Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 24-JAN-11 3QG9 TITLE CRYSTAL STRUCTURE OF FBF-2/GLD-1 FBEA A7U MUTANT COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FEM-3 MRNA-BINDING FACTOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PUM-HD DOMAIN, RESIDUES 164-575; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5'-R(*UP*GP*UP*GP*CP*CP*UP*UP*A)-3'; COMPND 8 CHAIN: B; COMPND 9 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: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: SYNTHETIC RNA KEYWDS PUF REPEATS, RNA BINDING DOMAIN, RNA BINDING PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Y.Y.KOH,Y.WANG,C.QIU,L.OPPERMAN,L.GROSS,T.M.T.HALL,M.WICKENS REVDAT 3 24-JAN-18 3QG9 1 AUTHOR REVDAT 2 30-MAR-11 3QG9 1 JRNL REVDAT 1 23-MAR-11 3QG9 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. 2.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.45 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8 REMARK 3 NUMBER OF REFLECTIONS : 23450 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1170 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 24.4518 - 4.4903 0.98 3029 153 0.1515 0.1908 REMARK 3 2 4.4903 - 3.5677 0.97 2930 161 0.1492 0.1872 REMARK 3 3 3.5677 - 3.1177 0.97 2938 165 0.1643 0.2254 REMARK 3 4 3.1177 - 2.8331 0.89 2718 119 0.1706 0.2333 REMARK 3 5 2.8331 - 2.6303 0.89 2672 141 0.1708 0.2313 REMARK 3 6 2.6303 - 2.4754 0.87 2626 153 0.1731 0.2623 REMARK 3 7 2.4754 - 2.3515 0.89 2723 138 0.1774 0.2387 REMARK 3 8 2.3515 - 2.2492 0.88 2644 140 0.1885 0.2743 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) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.007 3445 REMARK 3 ANGLE : 0.957 4681 REMARK 3 CHIRALITY : 0.062 545 REMARK 3 PLANARITY : 0.003 568 REMARK 3 DIHEDRAL : 17.554 1299 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 3QG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-11. REMARK 100 THE DEPOSITION ID IS D_1000063606. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25563 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 10.80 REMARK 200 R MERGE (I) : 0.14600 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 17.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.90 REMARK 200 R MERGE FOR SHELL (I) : 0.58800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 3.700 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.16 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG8000, 8% ETHYLENE GLYCOL, 0.1 M REMARK 280 TRIS (PH 7.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 33.72500 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 67.45000 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 50.58750 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 84.31250 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 16.86250 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: 2850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 312 -158.39 -119.99 REMARK 500 ARG A 441 -6.61 74.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 576 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: 3QGB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD-1 FBEA REMARK 900 RELATED ID: 3QGC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD-1 FBEA REMARK 900 A7U MUTANT DBREF 3QG9 A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3QG9 B 1 9 PDB 3QG9 3QG9 1 9 SEQADV 3QG9 GLY A 163 UNP Q09312 EXPRESSION TAG 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 ARG VAL ILE GLN SER SEQRES 11 A 413 SER LEU GLN ASN MET ASP LEU SER LEU ALA CYS LYS LEU SEQRES 12 A 413 VAL GLN ALA LEU PRO ARG ASP ALA ARG LEU ILE ALA ILE SEQRES 13 A 413 CYS VAL ASP GLN ASN ALA ASN HIS VAL ILE GLN LYS VAL SEQRES 14 A 413 VAL ALA VAL ILE PRO LEU LYS ASN TRP GLU PHE ILE VAL SEQRES 15 A 413 ASP PHE VAL ALA THR PRO GLU HIS LEU ARG GLN ILE CYS SEQRES 16 A 413 SER ASP LYS TYR GLY CYS ARG VAL VAL GLN THR ILE ILE SEQRES 17 A 413 GLU LYS LEU THR ALA ASP SER MET ASN VAL ASP LEU THR SEQRES 18 A 413 SER ALA ALA GLN ASN LEU ARG GLU ARG ALA LEU GLN ARG SEQRES 19 A 413 LEU MET THR SER VAL THR ASN ARG CYS GLN GLU LEU ALA SEQRES 20 A 413 THR ASN GLU TYR ALA ASN TYR ILE ILE GLN HIS ILE VAL SEQRES 21 A 413 SER ASN ASP ASP LEU ALA VAL TYR ARG GLU CYS ILE ILE SEQRES 22 A 413 GLU LYS CYS LEU MET ARG ASN LEU LEU SER LEU SER GLN SEQRES 23 A 413 GLU LYS PHE ALA SER HIS VAL VAL GLU LYS ALA PHE LEU SEQRES 24 A 413 HIS ALA PRO LEU GLU LEU LEU ALA GLU MET MET ASP GLU SEQRES 25 A 413 ILE PHE ASP GLY TYR ILE PRO HIS PRO ASP THR GLY LYS SEQRES 26 A 413 ASP ALA LEU ASP ILE MET MET PHE HIS GLN PHE GLY ASN SEQRES 27 A 413 TYR VAL VAL GLN CYS MET LEU THR ILE CYS CYS ASP ALA SEQRES 28 A 413 VAL SER GLY ARG ARG GLN THR LYS GLU GLY GLY TYR ASP SEQRES 29 A 413 HIS ALA ILE SER PHE GLN ASP TRP LEU LYS LYS LEU HIS SEQRES 30 A 413 SER ARG VAL THR LYS GLU ARG HIS ARG LEU SER ARG PHE SEQRES 31 A 413 SER SER GLY LYS LYS MET ILE GLU THR LEU ALA ASN LEU SEQRES 32 A 413 ARG SER THR HIS PRO ILE TYR GLU LEU GLN SEQRES 1 B 9 U G U G C C U U A HET EDO A 576 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO C2 H6 O2 FORMUL 4 HOH *290(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 GLY A 213 1 14 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 THR A 257 1 16 HELIX 8 8 GLY A 261 GLN A 276 1 16 HELIX 9 9 GLN A 276 ASP A 283 1 8 HELIX 10 10 PHE A 285 MET A 297 1 13 HELIX 11 11 ASP A 298 ALA A 308 1 11 HELIX 12 12 ASP A 312 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 ASP A 359 LEU A 373 1 15 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 ASN A 411 1 8 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 SSBOND 1 CYS A 405 CYS A 438 1555 1555 2.04 SITE 1 AC1 6 HOH A 8 PHE A 495 GLN A 497 ASN A 500 SITE 2 AC1 6 SER A 554 U B 1 CRYST1 96.750 96.750 101.175 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 0.010336 0.005967 0.000000 0.00000 SCALE2 0.000000 0.011935 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009884 0.00000 ATOM 1 N LEU A 168 -6.350 13.357 -22.062 1.00 44.52 N ANISOU 1 N LEU A 168 5554 5513 5847 545 -945 -867 N ATOM 2 CA LEU A 168 -7.150 14.552 -22.335 1.00 45.86 C ANISOU 2 CA LEU A 168 5723 5703 6000 505 -887 -826 C ATOM 3 C LEU A 168 -8.293 14.287 -23.329 1.00 42.27 C ANISOU 3 C LEU A 168 5277 5244 5541 492 -874 -806 C ATOM 4 O LEU A 168 -8.252 13.315 -24.075 1.00 39.33 O ANISOU 4 O LEU A 168 4900 4866 5177 515 -902 -833 O ATOM 5 CB LEU A 168 -6.262 15.727 -22.772 1.00 47.41 C ANISOU 5 CB LEU A 168 5875 5956 6184 495 -844 -850 C ATOM 6 CG LEU A 168 -5.372 15.671 -24.011 1.00 53.43 C ANISOU 6 CG LEU A 168 6591 6766 6946 514 -836 -906 C ATOM 7 CD1 LEU A 168 -4.578 16.969 -24.106 1.00 48.24 C ANISOU 7 CD1 LEU A 168 5898 6158 6273 495 -791 -918 C ATOM 8 CD2 LEU A 168 -4.432 14.463 -23.979 1.00 63.59 C ANISOU 8 CD2 LEU A 168 7867 8044 8250 559 -891 -958 C ATOM 9 N PRO A 169 -9.324 15.150 -23.321 1.00 37.96 N ANISOU 9 N PRO A 169 4743 4698 4980 456 -832 -757 N ATOM 10 CA PRO A 169 -10.559 14.958 -24.090 1.00 34.95 C ANISOU 10 CA PRO A 169 4376 4308 4595 441 -819 -730 C ATOM 11 C PRO A 169 -10.304 14.551 -25.532 1.00 38.46 C ANISOU 11 C PRO A 169 4791 4781 5040 457 -818 -769 C ATOM 12 O PRO A 169 -9.513 15.185 -26.233 1.00 40.05 O ANISOU 12 O PRO A 169 4956 5028 5235 459 -792 -801 O ATOM 13 CB PRO A 169 -11.197 16.346 -24.067 1.00 29.13 C ANISOU 13 CB PRO A 169 3637 3591 3839 404 -763 -690 C ATOM 14 CG PRO A 169 -10.709 16.955 -22.841 1.00 31.74 C ANISOU 14 CG PRO A 169 3976 3917 4168 397 -759 -678 C ATOM 15 CD PRO A 169 -9.313 16.456 -22.641 1.00 31.96 C ANISOU 15 CD PRO A 169 3983 3953 4208 429 -792 -729 C ATOM 16 N THR A 170 -10.990 13.508 -25.977 1.00 36.96 N ANISOU 16 N THR A 170 4620 4564 4858 466 -847 -766 N ATOM 17 CA THR A 170 -10.819 13.037 -27.339 1.00 39.62 C ANISOU 17 CA THR A 170 4933 4924 5196 482 -849 -802 C ATOM 18 C THR A 170 -11.200 14.117 -28.355 1.00 36.90 C ANISOU 18 C THR A 170 4566 4621 4835 457 -793 -792 C ATOM 19 O THR A 170 -10.563 14.250 -29.396 1.00 39.84 O ANISOU 19 O THR A 170 4904 5031 5203 467 -780 -831 O ATOM 20 CB THR A 170 -11.629 11.761 -27.587 1.00 42.38 C ANISOU 20 CB THR A 170 5312 5234 5557 493 -889 -794 C ATOM 21 OG1 THR A 170 -11.417 11.319 -28.935 1.00 43.18 O ANISOU 21 OG1 THR A 170 5390 5359 5659 510 -891 -831 O ATOM 22 CG2 THR A 170 -13.107 12.028 -27.354 1.00 42.18 C ANISOU 22 CG2 THR A 170 5317 5185 5523 459 -870 -735 C ATOM 23 N TRP A 171 -12.224 14.901 -28.041 1.00 33.12 N ANISOU 23 N TRP A 171 4105 4134 4344 424 -761 -741 N ATOM 24 CA TRP A 171 -12.668 15.969 -28.935 1.00 32.58 C ANISOU 24 CA TRP A 171 4020 4100 4258 399 -709 -727 C ATOM 25 C TRP A 171 -11.585 16.988 -29.256 1.00 36.42 C ANISOU 25 C TRP A 171 4471 4635 4733 396 -675 -756 C ATOM 26 O TRP A 171 -11.720 17.758 -30.204 1.00 39.25 O ANISOU 26 O TRP A 171 4811 5026 5076 380 -636 -758 O ATOM 27 CB TRP A 171 -13.876 16.700 -28.350 1.00 33.53 C ANISOU 27 CB TRP A 171 4168 4204 4369 367 -682 -668 C ATOM 28 CG TRP A 171 -13.591 17.518 -27.106 1.00 35.83 C ANISOU 28 CG TRP A 171 4468 4491 4656 354 -669 -646 C ATOM 29 CD1 TRP A 171 -13.850 17.162 -25.813 1.00 35.41 C ANISOU 29 CD1 TRP A 171 4444 4399 4610 353 -693 -621 C ATOM 30 CD2 TRP A 171 -13.019 18.833 -27.048 1.00 39.58 C