 -416 C ATOM 2148 O LEU A 439 35.749 32.705 24.269 1.00 33.73 O ANISOU 2148 O LEU A 439 3139 5304 4375 289 5 -379 O ATOM 2149 CB LEU A 439 33.781 34.178 21.973 1.00 29.10 C ANISOU 2149 CB LEU A 439 2684 4523 3848 320 -76 -481 C ATOM 2150 CG LEU A 439 32.726 33.996 20.878 1.00 35.27 C ANISOU 2150 CG LEU A 439 3522 5201 4676 327 -135 -482 C ATOM 2151 CD1 LEU A 439 33.087 34.810 19.652 1.00 32.07 C ANISOU 2151 CD1 LEU A 439 3218 4698 4268 351 -137 -546 C ATOM 2152 CD2 LEU A 439 32.593 32.531 20.515 1.00 34.26 C ANISOU 2152 CD2 LEU A 439 3412 5020 4584 317 -174 -409 C ATOM 2153 N MET A 440 34.667 34.575 24.888 1.00 33.92 N ANISOU 2153 N MET A 440 3099 5407 4381 294 23 -463 N ATOM 2154 CA MET A 440 35.691 35.035 25.808 1.00 25.31 C ANISOU 2154 CA MET A 440 1964 4410 3243 293 82 -481 C ATOM 2155 C MET A 440 36.037 33.943 26.813 1.00 25.03 C ANISOU 2155 C MET A 440 1858 4453 3200 273 95 -409 C ATOM 2156 O MET A 440 35.147 33.326 27.390 1.00 30.87 O ANISOU 2156 O MET A 440 2533 5236 3961 255 71 -359 O ATOM 2157 CB MET A 440 35.198 36.286 26.527 1.00 34.71 C ANISOU 2157 CB MET A 440 3093 5683 4413 294 107 -536 C ATOM 2158 CG MET A 440 36.245 37.343 26.695 1.00 38.34 C ANISOU 2158 CG MET A 440 3566 6175 4829 308 160 -599 C ATOM 2159 SD MET A 440 36.928 37.858 25.112 1.00 47.53 S ANISOU 2159 SD MET A 440 4864 7201 5995 334 154 -654 S ATOM 2160 CE MET A 440 38.630 38.003 25.609 1.00 21.87 C ANISOU 2160 CE MET A 440 1613 4002 2694 339 217 -668 C ATOM 2161 N ARG A 441 37.331 33.701 26.997 1.00 20.07 N ANISOU 2161 N ARG A 441 1242 3841 2541 276 132 -402 N ATOM 2162 CA ARG A 441 37.817 32.655 27.889 1.00 30.44 C ANISOU 2162 CA ARG A 441 2497 5223 3844 259 146 -334 C ATOM 2163 C ARG A 441 37.678 31.250 27.302 1.00 36.26 C ANISOU 2163 C ARG A 441 3270 5885 4620 251 102 -265 C ATOM 2164 O ARG A 441 38.082 30.277 27.921 1.00 45.99 O ANISOU 2164 O ARG A 441 4463 7162 5850 237 108 -204 O ATOM 2165 CB ARG A 441 37.125 32.731 29.254 1.00 30.67 C ANISOU 2165 CB ARG A 441 2409 5380 3864 240 159 -311 C ATOM 2166 CG ARG A 441 37.575 33.893 30.119 1.00 37.01 C ANISOU 2166 CG ARG A 441 3159 6281 4620 245 213 -366 C ATOM 2167 CD ARG A 441 36.733 33.984 31.378 1.00 40.06 C ANISOU 2167 CD ARG A 441 3433 6787 5002 227 220 -346 C ATOM 2168 NE ARG A 441 35.314 33.979 31.048 1.00 50.04 N ANISOU 2168 NE ARG A 441 4690 8016 6306 222 172 -340 N ATOM 2169 CZ ARG A 441 34.666 35.030 30.558 1.00 51.80 C ANISOU 2169 CZ ARG A 441 4939 8207 6537 234 161 -402 C ATOM 2170 NH1 ARG A 441 35.324 36.162 30.351 1.00 39.85 N ANISOU 2170 NH1 ARG A 441 3457 6690 4993 251 196 -474 N ATOM 2171 NH2 ARG A 441 33.367 34.947 30.274 1.00 52.35 N ANISOU 2171 NH2 ARG A 441 5001 8246 6644 228 116 -393 N ATOM 2172 N ASN A 442 37.103 31.141 26.111 1.00 35.26 N ANISOU 2172 N ASN A 442 3563 5752 4083 -257 -148 -662 N ATOM 2173 CA ASN A 442 36.977 29.847 25.461 1.00 24.21 C ANISOU 2173 CA ASN A 442 2196 4279 2724 -264 -170 -564 C ATOM 2174 C ASN A 442 37.636 29.869 24.103 1.00 30.73 C ANISOU 2174 C ASN A 442 3073 4954 3649 -218 -170 -571 C ATOM 2175 O ASN A 442 37.348 29.019 23.260 1.00 31.14 O ANISOU 2175 O ASN A 442 3159 4925 3749 -214 -177 -512 O ATOM 2176 CB ASN A 442 35.502 29.485 25.294 1.00 26.84 C ANISOU 2176 CB ASN A 442 2525 4637 3034 -282 -156 -548 C ATOM 2177 CG ASN A 442 34.802 29.266 26.622 1.00 36.04 C ANISOU 2177 CG ASN A 442 3643 5950 4102 -333 -159 -527 C ATOM 2178 OD1 ASN A 442 33.936 30.043 27.015 1.00 36.29 O ANISOU 2178 OD1 ASN A 442 3646 6054 4088 -339 -132 -593 O ATOM 2179 ND2 ASN A 442 35.192 28.213 27.329 1.00 40.22 N ANISOU 2179 ND2 ASN A 442 4162 6522 4597 -370 -192 -435 N ATOM 2180 N LEU A 443 38.509 30.852 23.887 1.00 25.34 N ANISOU 2180 N LEU A 443 2396 4235 2997 -183 -159 -644 N ATOM 2181 CA LEU A 443 39.049 31.099 22.555 1.00 23.50 C ANISOU 2181 CA LEU A 443 2210 3859 2858 -135 -151 -669 C ATOM 2182 C LEU A 443 39.933 29.952 22.079 1.00 23.36 C ANISOU 2182 C LEU A 443 2226 3756 2894 -136 -184 -577 C ATOM 2183 O LEU A 443 39.821 29.506 20.938 1.00 25.86 O ANISOU 2183 O LEU A 443 2585 3962 3279 -114 -183 -551 O ATOM 2184 CB LEU A 443 39.786 32.443 22.490 1.00 21.43 C ANISOU 2184 CB LEU A 443 1945 3582 2615 -99 -130 -771 C ATOM 2185 CG LEU A 443 38.938 33.708 22.687 1.00 23.72 C ANISOU 2185 CG LEU A 443 2210 3931 2871 -88 -91 -874 C ATOM 2186 CD1 LEU A 443 39.793 34.969 22.655 1.00 22.48 C ANISOU 2186 CD1 LEU A 443 2050 3756 2734 -54 -72 -968 C ATOM 2187 CD2 LEU A 443 37.801 33.812 21.663 1.00 21.93 C ANISOU 2187 CD2 LEU A 443 2008 3643 2681 -67 -66 -894 C ATOM 2188 N LEU A 444 40.804 29.465 22.953 1.00 23.67 N ANISOU 2188 N LEU A 444 2246 3845 2901 -161 -214 -527 N ATOM 2189 CA LEU A 444 41.683 28.360 22.586 1.00 24.78 C ANISOU 2189 CA LEU A 444 2415 3909 3090 -163 -247 -437 C ATOM 2190 C LEU A 444 40.865 27.110 22.255 1.00 27.39 C ANISOU 2190 C LEU A 444 2762 4218 3427 -187 -259 -346 C ATOM 2191 O LEU A 444 41.147 26.398 21.295 1.00 28.62 O ANISOU 2191 O LEU A 444 2958 4264 3653 -172 -269 -297 O ATOM 2192 CB LEU A 444 42.684 28.068 23.705 1.00 24.62 C ANISOU 2192 CB LEU A 444 2366 3962 3025 -189 -277 -398 C ATOM 2193 CG LEU A 444 43.542 26.818 23.478 1.00 29.23 C ANISOU 2193 CG LEU A 444 2975 4482 3651 -197 -314 -295 C ATOM 2194 CD1 LEU A 444 44.274 26.884 22.138 1.00 25.56 C ANISOU 2194 CD1 LEU A 444 2560 3865 3288 -152 -310 -308 C ATOM 2195 CD2 LEU A 444 44.518 26.610 24.625 1.00 23.25 C ANISOU 2195 CD2 LEU A 444 2186 3803 2846 -221 -343 -262 C ATOM 2196 N SER A 445 39.844 26.858 23.059 1.00 23.88 N ANISOU 2196 N SER A 445 2284 3879 2909 -225 -256 -326 N ATOM 2197 CA SER A 445 38.979 25.705 22.868 1.00 26.60 C ANISOU 2197 CA SER A 445 2638 4218 3250 -252 -265 -243 C ATOM 2198 C SER A 445 38.161 25.799 21.578 1.00 24.77 C ANISOU 2198 C SER A 445 2442 3891 3078 -224 -241 -269 C ATOM 2199 O SER A 445 38.116 24.861 20.779 1.00 25.41 O ANISOU 2199 O SER A 445 2557 3887 3212 -222 -252 -204 O ATOM 2200 CB SER A 445 38.041 25.573 24.067 1.00 23.09 C ANISOU 2200 CB SER A 445 2148 3915 2709 -298 -264 -229 C ATOM 2201 OG SER A 445 37.010 24.655 23.789 1.00 37.35 O ANISOU 2201 OG SER A 445 3963 5716 4513 -320 -264 -168 O ATOM 2202 N LEU A 446 37.509 26.935 21.383 1.00 22.19 N ANISOU 2202 N LEU A 446 2107 3583 2742 -202 -208 -364 N ATOM 2203 CA LEU A 446 36.649 27.125 20.221 1.00 22.68 C ANISOU 2203 CA LEU A 446 2198 3565 2853 -176 -184 -394 C ATOM 2204 C LEU A 446 37.446 27.184 18.918 1.00 21.44 C ANISOU 2204 C LEU A 446 2091 3262 2793 -131 -184 -404 C ATOM 2205 O LEU A 446 36.925 26.873 17.845 1.00 21.19 O ANISOU 2205 O LEU A 446 2092 3145 2814 -114 -175 -393 O ATOM 2206 CB LEU A 446 35.805 28.392 20.389 1.00 22.41 C ANISOU 2206 CB LEU A 446 2140 3591 2784 -162 -148 -497 C ATOM 2207 CG LEU A 446 34.801 28.376 21.549 1.00 25.22 C ANISOU 2207 CG LEU A 446 2449 4088 3047 -205 -143 -494 C ATOM 2208 CD1 LEU A 446 34.103 29.712 21.638 1.00 24.65 C ANISOU 2208 CD1 LEU A 446 2355 4061 2949 -187 -107 -602 C ATOM 2209 CD2 LEU A 446 33.791 27.250 21.389 1.00 21.79 C ANISOU 2209 CD2 LEU A 446 2019 3657 2602 -235 -150 -417 C ATOM 2210 N SER A 447 38.706 27.590 19.014 1.00 20.27 N ANISOU 2210 N SER A 447 1948 3086 2668 -112 -193 -426 N ATOM 2211 CA SER A 447 39.547 27.714 17.830 1.00 21.14 C ANISOU 2211 CA SER A 447 2104 3060 2869 -70 -192 -440 C ATOM 2212 C SER A 447 39.931 26.344 17.299 1.00 24.79 C ANISOU 2212 C SER A 447 2597 3443 3379 -81 -220 -338 C ATOM 2213 O SER A 447 40.444 26.231 16.196 1.00 27.42 O ANISOU 2213 O SER A 447 2972 3655 3791 -50 -219 -336 O ATOM 2214 CB SER A 447 40.807 28.533 18.126 1.00 19.79 C ANISOU 2214 CB SER A 447 1928 2885 2708 -48 -194 -492 C ATOM 2215 OG SER A 447 40.479 29.895 18.330 1.00 24.93 O ANISOU 2215 OG SER A 447 2558 3582 3333 -29 -163 -597 O ATOM 2216 N GLN A 448 39.688 25.304 18.088 1.00 25.27 N ANISOU 2216 N GLN A 448 2637 3571 3393 -125 -243 -252 N ATOM 2217 CA GLN A 448 39.991 23.953 17.641 1.00 29.02 C ANISOU 2217 CA GLN A 448 3139 3976 3910 -139 -269 -152 C ATOM 2218 C GLN A 448 38.737 23.197 17.205 1.00 22.19 C ANISOU 2218 C GLN A 448 2284 3103 3045 -157 -262 -108 C ATOM 2219 O GLN A 448 38.793 22.004 16.948 1.00 30.98 O ANISOU 2219 O GLN A 448 3415 4173 4184 -175 -281 -20 O ATOM 2220 CB GLN A 448 40.727 23.172 18.725 1.00 22.42 C ANISOU 2220 CB GLN A 448 2279 3205 3033 -175 -303 -75 C ATOM 2221 CG GLN A 448 42.070 23.754 19.096 1.00 30.96 C ANISOU 2221 CG GLN A 448 3354 4285 4122 -158 -314 -107 C ATOM 2222 CD GLN A 448 42.624 23.139 20.362 1.00 32.90 C ANISOU 2222 CD GLN A 448 3567 4624 4309 -196 -345 -41 C ATOM 2223 OE1 GLN A 448 43.103 22.004 20.361 1.00 33.56 O ANISOU 2223 OE1 GLN A 448 3662 4675 4414 -213 -372 51 O ATOM 2224 NE2 GLN A 448 42.549 23.882 21.455 1.00 29.28 N ANISOU 2224 NE2 GLN A 448 3065 4283 3776 -210 -340 -88 N ATOM 2225 N GLU A 449 37.614 23.897 17.120 1.00 21.99 N ANISOU 2225 N GLU A 449 2247 3118 2992 -152 -234 -170 N ATOM 2226 CA GLU A 449 36.358 23.295 16.676 1.00 25.17 C ANISOU 2226 CA GLU A 449 2656 3514 3393 -167 -224 -139 C ATOM 2227 C GLU A 449 36.179 23.553 15.192 1.00 21.26 C ANISOU 2227 C GLU A 449 2205 2893 2978 -125 -206 -175 C ATOM 2228 O GLU A 449 36.464 24.648 14.708 1.00 24.22 O ANISOU 2228 O GLU A 449 2591 3229 3382 -86 -186 -259 O ATOM 2229 CB GLU A 449 35.188 23.920 17.427 1.00 29.26 C ANISOU 2229 CB GLU A 449 3135 4149 3834 -185 -203 -188 C ATOM 2230 CG GLU A 449 35.272 23.776 18.935 1.00 39.54 C ANISOU 2230 CG GLU A 449 4390 5585 5050 -227 -218 -162 C ATOM 2231 CD GLU A 449 34.242 22.822 19.490 1.00 45.01 C ANISOU 2231 CD GLU A 449 5062 6349 5690 -273 -225 -93 C ATOM 2232 OE1 GLU A 449 34.244 22.595 20.716 1.00 52.72 O ANISOU 2232 OE1 GLU A 449 6002 7435 6594 -311 -238 -63 O ATOM 2233 OE2 GLU A 449 33.418 22.310 18.707 1.00 51.24 O ANISOU 2233 OE2 GLU A 449 5873 7087 6509 -273 -216 -70 O ATOM 2234 N LYS A 450 35.715 22.542 14.471 1.00 23.58 N ANISOU 2234 N LYS A 450 2525 3124 3309 -135 -211 -111 N ATOM 2235 CA LYS A 450 35.496 22.661 13.041 1.00 21.39 C ANISOU 2235 CA LYS A 450 2291 2730 3108 -99 -196 -137 C ATOM 2236 C LYS A 450 34.591 23.851 12.725 1.00 27.15 C ANISOU 2236 C LYS A 450 3013 3479 3825 -73 -162 -234 C ATOM 2237 O LYS A 450 34.891 24.665 11.849 1.00 24.40 O ANISOU 2237 O LYS A 450 2690 3052 3527 -29 -145 -299 O ATOM 2238 CB LYS A 450 34.884 21.367 12.489 1.00 25.50 C ANISOU 2238 CB LYS A 450 2831 3205 3654 -121 -205 -53 C ATOM 2239 CG LYS A 450 34.734 21.337 10.965 1.00 28.78 C ANISOU 2239 CG LYS A 450 3293 3491 4151 -87 -192 -69 C ATOM 2240 CD LYS A 450 34.141 20.009 10.503 1.00 33.02 C ANISOU 2240 CD LYS A 450 3846 3989 4709 -113 -201 15 C ATOM 2241 CE LYS A 450 33.733 20.044 9.039 1.00 33.02 C ANISOU 2241 CE LYS A 450 3887 3878 4779 -82 -185 -7 C ATOM 2242 NZ LYS A 450 34.876 20.375 8.141 1.00 40.83 N ANISOU 2242 NZ LYS A 450 4916 4753 5846 -42 -186 -32 N ATOM 2243 N PHE A 451 33.489 23.964 13.452 1.00 24.01 N ANISOU 2243 N PHE A 451 2579 3186 3357 -100 -152 -244 N ATOM 2244 CA PHE A 451 32.522 25.005 13.142 1.00 25.67 C ANISOU 2244 CA PHE A 451 2782 3417 3555 -77 -120 -330 C ATOM 2245 C PHE A 451 32.799 26.296 13.911 1.00 20.78 C ANISOU 2245 C PHE A 451 2131 2871 2892 -64 -105 -415 C ATOM 2246 O PHE A 451 32.830 27.371 13.319 1.00 25.80 O ANISOU 2246 O PHE A 451 2779 3466 3558 -23 -82 -498 O ATOM 2247 CB PHE A 451 31.092 24.488 13.357 1.00 21.64 C ANISOU 2247 CB PHE A 451 2251 2969 3000 -109 -112 -303 C ATOM 2248 CG PHE A 451 30.820 23.188 12.654 1.00 24.92 C ANISOU 2248 CG PHE A 451 2696 3317 3456 -124 -126 -219 C ATOM 2249 CD1 PHE A 451 30.890 23.110 11.269 1.00 24.86 C ANISOU 2249 CD1 PHE A 451 2732 3185 3528 -91 -119 -226 C ATOM 2250 CD2 PHE A 451 30.522 22.041 13.369 1.00 20.57 C ANISOU 2250 CD2 PHE A 451 2126 2823 2865 -173 -145 -132 C ATOM 2251 CE1 PHE A 451 30.651 21.923 10.612 1.00 22.37 C ANISOU 2251 CE1 PHE A 451 2443 2806 3251 -106 -131 -151 C ATOM 2252 CE2 PHE A 451 30.292 20.835 12.709 1.00 23.07 C ANISOU 2252 CE2 PHE A 451 2470 3074 3221 -187 -156 -55 C ATOM 2253 CZ PHE A 451 30.355 20.782 11.332 1.00 22.59 C ANISOU 2253 CZ PHE A 451 2452 2891 3240 -154 -149 -65 C ATOM 2254 N ALA A 452 33.038 26.194 15.214 1.00 19.08 N ANISOU 2254 N ALA A 452 1878 2763 2609 -98 -119 -395 N ATOM 2255 CA ALA A 452 33.222 27.398 16.020 1.00 20.39 C ANISOU 2255 CA ALA A 452 2010 3009 2728 -91 -104 -476 C ATOM 2256 C ALA A 452 34.458 28.215 15.625 1.00 19.71 C ANISOU 2256 C ALA A 452 1944 2855 2691 -50 -101 -530 C ATOM 2257 O ALA A 452 34.495 29.418 15.862 1.00 29.76 O ANISOU 2257 O ALA A 452 3200 4161 3947 -29 -80 -617 O ATOM 2258 CB ALA A 452 33.231 27.072 17.507 1.00 20.03 C ANISOU 2258 CB ALA A 452 1919 3094 2598 -138 -120 -440 C ATOM 2259 N SER A 453 35.459 27.578 15.021 1.00 19.03 N ANISOU 2259 N SER A 453 1893 2672 2667 -39 -122 -480 N ATOM 2260 CA SER A 453 36.650 28.316 14.585 1.00 19.17 C ANISOU 2260 CA SER A 453 1931 2617 2735 0 -119 -530 C ATOM 2261 C SER A 453 36.314 29.417 13.584 1.00 19.23 C ANISOU 2261 C SER A 453 1960 2558 2787 48 -86 -621 C ATOM 2262 O SER A 453 36.989 30.436 13.538 1.00 21.87 O ANISOU 2262 O SER A 453 2296 2876 3137 78 -73 -692 O ATOM 2263 CB SER A 453 37.743 27.393 14.027 1.00 18.05 C ANISOU 2263 CB SER A 453 1825 2377 2657 5 -146 -459 C ATOM 2264 OG SER A 453 37.307 26.692 12.879 1.00 22.42 O ANISOU 2264 OG SER A 453 2417 2834 3269 14 -145 -420 O ATOM 2265 N HIS A 454 35.272 29.215 12.784 1.00 19.55 N ANISOU 2265 N HIS A 454 2019 2562 2849 55 -72 -618 N ATOM 2266 CA HIS A 454 34.862 30.253 11.847 1.00 17.41 C ANISOU 2266 CA HIS A 454 1767 2232 2617 100 -41 -703 C ATOM 2267 C HIS A 454 34.260 31.438 12.601 1.00 22.16 C ANISOU 2267 C HIS A 454 2328 2934 3158 103 -15 -787 C ATOM 2268 O HIS A 454 34.422 32.586 12.206 1.00 25.08 O ANISOU 2268 O HIS A 454 2705 3273 3552 141 9 -872 O ATOM 2269 CB HIS A 454 33.862 29.708 10.836 1.00 16.76 C ANISOU 2269 CB HIS A 454 1710 2090 2567 105 -34 -677 C ATOM 2270 CG HIS A 454 34.453 28.720 9.886 1.00 17.16 C ANISOU 2270 CG HIS A 454 1806 2026 2688 111 -53 -609 C ATOM 2271 ND1 HIS A 454 35.176 29.098 8.776 1.00 20.03 N ANISOU 2271 ND1 HIS A 454 2211 2270 3128 155 -46 -639 N ATOM 2272 CD2 HIS A 454 34.433 27.367 9.879 1.00 17.83 C ANISOU 2272 CD2 HIS A 454 1900 2096 2779 79 -78 -513 C ATOM 2273 CE1 HIS A 454 35.572 28.022 8.124 1.00 18.10 C ANISOU 2273 CE1 HIS A 454 2000 1943 2934 149 -66 -566 C ATOM 2274 NE2 HIS A 454 35.137 26.959 8.775 1.00 18.00 N ANISOU 2274 NE2 HIS A 454 1968 1992 2881 103 -85 -488 N ATOM 2275 N VAL A 455 33.563 31.142 13.692 1.00 24.08 N ANISOU 2275 N VAL A 455 2530 3296 3325 61 -20 -764 N ATOM 2276 CA VAL A 455 32.971 32.177 14.522 1.00 19.55 C ANISOU 2276 CA VAL A 455 1914 2827 2688 57 3 -839 C ATOM 2277 C VAL A 455 34.064 32.988 15.204 1.00 25.61 C ANISOU 2277 C VAL A 455 2664 3626 3441 66 3 -888 C ATOM 2278 O VAL A 455 33.980 34.212 15.271 1.00 27.09 O ANISOU 2278 O VAL A 455 2839 3833 3622 91 30 -978 O ATOM 2279 CB VAL A 455 32.039 31.574 15.575 1.00 20.09 C ANISOU 2279 CB VAL A 455 1941 3016 2676 6 -5 -795 C ATOM 2280 CG1 VAL A 455 31.593 32.634 16.584 1.00 20.68 C ANISOU 2280 CG1 VAL A 455 1968 3207 2681 -2 17 -871 C ATOM 2281 CG2 VAL A 455 30.851 30.910 14.894 1.00 18.72 C ANISOU 2281 CG2 VAL A 455 1782 2817 2516 -1 0 -759 C ATOM 2282 N VAL A 456 35.095 32.297 15.688 1.00 21.09 N ANISOU 2282 N VAL A 456 2091 3055 2866 45 -27 -827 N ATOM 2283 CA VAL A 456 36.227 32.948 16.333 1.00 18.83 C ANISOU 2283 CA VAL A 456 1790 2796 2568 52 -30 -865 C ATOM 2284 C VAL A 456 36.929 33.932 15.388 1.00 18.20 C ANISOU 2284 C VAL A 456 1742 2615 2557 105 -10 -940 C ATOM 2285 O VAL A 456 37.245 35.054 15.774 1.00 20.08 O ANISOU 2285 O VAL A 456 1962 2888 2781 122 9 -1020 O ATOM 2286 CB VAL A 456 37.234 31.918 16.877 1.00 20.07 C ANISOU 2286 CB VAL A 456 1947 2960 2719 23 -68 -779 C ATOM 2287 CG1 VAL A 456 38.460 32.619 17.403 1.00 20.68 C ANISOU 2287 CG1 VAL A 456 2012 3051 2793 35 -72 -822 C ATOM 2288 CG2 VAL A 456 36.596 31.054 17.968 1.00 23.76 C ANISOU 2288 CG2 VAL A 456 2378 3540 3110 -31 -86 -711 C ATOM 2289 N GLU A 457 37.150 33.521 14.147 1.00 17.65 N ANISOU 2289 N GLU A 457 1720 2421 2565 132 -14 -915 N ATOM 2290 CA GLU A 457 37.691 34.429 13.137 1.00 21.12 C ANISOU 2290 CA GLU A 457 2194 2758 3074 184 7 -984 C ATOM 2291 C GLU A 457 36.830 35.683 12.981 1.00 23.06 C ANISOU 2291 C GLU A 457 2426 3029 3306 210 46 -1081 C ATOM 2292 O GLU A 457 37.351 36.798 12.978 1.00 28.31 O ANISOU 2292 O GLU A 457 3089 3685 3983 239 66 -1160 O ATOM 2293 CB GLU A 457 37.803 33.736 11.788 1.00 16.53 C ANISOU 2293 CB GLU A 457 1665 2045 2571 206 0 -940 C ATOM 2294 CG GLU A 457 38.714 32.533 11.764 1.00 18.15 C ANISOU 2294 CG GLU A 457 1888 2205 2802 186 -36 -848 C ATOM 2295 CD GLU A 457 38.880 32.001 10.361 1.00 27.59 C ANISOU 2295 CD GLU A 457 3138 3264 4082 212 -38 -817 C ATOM 2296 OE1 GLU A 457 39.309 32.785 9.491 1.00 32.72 O ANISOU 2296 OE1 GLU A 457 3816 3828 4788 256 -20 -877 O ATOM 2297 OE2 GLU A 457 38.567 30.817 10.121 1.00 30.51 O ANISOU 2297 OE2 GLU A 457 3519 3612 4461 189 -58 -734 O ATOM 2298 N LYS A 458 35.517 35.500 12.851 1.00 18.12 N ANISOU 2298 N LYS A 458 1793 2436 2657 199 57 -1074 N ATOM 2299 CA LYS A 458 34.593 36.632 12.738 1.00 23.22 C ANISOU 2299 CA LYS A 458 2423 3112 3287 222 93 -1162 C ATOM 2300 C LYS A 458 34.692 37.592 13.921 1.00 20.62 C ANISOU 2300 C LYS A 458 2047 2893 2895 211 107 -1227 C ATOM 2301 O LYS A 458 34.737 38.799 13.738 1.00 22.93 O ANISOU 2301 O LYS A 458 2337 3175 3200 244 137 -1316 O ATOM 2302 CB LYS A 458 33.149 36.154 12.580 1.00 25.80 C ANISOU 2302 CB LYS A 458 2742 3471 3590 204 98 -1135 C ATOM 2303 CG LYS A 458 32.828 35.606 11.198 1.00 28.40 C ANISOU 2303 CG LYS A 458 3118 3684 3986 227 97 -1103 C ATOM 2304 CD LYS A 458 33.547 36.396 10.123 1.00 29.21 C ANISOU 2304 CD LYS A 458 3261 3673 4165 281 113 -1159 C ATOM 2305 CE LYS A 458 32.852 36.259 8.785 1.00 30.09 C ANISOU 2305 CE LYS A 458 3411 3691 4332 309 124 -1157 C ATOM 2306 NZ LYS A 458 32.689 34.842 8.381 1.00 32.32 N ANISOU 2306 NZ LYS A 458 3714 3934 4632 284 97 -1060 N ATOM 2307 N ALA A 459 34.741 37.047 15.130 1.00 23.78 N ANISOU 2307 N ALA A 459 2411 3398 3228 165 87 -1183 N ATOM 2308 CA ALA A 459 34.885 37.864 16.328 1.00 23.11 C ANISOU 2308 CA ALA A 459 2279 3423 3079 149 98 -1240 C ATOM 2309 C ALA A 459 36.166 38.701 16.285 1.00 28.30 C ANISOU 2309 C ALA A 459 2944 4039 3769 179 104 -1296 C ATOM 2310 O ALA A 459 36.145 39.890 16.589 1.00 28.14 O ANISOU 2310 O ALA A 459 2904 4056 3733 196 132 -1384 O ATOM 2311 CB ALA A 459 34.860 36.995 17.569 1.00 20.51 C ANISOU 2311 CB ALA A 459 1913 3202 2676 94 70 -1171 C ATOM 2312 N PHE A 460 37.274 38.075 15.904 1.00 20.60 N ANISOU 2312 N PHE A 460 1999 2987 2839 184 79 -1245 N ATOM 2313 CA PHE A 460 38.529 38.793 15.748 1.00 25.00 C ANISOU 2313 CA PHE A 460 2569 3493 3435 214 84 -1295 C ATOM 2314 C PHE A 460 38.435 39.918 14.718 1.00 28.18 C ANISOU 2314 C PHE A 460 2999 3812 3897 267 120 -1382 C ATOM 2315 O PHE A 460 38.941 41.011 14.950 1.00 23.88 O ANISOU 2315 O PHE A 460 2443 3279 3353 287 141 -1461 O ATOM 2316 CB PHE A 460 39.661 37.840 15.356 1.00 25.52 C ANISOU 2316 CB PHE A 460 2668 3480 3550 213 51 -1220 C ATOM 2317 CG PHE A 460 40.418 37.285 16.526 1.00 24.06 C ANISOU 2317 CG PHE A 460 2453 3375 3315 174 21 -1171 C ATOM 2318 CD1 PHE A 460 40.316 35.947 16.866 1.00 24.66 C ANISOU 2318 CD1 PHE A 460 2526 3475 3369 135 -13 -1069 C ATOM 