ANISOU 30 CD2 TRP A 171 4923 5000 5114 338 -627 -648 C ATOM 31 NE1 TRP A 171 -13.473 18.167 -24.957 1.00 34.53 N ANISOU 31 NE1 TRP A 171 4332 4296 4490 339 -670 -607 N ATOM 32 CE2 TRP A 171 -12.956 19.203 -25.690 1.00 38.77 C ANISOU 32 CE2 TRP A 171 4839 4878 5013 330 -630 -623 C ATOM 33 CE3 TRP A 171 -12.549 19.731 -28.013 1.00 41.74 C ANISOU 33 CE3 TRP A 171 5167 5320 5373 329 -589 -668 C ATOM 34 CZ2 TRP A 171 -12.440 20.430 -25.272 1.00 39.32 C ANISOU 34 CZ2 TRP A 171 4900 4972 5070 314 -596 -618 C ATOM 35 CZ3 TRP A 171 -12.033 20.949 -27.595 1.00 41.18 C ANISOU 35 CZ3 TRP A 171 5087 5272 5289 312 -555 -662 C ATOM 36 CH2 TRP A 171 -11.983 21.285 -26.240 1.00 38.12 C ANISOU 36 CH2 TRP A 171 4719 4863 4903 305 -560 -638 C ATOM 37 N SER A 172 -10.522 17.006 -28.460 1.00 41.19 N ANISOU 37 N SER A 172 5065 5241 5343 410 -691 -779 N ATOM 38 CA SER A 172 -9.478 18.015 -28.610 1.00 41.83 C ANISOU 38 CA SER A 172 5113 5367 5412 403 -659 -805 C ATOM 39 C SER A 172 -8.241 17.436 -29.292 1.00 45.00 C ANISOU 39 C SER A 172 5479 5798 5821 433 -678 -868 C ATOM 40 O SER A 172 -7.280 18.152 -29.574 1.00 46.92 O ANISOU 40 O SER A 172 5689 6083 6054 429 -654 -898 O ATOM 41 CB SER A 172 -9.095 18.594 -27.243 1.00 36.03 C ANISOU 41 CB SER A 172 4389 4622 4677 395 -658 -787 C ATOM 42 OG SER A 172 -8.205 17.730 -26.557 1.00 29.01 O ANISOU 42 OG SER A 172 3499 3718 3807 425 -703 -818 O ATOM 43 N LEU A 173 -8.268 16.134 -29.545 1.00 44.93 N ANISOU 43 N LEU A 173 5476 5767 5828 462 -722 -890 N ATOM 44 CA LEU A 173 -7.131 15.451 -30.148 1.00 51.71 C ANISOU 44 CA LEU A 173 6302 6649 6695 495 -746 -952 C ATOM 45 C LEU A 173 -7.262 15.359 -31.658 1.00 57.75 C ANISOU 45 C LEU A 173 7045 7445 7453 496 -729 -975 C ATOM 46 O LEU A 173 -8.368 15.423 -32.199 1.00 58.94 O ANISOU 46 O LEU A 173 7213 7584 7597 478 -713 -943 O ATOM 47 CB LEU A 173 -6.984 14.046 -29.566 1.00 50.63 C ANISOU 47 CB LEU A 173 6186 6472 6581 531 -808 -968 C ATOM 48 CG LEU A 173 -6.590 14.022 -28.096 1.00 46.10 C ANISOU 48 CG LEU A 173 5629 5870 6015 537 -833 -956 C ATOM 49 CD1 LEU A 173 -6.340 12.593 -27.652 1.00 47.73 C ANISOU 49 CD1 LEU A 173 5855 6038 6243 574 -897 -979 C ATOM 50 CD2 LEU A 173 -5.356 14.890 -27.887 1.00 38.69 C ANISOU 50 CD2 LEU A 173 4655 4976 5071 536 -811 -987 C ATOM 51 N ASP A 174 -6.129 15.207 -32.335 1.00 61.97 N ANISOU 51 N ASP A 174 7541 8019 7988 516 -731 -1032 N ATOM 52 CA ASP A 174 -6.135 15.046 -33.784 1.00 67.99 C ANISOU 52 CA ASP A 174 8280 8812 8742 519 -717 -1060 C ATOM 53 C ASP A 174 -6.059 13.571 -34.166 1.00 69.04 C ANISOU 53 C ASP A 174 8416 8922 8892 558 -768 -1092 C ATOM 54 O ASP A 174 -6.203 12.696 -33.315 1.00 66.50 O ANISOU 54 O ASP A 174 8121 8557 8587 578 -813 -1085 O ATOM 55 CB ASP A 174 -5.012 15.859 -34.445 1.00 69.35 C ANISOU 55 CB ASP A 174 8405 9045 8899 513 -682 -1102 C ATOM 56 CG ASP A 174 -3.627 15.439 -33.984 1.00 69.93 C ANISOU 56 CG ASP A 174 8450 9136 8984 544 -710 -1155 C ATOM 57 OD1 ASP A 174 -2.697 16.267 -34.087 1.00 71.67 O ANISOU 57 OD1 ASP A 174 8636 9402 9192 534 -682 -1181 O ATOM 58 OD2 ASP A 174 -3.463 14.288 -33.525 1.00 69.40 O ANISOU 58 OD2 ASP A 174 8395 9036 8936 580 -762 -1172 O ATOM 59 N SER A 175 -5.835 13.305 -35.448 1.00 73.76 N ANISOU 59 N SER A 175 8990 9551 9485 568 -760 -1128 N ATOM 60 CA SER A 175 -5.843 11.942 -35.964 1.00 78.83 C ANISOU 60 CA SER A 175 9636 10173 10142 603 -806 -1158 C ATOM 61 C SER A 175 -4.784 11.057 -35.313 1.00 80.36 C ANISOU 61 C SER A 175 9821 10359 10354 646 -856 -1202 C ATOM 62 O SER A 175 -5.012 9.869 -35.091 1.00 79.75 O ANISOU 62 O SER A 175 9768 10240 10292 674 -906 -1208 O ATOM 63 CB SER A 175 -5.649 11.958 -37.477 1.00 81.21 C ANISOU 63 CB SER A 175 9908 10517 10433 605 -784 -1193 C ATOM 64 OG SER A 175 -6.551 12.864 -38.086 1.00 81.50 O ANISOU 64 OG SER A 175 9952 10565 10451 566 -737 -1154 O ATOM 65 N ASN A 176 -3.630 11.642 -35.008 1.00 80.90 N ANISOU 65 N ASN A 176 9856 10464 10418 650 -843 -1234 N ATOM 66 CA ASN A 176 -2.524 10.894 -34.417 1.00 82.81 C ANISOU 66 CA ASN A 176 10083 10703 10676 691 -888 -1281 C ATOM 67 C ASN A 176 -2.408 11.061 -32.903 1.00 80.23 C ANISOU 67 C ASN A 176 9779 10346 10358 689 -906 -1255 C ATOM 68 O ASN A 176 -1.314 10.983 -32.342 1.00 79.24 O ANISOU 68 O ASN A 176 9633 10235 10240 712 -925 -1291 O ATOM 69 CB ASN A 176 -1.201 11.255 -35.099 1.00 87.55 C ANISOU 69 CB ASN A 176 10627 11369 11269 703 -870 -1343 C ATOM 70 CG ASN A 176 -1.121 12.720 -35.476 1.00 90.90 C ANISOU 70 CG ASN A 176 11028 11840 11670 659 -805 -1329 C ATOM 71 OD1 ASN A 176 -1.857 13.192 -36.345 1.00 91.41 O ANISOU 71 OD1 ASN A 176 11096 11916 11720 632 -769 -1307 O ATOM 72 ND2 ASN A 176 -0.222 13.449 -34.826 1.00 92.37 N ANISOU 72 ND2 ASN A 176 11190 12053 11852 652 -791 -1342 N ATOM 73 N GLY A 177 -3.546 11.295 -32.254 1.00 78.88 N ANISOU 73 N GLY A 177 9651 10133 10186 662 -900 -1192 N ATOM 74 CA GLY A 177 -3.624 11.330 -30.803 1.00 77.09 C ANISOU 74 CA GLY A 177 9455 9869 9968 660 -920 -1162 C ATOM 75 C GLY A 177 -2.993 12.536 -30.131 1.00 76.52 C ANISOU 75 C GLY A 177 9363 9826 9886 638 -886 -1156 C ATOM 76 O GLY A 177 -2.724 12.511 -28.931 1.00 76.62 O ANISOU 76 O GLY A 177 9392 9815 9907 643 -908 -1145 O ATOM 77 N GLU A 178 -2.759 13.597 -30.894 1.00 74.34 N ANISOU 77 N GLU A 178 9054 9600 9591 613 -833 -1163 N ATOM 78 CA GLU A 178 -2.138 14.798 -30.346 1.00 72.84 C ANISOU 78 CA GLU A 178 8846 9442 9390 589 -798 -1158 C ATOM 79 C GLU A 178 -3.113 15.970 -30.232 1.00 64.93 C ANISOU 79 C GLU A 178 7864 8436 8370 542 -749 -1099 C ATOM 80 O GLU A 178 -4.072 16.069 -30.995 1.00 62.23 O ANISOU 80 O GLU A 178 7534 8090 8020 525 -729 -1074 O ATOM 81 CB GLU A 178 -0.930 15.207 -31.187 1.00 78.12 C ANISOU 81 CB GLU A 178 9459 10174 10049 595 -776 -1216 C ATOM 82 CG GLU A 178 0.242 14.250 -31.092 1.00 84.78 C ANISOU 82 CG GLU A 178 10276 11027 10909 642 -822 -1278 C ATOM 83 CD GLU A 178 1.506 14.832 -31.689 1.00 90.41 C ANISOU 83 CD GLU A 178 10932 11808 11610 643 -796 -1333 C ATOM 84 OE1 GLU A 178 2.608 14.360 -31.334 1.00 92.91 O ANISOU 84 OE1 GLU A 178 11224 12139 11938 676 -828 -1381 O ATOM 85 OE2 GLU A 178 1.398 15.769 -32.508 1.00 91.08 O ANISOU 85 OE2 GLU A 178 11000 11932 11675 609 -745 -1328 O ATOM 86 N MET A 179 -2.852 16.856 -29.275 1.00 58.68 N ANISOU 86 N MET A 179 7076 7647 7573 523 -731 -1078 N ATOM 87 CA MET A 179 -3.687 18.033 -29.062 1.00 55.31 C ANISOU 87 CA MET A 179 6668 7218 7128 480 -685 -1024 C ATOM 88 C MET A 179 -3.724 18.913 -30.314 1.00 51.32 C ANISOU 88 C MET A 179 6138 6760 6602 454 -635 -1031 C ATOM 89 O MET A 179 -2.682 19.316 -30.826 1.00 50.83 O ANISOU 89 O MET A 179 6037 6746 6531 454 -618 -1074 O ATOM 90 CB MET A 179 -3.177 18.834 -27.857 1.00 53.18 C ANISOU 90 CB MET A 179 6401 6948 6855 467 -676 -1010 C ATOM 91 CG MET A 179 -4.226 19.731 -27.211 1.00 52.79 C ANISOU 91 CG MET A 179 6388 6876 6795 431 -647 -946 C ATOM 92 SD MET A 179 -3.568 20.755 -25.872 1.00 39.34 S ANISOU 92 SD MET A 179 4686 5176 5085 414 -633 -931 S ATOM 93 CE MET A 179 -2.725 22.030 -26.813 1.00 32.55 C ANISOU 93 CE MET A 179 3783 4384 4200 388 -579 -960 C ATOM 94 N ARG A 180 -4.925 19.198 -30.807 1.00 50.71 N ANISOU 94 N ARG A 180 6084 6669 6515 431 -612 -990 N ATOM 95 CA ARG A 180 -5.093 20.012 -32.011 1.00 53.75 C ANISOU 95 CA ARG A 180 6451 7093 6878 406 -565 -993 C ATOM 96 C ARG A 180 -4.386 21.361 -31.893 1.00 59.60 C ANISOU 96 C ARG A 180 7173 7875 7599 378 -523 -996 C ATOM 97 O ARG A 180 -4.203 21.885 -30.791 1.00 59.98 O ANISOU 97 O ARG A 180 7232 7911 7647 369 -520 -976 O ATOM 98 CB ARG A 180 -6.578 20.215 -32.321 1.00 51.81 C ANISOU 98 CB ARG A 180 6239 6822 6626 385 -548 -940 C ATOM 99 CG ARG A 180 -7.270 18.989 -32.906 1.00 51.85 C ANISOU 99 CG ARG A 180 6256 6799 6644 406 -581 -943 C ATOM 100 CD ARG A 180 -8.770 19.038 -32.668 1.00 50.46 C ANISOU 100 CD ARG A 180 6121 6585 6468 388 -576 -884 C ATOM 101 NE ARG A 180 -9.315 20.371 -32.898 1.00 53.84 N ANISOU 101 NE ARG A 180 6553 7030 6873 352 -525 -850 N ATOM 102 CZ ARG A 180 -10.504 20.773 -32.458 1.00 59.16 C ANISOU 102 CZ ARG A 180 7259 7676 7542 331 -513 -796 C ATOM 103 NH1 ARG A 180 -11.266 19.940 -31.765 1.00 60.05 N ANISOU 103 NH1 ARG A 180 7401 7743 7671 341 -546 -770 N ATOM 104 NH2 ARG A 180 -10.931 22.006 -32.705 1.00 61.01 N ANISOU 104 NH2 ARG A 180 7498 7927 7755 300 -468 -769 N ATOM 105 N SER A 181 -4.001 21.923 -33.035 1.00 62.93 N ANISOU 105 N SER A 181 7566 8343 8002 363 -489 -1021 N ATOM 106 CA SER A 181 -3.196 23.146 -33.065 1.00 63.39 C ANISOU 106 CA SER A 181 7602 8445 8039 336 -449 -1033 C ATOM 107 C SER A 181 -4.019 24.433 -33.074 1.00 59.44 C ANISOU 107 C SER A 181 7127 7943 7516 294 -404 -982 C ATOM 108 O SER A 181 -3.538 25.487 -32.660 1.00 55.17 O ANISOU 108 O SER A 181 6581 7422 6958 270 -376 -976 O ATOM 109 CB SER A 181 -2.253 23.131 -34.270 1.00 64.78 C ANISOU 109 CB SER A 181 7734 8676 8204 339 -435 -1089 C ATOM 110 OG SER A 181 -1.241 22.156 -34.108 1.00 67.04 O ANISOU 110 OG SER A 181 7991 8971 8509 376 -473 -1142 O ATOM 111 N ARG A 182 -5.253 24.349 -33.555 1.00 60.23 N ANISOU 111 N ARG A 182 7253 8019 7613 286 -397 -946 N ATOM 112 CA ARG A 182 -6.102 25.529 -33.659 1.00 59.42 C ANISOU 112 CA ARG A 182 7175 