2319 CD2 PHE A 460 41.236 38.097 17.282 1.00 19.96 C ANISOU 2319 CD2 PHE A 460 1907 2905 2770 176 26 -1227 C ATOM 2320 CE1 PHE A 460 41.015 35.436 17.946 1.00 24.54 C ANISOU 2320 CE1 PHE A 460 2483 3533 3307 100 -41 -1022 C ATOM 2321 CE2 PHE A 460 41.935 37.589 18.358 1.00 22.04 C ANISOU 2321 CE2 PHE A 460 2143 3245 2988 140 -3 -1182 C ATOM 2322 CZ PHE A 460 41.828 36.260 18.687 1.00 19.20 C ANISOU 2322 CZ PHE A 460 1781 2908 2605 103 -37 -1079 C ATOM 2323 N LEU A 461 37.793 39.634 13.586 1.00 27.58 N ANISOU 2323 N LEU A 461 2958 3651 3869 288 126 -1365 N ATOM 2324 CA LEU A 461 37.654 40.602 12.502 1.00 22.89 C ANISOU 2324 CA LEU A 461 2384 2978 3335 324 145 -1415 C ATOM 2325 C LEU A 461 36.751 41.787 12.826 1.00 22.38 C ANISOU 2325 C LEU A 461 2278 2987 3238 318 166 -1477 C ATOM 2326 O LEU A 461 36.924 42.862 12.263 1.00 25.29 O ANISOU 2326 O LEU A 461 2635 3327 3649 319 160 -1494 O ATOM 2327 CB LEU A 461 37.134 39.917 11.234 1.00 23.17 C ANISOU 2327 CB LEU A 461 2454 2924 3426 325 129 -1347 C ATOM 2328 CG LEU A 461 38.101 38.984 10.514 1.00 25.43 C ANISOU 2328 CG LEU A 461 2780 3111 3769 328 101 -1275 C ATOM 2329 CD1 LEU A 461 37.370 38.076 9.538 1.00 17.99 C ANISOU 2329 CD1 LEU A 461 1869 2107 2860 325 92 -1211 C ATOM 2330 CD2 LEU A 461 39.175 39.812 9.806 1.00 21.25 C ANISOU 2330 CD2 LEU A 461 2250 2528 3297 327 84 -1267 C ATOM 2331 N HIS A 462 35.784 41.594 13.716 1.00 21.61 N ANISOU 2331 N HIS A 462 2158 2988 3065 311 192 -1510 N ATOM 2332 CA HIS A 462 34.773 42.625 13.934 1.00 21.33 C ANISOU 2332 CA HIS A 462 2085 3017 3004 305 210 -1564 C ATOM 2333 C HIS A 462 34.636 43.121 15.374 1.00 27.27 C ANISOU 2333 C HIS A 462 2793 3901 3669 292 237 -1631 C ATOM 2334 O HIS A 462 33.821 43.999 15.651 1.00 35.40 O ANISOU 2334 O HIS A 462 3788 4989 4675 286 253 -1678 O ATOM 2335 CB HIS A 462 33.415 42.151 13.431 1.00 17.37 C ANISOU 2335 CB HIS A 462 1591 2512 2497 304 217 -1540 C ATOM 2336 CG HIS A 462 33.397 41.818 11.974 1.00 26.52 C ANISOU 2336 CG HIS A 462 2789 3552 3737 312 193 -1478 C ATOM 2337 ND1 HIS A 462 33.236 42.774 10.995 1.00 25.48 N ANISOU 2337 ND1 HIS A 462 2654 3366 3660 315 183 -1479 N ATOM 2338 CD2 HIS A 462 33.504 40.633 11.330 1.00 26.24 C ANISOU 2338 CD2 HIS A 462 2793 3445 3731 316 178 -1412 C ATOM 2339 CE1 HIS A 462 33.257 42.193 9.808 1.00 23.14 C ANISOU 2339 CE1 HIS A 462 2393 2979 3419 317 163 -1415 C ATOM 2340 NE2 HIS A 462 33.417 40.895 9.985 1.00 27.97 N ANISOU 2340 NE2 HIS A 462 3032 3577 4020 318 159 -1374 N ATOM 2341 N ALA A 463 35.419 42.566 16.289 1.00 23.89 N ANISOU 2341 N ALA A 463 2345 3528 3203 258 210 -1588 N ATOM 2342 CA ALA A 463 35.345 43.009 17.676 1.00 26.37 C ANISOU 2342 CA ALA A 463 2605 3975 3439 226 215 -1620 C ATOM 2343 C ALA A 463 35.744 44.475 17.794 1.00 30.53 C ANISOU 2343 C ALA A 463 3119 4507 3974 257 250 -1729 C ATOM 2344 O ALA A 463 36.628 44.933 17.076 1.00 30.46 O ANISOU 2344 O ALA A 463 3134 4406 4032 283 245 -1742 O ATOM 2345 CB ALA A 463 36.224 42.156 18.563 1.00 19.39 C ANISOU 2345 CB ALA A 463 1707 3142 2519 186 178 -1552 C ATOM 2346 N PRO A 464 35.077 45.215 18.698 1.00 26.09 N ANISOU 2346 N PRO A 464 2511 4054 3349 240 273 -1788 N ATOM 2347 CA PRO A 464 35.487 46.569 19.102 1.00 30.67 C ANISOU 2347 CA PRO A 464 3063 4664 3928 251 294 -1875 C ATOM 2348 C PRO A 464 36.895 46.490 19.673 1.00 33.48 C ANISOU 2348 C PRO A 464 3419 5029 4274 248 284 -1880 C ATOM 2349 O PRO A 464 37.215 45.482 20.302 1.00 32.41 O ANISOU 2349 O PRO A 464 3273 4939 4102 210 249 -1802 O ATOM 2350 CB PRO A 464 34.515 46.919 20.234 1.00 23.99 C ANISOU 2350 CB PRO A 464 2167 3956 2993 225 319 -1921 C ATOM 2351 CG PRO A 464 33.416 45.953 20.139 1.00 32.82 C ANISOU 2351 CG PRO A 464 3285 5097 4088 200 304 -1852 C ATOM 2352 CD PRO A 464 33.945 44.712 19.490 1.00 27.07 C ANISOU 2352 CD PRO A 464 2597 4286 3401 197 267 -1755 C ATOM 2353 N LEU A 465 37.715 47.516 19.475 1.00 38.55 N ANISOU 2353 N LEU A 465 4050 5630 4966 257 277 -1914 N ATOM 2354 CA LEU A 465 39.131 47.421 19.845 1.00 45.34 C ANISOU 2354 CA LEU A 465 4916 6481 5829 259 266 -1916 C ATOM 2355 C LEU A 465 39.383 47.018 21.303 1.00 41.16 C ANISOU 2355 C LEU A 465 4352 6082 5206 224 263 -1916 C ATOM 2356 O LEU A 465 40.347 46.317 21.594 1.00 47.85 O ANISOU 2356 O LEU A 465 5204 6925 6053 207 230 -1860 O ATOM 2357 CB LEU A 465 39.887 48.706 19.493 1.00 50.99 C ANISOU 2357 CB LEU A 465 5614 7149 6609 266 259 -1952 C ATOM 2358 CG LEU A 465 39.881 49.046 17.999 1.00 56.91 C ANISOU 2358 CG LEU A 465 6391 7771 7460 281 240 -1912 C ATOM 2359 CD1 LEU A 465 40.945 50.075 17.666 1.00 58.22 C ANISOU 2359 CD1 LEU A 465 6548 7888 7685 286 231 -1934 C ATOM 2360 CD2 LEU A 465 40.076 47.794 17.160 1.00 57.48 C ANISOU 2360 CD2 LEU A 465 6516 7757 7568 292 219 -1833 C ATOM 2361 N GLU A 466 38.516 47.440 22.213 1.00 36.06 N ANISOU 2361 N GLU A 466 3660 5552 4491 197 280 -1953 N ATOM 2362 CA GLU A 466 38.686 47.092 23.620 1.00 43.02 C ANISOU 2362 CA GLU A 466 4493 6563 5288 146 260 -1927 C ATOM 2363 C GLU A 466 38.564 45.584 23.831 1.00 41.37 C ANISOU 2363 C GLU A 466 4290 6372 5055 109 217 -1808 C ATOM 2364 O GLU A 466 39.377 44.976 24.525 1.00 42.13 O ANISOU 2364 O GLU A 466 4374 6509 5123 81 185 -1757 O ATOM 2365 CB GLU A 466 37.670 47.828 24.487 1.00 56.20 C ANISOU 2365 CB GLU A 466 6113 8350 6889 126 290 -1989 C ATOM 2366 CG GLU A 466 37.979 47.772 25.976 1.00 77.20 C ANISOU 2366 CG GLU A 466 8721 11146 9464 78 276 -1986 C ATOM 2367 CD GLU A 466 36.863 48.361 26.831 1.00 90.26 C ANISOU 2367 CD GLU A 466 10326 12919 11048 53 303 -2038 C ATOM 2368 OE1 GLU A 466 35.781 47.737 26.917 1.00 92.63 O ANISOU 2368 OE1 GLU A 466 10620 13258 11317 30 297 -1993 O ATOM 2369 OE2 GLU A 466 37.076 49.441 27.426 1.00 91.51 O ANISOU 2369 OE2 GLU A 466 10453 13134 11182 55 331 -2126 O ATOM 2370 N LEU A 467 37.544 44.986 23.224 1.00 36.86 N ANISOU 2370 N LEU A 467 3738 5771 4497 109 215 -1764 N ATOM 2371 CA LEU A 467 37.351 43.544 23.292 1.00 31.35 C ANISOU 2371 CA LEU A 467 3050 5078 3784 77 176 -1652 C ATOM 2372 C LEU A 467 38.408 42.807 22.472 1.00 27.27 C ANISOU 2372 C LEU A 467 2580 4447 3336 96 148 -1590 C ATOM 2373 O LEU A 467 38.827 41.708 22.827 1.00 32.88 O ANISOU 2373 O LEU A 467 3291 5172 4030 66 111 -1502 O ATOM 2374 CB LEU A 467 35.952 43.163 22.807 1.00 33.50 C ANISOU 2374 CB LEU A 467 3329 5345 4054 74 185 -1628 C ATOM 2375 CG LEU A 467 34.842 43.056 23.848 1.00 51.35 C ANISOU 2375 CG LEU A 467 5543 7739 6229 30 190 -1624 C ATOM 2376 CD1 LEU A 467 34.701 44.347 24.653 1.00 58.05 C ANISOU 2376 CD1 LEU A 467 6348 8676 7033 30 224 -1726 C ATOM 2377 CD2 LEU A 467 33.522 42.698 23.169 1.00 54.10 C ANISOU 2377 CD2 LEU A 467 5905 8061 6590 35 200 -1603 C ATOM 2378 N LEU A 468 38.829 43.409 21.367 1.00 21.80 N ANISOU 2378 N LEU A 468 1925 3637 2720 145 166 -1637 N ATOM 2379 CA LEU A 468 39.869 42.811 20.534 1.00 23.03 C ANISOU 2379 CA LEU A 468 2127 3678 2947 166 143 -1588 C ATOM 2380 C LEU A 468 41.158 42.651 21.331 1.00 25.33 C ANISOU 2380 C LEU A 468 2402 4005 3218 148 119 -1570 C ATOM 2381 O LEU A 468 41.858 41.652 21.202 1.00 27.14 O ANISOU 2381 O LEU A 468 2651 4194 3468 137 84 -1490 O ATOM 2382 CB LEU A 468 40.127 43.663 19.290 1.00 21.35 C ANISOU 2382 CB LEU A 468 1955 3342 2816 223 172 -1654 C ATOM 2383 CG LEU A 468 41.268 43.205 18.383 1.00 23.23 C ANISOU 2383 CG LEU A 468 2241 3456 3131 249 152 -1616 C ATOM 2384 CD1 LEU A 468 41.069 41.763 17.962 1.00 21.86 C ANISOU 2384 CD1 LEU A 468 2093 3241 2974 230 118 -1507 C ATOM 2385 CD2 LEU A 468 41.363 44.108 17.177 1.00 28.07 C ANISOU 2385 CD2 LEU A 468 2891 3955 3819 304 184 -1686 C ATOM 2386 N ALA A 469 41.457 43.643 22.161 1.00 28.69 N ANISOU 2386 N ALA A 469 2790 4507 3603 144 137 -1647 N ATOM 2387 CA ALA A 469 42.651 43.618 23.000 1.00 27.23 C ANISOU 2387 CA ALA A 469 2585 4368 3394 127 117 -1641 C ATOM 2388 C ALA A 469 42.577 42.475 24.000 1.00 32.02 C ANISOU 2388 C ALA A 469 3164 5068 3933 74 78 -1549 C ATOM 2389 O ALA A 469 43.573 41.800 24.243 1.00 38.92 O ANISOU 2389 O ALA A 469 4043 5932 4812 61 45 -1492 O ATOM 2390 CB ALA A 469 42.819 44.950 23.722 1.00 23.13 C ANISOU 2390 CB ALA A 469 2028 3922 2839 131 148 -1747 C ATOM 2391 N GLU A 470 41.396 42.253 24.574 1.00 32.17 N ANISOU 2391 N GLU A 470 3154 5177 3890 42 83 -1534 N ATOM 2392 CA GLU A 470 41.185 41.126 25.487 1.00 31.91 C ANISOU 2392 CA GLU A 470 3098 5234 3793 -9 48 -1443 C ATOM 2393 C GLU A 470 41.309 39.782 24.783 1.00 27.38 C ANISOU 2393 C GLU A 470 2564 4578 3263 -12 15 -1336 C ATOM 2394 O GLU A 470 41.839 38.827 25.346 1.00 39.44 O ANISOU 2394 O GLU A 470 4084 6137 4765 -42 -21 -1255 O ATOM 2395 CB GLU A 470 39.814 41.211 26.153 1.00 33.83 C ANISOU 2395 CB GLU A 470 3305 5584 3965 -39 64 -1453 C ATOM 2396 CG GLU A 470 39.660 42.346 27.134 1.00 45.82 C ANISOU 2396 CG GLU A 470 4775 7211 5423 -50 91 -1544 C ATOM 2397 CD GLU A 470 38.258 42.410 27.704 1.00 57.18 C ANISOU 2397 CD GLU A 470 6181 8748 6798 -79 108 -1555 C ATOM 2398 OE1 GLU A 470 37.728 43.531 27.868 1.00 68.06 O ANISOU 2398 OE1 GLU A 470 7536 10164 8160 -68 145 -1647 O ATOM 2399 OE2 GLU A 470 37.677 41.335 27.970 1.00 52.44 O ANISOU 2399 OE2 GLU A 470 5577 8184 6164 -113 84 -1470 O ATOM 2400 N MET A 471 40.803 39.700 23.560 1.00 21.37 N ANISOU 2400 N MET A 471 1844 3712 2566 20 28 -1334 N ATOM 2401 CA MET A 471 40.945 38.473 22.777 1.00 21.71 C ANISOU 2401 CA MET A 471 1927 3665 2658 21 0 -1239 C ATOM 2402 C MET A 471 42.408 38.185 22.486 1.00 22.67 C ANISOU 2402 C MET A 471 2073 3711 2829 36 -24 -1212 C ATOM 2403 O MET A 471 42.871 37.060 22.661 1.00 32.31 O ANISOU 2403 O MET A 471 3302 4926 4050 13 -60 -1120 O ATOM 2404 CB MET A 471 40.155 38.556 21.472 1.00 21.49 C ANISOU 2404 CB MET A 471 1938 3535 2691 55 21 -1253 C ATOM 2405 CG MET A 471 38.643 38.613 21.671 1.00 23.09 C ANISOU 2405 CG MET A 471 2120 3806 2848 38 39 -1263 C ATOM 2406 SD MET A 471 37.738 38.915 20.142 1.00 29.98 S ANISOU 2406 SD MET A 471 3035 4563 3792 82 68 -1295 S ATOM 2407 CE MET A 471 38.118 37.421 19.227 1.00 23.91 C ANISOU 2407 CE MET A 471 2316 3685 3085 81 32 -1181 C ATOM 2408 N MET A 472 43.133 39.210 22.045 1.00 22.02 N ANISOU 2408 N MET A 472 2003 3572 2792 75 -3 -1292 N ATOM 2409 CA MET A 472 44.569 39.082 21.774 1.00 23.12 C ANISOU 2409 CA MET A 472 2164 3639 2980 92 -22 -1278 C ATOM 2410 C MET A 472 45.303 38.636 23.026 1.00 21.67 C ANISOU 2410 C MET A 472 1944 3553 2737 53 -53 -1236 C ATOM 2411 O MET A 472 46.102 37.709 22.985 1.00 24.10 O ANISOU 2411 O MET A 472 2267 3825 3066 44 -87 -1160 O ATOM 2412 CB MET A 472 45.149 40.411 21.293 1.00 21.19 C ANISOU 2412 CB MET A 472 1931 3340 2781 136 10 -1384 C ATOM 2413 CG MET A 472 44.701 40.810 19.895 1.00 19.88 C ANISOU 2413 CG MET A 472 1809 3054 2689 181 37 -1420 C ATOM 2414 SD MET A 472 45.368 39.677 18.660 1.00 29.22 S ANISOU 2414 SD MET A 472 3052 4089 3960 200 9 -1334 S ATOM 2415 CE MET A 472 45.050 40.562 17.129 1.00 20.20 C ANISOU 2415 CE MET A 472 1956 2816 2902 258 48 -1408 C ATOM 2416 N ASP A 473 45.009 39.301 24.141 1.00 23.22 N ANISOU 2416 N ASP A 473 2091 3873 2857 30 -41 -1287 N ATOM 2417 CA ASP A 473 45.679 39.025 25.404 1.00 28.15 C ANISOU 2417 CA ASP A 473 2677 4601 3418 -7 -67 -1258 C ATOM 2418 C ASP A 473 45.402 37.604 25.879 1.00 31.44 C ANISOU 2418 C ASP A 473 3087 5061 3797 -49 -105 -1141 C ATOM 2419 O ASP A 473 46.273 36.965 26.466 1.00 29.36 O ANISOU 2419 O ASP A 473 2814 4826 3517 -70 -139 -1084 O ATOM 2420 CB ASP A 473 45.253 40.030 26.481 1.00 45.75 C ANISOU 2420 CB ASP A 473 4853 6958 5570 -25 -43 -1338 C ATOM 2421 CG ASP A 473 45.737 41.456 26.193 1.00 60.15 C ANISOU 2421 CG ASP A 473 6678 8749 7426 13 -7 -1454 C ATOM 2422 OD1 ASP A 473 45.415 42.362 26.998 1.00 60.93 O ANISOU 2422 OD1 ASP A 473 6736 8945 7469 1 17 -1528 O ATOM 2423 OD2 ASP A 473 46.431 41.673 25.168 1.00 62.23 O ANISOU 2423 OD2 ASP A 473 6982 8891 7770 54 -1 -1473 O ATOM 2424 N GLU A 474 44.193 37.109 25.623 1.00 22.35 N ANISOU 2424 N GLU A 474 1942 3916 2635 -61 -100 -1106 N ATOM 2425 CA GLU A 474 43.843 35.762 26.042 1.00 23.49 C ANISOU 2425 CA GLU A 474 2081 4100 2744 -101 -133 -996 C ATOM 2426 C GLU A 474 44.664 34.719 25.285 1.00 23.86 C ANISOU 2426 C GLU A 474 2170 4037 2859 -90 -164 -912 C ATOM 2427 O GLU A 474 45.099 33.721 25.857 1.00 28.43 O ANISOU 2427 O GLU A 474 2741 4649 3413 -121 -200 -826 O ATOM 2428 CB GLU A 474 42.346 35.495 25.862 1.00 22.69 C ANISOU 2428 CB GLU A 474 1979 4023 2620 -115 -118 -982 C ATOM 2429 CG GLU A 474 41.993 34.020 25.970 1.00 25.74 C ANISOU 2429 CG GLU A 474 2373 4416 2993 -149 -150 -864 C ATOM 2430 CD GLU A 474 40.498 33.772 26.025 1.00 33.63 C ANISOU 2430 CD GLU A 474 3361 5463 3955 -170 -135 -852 C ATOM 2431 OE1 GLU A 474 39.741 34.748 26.229 1.00 29.91 O ANISOU 2431 OE1 GLU A 474 2868 5044 3453 -165 -103 -934 O ATOM 2432 OE2 GLU A 474 40.087 32.603 25.876 1.00 28.74 O ANISOU 2432 OE2 GLU A 474 2755 4829 3337 -191 -156 -761 O ATOM 2433 N ILE A 475 44.875 34.960 23.999 1.00 21.67 N ANISOU 2433 N ILE A 475 1938 3629 2667 -47 -150 -938 N ATOM 2434 CA ILE A 475 45.690 34.075 23.186 1.00 25.92 C ANISOU 2434 CA ILE A 475 2518 4053 3277 -32 -176 -868 C ATOM 2435 C ILE A 475 47.168 34.140 23.599 1.00 30.19 C ANISOU 2435 C ILE A 475 3053 4591 3828 -29 -198 -866 C ATOM 2436 O ILE A 475 47.816 33.115 23.786 1.00 27.80 O ANISOU 2436 O ILE A 475 2756 4277 3531 -46 -234 -780 O ATOM 2437 CB ILE A 475 45.546 34.411 21.700 1.00 20.55 C ANISOU 2437 CB ILE A 475 1888 3236 2685 14 -153 -905 C ATOM 2438 CG1 ILE A 475 44.093 34.233 21.270 1.00 20.79 C ANISOU 2438 CG1 ILE A 475 1925 3268 2707 10 -135 -898 C ATOM 2439 CG2 ILE A 475 46.490 33.545 20.863 1.00 20.70 C ANISOU 2439 CG2 ILE A 475 1949 3135 2780 30 -179 -838 C ATOM 2440 CD1 ILE A 475 43.559 32.831 21.516 1.00 23.82 C ANISOU 2440 CD1 ILE A 475 2307 3677 3065 -29 -163 -788 C ATOM 2441 N PHE A 476 47.692 35.350 23.755 1.00 28.06 N ANISOU 2441 N PHE A 476 2770 4333 3558 -7 -176 -961 N ATOM 2442 CA PHE A 476 49.109 35.522 24.061 1.00 28.52 C ANISOU 2442 CA PHE A 476 2824 4382 3632 1 -193 -970 C ATOM 2443 C PHE A 476 49.468 35.159 25.501 1.00 27.72 C ANISOU 2443 C PHE A 476 2675 4410 3447 -43 -221 -931 C ATOM 2444 O PHE A 476 50.602 34.789 25.782 1.00 22.84 O ANISOU 2444 O PHE A 476 2055 3784 2839 -47 -249 -896 O ATOM 2445 CB PHE A 476 49.551 36.965 23.779 1.00 22.91 C ANISOU 2445 CB PHE A 476 2114 3644 2948 38 -159 -1088 C ATOM 2446 CG PHE A 476 49.542 37.329 22.322 1.00 21.54 C ANISOU 2446 CG PHE A 476 1991 3328 2865 86 -135 -1125 C ATOM 2447 CD1 PHE A 476 50.269 36.588 21.406 1.00 20.03 C ANISOU 2447 CD1 PHE A 476 1844 3017 2749 104 -155 -1068 C ATOM 2448 CD2 PHE A 476 48.812 38.411 21.869 1.00 20.18 C ANISOU 2448 CD2 PHE A 476 1823 3142 2702 112 -93 -1215 C ATOM 2449 CE1 PHE A 476 50.272 36.918 20.061 1.00 20.41 C ANISOU 2449 CE1 PHE A 476 1939 2936 2879 147 -134 -1102 C ATOM 2450 CE2 PHE A 476 48.806 38.746 20.524 1.00 21.78 C ANISOU 2450 CE2 PHE A 476 2072 3215 2987 156 -72 -1248 C ATOM 2451 CZ PHE A 476 49.543 38.002 19.622 1.00 22.12 C ANISOU 2451 CZ PHE A 476 2159 3141 3104 173 -92 -1191 C ATOM 2452 N ASP A 477 48.505 35.259 26.411 1.00 27.93 N ANISOU 2452 N ASP A 477 2662 4557 3392 -77 -214 -936 N ATOM 2453 CA ASP A 477 48.834 35.205 27.829 1.00 34.08 C ANISOU 2453 CA ASP A 477 3392 5470 4088 -116 -233 -923 C ATOM 2454 C ASP A 477 47.691 34.697 28.706 1.00 36.22 C ANISOU 2454 C ASP A 477 3630 5857 4275 -161 -238 -879 C ATOM 2455 O ASP A 477 47.733 34.823 29.928 1.00 37.23 O ANISOU 2455 O ASP A 477 3712 6109 4323 -195 -246 -882 O ATOM 2456 CB ASP A 477 49.263 36.601 28.294 1.00 36.52 C ANISOU 2456 CB ASP A 477 3674 5829 4375 -102 -207 -1036 C ATOM 2457 CG ASP A 477 49.920 36.590 29.656 1.00 50.36 C ANISOU 2457 CG ASP A 477 5379 7702 6054 -136 -229 -1026 C ATOM 2458 OD1 ASP A 477 50.469 35.540 30.053 1.00 51.78 O ANISOU 2458 OD1 ASP A 477 5556 7897 6221 -159 -269 -933 O ATOM 2459 OD2 ASP A 477 49.881 37.640 30.333 1.00 58.92 O ANISOU 2459 OD2 ASP A 477 6427 8867 7092 -140 -206 -1111 O ATOM 2460 N GLY A 478 46.667 34.120 28.092 1.00 35.49 N ANISOU 2460 N GLY A 478 3560 5726 4200 -163 -232 -839 N ATOM 2461 CA GLY A 478 45.507 33.700 28.854 1.00 32.49 C ANISOU 2461 CA GLY A 478 3150 5451 3743 -204 -232 -804 C ATOM 2462 C GLY A 478 45.585 32.268 29.344 1.00 36.90 C ANISOU 2462 C GLY A 478 3706 6041 4274 -242 -273 -681 C ATOM 2463 O GLY A 478 44.771 31.851 30.153 1.00 46.85 O ANISOU 2463 O GLY A 478 4936 7401 5463 -282 -278 -645 O ATOM 2464 N TYR A 479 46.562 31.513 28.856 1.00 34.89 N ANISOU 2464 N TYR A 479 3481 5700 4077 -231 -302 -617 N ATOM 2465 CA TYR A 479 46.639 30.085 29.156 1.00 35.68 C ANISOU 2465 CA TYR A 479 3583 5811 4163 -262 -340 -495 C ATOM 2466 C TYR A 479 47.993 29.659 29.702 1.00 30.56 C ANISOU 2466 C TYR A 479 2925 5173 3512 -270 -376 -448 C ATOM 2467 O TYR A 479 49.027 30.207 29.328 1.00 36.97 O ANISOU 2467 O TYR A 479 3750 5925 4372 -239 -375 -493 O ATOM 2468 CB TYR A 479 46.322 29.265 27.907 1.00 28.15 C ANISOU 2468 CB TYR A 479 2680 4730 3287 -244 -342 -439 C ATOM 2469 CG TYR A 479 44.945 29.515 27.384 1.00 27.05 C ANISOU 2469 CG TYR A 479 2548 4582 3147 -240 -311 -471 C ATOM 2470 CD1 TYR A 479 43.868 28.774 27.847 1.00 28.52 C ANISOU 2470 CD1 TYR A 479 2719 4837 3280 -278 -316 -413 C ATOM 2471 CD2 TYR A 479 44.707 30.509 26.440 1.00 25.38 C ANISOU 2471 CD2 TYR A 479 2360 4296 2988 -199 -276 -562 C ATOM 2472 CE1 TYR A 479 42.593 29.006 27.379 1.00 26.77 C ANISOU 2472 CE1 TYR A 479 2504 4609 3058 -275 -287 -444 C ATOM 2473 CE2 TYR A 479 43.436 30.744 25.966 1.00 28.96 C ANISOU 2473 CE2 TYR A 479 2820 4743 3440 -194 -248 -591 C ATOM 2474 CZ TYR A 479 42.382 29.992 26.439 1.00 27.67 C ANISOU 2474 CZ TYR A 479 2640 4649 3224 -233 -254 -533 C ATOM 2475 OH TYR A 479 41.109 30.221 25.969 1.00 27.71 O ANISOU 2475 OH TYR A 479 2650 4649 3228 -228 -226 -562 O ATOM 2476 N ILE A 480 47.979 28.670 30.586 1.00 32.55 N ANISOU 2476 N ILE A 480 3156 5503 3709 -312 -408 -357 N ATOM 2477 CA ILE A 480 49.217 28.126 31.118 1.00 32.65 C ANISOU 2477 CA ILE A 480 3160 5527 3718 -321 -446 -300 C ATOM 2478 C ILE A 480 49.810 27.103 30.138 1.00 33.18 C ANISOU 2478 C ILE A 480 3273 5463 3871 -303 -468 -220 C ATOM 2479 O ILE A 480 49.112 26.200 29.667 1.00 31.84 O ANISOU 2479 O ILE A 480 3126 5252 3721 -313 -472 -152 O ATOM 2480 CB ILE A 480 49.006 27.499 32.521 1.00 54.61 C ANISOU 2480 CB ILE A 480 5897 8451 6403 -373 -471 -234 C ATOM 2481 CG1 ILE A 480 48.723 28.587 33.569 1.00 60.76 C ANISOU 2481 CG1 ILE A 480 6627 9360 7097 -390 -452 -320 C ATOM 2482 CG2 ILE A 480 50.241 26.706 32.947 1.00 47.34 C ANISOU 2482 CG2 ILE A 480 4973 7528 5487 -382 -514 -155 C ATOM 2483 CD1 ILE A 480 47.477 29.427 33.326 1.00 62.17 C ANISOU 2483 CD1 ILE A 480 6801 9560 7260 -384 -409 -401 C ATOM 2484 N PRO A 481 51.101 27.264 29.810 1.00 31.10 N ANISOU 2484 N PRO A 481 3024 5132 3661 -276 -482 -231 N ATOM 2485 CA PRO A 481 51.824 26.376 28.892 1.00 31.44 C ANISOU 2485 CA PRO A 481 3109 5047 3789 -257 -503 -162 C ATOM 2486 C PRO A 481 51.808 24.937 29.396 1.00 36.87 C ANISOU 2486 C PRO A 481 3792 5765 4452 -293 -541 -34 C ATOM 2487 O PRO A 481 51.618 24.722 30.597 1.00 29.34 O ANISOU 2487 O PRO A 481 2798 4937 3414 -331 -556 -3 O ATOM 2488 CB PRO A 481 53.265 26.915 28.935 1.00 27.20 C ANISOU 2488 CB PRO A 481 2571 4482 3283 -233 -514 -201 C ATOM 2489 CG PRO A 481 53.147 28.314 29.417 1.00 30.03 C ANISOU 2489 CG PRO A 481 2899 4913 3597 -225 -485 -315 C ATOM 2490 CD PRO A 481 51.961 28.340 30.335 1.00 36.17 C ANISOU 2490 CD PRO A 481 3640 5819 4283 -264 -476 -313 C ATOM 2491 N HIS A 482 52.011 23.971 28.502 1.00 34.98 N ANISOU 2491 N HIS A 482 3593 5413 4285 -282 -555 38 N ATOM 2492 CA HIS A 482 52.083 22.578 28.922 1.00 43.38 C ANISOU 2492 CA HIS A 482 4654 6496 5334 -315 -590 161 C ATOM 2493 C HIS A 482 53.215 22.395 29.920 1.00 41.12 C ANISOU 2493 C HIS A 482 4337 6276 5010 -329 -624 195 C ATOM 2494 O HIS A 482 54.352 22.772 29.651 1.00 36.33 O ANISOU 2494 O HIS A 482 3739 5615 4449 -302 -632 165 O ATOM 2495 CB HIS A 482 52.277 21.630 27.739 1.00 47.23 C ANISOU 2495 CB HIS A 482 5191 6842 5914 -297 -599 227 C ATOM 2496 CG HIS A 482 52.297 20.189 28.139 1.00 56.73 C ANISOU 2496 CG HIS A 482 6392 8060 7104 -330 -632 354 C ATOM 2497 ND1 HIS A 482 51.155 19.420 28.202 1.00 58.63 N ANISOU 2497 ND1 HIS A 482 6634 8327 7318 -358 -629 413 N ATOM 2498 CD2 HIS A 482 53.315 19.387 28.532 1.00 60.04 C ANISOU 2498 CD2 HIS A 482 6807 8475 7532 -339 -670 433 C ATOM 2499 CE1 HIS A 482 51.470 18.201 28.601 1.00 63.89 C ANISOU 2499 CE1 HIS A 482 7297 9001 7977 -384 -662 523 C ATOM 2500 NE2 HIS A 482 52.775 18.155 28.808 1.00 66.47 N ANISOU 2500 NE2 HIS A 482 7620 9310 8326 -372 -688 538 N ATOM 2501 N PRO A 483 52.900 21.811 31.080 1.00 43.37 N ANISOU 2501 N PRO A 483 4587 6679 5213 -372 -645 258 N ATOM 2502 CA PRO A 483 53.831 21.664 32.205 1.00 41.94 C ANISOU 2502 CA PRO A 483 4369 6586 4980 -392 -677 291 C ATOM 2503 C PRO A 483 55.116 20.926 31.827 1.00 42.37 C ANISOU 2503 C PRO A 483 4446 6553 5101 -376 -710 356 C ATOM 2504 O PRO A 483 56.136 21.072 32.497 1.00 37.90 O ANISOU 2504 O PRO A 483 3855 6031 4513 -378 -734 358 O ATOM 2505 CB PRO A 483 53.017 20.842 33.214 1.00 39.09 C ANISOU 2505 CB PRO A 483 3979 6338 4534 -442 -693 371 C ATOM 2506 CG PRO A 483 51.915 20.203 32.379 1.00 44.75 C ANISOU 2506 CG PRO A 483 4728 6987 5286 -444 -676 408 C ATOM 2507 CD PRO A 483 51.571 21.272 31.407 1.00 42.54 C ANISOU 2507 CD PRO A 483 4471 6636 5055 -407 -637 301 C ATOM 2508 N ASP A 484 55.062 20.143 30.757 1.00 49.44 N ANISOU 2508 N ASP A 484 5384 7324 6076 -361 -712 409 N ATOM 2509 CA ASP A 484 56.200 19.323 30.362 1.00 52.23 C ANISOU 2509 CA ASP A 484 5760 7590 6496 -348 -743 480 C ATOM 2510 C ASP A 484 56.979 19.901 29.182 1.00 45.35 C ANISOU 2510 C ASP A 484 4926 6585 5721 -299 -729 417 C ATOM 2511 O ASP A 484 58.190 20.070 29.271 1.00 43.33 O ANISOU 2511 O ASP A 484 4666 6307 5490 -283 -747 409 O ATOM 2512 CB ASP A 484 55.745 17.891 30.061 1.00 60.46 C ANISOU 2512 CB ASP A 484 6823 8587 7562 -367 -759 597 C ATOM 2513 CG ASP A 484 55.139 17.202 31.279 1.00 67.42 C ANISOU 2513 CG ASP A 484 7668 9598 8351 -416 -778 671 C ATOM 2514 OD1 ASP A 484 55.601 17.465 32.415 1.00 61.34 O ANISOU 2514 OD1 ASP A 484 6857 8938 7510 -434 -796 669 O ATOM 2515 OD2 ASP A 484 54.200 16.397 31.098 1.00 72.62 O ANISOU 2515 OD2 ASP A 484 8338 10248 9005 -436 -774 732 O ATOM 2516 N THR A 485 56.286 20.209 28.087 1.00 41.00 N ANISOU 2516 N THR A 485 4409 5946 5222 -277 -697 372 N ATOM 2517 CA THR A 485 56.940 20.693 26.869 1.00 37.14 C ANISOU 2517 CA THR A 485 3961 5323 4829 -231 -682 317 C ATOM 2518 C THR A 485 57.105 22.207 26.811 1.00 36.65 C ANISOU 2518 C THR A 485 3890 5277 4761 -205 -653 188 C ATOM 2519 O THR A 485 58.061 22.709 26.227 1.00 30.38 O ANISOU 2519 O THR A 485 3114 4403 4027 -171 -650 141 O ATOM 2520 CB THR A 485 56.174 20.269 25.610 1.00 37.10 C ANISOU 2520 CB THR A 485 4001 5205 4891 -217 -662 332 C ATOM 2521 OG1 THR A 485 54.836 20.778 25.677 1.00 33.20 O ANISOU 2521 OG1 THR A 485 3499 4766 4351 -227 -632 284 O ATOM 2522 CG2 THR A 485 56.149 18.745 25.482 1.00 39.09 C ANISOU 2522 CG2 THR A 485 4269 5417 5167 -238 -690 457 C ATOM 2523 N GLY A 486 56.164 22.934 27.401 1.00 38.97 N ANISOU 2523 N GLY A 486 4156 5670 4983 -220 -630 131 N ATOM 2524 CA GLY A 486 56.197 24.382 27.358 1.00 32.25 C ANISOU 2524 CA GLY A 486 3295 4837 4123 -196 -598 7 C ATOM 2525 C GLY A 486 55.463 24.964 26.162 1.00 31.83 C ANISOU 2525 C GLY A 486 3278 4692 4125 -165 -559 -58 C ATOM 2526 O GLY A 486 55.584 26.158 25.879 1.00 29.20 O ANISOU 2526 O GLY A 486 2945 4344 3804 -138 -531 -162 O ATOM 2527 N LYS A 487 54.714 24.122 25.452 1.00 33.29 N ANISOU 2527 N LYS A 487 3492 4814 4344 -169 -558 1 N ATOM 2528 CA LYS A 487 53.821 24.587 24.390 1.00 35.63 C ANISOU 2528 CA LYS A 487 3820 5037 4682 -145 -521 -54 C ATOM 2529 C LYS A 487 52.736 25.487 24.962 1.00 35.35 C ANISOU 2529 C LYS A 487 3754 5104 4573 -157 -492 -126 C ATOM 2530 O LYS A 487 52.067 25.117 25.920 1.00 33.28 O ANISOU 2530 O LYS A 487 3458 4952 4233 -196 -501 -87 O ATOM 2531 CB LYS A 487 53.127 23.406 23.714 1.00 43.33 C ANISOU 2531 CB LYS A 487 4825 5946 5691 -156 -528 33 C ATOM 2532 CG LYS A 487 53.935 22.695 22.656 1.00 48.98 C ANISOU 2532 CG LYS A 487 5585 6520 6503 -133 -542 82 C ATOM 2533 CD LYS A 487 53.051 21.689 21.935 1.00 47.02 C ANISOU 2533 CD LYS A 487 5367 6212 6288 -143 -540 151 C ATOM 2534 CE LYS A 487 53.785 21.026 20.792 1.00 47.68 C ANISOU 2534 CE LYS A 487 5496 6149 6470 -118 -550 193 C ATOM 2535 NZ LYS A 487 53.023 19.859 20.278 1.00 48.81 N ANISOU 2535 NZ LYS A 487 5662 6246 6637 -135 -555 277 N ATOM 2536 N ASP A 488 52.548 26.659 24.369 1.00 33.65 N ANISOU 2536 N ASP A 488 3548 4168 5072 -473 -163 -62 N ATOM 2537 CA ASP A 488 51.487 27.554 24.807 1.00 23.42 C ANISOU 2537 CA ASP A 488 2284 2869 3744 -466 -173 -97 C ATOM 2538 C ASP A 488 50.317 27.549 23.827 1.00 26.95 C ANISOU 2538 C ASP A 488 2744 3313 4181 -393 -185 -161 C ATOM 2539 O ASP A 488 50.305 26.783 22.857 1.00 26.38 O ANISOU 2539 O ASP A 488 2653 3241 4130 -350 -187 -177 O ATOM 2540 CB ASP A 488 52.012 28.979 25.044 1.00 28.00 C ANISOU 2540 CB ASP A 488 2922 3440 4275 -488 -163 -70 C ATOM 2541 CG ASP A 488 52.684 29.584 23.822 1.00 34.71 C ANISOU 2541 CG ASP A 488 3815 4278 5093 -452 -153 -58 C ATOM 2542 OD1 ASP A 488 52.438 29.113 22.689 1.00 31.69 O ANISOU 2542 OD1 ASP A 488 3429 3894 4717 -396 -156 -86 O ATOM 2543 OD2 ASP A 488 53.461 30.549 24.006 1.00 32.25 O ANISOU 2543 OD2 ASP A 488 3543 3960 4750 -480 -142 -22 O ATOM 2544 N ALA A 489 49.337 28.402 24.090 1.00 22.88 N ANISOU 2544 N ALA A 489 2262 2796 3635 -379 -195 -197 N ATOM 2545 CA ALA A 489 48.157 28.505 23.249 1.00 25.68 C ANISOU 2545 CA ALA A 489 2633 3148 3978 -311 -208 -260 C ATOM 2546 C ALA A 489 48.550 28.727 21.793 1.00 29.46 C ANISOU 2546 C ALA A 489 3143 3616 4436 -256 -202 -265 C ATOM 2547 O ALA A 489 48.136 27.990 20.905 1.00 32.23 O ANISOU 2547 O ALA A 489 3473 3968 4805 -206 -208 -298 O ATOM 2548 CB ALA A 489 47.282 29.632 23.735 1.00 21.13 C ANISOU 2548 CB ALA A 489 2097 2569 3362 -308 -217 -290 C ATOM 2549 N LEU A 490 49.370 29.739 21.566 1.00 29.84 N ANISOU 2549 N LEU A 490 3240 3653 4445 -266 -191 -230 N ATOM 2550 CA LEU A 490 49.823 30.087 20.233 1.00 28.42 C ANISOU 2550 CA LEU A 490 3096 3464 4240 -218 -184 -229 C ATOM 2551 C LEU A 490 50.488 28.899 19.525 1.00 28.97 C ANISOU 2551 C LEU A 490 3121 3540 4347 -205 -177 -215 C ATOM 2552 O LEU A 490 50.283 28.691 18.330 1.00 29.02 O ANISOU 2552 O LEU A 490 3134 3544 4348 -145 -180 -242 O ATOM 2553 CB LEU A 490 50.781 31.263 20.337 1.00 31.91 C ANISOU 2553 CB LEU A 490 3589 3895 4641 -249 -170 -183 C ATOM 2554 CG LEU A 490 51.059 32.065 19.078 1.00 39.18 C ANISOU 2554 CG LEU A 490 4565 4803 5518 -201 -165 -185 C ATOM 2555 CD1 LEU A 490 49.752 32.528 18.442 1.00 25.36 C ANISOU 2555 CD1 LEU A 490 2847 3046 3743 -137 -182 -248 C ATOM 2556 CD2 LEU A 490 51.950 33.251 19.426 1.00 41.14 C ANISOU 2556 CD2 LEU A 490 4862 5040 5729 -243 -153 -137 C ATOM 2557 N ASP A 491 51.277 28.122 20.266 1.00 20.04 N ANISOU 2557 N ASP A 491 1944 2417 3253 -258 -170 -173 N ATOM 2558 CA ASP A 491 51.919 26.925 19.723 1.00 20.24 C ANISOU 2558 CA ASP A 491 1922 2449 3318 -250 -166 -159 C ATOM 2559 C ASP A 491 50.869 25.924 19.263 1.00 31.42 C ANISOU 2559 C ASP A 491 3301 3871 4768 -202 -182 -213 C ATOM 2560 O ASP A 491 50.980 25.340 18.182 1.00 33.71 O ANISOU 2560 O ASP A 491 3579 4162 5069 -155 -183 -229 O ATOM 2561 CB ASP A 491 52.796 26.242 20.773 1.00 30.31 C ANISOU 2561 CB ASP A 491 3153 3732 4630 -319 -159 -109 C ATOM 2562 CG ASP A 491 54.159 26.885 20.918 1.00 48.35 C ANISOU 2562 CG ASP A 491 5463 6015 6893 -361 -141 -49 C ATOM 2563 OD1 ASP A 491 54.729 27.323 19.891 1.00 52.92 O ANISOU 2563 OD1 ASP A 491 6073 6589 7445 -331 -132 -41 O ATOM 2564 OD2 ASP A 491 54.664 26.930 22.068 1.00 48.42 O ANISOU 2564 OD2 ASP A 491 5458 6027 6912 -424 -136 -12 O ATOM 2565 N ILE A 492 49.863 25.702 20.102 1.00 25.39 N ANISOU 2565 N ILE A 492 2517 3111 4020 -215 -195 -243 N ATOM 2566 CA ILE A 492 48.835 24.739 19.764 1.00 22.52 C ANISOU 2566 CA ILE A 492 2115 2752 3689 -174 -210 -295 C ATOM 2567 C ILE A 492 48.110 25.193 18.503 1.00 22.24 C ANISOU 2567 C ILE A 492 2115 2711 3624 -97 -216 -345 C ATOM 2568 O ILE A 492 47.947 24.424 17.563 1.00 27.14 O ANISOU 2568 O ILE A 492 2714 3333 4265 -49 -221 -370 O ATOM 2569 CB ILE A 492 47.803 24.563 20.887 1.00 22.07 C ANISOU 2569 CB ILE A 492 2035 2703 3649 -201 -222 -320 C ATOM 2570 CG1 ILE A 492 48.467 24.005 22.145 1.00 26.05 C ANISOU 2570 CG1 ILE A 492 2498 3213 4185 -276 -217 -271 C ATOM 2571 CG2 ILE A 492 46.690 23.640 20.419 1.00 21.67 C ANISOU 2571 CG2 ILE A 492 1949 2657 3629 -154 -238 -378 C ATOM 2572 CD1 ILE A 492 49.254 22.749 21.896 1.00 29.07 C ANISOU 2572 CD1 ILE A 492 2832 3599 4616 -285 -215 -245 C ATOM 2573 N MET A 493 47.694 26.454 18.486 1.00 24.18 N ANISOU 2573 N MET A 493 2417 2949 3820 -85 -217 -359 N ATOM 2574 CA MET A 493 46.829 26.958 17.425 1.00 22.16 C ANISOU 2574 CA MET A 493 2199 2688 3534 -12 -225 -412 C ATOM 2575 C MET A 493 47.524 27.054 16.073 1.00 26.88 C ANISOU 2575 C MET A 493 2820 3281 4114 32 -217 -403 C ATOM 2576 O MET A 493 46.933 26.690 15.057 1.00 31.78 O ANISOU 2576 O MET A 493 3437 3901 4737 96 -225 -446 O ATOM 2577 CB MET A 493 46.224 28.303 17.811 1.00 22.66 C ANISOU 2577 CB MET A 493 2319 2744 3549 -13 -230 -429 C ATOM 2578 CG MET A 493 45.239 28.221 18.959 1.00 19.96 C ANISOU 2578 CG MET A 493 1954 2409 3219 -40 -242 -455 C ATOM 2579 SD MET A 493 44.905 29.864 19.609 1.00 32.91 S ANISOU 2579 SD MET A 493 3660 4041 4804 -57 -245 -457 S ATOM 2580 CE MET A 493 44.165 30.635 18.170 1.00 27.57 C ANISOU 2580 CE MET A 493 3040 3352 4082 31 -254 -511 C ATOM 2581 N MET A 494 48.774 27.520 16.063 1.00 21.65 N ANISOU 2581 N MET A 494 2179 2614 3434 -1 -200 -346 N ATOM 2582 CA MET A 494 49.522 27.668 14.817 1.00 24.46 C ANISOU 2582 CA MET A 494 2557 2967 3769 36 -190 -332 C ATOM 2583 C MET A 494 49.575 26.372 14.020 1.00 28.87 C ANISOU 2583 C MET A 494 3065 3535 4368 73 -193 -350 C ATOM 2584 O MET A 494 49.659 26.394 12.796 1.00 29.94 O ANISOU 2584 O MET A 494 3217 3671 4489 128 -192 -365 O ATOM 2585 CB MET A 494 50.955 28.125 15.084 1.00 26.38 C ANISOU 2585 CB MET A 494 2817 3209 3998 -16 -171 -264 C ATOM 2586 CG MET A 494 51.089 29.576 15.412 1.00 25.35 C ANISOU 2586 CG MET A 494 2749 3066 3816 -37 -165 -246 C ATOM 2587 SD MET A 494 52.803 30.103 15.398 1.00 36.46 S ANISOU 2587 SD MET A 494 4178 4471 5203 -85 -142 -170 S ATOM 2588 CE MET A 494 53.595 28.902 16.470 1.00 23.34 C ANISOU 2588 CE MET A 494 2445 2824 3600 -152 -136 -129 C ATOM 2589 N PHE A 495 49.532 25.245 14.717 1.00 25.48 N ANISOU 2589 N PHE A 495 2576 3115 3992 43 -199 -347 N ATOM 2590 CA PHE A 495 49.742 23.960 14.072 1.00 32.78 C ANISOU 2590 CA PHE A 495 3449 4047 4960 69 -202 -356 C ATOM 2591 C PHE A 495 48.488 23.101 14.074 1.00 30.97 C ANISOU 2591 C PHE A 495 3181 3821 4766 102 -221 -414 C ATOM 2592 O PHE A 495 48.520 21.948 13.648 1.00 33.89 O ANISOU 2592 O PHE A 495 3502 4196 5177 123 -227 -426 O ATOM 2593 CB PHE A 495 50.910 23.206 14.729 1.00 28.64 C ANISOU 2593 CB PHE A 495 2880 3528 4472 10 -193 -300 C ATOM 2594 CG PHE A 495 52.255 23.811 14.441 1.00 27.55 C ANISOU 2594 CG PHE A 495 2771 3390 4305 -12 -174 -247 C ATOM 2595 CD1 PHE A 495 52.858 23.628 13.209 1.00 29.22 C ANISOU 2595 CD1 PHE A 495 2986 3606 4509 30 -167 -244 C ATOM 2596 CD2 PHE A 495 52.913 24.564 15.396 1.00 27.25 C ANISOU 2596 CD2 PHE A 495 2755 3349 4249 -75 -162 -199 C ATOM 2597 CE1 PHE A 495 54.093 24.189 12.933 1.00 25.14 C ANISOU 2597 CE1 PHE A 495 2496 3092 3965 8 -149 -195 C ATOM 2598 CE2 PHE A 495 54.144 25.122 15.128 1.00 30.60 C ANISOU 2598 CE2 PHE A 495 3205 3774 4647 -97 -145 -151 C ATOM 2599 CZ PHE A 495 54.735 24.941 13.891 1.00 27.58 C ANISOU 2599 CZ PHE A 495 2827 3397 4256 -55 -138 -148 C ATOM 2600 N HIS A 496 47.382 23.661 14.542 1.00 22.56 N ANISOU 2600 N HIS A 496 2136 2753 3684 108 -231 -450 N ATOM 2601 CA HIS A 496 46.136 22.899 14.611 1.00 18.89 C ANISOU 2601 CA HIS A 496 1636 2292 3251 136 -248 -506 C ATOM 2602 C HIS A 496 45.383 22.967 13.285 1.00 20.25 C ANISOU 2602 C HIS A 496 1826 2463 3406 220 -257 -563 C ATOM 2603 O HIS A 496 45.436 23.981 12.586 1.00 24.46 O ANISOU 2603 O HIS A 496 2415 2990 3890 253 -252 -567 O ATOM 2604 CB HIS A 496 45.273 23.410 15.756 1.00 17.06 C ANISOU 2604 CB HIS A 496 1412 2060 3010 103 -255 -522 C ATOM 2605 CG HIS A 496 44.117 22.521 16.088 1.00 24.21 C ANISOU 2605 CG HIS A 496 2272 2973 3954 115 -272 -570 C ATOM 2606 ND1 HIS A 496 42.880 22.660 15.499 1.00 22.15 N ANISOU 2606 ND1 HIS A 496 2023 2712 3682 174 -285 -636 N ATOM 2607 CD2 HIS A 496 44.009 21.493 16.964 1.00 18.74 C ANISOU 2607 CD2 HIS A 496 1522 2287 3311 73 -277 -562 C ATOM 2608 CE1 HIS A 496 42.058 21.750 15.993 1.00 27.19 C ANISOU 2608 CE1 HIS A 496 2611 3358 4361 168 -298 -667 C ATOM 2609 NE2 HIS A 496 42.721 21.027 16.879 1.00 26.96 N ANISOU 2609 NE2 HIS A 496 2540 3332 4369 106 -293 -622 N ATOM 2610 N GLN A 497 44.704 21.878 12.939 1.00 23.31 N ANISOU 2610 N GLN A 497 2167 2855 3834 253 -270 -604 N ATOM 2611 CA GLN A 497 44.024 21.758 11.654 1.00 21.77 C ANISOU 2611 CA GLN A 497 1980 2660 3630 334 -279 -659 C ATOM 2612 C GLN A 497 43.002 22.868 11.449 1.00 19.47 C ANISOU 2612 C GLN A 497 1743 2364 3291 371 -286 -703 C ATOM 2613 O GLN A 497 42.771 23.296 10.325 1.00 24.98 O ANISOU 2613 O GLN A 497 2473 3059 3958 434 -288 -731 O ATOM 2614 CB GLN A 497 43.351 20.382 11.512 1.00 15.91 C ANISOU 2614 CB GLN A 497 1175 1924 2944 357 -294 -699 C ATOM 2615 CG GLN A 497 42.230 20.155 12.504 1.00 29.88 C ANISOU 2615 CG GLN A 497 2922 3696 4734 335 -306 -731 C ATOM 2616 CD GLN A 497 41.694 18.734 12.499 1.00 34.89 C ANISOU 2616 CD GLN A 497 3491 4336 5430 345 -320 -762 C ATOM 2617 OE1 GLN A 497 41.496 18.133 11.445 1.00 34.85 O ANISOU 2617 OE1 GLN A 497 3470 4332 5439 403 -327 -795 O ATOM 2618 NE2 GLN A 497 41.445 18.196 13.686 1.00 37.61 N ANISOU 2618 NE2 GLN A 497 3797 4684 5808 290 -325 -751 N ATOM 2619 N PHE A 498 42.397 23.335 12.537 1.00 19.45 N ANISOU 2619 N PHE A 498 1748 2361 3281 334 -290 -709 N ATOM 2620 CA PHE A 498 41.465 24.455 12.465 1.00 18.54 C ANISOU 2620 CA PHE A 498 1684 2241 3119 364 -298 -748 C ATOM 2621 C PHE A 498 42.051 25.736 13.072 1.00 25.28 C ANISOU 2621 C PHE A 498 2591 3086 3927 321 -287 -705 C ATOM 2622 O PHE A 498 41.835 26.838 12.556 1.00 16.91 O ANISOU 2622 O PHE A 498 1590 2018 2817 354 -288 -719 O ATOM 2623 CB PHE A 498 40.131 24.107 13.140 1.00 20.93 C ANISOU 2623 CB PHE A 498 1959 2551 3443 365 -314 -800 C ATOM 2624 CG PHE A 498 39.516 22.825 12.643 1.00 26.95 C ANISOU 2624 CG PHE A 498 2666 3321 4253 402 -325 -843 C ATOM 2625 CD1 PHE A 498 39.467 22.541 11.285 1.00 30.49 C ANISOU 2625 CD1 PHE A 498 3119 3767 4699 471 -328 -871 C ATOM 2626 CD2 PHE A 498 38.986 21.903 13.531 1.00 23.04 C ANISOU 2626 CD2 PHE A 498 2115 2833 3804 368 -333 -855 C ATOM 2627 CE1 PHE A 498 38.905 21.352 10.822 1.00 26.48 C ANISOU 2627 CE1 PHE A 498 2560 3266 4236 506 -340 -912 C ATOM 2628 CE2 PHE A 498 38.421 20.722 13.076 1.00 22.57 C ANISOU 2628 CE2 PHE A 498 2006 2780 3790 401 -344 -894 C ATOM 2629 CZ PHE A 498 38.385 20.445 11.718 1.00 21.17 C ANISOU 2629 CZ PHE A 498 1832 2600 3610 470 -348 -923 C ATOM 2630 N GLY A 499 42.796 25.589 14.165 1.00 25.25 N ANISOU 2630 N GLY A 499 2567 3085 3942 247 -278 -652 N ATOM 2631 CA GLY A 499 43.307 26.741 14.882 1.00 17.34 C ANISOU 2631 CA GLY A 499 1610 2077 2902 201 -269 -613 C ATOM 2632 C GLY A 499 44.246 27.591 14.044 1.00 23.48 C ANISOU 2632 C GLY A 499 2440 2843 3637 217 -256 -579 C ATOM 2633 O GLY A 499 44.399 28.785 14.300 1.00 24.18 O ANISOU 2633 O GLY A 499 2582 2923 3683 202 -252 -563 O ATOM 2634 N ASN A 500 44.885 26.990 13.044 1.00 17.98 N ANISOU 2634 N ASN A 500 1730 2150 2954 247 -249 -569 N ATOM 2635 CA ASN A 500 45.860 27.744 12.261 1.00 18.14 C ANISOU 2635 CA ASN A 500 1796 2162 2935 257 -235 -533 C ATOM 2636 C ASN A 500 45.216 28.906 11.499 1.00 17.22 C ANISOU 2636 C ASN A 500 1746 2034 2763 311 -242 -567 C ATOM 2637 O ASN A 500 45.851 29.932 11.260 1.00 16.44 O ANISOU 2637 O ASN A 500 1699 1925 2620 304 -232 -536 O ATOM 2638 CB ASN A 500 46.649 26.841 11.315 1.00 18.17 C ANISOU 2638 CB ASN A 500 1769 2173 2963 280 -228 -518 C ATOM 2639 CG ASN A 500 45.851 26.443 10.084 1.00 20.89 C ANISOU 2639 CG ASN A 500 2110 2520 3307 362 -239 -576 C ATOM 2640 OD1 ASN A 500 45.915 27.106 9.054 1.00 21.67 O ANISOU 2640 OD1 ASN A 500 2254 2614 3367 409 -236 -585 O ATOM 2641 ND2 ASN A 500 45.092 25.361 10.191 1.00 17.05 N ANISOU 2641 ND2 ASN A 500 1571 2041 2867 378 -252 -615 N ATOM 2642 N TYR A 501 43.949 28.750 11.136 1.00 16.84 N ANISOU 2642 N TYR A 501 1695 1988 2716 365 -259 -632 N ATOM 2643 CA TYR A 501 43.254 29.813 10.423 1.00 17.10 C ANISOU 2643 CA TYR A 501 1789 2010 2698 420 -267 -670 C ATOM 2644 C TYR A 501 42.977 31.017 11.315 1.00 23.85 C ANISOU 2644 C TYR A 501 2690 2855 3517 387 -271 -663 C ATOM 2645 O TYR A 501 42.867 32.143 10.834 1.00 26.23 O ANISOU 2645 O TYR A 501 3054 3143 3768 414 -273 -669 O ATOM 2646 CB TYR A 501 41.957 29.297 9.834 1.00 17.37 C ANISOU 2646 CB TYR A 501 1806 2050 2745 486 -285 -743 C ATOM 2647 CG TYR A 501 42.173 28.270 8.758 1.00 16.97 C ANISOU 2647 CG TYR A 501 1720 2008 2722 531 -283 -756 C ATOM 2648 CD1 TYR A 501 42.050 26.914 9.035 1.00 16.46 C ANISOU 2648 CD1 TYR A 501 1584 1954 2715 520 -287 -765 C ATOM 2649 CD2 TYR A 501 42.493 28.654 7.464 1.00 18.50 C ANISOU 2649 CD2 TYR A 501 1950 2197 2882 585 -279 -758 C ATOM 2650 CE1 TYR A 501 42.238 25.974 8.057 1.00 19.67 C ANISOU 2650 CE1 TYR A 501 1958 2369 3148 562 -287 -779 C ATOM 2651 CE2 TYR A 501 42.683 27.715 6.472 1.00 17.27 C ANISOU 2651 CE2 TYR A 501 1761 2051 2751 628 -278 -771 C ATOM 2652 CZ TYR A 501 42.559 26.375 6.777 1.00 24.49 C ANISOU 2652 CZ TYR A 501 2604 2976 3724 617 -282 -782 C ATOM 2653 OH TYR A 501 42.747 25.427 5.802 1.00 29.00 O ANISOU 2653 OH TYR A 501 3141 3557 4321 660 -283 -796 O ATOM 2654 N VAL A 502 42.873 30.771 12.617 1.00 21.07 N ANISOU 2654 N VAL A 502 2306 2509 3191 328 -272 -651 N ATOM 2655 CA VAL A 502 42.583 31.833 13.558 1.00 21.03 C ANISOU 2655 CA VAL A 502 2339 2497 3156 294 -276 -647 C ATOM 2656 C VAL A 502 43.808 32.712 13.756 1.00 23.70 C ANISOU 2656 C VAL A 502 2717 2823 3464 249 -260 -582 C ATOM 2657 O VAL A 502 43.714 33.937 13.746 1.00 25.53 O ANISOU 2657 O VAL A 502 3010 3042 3650 254 -263 -581 O ATOM 2658 CB VAL A 502 42.117 31.271 14.891 1.00 19.64 C ANISOU 2658 CB VAL A 502 2114 2332 3016 243 -282 -652 C ATOM 2659 CG1 VAL A 502 41.817 32.402 15.857 1.00 16.22 C ANISOU 2659 CG1 VAL