7915 7488 250 -356 -900 C ATOM 113 C ARG A 182 -7.184 25.512 -32.592 1.00 46.82 C ANISOU 113 C ARG A 182 5620 6269 5902 248 -368 -845 C ATOM 114 O ARG A 182 -8.317 25.931 -32.834 1.00 46.83 O ANISOU 114 O ARG A 182 5647 6254 5893 231 -349 -804 O ATOM 115 CB ARG A 182 -6.739 25.606 -35.045 1.00 70.28 C ANISOU 115 CB ARG A 182 8549 9304 8849 239 -335 -899 C ATOM 116 CG ARG A 182 -5.745 25.763 -36.183 1.00 80.38 C ANISOU 116 CG ARG A 182 9790 10636 10114 235 -317 -951 C ATOM 117 CD ARG A 182 -6.442 25.621 -37.532 1.00 89.64 C ANISOU 117 CD ARG A 182 10965 11816 11277 230 -304 -950 C ATOM 118 NE ARG A 182 -7.611 26.493 -37.645 1.00 96.65 N ANISOU 118 NE ARG A 182 11886 12687 12148 202 -275 -898 N ATOM 119 CZ ARG A 182 -8.864 26.111 -37.407 1.00101.13 C ANISOU 119 CZ ARG A 182 12486 13214 12727 208 -289 -856 C ATOM 120 NH1 ARG A 182 -9.127 24.862 -37.040 1.00102.53 N ANISOU 120 NH1 ARG A 182 12667 13360 12930 238 -332 -860 N ATOM 121 NH2 ARG A 182 -9.859 26.980 -37.536 1.00101.46 N ANISOU 121 NH2 ARG A 182 12554 13245 12751 183 -262 -812 N ATOM 122 N LEU A 183 -6.825 25.015 -31.416 1.00 37.03 N ANISOU 122 N LEU A 183 4385 5005 4680 266 -399 -845 N ATOM 123 CA LEU A 183 -7.735 24.961 -30.285 1.00 34.14 C ANISOU 123 CA LEU A 183 4056 4592 4323 264 -412 -796 C ATOM 124 C LEU A 183 -7.883 26.348 -29.666 1.00 30.34 C ANISOU 124 C LEU A 183 3590 4115 3822 232 -375 -761 C ATOM 125 O LEU A 183 -6.893 27.041 -29.442 1.00 29.02 O ANISOU 125 O LEU A 183 3405 3976 3644 222 -360 -781 O ATOM 126 CB LEU A 183 -7.191 23.992 -29.243 1.00 38.00 C ANISOU 126 CB LEU A 183 4546 5055 4836 293 -458 -811 C ATOM 127 CG LEU A 183 -8.184 23.462 -28.218 1.00 42.39 C ANISOU 127 CG LEU A 183 5142 5559 5407 298 -484 -768 C ATOM 128 CD1 LEU A 183 -9.058 22.406 -28.872 1.00 44.58 C ANISOU 128 CD1 LEU A 183 5430 5813 5696 313 -507 -763 C ATOM 129 CD2 LEU A 183 -7.429 22.887 -27.035 1.00 45.52 C ANISOU 129 CD2 LEU A 183 5539 5935 5820 320 -521 -782 C ATOM 130 N SER A 184 -9.113 26.766 -29.400 1.00 31.81 N ANISOU 130 N SER A 184 3810 4275 4002 217 -362 -710 N ATOM 131 CA SER A 184 -9.332 28.074 -28.784 1.00 31.28 C ANISOU 131 CA SER A 184 3760 4209 3916 188 -328 -675 C ATOM 132 C SER A 184 -9.533 27.932 -27.278 1.00 29.74 C ANISOU 132 C SER A 184 3590 3977 3734 194 -349 -647 C ATOM 133 O SER A 184 -9.994 26.895 -26.807 1.00 33.97 O ANISOU 133 O SER A 184 4138 4478 4289 213 -384 -638 O ATOM 134 CB SER A 184 -10.529 28.796 -29.423 1.00 25.95 C ANISOU 134 CB SER A 184 3106 3531 3222 167 -297 -637 C ATOM 135 OG SER A 184 -11.767 28.259 -28.983 1.00 24.69 O ANISOU 135 OG SER A 184 2975 3331 3074 173 -314 -599 O ATOM 136 N LEU A 185 -9.184 28.970 -26.526 1.00 24.88 N ANISOU 136 N LEU A 185 2982 3368 3105 175 -328 -632 N ATOM 137 CA LEU A 185 -9.416 28.972 -25.088 1.00 24.50 C ANISOU 137 CA LEU A 185 2958 3285 3065 177 -343 -602 C ATOM 138 C LEU A 185 -10.900 28.746 -24.789 1.00 24.31 C ANISOU 138 C LEU A 185 2968 3224 3045 174 -346 -554 C ATOM 139 O LEU A 185 -11.249 27.998 -23.869 1.00 21.33 O ANISOU 139 O LEU A 185 2608 2811 2684 187 -377 -538 O ATOM 140 CB LEU A 185 -8.929 30.280 -24.455 1.00 23.35 C ANISOU 140 CB LEU A 185 2817 3154 2900 153 -313 -590 C ATOM 141 CG LEU A 185 -9.270 30.541 -22.979 1.00 20.28 C ANISOU 141 CG LEU A 185 2458 2732 2515 149 -320 -553 C ATOM 142 CD1 LEU A 185 -8.578 29.550 -22.060 1.00 17.38 C ANISOU 142 CD1 LEU A 185 2086 2345 2171 174 -363 -573 C ATOM 143 CD2 LEU A 185 -8.906 31.964 -22.578 1.00 18.53 C ANISOU 143 CD2 LEU A 185 2243 2527 2270 123 -285 -539 C ATOM 144 N SER A 186 -11.774 29.378 -25.570 1.00 23.96 N ANISOU 144 N SER A 186 2932 3187 2984 157 -316 -531 N ATOM 145 CA SER A 186 -13.210 29.277 -25.307 1.00 24.82 C ANISOU 145 CA SER A 186 3071 3266 3094 153 -316 -486 C ATOM 146 C SER A 186 -13.739 27.854 -25.474 1.00 28.05 C ANISOU 146 C SER A 186 3482 3649 3525 174 -353 -490 C ATOM 147 O SER A 186 -14.539 27.394 -24.661 1.00 29.45 O ANISOU 147 O SER A 186 3684 3793 3714 177 -371 -460 O ATOM 148 CB SER A 186 -14.016 30.275 -26.143 1.00 24.26 C ANISOU 148 CB SER A 186 3008 3210 3000 132 -277 -463 C ATOM 149 OG SER A 186 -13.901 31.591 -25.608 1.00 24.52 O ANISOU 149 OG SER A 186 3054 3251 3013 111 -246 -442 O ATOM 150 N GLU A 187 -13.295 27.152 -26.514 1.00 30.68 N ANISOU 150 N GLU A 187 3792 4000 3866 188 -366 -528 N ATOM 151 CA GLU A 187 -13.667 25.743 -26.655 1.00 29.68 C ANISOU 151 CA GLU A 187 3668 3849 3761 210 -405 -536 C ATOM 152 C GLU A 187 -13.362 25.004 -25.359 1.00 23.84 C ANISOU 152 C GLU A 187 2940 3077 3039 225 -442 -534 C ATOM 153 O GLU A 187 -14.219 24.317 -24.818 1.00 27.21 O ANISOU 153 O GLU A 187 3392 3469 3477 229 -464 -508 O ATOM 154 CB GLU A 187 -12.906 25.062 -27.790 1.00 29.84 C ANISOU 154 CB GLU A 187 3657 3893 3787 228 -417 -586 C ATOM 155 CG GLU A 187 -13.144 25.617 -29.169 1.00 38.32 C ANISOU 155 CG GLU A 187 4717 4998 4843 215 -386 -593 C ATOM 156 CD GLU A 187 -12.264 24.930 -30.203 1.00 46.73 C ANISOU 156 CD GLU A 187 5751 6089 5915 233 -399 -646 C ATOM 157 OE1 GLU A 187 -12.329 23.686 -30.301 1.00 47.60 O ANISOU 157 OE1 GLU A 187 5860 6181 6044 257 -436 -661 O ATOM 158 OE2 GLU A 187 -11.502 25.627 -30.909 1.00 53.01 O ANISOU 158 OE2 GLU A 187 6523 6924 6695 223 -372 -672 O ATOM 159 N VAL A 188 -12.134 25.142 -24.865 1.00 24.80 N ANISOU 159 N VAL A 188 3047 3212 3164 233 -449 -562 N ATOM 160 CA VAL A 188 -11.754 24.483 -23.614 1.00 28.72 C ANISOU 160 CA VAL A 188 3556 3678 3677 247 -485 -562 C ATOM 161 C VAL A 188 -12.627 24.906 -22.414 1.00 20.73 C ANISOU 161 C VAL A 188 2580 2635 2661 231 -479 -511 C ATOM 162 O VAL A 188 -13.088 24.060 -21.646 1.00 21.03 O ANISOU 162 O VAL A 188 2641 2637 2714 240 -511 -495 O ATOM 163 CB VAL A 188 -10.261 24.692 -23.282 1.00 32.20 C ANISOU 163 CB VAL A 188 3973 4142 4119 257 -491 -602 C ATOM 164 CG1 VAL A 188 -9.897 23.973 -21.991 1.00 34.05 C ANISOU 164 CG1 VAL A 188 4223 4343 4371 274 -532 -602 C ATOM 165 CG2 VAL A 188 -9.394 24.194 -24.421 1.00 32.79 C ANISOU 165 CG2 VAL A 188 4012 4249 4199 275 -499 -655 C ATOM 166 N LEU A 189 -12.866 26.202 -22.261 1.00 17.06 N ANISOU 166 N LEU A 189 2121 2185 2177 207 -439 -486 N ATOM 167 CA LEU A 189 -13.651 26.692 -21.120 1.00 23.01 C ANISOU 167 CA LEU A 189 2907 2912 2926 192 -431 -439 C ATOM 168 C LEU A 189 -15.093 26.195 -21.158 1.00 29.37 C ANISOU 168 C LEU A 189 3734 3690 3734 188 -436 -404 C ATOM 169 O LEU A 189 -15.647 25.822 -20.127 1.00 33.48 O ANISOU 169 O LEU A 189 4281 4179 4262 186 -453 -376 O ATOM 170 CB LEU A 189 -13.629 28.227 -21.037 1.00 17.26 C ANISOU 170 CB LEU A 189 2179 2205 2173 168 -386 -421 C ATOM 171 CG LEU A 189 -12.275 28.863 -20.714 1.00 17.88 C ANISOU 171 CG LEU A 189 2241 2307 2246 166 -378 -448 C ATOM 172 CD1 LEU A 189 -12.297 30.403 -20.878 1.00 6.46 C ANISOU 172 CD1 LEU A 189 796 885 773 141 -331 -432 C ATOM 173 CD2 LEU A 189 -11.837 28.459 -19.313 1.00 15.50 C ANISOU 173 CD2 LEU A 189 1954 1979 1958 176 -407 -444 C ATOM 174 N ASP A 190 -15.693 26.198 -22.348 1.00 29.98 N ANISOU 174 N ASP A 190 3803 3782 3806 185 -422 -405 N ATOM 175 CA ASP A 190 -17.077 25.752 -22.533 1.00 31.23 C ANISOU 175 CA ASP A 190 3979 3920 3966 180 -425 -373 C ATOM 176 C ASP A 190 -17.240 24.232 -22.366 1.00 31.98 C ANISOU 176 C ASP A 190 4082 3985 4083 198 -471 -382 C ATOM 177 O ASP A 190 -18.330 23.752 -22.049 1.00 34.90 O ANISOU 177 O ASP A 190 4473 4329 4456 192 -482 -352 O ATOM 178 CB ASP A 190 -17.612 26.167 -23.919 1.00 27.77 C ANISOU 178 CB ASP A 190 3528 3507 3516 172 -398 -375 C ATOM 179 CG ASP A 190 -17.750 27.680 -24.080 1.00 31.86 C ANISOU 179 CG ASP A 190 4047 4048 4009 152 -352 -357 C ATOM 180 OD1 ASP A 190 -17.760 28.149 -25.236 1.00 31.73 O ANISOU 180 OD1 ASP A 190 4016 4059 3981 147 -330 -369 O ATOM 181 OD2 ASP A 190 -17.848 28.407 -23.067 1.00 36.07 O ANISOU 181 OD2 ASP A 190 4597 4573 4535 141 -339 -332 O ATOM 182 N SER A 191 -16.162 23.485 -22.586 1.00 24.46 N ANISOU 182 N SER A 191 3112 3037 3143 219 -500 -425 N ATOM 183 CA SER A 191 -16.235 22.023 -22.661 1.00 23.60 C ANISOU 183 CA SER A 191 3010 2903 3054 239 -545 -440 C ATOM 184 C SER A 191 -16.447 21.342 -21.307 1.00 25.49 C ANISOU 184 C SER A 191 3279 3101 3305 241 -578 -420 C ATOM 185 O SER A 191 -16.909 20.208 -21.244 1.00 27.46 O ANISOU 185 O SER A 191 3544 3323 3567 250 -613 -417 O ATOM 186 CB SER A 191 -14.959 21.475 -23.283 1.00 19.32 C ANISOU 186 CB SER A 191 2439 2379 2521 263 -565 -494 C ATOM 187 OG SER A 191 -13.877 21.720 -22.405 1.00 23.43 O ANISOU 187 OG SER A 191 2955 2902 3045 270 -574 -510 O ATOM 188 N GLY A 192 -16.092 22.031 -20.230 1.00 26.92 N ANISOU 188 N GLY A 192 3469 3278 3480 233 -569 -406 N ATOM 189 CA GLY A 192 -16.142 21.446 -18.904 1.00 26.28 C ANISOU 189 CA GLY A 192 3417 3160 3409 235 -600 -390 C ATOM 190 C GLY A 192 -14.932 20.572 -18.618 1.00 28.86 C ANISOU 190 C GLY A 192 3737 3478 3753 262 -642 -430 C ATOM 191 O GLY A 192 -14.821 19.988 -17.543 1.00 28.63 O ANISOU 191 O GLY A 192 3731 3415 3731 268 -674 -423 O ATOM 192 N ASP A 193 -14.021 20.492 -19.583 1.00 29.25 N ANISOU 192 N ASP A 193 3754 3556 3805 279 -643 -475 N ATOM 193 CA ASP A 193 -12.859 19.610 -19.488 1.00 28.23 C ANISOU 193 CA ASP A 193 3613 3422 3691 309 -685 -519 C ATOM 194 C ASP A 193 -11.568 20.317 -19.050 1.00 25.22 C ANISOU 194 C ASP A 193 3211 3065 3307 314 -676 -545 C ATOM 195 O ASP A 193 -10.481 19.764 -19.186 1.00 27.47 O ANISOU 195 O ASP A 193 3477 3358 3603 340 -704 -589 O ATOM 196 CB ASP A 193 -12.628 18.911 -20.834 1.00 27.83 C ANISOU 196 CB ASP A 193 3539 3390 3648 328 -696 -557 C ATOM 197 CG ASP A 193 -13.698 17.877 -21.142 1.00 30.40 C ANISOU 197 CG ASP A 193 3886 3684 3979 329 -720 -540 C ATOM 198 OD1 ASP A 193 -14.101 17.756 -22.317 1.00 29.62 O ANISOU 198 OD1 ASP A 193 3773 3602 3878 329 -708 -548 O ATOM 199 OD2 ASP A 193 -14.138 17.191 -20.199 1.00 33.88 O ANISOU 199 OD2 ASP A 193 4360 4084 4428 329 -751 -518 O ATOM 200 N LEU A 194 -11.683 21.531 -18.527 1.00 20.37 N ANISOU 200 N LEU A 194 2364 2448 2929 -68 -550 191 N ATOM 201 CA LEU A 194 -10.493 22.315 -18.169 1.00 23.87 C ANISOU 201 CA LEU A 194 2820 2926 3324 -55 -493 170 C ATOM 202 C LEU A 194 -9.518 21.576 -17.234 1.00 21.04 C ANISOU 202 C LEU A 194 2475 2575 2944 -58 -481 157 C ATOM 203 O LEU A 194 -8.312 21.569 -17.466 1.00 19.30 O ANISOU 203 O LEU A 194 2282 2374 2677 -39 -472 129 O ATOM 204 CB LEU A 194 -10.901 23.669 -17.574 1.00 22.07 C ANISOU 204 CB LEU A 194 2562 2715 3109 -65 -432 190 C ATOM 205 CG LEU A 194 -9.788 24.576 -17.056 1.00 21.45 C ANISOU 205 CG LEU A 194 2493 2668 2988 -58 -372 175 C ATOM 206 CD1 LEU A 194 -10.103 26.036 -17.366 1.00 19.92 C ANISOU 206 CD1 LEU A 194 2288 2488 2794 -53 -335 183 C ATOM 207 CD2 LEU A 194 -9.579 24.364 -15.554 1.00 21.66 C ANISOU 207 CD2 LEU A 194 2509 2700 3022 -76 -335 185 C ATOM 208 N MET A 195 -10.042 20.964 -16.180 1.00 18.32 N ANISOU 208 N MET A 195 2111 2217 2634 -82 -479 179 N ATOM 209 CA MET A 195 -9.208 20.226 -15.230 1.00 21.41 C ANISOU 209 CA MET A 195 2514 2613 3009 -87 -469 170 C ATOM 210 C MET A 195 -8.314 19.192 -15.918 1.00 27.61 C ANISOU 210 C MET A 195 3338 3391 3761 -66 -517 138 C ATOM 211 O MET A 195 -7.171 18.984 -15.512 1.00 34.15 O ANISOU 211 O MET A 195 4184 4236 4554 -57 -500 118 O ATOM 212 CB MET A 195 -10.071 19.553 -14.152 1.00 18.85 C ANISOU 212 CB MET A 195 2164 2269 2731 -117 -472 201 C ATOM 213 CG MET A 195 -10.775 20.552 -13.225 1.00 23.77 C ANISOU 213 CG MET A 195 2751 2902 3378 -134 -413 231 C ATOM 214 SD MET A 195 -9.564 21.557 -12.328 1.00 25.13 S ANISOU 214 SD MET A 195 2936 3110 3504 -127 -340 214 S ATOM 215 CE MET A 195 -8.797 20.303 -11.307 1.00 16.73 C ANISOU 215 CE MET A 195 1889 2041 2429 -137 -350 207 C ATOM 216 N LYS A 196 -8.830 18.544 -16.957 1.00 22.62 N ANISOU 216 N LYS A 196 2718 2734 3141 -58 -579 135 N ATOM 217 CA LYS A 196 -8.013 17.616 -17.740 1.00 24.24 C ANISOU 217 CA LYS A 196 2966 2933 3312 -32 -626 103 C ATOM 218 C LYS A 196 -6.812 18.302 -18.407 1.00 20.02 C ANISOU 218 C LYS A 196 2455 2432 2720 1 -599 73 C ATOM 219 O LYS A 196 -5.703 17.803 -18.320 1.00 23.34 O ANISOU 219 O LYS A 196 2899 2864 3104 18 -598 50 O ATOM 220 CB LYS A 196 -8.861 16.871 -18.775 1.00 27.57 C ANISOU 220 CB LYS A 196 3401 3319 3756 -28 -700 105 C ATOM 221 CG LYS A 196 -10.008 16.065 -18.156 1.00 38.51 C ANISOU 221 CG LYS A 196 4762 4669 5200 -62 -734 137 C ATOM 222 CD LYS A 196 -10.604 15.064 -19.143 1.00 46.34 C ANISOU 222 CD LYS A 196 5777 5621 6209 -57 -818 133 C ATOM 223 CE LYS A 196 -11.867 14.399 -18.587 1.00 52.22 C ANISOU 223 CE LYS A 196 6491 6332 7019 -94 -853 173 C ATOM 224 NZ LYS A 196 -12.976 15.387 -18.341 1.00 56.41 N ANISOU 224 NZ LYS A 196 6972 6868 7593 -117 -820 210 N ATOM 225 N PHE A 197 -7.035 19.439 -19.067 1.00 17.23 N ANISOU 225 N PHE A 197 2093 2094 2360 8 -576 76 N ATOM 226 CA PHE A 197 -5.945 20.193 -19.700 1.00 19.79 C ANISOU 226 CA PHE A 197 2436 2451 2632 36 -547 53 C ATOM 227 C PHE A 197 -4.956 20.753 -18.682 1.00 19.30 C ANISOU 227 C PHE A 197 2365 2420 2549 30 -486 50 C ATOM 228 O PHE A 197 -3.754 20.821 -18.939 1.00 18.21 O ANISOU 228 O PHE A 197 2245 2307 2366 53 -472 29 O ATOM 229 CB PHE A 197 -6.496 21.375 -20.505 1.00 23.23 C ANISOU 229 CB PHE A 197 2861 2894 3070 40 -533 61 C ATOM 230 CG PHE A 197 -7.225 20.982 -21.765 1.00 27.20 C ANISOU 230 CG PHE A 197 3382 3373 3581 54 -593 58 C ATOM 231 CD1 PHE A 197 -6.558 20.934 -22.983 1.00 27.68 C ANISOU 231 CD1 PHE A 197 3478 3443 3597 89 -614 32 C ATOM 232 CD2 PHE A 197 -8.578 20.677 -21.736 1.00 30.54 C ANISOU 232 CD2 PHE A 197 3784 3762 4056 32 -628 82 C ATOM 233 CE1 PHE A 197 -7.227 20.581 -24.152 1.00 27.62 C ANISOU 233 CE1 PHE A 197 3491 3410 3593 103 -671 28 C ATOM 234 CE2 PHE A 197 -9.252 20.318 -22.907 1.00 32.57 C ANISOU 234 CE2 PHE A 197 4060 3995 4322 43 -688 79 C ATOM 235 CZ PHE A 197 -8.571 20.274 -24.114 1.00 27.53 C ANISOU 235 CZ PHE A 197 3462 3364 3635 79 -710 51 C ATOM 236 N ALA A 198 -5.479 21.181 -17.537 1.00 19.36 N ANISOU 236 N ALA A 198 2343 2427 2587 1 -451 74 N ATOM 237 CA ALA A 198 -4.685 21.904 -16.556 1.00 19.88 C ANISOU 237 CA ALA A 198 2400 2520 2635 -7 -393 74 C ATOM 238 C ALA A 198 -3.642 21.021 -15.882 1.00 22.42 C ANISOU 238 C ALA A 198 2737 2847 2935 -4 -395 59 C ATOM 239 O ALA A 198 -2.636 21.529 -15.420 1.00 16.62 O ANISOU 239 O ALA A 198 2005 2138 2172 -1 -357 51 O ATOM 240 CB ALA A 198 -5.582 22.534 -15.517 1.00 16.81 C ANISOU 240 CB ALA A 198 1981 2125 2283 -36 -357 103 C ATOM 241 N VAL A 199 -3.893 19.711 -15.805 1.00 23.56 N ANISOU 241 N VAL A 199 2892 2966 3095 -5 -441 57 N ATOM 242 CA VAL A 199 -2.944 18.794 -15.175 1.00 23.41 C ANISOU 242 CA VAL A 199 2889 2949 3057 -1 -448 43 C ATOM 243 C VAL A 199 -2.109 18.052 -16.219 1.00 29.67 C ANISOU 243 C VAL A 199 3715 3745 3814 35 -487 14 C ATOM 244 O VAL A 199 -1.317 17.173 -15.880 1.00 29.47 O ANISOU 244 O VAL A 199 3705 3719 3772 44 -501 0 O ATOM 245 CB VAL A 199 -3.633 17.768 -14.257 1.00 20.89 C ANISOU 245 CB VAL A 199 2562 2601 2776 -26 -472 60 C ATOM 246 CG1 VAL A 199 -4.442 18.474 -13.177 1.00 25.13 C ANISOU 246 CG1 VAL A 199 3067 3137 3345 -58 -430 90 C ATOM 247 CG2 VAL A 199 -4.519 16.806 -15.070 1.00 12.28 C ANISOU 247 CG2 VAL A 199 1480 1475 1710 -23 -538 62 C ATOM 248 N ASP A 200 -2.297 18.409 -17.486 1.00 30.41 N ANISOU 248 N ASP A 200 3819 3841 3895 56 -504 5 N ATOM 249 CA ASP A 200 -1.492 17.862 -18.575 1.00 28.55 C ANISOU 249 CA ASP A 200 3617 3612 3620 96 -535 -23 C ATOM 250 C ASP A 200 -0.462 18.904 -19.007 1.00 31.68 C ANISOU 250 C ASP A 200 4014 4050 3974 116 -490 -32 C ATOM 251 O ASP A 200 -0.775 20.084 -19.099 1.00 34.93 O ANISOU 251 O ASP A 200 4406 4474 4390 105 -456 -19 O ATOM 252 CB ASP A 200 -2.390 17.487 -19.755 1.00 25.47 C ANISOU 252 CB ASP A 200 3244 3194 3240 108 -589 -26 C ATOM 253 CG ASP A 200 -1.602 16.967 -20.957 1.00 27.69 C ANISOU 253 CG ASP A 200 3565 3482 3475 154 -620 -55 C ATOM 254 OD1 ASP A 200 -1.110 15.810 -20.917 1.00 28.59 O ANISOU 254 OD1 ASP A 200 3704 3583 3576 171 -654 -72 O ATOM 255 OD2 ASP A 200 -1.493 17.722 -21.948 1.00 20.23 O ANISOU 255 OD2 ASP A 200 2627 2554 2505 174 -610 -61 O ATOM 256 N LYS A 201 0.764 18.478 -19.282 1.00 31.90 N ANISOU 256 N LYS A 201 4061 4098 3961 146 -490 -54 N ATOM 257 CA LYS A 201 1.820 19.430 -19.599 1.00 31.06 C ANISOU 257 CA LYS A 201 3952 4034 3817 163 -445 -59 C ATOM 258 C LYS A 201 1.491 20.261 -20.833 1.00 31.82 C ANISOU 258 C LYS A 201 4052 4139 3899 179 -444 -58 C ATOM 259 O LYS A 201 1.578 21.492 -20.814 1.00 39.50 O ANISOU 259 O LYS A 201 5006 5133 4868 168 -402 -46 O ATOM 260 CB LYS A 201 3.157 18.715 -19.777 1.00 37.41 C ANISOU 260 CB LYS A 201 4775 4857 4581 197 -450 -80 C ATOM 261 CG LYS A 201 4.294 19.629 -20.201 1.00 43.86 C ANISOU 261 CG LYS A 201 5586 5719 5359 216 -407 -82 C ATOM 262 CD LYS A 201 5.598 18.853 -20.303 1.00 49.61 C ANISOU 262 CD LYS A 201 6329 6467 6052 250 -410 -100 C ATOM 263 CE LYS A 201 6.682 19.659 -21.024 1.00 49.23 C ANISOU 263 CE LYS A 201 6278 6465 5964 277 -374 -101 C ATOM 264 NZ LYS A 201 6.976 20.943 -20.344 1.00 40.60 N ANISOU 264 NZ LYS A 201 5153 5396 4878 246 -323 -80 N ATOM 265 N THR A 202 1.109 19.589 -21.908 1.00 29.00 N ANISOU 265 N THR A 202 3722 3762 3533 205 -492 -72 N ATOM 266 CA THR A 202 0.808 20.275 -23.152 1.00 24.38 C ANISOU 266 CA THR A 202 3147 3185 2931 224 -496 -73 C ATOM 267 C THR A 202 -0.416 21.160 -22.964 1.00 27.99 C ANISOU 267 C THR A 202 3579 3626 3429 190 -486 -49 C ATOM 268 O THR A 202 -0.403 22.341 -23.320 1.00 26.47 O ANISOU 268 O THR A 202 3374 3454 3228 188 -453 -40 O ATOM 269 CB THR A 202 0.571 19.283 -24.305 1.00 24.75 C ANISOU 269 CB THR A 202 3234 3208 2961 259 -556 -93 C ATOM 270 OG1 THR A 202 1.651 18.336 -24.354 1.00 27.80 O ANISOU 270 OG1 THR A 202 3645 3605 3313 291 -567 -115 O ATOM 271 CG2 THR A 202 0.491 20.033 -25.640 1.00 25.03 C ANISOU 271 CG2 THR A 202 3284 3257 2968 284 -555 -96 C ATOM 272 N GLY A 203 -1.464 20.585 -22.387 1.00 24.57 N ANISOU 272 N GLY A 203 3137 3159 3041 164 -515 -38 N ATOM 273 CA GLY A 203 -2.698 21.309 -22.142 1.00 26.57 C ANISOU 273 CA GLY A 203 3363 3396 3337 133 -508 -14 C ATOM 274 C GLY A 203 -2.506 22.542 -21.277 1.00 30.58 C ANISOU 274 C GLY A 203 3840 3928 3851 110 -444 3 C ATOM 275 O GLY A 203 -2.996 23.623 -21.612 1.00 24.97 O ANISOU 275 O GLY A 203 3117 3224 3148 103 -424 15 O ATOM 276 N CYS A 204 -1.780 22.391 -20.169 1.00 33.92 N ANISOU 276 N CYS A 204 4255 4363 4270 98 -415 3 N ATOM 277 CA