A 502 1719 1894 2550 210 -287 -650 C ATOM 2660 CG2 VAL A 502 40.890 30.394 14.667 1.00 16.18 C ANISOU 2660 CG2 VAL A 502 1635 1906 2608 287 -298 -717 C ATOM 2661 N VAL A 503 44.960 32.077 13.926 1.00 20.74 N ANISOU 2661 N VAL A 503 2309 2453 3116 207 -244 -528 N ATOM 2662 CA VAL A 503 46.224 32.795 14.038 1.00 18.71 C ANISOU 2662 CA VAL A 503 2086 2189 2835 164 -227 -464 C ATOM 2663 C VAL A 503 46.555 33.543 12.741 1.00 24.62 C ANISOU 2663 C VAL A 503 2891 2925 3539 214 -222 -462 C ATOM 2664 O VAL A 503 47.082 34.652 12.770 1.00 26.17 O ANISOU 2664 O VAL A 503 3141 3108 3694 196 -216 -431 O ATOM 2665 CB VAL A 503 47.359 31.831 14.363 1.00 17.55 C ANISOU 2665 CB VAL A 503 1887 2052 2729 116 -211 -413 C ATOM 2666 CG1 VAL A 503 48.687 32.596 14.493 1.00 18.28 C ANISOU 2666 CG1 VAL A 503 2013 2136 2795 71 -193 -347 C ATOM 2667 CG2 VAL A 503 47.027 31.051 15.631 1.00 16.10 C ANISOU 2667 CG2 VAL A 503 1647 1879 2589 68 -216 -414 C ATOM 2668 N GLN A 504 46.243 32.921 11.611 1.00 24.09 N ANISOU 2668 N GLN A 504 2810 2863 3479 275 -225 -495 N ATOM 2669 CA GLN A 504 46.345 33.561 10.304 1.00 27.12 C ANISOU 2669 CA GLN A 504 3245 3237 3821 332 -224 -503 C ATOM 2670 C GLN A 504 45.525 34.847 10.304 1.00 27.79 C ANISOU 2670 C GLN A 504 3395 3306 3857 357 -237 -533 C ATOM 2671 O GLN A 504 45.972 35.907 9.866 1.00 25.47 O ANISOU 2671 O GLN A 504 3162 2998 3518 362 -232 -510 O ATOM 2672 CB GLN A 504 45.751 32.627 9.262 1.00 26.76 C ANISOU 2672 CB GLN A 504 3169 3203 3797 399 -231 -551 C ATOM 2673 CG GLN A 504 46.434 32.638 7.929 1.00 41.30 C ANISOU 2673 CG GLN A 504 5029 5045 5618 440 -221 -536 C ATOM 2674 CD GLN A 504 47.180 31.343 7.667 1.00 45.48 C ANISOU 2674 CD GLN A 504 5496 5591 6193 431 -211 -516 C ATOM 2675 OE1 GLN A 504 48.411 31.329 7.662 1.00 57.25 O ANISOU 2675 OE1 GLN A 504 6984 7085 7683 393 -193 -460 O ATOM 2676 NE2 GLN A 504 46.436 30.239 7.472 1.00 23.05 N ANISOU 2676 NE2 GLN A 504 2603 2761 3393 465 -222 -561 N ATOM 2677 N CYS A 505 44.299 34.721 10.787 1.00 20.70 N ANISOU 2677 N CYS A 505 2484 2411 2971 373 -255 -586 N ATOM 2678 CA CYS A 505 43.387 35.837 10.915 1.00 17.01 C ANISOU 2678 CA CYS A 505 2071 1930 2462 397 -272 -622 C ATOM 2679 C CYS A 505 43.973 36.942 11.808 1.00 19.79 C ANISOU 2679 C CYS A 505 2465 2270 2787 338 -266 -577 C ATOM 2680 O CYS A 505 43.955 38.115 11.428 1.00 19.79 O ANISOU 2680 O CYS A 505 2530 2251 2737 357 -271 -576 O ATOM 2681 CB CYS A 505 42.068 35.322 11.487 1.00 19.45 C ANISOU 2681 CB CYS A 505 2344 2250 2797 412 -290 -683 C ATOM 2682 SG CYS A 505 40.767 36.522 11.639 1.00 27.81 S ANISOU 2682 SG CYS A 505 3460 3297 3811 448 -314 -740 S ATOM 2683 N MET A 506 44.497 36.569 12.981 1.00 18.35 N ANISOU 2683 N MET A 506 2243 2094 2633 268 -258 -540 N ATOM 2684 CA MET A 506 45.109 37.536 13.902 1.00 20.47 C ANISOU 2684 CA MET A 506 2545 2353 2880 207 -252 -496 C ATOM 2685 C MET A 506 46.239 38.309 13.237 1.00 18.06 C ANISOU 2685 C MET A 506 2290 2034 2540 201 -237 -445 C ATOM 2686 O MET A 506 46.325 39.531 13.348 1.00 26.72 O ANISOU 2686 O MET A 506 3446 3111 3594 193 -241 -433 O ATOM 2687 CB MET A 506 45.661 36.841 15.147 1.00 19.34 C ANISOU 2687 CB MET A 506 2346 2223 2779 134 -243 -458 C ATOM 2688 CG MET A 506 44.628 36.111 15.975 1.00 21.12 C ANISOU 2688 CG MET A 506 2521 2464 3040 128 -256 -501 C ATOM 2689 SD MET A 506 45.367 35.023 17.207 1.00 29.43 S ANISOU 2689 SD MET A 506 3500 3534 4147 49 -243 -455 S ATOM 2690 CE MET A 506 46.397 36.201 18.092 1.00 19.19 C ANISOU 2690 CE MET A 506 2246 2225 2820 -20 -232 -392 C ATOM 2691 N LEU A 507 47.117 37.581 12.556 1.00 20.62 N ANISOU 2691 N LEU A 507 2588 2366 2882 203 -221 -415 N ATOM 2692 CA LEU A 507 48.241 38.193 11.862 1.00 28.55 C ANISOU 2692 CA LEU A 507 3634 3360 3855 196 -204 -365 C ATOM 2693 C LEU A 507 47.769 39.193 10.804 1.00 26.02 C ANISOU 2693 C LEU A 507 3382 3022 3482 257 -214 -392 C ATOM 2694 O LEU A 507 48.295 40.297 10.698 1.00 32.19 O ANISOU 2694 O LEU A 507 4221 3786 4223 243 -209 -361 O ATOM 2695 CB LEU A 507 49.116 37.112 11.225 1.00 29.49 C ANISOU 2695 CB LEU A 507 3706 3495 4004 198 -188 -339 C ATOM 2696 CG LEU A 507 50.353 37.584 10.454 1.00 29.18 C ANISOU 2696 CG LEU A 507 3700 3451 3936 190 -168 -287 C ATOM 2697 CD1 LEU A 507 51.171 38.553 11.290 1.00 20.90 C ANISOU 2697 CD1 LEU A 507 2685 2390 2865 124 -159 -234 C ATOM 2698 CD2 LEU A 507 51.196 36.391 10.038 1.00 25.20 C ANISOU 2698 CD2 LEU A 507 3140 2967 3468 184 -153 -263 C ATOM 2699 N THR A 508 46.763 38.801 10.035 1.00 18.19 N ANISOU 2699 N THR A 508 2385 2035 2492 326 -228 -451 N ATOM 2700 CA THR A 508 46.266 39.633 8.947 1.00 20.68 C ANISOU 2700 CA THR A 508 2762 2335 2760 390 -238 -480 C ATOM 2701 C THR A 508 45.649 40.912 9.480 1.00 23.69 C ANISOU 2701 C THR A 508 3202 2696 3104 386 -254 -496 C ATOM 2702 O THR A 508 45.798 41.981 8.891 1.00 25.34 O ANISOU 2702 O THR A 508 3478 2886 3265 406 -256 -486 O ATOM 2703 CB THR A 508 45.242 38.874 8.090 1.00 30.04 C ANISOU 2703 CB THR A 508 3923 3530 3959 464 -251 -544 C ATOM 2704 OG1 THR A 508 45.937 37.961 7.232 1.00 33.52 O ANISOU 2704 OG1 THR A 508 4330 3986 4421 481 -236 -526 O ATOM 2705 CG2 THR A 508 44.406 39.836 7.251 1.00 25.02 C ANISOU 2705 CG2 THR A 508 3354 2879 3275 530 -268 -587 C ATOM 2706 N ILE A 509 44.958 40.805 10.607 1.00 29.87 N ANISOU 2706 N ILE A 509 3960 3483 3906 360 -266 -519 N ATOM 2707 CA ILE A 509 44.401 41.984 11.240 1.00 24.42 C ANISOU 2707 CA ILE A 509 3321 2776 3184 352 -282 -534 C ATOM 2708 C ILE A 509 45.512 42.976 11.593 1.00 24.40 C ANISOU 2708 C ILE A 509 3362 2755 3153 298 -269 -470 C ATOM 2709 O ILE A 509 45.400 44.171 11.311 1.00 24.18 O ANISOU 2709 O ILE A 509 3403 2706 3079 314 -279 -471 O ATOM 2710 CB ILE A 509 43.597 41.626 12.499 1.00 23.51 C ANISOU 2710 CB ILE A 509 3163 2672 3098 323 -294 -565 C ATOM 2711 CG1 ILE A 509 42.304 40.916 12.109 1.00 26.27 C ANISOU 2711 CG1 ILE A 509 3482 3034 3464 384 -311 -637 C ATOM 2712 CG2 ILE A 509 43.284 42.883 13.311 1.00 18.67 C ANISOU 2712 CG2 ILE A 509 2600 2043 2452 300 -308 -567 C ATOM 2713 CD1 ILE A 509 41.616 40.245 13.275 1.00 29.69 C ANISOU 2713 CD1 ILE A 509 3859 3486 3937 353 -319 -663 C ATOM 2714 N CYS A 510 46.590 42.481 12.193 1.00 17.68 N ANISOU 2714 N CYS A 510 2473 1915 2329 234 -249 -415 N ATOM 2715 CA CYS A 510 47.659 43.375 12.622 1.00 24.98 C ANISOU 2715 CA CYS A 510 3435 2825 3231 178 -237 -354 C ATOM 2716 C CYS A 510 48.380 44.005 11.439 1.00 30.84 C ANISOU 2716 C CYS A 510 4231 3553 3934 202 -227 -325 C ATOM 2717 O CYS A 510 48.718 45.187 11.469 1.00 33.71 O ANISOU 2717 O CYS A 510 4655 3894 4258 187 -228 -300 O ATOM 2718 CB CYS A 510 48.654 42.661 13.531 1.00 18.88 C ANISOU 2718 CB CYS A 510 2608 2068 2498 106 -218 -303 C ATOM 2719 SG CYS A 510 47.909 42.040 15.048 1.00 23.29 S ANISOU 2719 SG CYS A 510 3108 2644 3099 67 -229 -328 S ATOM 2720 N CYS A 511 48.603 43.217 10.396 1.00 29.69 N ANISOU 2720 N CYS A 511 4063 3420 3800 240 -217 -328 N ATOM 2721 CA CYS A 511 49.301 43.718 9.224 1.00 28.24 C ANISOU 2721 CA CYS A 511 3925 3226 3580 264 -206 -300 C ATOM 2722 C CYS A 511 48.472 44.789 8.513 1.00 26.55 C ANISOU 2722 C CYS A 511 3783 2990 3316 322 -225 -337 C ATOM 2723 O CYS A 511 49.017 45.781 8.047 1.00 33.83 O ANISOU 2723 O CYS A 511 4765 3893 4196 320 -221 -305 O ATOM 2724 CB CYS A 511 49.686 42.567 8.280 1.00 21.15 C ANISOU 2724 CB CYS A 511 2980 2349 2705 294 -192 -299 C ATOM 2725 SG CYS A 511 50.981 41.474 8.947 1.00 34.11 S ANISOU 2725 SG CYS A 511 4549 4014 4397 223 -166 -241 S ATOM 2726 N ASP A 512 47.157 44.594 8.442 1.00 24.47 N ANISOU 2726 N ASP A 512 3513 2728 3057 374 -247 -403 N ATOM 2727 CA ASP A 512 46.272 45.615 7.881 1.00 30.04 C ANISOU 2727 CA ASP A 512 4285 3411 3716 429 -269 -444 C ATOM 2728 C ASP A 512 46.318 46.894 8.708 1.00 36.54 C ANISOU 2728 C ASP A 512 5163 4210 4511 390 -279 -426 C ATOM 2729 O ASP A 512 46.343 47.990 8.157 1.00 43.66 O ANISOU 2729 O ASP A 512 6135 5087 5365 411 -286 -420 O ATOM 2730 CB ASP A 512 44.825 45.128 7.808 1.00 26.45 C ANISOU 2730 CB ASP A 512 3809 2966 3277 486 -291 -521 C ATOM 2731 CG ASP A 512 44.609 44.106 6.711 1.00 40.06 C ANISOU 2731 CG ASP A 512 5498 4707 5017 543 -287 -548 C ATOM 2732 OD1 ASP A 512 45.524 43.923 5.879 1.00 42.68 O ANISOU 2732 OD1 ASP A 512 5834 5043 5342 547 -269 -510 O ATOM 2733 OD2 ASP A 512 43.524 43.483 6.688 1.00 47.02 O ANISOU 2733 OD2 ASP A 512 6347 5600 5919 585 -302 -609 O ATOM 2734 N ALA A 513 46.314 46.745 10.029 1.00 37.02 N ANISOU 2734 N ALA A 513 5190 4277 4598 334 -279 -418 N ATOM 2735 CA ALA A 513 46.323 47.889 10.933 1.00 34.83 C ANISOU 2735 CA ALA A 513 4957 3980 4298 295 -290 -404 C ATOM 2736 C ALA A 513 47.571 48.737 10.755 1.00 31.27 C ANISOU 2736 C ALA A 513 4553 3511 3818 255 -274 -337 C ATOM 2737 O ALA A 513 47.473 49.944 10.548 1.00 37.87 O ANISOU 2737 O ALA A 513 5459 4320 4611 265 -286 -335 O ATOM 2738 CB ALA A 513 46.196 47.431 12.378 1.00 32.29 C ANISOU 2738 CB ALA A 513 4581 3673 4014 239 -291 -404 C ATOM 2739 N VAL A 514 48.741 48.107 10.817 1.00 27.87 N ANISOU 2739 N VAL A 514 4084 3094 3411 209 -247 -283 N ATOM 2740 CA VAL A 514 49.993 48.858 10.787 1.00 32.18 C ANISOU 2740 CA VAL A 514 4668 3626 3934 162 -230 -216 C ATOM 2741 C VAL A 514 50.331 49.399 9.399 1.00 39.94 C ANISOU 2741 C VAL A 514 5706 4594 4874 204 -225 -203 C ATOM 2742 O VAL A 514 51.198 50.260 9.262 1.00 43.36 O ANISOU 2742 O VAL A 514 6187 5011 5278 173 -216 -154 O ATOM 2743 CB VAL A 514 51.189 48.044 11.318 1.00 26.23 C ANISOU 2743 CB VAL A 514 3857 2893 3217 97 -203 -161 C ATOM 2744 CG1 VAL A 514 50.916 47.564 12.724 1.00 23.64 C ANISOU 2744 CG1 VAL A 514 3477 2579 2928 51 -208 -170 C ATOM 2745 CG2 VAL A 514 51.490 46.874 10.391 1.00 32.07 C ANISOU 2745 CG2 VAL A 514 4550 3656 3979 127 -188 -162 C ATOM 2746 N SER A 515 49.654 48.900 8.372 1.00 41.90 N ANISOU 2746 N SER A 515 5949 4850 5119 274 -232 -246 N ATOM 2747 CA SER A 515 49.926 49.358 7.016 1.00 41.15 C ANISOU 2747 CA SER A 515 5906 4745 4985 318 -228 -236 C ATOM 2748 C SER A 515 48.849 50.314 6.511 1.00 47.21 C ANISOU 2748 C SER A 515 6739 5487 5710 378 -255 -283 C ATOM 2749 O SER A 515 48.866 50.720 5.353 1.00 49.13 O ANISOU 2749 O SER A 515 7029 5721 5918 424 -256 -284 O ATOM 2750 CB SER A 515 50.083 48.171 6.063 1.00 42.36 C ANISOU 2750 CB SER A 515 6010 4925 5159 355 -214 -245 C ATOM 2751 OG SER A 515 48.830 47.590 5.753 1.00 46.96 O ANISOU 2751 OG SER A 515 6571 5517 5756 419 -232 -314 O ATOM 2752 N GLY A 516 47.911 50.670 7.383 1.00 44.70 N ANISOU 2752 N GLY A 516 6427 5160 5396 378 -278 -323 N ATOM 2753 CA GLY A 516 46.897 51.652 7.045 1.00 46.87 C ANISOU 2753 CA GLY A 516 6767 5410 5631 430 -307 -368 C ATOM 2754 C GLY A 516 45.660 51.101 6.355 1.00 53.65 C ANISOU 2754 C GLY A 516 7612 6280 6494 510 -325 -440 C ATOM 2755 O GLY A 516 44.734 51.846 6.037 1.00 58.52 O ANISOU 2755 O GLY A 516 8279 6877 7079 559 -350 -484 O ATOM 2756 N ARG A 517 45.632 49.797 6.120 1.00 50.52 N ANISOU 2756 N ARG A 517 7146 5912 6136 523 -312 -454 N ATOM 2757 CA ARG A 517 44.485 49.184 5.463 1.00 49.22 C ANISOU 2757 CA ARG A 517 6963 5760 5979 597 -328 -522 C ATOM 2758 C ARG A 517 43.319 48.988 6.425 1.00 51.91 C ANISOU 2758 C ARG A 517 7274 6106 6342 601 -349 -579 C ATOM 2759 O ARG A 517 42.262 48.503 6.029 1.00 56.56 O ANISOU 2759 O ARG A 517 7846 6706 6940 660 -364 -641 O ATOM 2760 CB ARG A 517 44.874 47.849 4.818 1.00 47.13 C ANISOU 2760 CB ARG A 517 6635 5524 5748 611 -308 -517 C ATOM 2761 CG ARG A 517 45.908 47.981 3.699 1.00 51.30 C ANISOU 2761 CG ARG A 517 7190 6051 6252 619 -287 -470 C ATOM 2762 CD ARG A 517 46.035 46.701 2.873 1.00 56.73 C ANISOU 2762 CD ARG A 517 7821 6767 6968 653 -274 -481 C ATOM 2763 NE ARG A 517 46.566 45.584 3.651 1.00 57.77 N ANISOU 2763 NE ARG A 517 7874 6923 7154 602 -257 -460 N ATOM 2764 CZ ARG A 517 47.860 45.380 3.884 1.00 62.32 C ANISOU 2764 CZ ARG A 517 8431 7507 7742 543 -232 -396 C ATOM 2765 NH1 ARG A 517 48.762 46.226 3.404 1.00 61.69 N ANISOU 2765 NH1 ARG A 517 8404 7413 7623 526 -220 -346 N ATOM 2766 NH2 ARG A 517 48.251 44.334 4.605 1.00 64.12 N ANISOU 2766 NH2 ARG A 517 8587 7756 8020 500 -220 -381 N ATOM 2767 N ARG A 518 43.512 49.369 7.685 1.00 46.37 N ANISOU 2767 N ARG A 518 6568 5399 5650 539 -351 -559 N ATOM 2768 CA ARG A 518 42.471 49.200 8.696 1.00 43.18 C ANISOU 2768 CA ARG A 518 6135 5004 5268 536 -370 -609 C ATOM 2769 C ARG A 518 42.505 50.293 9.767 1.00 42.49 C ANISOU 2769 C ARG A 518 6085 4897 5161 490 -382 -594 C ATOM 2770 O ARG A 518 43.530 50.516 10.408 1.00 39.68 O ANISOU 2770 O ARG A 518 5727 4537 4811 423 -366 -535 O ATOM 2771 CB ARG A 518 42.582 47.824 9.358 1.00 48.59 C ANISOU 2771 CB ARG A 518 6731 5721 6010 503 -356 -608 C ATOM 2772 CG ARG A 518 41.724 47.678 10.604 1.00 51.56 C ANISOU 2772 CG ARG A 518 7073 6108 6409 481 -371 -645 C ATOM 2773 CD ARG A 518 41.979 46.358 11.312 1.00 51.76 C ANISOU 2773 CD ARG A 518 7013 6163 6491 439 -356 -634 C ATOM 2774 NE ARG A 518 41.242 46.298 12.569 1.00 51.85 N ANISOU 2774 NE ARG A 518 6995 6184 6521 411 -369 -664 N ATOM 2775 CZ ARG A 518 40.238 45.464 12.821 1.00 48.23 C ANISOU 2775 CZ ARG A 518 6485 5746 6092 434 -379 -718 C ATOM 2776 NH1 ARG A 518 39.839 44.582 11.906 1.00 39.26 N ANISOU 2776 NH1 ARG A 518 5321 4622 4972 486 -378 -750 N ATOM 2777 NH2 ARG A 518 39.638 45.509 14.002 1.00 47.65 N ANISOU 2777 NH2 ARG A 518 6389 5683 6032 403 -391 -740 N ATOM 2778 N GLN A 519 41.369 50.958 9.956 1.00 50.44 N ANISOU 2778 N GLN A 519 7125 5893 6147 527 -411 -651 N ATOM 2779 CA GLN A 519 41.235 52.037 10.934 1.00 50.03 C ANISOU 2779 CA GLN A 519 7111 5823 6075 492 -428 -647 C ATOM 2780 C GLN A 519 41.626 51.594 12.348 1.00 44.39 C ANISOU 2780 C GLN A 519 6341 5126 5399 416 -417 -621 C ATOM 2781 O GLN A 519 41.066 50.639 12.884 1.00 48.55 O ANISOU 2781 O GLN A 519 6803 5680 5963 413 -417 -653 O ATOM 2782 CB GLN A 519 39.795 52.567 10.922 1.00 51.73 C ANISOU 2782 CB GLN A 519 7356 6030 6269 550 -462 -724 C ATOM 2783 CG GLN A 519 39.540 53.747 11.845 1.00 54.67 C ANISOU 2783 CG GLN A 519 7772 6383 6618 524 -484 -729 C ATOM 2784 CD GLN A 519 40.497 54.894 11.599 1.00 60.29 C ANISOU 2784 CD GLN A 519 8554 7061 7292 499 -480 -672 C ATOM 2785 OE1 GLN A 519 41.572 54.961 12.192 1.00 62.90 O ANISOU 2785 OE1 GLN A 519 8875 7391 7634 431 -460 -610 O ATOM 2786 NE2 GLN A 519 40.107 55.809 10.723 1.00 61.76 N ANISOU 2786 NE2 GLN A 519 8813 7220 7434 553 -500 -692 N ATOM 2787 N THR A 520 42.587 52.295 12.943 1.00 38.27 N ANISOU 2787 N THR A 520 5591 4337 4614 355 -408 -564 N ATOM 2788 CA THR A 520 43.072 51.974 14.288 1.00 37.45 C ANISOU 2788 CA THR A 520 5440 4248 4542 280 -397 -533 C ATOM 2789 C THR A 520 42.490 52.922 15.344 1.00 41.35 C ANISOU 2789 C THR A 520 5961 4731 5021 261 -421 -556 C ATOM 2790 O THR A 520 42.638 52.703 16.545 1.00 35.04 O ANISOU 2790 O THR A 520 5121 3945 4246 206 -417 -544 O ATOM 2791 CB THR A 520 44.615 52.044 14.362 1.00 32.44 C ANISOU 2791 CB THR A 520 4807 3608 3912 218 -368 -452 C ATOM 2792 OG1 THR A 520 45.053 53.355 13.996 1.00 30.61 O ANISOU 2792 OG1 THR A 520 4655 3342 3634 217 -375 -424 O ATOM 2793 CG2 THR A 520 45.260 51.035 13.420 1.00 32.07 C ANISOU 2793 CG2 THR A 520 4726 3576 3884 231 -343 -427 C ATOM 2794 N LYS A 521 41.826 53.978 14.890 1.00 53.02 N ANISOU 2794 N LYS A 521 7506 6183 6456 308 -446 -590 N ATOM 2795 CA LYS A 521 41.282 54.980 15.798 1.00 51.56 C ANISOU 2795 CA LYS A 521 7353 5985 6252 295 -472 -614 C ATOM 2796 C LYS A 521 39.872 54.596 16.223 1.00 50.97 C ANISOU 2796 C LYS A 521 7245 5930 6189 331 -494 -691 C ATOM 2797 O LYS A 521 38.984 54.437 15.392 1.00 49.58 O ANISOU 2797 O LYS A 521 7079 5755 6002 400 -508 -743 O ATOM 2798 CB LYS A 521 41.274 56.349 15.122 1.00 56.71 C ANISOU 2798 CB LYS A 521 8097 6597 6852 327 -490 -612 C ATOM 2799 CG LYS A 521 41.584 57.505 16.049 1.00 68.22 C ANISOU 2799 CG LYS A 521 9597 8034 8291 280 -503 -590 C ATOM 2800 CD LYS A 521 41.483 58.841 15.319 1.00 74.39 C ANISOU 2800 CD LYS A 521 10470 8774 9021 317 -524 -593 C ATOM 2801 CE LYS A 521 42.435 58.908 14.133 1.00 74.29 C ANISOU 2801 CE LYS A 521 10491 8744 8991 325 -504 -541 C ATOM 2802 NZ LYS A 521 42.350 60.220 13.431 1.00 75.05 N ANISOU 2802 NZ LYS A 521 10680 8799 9037 359 -525 -542 N ATOM 2803 N GLU A 522 39.673 54.436 17.525 1.00 57.98 N ANISOU 2803 N GLU A 522 8093 6837 7100 285 -497 -697 N ATOM 2804 CA GLU A 522 38.370 54.071 18.065 1.00 58.23 C ANISOU 2804 CA GLU A 522 8089 6892 7144 311 -518 -768 C ATOM 2805 C GLU A 522 38.309 54.412 19.552 1.00 55.90 C ANISOU 2805 C GLU A 522 7775 6607 6858 254 -525 -765 C ATOM 2806 O GLU A 522 39.301 54.278 20.269 1.00 54.35 O ANISOU 2806 O GLU A 522 7557 6416 6680 186 -506 -708 O ATOM 2807 CB GLU A 522 38.098 52.577 17.853 1.00 59.15 C ANISOU 2807 CB GLU A 522 8130 7042 7303 323 -502 -785 C ATOM 2808 CG GLU A 522 36.695 52.134 18.263 1.00 64.90 C ANISOU 2808 CG GLU A 522 8820 7795 8044 356 -522 -862 C ATOM 2809 CD GLU A 522 36.576 50.626 18.465 1.00 70.36 C ANISOU 2809 CD GLU A 522 9427 8522 8786 343 -504 -868 C ATOM 2810 OE1 GLU A 522 36.648 49.873 17.466 1.00 68.46 O ANISOU 2810 OE1 GLU A 522 9170 8284 8557 379 -493 -870 O ATOM 2811 OE2 GLU A 522 36.397 50.198 19.628 1.00 72.36 O ANISOU 2811 OE2 GLU A 522 9630 8799 9066 297 -503 -871 O ATOM 2812 N GLY A 523 37.147 54.861 20.011 1.00 58.17 N ANISOU 2812 N GLY A 523 8071 6899 7131 281 -555 -829 N ATOM 2813 CA GLY A 523 36.942 55.150 21.419 1.00 65.45 C ANISOU 2813 CA GLY A 523 8971 7836 8060 233 -564 -836 C ATOM 2814 C GLY A 523 37.775 56.309 21.944 1.00 69.38 C ANISOU 2814 C GLY A 523 9520 8306 8535 187 -567 -788 C ATOM 2815 O GLY A 523 38.202 56.306 23.104 1.00 65.45 O ANISOU 2815 O GLY A 523 8993 7822 8054 124 -561 -761 O ATOM 2816 N GLY A 524 38.006 57.301 21.087 1.00 66.45 N ANISOU 2816 N GLY A 524 9225 7898 8126 219 -578 -778 N ATOM 2817 CA GLY A 524 38.737 58.496 21.465 1.00 67.99 C ANISOU 2817 CA GLY A 524 9476 8062 8294 182 -584 -737 C ATOM 2818 C GLY A 524 40.233 58.268 21.533 1.00 73.07 C ANISOU 2818 C GLY A 524 10109 8700 8954 119 -551 -652 C ATOM 2819 O GLY A 524 40.972 59.068 22.116 1.00 71.20 O ANISOU 2819 O GLY A 524 9901 8445 8706 71 -550 -610 O ATOM 2820 N TYR A 525 40.687 57.173 20.931 1.00 75.77 N ANISOU 2820 N TYR A 525 10409 9058 9322 120 -523 -628 N ATOM 2821 CA TYR A 525 42.103 56.843 20.955 1.00 74.89 C ANISOU 2821 CA TYR A 525 10281 8945 9227 63 -491 -551 C ATOM 2822 C TYR A 525 42.577 56.147 19.682 1.00 62.91 C ANISOU 2822 C TYR A 525 8760 7427 7716 92 -469 -529 C ATOM 2823 O TYR A 525 41.797 55.513 18.977 1.00 60.68 O ANISOU 2823 O TYR A 525 8461 7157 7439 148 -474 -574 O ATOM 2824 CB TYR A 525 42.431 55.983 22.180 1.00 84.59 C ANISOU 2824 CB TYR A 525 11435 10208 10499 -1 -474 -530 C ATOM 2825 CG TYR A 525 43.899 55.991 22.540 1.00 95.37 C ANISOU 2825 CG TYR A 525 12793 11567 11876 -71 -447 -451 C ATOM 2826 CD1 TYR A 525 44.514 57.153 22.990 1.00 97.24 C ANISOU 2826 CD1 TYR A 525 13081 11779 12089 -108 -453 -417 C ATOM 2827 CD2 TYR A 525 44.673 54.841 22.421 1.00100.12 C ANISOU 2827 CD2 TYR A 525 13339 12190 12513 -100 -416 -411 C ATOM 2828 CE1 TYR A 525 45.858 57.173 23.314 1.00 98.22 C ANISOU 2828 CE1 TYR A 525 13199 11899 12223 -172 -428 -345 C ATOM 2829 CE2 TYR A 525 46.019 54.851 22.744 1.00100.92 C ANISOU 2829 CE2 TYR A 525 13433 12288 12624 -162 -392 -340 C ATOM 2830 CZ TYR A 525 46.605 56.020 23.190 1.00101.15 C ANISOU 2830 CZ TYR A 525 13513 12292 12629 -198 -397 -307 C ATOM 2831 OH TYR A 525 47.941 56.038 23.516 1.00103.08 O ANISOU 2831 OH TYR A 525 13750 12534 12883 -261 -373 -238 O ATOM 2832 N ASP A 526 43.866 56.294 19.392 1.00 53.59 N ANISOU 2832 N ASP A 526 7596 6233 6533 54 -446 -460 N ATOM 2833 CA ASP A 526 44.514 55.565 18.312 1.00 50.36 C ANISOU 2833 CA ASP A 526 7174 5828 6132 69 -421 -431 C ATOM 2834 C ASP A 526 45.196 54.333 18.914 1.00 50.16 C ANISOU 2834 C ASP A 526 7069 5835 6156 17 -393 -396 C ATOM 2835 O ASP A 526 46.126 54.457 19.709 1.00 47.39 O ANISOU 2835 O ASP A 526 6706 5485 5816 -50 -379 -345 O ATOM 2836 CB ASP A 526 45.535 56.461 17.606 1.00 43.98 C ANISOU 2836 CB ASP A 526 6432 4988 5291 59 -412 -376 C ATOM 2837 CG ASP A 526 46.015 55.875 16.298 1.00 50.67 C ANISOU 2837 CG ASP A 526 7278 5837 6137 90 -392 -356 C ATOM 2838 OD1 ASP A 526 45.919 54.645 16.132 1.00 54.18 O ANISOU 2838 OD1 ASP A 526 7660 6310 6616 99 -378 -366 O ATOM 2839 OD2 ASP A 526 46.488 56.640 15.433 1.00 50.68 O ANISOU 2839 OD2 ASP A 526 7342 5811 6104 106 -391 -330 O ATOM 2840 N HIS A 527 44.724 53.145 18.546 1.00 39.35 N ANISOU 2840 N HIS A 527 5645 4491 4815 47 -386 -425 N ATOM 2841 CA HIS A 527 45.227 51.921 19.151 1.00 35.39 C ANISOU 2841 CA HIS A 527 5066 4020 4361 1 -364 -399 C ATOM 2842 C HIS A 527 46.391 51.333 18.372 1.00 33.25 C ANISOU 2842 C HIS A 527 4782 3751 4101 -12 -334 -344 C ATOM 2843 O HIS A 527 46.756 50.179 18.566 1.00 46.07 O ANISOU 2843 O HIS A 527 6341 5400 5765 -34 -316 -328 O ATOM 2844 CB HIS A 527 44.108 50.896 19.284 1.00 37.02 C ANISOU 2844 CB HIS A 527 5216 4255 4597 35 -373 -458 C ATOM 2845 CG HIS A 527 43.058 51.280 20.278 1.00 46.68 C ANISOU 2845 CG HIS A 527 6435 5485 5817 34 -397 -507 C ATOM 2846 ND1 HIS A 527 42.319 52.437 20.171 1.00 52.14 N ANISOU 2846 ND1 HIS A 527 7188 6155 6468 69 -425 -546 N ATOM 2847 CD2 HIS A 527 42.614 50.652 21.393 1.00 56.72 C ANISOU 2847 CD2 HIS A 527 7647 6784 7119 2 -399 -526 C ATOM 2848 CE1 HIS A 527 41.468 52.508 21.178 1.00 54.75 C ANISOU 2848 CE1 HIS A 527 7496 6500 6805 60 -443 -587 C ATOM 2849 NE2 HIS A 527 41.628 51.439 21.935 1.00 60.53 N ANISOU 2849 NE2 HIS A 527 8156 7263 7581 19 -427 -575 N ATOM 2850 N ALA A 528 46.980 52.142 17.505 1.00 30.41 N ANISOU 2850 N ALA A 528 4483 3365 3706 2 -331 -316 N ATOM 2851 CA ALA A 528 48.102 51.712 16.678 1.00 36.25 C ANISOU 2851 CA ALA A 528 5218 4106 4450 -8 -304 -264 C ATOM 2852 C ALA A 528 49.236 51.032 17.461 1.00 33.95 C ANISOU 2852 C ALA A 528 4872 3834 4195 -81 -278 -207 C ATOM 2853 O ALA A 528 49.821 50.058 16.984 1.00 28.36 O ANISOU 2853 O ALA A 528 4122 3143 3511 -83 -257 -185 O ATOM 2854 CB ALA A 528 48.636 52.884 15.866 1.00 33.79 C ANISOU 2854 CB ALA A 528 4986 3762 4091 4 -304 -235 C ATOM 2855 N ILE A 529 49.559 51.537 18.650 1.00 32.45 N ANISOU 2855 N ILE A 529 4682 3641 4008 -140 -279 -184 N ATOM 2856 CA ILE A 529 50.618 50.908 19.444 1.00 35.17 C ANISOU 2856 CA ILE A 529 4974 4002 4385 -209 -256 -131 C ATOM 2857 C ILE A 529 50.229 49.509 19.912 1.00 32.03 C ANISOU 2857 C ILE A 529 4496 3638 4037 -214 -251 -152 C ATOM 2858 O ILE A 529 51.091 48.665 20.146 1.00 34.82 O ANISOU 2858 O ILE A 529 4800 4009 4422 -253 -229 -113 O ATOM 2859 CB ILE A 529 51.058 51.750 20.663 1.00 38.21 C ANISOU 2859 CB ILE A 529 5376 4379 4765 -273 -259 -102 C ATOM 2860 CG1 ILE A 529 50.012 51.680 21.779 1.00 48.22 C ANISOU 2860 CG1 ILE A 529 6617 5659 6046 -278 -280 -148 C ATOM 2861 CG2 ILE A 529 51.331 53.176 20.249 1.00 47.98 C ANISOU 2861 CG2 ILE A 529 6696 5580 5954 -267 -268 -85 C ATOM 2862 CD1 ILE A 529 48.725 52.420 21.479 1.00 53.25 C ANISOU 2862 CD1 ILE A 529 7300 6281 6653 -218 -310 -211 C ATOM 2863 N SER A 530 48.931 49.266 20.050 1.00 28.22 N ANISOU 2863 N SER A 530 3999 3164 3559 -173 -272 -215 N ATOM 2864 CA SER A 530 48.459 47.942 20.420 1.00 31.17 C ANISOU 2864 CA SER A 530 4298 3567 3977 -172 -269 -240 C ATOM 2865 C SER A 530 48.645 46.926 19.289 1.00 27.98 C ANISOU 2865 C SER A 530 3867 3174 3592 -134 -255 -241 C ATOM 2866 O SER A 530 49.137 45.822 19.512 1.00 26.51 O ANISOU 2866 O SER A 530 3619 3009 3445 -160 -239 -219 O ATOM 2867 CB SER A 530 47.005 48.003 20.873 1.00 31.89 C ANISOU 2867 CB SER A 530 4383 3665 4067 -140 -295 -308 C ATOM 2868 OG SER A 530 46.919 48.720 22.085 1.00 36.33 O ANISOU 2868 OG SER A 530 4956 4226 4623 -184 -305 -304 O ATOM 2869 N PHE A 531 48.255 47.307 18.077 1.00 22.53 N ANISOU 2869 N PHE A 531 3220 2468 2871 -71 -263 -266 N ATOM 2870 CA PHE A 531 48.462 46.461 16.910 1.00 26.36 C ANISOU 2870 CA PHE A 531 3685 2962 3367 -31 -250 -267 C ATOM 2871 C PHE A 531 49.944 46.221 16.676 1.00 28.98 C ANISOU 2871 C PHE A 531 4008 3296 3707 -73 -223 -199 C ATOM 2872 O PHE A 531 50.343 45.141 16.235 1.00 30.95 O ANISOU 2872 O PHE A 531 4209 3563 3986 -68 -208 -188 O ATOM 2873 CB PHE A 531 47.852 47.096 15.664 1.00 29.22 C ANISOU 2873 CB PHE A 531 4107 3306 3690 42 -264 -302 C ATOM 2874 CG PHE A 531 46.361 47.136 15.682 1.00 33.86 C ANISOU 2874 CG PHE A 531 4698 3896 4274 95 -290 -376 C ATOM 2875 CD1 PHE A 531 45.625 46.008 15.370 1.00 28.10 C ANISOU 2875 CD1 PHE A 531 3916 3187 3574 133 -293 -420 C ATOM 2876 CD2 PHE A 531 45.690 48.302 16.010 1.00 30.81 C ANISOU 2876 CD2 PHE A 531 4365 3489 3851 106 -313 -403 C ATOM 2877 CE1 PHE A 531 44.247 46.042 15.384 1.00 27.93 C ANISOU 2877 CE1 PHE A 531 3895 3168 3548 181 -317 -489 C ATOM 2878 CE2 PHE A 531 44.306 48.341 16.021 1.00 28.18 C ANISOU 2878 CE2 PHE A 531 4033 3159 3513 156 -338 -473 C ATOM 2879 CZ PHE A 531 43.587 47.212 15.711 1.00 28.74 C ANISOU 2879 CZ PHE A 531 4053 3253 3616 193 -339 -516 C ATOM 2880 N GLN A 532 50.755 47.233 16.966 1.00 29.51 N ANISOU 2880 N GLN A 532 4120 3346 3748 -114 -217 -153 N ATOM 2881 CA GLN A 532 52.196 47.120 16.783 1.00 33.43 C ANISOU 2881 CA GLN A 532 4611 3844 4248 -158 -191 -87 C ATOM 2882 C GLN A 532 52.753 46.087 17.732 1.00 24.70 C ANISOU 2882 C GLN A 532 3432 2762 3190 -214 -176 -60 C ATOM 2883 O GLN A 532 53.580 45.259 17.356 1.00 30.56 O ANISOU 2883 O GLN A 532 4137 3519 3955 -226 -157 -29 O ATOM 2884 CB GLN A 532 52.887 48.457 17.017 1.00 38.27 C ANISOU 2884 CB GLN A 532 5286 4431 4823 -194 -189 -46 C ATOM 2885 CG GLN A 532 52.764 49.418 15.864 1.00 50.74 C ANISOU 2885 CG GLN A 532 6939 5986 6355 -146 -195 -53 C ATOM 2886 CD GLN A 532 53.593 50.664 16.083 1.00 65.67 C ANISOU 2886 CD GLN A 532 8888 7851 8211 -188 -191 -5 C ATOM 2887 OE1 GLN A 532 54.558 50.648 16.851 1.00 72.19 O ANISOU 2887 OE1 GLN A 532 9694 8683 9052 -254 -175 43 O ATOM 2888 NE2 GLN A 532 53.224 51.753 15.410 1.00 65.10 N ANISOU 2888 NE2 GLN A 532 8888 7752 8094 -151 -206 -19 N ATOM 2889 N ASP A 533 52.277 46.140 18.967 1.00 18.61 N ANISOU 2889 N ASP A 533 2641 1996 2434 -246 -187 -74 N ATOM 2890 CA ASP A 533 52.678 45.186 19.979 1.00 22.61 C ANISOU 2890 CA ASP A 533 3079 2526 2986 -299 -177 -52 C ATOM 2891 C ASP A 533 52.310 43.770 19.548 1.00 25.15 C ANISOU 2891 C ASP A 533 3340 2870 3347 -268 -174 -78 C ATOM 2892 O ASP A 533 53.161 42.876 19.534 1.00 28.40 O ANISOU 2892 O ASP A 533 3705 3296 3788 -295 -156 -43 O ATOM 2893 CB ASP A 533 52.009 45.524 21.306 1.00 31.69 C ANISOU 2893 CB ASP A 533 4221 3678 4141 -330 -193 -73 C ATOM 2894 CG ASP A 533 52.601 44.762 22.463 1.00 45.41 C ANISOU 2894 CG ASP A 533 5898 5437 5919 -395 -181 -40 C ATOM 2895 OD1 ASP A 533 53.824 44.844 22.655 1.00 55.98 O ANISOU 2895 OD1 ASP A 533 7235 6775 7261 -443 -162 17 O ATOM 2896 OD2 ASP A 533 51.848 44.082 23.183 1.00 46.47 O ANISOU 2896 OD2 ASP A 533 5986 5589 6082 -399 -190 -70 O ATOM 2897 N TRP A 534 51.046 43.566 19.180 1.00 23.62 N ANISOU 2897 N TRP A 534 3145 2678 3152 -211 -193 -140 N ATOM 2898 CA TRP A 534 50.590 42.226 18.802 1.00 25.82 C ANISOU 2898 CA TRP A 534 3365 2977 3469 -180 -192 -169 C ATOM 2899 C TRP A 534 51.363 41.677 17.612 1.00 19.79 C ANISOU 2899 C TRP A 534 2595 2217 2709 -156 -176 -146 C ATOM 2900 O TRP A 534 51.680 40.491 17.559 1.00 23.72 O ANISOU 2900 O TRP A 534 3034 2733 3247 -163 -166 -138 O ATOM 2901 CB TRP A 534 49.089 42.209 18.508 1.00 22.52 C ANISOU 2901 CB TRP A 534 2953 2559 3044 -119 -216 -242 C ATOM 2902 CG TRP A 534 48.266 42.705 19.643 1.00 20.65 C ANISOU 2902 CG TRP A 534 2719 2322 2803 -139 -233 -269 C ATOM 2903 CD1 TRP A 534 48.516 42.531 20.972 1.00 19.87 C ANISOU 2903 CD1 TRP A 534 2586 2235 2727 -202 -230 -246 C ATOM 2904 CD2 TRP A 534 47.053 43.456 19.555 1.00 21.08 C ANISOU 2904 CD2 TRP A 534 2814 2368 2830 -94 -257 -326 C ATOM 2905 NE1 TRP A 534 47.533 43.132 21.720 1.00 27.15 N ANISOU 2905 NE1 TRP A 534 3523 3156 3636 -200 -250 -285 N ATOM 2906 CE2 TRP A 534 46.623 43.710 20.872 1.00 23.72 C ANISOU 2906 CE2 TRP A 534 3134 2709 3170 -134 -267 -335 C ATOM 2907 CE3 TRP A 534 46.286 43.937 18.488 1.00 22.55 C ANISOU 2907 CE3 TRP A 534 3044 2539 2983 -23 -271 -370 C ATOM 2908 CZ2 TRP A 534 45.461 44.426 21.153 1.00 25.20 C ANISOU 2908 CZ2 TRP A 534 3351 2891 3334 -106 -291 -389 C ATOM 2909 CZ3 TRP A 534 45.136 44.657 18.765 1.00 19.00 C ANISOU 2909 CZ3 TRP A 534 2626 2084 2511 5 -295 -423 C ATOM 2910 CH2 TRP A 534 44.733 44.892 20.086 1.00 25.53 C ANISOU 2910 CH2 TRP A 534 3436 2918 3345 -36 -305 -432 C ATOM 2911 N LEU A 535 51.670 42.549 16.662 1.00 18.50 N ANISOU 2911 N LEU A 535 2491 2035 2504 -128 -173 -136 N ATOM 2912 CA LEU A 535 52.404 42.136 15.482 1.00 21.81 C ANISOU 2912 CA LEU A 535 2909 2457 2920 -103 -157 -115 C ATOM 2913 C LEU A 535 53.818 41.687 15.849 1.00 25.11 C ANISOU 2913 C LEU A 535 3294 2887 3361 -164 -133 -51 C ATOM 2914 O LEU A 535 54.266 40.626 15.402 1.00 23.72 O ANISOU 2914 O LEU A 535 3071 2728 3214 -158 -122 -41 O ATOM 2915 CB LEU A 535 52.425 43.259 14.454 1.00 26.74 C ANISOU 2915 CB LEU A 535 3608 3060 3491 -64 -160 -115 C ATOM 2916 CG LEU A 535 53.224 43.021 13.182 1.00 27.81 C ANISOU 2916 CG LEU A 535 3752 3199 3617 -38 -143 -91 C ATOM 2917 CD1 LEU A 535 52.660 41.839 12.407 1.00 25.49 C ANISOU 2917 CD1 LEU A 535 3413 2923 3350 17 -146 -131 C ATOM 2918 CD2 LEU A 535 53.193 44.287 12.356 1.00 32.64 C ANISOU 2918 CD2 LEU A 535 4444 3786 4172 -7 -147 -89 C ATOM 2919 N LYS A 536 54.498 42.477 16.683 1.00 19.42 N ANISOU 2919 N LYS A 536 2595 2156 2626 -223 -127 -9 N ATOM 2920 CA LYS A 536 55.818 42.110 17.192 1.00 28.51 C ANISOU 2920 CA LYS A 536 3715 3318 3798 -287 -106 51 C ATOM 2921 C LYS A 536 55.825 40.748 17.881 1.00 25.14 C ANISOU 2921 C LYS A 536 3210 2915 3427 -310 -103 49 C ATOM 2922 O LYS A 536 56.779 39.990 17.736 1.00 29.29 O ANISOU 2922 O LYS A 536 3698 3456 3977 -333 -86 84 O ATOM 2923 CB LYS A 536 56.364 43.164 18.159 1.00 38.92 C ANISOU 2923 CB LYS A 536 5067 4623 5097 -347 -103 89 C ATOM 2924 CG LYS A 536 56.637 44.520 17.534 1.00 58.24 C ANISOU 2924 CG LYS A 536 7593 7046 7492 -336 -102 104 C ATOM 2925 CD LYS A 536 56.956 45.548 18.614 1.00 72.89 C ANISOU 2925 CD LYS A 536 9478 8887 9331 -392 -105 132 C ATOM 2926 CE LYS A 536 56.456 46.937 18.235 1.00 77.87 C ANISOU 2926 CE LYS A 536 10188 9488 9912 -365 -120 115 C ATOM 2927 NZ LYS A 536 56.574 47.897 19.370 1.00 76.99 N ANISOU 2927 NZ LYS A 536 10103 9363 9788 -415 -127 132 N ATOM 2928 N LYS A 537 54.776 40.442 18.636 1.00 23.69 N ANISOU 2928 N LYS A 537 3002 2737 3263 -306 -120 9 N ATOM 2929 CA LYS A 537 54.687 39.129 19.282 1.00 25.25 C ANISOU 2929 CA LYS A 537 3124 2956 3513 -327 -119 5 C ATOM 2930 C LYS A 537 54.600 38.019 18.242 1.00 23.30 C ANISOU 2930 C LYS A 537 2842 2722 3291 -279 -117 -15 C ATOM 2931 O LYS A 537 55.278 37.001 18.342 1.00 27.61 O ANISOU 2931 O LYS A 537 3335 3283 3873 -302 -106 10 O ATOM 2932 CB LYS A 537 53.471 39.043 20.205 1.00 22.53 C ANISOU 2932 CB LYS A 537 2764 2616 3182 -327 -139 -39 C ATOM 2933 CG LYS A 537 53.532 39.917 21.457 1.00 24.56 C ANISOU 2933 CG LYS A 537 3041 2866 3425 -381 -143 -21 C ATOM 2934 CD LYS A 537 52.276 39.678 22.293 1.00 27.74 C ANISOU 2934 CD LYS A 537 3420 3278 3844 -377 -162 -70 C ATOM 2935 CE LYS A 537 52.232 40.530 23.533 1.00 26.58 C ANISOU 2935 CE LYS A 537 3291 3127 3683 -426 -168 -58 C ATOM 2936 NZ LYS A 537 53.079 39.952 24.592 1.00 32.99 N ANISOU 2936 NZ LYS A 537 4054 3953 4527 -495 -155 -12 N ATOM 2937 N LEU A 538 53.754 38.226 17.245 1.00 20.19 N ANISOU 2937 N LEU A 538 2476 2320 2875 -212 -128 -60 N ATOM 2938 CA LEU A 538 53.528 37.228 16.212 1.00 22.73 C ANISOU 2938 CA LEU A 538 2767 2653 3217 -159 -128 -87 C ATOM 2939 C LEU A 538 54.780 37.060 15.349 1.00 22.79 C ANISOU 2939 C LEU A 538 2775 2664 3218 -161 -108 -43 C ATOM 2940 O LEU A 538 55.168 35.947 15.013 1.00 25.07 O ANISOU 2940 O LEU A 538 3014 2970 3542 -155 -101 -37 O ATOM 2941 CB LEU A 538 52.309 37.615 15.358 1.00 28.45 C ANISOU 2941 CB LEU A 538 3526 3367 3915 -85 -145 -147 C ATOM 2942 CG LEU A 538 50.922 37.526 16.019 1.00 27.52 C ANISOU 2942 CG LEU A 538 3397 3252 3809 -70 -167 -202 C ATOM 2943 CD1 LEU A 538 49.827 38.109 15.141 1.00 25.10 C ANISOU 2943 CD1 LEU A 538 3135 2933 3468 2 -184 -258 C ATOM 2944 CD2 LEU A 538 50.588 36.089 16.359 1.00 23.79 C ANISOU 2944 CD2 LEU A 538 2850 2799 3391 -72 -170 -221 C ATOM 2945 N HIS A 539 55.412 38.175 15.008 1.00 22.78 N ANISOU 2945 N HIS A 539 2833 2649 3174 -171 -99 -12 N ATOM 2946 CA HIS A 539 56.610 38.159 14.187 1.00 27.29 C ANISOU 2946 CA HIS A 539 3411 3225 3734 -175 -79 31 C ATOM 2947 C HIS A 539 57.741 37.442 14.903 1.00 32.46 C ANISOU 2947 C HIS A 539 4014 3895 4423 -237 -63 80 C ATOM 2948 O HIS A 539 58.510 36.701 14.297 1.00 38.23 O ANISOU 2948 O HIS A 539 4714 4640 5170 -233 -50 100 O ATOM 2949 CB HIS A 539 57.049 39.585 13.864 1.00 26.06 C ANISOU 2949 CB HIS A 539 3329 3050 3524 -182 -73 57 C ATOM 2950 CG HIS A 539 58.304 39.654 13.057 1.00 41.16 C ANISOU 2950 CG HIS A 539 5252 4968 5421 -191 -51 103 C ATOM 2951 ND1 HIS A 539 59.557 39.681 13.630 1.00 51.25 N ANISOU 2951 ND1 HIS A 539 6515 6252 6706 -256 -33 161 N ATOM 2952 CD2 HIS A 539 58.500 39.695 11.718 1.00 44.55 C ANISOU 2952 CD2 HIS A 539 5703 5400 5826 -143 -45 100 C ATOM 2953 CE1 HIS A 539 60.472 39.738 12.679 1.00 51.74 C ANISOU 2953 CE1 HIS A 539 6589 6320 6750 -248 -16 190 C ATOM 2954 NE2 HIS A 539 59.857 39.749 11.509 1.00 48.79 N ANISOU 2954 NE2 HIS A 539 6238 5945 6357 -180 -23 155 N ATOM 2955 N SER A 540 57.839 37.670 16.203 1.00 31.53 N ANISOU 2955 N SER A 540 3888 3775 4317 -295 -64 99 N ATOM 2956 CA SER A 540 58.875 37.041 17.003 1.00 25.19 C ANISOU 2956 CA SER A 540 3038 2986 3548 -357 -51 145 C ATOM 2957 C SER A 540 58.649 35.530 17.081 1.00 19.20 C ANISOU 2957 C SER A 540 2206 2246 2842 -347 -55 126 C ATOM 2958 O SER A 540 59.596 34.749 17.023 1.00 25.00 O ANISOU 2958 O SER A 540 2900 2995 3603 -369 -42 158 O ATOM 2959 CB SER A 540 58.906 37.660 18.403 1.00 27.49 C ANISOU 2959 CB SER A 540 3337 3270 3838 -418 -53 165 C ATOM 2960 OG SER A 540 59.782 36.940 19.244 1.00 36.01 O ANISOU 2960 OG SER A 540 4365 4363 4953 -475 -43 204 O ATOM 2961 N ARG A 541 57.391 35.121 17.211 1.00 20.34 N ANISOU 2961 N ARG A 541 2335 2391 3004 -313 -74 74 N ATOM 2962 CA ARG A 541 57.063 33.701 17.273 1.00 17.80 C ANISOU 2962 CA ARG A 541 1946 2084 2732 -300 -80 52 C ATOM 2963 C ARG A 541 57.351 33.019 15.937 1.00 19.32 C ANISOU 2963 C ARG A 541 2124 2286 2931 -249 -75 43 C ATOM 2964 O ARG A 541 57.963 31.959 15.889 1.00 21.40 O ANISOU 2964 O ARG A 541 2335 2564 3232 -261 -69 60 O ATOM 2965 CB ARG A 541 55.594 33.496 17.647 1.00 18.98 C ANISOU 2965 CB ARG A 541 2085 2232 2894 -272 -101 -4 C ATOM 2966 CG ARG A 541 55.182 32.020 17.739 1.00 21.72 C ANISOU 2966 CG ARG A 541 2363 2594 3295 -260 -109 -29 C ATOM 2967 CD ARG A 541 56.060 31.297 18.770 1.00 27.27 C ANISOU 2967 CD ARG A 541 3016 3309 4038 -327 -101 17 C ATOM 2968 NE ARG A 541 55.795 31.814 20.104 1.00 28.53 N ANISOU 2968 NE ARG A 541 3182 3465 4194 -378 -105 26 N ATOM 2969 CZ ARG A 541 54.964 31.249 20.974 1.00 29.09 C ANISOU 2969 CZ ARG A 541 3216 3542 4295 -391 -118 1 C ATOM 2970 NH1 ARG A 541 54.343 30.119 20.662 1.00 25.01 N ANISOU 2970 NH1 ARG A 541 2654 3034 3815 -359 -128 -33 N ATOM 2971 NH2 ARG A 541 54.767 31.811 22.161 1.00 30.71 N ANISOU 2971 NH2 ARG A 541 3430 3745 4492 -437 -121 11 N ATOM 2972 N VAL A 542 56.893 33.634 14.856 1.00 20.86 N ANISOU 2972 N VAL A 542 2365 2472 3089 -192 -78 16 N ATOM 2973 CA VAL A 542 57.104 33.094 13.526 1.00 21.49 C ANISOU 2973 CA VAL A 542 2436 2561 3169 -140 -74 4 C ATOM 2974 C VAL A 542 58.588 33.000 13.188 1.00 29.61 C ANISOU 2974 C VAL A 542 3457 3599 4195 -169 -52 59 C ATOM 2975 O VAL A 542 59.054 31.974 12.688 1.00 26.24 O ANISOU 2975 O VAL A 542 2985 3188 3797 -156 -48 62 O ATOM 2976 CB VAL A 542 56.374 33.923 12.481 1.00 20.60 C ANISOU 2976 CB VAL A 542 2381 2436 3011 -76 -81 -32 C ATOM 2977 CG1 VAL A 542 56.774 33.490 11.085 1.00 16.98 C ANISOU 2977 CG1 VAL A 542 1918 1988 2547 -26 -73 -36 C ATOM 2978 CG2 VAL A 542 54.863 33.791 12.683 1.00 18.26 C ANISOU 2978 CG2 VAL A 542 2080 2133 2723 -38 -103 -93 C ATOM 2979 N THR A 543 59.327 34.069 13.471 1.00 26.69 N ANISOU 2979 N THR A 543 3132 3220 3790 -210 -40 101 N ATOM 2980 CA THR A 543 60.773 34.053 13.313 1.00 24.62 C ANISOU 2980 CA THR A 543 2862 2968 3523 -247 -19 156 C ATOM 2981 C THR A 543 61.388 32.852 14.023 1.00 28.68 C ANISOU 2981 C THR A 543 3307 3500 4092 -288 -15 178 C ATOM 2982 O THR A 543 62.135 32.094 13.418 1.00 30.33 O ANISOU 2982 O THR A 543 3482 3725 4318 -279 -6 192 O ATOM 2983 CB THR A 543 61.427 35.341 13.850 1.00 27.28 C ANISOU 2983 CB THR A 543 3251 3292 3823 -298 -8 200 C ATOM 2984 OG1 THR A 543 61.002 36.458 13.064 1.00 33.31 O ANISOU 2984 OG1 THR A 543 4083 4038 4535 -260 -10 185 O ATOM 2985 CG2 THR A 543 62.947 35.243 13.776 1.00 22.22 C ANISOU 2985 CG2 THR A 543 2597 2663 3182 -341 14 257 C ATOM 2986 N LYS A 544 61.064 32.674 15.300 1.00 29.90 N ANISOU 2986 N LYS A 544 3438 3651 4272 -330 -23 179 N ATOM 2987 CA LYS A 544 61.672 31.603 16.092 1.00 28.81 C ANISOU 2987 CA LYS A 544 3236 3526 4183 -374 -21 203 C ATOM 2988 C LYS A 544 61.280 30.218 15.592 1.00 27.62 C ANISOU 2988 C LYS A 544 3029 3389 4076 -334 -31 171 C ATOM 2989 O LYS A 544 62.086 29.302 15.622 1.00 25.92 O ANISOU 2989 O LYS A 544 2767 3188 3894 -352 -25 193 O ATOM 2990 CB LYS A 544 61.258 31.696 17.556 1.00 26.01 C ANISOU 2990 CB LYS A 544 2869 3166 3845 -424 -29 207 C ATOM 2991 CG LYS A 544 61.834 32.838 18.349 1.00 24.46 C ANISOU 2991 CG LYS A 544 2714 2961 3620 -479 -19 247 C ATOM 2992 CD LYS A 544 61.146 32.845 19.707 1.00 27.48 C ANISOU 2992 CD LYS A 544 3081 3339 4020 -515 -32 237 C ATOM 2993 CE LYS A 544 61.559 34.005 20.567 1.00 31.52 C ANISOU 2993 CE LYS A 544 3632 3841 4503 -568 -25 270 C ATOM 2994 NZ LYS A 544 60.914 33.918 21.908 1.00 31.61 N ANISOU 2994 NZ LYS A 544 3624 3853 4534 -603 -37 260 N ATOM 2995 N GLU A 545 60.032 30.066 15.156 1.00 24.68 N ANISOU 2995 N GLU A 545 2662 3012 3705 -279 -47 116 N ATOM 2996 CA GLU A 545 59.530 28.766 14.742 1.00 19.25 C ANISOU 2996 CA GLU A 545 1920 2333 3060 -240 -59 81 C ATOM 2997 C GLU A 545 59.501 28.603 13.220 1.00 22.49 C ANISOU 2997 C GLU A 545 2341 2750 3455 -172 -57 57 C ATOM 2998 O GLU A 545 58.817 27.715 12.691 1.00 28.24 O ANISOU 2998 O GLU A 545 3037 3483 4210 -125 -70 15 O ATOM 2999 CB GLU A 545 58.143 28.523 15.350 1.00 17.60 C ANISOU 2999 CB GLU A 545 1699 2117 2869 -227 -79 34 C ATOM 3000 CG GLU A 545 58.172 27.912 16.755 1.00 27.25 C ANISOU 3000 CG GLU A 545 2877 3344 4134 -286 -84 51 C ATOM 3001 CD GLU A 545 58.762 26.495 16.765 1.00 