CYS A 204 -1.560 23.509 -19.253 1.00 33.28 C ANISOU 277 CA CYS A 204 4149 4302 4193 75 -358 17 C ATOM 278 C CYS A 204 -0.735 24.623 -19.888 1.00 33.23 C ANISOU 278 C CYS A 204 4145 4329 4150 91 -325 13 C ATOM 279 O CYS A 204 -0.974 25.798 -19.620 1.00 31.85 O ANISOU 279 O CYS A 204 3954 4163 3985 75 -289 27 O ATOM 280 CB CYS A 204 -0.900 23.052 -17.945 1.00 34.40 C ANISOU 280 CB CYS A 204 4286 4448 4335 61 -339 17 C ATOM 281 SG CYS A 204 -1.026 24.281 -16.589 1.00 34.46 S ANISOU 281 SG CYS A 204 4267 4467 4361 27 -278 38 S ATOM 282 N GLN A 205 0.245 24.258 -20.710 1.00 32.42 N ANISOU 282 N GLN A 205 4065 4246 4008 123 -336 -6 N ATOM 283 CA GLN A 205 1.040 25.268 -21.402 1.00 34.40 C ANISOU 283 CA GLN A 205 4316 4530 4223 138 -305 -7 C ATOM 284 C GLN A 205 0.194 26.045 -22.411 1.00 36.19 C ANISOU 284 C GLN A 205 4544 4751 4456 143 -313 1 C ATOM 285 O GLN A 205 0.337 27.268 -22.537 1.00 34.36 O ANISOU 285 O GLN A 205 4301 4537 4217 136 -278 12 O ATOM 286 CB GLN A 205 2.263 24.657 -22.087 1.00 35.77 C ANISOU 286 CB GLN A 205 4511 4727 4352 175 -314 -26 C ATOM 287 CG GLN A 205 3.307 24.143 -21.105 1.00 46.23 C ANISOU 287 CG GLN A 205 5831 6066 5667 172 -298 -31 C ATOM 288 CD GLN A 205 4.615 23.809 -21.784 1.00 51.76 C ANISOU 288 CD GLN A 205 6547 6798 6322 209 -296 -46 C ATOM 289 OE1 GLN A 205 4.629 23.269 -22.891 1.00 53.97 O ANISOU 289 OE1 GLN A 205 6850 7076 6579 244 -325 -60 O ATOM 290 NE2 GLN A 205 5.724 24.126 -21.125 1.00 53.28 N ANISOU 290 NE2 GLN A 205 6725 7019 6501 204 -261 -42 N ATOM 291 N PHE A 206 -0.682 25.341 -23.127 1.00 27.30 N ANISOU 291 N PHE A 206 3433 3598 3343 153 -360 -4 N ATOM 292 CA PHE A 206 -1.588 26.014 -24.047 1.00 27.40 C ANISOU 292 CA PHE A 206 3447 3600 3365 155 -373 4 C ATOM 293 C PHE A 206 -2.433 27.011 -23.238 1.00 25.17 C ANISOU 293 C PHE A 206 3133 3310 3122 121 -342 28 C ATOM 294 O PHE A 206 -2.572 28.177 -23.616 1.00 18.10 O ANISOU 294 O PHE A 206 2230 2425 2223 118 -318 38 O ATOM 295 CB PHE A 206 -2.463 25.015 -24.806 1.00 27.60 C ANISOU 295 CB PHE A 206 3491 3591 3403 168 -435 -3 C ATOM 296 CG PHE A 206 -3.749 25.605 -25.293 1.00 30.32 C ANISOU 296 CG PHE A 206 3826 3914 3779 156 -451 12 C ATOM 297 CD1 PHE A 206 -3.807 26.280 -26.505 1.00 35.02 C ANISOU 297 CD1 PHE A 206 4436 4519 4351 176 -456 11 C ATOM 298 CD2 PHE A 206 -4.900 25.511 -24.518 1.00 32.93 C ANISOU 298 CD2 PHE A 206 4131 4217 4163 125 -459 32 C ATOM 299 CE1 PHE A 206 -4.998 26.842 -26.945 1.00 37.23 C ANISOU 299 CE1 PHE A 206 4705 4778 4661 165 -472 26 C ATOM 300 CE2 PHE A 206 -6.091 26.068 -24.939 1.00 33.69 C ANISOU 300 CE2 PHE A 206 4214 4295 4291 114 -473 49 C ATOM 301 CZ PHE A 206 -6.142 26.737 -26.155 1.00 36.12 C ANISOU 301 CZ PHE A 206 4537 4610 4576 134 -480 46 C ATOM 302 N LEU A 207 -2.947 26.556 -22.095 1.00 24.56 N ANISOU 302 N LEU A 207 3039 3213 3080 96 -341 37 N ATOM 303 CA LEU A 207 -3.743 27.418 -21.226 1.00 25.06 C ANISOU 303 CA LEU A 207 3075 3269 3180 66 -310 59 C ATOM 304 C LEU A 207 -2.940 28.634 -20.752 1.00 25.41 C ANISOU 304 C LEU A 207 3110 3341 3203 59 -255 64 C ATOM 305 O LEU A 207 -3.433 29.762 -20.771 1.00 25.42 O ANISOU 305 O LEU A 207 3100 3344 3217 49 -231 78 O ATOM 306 CB LEU A 207 -4.326 26.634 -20.044 1.00 24.59 C ANISOU 306 CB LEU A 207 2999 3186 3157 43 -316 69 C ATOM 307 CG LEU A 207 -5.413 25.627 -20.405 1.00 24.54 C ANISOU 307 CG LEU A 207 2993 3146 3184 41 -370 73 C ATOM 308 CD1 LEU A 207 -5.967 24.879 -19.211 1.00 22.66 C ANISOU 308 CD1 LEU A 207 2739 2889 2984 17 -373 87 C ATOM 309 CD2 LEU A 207 -6.543 26.328 -21.118 1.00 27.35 C ANISOU 309 CD2 LEU A 207 3338 3489 3565 39 -380 89 C ATOM 310 N GLU A 208 -1.699 28.392 -20.347 1.00 25.53 N ANISOU 310 N GLU A 208 3133 3378 3188 64 -238 52 N ATOM 311 CA GLU A 208 -0.774 29.439 -19.924 1.00 29.25 C ANISOU 311 CA GLU A 208 3599 3876 3638 57 -193 56 C ATOM 312 C GLU A 208 -0.681 30.555 -20.963 1.00 30.42 C ANISOU 312 C GLU A 208 3750 4040 3767 68 -181 60 C ATOM 313 O GLU A 208 -0.890 31.737 -20.658 1.00 28.88 O ANISOU 313 O GLU A 208 3544 3847 3580 52 -150 74 O ATOM 314 CB GLU A 208 0.621 28.836 -19.758 1.00 39.38 C ANISOU 314 CB GLU A 208 4893 5182 4887 70 -189 41 C ATOM 315 CG GLU A 208 1.267 29.072 -18.413 1.00 48.56 C ANISOU 315 CG GLU A 208 6047 6354 6052 48 -156 46 C ATOM 316 CD GLU A 208 0.831 28.058 -17.394 1.00 48.33 C ANISOU 316 CD GLU A 208 6014 6302 6048 34 -170 45 C ATOM 317 OE1 GLU A 208 1.672 27.246 -16.983 1.00 45.73 O ANISOU 317 OE1 GLU A 208 5692 5980 5704 39 -177 35 O ATOM 318 OE2 GLU A 208 -0.359 28.054 -17.027 1.00 52.30 O ANISOU 318 OE2 GLU A 208 6507 6779 6585 19 -175 57 O ATOM 319 N LYS A 209 -0.338 30.168 -22.189 1.00 30.18 N ANISOU 319 N LYS A 209 3738 4020 3710 96 -206 49 N ATOM 320 CA LYS A 209 -0.203 31.123 -23.279 1.00 33.53 C ANISOU 320 CA LYS A 209 4168 4461 4113 110 -198 53 C ATOM 321 C LYS A 209 -1.552 31.784 -23.543 1.00 27.56 C ANISOU 321 C LYS A 209 3403 3680 3388 99 -205 67 C ATOM 322 O LYS A 209 -1.643 33.009 -23.648 1.00 28.17 O ANISOU 322 O LYS A 209 3473 3765 3466 90 -178 80 O ATOM 323 CB LYS A 209 0.312 30.440 -24.546 1.00 40.32 C ANISOU 323 CB LYS A 209 5052 5333 4937 146 -226 37 C ATOM 324 CG LYS A 209 1.227 31.317 -25.389 1.00 53.08 C ANISOU 324 CG LYS A 209 6673 6982 6512 162 -202 41 C ATOM 325 CD LYS A 209 2.411 31.822 -24.560 1.00 63.86 C ANISOU 325 CD LYS A 209 8024 8375 7864 149 -160 47 C ATOM 326 CE LYS A 209 3.572 32.282 -25.437 1.00 67.26 C ANISOU 326 CE LYS A 209 8461 8845 8250 171 -142 50 C ATOM 327 NZ LYS A 209 3.172 33.356 -26.394 1.00 69.38 N ANISOU 327 NZ LYS A 209 8732 9117 8511 174 -136 62 N ATOM 328 N ALA A 210 -2.598 30.972 -23.631 1.00 22.63 N ANISOU 328 N ALA A 210 2778 3026 2793 98 -242 66 N ATOM 329 CA ALA A 210 -3.932 31.503 -23.901 1.00 25.82 C ANISOU 329 CA ALA A 210 3172 3408 3233 89 -253 81 C ATOM 330 C ALA A 210 -4.380 32.570 -22.890 1.00 26.06 C ANISOU 330 C ALA A 210 3178 3434 3290 62 -212 99 C ATOM 331 O ALA A 210 -5.065 33.518 -23.257 1.00 32.39 O ANISOU 331 O ALA A 210 3972 4230 4105 59 -204 112 O ATOM 332 CB ALA A 210 -4.953 30.374 -23.986 1.00 20.82 C ANISOU 332 CB ALA A 210 2537 2742 2631 88 -301 80 C ATOM 333 N VAL A 211 -4.000 32.434 -21.624 1.00 24.42 N ANISOU 333 N VAL A 211 2960 3229 3088 46 -185 100 N ATOM 334 CA VAL A 211 -4.500 33.379 -20.618 1.00 29.37 C ANISOU 334 CA VAL A 211 3570 3849 3740 24 -148 117 C ATOM 335 C VAL A 211 -3.614 34.617 -20.408 1.00 32.69 C ANISOU 335 C VAL A 211 3994 4291 4134 19 -107 119 C ATOM 336 O VAL A 211 -3.988 35.535 -19.671 1.00 33.31 O ANISOU 336 O VAL A 211 4063 4364 4229 4 -76 132 O ATOM 337 CB VAL A 211 -4.823 32.698 -19.262 1.00 33.18 C ANISOU 337 CB VAL A 211 4040 4318 4250 6 -140 122 C ATOM 338 CG1 VAL A 211 -5.621 31.421 -19.489 1.00 34.53 C ANISOU 338 CG1 VAL A 211 4207 4466 4446 8 -185 121 C ATOM 339 CG2 VAL A 211 -3.563 32.414 -18.479 1.00 35.25 C ANISOU 339 CG2 VAL A 211 4311 4598 4484 1 -121 110 C ATOM 340 N LYS A 212 -2.459 34.643 -21.073 1.00 30.86 N ANISOU 340 N LYS A 212 3776 4085 3863 32 -107 109 N ATOM 341 CA LYS A 212 -1.567 35.795 -21.045 1.00 29.22 C ANISOU 341 CA LYS A 212 3572 3900 3631 27 -74 114 C ATOM 342 C LYS A 212 -2.001 36.887 -22.015 1.00 30.98 C ANISOU 342 C LYS A 212 3797 4123 3851 33 -72 124 C ATOM 343 O LYS A 212 -1.580 38.037 -21.877 1.00 30.54 O ANISOU 343 O LYS A 212 3741 4077 3785 23 -44 133 O ATOM 344 CB LYS A 212 -0.129 35.378 -21.368 1.00 33.18 C ANISOU 344 CB LYS A 212 4084 4431 4092 39 -74 103 C ATOM 345 CG LYS A 212 0.617 34.802 -20.180 1.00 45.58 C ANISOU 345 CG LYS A 212 5651 6006 5660 27 -61 97 C ATOM 346 CD LYS A 212 2.102 34.623 -20.473 1.00 55.20 C ANISOU 346 CD LYS A 212 6876 7257 6841 38 -55 90 C ATOM 347 CE LYS A 212 2.803 35.962 -20.670 1.00 61.89 C ANISOU 347 CE LYS A 212 7720 8124 7669 30 -27 104 C ATOM 348 NZ LYS A 212 4.282 35.801 -20.805 1.00 65.91 N ANISOU 348 NZ LYS A 212 8229 8667 8146 38 -18 102 N ATOM 349 N GLY A 213 -2.829 36.524 -22.997 1.00 32.76 N ANISOU 349 N GLY A 213 4024 4336 4086 48 -104 123 N ATOM 350 CA GLY A 213 -3.262 37.456 -24.030 1.00 28.60 C ANISOU 350 CA GLY A 213 3501 3808 3556 56 -108 132 C ATOM 351 C GLY A 213 -4.468 38.290 -23.636 1.00 25.97 C ANISOU 351 C GLY A 213 3155 3452 3261 42 -97 148 C ATOM 352 O GLY A 213 -4.729 38.495 -22.445 1.00 23.72 O ANISOU 352 O GLY A 213 2858 3157 2998 25 -74 153 O ATOM 353 N SER A 214 -5.199 38.787 -24.631 1.00 20.98 N ANISOU 353 N SER A 214 2525 2811 2636 52 -114 155 N ATOM 354 CA SER A 214 -6.450 39.490 -24.367 1.00 27.29 C ANISOU 354 CA SER A 214 3308 3587 3475 43 -109 171 C ATOM 355 C SER A 214 -7.512 38.489 -23.933 1.00 28.74 C ANISOU 355 C SER A 214 3476 3746 3698 40 -132 173 C ATOM 356 O SER A 214 -7.529 37.345 -24.379 1.00 31.65 O ANISOU 356 O SER A 214 3850 4112 4064 49 -168 163 O ATOM 357 CB SER A 214 -6.927 40.267 -25.593 1.00 24.32 C ANISOU 357 CB SER A 214 2939 3207 3095 55 -124 179 C ATOM 358 OG SER A 214 -5.959 41.223 -25.979 1.00 22.54 O ANISOU 358 OG SER A 214 2727 3004 2834 56 -101 180 O ATOM 359 N LEU A 215 -8.387 38.921 -23.041 1.00 25.95 N ANISOU 359 N LEU A 215 3102 3376 3381 28 -112 187 N ATOM 360 CA LEU A 215 -9.442 38.050 -22.540 1.00 22.31 C ANISOU 360 CA LEU A 215 2621 2893 2962 22 -130 195 C ATOM 361 C LEU A 215 -10.707 38.869 -22.454 1.00 19.36 C ANISOU 361 C LEU A 215 2227 2502 2629 20 -121 216 C ATOM 362 O LEU A 215 -10.701 39.995 -21.940 1.00 16.31 O ANISOU 362 O LEU A 215 1839 2116 2241 16 -83 224 O ATOM 363 CB LEU A 215 -9.101 37.501 -21.148 1.00 18.44 C ANISOU 363 CB LEU A 215 2124 2404 2477 8 -106 193 C ATOM 364 CG LEU A 215 -7.871 36.603 -20.984 1.00 19.99 C ANISOU 364 CG LEU A 215 2338 2618 2639 9 -112 173 C ATOM 365 CD1 LEU A 215 -7.637 36.285 -19.522 1.00 17.57 C ANISOU 365 CD1 LEU A 215 2025 2311 2341 -6 -84 174 C ATOM 366 CD2 LEU A 215 -8.038 35.331 -21.776 1.00 21.25 C ANISOU 366 CD2 LEU A 215 2503 2771 2801 20 -162 164 C ATOM 367 N THR A 216 -11.788 38.307 -22.971 1.00 16.38 N ANISOU 367 N THR A 216 1834 2105 2285 23 -158 226 N ATOM 368 CA THR A 216 -13.085 38.928 -22.835 1.00 18.48 C ANISOU 368 CA THR A 216 2074 2352 2595 22 -152 250 C ATOM 369 C THR A 216 -13.538 38.690 -21.407 1.00 21.20 C ANISOU 369 C THR A 216 2396 2691 2969 10 -121 262 C ATOM 370 O THR A 216 -13.007 37.809 -20.713 1.00 21.92 O ANISOU 370 O THR A 216 2490 2787 3051 2 -119 253 O ATOM 371 CB THR A 216 -14.100 38.307 -23.804 1.00 21.49 C ANISOU 371 CB THR A 216 2444 2716 3007 27 -206 259 C ATOM 372 OG1 THR A 216 -14.384 36.964 -23.400 1.00 19.30 O ANISOU 372 OG1 THR A 216 2155 2428 2751 19 -232 260 O ATOM 373 CG2 THR A 216 -13.549 38.307 -25.235 1.00 22.11 C ANISOU 373 CG2 THR A 216 2552 2801 3049 41 -241 244 C ATOM 374 N SER A 217 -14.517 39.474 -20.973 1.00 16.55 N ANISOU 374 N SER A 217 1784 2090 2414 10 -98 283 N ATOM 375 CA SER A 217 -15.037 39.381 -19.624 1.00 16.35 C ANISOU 375 CA SER A 217 1737 2059 2416 3 -63 298 C ATOM 376 C SER A 217 -15.519 37.974 -19.298 1.00 21.99 C ANISOU 376 C SER A 217 2431 2764 3159 -7 -90 306 C ATOM 377 O SER A 217 -15.235 37.449 -18.219 1.00 25.57 O ANISOU 377 O SER A 217 2882 3221 3610 -16 -68 305 O ATOM 378 CB SER A 217 -16.175 40.370 -19.442 1.00 17.80 C ANISOU 378 CB SER A 217 1898 2232 2636 10 -40 322 C ATOM 379 OG SER A 217 -16.785 40.184 -18.192 1.00 17.00 O ANISOU 379 OG SER A 217 1772 2125 2562 6 -8 339 O ATOM 380 N TYR A 218 -16.237 37.352 -20.227 1.00 18.65 N ANISOU 380 N TYR A 218 1996 2328 2763 -6 -140 314 N ATOM 381 CA TYR A 218 -16.758 36.015 -19.961 1.00 20.63 C ANISOU 381 CA TYR A 218 2227 2567 3045 -17 -172 325 C ATOM 382 C TYR A 218 -15.637 34.995 -19.827 1.00 19.83 C ANISOU 382 C TYR A 218 2152 2474 2908 -23 -187 300 C ATOM 383 O TYR A 218 -15.668 34.151 -18.927 1.00 17.18 O ANISOU 383 O TYR A 218 1806 2135 2585 -35 -183 306 O ATOM 384 CB TYR A 218 -17.761 35.565 -21.021 1.00 25.39 C ANISOU 384 CB TYR A 218 2814 3151 3685 -16 -229 339 C ATOM 385 CG TYR A 218 -18.500 34.305 -20.632 1.00 27.94 C ANISOU 385 CG TYR A 218 3109 3456 4049 -31 -260 358 C ATOM 386 CD1 TYR A 218 -19.158 34.216 -19.411 1.00 32.56 C ANISOU 386 CD1 TYR A 218 3660 4039 4670 -41 -225 384 C ATOM 387 CD2 TYR A 218 -18.555 33.208 -21.490 1.00 29.17 C ANISOU 387 CD2 TYR A 218 3275 3598 4210 -35 -325 352 C ATOM 388 CE1 TYR A 218 -19.851 33.070 -19.049 1.00 32.42 C ANISOU 388 CE1 TYR A 218 3616 4007 4694 -57 -253 406 C ATOM 389 CE2 TYR A 218 -19.249 32.057 -21.141 1.00 29.17 C ANISOU 389 CE2 TYR A 218 3251 3580 4251 -51 -358 371 C ATOM 390 CZ TYR A 218 -19.891 31.995 -19.919 1.00 32.87 C ANISOU 390 CZ TYR A 218 3683 4048 4757 -63 -322 399 C ATOM 391 OH TYR A 218 -20.577 30.859 -19.560 1.00 34.23 O ANISOU 391 OH TYR A 218 3829 4203 4973 -81 -353 422 O ATOM 392 N GLN A 219 -14.640 35.069 -20.709 1.00 16.42 N ANISOU 392 N GLN A 219 1754 2054 2432 -13 -204 274 N ATOM 393 CA GLN A 219 -13.472 34.205 -20.550 1.00 18.41 C ANISOU 393 CA GLN A 219 2032 2317 2647 -14 -212 250 C ATOM 394 C GLN A 219 -12.894 34.302 -19.142 1.00 19.13 C ANISOU 394 C GLN A 219 2123 2420 2727 -24 -163 248 C ATOM 395 O GLN A 219 -12.625 33.292 -18.504 1.00 22.50 O ANISOU 395 O GLN A 219 2549 2845 3155 -33 -170 245 O ATOM 396 CB GLN A 219 -12.403 34.511 -21.596 1.00 14.82 C ANISOU 396 CB GLN A 219 1610 1878 2141 1 -224 225 C ATOM 397 CG GLN A 219 -12.713 33.870 -22.941 1.00 20.67 C ANISOU 397 CG GLN A 219 2363 2608 2882 12 -284 219 C ATOM 398 CD GLN A 219 -11.861 34.417 -24.059 1.00 18.66 C ANISOU 398 CD GLN A 219 2139 2370 2580 30 -289 201 C ATOM 399 OE1 GLN A 219 -11.310 35.507 -23.951 1.00 21.20 O ANISOU 399 OE1 GLN A 219 2466 2709 2879 32 -249 199 O ATOM 400 NE2 GLN A 219 -11.734 33.656 -25.135 1.00 16.58 N ANISOU 400 NE2 GLN A 219 1897 2101 2301 44 -339 188 N ATOM 401 N LYS A 220 -12.712 35.524 -18.661 1.00 18.44 N ANISOU 401 N LYS A 220 2036 2342 2628 -23 -116 251 N ATOM 402 CA LYS A 220 -12.238 35.745 -17.297 1.00 20.35 C ANISOU 402 CA LYS A 220 2280 2592 2859 -31 -69 251 C ATOM 403 C LYS A 220 -13.179 35.083 -16.305 1.00 14.15 C ANISOU 403 C LYS A 220 1467 1793 2116 -42 -62 273 C ATOM 404 O LYS A 220 -12.740 34.347 -15.421 1.00 12.23 O ANISOU 404 O LYS A 220 1228 1553 1866 -51 -53 268 O ATOM 405 CB LYS A 220 -12.141 37.247 -16.994 1.00 18.57 C ANISOU 405 CB LYS A 220 2061 2372 2622 -27 -24 254 C ATOM 406 CG LYS A 220 -11.009 37.960 -17.740 1.00 19.28 C ANISOU 406 CG LYS A 220 2179 2478 2666 -20 -23 234 C ATOM 407 CD LYS A 220 -10.968 39.470 -17.410 1.00 22.74 C ANISOU 407 CD LYS A 220 2625 2919 3096 -18 18 239 C ATOM 408 CE LYS A 220 -9.974 40.210 -18.309 1.00 22.88 C ANISOU 408 CE LYS A 220 2667 2952 3075 -13 14 225 C ATOM 409 NZ LYS A 220 -9.969 41.678 -18.074 1.00 22.51 N ANISOU 409 NZ LYS A 220 2629 2903 3021 -11 48 231 N ATOM 410 N PHE A 221 -14.476 35.339 -16.469 1.00 12.67 N ANISOU 410 N PHE A 221 1250 1591 1972 -40 -66 298 N ATOM 411 CA PHE A 221 -15.494 34.830 -15.548 1.00 14.36 C ANISOU 411 CA PHE A 221 1431 1794 2230 -49 -54 325 C ATOM 412 C PHE A 221 -15.376 33.303 -15.410 1.00 18.03 C ANISOU 412 C PHE A 221 1894 2252 2705 -62 -92 324 C ATOM 413 O PHE A 221 -15.422 32.763 -14.303 1.00 22.60 O ANISOU 413 O PHE A 221 2464 2831 3293 -72 -72 334 O ATOM 414 CB PHE A 221 -16.887 35.229 -16.051 1.00 11.59 C ANISOU 414 CB PHE A 221 1046 1429 1927 -44 -65 354 C ATOM 415 CG PHE A 221 -18.020 34.894 -15.102 1.00 15.06 C ANISOU 415 CG PHE A 221 1446 1859 2415 -51 -46 388 C ATOM 416 CD1 PHE A 221 -18.366 35.766 -14.073 1.00 20.40 C ANISOU 416 CD1 PHE A 221 2112 2541 3097 -44 13 403 C ATOM 417 CD2 PHE A 221 -18.761 33.730 -15.265 1.00 16.29 C ANISOU 417 CD2 PHE A 221 1576 2002 2613 -64 -88 408 C ATOM 418 CE1 PHE A 221 -19.420 35.475 -13.210 1.00 20.93 C ANISOU 418 CE1 PHE A 221 2143 2603 3208 -47 35 437 C ATOM 419 CE2 PHE A 221 -19.819 33.422 -14.407 1.00 15.92 C ANISOU 419 CE2 PHE A 221 1489 1949 2613 -71 -69 445 C ATOM 420 CZ PHE A 221 -20.148 34.297 -13.377 1.00 19.58 C ANISOU 420 CZ PHE A 221 1940 2420 3079 -62 -6 460 C ATOM 421 N GLN A 222 -15.214 32.621 -16.540 1.00 12.67 N ANISOU 421 N GLN A 222 1226 1567 2022 -60 -147 312 N ATOM 422 CA GLN A 222 -15.139 31.165 -16.571 1.00 12.71 C ANISOU 422 CA GLN A 222 1232 1562 2036 -70 -191 309 C ATOM 423 C GLN A 222 -13.881 30.656 -15.893 1.00 15.00 C ANISOU 423 C GLN A 222 1549 1865 2286 -73 -177 286 C ATOM 424 O GLN A 222 -13.921 29.671 -15.158 1.00 17.15 O ANISOU 424 O GLN A 222 1816 2131 2571 -86 -184 292 O ATOM 425 CB GLN A 222 -15.145 30.660 -18.016 1.00 11.52 C ANISOU 425 CB GLN A 222 1095 1401 1881 -62 -254 296 C ATOM 426 CG GLN A 222 -16.453 30.896 -18.769 1.00 16.08 C ANISOU 426 CG GLN A 222 1645 1960 2504 -62 -283 321 C ATOM 427 CD GLN A 222 -16.370 30.413 -20.210 1.00 19.66 C ANISOU 427 CD GLN A 222 2121 2403 2947 -53 -347 305 C ATOM 428 OE1 GLN A 222 -15.662 31.000 -21.030 1.00 17.77 O ANISOU 428 OE1 GLN A 222 1910 2176 2667 -36 -347 283 O ATOM 429 NE2 GLN A 222 -17.080 29.328 -20.520 1.00 18.64 N ANISOU 429 NE2 GLN A 222 1980 2249 2852 -63 -403 318 N ATOM 430 N LEU A 223 -12.753 31.298 -16.187 1.00 17.58 N ANISOU 430 N LEU A 223 1905 2209 2564 -63 -160 260 N ATOM 431 CA LEU A 223 -11.483 30.936 -15.567 1.00 16.21 C ANISOU 431 CA LEU A 223 1756 2051 2351 -65 -145 238 C ATOM 432 C LEU A 223 -11.602 31.109 -14.067 1.00 14.71 C ANISOU 432 C LEU A 223 1556 1863 2171 -77 -98 252 C ATOM 433 O LEU A 223 -11.155 30.257 -13.311 1.00 21.87 O ANISOU 433 O LEU A 223 2469 2770 3071 -86 -99 248 O ATOM 434 CB LEU A 223 -10.339 31.806 -16.109 1.00 20.96 C ANISOU 434 CB LEU A 223 2385 2674 2905 -52 -129 214 C ATOM 435 CG LEU A 223 -9.757 31.437 -17.479 1.00 21.50 C ANISOU 435 CG LEU A 223 2475 2747 2947 -37 -172 194 C ATOM 436 CD1 LEU A 223 -8.962 32.595 -18.072 1.00 22.63 C ANISOU 436 CD1 LEU A 223 2636 2911 3053 -26 -150 182 C ATOM 437 CD2 LEU A 223 -8.901 30.191 -17.380 1.00 12.41 C ANISOU 437 CD2 LEU A 223 1341 1598 1775 -36 -197 176 C ATOM 438 N PHE A 224 -12.220 32.209 -13.636 1.00 13.74 N ANISOU 438 N PHE A 224 1419 1740 2061 -75 -57 268 N ATOM 439 CA PHE A 224 -12.385 32.463 -12.208 1.00 14.31 C ANISOU 439 CA PHE A 224 1485 1814 2139 -83 -9 282 C ATOM 440 C PHE A 224 -13.160 31.320 -11.546 1.00 18.50 C ANISOU 440 C PHE A 224 1990 2331 2706 -96 -22 304 C ATOM 441 O PHE A 224 -12.807 30.859 -10.456 1.00 13.14 O ANISOU 441 O PHE A 224 1318 1655 2019 -105 -1 305 O ATOM 442 CB PHE A 224 -13.100 33.792 -11.922 1.00 8.75 C ANISOU 442 CB PHE A 224 768 1109 1447 -74 34 298 C ATOM 443 CG PHE A 224 -12.370 35.027 -12.422 1.00 16.96 C ANISOU 443 CG