42.61 C ANISOU 3001 CD GLU A 545 4756 5303 6132 -296 -84 64 C ATOM 3002 OE1 GLU A 545 60.007 26.357 16.683 1.00 42.94 O ANISOU 3002 OE1 GLU A 545 4787 5353 6177 -324 -70 108 O ATOM 3003 OE2 GLU A 545 57.981 25.516 16.860 1.00 42.81 O ANISOU 3003 OE2 GLU A 545 4738 5331 6196 -275 -99 29 O ATOM 3004 N ARG A 546 60.260 29.441 12.518 1.00 21.49 N ANISOU 3004 N ARG A 546 2525 3127 2513 -14 -127 2 N ATOM 3005 CA ARG A 546 60.183 29.491 11.058 1.00 24.68 C ANISOU 3005 CA ARG A 546 2982 3549 2844 11 -82 -14 C ATOM 3006 C ARG A 546 60.456 28.161 10.363 1.00 22.68 C ANISOU 3006 C ARG A 546 2668 3333 2616 61 -60 -61 C ATOM 3007 O ARG A 546 59.877 27.880 9.319 1.00 22.64 O ANISOU 3007 O ARG A 546 2709 3333 2561 109 -52 -87 O ATOM 3008 CB ARG A 546 61.089 30.586 10.486 1.00 29.90 C ANISOU 3008 CB ARG A 546 3680 4225 3454 -50 -16 19 C ATOM 3009 CG ARG A 546 62.564 30.282 10.552 1.00 39.09 C ANISOU 3009 CG ARG A 546 4757 5431 4663 -91 38 21 C ATOM 3010 CD ARG A 546 63.380 31.501 10.156 1.00 44.88 C ANISOU 3010 CD ARG A 546 5533 6174 5347 -157 95 59 C ATOM 3011 NE ARG A 546 64.812 31.284 10.329 1.00 51.76 N ANISOU 3011 NE ARG A 546 6319 7083 6264 -202 145 64 N ATOM 3012 CZ ARG A 546 65.427 31.238 11.507 1.00 57.84 C ANISOU 3012 CZ ARG A 546 7019 7852 7104 -241 129 80 C ATOM 3013 NH1 ARG A 546 64.734 31.384 12.633 1.00 55.37 N ANISOU 3013 NH1 ARG A 546 6711 7504 6825 -240 65 94 N ATOM 3014 NH2 ARG A 546 66.739 31.036 11.562 1.00 55.30 N ANISOU 3014 NH2 ARG A 546 6623 7567 6820 -279 178 83 N ATOM 3015 N HIS A 547 61.324 27.338 10.939 1.00 24.17 N ANISOU 3015 N HIS A 547 2754 3549 2881 52 -53 -74 N ATOM 3016 CA HIS A 547 61.649 26.064 10.309 1.00 29.23 C ANISOU 3016 CA HIS A 547 3331 4226 3548 97 -31 -118 C ATOM 3017 C HIS A 547 60.499 25.057 10.346 1.00 32.03 C ANISOU 3017 C HIS A 547 3684 4565 3921 172 -88 -157 C ATOM 3018 O HIS A 547 60.151 24.487 9.317 1.00 37.79 O ANISOU 3018 O HIS A 547 4431 5309 4617 222 -73 -189 O ATOM 3019 CB HIS A 547 62.932 25.474 10.883 1.00 30.39 C ANISOU 3019 CB HIS A 547 3368 4406 3772 65 -6 -121 C ATOM 3020 CG HIS A 547 64.166 26.178 10.420 1.00 37.73 C ANISOU 3020 CG HIS A 547 4294 5365 4679 4 66 -97 C ATOM 3021 ND1 HIS A 547 64.965 26.918 11.264 1.00 48.23 N ANISOU 3021 ND1 HIS A 547 5598 6691 6034 -64 76 -59 N ATOM 3022 CD2 HIS A 547 64.732 26.265 9.194 1.00 36.82 C ANISOU 3022 CD2 HIS A 547 4195 5280 4513 2 131 -106 C ATOM 3023 CE1 HIS A 547 65.975 27.423 10.579 1.00 46.62 C ANISOU 3023 CE1 HIS A 547 5397 6517 5801 -106 145 -45 C ATOM 3024 NE2 HIS A 547 65.855 27.043 9.321 1.00 41.05 N ANISOU 3024 NE2 HIS A 547 4717 5833 5048 -68 179 -73 N ATOM 3025 N ARG A 548 59.912 24.835 11.518 1.00 25.76 N ANISOU 3025 N ARG A 548 2866 3742 3178 180 -152 -153 N ATOM 3026 CA ARG A 548 58.711 24.009 11.594 1.00 24.84 C ANISOU 3026 CA ARG A 548 2759 3606 3074 250 -210 -186 C ATOM 3027 C ARG A 548 57.551 24.588 10.778 1.00 24.30 C ANISOU 3027 C ARG A 548 2800 3510 2921 283 -223 -187 C ATOM 3028 O ARG A 548 56.873 23.860 10.057 1.00 24.69 O ANISOU 3028 O ARG A 548 2865 3563 2952 344 -234 -223 O ATOM 3029 CB ARG A 548 58.293 23.766 13.042 1.00 23.05 C ANISOU 3029 CB ARG A 548 2492 3351 2915 248 -277 -179 C ATOM 3030 CG ARG A 548 58.958 22.529 13.640 1.00 28.62 C ANISOU 3030 CG ARG A 548 3082 4083 3710 259 -283 -204 C ATOM 3031 CD ARG A 548 58.536 22.294 15.079 1.00 25.98 C ANISOU 3031 CD ARG A 548 2710 3721 3443 257 -349 -197 C ATOM 3032 NE ARG A 548 59.320 23.101 16.008 1.00 29.35 N ANISOU 3032 NE ARG A 548 3113 4142 3896 185 -342 -155 N ATOM 3033 CZ ARG A 548 60.517 22.753 16.480 1.00 29.23 C ANISOU 3033 CZ ARG A 548 3010 4155 3941 149 -315 -151 C ATOM 3034 NH1 ARG A 548 61.084 21.606 16.112 1.00 23.19 N ANISOU 3034 NH1 ARG A 548 2170 3427 3216 177 -293 -186 N ATOM 3035 NH2 ARG A 548 61.151 23.557 17.325 1.00 23.51 N ANISOU 3035 NH2 ARG A 548 2273 3423 3236 84 -310 -112 N ATOM 3036 N LEU A 549 57.335 25.896 10.876 1.00 26.57 N ANISOU 3036 N LEU A 549 3165 3771 3158 242 -223 -147 N ATOM 3037 CA LEU A 549 56.225 26.527 10.164 1.00 21.69 C ANISOU 3037 CA LEU A 549 2655 3125 2461 269 -237 -145 C ATOM 3038 C LEU A 549 56.377 26.388 8.645 1.00 22.16 C ANISOU 3038 C LEU A 549 2750 3212 2458 295 -183 -166 C ATOM 3039 O LEU A 549 55.390 26.341 7.924 1.00 23.55 O ANISOU 3039 O LEU A 549 2991 3373 2582 343 -200 -184 O ATOM 3040 CB LEU A 549 56.094 28.008 10.559 1.00 20.00 C ANISOU 3040 CB LEU A 549 2514 2880 2206 214 -242 -96 C ATOM 3041 CG LEU A 549 55.684 28.325 12.003 1.00 20.14 C ANISOU 3041 CG LEU A 549 2520 2862 2271 192 -302 -73 C ATOM 3042 CD1 LEU A 549 56.017 29.767 12.359 1.00 20.63 C ANISOU 3042 CD1 LEU A 549 2632 2905 2301 123 -287 -23 C ATOM 3043 CD2 LEU A 549 54.216 28.060 12.208 1.00 18.95 C ANISOU 3043 CD2 LEU A 549 2414 2674 2112 249 -369 -91 C ATOM 3044 N SER A 550 57.618 26.328 8.170 1.00 28.44 N ANISOU 3044 N SER A 550 3501 4048 3257 262 -119 -164 N ATOM 3045 CA SER A 550 57.910 26.145 6.747 1.00 33.52 C ANISOU 3045 CA SER A 550 4168 4722 3847 282 -62 -185 C ATOM 3046 C SER A 550 57.347 24.837 6.186 1.00 31.74 C ANISOU 3046 C SER A 550 3916 4510 3635 358 -79 -236 C ATOM 3047 O SER A 550 57.170 24.692 4.978 1.00 29.33 O ANISOU 3047 O SER A 550 3651 4219 3274 390 -48 -256 O ATOM 3048 CB SER A 550 59.425 26.166 6.514 1.00 37.60 C ANISOU 3048 CB SER A 550 4624 5282 4381 233 7 -176 C ATOM 3049 OG SER A 550 59.921 27.489 6.524 1.00 45.32 O ANISOU 3049 OG SER A 550 5650 6251 5317 167 39 -132 O ATOM 3050 N ARG A 551 57.089 23.885 7.074 1.00 28.54 N ANISOU 3050 N ARG A 551 3441 4099 3303 387 -127 -256 N ATOM 3051 CA ARG A 551 56.555 22.583 6.690 1.00 32.75 C ANISOU 3051 CA ARG A 551 3942 4644 3859 458 -148 -305 C ATOM 3052 C ARG A 551 55.082 22.626 6.276 1.00 30.76 C ANISOU 3052 C ARG A 551 3773 4358 3557 515 -193 -320 C ATOM 3053 O ARG A 551 54.602 21.706 5.622 1.00 30.78 O ANISOU 3053 O ARG A 551 3768 4371 3555 575 -200 -359 O ATOM 3054 CB ARG A 551 56.716 21.596 7.855 1.00 23.49 C ANISOU 3054 CB ARG A 551 2670 3473 2783 469 -190 -320 C ATOM 3055 CG ARG A 551 58.161 21.244 8.158 1.00 26.71 C ANISOU 3055 CG ARG A 551 2982 3918 3247 427 -146 -317 C ATOM 3056 CD ARG A 551 58.255 20.472 9.445 1.00 25.26 C ANISOU 3056 CD ARG A 551 2712 3730 3157 429 -192 -324 C ATOM 3057 NE ARG A 551 57.345 19.339 9.443 1.00 33.12 N ANISOU 3057 NE ARG A 551 3689 4719 4179 501 -240 -365 N ATOM 3058 CZ ARG A 551 56.975 18.683 10.533 1.00 32.46 C ANISOU 3058 CZ ARG A 551 3552 4618 4164 518 -297 -374 C ATOM 3059 NH1 ARG A 551 57.451 19.054 11.720 1.00 22.64 N ANISOU 3059 NH1 ARG A 551 2269 3365 2970 468 -314 -344 N ATOM 3060 NH2 ARG A 551 56.132 17.659 10.430 1.00 26.73 N ANISOU 3060 NH2 ARG A 551 2813 3887 3456 585 -337 -412 N ATOM 3061 N PHE A 552 54.368 23.678 6.673 1.00 25.02 N ANISOU 3061 N PHE A 552 3122 3591 2794 495 -225 -288 N ATOM 3062 CA PHE A 552 52.923 23.758 6.449 1.00 26.23 C ANISOU 3062 CA PHE A 552 3352 3708 2906 546 -275 -300 C ATOM 3063 C PHE A 552 52.554 24.927 5.552 1.00 24.34 C ANISOU 3063 C PHE A 552 3223 3454 2572 532 -250 -277 C ATOM 3064 O PHE A 552 53.272 25.917 5.495 1.00 31.06 O ANISOU 3064 O PHE A 552 4097 4309 3395 473 -211 -242 O ATOM 3065 CB PHE A 552 52.185 23.855 7.784 1.00 20.80 C ANISOU 3065 CB PHE A 552 2660 2981 2264 545 -346 -287 C ATOM 3066 CG PHE A 552 52.536 22.749 8.736 1.00 26.81 C ANISOU 3066 CG PHE A 552 3313 3754 3118 556 -373 -306 C ATOM 3067 CD1 PHE A 552 51.771 21.589 8.790 1.00 28.22 C ANISOU 3067 CD1 PHE A 552 3462 3929 3330 622 -416 -347 C ATOM 3068 CD2 PHE A 552 53.656 22.854 9.556 1.00 22.39 C ANISOU 3068 CD2 PHE A 552 2683 3211 2615 499 -354 -284 C ATOM 3069 CE1 PHE A 552 52.109 20.561 9.662 1.00 34.36 C ANISOU 3069 CE1 PHE A 552 4143 4719 4195 632 -440 -365 C ATOM 3070 CE2 PHE A 552 54.005 21.832 10.423 1.00 18.81 C ANISOU 3070 CE2 PHE A 552 2130 2768 2247 509 -378 -302 C ATOM 3071 CZ PHE A 552 53.230 20.682 10.476 1.00 27.72 C ANISOU 3071 CZ PHE A 552 3231 3893 3408 575 -421 -342 C ATOM 3072 N SER A 553 51.448 24.786 4.830 1.00 25.57 N ANISOU 3072 N SER A 553 3444 3592 2678 588 -273 -299 N ATOM 3073 CA SER A 553 50.916 25.858 4.001 1.00 22.29 C ANISOU 3073 CA SER A 553 3139 3158 2172 582 -259 -280 C ATOM 3074 C SER A 553 50.574 27.087 4.843 1.00 24.55 C ANISOU 3074 C SER A 553 3479 3404 2444 536 -289 -236 C ATOM 3075 O SER A 553 50.900 28.213 4.478 1.00 26.82 O ANISOU 3075 O SER A 553 3825 3687 2677 490 -255 -203 O ATOM 3076 CB SER A 553 49.670 25.381 3.262 1.00 29.27 C ANISOU 3076 CB SER A 553 4078 4026 3016 655 -291 -314 C ATOM 3077 OG SER A 553 49.952 24.256 2.450 1.00 27.53 O ANISOU 3077 OG SER A 553 3812 3843 2807 699 -263 -356 O ATOM 3078 N SER A 554 49.927 26.855 5.977 1.00 19.14 N ANISOU 3078 N SER A 554 2773 2690 1811 547 -353 -235 N ATOM 3079 CA SER A 554 49.574 27.932 6.888 1.00 23.20 C ANISOU 3079 CA SER A 554 3330 3166 2320 506 -387 -195 C ATOM 3080 C SER A 554 50.812 28.715 7.342 1.00 22.82 C ANISOU 3080 C SER A 554 3254 3132 2286 427 -345 -155 C ATOM 3081 O SER A 554 50.788 29.942 7.387 1.00 19.67 O ANISOU 3081 O SER A 554 2920 2712 1841 383 -337 -118 O ATOM 3082 CB SER A 554 48.826 27.375 8.107 1.00 19.34 C ANISOU 3082 CB SER A 554 2803 2648 1896 530 -460 -205 C ATOM 3083 OG SER A 554 49.625 26.416 8.798 1.00 22.01 O ANISOU 3083 OG SER A 554 3032 3014 2318 525 -458 -219 O ATOM 3084 N GLY A 555 51.880 27.994 7.686 1.00 19.34 N ANISOU 3084 N GLY A 555 2714 2725 1908 410 -319 -164 N ATOM 3085 CA GLY A 555 53.094 28.606 8.186 1.00 19.66 C ANISOU 3085 CA GLY A 555 2716 2782 1971 337 -280 -130 C ATOM 3086 C GLY A 555 53.792 29.385 7.091 1.00 24.23 C ANISOU 3086 C GLY A 555 3343 3382 2481 303 -211 -113 C ATOM 3087 O GLY A 555 54.246 30.508 7.311 1.00 24.75 O ANISOU 3087 O GLY A 555 3441 3439 2523 244 -190 -72 O ATOM 3088 N LYS A 556 53.867 28.792 5.904 1.00 20.81 N ANISOU 3088 N LYS A 556 2914 2976 2016 342 -175 -144 N ATOM 3089 CA LYS A 556 54.422 29.491 4.755 1.00 28.44 C ANISOU 3089 CA LYS A 556 3932 3962 2911 316 -109 -131 C ATOM 3090 C LYS A 556 53.654 30.772 4.453 1.00 29.56 C ANISOU 3090 C LYS A 556 4189 4068 2975 302 -120 -101 C ATOM 3091 O LYS A 556 54.261 31.773 4.083 1.00 27.17 O ANISOU 3091 O LYS A 556 3926 3771 2627 251 -75 -70 O ATOM 3092 CB LYS A 556 54.479 28.584 3.525 1.00 28.51 C ANISOU 3092 CB LYS A 556 3931 4005 2898 367 -75 -173 C ATOM 3093 CG LYS A 556 55.572 27.524 3.632 1.00 36.17 C ANISOU 3093 CG LYS A 556 4790 5019 3935 365 -43 -196 C ATOM 3094 CD LYS A 556 55.996 26.968 2.280 1.00 43.41 C ANISOU 3094 CD LYS A 556 5703 5975 4816 392 13 -226 C ATOM 3095 CE LYS A 556 55.222 25.714 1.921 1.00 51.81 C ANISOU 3095 CE LYS A 556 6745 7043 5897 471 -18 -275 C ATOM 3096 NZ LYS A 556 54.026 25.999 1.079 1.00 62.33 N ANISOU 3096 NZ LYS A 556 8176 8350 7155 516 -38 -285 N ATOM 3097 N LYS A 557 52.332 30.743 4.626 1.00 27.09 N ANISOU 3097 N LYS A 557 3928 3718 2647 347 -180 -111 N ATOM 3098 CA LYS A 557 51.513 31.920 4.361 1.00 30.53 C ANISOU 3098 CA LYS A 557 4474 4116 3011 338 -196 -85 C ATOM 3099 C LYS A 557 51.798 33.021 5.370 1.00 27.02 C ANISOU 3099 C LYS A 557 4041 3648 2577 272 -207 -37 C ATOM 3100 O LYS A 557 51.840 34.191 5.013 1.00 24.87 O ANISOU 3100 O LYS A 557 3843 3362 2244 235 -185 -5 O ATOM 3101 CB LYS A 557 50.024 31.578 4.336 1.00 35.55 C ANISOU 3101 CB LYS A 557 5158 4718 3631 403 -259 -109 C ATOM 3102 CG LYS A 557 49.638 30.676 3.163 1.00 50.64 C ANISOU 3102 CG LYS A 557 7078 6650 5515 469 -246 -153 C ATOM 3103 CD LYS A 557 48.153 30.748 2.813 1.00 55.06 C ANISOU 3103 CD LYS A 557 7720 7172 6028 524 -296 -167 C ATOM 3104 CE LYS A 557 47.268 30.198 3.922 1.00 59.35 C ANISOU 3104 CE LYS A 557 8234 7686 6630 557 -370 -180 C ATOM 3105 NZ LYS A 557 45.875 29.920 3.437 1.00 61.95 N ANISOU 3105 NZ LYS A 557 8626 7989 6923 624 -415 -207 N ATOM 3106 N MET A 558 52.017 32.641 6.624 1.00 20.36 N ANISOU 3106 N MET A 558 3125 2800 1812 257 -241 -33 N ATOM 3107 CA MET A 558 52.351 33.623 7.642 1.00 26.77 C ANISOU 3107 CA MET A 558 3939 3590 2640 193 -251 11 C ATOM 3108 C MET A 558 53.707 34.267 7.380 1.00 24.41 C ANISOU 3108 C MET A 558 3624 3321 2330 127 -182 39 C ATOM 3109 O MET A 558 53.850 35.481 7.468 1.00 22.40 O ANISOU 3109 O MET A 558 3426 3049 2036 77 -170 78 O ATOM 3110 CB MET A 558 52.324 32.995 9.031 1.00 21.91 C ANISOU 3110 CB MET A 558 3245 2966 2115 193 -301 7 C ATOM 3111 CG MET A 558 50.939 32.630 9.496 1.00 26.20 C ANISOU 3111 CG MET A 558 3815 3472 2669 247 -375 -12 C ATOM 3112 SD MET A 558 50.866 32.447 11.280 1.00 33.31 S ANISOU 3112 SD MET A 558 4648 4349 3658 225 -435 2 S ATOM 3113 CE MET A 558 51.809 30.952 11.537 1.00 18.25 C ANISOU 3113 CE MET A 558 2611 2487 1837 241 -418 -32 C ATOM 3114 N ILE A 559 54.699 33.441 7.065 1.00 30.81 N ANISOU 3114 N ILE A 559 4357 4176 3176 127 -139 19 N ATOM 3115 CA ILE A 559 56.044 33.927 6.804 1.00 31.97 C ANISOU 3115 CA ILE A 559 4477 4354 3316 66 -71 41 C ATOM 3116 C ILE A 559 55.978 34.916 5.657 1.00 35.42 C ANISOU 3116 C ILE A 559 5010 4789 3659 52 -29 59 C ATOM 3117 O ILE A 559 56.592 35.981 5.692 1.00 42.10 O ANISOU 3117 O ILE A 559 5886 5634 4478 -9 4 97 O ATOM 3118 CB ILE A 559 56.983 32.769 6.436 1.00 30.58 C ANISOU 3118 CB ILE A 559 4208 4226 3184 81 -31 9 C ATOM 3119 CG1 ILE A 559 57.265 31.912 7.668 1.00 27.83 C ANISOU 3119 CG1 ILE A 559 3759 3882 2933 82 -66 -1 C ATOM 3120 CG2 ILE A 559 58.276 33.287 5.824 1.00 23.50 C ANISOU 3120 CG2 ILE A 559 3302 3365 2264 26 46 28 C ATOM 3121 CD1 ILE A 559 57.810 30.530 7.339 1.00 24.45 C ANISOU 3121 CD1 ILE A 559 3242 3494 2553 118 -46 -43 C ATOM 3122 N GLU A 560 55.195 34.555 4.651 1.00 39.98 N ANISOU 3122 N GLU A 560 5639 5366 4188 108 -32 30 N ATOM 3123 CA GLU A 560 54.998 35.387 3.476 1.00 42.09 C ANISOU 3123 CA GLU A 560 6001 5629 4362 104 3 41 C ATOM 3124 C GLU A 560 54.272 36.696 3.819 1.00 40.77 C ANISOU 3124 C GLU A 560 5927 5417 4149 78 -27 80 C ATOM 3125 O GLU A 560 54.631 37.760 3.318 1.00 41.49 O ANISOU 3125 O GLU A 560 6077 5507 4182 34 12 110 O ATOM 3126 CB GLU A 560 54.222 34.596 2.428 1.00 48.06 C ANISOU 3126 CB GLU A 560 6786 6392 5084 177 -2 -1 C ATOM 3127 CG GLU A 560 54.109 35.267 1.079 1.00 68.79 C ANISOU 3127 CG GLU A 560 9500 9022 7616 178 41 4 C ATOM 3128 CD GLU A 560 53.144 34.540 0.154 1.00 84.51 C ANISOU 3128 CD GLU A 560 11526 11010 9572 254 25 -36 C ATOM 3129 OE1 GLU A 560 52.454 35.225 -0.633 1.00 90.08 O ANISOU 3129 OE1 GLU A 560 12329 11697 10201 266 25 -29 O ATOM 3130 OE2 GLU A 560 53.067 33.290 0.222 1.00 85.48 O ANISOU 3130 OE2 GLU A 560 11582 11152 9746 301 10 -75 O ATOM 3131 N THR A 561 53.256 36.613 4.673 1.00 26.54 N ANISOU 3131 N THR A 561 4135 3577 2372 103 -97 78 N ATOM 3132 CA THR A 561 52.506 37.789 5.085 1.00 30.57 C ANISOU 3132 CA THR A 561 4729 4042 2844 81 -132 112 C ATOM 3133 C THR A 561 53.447 38.814 5.722 1.00 31.22 C ANISOU 3133 C THR A 561 4803 4124 2936 0 -106 158 C ATOM 3134 O THR A 561 53.386 40.007 5.426 1.00 30.46 O ANISOU 3134 O THR A 561 4785 4010 2779 -36 -90 191 O ATOM 3135 CB THR A 561 51.382 37.410 6.075 1.00 37.46 C ANISOU 3135 CB THR A 561 5597 4878 3760 118 -213 101 C ATOM 3136 OG1 THR A 561 50.370 36.655 5.392 1.00 34.08 O ANISOU 3136 OG1 THR A 561 5196 4444 3309 192 -239 61 O ATOM 3137 CG2 THR A 561 50.750 38.657 6.691 1.00 31.88 C ANISOU 3137 CG2 THR A 561 4964 4124 3023 86 -249 140 C ATOM 3138 N LEU A 562 54.335 38.331 6.579 1.00 31.63 N ANISOU 3138 N LEU A 562 4759 4196 3063 -28 -99 160 N ATOM 3139 CA LEU A 562 55.288 39.191 7.257 1.00 33.14 C ANISOU 3139 CA LEU A 562 4930 4390 3272 -103 -75 202 C ATOM 3140 C LEU A 562 56.294 39.759 6.272 1.00 39.61 C ANISOU 3140 C LEU A 562 5770 5240 4040 -144 2 217 C ATOM 3141 O LEU A 562 56.603 40.947 6.314 1.00 42.99 O ANISOU 3141 O LEU A 562 6247 5655 4431 -198 23 257 O ATOM 3142 CB LEU A 562 55.999 38.419 8.362 1.00 27.32 C ANISOU 3142 CB LEU A 562 4081 3670 2630 -119 -86 196 C ATOM 3143 CG LEU A 562 55.119 38.187 9.589 1.00 27.41 C ANISOU 3143 CG LEU A 562 4077 3644 2692 -100 -163 195 C ATOM 3144 CD1 LEU A 562 55.628 37.015 10.428 1.00 24.00 C ANISOU 3144 CD1 LEU A 562 3531 3235 2354 -89 -179 172 C ATOM 3145 CD2 LEU A 562 55.034 39.461 10.414 1.00 20.96 C ANISOU 3145 CD2 LEU A 562 3305 2794 1865 -156 -183 241 C ATOM 3146 N ALA A 563 56.796 38.904 5.386 1.00 40.27 N ANISOU 3146 N ALA A 563 5815 5363 4123 -117 45 185 N ATOM 3147 CA ALA A 563 57.720 39.328 4.337 1.00 46.77 C ANISOU 3147 CA ALA A 563 6656 6219 4897 -149 120 195 C ATOM 3148 C ALA A 563 57.092 40.423 3.477 1.00 44.64 C ANISOU 3148 C ALA A 563 6505 5925 4531 -153 130 215 C ATOM 3149 O ALA A 563 57.737 41.415 3.147 1.00 47.01 O ANISOU 3149 O ALA A 563 6842 6230 4789 -207 175 247 O ATOM 3150 CB ALA A 563 58.123 38.133 3.467 1.00 40.50 C ANISOU 3150 CB ALA A 563 5808 5467 4113 -106 156 151 C ATOM 3151 N ASN A 564 55.825 40.225 3.131 1.00 42.44 N ANISOU 3151 N ASN A 564 6285 5620 4220 -95 86 195 N ATOM 3152 CA ASN A 564 55.059 41.152 2.309 1.00 52.91 C ANISOU 3152 CA ASN A 564 7726 6920 5457 -88 86 208 C ATOM 3153 C ASN A 564 54.925 42.531 2.961 1.00 56.91 C ANISOU 3153 C ASN A 564 8291 7390 5941 -143 70 257 C ATOM 3154 O ASN A 564 54.835 43.552 2.276 1.00 57.15 O ANISOU 3154 O ASN A 564 8407 7411 5898 -166 95 281 O ATOM 3155 CB ASN A 564 53.666 40.569 2.070 1.00 57.59 C ANISOU 3155 CB ASN A 564 8358 7488 6035 -13 31 176 C ATOM 3156 CG ASN A 564 53.249 40.623 0.618 1.00 67.56 C ANISOU 3156 CG ASN A 564 9694 8758 7218 23 59 159 C ATOM 3157 OD1 ASN A 564 53.152 41.698 0.020 1.00 78.31 O ANISOU 3157 OD1 ASN A 564 11141 10106 8508 -3 81 186 O ATOM 3158 ND2 ASN A 564 52.980 39.454 0.043 1.00 62.23 N ANISOU 3158 ND2 ASN A 564 8987 8103 6554 84 57 114 N ATOM 3159 N LEU A 565 54.900 42.545 4.290 1.00 53.05 N ANISOU 3159 N LEU A 565 7756 6883 5515 -163 27 271 N ATOM 3160 CA LEU A 565 54.739 43.777 5.050 1.00 52.93 C ANISOU 3160 CA LEU A 565 7790 6833 5489 -214 5 315 C ATOM 3161 C LEU A 565 56.005 44.630 5.006 1.00 64.49 C ANISOU 3161 C LEU A 565 9245 8318 6941 -289 66 352 C ATOM 3162 O LEU A 565 55.929 45.855 4.864 1.00 60.51 O ANISOU 3162 O LEU A 565 8817 7792 6383 -328 76 388 O ATOM 3163 CB LEU A 565 54.364 43.459 6.501 1.00 41.05 C ANISOU 3163 CB LEU A 565 6233 5305 4060 -212 -58 317 C ATOM 3164 CG LEU A 565 53.865 44.612 7.369 1.00 38.56 C ANISOU 3164 CG LEU A 565 5972 4945 3734 -249 -98 357 C ATOM 3165 CD1 LEU A 565 52.571 45.166 6.815 1.00 47.85 C ANISOU 3165 CD1 LEU A 565 7256 6084 4841 -213 -131 356 C ATOM 3166 CD2 LEU A 565 53.657 44.132 8.778 1.00 34.16 C ANISOU 3166 CD2 LEU A 565 5349 4372 3259 -247 -153 354 C ATOM 3167 N ARG A 566 57.160 43.976 5.130 1.00 76.40 N ANISOU 3167 N ARG A 566 10661 9867 8501 -309 106 343 N ATOM 3168 CA ARG A 566 58.457 44.657 5.099 1.00 89.61 C ANISOU 3168 CA ARG A 566 12314 11563 10170 -380 167 374 C ATOM 3169 C ARG A 566 58.573 45.587 3.898 1.00 89.23 C ANISOU 3169 C ARG A 566 12355 11519 10031 -400 217 392 C ATOM 3170 O ARG A 566 58.970 46.746 4.032 1.00 93.51 O ANISOU 3170 O ARG A 566 12937 12049 10542 -458 237 432 O ATOM 3171 CB ARG A 566 59.604 43.643 5.069 1.00 99.73 C ANISOU 3171 CB ARG A 566 13488 12893 11510 -384 209 351 C ATOM 3172 CG ARG A 566 59.801 42.867 6.358 1.00107.99 C ANISOU 3172 CG ARG A 566 14438 13941 12652 -383 170 342 C ATOM 3173 CD ARG A 566 60.873 41.799 6.189 1.00114.87 C ANISOU 3173 CD ARG A 566 15207 14861 13575 -380 212 315 C ATOM 3174 NE ARG A 566 61.041 40.978 7.387 1.00118.80 N ANISOU 3174 NE ARG A 566 15611 15361 