PHE A 224 1832 2160 2452 -64 50 279 C ATOM 444 CD1 PHE A 224 -10.997 35.032 -12.589 1.00 14.37 C ANISOU 444 CD1 PHE A 224 1536 1846 2079 -65 46 252 C ATOM 445 CD2 PHE A 224 -13.078 36.203 -12.700 1.00 19.19 C ANISOU 445 CD2 PHE A 224 2105 2438 2747 -53 71 291 C ATOM 446 CE1 PHE A 224 -10.347 36.166 -13.042 1.00 14.62 C ANISOU 446 CE1 PHE A 224 1587 1888 2081 -58 60 240 C ATOM 447 CE2 PHE A 224 -12.428 37.348 -13.147 1.00 7.58 C ANISOU 447 CE2 PHE A 224 658 976 1246 -45 84 277 C ATOM 448 CZ PHE A 224 -11.069 37.322 -13.324 1.00 15.69 C ANISOU 448 CZ PHE A 224 1715 2017 2230 -49 78 252 C ATOM 449 N GLU A 225 -14.216 30.861 -12.204 1.00 14.86 N ANISOU 449 N GLU A 225 1502 1855 2287 -98 -56 324 N ATOM 450 CA GLU A 225 -15.054 29.838 -11.609 1.00 21.75 C ANISOU 450 CA GLU A 225 2348 2715 3201 -112 -69 351 C ATOM 451 C GLU A 225 -14.398 28.454 -11.671 1.00 23.55 C ANISOU 451 C GLU A 225 2592 2937 3419 -122 -113 336 C ATOM 452 O GLU A 225 -14.563 27.647 -10.757 1.00 25.90 O ANISOU 452 O GLU A 225 2881 3230 3731 -136 -109 351 O ATOM 453 CB GLU A 225 -16.431 29.803 -12.280 1.00 34.68 C ANISOU 453 CB GLU A 225 3948 4337 4892 -113 -96 380 C ATOM 454 CG GLU A 225 -17.236 31.093 -12.144 1.00 52.57 C ANISOU 454 CG GLU A 225 6193 6607 7175 -102 -53 400 C ATOM 455 CD GLU A 225 -17.703 31.361 -10.717 1.00 66.26 C ANISOU 455 CD GLU A 225 7908 8346 8922 -104 5 425 C ATOM 456 OE1 GLU A 225 -17.542 30.469 -9.854 1.00 71.35 O ANISOU 456 OE1 GLU A 225 8553 8990 9569 -117 8 432 O ATOM 457 OE2 GLU A 225 -18.236 32.466 -10.462 1.00 67.94 O ANISOU 457 OE2 GLU A 225 8110 8563 9143 -91 47 438 O ATOM 458 N GLN A 226 -13.649 28.183 -12.735 1.00 17.60 N ANISOU 458 N GLN A 226 1864 2185 2639 -114 -153 308 N ATOM 459 CA GLN A 226 -13.153 26.824 -12.966 1.00 13.85 C ANISOU 459 CA GLN A 226 1404 1701 2157 -120 -202 294 C ATOM 460 C GLN A 226 -11.752 26.583 -12.413 1.00 18.94 C ANISOU 460 C GLN A 226 2081 2360 2754 -117 -186 267 C ATOM 461 O GLN A 226 -11.396 25.448 -12.137 1.00 19.70 O ANISOU 461 O GLN A 226 2187 2450 2849 -125 -213 261 O ATOM 462 CB GLN A 226 -13.170 26.486 -14.454 1.00 18.00 C ANISOU 462 CB GLN A 226 1942 2217 2680 -109 -260 280 C ATOM 463 CG GLN A 226 -14.544 26.469 -15.083 1.00 17.64 C ANISOU 463 CG GLN A 226 1867 2152 2685 -113 -290 307 C ATOM 464 CD GLN A 226 -14.479 26.138 -16.567 1.00 22.58 C ANISOU 464 CD GLN A 226 2511 2766 3302 -101 -351 290 C ATOM 465 OE1 GLN A 226 -13.753 25.228 -16.977 1.00 20.42 O ANISOU 465 OE1 GLN A 226 2267 2488 3004 -96 -389 266 O ATOM 466 NE2 GLN A 226 -15.249 26.869 -17.377 1.00 22.12 N ANISOU 466 NE2 GLN A 226 2439 2703 3263 -95 -360 301 N ATOM 467 N VAL A 227 -10.958 27.643 -12.269 1.00 19.33 N ANISOU 467 N VAL A 227 2147 2431 2768 -108 -145 251 N ATOM 468 CA VAL A 227 -9.616 27.504 -11.712 1.00 21.45 C ANISOU 468 CA VAL A 227 2443 2714 2992 -107 -129 227 C ATOM 469 C VAL A 227 -9.530 27.882 -10.228 1.00 20.05 C ANISOU 469 C VAL A 227 2263 2542 2811 -118 -78 238 C ATOM 470 O VAL A 227 -8.794 27.251 -9.475 1.00 18.92 O ANISOU 470 O VAL A 227 2134 2402 2651 -125 -75 229 O ATOM 471 CB VAL A 227 -8.551 28.281 -12.545 1.00 18.26 C ANISOU 471 CB VAL A 227 2063 2330 2546 -91 -125 200 C ATOM 472 CG1 VAL A 227 -7.179 28.195 -11.888 1.00 12.86 C ANISOU 472 CG1 VAL A 227 1403 1663 1821 -92 -106 180 C ATOM 473 CG2 VAL A 227 -8.494 27.726 -13.963 1.00 17.77 C ANISOU 473 CG2 VAL A 227 2009 2263 2479 -77 -178 187 C ATOM 474 N ILE A 228 -10.287 28.890 -9.803 1.00 13.29 N ANISOU 474 N ILE A 228 1391 1686 1971 -118 -38 257 N ATOM 475 CA ILE A 228 -10.201 29.352 -8.418 1.00 18.93 C ANISOU 475 CA ILE A 228 2109 2405 2677 -124 13 266 C ATOM 476 C ILE A 228 -11.556 29.581 -7.766 1.00 19.41 C ANISOU 476 C ILE A 228 2139 2456 2778 -128 41 301 C ATOM 477 O ILE A 228 -11.651 30.336 -6.800 1.00 15.59 O ANISOU 477 O ILE A 228 1660 1976 2286 -126 89 309 O ATOM 478 CB ILE A 228 -9.407 30.683 -8.275 1.00 20.42 C ANISOU 478 CB ILE A 228 2321 2608 2828 -116 51 250 C ATOM 479 CG1 ILE A 228 -10.070 31.818 -9.065 1.00 18.82 C ANISOU 479 CG1 ILE A 228 2107 2405 2637 -104 60 256 C ATOM 480 CG2 ILE A 228 -7.956 30.505 -8.694 1.00 19.27 C ANISOU 480 CG2 ILE A 228 2203 2477 2641 -113 32 219 C ATOM 481 CD1 ILE A 228 -9.456 33.183 -8.771 1.00 17.37 C ANISOU 481 CD1 ILE A 228 1946 2233 2423 -98 99 246 C ATOM 482 N GLY A 229 -12.595 28.932 -8.283 1.00 18.26 N ANISOU 482 N GLY A 229 1964 2296 2676 -132 9 322 N ATOM 483 CA GLY A 229 -13.941 29.153 -7.780 1.00 18.73 C ANISOU 483 CA GLY A 229 1989 2349 2779 -134 33 359 C ATOM 484 C GLY A 229 -14.440 28.081 -6.828 1.00 17.38 C ANISOU 484 C GLY A 229 1800 2170 2634 -150 33 385 C ATOM 485 O GLY A 229 -15.270 28.355 -5.956 1.00 19.39 O ANISOU 485 O GLY A 229 2032 2424 2911 -151 73 414 O ATOM 486 N ARG A 230 -13.945 26.858 -7.001 1.00 17.73 N ANISOU 486 N ARG A 230 1854 2206 2675 -162 -11 374 N ATOM 487 CA ARG A 230 -14.344 25.736 -6.146 1.00 26.25 C ANISOU 487 CA ARG A 230 2919 3276 3779 -179 -18 398 C ATOM 488 C ARG A 230 -13.145 25.222 -5.365 1.00 25.47 C ANISOU 488 C ARG A 230 2854 3183 3640 -184 -12 376 C ATOM 489 O ARG A 230 -12.088 24.968 -5.950 1.00 20.95 O ANISOU 489 O ARG A 230 2311 2615 3036 -180 -41 342 O ATOM 490 CB ARG A 230 -14.918 24.589 -6.980 1.00 29.58 C ANISOU 490 CB ARG A 230 3322 3678 4239 -191 -83 410 C ATOM 491 CG ARG A 230 -16.446 24.534 -7.087 1.00 39.51 C ANISOU 491 CG ARG A 230 4532 4924 5557 -199 -88 454 C ATOM 492 CD ARG A 230 -17.013 25.356 -8.249 1.00 49.51 C ANISOU 492 CD ARG A 230 5784 6189 6839 -186 -101 454 C ATOM 493 NE ARG A 230 -16.338 25.183 -9.543 1.00 53.28 N ANISOU 493 NE ARG A 230 6288 6661 7293 -178 -153 420 N ATOM 494 CZ ARG A 230 -15.783 24.057 -9.992 1.00 53.70 C ANISOU 494 CZ ARG A 230 6362 6704 7338 -185 -207 402 C ATOM 495 NH1 ARG A 230 -15.802 22.947 -9.264 1.00 52.76 N ANISOU 495 NH1 ARG A 230 6240 6574 7232 -202 -222 415 N ATOM 496 NH2 ARG A 230 -15.204 24.044 -11.187 1.00 51.79 N ANISOU 496 NH2 ARG A 230 6146 6460 7072 -172 -247 371 N ATOM 497 N LYS A 231 -13.321 25.044 -4.056 1.00 23.75 N ANISOU 497 N LYS A 231 2634 2968 3424 -193 25 395 N ATOM 498 CA LYS A 231 -12.216 24.687 -3.172 1.00 21.13 C ANISOU 498 CA LYS A 231 2335 2642 3053 -198 36 376 C ATOM 499 C LYS A 231 -11.470 23.439 -3.608 1.00 21.58 C ANISOU 499 C LYS A 231 2408 2691 3102 -206 -20 357 C ATOM 500 O LYS A 231 -10.238 23.432 -3.637 1.00 17.46 O ANISOU 500 O LYS A 231 1918 2177 2539 -201 -26 325 O ATOM 501 CB LYS A 231 -12.679 24.494 -1.730 1.00 26.80 C ANISOU 501 CB LYS A 231 3044 3359 3778 -207 78 406 C ATOM 502 CG LYS A 231 -11.497 24.354 -0.762 1.00 35.14 C ANISOU 502 CG LYS A 231 4140 4423 4789 -209 95 384 C ATOM 503 CD LYS A 231 -11.908 23.704 0.546 1.00 40.55 C ANISOU 503 CD LYS A 231 4819 5104 5484 -222 119 414 C ATOM 504 CE LYS A 231 -12.868 24.577 1.318 1.00 46.21 C ANISOU 504 CE LYS A 231 5519 5827 6212 -213 179 444 C ATOM 505 NZ LYS A 231 -12.158 25.431 2.305 1.00 51.62 N ANISOU 505 NZ LYS A 231 6240 6522 6850 -203 227 428 N ATOM 506 N ASP A 232 -12.198 22.373 -3.923 1.00 18.41 N ANISOU 506 N ASP A 232 1984 2272 2740 -219 -63 378 N ATOM 507 CA ASP A 232 -11.524 21.117 -4.226 1.00 20.74 C ANISOU 507 CA ASP A 232 2297 2555 3028 -226 -117 360 C ATOM 508 C ASP A 232 -10.713 21.177 -5.530 1.00 20.03 C ANISOU 508 C ASP A 232 2229 2467 2912 -210 -156 322 C ATOM 509 O ASP A 232 -9.543 20.802 -5.538 1.00 22.65 O ANISOU 509 O ASP A 232 2592 2806 3209 -204 -169 293 O ATOM 510 CB ASP A 232 -12.456 19.891 -4.130 1.00 22.00 C ANISOU 510 CB ASP A 232 2432 2692 3235 -246 -156 393 C ATOM 511 CG ASP A 232 -13.709 20.013 -4.991 1.00 25.36 C ANISOU 511 CG ASP A 232 2821 3105 3708 -248 -179 418 C ATOM 512 OD1 ASP A 232 -13.928 21.053 -5.652 1.00 25.74 O ANISOU 512 OD1 ASP A 232 2863 3163 3754 -233 -163 412 O ATOM 513 OD2 ASP A 232 -14.491 19.044 -5.005 1.00 26.62 O ANISOU 513 OD2 ASP A 232 2959 3245 3910 -266 -216 447 O ATOM 514 N ASP A 233 -11.298 21.689 -6.610 1.00 16.92 N ANISOU 514 N ASP A 233 1821 2071 2535 -201 -171 324 N ATOM 515 CA ASP A 233 -10.531 21.855 -7.843 1.00 19.00 C ANISOU 515 CA ASP A 233 2107 2340 2770 -183 -202 289 C ATOM 516 C ASP A 233 -9.337 22.812 -7.656 1.00 20.52 C ANISOU 516 C ASP A 233 2327 2558 2914 -169 -163 261 C ATOM 517 O ASP A 233 -8.264 22.603 -8.227 1.00 19.86 O ANISOU 517 O ASP A 233 2268 2482 2795 -157 -184 230 O ATOM 518 CB ASP A 233 -11.421 22.315 -8.990 1.00 22.49 C ANISOU 518 CB ASP A 233 2530 2775 3239 -176 -223 298 C ATOM 519 CG ASP A 233 -12.261 21.187 -9.558 1.00 27.99 C ANISOU 519 CG ASP A 233 3213 3445 3978 -186 -284 315 C ATOM 520 OD1 ASP A 233 -12.093 20.041 -9.097 1.00 31.66 O ANISOU 520 OD1 ASP A 233 3684 3897 4449 -199 -311 318 O ATOM 521 OD2 ASP A 233 -13.083 21.443 -10.466 1.00 28.40 O ANISOU 521 OD2 ASP A 233 3247 3487 4055 -183 -308 325 O ATOM 522 N PHE A 234 -9.535 23.854 -6.855 1.00 17.40 N ANISOU 522 N PHE A 234 1924 2174 2514 -170 -106 273 N ATOM 523 CA PHE A 234 -8.466 24.798 -6.551 1.00 14.73 C ANISOU 523 CA PHE A 234 1609 1855 2130 -161 -70 250 C ATOM 524 C PHE A 234 -7.261 24.117 -5.871 1.00 15.35 C ANISOU 524 C PHE A 234 1715 1940 2178 -166 -74 231 C ATOM 525 O PHE A 234 -6.107 24.330 -6.255 1.00 15.16 O ANISOU 525 O PHE A 234 1712 1929 2117 -156 -79 204 O ATOM 526 CB PHE