14166 -375 173 304 N ATOM 3175 CZ ARG A 566 60.353 39.868 7.640 1.00119.92 C ANISOU 3175 CZ ARG A 566 15715 15499 14349 -314 128 267 C ATOM 3176 NH1 ARG A 566 59.440 39.437 6.780 1.00120.40 N ANISOU 3176 NH1 ARG A 566 15824 15555 14368 -252 114 238 N ATOM 3177 NH2 ARG A 566 60.578 39.187 8.757 1.00118.84 N ANISOU 3177 NH2 ARG A 566 15493 15365 14297 -315 95 260 N ATOM 3178 N SER A 567 58.230 45.067 2.724 1.00 79.10 N ANISOU 3178 N SER A 567 11100 10251 8703 -351 236 361 N ATOM 3179 CA SER A 567 58.220 45.867 1.507 1.00 78.03 C ANISOU 3179 CA SER A 567 11054 10117 8477 -361 279 373 C ATOM 3180 C SER A 567 56.834 46.465 1.266 1.00 80.99 C ANISOU 3180 C SER A 567 11533 10446 8792 -329 232 378 C ATOM 3181 O SER A 567 56.332 46.465 0.142 1.00 81.47 O ANISOU 3181 O SER A 567 11658 10509 8790 -294 245 363 O ATOM 3182 CB SER A 567 58.648 45.023 0.306 1.00 78.14 C ANISOU 3182 CB SER A 567 11045 10174 8472 -328 330 338 C ATOM 3183 OG SER A 567 57.701 44.006 0.031 1.00 74.97 O ANISOU 3183 OG SER A 567 10639 9767 8078 -252 291 295 O TER 3184 SER A 567 ATOM 3185 O5' U B 1 46.149 21.066 1.185 1.00 34.69 O ANISOU 3185 O5' U B 1 3382 4807 4991 306 -845 -892 O ATOM 3186 C5' U B 1 45.073 21.828 1.692 1.00 27.22 C ANISOU 3186 C5' U B 1 2485 3862 3994 303 -861 -892 C ATOM 3187 C4' U B 1 44.732 21.391 3.100 1.00 27.42 C ANISOU 3187 C4' U B 1 2581 3803 4035 283 -891 -907 C ATOM 3188 O4' U B 1 45.748 21.796 4.022 1.00 31.45 O ANISOU 3188 O4' U B 1 3120 4230 4599 272 -944 -847 O ATOM 3189 C3' U B 1 43.446 22.009 3.632 1.00 27.79 C ANISOU 3189 C3' U B 1 2682 3853 4024 280 -900 -919 C ATOM 3190 O3' U B 1 42.301 21.227 3.297 1.00 26.56 O ANISOU 3190 O3' U B 1 2525 3745 3823 282 -856 -993 O ATOM 3191 C2' U B 1 43.696 22.093 5.124 1.00 29.31 C ANISOU 3191 C2' U B 1 2942 3943 4251 261 -953 -892 C ATOM 3192 O2' U B 1 43.389 20.922 5.798 1.00 32.10 O ANISOU 3192 O2' U B 1 3324 4254 4620 249 -945 -943 O ATOM 3193 C1' U B 1 45.190 22.341 5.181 1.00 26.68 C ANISOU 3193 C1' U B 1 2586 3570 3982 259 -983 -832 C ATOM 3194 N1 U B 1 45.483 23.770 5.250 1.00 26.66 N ANISOU 3194 N1 U B 1 2594 3564 3973 263 -1019 -764 N ATOM 3195 C2 U B 1 45.490 24.358 6.475 1.00 26.47 C ANISOU 3195 C2 U B 1 2633 3464 3960 248 -1069 -728 C ATOM 3196 O2 U B 1 45.291 23.703 7.475 1.00 30.44 O ANISOU 3196 O2 U B 1 3182 3905 4479 233 -1085 -751 O ATOM 3197 N3 U B 1 45.761 25.702 6.447 1.00 26.46 N ANISOU 3197 N3 U B 1 2637 3465 3951 252 -1098 -666 N ATOM 3198 C4 U B 1 45.989 26.504 5.341 1.00 29.49 C ANISOU 3198 C4 U B 1 2970 3918 4316 270 -1082 -637 C ATOM 3199 O4 U B 1 46.209 27.704 5.464 1.00 31.77 O ANISOU 3199 O4 U B 1 3272 4200 4601 272 -1111 -581 O ATOM 3200 C5 U B 1 45.955 25.802 4.088 1.00 26.78 C ANISOU 3200 C5 U B 1 2561 3652 3961 286 -1028 -678 C ATOM 3201 C6 U B 1 45.704 24.475 4.082 1.00 26.80 C ANISOU 3201 C6 U B 1 2557 3654 3971 281 -999 -740 C ATOM 3202 P G B 2 40.890 21.926 2.954 1.00 26.81 P ANISOU 3202 P G B 2 2571 3841 3775 291 -837 -1013 P ATOM 3203 OP1 G B 2 40.076 20.875 2.378 1.00 26.39 O ANISOU 3203 OP1 G B 2 2496 3841 3690 294 -786 -1089 O ATOM 3204 OP2 G B 2 41.148 23.199 2.250 1.00 28.55 O ANISOU 3204 OP2 G B 2 2763 4109 3977 305 -844 -959 O ATOM 3205 O5' G B 2 40.294 22.312 4.432 1.00 26.07 O ANISOU 3205 O5' G B 2 2563 3667 3674 275 -882 -1001 O ATOM 3206 C5' G B 2 40.011 21.305 5.341 1.00 28.54 C ANISOU 3206 C5' G B 2 2917 3923 4006 260 -886 -1042 C ATOM 3207 C4' G B 2 39.093 21.773 6.446 1.00 28.21 C ANISOU 3207 C4' G B 2 2949 3834 3935 250 -916 -1040 C ATOM 3208 O4' G B 2 39.755 22.909 7.167 1.00 27.72 O ANISOU 3208 O4' G B 2 2921 3715 3897 245 -971 -965 O ATOM 3209 C3' G B 2 37.788 22.371 5.944 1.00 30.21 C ANISOU 3209 C3' G B 2 3207 4158 4112 260 -891 -1061 C ATOM 3210 O3' G B 2 36.916 21.296 5.772 1.00 27.63 O ANISOU 3210 O3' G B 2 2879 3859 3760 259 -852 -1135 O ATOM 3211 C2' G B 2 37.387 23.258 7.148 1.00 25.23 C ANISOU 3211 C2' G B 2 2651 3463 3471 250 -940 -1024 C ATOM 3212 O2' G B 2 36.841 22.483 8.225 1.00 29.64 O ANISOU 3212 O2' G B 2 3266 3960 4037 236 -950 -1062 O ATOM 3213 C1' G B 2 38.738 23.847 7.594 1.00 26.85 C ANISOU 3213 C1' G B 2 2859 3608 3735 244 -986 -953 C ATOM 3214 N9 G B 2 39.000 25.099 6.944 1.00 26.99 N ANISOU 3214 N9 G B 2 2852 3669 3736 256 -993 -900 N ATOM 3215 C8 G B 2 39.302 25.409 5.689 1.00 26.20 C ANISOU 3215 C8 G B 2 2687 3646 3623 273 -964 -890 C ATOM 3216 N7 G B 2 39.416 26.711 5.475 1.00 26.26 N ANISOU 3216 N7 G B 2 2692 3671 3613 280 -982 -835 N ATOM 3217 C5 G B 2 39.177 27.285 6.664 1.00 30.02 C ANISOU 3217 C5 G B 2 3237 4077 4090 267 -1025 -806 C ATOM 3218 C6 G B 2 39.158 28.635 7.098 1.00 29.12 C ANISOU 3218 C6 G B 2 3158 3942 3964 266 -1060 -747 C ATOM 3219 O6 G B 2 39.368 29.661 6.449 1.00 30.63 O ANISOU 3219 O6 G B 2 3322 4176 4139 278 -1060 -704 O ATOM 3220 N1 G B 2 38.849 28.777 8.463 1.00 25.04 N ANISOU 3220 N1 G B 2 2717 3344 3454 249 -1101 -737 N ATOM 3221 C2 G B 2 38.585 27.741 9.323 1.00 24.93 C ANISOU 3221 C2 G B 2 2741 3275 3457 235 -1106 -780 C ATOM 3222 N2 G B 2 38.307 28.048 10.562 1.00 24.72 N ANISOU 3222 N2 G B 2 2785 3174 3434 220 -1146 -764 N ATOM 3223 N3 G B 2 38.581 26.470 8.966 1.00 29.65 N ANISOU 3223 N3 G B 2 3308 3889 4067 236 -1074 -836 N ATOM 3224 C4 G B 2 38.899 26.297 7.591 1.00 31.15 C ANISOU 3224 C4 G B 2 3423 4161 4251 252 -1033 -847 C ATOM 3225 P U B 3 35.696 21.415 4.724 1.00 28.21 P ANISOU 3225 P U B 3 2924 4036 3759 273 -802 -1179 P ATOM 3226 OP1 U B 3 34.928 20.150 4.802 1.00 35.16 O ANISOU 3226 OP1 U B 3 3810 4923 4625 268 -768 -1256 O ATOM 3227 OP2 U B 3 36.249 21.868 3.429 1.00 28.17 O ANISOU 3227 OP2 U B 3 2850 4107 3749 290 -779 -1157 O ATOM 3228 O5' U B 3 34.840 22.590 5.310 1.00 28.15 O ANISOU 3228 O5' U B 3 2970 4018 3705 273 -829 -1148 O ATOM 3229 C5' U B 3 33.698 23.069 4.564 1.00 29.51 C ANISOU 3229 C5' U B 3 3131 4276 3807 285 -797 -1169 C ATOM 3230 C4' U B 3 32.422 22.876 5.359 1.00 30.69 C ANISOU 3230 C4' U B 3 3340 4402 3916 277 -798 -1207 C ATOM 3231 O4' U B 3 32.567 23.481 6.663 1.00 31.68 O ANISOU 3231 O4' U B 3 3535 4439 4063 265 -852 -1162 O ATOM 3232 C3' U B 3 31.193 23.527 4.775 1.00 31.38 C ANISOU 3232 C3' U B 3 3426 4567 3928 288 -772 -1220 C ATOM 3233 O3' U B 3 30.586 22.618 3.880 1.00 31.86 O ANISOU 3233 O3' U B 3 3445 4701 3959 294 -718 -1287 O ATOM 3234 C2' U B 3 30.323 23.661 6.009 1.00 32.27 C ANISOU 3234 C2' U B 3 3618 4619 4024 276 -798 -1225 C ATOM 3235 O2' U B 3 29.711 22.431 6.328 1.00 35.26 O ANISOU 3235 O2' U B 3 4012 4984 4400 268 -777 -1294 O ATOM 3236 C1' U B 3 31.337 24.013 7.086 1.00 33.03 C ANISOU 3236 C1' U B 3 3754 4616 4179 264 -854 -1170 C ATOM 3237 N1 U B 3 31.443 25.480 7.303 1.00 32.77 N ANISOU 3237 N1 U B 3 3744 4574 4133 268 -888 -1101 N ATOM 3238 C2 U B 3 30.650 26.050 8.277 1.00 31.23 C ANISOU 3238 C2 U B 3 3618 4336 3912 260 -914 -1088 C ATOM 3239 O2 U B 3 29.885 25.402 8.963 1.00 30.93 O ANISOU 3239 O2 U B 3 3623 4267 3863 252 -913 -1131 O ATOM 3240 N3 U B 3 30.777 27.409 8.421 1.00 28.47 N ANISOU 3240 N3 U B 3 3287 3980 3551 263 -942 -1024 N ATOM 3241 C4 U B 3 31.614 28.244 7.704 1.00 30.86 C ANISOU 3241 C4 U B 3 3545 4314 3865 273 -946 -972 C ATOM 3242 O4 U B 3 31.642 29.445 7.940 1.00 28.12 O ANISOU 3242 O4 U B 3 3222 3957 3507 275 -972 -917 O ATOM 3243 C5 U B 3 32.413 27.571 6.708 1.00 24.38 C ANISOU 3243 C5 U B 3 2653 3538 3073 281 -918 -989 C ATOM 3244 C6 U B 3 32.298 26.252 6.543 1.00 25.63 C ANISOU 3244 C6 U B 3 2792 3703 3241 278 -890 -1051 C ATOM 3245 P G B 4 29.928 23.182 2.545 1.00 29.28 P ANISOU 3245 P G B 4 3067 4490 3569 312 -676 -1295 P ATOM 3246 OP1 G B 4 29.884 22.078 1.564 1.00 26.63 O ANISOU 3246 OP1 G B 4 2673 4217 3229 317 -626 -1356 O ATOM 3247 OP2 G B 4 30.588 24.448 2.176 1.00 38.03 O ANISOU 3247 OP2 G B 4 4156 5614 4681 323 -697 -1223 O ATOM 3248 O5' G B 4 28.456 23.529 3.067 1.00 35.77 O ANISOU 3248 O5' G B 4 3943 5318 4329 310 -675 -1315 O ATOM 3249 C5' G B 4 27.741 22.564 3.803 1.00 29.13 C ANISOU 3249 C5' G B 4 3144 4439 3485 298 -670 -1370 C ATOM 3250 C4' G B 4 26.325 23.015 4.110 1.00 31.78 C ANISOU 3250 C4' G B 4 3524 4795 3757 299 -665 -1385 C ATOM 3251 O4' G B 4 26.375 24.091 5.089 1.00 33.25 O ANISOU 3251 O4' G B 4 3769 4917 3948 294 -714 -1324 O ATOM 3252 C3' G B 4 25.477 23.563 2.965 1.00 34.97 C ANISOU 3252 C3' G B 4 3888 5308 4092 314 -625 -1395 C ATOM 3253 O3' G B 4 24.854 22.509 2.221 1.00 33.19 O ANISOU 3253 O3' G B 4 3626 5147 3839 316 -575 -1468 O ATOM 3254 C2' G B 4 24.435 24.328 3.758 1.00 28.92 C ANISOU 3254 C2' G B 4 3187 4519 3282 312 -645 -1379 C ATOM 3255 O2' G B 4 23.575 23.427 4.395 1.00 33.89 O ANISOU 3255 O2' G B 4 3856 5121 3900 302 -637 -1436 O ATOM 3256 C1' G B 4 25.297 24.982 4.830 1.00 33.88 C ANISOU 3256 C1' G B 4 3862 5050 3961 303 -703 -1315 C ATOM 3257 N9 G B 4 25.855 26.262 4.442 1.00 31.11 N ANISOU 3257 N9 G B 4 3492 4719 3608 313 -719 -1246 N ATOM 3258 C8 G B 4 26.976 26.494 3.687 1.00 25.57 C ANISOU 3258 C8 G B 4 2734 4042 2939 321 -718 -1214 C ATOM 3259 N7 G B 4 27.204 27.776 3.515 1.00 24.22 N ANISOU 3259 N7 G B 4 2561 3884 2756 329 -735 -1152 N ATOM 3260 C5 G B 4 26.170 28.412 4.184 1.00 25.82 C ANISOU 3260 C5 G B 4 2823 4071 2917 327 -748 -1143 C ATOM 3261 C6 G B 4 25.884 29.793 4.355 1.00 34.33 C ANISOU 3261 C6 G B 4 3926 5152 3965 332 -767 -1086 C ATOM 3262 O6 G B 4 26.514 30.776 3.925 1.00 33.20 O ANISOU 3262 O6 G B 4 3759 5028 3829 342 -777 -1029 O ATOM 3263 N1 G B 4 24.723 30.001 5.117 1.00 25.80 N ANISOU 3263 N1 G B 4 2908 4050 2844 327 -774 -1098 N ATOM 3264 C2 G B 4 23.949 28.980 5.641 1.00 23.81 C ANISOU 3264 C2 G B 4 2688 3776 2582 317 -763 -1158 C ATOM 3265 N2 G B 4 22.886 29.328 6.332 1.00 23.03 N ANISOU 3265 N2 G B 4 2648 3658 2444 313 -772 -1161 N ATOM 3266 N3 G B 4 24.202 27.681 5.493 1.00 24.18 N ANISOU 3266 N3 G B 4 2711 3820 2656 311 -745 -1213 N ATOM 3267 C4 G B 4 25.329 27.484 4.755 1.00 24.97 C ANISOU 3267 C4 G B 4 2751 3941 2796 317 -738 -1201 C ATOM 3268 P C B 5 24.234 22.733 0.755 1.00 35.29 P ANISOU 3268 P C B 5 3827 5537 4043 333 -524 -1490 P ATOM 3269 OP1 C B 5 23.833 21.386 0.319 1.00 38.93 O ANISOU 3269 OP1 C B 5 4262 6033 4497 329 -481 -1568 O ATOM 3270 OP2 C B 5 25.102 23.595 -0.061 1.00 33.27 O ANISOU 3270 OP2 C B 5 3522 5321 3797 346 -526 -1436 O ATOM 3271 O5' C B 5 22.915 23.629 0.994 1.00 28.39 O ANISOU 3271 O5' C B 5 2995 4691 3101 337 -525 -1480 O ATOM 3272 C5' C B 5 21.833 23.151 1.710 1.00 27.56 C ANISOU 3272 C5' C B 5 2941 4561 2969 328 -522 -1523 C ATOM 3273 C4' C B 5 20.794 24.252 1.781 1.00 34.17 C ANISOU 3273 C4' C B 5 3808 5431 3743 335 -525 -1496 C ATOM 3274 O4' C B 5 21.228 25.291 2.693 1.00 26.07 O ANISOU 3274 O4' C B 5 2832 4332 2741 332 -576 -1427 O ATOM 3275 C3' C B 5 20.506 24.984 0.474 1.00 36.33 C ANISOU 3275 C3' C B 5 4024 5815 3966 353 -491 -1482 C ATOM 3276 O3' C B 5 19.527 24.302 -0.311 1.00 32.25 O ANISOU 3276 O3' C B 5 3475 5380 3398 357 -441 -1547 O ATOM 3277 C2' C B 5 19.921 26.285 0.997 1.00 28.19 C ANISOU 3277 C2' C B 5 3040 4771 2901 357 -516 -1429 C ATOM 3278 O2' C B 5 18.576 26.102 1.354 1.00 33.58 O ANISOU 3278 O2' C B 5 3762 5465 3532 353 -503 -1466 O ATOM 3279 C1' C B 5 20.752 26.538 2.251 1.00 33.05 C ANISOU 3279 C1' C B 5 3711 5270 3576 345 -572 -1384 C ATOM 3280 N1 C B 5 21.889 27.456 1.979 1.00 34.51 N ANISOU 3280 N1 C B 5 3871 5448 3794 352 -595 -1316 N ATOM 3281 C2 C B 5 21.677 28.830 2.126 1.00 32.52 C ANISOU 3281 C2 C B 5 3641 5199 3516 359 -614 -1255 C ATOM 3282 O2 C B 5 20.558 29.232 2.496 1.00 34.32 O ANISOU 3282 O2 C B 5 3912 5435 3695 359 -612 -1259 O ATOM 3283 N3 C B 5 22.697 29.682 1.862 1.00 34.93 N ANISOU 3283 N3 C B 5 3923 5499 3850 366 -634 -1193 N ATOM 3284 C4 C B 5 23.874 29.208 1.459 1.00 34.13 C ANISOU 3284 C4 C B 5 3776 5391 3801 366 -635 -1191 C ATOM 3285 N4 C B 5 24.842 30.099 1.209 1.00 24.88 N ANISOU 3285 N4 C B 5 2583 4214 2656 373 -655 -1128 N ATOM 3286 C5 C B 5 24.085 27.803 1.284 1.00 34.63 C ANISOU 3286 C5 C B 5 3816 5453 3890 359 -615 -1252 C ATOM 3287 C6 C B 5 23.085 26.966 1.552 1.00 31.15 C ANISOU 3287 C6 C B 5 3398 5016 3421 352 -595 -1314 C ATOM 3288 P C B 6 19.627 24.326 -1.900 1.00 31.90 P ANISOU 3288 P C B 6 3345 5452 3324 372 -394 -1561 P ATOM 3289 OP1 C B 6 18.692 23.318 -2.447 1.00 36.50 O ANISOU 3289 OP1 C B 6 3906 6098 3867 370 -348 -1639 O ATOM 3290 OP2 C B 6 21.044 24.245 -2.293 1.00 31.59 O ANISOU 3290 OP2 C B 6 3262 5399 3343 375 -403 -1534 O ATOM 3291 O5' C B 6 19.148 25.789 -2.282 1.00 37.27 O ANISOU 3291 O5' C B 6 4022 6185 3952 387 -396 -1506 O ATOM 3292 C5' C B 6 17.914 26.289 -1.826 1.00 29.15 C ANISOU 3292 C5' C B 6 3041 5164 2869 387 -397 -1506 C ATOM 3293 C4' C B 6 17.751 27.716 -2.315 1.00 32.29 C ANISOU 3293 C4' C B 6 3427 5614 3230 403 -398 -1445 C ATOM 3294 O4' C B 6 18.497 28.592 -1.436 1.00 34.63 O ANISOU 3294 O4' C B 6 3766 5826 3567 400 -448 -1377 O ATOM 3295 C3' C B 6 18.290 28.005 -3.718 1.00 33.35 C ANISOU 3295 C3' C B 6 3478 5839 3354 420 -367 -1433 C ATOM 3296 O3' C B 6 17.312 27.702 -4.704 1.00 31.66 O ANISOU 3296 O3' C B 6 3223 5730 3077 428 -317 -1481 O ATOM 3297 C2' C B 6 18.540 29.512 -3.622 1.00 41.11 C ANISOU 3297 C2' C B 6 4473 6817 4330 431 -392 -1353 C ATOM 3298 O2' C B 6 17.379 30.309 -3.775 1.00 42.15 O ANISOU 3298 O2' C B 6 4620 7002 4394 439 -377 -1341 O ATOM 3299 C1' C B 6 19.028 29.668 -2.187 1.00 38.69 C ANISOU 3299 C1' C B 6 4238 6387 4074 416 -447 -1320 C ATOM 3300 N1 C B 6 20.509 29.640 -2.140 1.00 39.87 N ANISOU 3300 N1 C B 6 4367 6487 4294 414 -473 -1286 N ATOM 3301 C2 C B 6 21.195 30.840 -2.320 1.00 43.26 C ANISOU 3301 C2 C B 6 4785 6917 4735 424 -493 -1214 C ATOM 3302 O2 C B 6 20.550 31.876 -2.503 1.00 49.40 O ANISOU 3302 O2 C B 6 5571 7734 5466 435 -488 -1181 O ATOM 3303 N3 C B 6 22.544 30.843 -2.286 1.00 39.99 N ANISOU 3303 N3 C B 6 4352 6459 4385 423 -517 -1182 N ATOM 3304 C4 C B 6 23.195 29.697 -2.087 1.00 42.68 C ANISOU 3304 C4 C B 6 4684 6758 4774 412 -520 -1219 C ATOM 3305 N4 C B 6 24.530 29.757 -2.063 1.00 44.59 N ANISOU 3305 N4 C B 6 4906 6958 5078 411 -544 -1183 N ATOM 3306 C5 C B 6 22.518 28.451 -1.905 1.00 38.87 C ANISOU 3306 C5 C B 6 4212 6274 4281 401 -498 -1293 C ATOM 3307 C6 C B 6 21.180 28.467 -1.943 1.00 35.66 C ANISOU 3307 C6 C B 6 3826 5912 3812 402 -475 -1325 C ATOM 3308 P A B 7 17.736 27.226 -6.168 1.00 34.75 P ANISOU 3308 P A B 7 3525 6217 3463 439 -273 -1510 P ATOM 3309 OP1 A B 7 19.151 26.816 -6.088 1.00 38.72 O ANISOU 3309 OP1 A B 7 4008 6665 4039 435 -293 -1496 O ATOM 3310 OP2 A B 7 17.312 28.223 -7.171 1.00 40.76 O ANISOU 3310 OP2 A B 7 4244 7076 4168 459 -247 -1480 O ATOM 3311 O5' A B 7 16.829 25.936 -6.426 1.00 33.56 O ANISOU 3311 O5' A B 7 3364 6105 3281 430 -233 -1598 O ATOM 3312 C5' A B 7 17.018 24.747 -5.680 1.00 31.91 C ANISOU 3312 C5' A B 7 3186 5825 3115 412 -243 -1644 C ATOM 3313 C4' A B 7 15.678 24.201 -5.220 1.00 31.95 C ANISOU 3313 C4' A B 7 3231 5832 3075 403 -228 -1698 C ATOM 3314 O4' A B 7 15.239 24.930 -4.051 1.00 34.77 O ANISOU 3314 O4' A B 7 3664 6119 3428 398 -268 -1659 O ATOM 3315 C3' A B 7 14.536 24.384 -6.207 1.00 30.56 C ANISOU 3315 C3' A B 7 3020 5772 2821 413 -183 -1726 C ATOM 3316 O3' A B 7 14.531 23.307 -7.100 1.00 30.61 O ANISOU 3316 O3' A B 7 2970 5839 2822 412 -140 -1790 O ATOM 3317 C2' A B 7 13.357 24.250 -5.273 1.00 29.96 C ANISOU 3317 C2' A B 7 3011 5660 2713 403 -191 -1750 C ATOM 3318 O2' A B 7 13.128 22.898 -4.947 1.00 32.80 O ANISOU 3318 O2' A B 7 3381 5991 3089 388 -179 -1819 O ATOM 3319 C1' A B 7 13.839 24.991 -4.033 1.00 29.48 C ANISOU 3319 C1' A B 7 3016 5493 2693 398 -247 -1688 C ATOM 3320 N9 A B 7 13.386 26.383 -4.036 1.00 32.00 N ANISOU 3320 N9 A B 7 3351 5837 2970 410 -257 -1628 N ATOM 3321 C8 A B 7 14.077 27.497 -4.435 1.00 33.17 C ANISOU 3321 C8 A B 7 3475 6001 3126 424 -270 -1561 C ATOM 3322 N7 A B 7 13.400 28.601 -4.337 1.00 33.22 N ANISOU 3322 N7 A B 7 3505 6029 3087 432 -275 -1519 N ATOM 3323 C5 A B 7 12.173 28.182 -3.836 1.00 28.34 C ANISOU 3323 C5 A B 7 2930 5409 2430 424 -265 -1561 C ATOM 3324 C6 A B 7 11.003 28.882 -3.506 1.00 27.64 C ANISOU 3324 C6 A B 7 2882 5336 2284 427 -264 -1547 C ATOM 3325 N6 A B 7 10.914 30.202 -3.654 1.00 24.12 N ANISOU 3325 N6 A B 7 2438 4912 1812 440 -272 -1483 N ATOM 3326 N1 A B 7 9.952 28.180 -3.038 1.00 28.64 N ANISOU 3326 N1 A B 7 3045 5454 2383 417 -253 -1599 N ATOM 3327 C2 A B 7 10.067 26.856 -2.912 1.00 28.98 C ANISOU 3327 C2 A B 7 3083 5474 2453 405 -244 -1663 C ATOM 3328 N3 A B 7 11.123 26.096 -3.183 1.00 32.13 N ANISOU 3328 N3 A B 7 3446 5856 2906 400 -244 -1682 N ATOM 3329 C4 A B 7 12.146 26.822 -3.643 1.00 33.10 C ANISOU 3329 C4 A B 7 3534 5988 3055 411 -255 -1629 C ATOM 3330 P U B 8 14.256 23.534 -8.641 1.00 39.57 P ANISOU 3330 P U B 8 4026 7104 3903 428 -92 -1802 P ATOM 3331 OP1 U B 8 14.439 22.228 -9.300 1.00 41.79 O ANISOU 3331 OP1 U B 8 4261 7421 4197 421 -56 -1872 O ATOM 3332 OP2 U B 8 14.917 24.737 -9.162 1.00 37.73 O ANISOU 3332 OP2 U B 8 3763 6899 3672 445 -103 -1732 O ATOM 3333 O5' U B 8 12.710 23.894 -8.607 1.00 44.32 O ANISOU 3333 O5' U B 8 4654 7759 4428 429 -74 -1819 O ATOM 3334 C5' U B 8 12.135 24.267 -9.812 1.00 42.52 C ANISOU 3334 C5' U B 8 4370 7648 4139 443 -34 -1826 C ATOM 3335 C4' U B 8 10.912 23.413 -10.042 1.00 38.58 C ANISOU 3335 C4' U B 8 3870 7202 3588 435 4 -1900 C ATOM 3336 O4' U B 8 9.860 23.829 -9.141 1.00 35.32 O ANISOU 3336 O4' U B 8 3523 6757 3142 431 -13 -1892 O ATOM 3337 C3' U B 8 10.350 23.569 -11.441 1.00 39.82 C ANISOU 3337 C3' U B 8 3957 7491 3681 448 53 -1920 C ATOM 3338 O3' U B 8 10.985 22.576 -12.236 1.00 51.62 O ANISOU 3338 O3' U B 8 5394 9019 5201 445 81 -1967 O ATOM 3339 C2' U B 8 8.892 23.232 -11.205 1.00 43.02 C ANISOU 3339 C2' U B 8 4392 7925 4027 441 72 -1967 C ATOM 3340 O2' U B 8 8.739 21.832 -11.092 1.00 51.60 O ANISOU 3340 O2' U B 8 5480 8997 5131 424 90 -2043 O ATOM 3341 C1' U B 8 8.632 23.817 -9.825 1.00 33.31 C ANISOU 3341 C1' U B 8 3246 6597 2811 435 27 -1926 C ATOM 3342 N1 U B 8 7.969 25.164 -9.758 1.00 34.74 N ANISOU 3342 N1 U B 8 3449 6808 2944 448 18 -1868 N ATOM 3343 C2 U B 8 6.587 25.191 -9.799 1.00 31.65 C ANISOU 3343 C2 U B 8 3056 6456 2512 444 33 -1877 C ATOM 3344 O2 U B 8 5.911 24.196 -9.894 1.00 33.48 O ANISOU 3344 O2 U B 8 3266 6700 2756 430 49 -1922 O ATOM 3345 N3 U B 8 6.017 26.426 -9.703 1.00 34.12 N ANISOU 3345 N3 U B 8 3386 6788 2790 456 24 -1818 N ATOM 3346 C4 U B 8 6.673 27.634 -9.581 1.00 36.55 C ANISOU 3346 C4 U B 8 3720 7086 3082 472 5 -1762 C ATOM 3347 O4 U B 8 5.979 28.648 -9.520 1.00 33.13 O ANISOU 3347 O4 U B 8 3297 6673 2616 480 1 -1712 O ATOM 3348 C5 U B 8 8.120 27.554 -9.547 1.00 29.62 C ANISOU 3348 C5 U B 8 2824 6155 2274 471 -18 -1737 C ATOM 3349 C6 U B 8 8.697 26.339 -9.630 1.00 35.44 C ANISOU 3349 C6 U B 8 3542 6871 3054 460 -11 -1790 C ATOM 3350 P A B 9 11.163 22.766 -13.813 1.00 70.11 P ANISOU 3350 P A B 9 7647 11482 7509 461 123 -1971 P ATOM 3351 OP1 A B 9 12.137 21.757 -14.268 1.00 72.69 O ANISOU 3351 OP1 A B 9 7931 11801 7885 456 137 -2007 O ATOM 3352 OP2 A B 9 11.348 24.199 -14.145 1.00 65.86 O ANISOU 3352 OP2 A B 9 7095 10976 6951 481 111 -1895 O ATOM 3353 O5' A B 9 9.724 22.297 -14.311 1.00 81.02 O ANISOU 3353 O5' A B 9 9017 12951 8815 458 167 -2034 O ATOM 3354 C5' A B 9 9.278 20.981 -14.002 1.00 75.85 C ANISOU 3354 C5' A B 9 8378 12275 8165 439 183 -2110 C ATOM 3355 C4' A B 9 8.414 20.523 -15.150 1.00 73.88 C ANISOU 3355 C4' A B 9 8056 12132 7883 432 218 -2143 C ATOM 3356 O4' A B 9 7.208 21.321 -15.152 1.00 71.28 O ANISOU 3356 O4' A B 9 7730 11842 7512 433 209 -2107 O ATOM 3357 C3' A B 9 9.094 20.762 -16.490 1.00 79.10 C ANISOU 3357 C3' A B 9 8645 12886 8525 451 252 -2142 C ATOM 3358 O3' A B 9 9.651 19.545 -16.955 1.00 89.76 O ANISOU 3358 O3' A B 9 9958 14242 9906 440 275 -2200 O ATOM 3359 C2' A B 9 7.977 21.200 -17.415 1.00 74.24 C ANISOU 3359 C2' A B 9 7977 12374 7857 451 266 -2130 C ATOM 3360 O2' A B 9 7.506 20.064 -18.107 1.00 77.91 O ANISOU 3360 O2' A B 9 8392 12890 8322 431 288 -2190 O ATOM 3361 C1' A B 9 6.910 21.754 -16.464 1.00 72.37 C ANISOU 3361 C1' A B 9 7796 12095 7605 444 236 -2098 C ATOM 3362 N9 A B 9 6.784 23.212 -16.446 1.00 64.77 N ANISOU 3362 N9 A B 9 6847 11153 6608 465 225 -2029 N ATOM 3363 C8 A B 9 7.732 24.137 -16.115 1.00 61.90 C ANISOU 3363 C8 A B 9 6515 10754 6250 485 212 -1982 C ATOM 3364 N7 A B 9 7.316 25.378 -16.191 1.00 57.45 N ANISOU 3364 N7 A B 9 5957 10221 5650 500 205 -1924 N ATOM 3365 C5 A B 9 6.004 25.258 -16.601 1.00 55.42 C ANISOU 3365 C5 A B 9 5671 10025 5363 489 213 -1933 C ATOM 3366 C6 A B 9 5.001 26.203 -16.869 1.00 55.75 C ANISOU 3366 C6 A B 9 5701 10122 5361 496 211 -1890 C ATOM 3367 N6 A B 9 5.185 27.519 -16.758 1.00 54.79 N ANISOU 3367 N6 A B 9 5598 10003 5218 517 202 -1825 N ATOM 3368 N1 A B 9 3.790 25.746 -17.254 1.00 62.02 N ANISOU 3368 N1 A B 9 6464 10969 6134 481 220 -1916 N ATOM 3369 C2 A B 9 3.596 24.429 -17.367 1.00 64.81 C ANISOU 3369 C2 A B 9 6797 11319 6507 460 230 -1981 C ATOM 3370 N3 A B 9 4.467 23.448 -17.139 1.00 66.97 N ANISOU 3370 N3 A B 9 7079 11543 6823 451 234 -2026 N ATOM 3371 C4 A B 9 5.659 23.934 -16.757 1.00 62.44 C ANISOU 3371 C4 A B 9 6537 10918 6270 467 224 -1998 C TER 3372 A B 9 HETATM 3373 O HOH A 1 -2.714 46.423 -1.098 1.00 34.06 O HETATM 3374 O HOH A 3 13.250 32.200 -0.463 1.00 28.51 O HETATM 3375 O HOH A 4 48.021 22.871 9.748 1.00 43.47 O HETATM 3376 O HOH A 5 21.046 41.454 9.998 1.00 21.47 O HETATM 3377 O HOH A 6 -6.739 40.711 -2.815 1.00 34.28 O HETATM 3378 O HOH A 7 33.329 45.436 11.486 1.00 32.21 O HETATM 3379 O HOH A 8 16.798 30.547 0.814 1.00 21.54 O HETATM 3380 O HOH A 9 40.048 32.074 7.140 1.00 26.82 O HETATM 3381 O HOH A 10 1.684 17.589 -5.034 1.00 30.48 O HETATM 3382 O HOH A 11 55.187 30.833 26.263 1.00 26.73 O HETATM 3383 O HOH A 13 1.767 16.850 -9.591 1.00 29.79 O HETATM 3384 O HOH A 14 -13.605 44.398 1.478 1.00 50.89 O HETATM 3385 O HOH A 15 14.316 52.659 17.217 1.00 46.99 O HETATM 3386 O HOH A 16 12.226 18.921 3.775 1.00 39.97 O HETATM 3387 O HOH A 17 23.999 35.048 3.665 1.00 42.13 O HETATM 3388 O HOH A 18 13.530 41.210 2.530 1.00 44.79 O HETATM 3389 O HOH A 19 -15.294 39.142 -15.234 1.00 49.28 O HETATM 3390 O HOH A 20 18.920 35.311 4.680 1.00 24.36 O HETATM 3391 O HOH A 21 8.242 42.720 6.735 1.00 33.29 O HETATM 3392 O HOH A 22 45.241 19.306 14.396 1.00 34.72 O HETATM 3393 O HOH A 23 -16.737 34.872 -1.202 1.00 45.24 O HETATM 3394 O HOH A 24 39.643 27.708 25.968 1.00 31.05 O HETATM 3395 O HOH A 25 -13.686 23.556 -19.098 1.00 22.51 O HETATM 3396 O HOH A 26 -16.050 25.348 -2.991 1.00 33.46 O HETATM 3397 O HOH A 27 66.432 29.038 13.906 1.00 48.85 O HETATM 3398 O HOH A 29 54.714 18.568 18.400 1.00 29.95 O HETATM 3399 O HOH A 30 30.598 27.888 3.933 1.00 37.37 O HETATM 3400 O HOH A 31 27.443 22.730 7.704 1.00 32.97 O HETATM 3401 O HOH A 32 1.408 18.733 1.446 1.00 36.92 O HETATM 3402 O HOH A 33 -12.217 42.747 -17.870 1.00 39.14 O HETATM 3403 O HOH A 34 16.528 51.256 10.065 1.00 29.64 O HETATM 3404 O HOH A 35 -23.689 42.092 -3.687 1.00 52.93 O HETATM 3405 O HOH A 36 62.503 28.840 6.718 1.00 51.76 O HETATM 3406 O HOH A 37 -4.347 38.371 -19.732 1.00 33.93 O HETATM 3407 O HOH A 38 8.292 44.730 8.901 1.00 39.62 O HETATM 3408 O HOH A 39 42.313 21.682 8.262 1.00 33.59 O HETATM 3409 O HOH A 40 -11.972 44.350 -2.058 1.00 42.63 O HETATM 3410 O HOH A 41 2.352 31.490 -13.938 1.00 33.88 O HETATM 3411 O HOH A 42 -15.466 31.711 0.850 1.00 49.58 O HETATM 3412 O HOH A 44 22.976 45.374 8.274 1.00 31.86 O HETATM 3413 O HOH A 45 48.443 34.968 7.310 1.00 39.56 O HETATM 3414 O HOH A 46 41.180 19.076 8.779 1.00 39.58 O HETATM 3415 O HOH A 49 -1.308 36.897 -14.826 1.00 37.89 O HETATM 3416 O HOH A 55 -2.456 39.835 -18.291 1.00 49.08 O HETATM 3417 O HOH A 56 -15.230 22.339 -3.319 1.00 43.92 O HETATM 3418 O HOH A 58 -6.070 46.149 -9.340 1.00 39.90 O HETATM 3419 O HOH A 59 28.389 45.465 8.483 1.00 43.19 O HETATM 3420 O HOH A 60 13.091 36.676 2.356 1.00 44.33 O HETATM 3421 O HOH A 61 48.651 24.137 6.597 1.00 27.60 O HETATM 3422 O HOH A 62 32.168 23.481 16.312 1.00 30.16 O HETATM 3423 O HOH A 63 22.270 25.690 5.633 1.00 26.53 O HETATM 3424 O HOH A 64 11.052 23.394 -3.349 1.00 36.07 O HETATM 3425 O HOH A 65 14.663 24.792 -0.723 1.00 27.26 O HETATM 3426 O HOH A 67 35.862 31.717 8.100 1.00 45.31 O HETATM 3427 O HOH A 68 25.027 50.698 9.077 1.00 39.60 O HETATM 3428 O HOH A 69 -13.017 23.366 -12.598 1.00 28.16 O HETATM 3429 O HOH A 70 61.491 25.346 14.174 1.00 28.84 O HETATM 3430 O HOH A 71 27.617 33.046 20.448 1.00 47.07 O HETATM 3431 O HOH A 72 50.535 27.955 10.762 1.00 29.59 O HETATM 3432 O HOH A 73 42.525 32.618 8.031 1.00 41.25 O HETATM 3433 O HOH A 75 26.886 19.934 7.285 1.00 38.65 O HETATM 3434 O HOH A 77 4.250 45.834 11.701 1.00 30.56 O HETATM 3435 O HOH A 78 22.673 20.005 13.396 1.00 30.03 O HETATM 3436 O HOH A 79 -5.825 12.021 -20.101 1.00 51.41 O HETATM 3437 O HOH A 80 -16.038 31.859 -23.630 1.00 34.89 O HETATM 3438 O HOH A 81 38.342 43.827 15.354 1.00 29.03 O HETATM 3439 O HOH A 82 27.009 33.770 7.870 1.00 32.30 O HETATM 3440 O HOH A 83 11.946 27.342 -7.474 1.00 37.00 O HETATM 3441 O HOH A 84 48.233 31.924 26.464 1.00 32.69 O HETATM 3442 O HOH A 85 9.589 22.806 -5.825 1.00 44.22 O HETATM 3443 O HOH A 86 52.055 33.907 23.610 1.00 31.66 O HETATM 3444 O HOH A 87 -12.951 20.494 -15.735 1.00 39.52 O HETATM 3445 O HOH A 89 48.600 30.041 11.453 1.00 31.64 O HETATM 3446 O HOH A 90 10.671 33.220 -0.848 1.00 36.72 O HETATM 3447 O HOH A 91 57.047 48.967 3.880 1.00 53.10 O HETATM 3448 O HOH A 92 50.030 21.957 4.981 1.00 42.99 O HETATM 3449 O HOH A 93 50.279 31.613 23.892 1.00 31.66 O HETATM 3450 O HOH A 95 4.198 43.807 20.022 1.00 37.79 O HETATM 3451 O HOH A 96 19.607 46.512 14.499 1.00 37.33 O HETATM 3452 O HOH A 97 48.421 47.290 24.117 1.00 43.03 O HETATM 3453 O HOH A 98 62.805 27.368 13.321 1.00 33.04 O HETATM 3454 O HOH A 99 14.011 45.301 5.439 1.00 37.92 O HETATM 3455 O HOH A 100 -11.953 33.148 -6.297 1.00 38.45 O HETATM 3456 O HOH A 101 4.963 56.157 14.452 1.00 34.85 O HETATM 3457 O HOH A 102 55.459 25.321 17.991 1.00 37.09 O HETATM 3458 O HOH A 104 12.870 54.517 10.405 1.00 41.48 O HETATM 3459 O HOH A 106 5.633 31.704 -6.464 1.00 34.65 O HETATM 3460 O HOH A 107 9.431 44.198 4.530 1.00 43.47 O HETATM 3461 O HOH A 108 16.577 44.840 6.852 1.00 39.16 O HETATM 3462 O HOH A 109 -16.291 36.615 -10.878 1.00 38.02 O HETATM 3463 O HOH A 110 -18.699 24.749 -19.260 1.00 39.73 O HETATM 3464 O HOH A 111 16.244 19.492 12.694 1.00 44.78 O HETATM 3465 O HOH A 112 3.765 41.881 22.458 1.00 43.67 O HETATM 3466 O HOH A 113 33.329 39.454 7.689 1.00 35.08 O HETATM 3467 O HOH A 114 19.225 19.785 8.318 1.00 39.20 O HETATM 3468 O HOH A 115 55.863 25.041 30.999 1.00 34.38 O HETATM 3469 O HOH A 116 49.622 29.247 26.847 1.00 35.24 O HETATM 3470 O HOH A 117 7.906 43.996 19.517 1.00 52.41 O HETATM 3471 O HOH A 118 22.952 49.537 6.899 1.00 38.74 O HETATM 3472 O HOH A 119 -12.184 26.083 -9.232 1.00 39.58 O HETATM 3473 O HOH A 120 -16.855 26.944 -27.578 1.00 46.84 O HETATM 3474 O HOH A 122 48.405 26.490 26.851 1.00 39.75 O HETATM 3475 O HOH A 123 55.065 48.971 5.860 1.00 49.08 O HETATM 3476 O HOH A 124 53.005 41.100 28.138 1.00 41.57 O HETATM 3477 O HOH A 125 51.920 34.170 -3.065 1.00 41.71 O HETATM 3478 O HOH A 127 24.080 47.668 18.184 1.00 38.75 O HETATM 3479 O HOH A 128 22.055 31.276 8.099 1.00 40.56 O HETATM 3480 O HOH A 129 53.232 48.720 23.304 1.00 40.95 O HETATM 3481 O HOH A 130 -16.804 20.331 -27.099 1.00 53.72 O HETATM 3482 O HOH A 132 40.895 43.753 9.444 1.00 44.00 O HETATM 3483 O HOH A 133 8.339 17.661 -1.083 1.00 40.66 O HETATM 3484 O HOH A 134 -16.137 44.149 -5.679 1.00 40.36 O HETATM 3485 O HOH A 135 -2.203 17.135 -8.489 1.00 44.39 O HETATM 3486 O HOH A 136 -1.941 25.615 15.928 1.00 42.13 O HETATM 3487 O HOH A 137 36.866 24.648 10.070 1.00 37.78 O HETATM 3488 O HOH A 138 -7.850 31.284 -27.890 1.00 45.31 O HETATM 3489 O HOH A 139 -14.417 33.036 -8.066 1.00 48.00 O HETATM 3490 O HOH A 140 1.033 23.775 -26.297 1.00 41.50 O HETATM 3491 O HOH A 141 19.886 20.120 -0.561 1.00 47.53 O HETATM 3492 O HOH A 142 11.432 36.851 -0.791 1.00 45.35 O HETATM 3493 O HOH A 143 59.731 40.885 17.229 1.00 47.62 O HETATM 3494 O HOH A 145 -18.633 38.259 -17.864 1.00 39.02 O HETATM 3495 O HOH A 146 -11.142 31.702 -27.342 1.00 37.76 O HETATM 3496 O HOH A 147 52.948 48.478 4.046 1.00 48.92 O HETATM 3497 O HOH A 148 35.661 26.251 5.395 1.00 35.78 O HETATM 3498 O HOH A 149 15.150 39.427 5.495 1.00 40.32 O HETATM 3499 O HOH A 151 48.492 21.599 17.329 1.00 32.74 O HETATM 3500 O HOH A 152 2.961 28.668 -22.592 1.00 38.86 O HETATM 3501 O HOH A 153 37.097 28.313 30.239 1.00 39.93 O HETATM 3502 O HOH A 155 -3.906 43.589 -9.911 1.00 40.35 O HETATM 3503 O HOH A 156 19.058 47.563 17.039 1.00 45.59 O HETATM 3504 O HOH A 157 51.681 22.126 18.326 1.00 34.25 O HETATM 3505 O HOH A 158 40.276 36.105 28.582 1.00 39.93 O HETATM 3506 O HOH A 159 -8.972 42.833 -19.991 1.00 48.31 O HETATM 3507 O HOH A 161 -14.915 14.061 -25.999 1.00 47.44 O HETATM 3508 O HOH A 162 -0.647 15.938 -26.903 1.00 46.67 O HETATM 3509 O HOH A 576 27.137 19.981 14.724 1.00 42.71 O HETATM 3510 O HOH A 577 14.197 12.670 -2.831 1.00 41.86 O HETATM 3511 O HOH A 578 59.702 18.635 31.309 1.00 49.38 O HETATM 3512 O HOH A 579 42.763 35.413 7.340 1.00 46.44 O HETATM 3513 O HOH A 580 41.085 58.154 9.259 1.00 51.32 O HETATM 3514 O HOH A 581 -17.763 28.406 -16.449 1.00 42.03 O HETATM 3515 O HOH A 582 9.349 27.898 -12.969 1.00 37.10 O HETATM 3516 O HOH A 583 -2.676 13.477 -24.736 1.00 42.55 O HETATM 3517 O HOH A 584 39.738 59.115 18.014 1.00 41.12 O HETATM 3518 O HOH A 585 4.164 44.914 3.554 1.00 42.56 O HETATM 3519 O HOH A 586 -20.461 28.466 -22.098 1.00 42.97 O HETATM 3520 O HOH A 587 41.915 32.981 29.788 1.00 45.08 O HETATM 3521 O HOH A 588 -3.633 24.317 -29.780 1.00 49.28 O HETATM 3522 O HOH A 589 17.814 36.018 29.855 1.00 48.29 O HETATM 3523 O HOH A 590 56.670 27.590 29.813 1.00 37.18 O HETATM 3524 O HOH A 591 10.346 56.993 9.054 1.00 46.77 O HETATM 3525 O HOH A 592 1.455 15.382 -19.265 1.00 46.16 O HETATM 3526 O HOH A 593 -16.644 23.183 -26.564 1.00 48.60 O HETATM 3527 O HOH A 594 9.527 33.241 23.179 1.00 44.71 O HETATM 3528 O HOH A 595 33.535 38.601 29.395 1.00 46.53 O HETATM 3529 O HOH A 596 53.877 48.900 20.267 1.00 48.05 O HETATM 3530 O HOH A 597 25.791 29.797 25.916 1.00 54.42 O HETATM 3531 O HOH A 598 -17.429 24.314 -16.957 1.00 51.63 O HETATM 3532 O HOH A 599 -13.582 10.284 -32.510 1.00 51.32 O HETATM 3533 O HOH A 600 31.224 21.043 21.996 1.00 52.89 O HETATM 3534 O HOH A 601 60.418 35.482 9.196 1.00 47.35 O HETATM 3535 O HOH A 602 2.448 31.246 -16.701 1.00 42.91 O HETATM 3536 O HOH A 603 6.943 18.401 2.703 1.00 38.32 O HETATM 3537 O HOH A 604 -0.090 40.512 -9.449 1.00 43.60 O HETATM 3538 O HOH A 605 16.787 53.938 10.367 1.00 34.84 O HETATM 3539 O HOH A 606 -2.210 41.489 -11.122 1.00 35.29 O HETATM 3540 O HOH A 607 -6.012 40.591 -17.390 1.00 43.84 O HETATM 3541 O HOH A 608 31.380 46.587 17.901 1.00 38.88 O HETATM 3542 O HOH A 609 34.068 46.962 14.663 1.00 46.06 O HETATM 3543 O HOH A 610 1.848 38.494 15.566 1.00 44.72 O HETATM 3544 O HOH A 611 36.078 29.022 4.672 1.00 52.45 O HETATM 3545 O HOH A 612 41.214 25.286 26.280 1.00 50.58 O HETATM 3546 O HOH A 613 6.141 35.038 -8.402 1.00 49.64 O HETATM 3547 O HOH A 614 7.655 56.777 19.223 1.00 48.76 O HETATM 3548 O HOH A 615 20.730 43.047 7.751 1.00 47.13 O HETATM 3549 O HOH A 616 -3.441 24.557 8.426 1.00 52.05 O HETATM 3550 O HOH A 617 -7.224 33.167 8.134 1.00 47.93 O HETATM 3551 O HOH A 618 5.278 17.593 -1.704 1.00 42.42 O HETATM 3552 O HOH A 619 9.368 34.184 -4.961 1.00 55.21 O HETATM 3553 O HOH A 620 6.476 46.756 10.109 1.00 40.22 O HETATM 3554 O HOH A 621 39.757 50.379 25.042 1.00 49.54 O HETATM 3555 O HOH A 622 26.481 37.798 6.667 1.00 54.08 O HETATM 3556 O HOH A 623 32.340 49.352 22.345 1.00 52.93 O HETATM 3557 O HOH A 624 21.809 21.532 18.527 1.00 45.08 O HETATM 3558 O HOH A 625 17.438 16.739 22.302 1.00 49.56 O HETATM 3559 O HOH A 626 60.527 47.838 7.567 1.00 53.86 O HETATM 3560 O HOH A 627 -1.506 47.937 1.273 1.00 38.05 O HETATM 3561 O HOH A 628 28.744 36.466 8.023 1.00 42.63 O HETATM 3562 O HOH A 629 50.296 17.933 34.236 1.00 53.05 O HETATM 3563 O HOH A 630 56.539 28.777 23.528 1.00 47.41 O HETATM 3564 O HOH A 631 7.188 45.503 2.923 1.00 45.72 O HETATM 3565 O HOH A 632 -5.380 22.260 7.981 1.00 43.72 O HETATM 3566 O HOH A 633 36.561 35.131 7.409 1.00 49.59 O HETATM 3567 O HOH A 634 11.540 25.379 25.396 1.00 48.39 O HETATM 3568 O HOH A 635 2.623 20.133 18.952 1.00 55.72 O HETATM 3569 O HOH A 636 42.082 18.766 19.401 1.00 52.37 O HETATM 3570 O HOH A 637 26.355 22.103 19.289 1.00 42.31 O HETATM 3571 O HOH A 638 40.380 30.546 30.186 1.00 47.35 O HETATM 3572 O HOH A 639 -11.735 17.530 -11.031 1.00 42.38 O HETATM 3573 O HOH A 640 39.934 18.678 16.519 1.00 51.16 O HETATM 3574 O HOH A 641 39.675 19.623 20.766 1.00 51.96 O HETATM 3575 O HOH A 642 50.176 42.988 24.793 1.00 46.58 O HETATM 3576 O HOH A 643 -0.183 35.384 -8.741 1.00 32.01 O HETATM 3577 O HOH A 644 10.755 39.089 26.796 1.00 49.34 O HETATM 3578 O HOH A 645 18.361 40.721 24.185 1.00 50.46 O HETATM 3579 O HOH A 646 6.552 34.394 -5.675 1.00 47.34 O HETATM 3580 O HOH A 647 42.491 25.739 2.976 1.00 44.28 O HETATM 3581 O HOH A 648 18.959 53.410 2.320 1.00 48.23 O HETATM 3582 O HOH A 649 6.884 20.993 19.843 1.00 49.87 O HETATM 3583 O HOH A 650 58.937 29.716 3.736 1.00 46.34 O HETATM 3584 O HOH A 651 -5.360 15.053 -18.112 1.00 43.15 O HETATM 3585 O HOH A 652 36.926 58.044 18.711 1.00 49.95 O HETATM 3586 O HOH A 653 40.976 45.829 27.033 1.00 51.62 O HETATM 3587 O HOH A 654 -13.520 22.303 -33.399 1.00 54.30 O HETATM 3588 O HOH A 655 12.758 35.792 24.773 1.00 52.26 O HETATM 3589 O HOH A 656 -12.760 36.130 -28.124 1.00 45.06 O HETATM 3590 O HOH A 657 8.017 19.557 14.114 1.00 53.44 O HETATM 3591 O HOH A 658 51.780 30.809 -0.313 1.00 56.14 O HETATM 3592 O HOH A 659 47.942 44.767 25.194 1.00 49.78 O HETATM 3593 O HOH A 660 -6.749 20.036 14.089 1.00 49.93 O HETATM 3594 O HOH A 661 35.292 19.701 15.772 1.00 36.04 O HETATM 3595 O HOH A 662 4.355 37.195 -8.662 1.00 44.77 O HETATM 3596 O HOH A 663 14.805 44.277 2.176 1.00 51.52 O HETATM 3597 O HOH A 664 -3.539 21.720 5.979 1.00 45.42 O HETATM 3598 O HOH A 665 15.156 19.631 7.312 1.00 39.11 O HETATM 3599 O HOH A 666 -13.768 23.116 -15.315 1.00 33.51 O HETATM 3600 O HOH A 667 13.343 51.461 19.587 1.00 50.44 O HETATM 3601 O HOH A 668 23.702 20.573 4.339 1.00 46.53 O HETATM 3602 O HOH A 669 -12.673 26.951 2.236 1.00 51.38 O HETATM 3603 O HOH A 670 -16.088 21.342 -7.225 1.00 53.00 O HETATM 3604 O HOH A 671 -14.087 21.029 -1.047 1.00 40.79 O HETATM 3605 O HOH A 672 40.620 52.559 6.951 1.00 48.52 O HETATM 3606 O HOH A 673 50.816 42.644 27.536 1.00 49.50 O HETATM 3607 O HOH A 674 9.655 20.889 20.526 1.00 46.81 O HETATM 3608 O HOH A 675 51.104 41.811 4.364 1.00 46.69 O HETATM 3609 O HOH A 676 59.682 50.316 7.088 1.00 46.84 O HETATM 3610 O HOH A 677 -18.048 26.232 -14.781 1.00 46.86 O HETATM 3611 O HOH A 678 44.148 31.799 5.150 1.00 52.03 O HETATM 3612 O HOH A 679 11.515 17.755 6.204 1.00 52.95 O HETATM 3613 O HOH A 680 8.144 46.658 12.493 1.00 41.45 O HETATM 3614 O HOH A 681 22.902 47.158 5.028 1.00 54.78 O HETATM 3615 O HOH A 682 4.718 47.638 3.733 1.00 48.16 O HETATM 3616 O HOH A 683 3.829 32.272 19.001 1.00 46.07 O HETATM 3617 O HOH A 684 -14.399 46.004 -7.148 1.00 47.63 O HETATM 3618 O HOH A 685 57.223 44.160 11.202 1.00 39.79 O HETATM 3619 O HOH A 686 -1.766 19.906 8.858 1.00 51.87 O HETATM 3620 O HOH A 687 9.269 46.485 6.137 1.00 41.27 O HETATM 3621 O HOH A 688 24.740 32.785 5.974 1.00 49.18 O HETATM 3622 O HOH A 689 45.481 27.207 31.252 1.00 47.63 O HETATM 3623 O HOH A 690 33.032 48.672 11.721 1.00 51.64 O HETATM 3624 O HOH A 691 21.030 39.650 25.401 1.00 54.54 O HETATM 3625 O HOH A 692 21.799 37.292 3.147 1.00 46.17 O HETATM 3626 O HOH A 693 61.850 33.094 6.790 1.00 55.58 O HETATM 3627 O HOH A 694 26.164 24.842 25.888 1.00 45.91 O HETATM 3628 O HOH A 695 43.231 17.623 16.010 1.00 52.41 O HETATM 3629 O HOH A 696 2.973 37.172 19.301 1.00 55.00 O HETATM 3630 O HOH A 697 29.796 33.114 6.786 1.00 42.61 O HETATM 3631 O HOH A 698 31.104 44.780 8.494 1.00 54.88 O HETATM 3632 O HOH A 699 -0.577 15.638 -13.735 1.00 49.76 O HETATM 3633 O HOH A 700 16.037 42.613 4.456 1.00 45.12 O HETATM 3634 O HOH A 701 7.205 50.737 23.400 1.00 53.98 O HETATM 3635 O HOH A 702 39.947 59.988 24.831 1.00 48.75 O HETATM 3636 O HOH A 703 28.246 29.410 27.822 1.00 51.90 O HETATM 3637 O HOH A 704 26.148 47.207 8.167 1.00 56.20 O HETATM 3638 O HOH A 705 -5.090 27.960 -40.507 1.00 51.68 O HETATM 3639 O HOH A 706 5.432 30.619 21.206 1.00 54.51 O HETATM 3640 O HOH A 707 13.637 17.501 8.568 1.00 50.04 O HETATM 3641 O HOH A 708 -14.750 14.174 -21.242 1.00 53.02 O HETATM 3642 O HOH B 10 24.993 33.038 1.638 1.00 35.79 O HETATM 3643 O HOH B 12 6.857 31.362 -8.894 1.00 32.66 O HETATM 3644 O HOH B 43 41.766 29.803 3.959 1.00 42.33 O HETATM 3645 O HOH B 47 48.448 21.828 2.498 1.00 35.75 O HETATM 3646 O HOH B 66 29.032 29.393 2.314 1.00 43.97 O HETATM 3647 O HOH B 74 6.482 22.045 -12.666 1.00 45.38 O HETATM 3648 O HOH B 76 40.262 27.610 3.046 1.00 35.98 O HETATM 3649 O HOH B 88 36.530 24.627 3.103 1.00 31.19 O HETATM 3650 O HOH B 94 27.375 29.142 0.044 1.00 41.42 O HETATM 3651 O HOH B 103 39.100 24.776 1.770 1.00 38.74 O HETATM 3652 O HOH B 105 16.492 30.512 -6.403 1.00 38.00 O HETATM 3653 O HOH B 121 14.998 27.447 -8.690 1.00 45.28 O HETATM 3654 O HOH B 126 16.526 22.627 -1.321 1.00 37.42 O HETATM 3655 O HOH B 150 16.555 27.970 1.645 1.00 36.38 O HETATM 3656 O HOH B 154 23.602 25.118 -1.846 1.00 46.86 O HETATM 3657 O HOH B 160 21.546 25.035 -4.791 1.00 44.72 O HETATM 3658 O HOH B 183 13.301 32.079 -3.654 1.00 50.67 O HETATM 3659 O HOH B 187 18.785 21.753 -4.755 1.00 41.99 O HETATM 3660 O HOH B 189 26.631 25.679 -0.068 1.00 41.90 O HETATM 3661 O HOH B 197 18.429 25.643 -10.700 1.00 49.64 O HETATM 3662 O HOH B 204 26.176 19.090 2.286 1.00 42.29 O HETATM 3663 O HOH B 215 30.681 19.729 6.718 1.00 46.93 O HETATM 3664 O HOH B 225 12.558 18.633 -14.939 1.00 54.45 O HETATM 3665 O HOH B 236 19.559 31.444 0.746 1.00 43.47 O HETATM 3666 O HOH B 239 32.899 31.730 6.814 1.00 46.94 O HETATM 3667 O HOH B 248 23.166 21.026 -3.479 1.00 50.96 O HETATM 3668 O HOH B 291 23.835 33.398 -1.226 1.00 51.40 O HETATM 3669 O HOH B 300 14.098 20.544 -11.246 1.00 45.50 O HETATM 3670 O HOH B 322 23.065 33.146 -4.697 1.00 56.10 O MASTER 280 0 0 29 2 0 0 6 3668 2 0 33 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3qgb
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-UGUGCCAUA-3)
EC.Number
E.C.-.-.-.-
Resolution
2.4(Å)
Affinity (Kd/Ki/IC50)
Kd=3.5nM
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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