A 234 -9.004 25.922 -5.674 1.00 8.76 C ANISOU 526 CB PHE A 234 844 1105 1378 -163 -12 269 C ATOM 527 CG PHE A 234 -7.927 26.801 -5.080 1.00 17.60 C ANISOU 527 CG PHE A 234 1992 2241 2454 -158 25 249 C ATOM 528 CD1 PHE A 234 -7.350 27.824 -5.832 1.00 18.55 C ANISOU 528 CD1 PHE A 234 2125 2374 2551 -146 32 230 C ATOM 529 CD2 PHE A 234 -7.490 26.601 -3.774 1.00 13.11 C ANISOU 529 CD2 PHE A 234 1438 1673 1869 -168 51 251 C ATOM 530 CE1 PHE A 234 -6.358 28.643 -5.284 1.00 11.72 C ANISOU 530 CE1 PHE A 234 1285 1521 1648 -145 62 215 C ATOM 531 CE2 PHE A 234 -6.500 27.400 -3.225 1.00 13.90 C ANISOU 531 CE2 PHE A 234 1566 1785 1930 -165 80 234 C ATOM 532 CZ PHE A 234 -5.934 28.426 -3.984 1.00 13.64 C ANISOU 532 CZ PHE A 234 1543 1764 1875 -155 84 216 C ATOM 533 N LEU A 235 -7.533 23.297 -4.866 1.00 14.30 N ANISOU 533 N LEU A 235 1577 1796 2058 -180 -72 248 N ATOM 534 CA LEU A 235 -6.469 22.550 -4.196 1.00 21.67 C ANISOU 534 CA LEU A 235 2536 2733 2966 -185 -81 233 C ATOM 535 C LEU A 235 -5.796 21.592 -5.163 1.00 19.12 C ANISOU 535 C LEU A 235 2225 2406 2633 -176 -136 210 C ATOM 536 O LEU A 235 -4.572 21.460 -5.182 1.00 16.25 O ANISOU 536 O LEU A 235 1884 2054 2235 -168 -142 185 O ATOM 537 CB LEU A 235 -7.014 21.782 -2.985 1.00 22.02 C ANISOU 537 CB LEU A 235 2572 2764 3030 -203 -72 259 C ATOM 538 CG LEU A 235 -7.185 22.705 -1.776 1.00 34.56 C ANISOU 538 CG LEU A 235 4162 4361 4608 -207 -11 273 C ATOM 539 CD1 LEU A 235 -8.025 22.079 -0.647 1.00 35.45 C ANISOU 539 CD1 LEU A 235 4261 4462 4746 -223 4 307 C ATOM 540 CD2 LEU A 235 -5.809 23.150 -1.274 1.00 32.60 C ANISOU 540 CD2 LEU A 235 3947 4127 4312 -203 6 246 C ATOM 541 N LYS A 236 -6.613 20.924 -5.965 1.00 18.99 N ANISOU 541 N LYS A 236 2194 2373 2649 -177 -177 219 N ATOM 542 CA LYS A 236 -6.120 19.947 -6.917 1.00 20.93 C ANISOU 542 CA LYS A 236 2454 2610 2887 -166 -233 198 C ATOM 543 C LYS A 236 -5.097 20.563 -7.871 1.00 18.52 C ANISOU 543 C LYS A 236 2168 2325 2544 -143 -234 167 C ATOM 544 O LYS A 236 -4.051 19.976 -8.130 1.00 23.73 O ANISOU 544 O LYS A 236 2850 2992 3177 -131 -257 143 O ATOM 545 CB LYS A 236 -7.293 19.359 -7.691 1.00 22.73 C ANISOU 545 CB LYS A 236 2664 2815 3158 -170 -277 215 C ATOM 546 CG LYS A 236 -6.904 18.522 -8.877 1.00 32.87 C ANISOU 546 CG LYS A 236 3967 4089 4433 -154 -337 192 C ATOM 547 CD LYS A 236 -6.354 17.193 -8.445 1.00 47.98 C ANISOU 547 CD LYS A 236 5900 5990 6342 -158 -371 184 C ATOM 548 CE LYS A 236 -6.798 16.105 -9.412 1.00 53.83 C ANISOU 548 CE LYS A 236 6648 6702 7102 -154 -440 181 C ATOM 549 NZ LYS A 236 -8.281 16.077 -9.517 1.00 52.00 N ANISOU 549 NZ LYS A 236 6386 6450 6923 -173 -454 215 N ATOM 550 N LEU A 237 -5.392 21.749 -8.390 1.00 15.02 N ANISOU 550 N LEU A 237 1715 1893 2098 -136 -209 168 N ATOM 551 CA LEU A 237 -4.479 22.390 -9.329 1.00 16.87 C ANISOU 551 CA LEU A 237 1964 2147 2297 -115 -209 143 C ATOM 552 C LEU A 237 -3.305 23.046 -8.613 1.00 16.38 C ANISOU 552 C LEU A 237 1917 2108 2200 -115 -170 131 C ATOM 553 O LEU A 237 -2.178 23.080 -9.141 1.00 17.39 O ANISOU 553 O LEU A 237 2061 2253 2294 -100 -177 108 O ATOM 554 CB LEU A 237 -5.207 23.418 -10.187 1.00 17.12 C ANISOU 554 CB LEU A 237 1982 2181 2340 -109 -199 150 C ATOM 555 CG LEU A 237 -6.326 22.876 -11.066 1.00 16.81 C ANISOU 555 CG LEU A 237 1931 2121 2337 -107 -242 161 C ATOM 556 CD1 LEU A 237 -6.907 23.990 -11.922 1.00 21.64 C ANISOU 556 CD1 LEU A 237 2531 2737 2955 -99 -231 167 C ATOM 557 CD2 LEU A 237 -5.813 21.754 -11.951 1.00 17.81 C ANISOU 557 CD2 LEU A 237 2078 2239 2450 -92 -298 140 C ATOM 558 N SER A 238 -3.561 23.571 -7.416 1.00 15.32 N ANISOU 558 N SER A 238 1777 1974 2071 -131 -129 147 N ATOM 559 CA SER A 238 -2.502 24.218 -6.649 1.00 17.50 C ANISOU 559 CA SER A 238 2068 2268 2314 -134 -95 137 C ATOM 560 C SER A 238 -1.410 23.220 -6.279 1.00 23.70 C ANISOU 560 C SER A 238 2870 3057 3078 -133 -116 121 C ATOM 561 O SER A 238 -0.229 23.579 -6.217 1.00 22.27 O ANISOU 561 O SER A 238 2703 2894 2866 -127 -106 106 O ATOM 562 CB SER A 238 -3.062 24.877 -5.391 1.00 12.30 C ANISOU 562 CB SER A 238 1405 1605 1665 -150 -50 157 C ATOM 563 OG SER A 238 -3.873 25.980 -5.744 1.00 18.20 O ANISOU 563 OG SER A 238 2139 2352 2425 -146 -26 168 O ATOM 564 N THR A 239 -1.813 21.971 -6.046 1.00 22.62 N ANISOU 564 N THR A 239 2732 2901 2961 -138 -147 127 N ATOM 565 CA THR A 239 -0.883 20.912 -5.659 1.00 29.08 C ANISOU 565 CA THR A 239 3566 3719 3764 -137 -170 114 C ATOM 566 C THR A 239 -0.354 20.151 -6.878 1.00 30.01 C ANISOU 566 C THR A 239 3693 3838 3870 -115 -216 93 C ATOM 567 O THR A 239 0.380 19.170 -6.745 1.00 27.72 O ANISOU 567 O THR A 239 3417 3546 3569 -108 -242 80 O ATOM 568 CB THR A 239 -1.543 19.898 -4.676 1.00 14.16 C ANISOU 568 CB THR A 239 1673 1807 1900 -156 -181 133 C ATOM 569 OG1 THR A 239 -2.762 19.388 -5.248 1.00 18.23 O ANISOU 569 OG1 THR A 239 2172 2302 2453 -159 -209 148 O ATOM 570 CG2 THR A 239 -1.843 20.563 -3.305 1.00 11.99 C ANISOU 570 CG2 THR A 239 1396 1533 1626 -174 -133 152 C ATOM 571 N ASN A 240 -0.737 20.602 -8.066 1.00 24.14 N ANISOU 571 N ASN A 240 2944 3098 3130 -101 -226 89 N ATOM 572 CA ASN A 240 -0.320 19.932 -9.284 1.00 19.34 C ANISOU 572 CA ASN A 240 2349 2491 2510 -76 -268 68 C ATOM 573 C ASN A 240 0.916 20.560 -9.897 1.00 17.63 C ANISOU 573 C ASN A 240 2142 2305 2254 -55 -254 48 C ATOM 574 O ASN A 240 1.043 21.789 -9.970 1.00 14.95 O ANISOU 574 O ASN A 240 1794 1982 1904 -57 -219 52 O ATOM 575 CB ASN A 240 -1.444 19.912 -10.314 1.00 15.86 C ANISOU 575 CB ASN A 240 1899 2034 2094 -71 -294 75 C ATOM 576 CG ASN A 240 -1.069 19.131 -11.561 1.00 22.00 C ANISOU 576 CG ASN A 240 2695 2808 2856 -43 -342 53 C ATOM 577 OD1 ASN A 240 -0.809 19.716 -12.615 1.00 26.16 O ANISOU 577 OD1 ASN A 240 3227 3350 3364 -23 -342 42 O ATOM 578 ND2 ASN A 240 -1.022 17.801 -11.442 1.00 15.41 N ANISOU 578 ND2 ASN A 240 1873 1953 2028 -41 -384 48 N ATOM 579 N ILE A 241 1.804 19.695 -10.370 1.00 20.28 N ANISOU 579 N ILE A 241 2493 2645 2567 -33 -284 29 N ATOM 580 CA ILE A 241 3.091 20.090 -10.941 1.00 18.66 C ANISOU 580 CA ILE A 241 2296 2471 2324 -11 -273 11 C ATOM 581 C ILE A 241 2.922 21.123 -12.063 1.00 21.62 C ANISOU 581 C ILE A 241 2665 2860 2688 3 -261 11 C ATOM 582 O ILE A 241 3.690 22.086 -12.163 1.00 21.02 O ANISOU 582 O ILE A 241 2585 2811 2590 6 -230 10 O ATOM 583 CB ILE A 241 3.839 18.836 -11.415 1.00 22.29 C ANISOU 583 CB ILE A 241 2774 2930 2766 16 -313 -9 C ATOM 584 CG1 ILE A 241 5.133 19.188 -12.152 1.00 27.68 C ANISOU 584 CG1 ILE A 241 3462 3646 3410 45 -302 -24 C ATOM 585 CG2 ILE A 241 2.913 17.948 -12.278 1.00 14.87 C ANISOU 585 CG2 ILE A 241 1844 1961 1844 28 -361 -13 C ATOM 586 CD1 ILE A 241 5.990 17.941 -12.436 1.00 30.10 C ANISOU 586 CD1 ILE A 241 3786 3953 3696 74 -336 -44 C ATOM 587 N PHE A 242 1.900 20.950 -12.894 1.00 24.01 N ANISOU 587 N PHE A 242 2968 3145 3010 8 -286 13 N ATOM 588 CA PHE A 242 1.625 21.940 -13.936 1.00 23.14 C ANISOU 588 CA PHE A 242 2853 3046 2892 19 -276 14 C ATOM 589 C PHE A 242 0.553 22.925 -13.522 1.00 23.10 C ANISOU 589 C PHE A 242 2829 3032 2916 -6 -249 35 C ATOM 590 O PHE A 242 0.713 24.125 -13.713 1.00 20.02 O ANISOU 590 O PHE A 242 2433 2659 2515 -7 -217 40 O ATOM 591 CB PHE A 242 1.225 21.258 -15.230 1.00 16.82 C ANISOU 591 CB PHE A 242 2067 2234 2090 44 -322 2 C ATOM 592 CG PHE A 242 2.149 20.160 -15.607 1.00 23.07 C ANISOU 592 CG PHE A 242 2880 3029 2856 72 -352 -19 C ATOM 593 CD1 PHE A 242 3.519 20.412 -15.727 1.00 20.69 C ANISOU 593 CD1 PHE A 242 2584 2761 2517 91 -330 -31 C ATOM 594 CD2 PHE A 242 1.674 18.876 -15.807 1.00 23.01 C ANISOU 594 CD2 PHE A 242 2889 2993 2862 79 -402 -26 C ATOM 595 CE1 PHE A 242 4.393 19.404 -16.056 1.00 21.54 C ANISOU 595 CE1 PHE A 242 2711 2875 2600 120 -355 -50 C ATOM 596 CE2 PHE A 242 2.548 17.855 -16.145 1.00 29.43 C ANISOU 596 CE2 PHE A 242 3725 3808 3649 108 -430 -48 C ATOM 597 CZ PHE A 242 3.906 18.117 -16.271 1.00 25.30 C ANISOU 597 CZ PHE A 242 3206 3320 3088 130 -405 -60 C ATOM 598 N GLY A 243 -0.535 22.408 -12.958 1.00 17.28 N ANISOU 598 N GLY A 243 2084 2268 2216 -24 -262 50 N ATOM 599 CA GLY A 243 -1.661 23.241 -12.578 1.00 16.73 C ANISOU 599 CA GLY A 243 1993 2187 2175 -44 -238 72 C ATOM 600 C GLY A 243 -1.308 24.463 -11.746 1.00 18.28 C ANISOU 600 C GLY A 243 2183 2400 2361 -58 -185 80 C ATOM 601 O GLY A 243 -1.960 25.499 -11.856 1.00 18.03 O ANISOU 601 O GLY A 243 2140 2369 2342 -63 -161 93 O ATOM 602 N ASN A 244 -0.288 24.356 -10.898 1.00 18.02 N ANISOU 602 N ASN A 244 2159 2380 2307 -63 -168 73 N ATOM 603 CA ASN A 244 -0.030 25.431 -9.953 1.00 14.23 C ANISOU 603 CA ASN A 244 1676 1910 1820 -78 -122 82 C ATOM 604 C ASN A 244 0.310 26.735 -10.667 1.00 18.43 C ANISOU 604 C ASN A 244 2207 2461 2334 -71 -100 80 C ATOM 605 O ASN A 244 0.048 27.813 -10.144 1.00 21.44 O ANISOU 605 O ASN A 244 2585 2844 2719 -83 -66 91 O ATOM 606 CB ASN A 244 1.056 25.040 -8.945 1.00 13.91 C ANISOU 606 CB ASN A 244 1646 1878 1759 -86 -114 75 C ATOM 607 CG ASN A 244 2.453 25.170 -9.508 1.00 17.71 C ANISOU 607 CG ASN A 244 2137 2386 2206 -70 -117 58 C ATOM 608 OD1 ASN A 244 3.019 26.265 -9.525 1.00 18.91 O ANISOU 608 OD1 ASN A 244 2289 2556 2341 -72 -89 59 O ATOM 609 ND2 ASN A 244 3.026 24.051 -9.965 1.00 9.94 N ANISOU 609 ND2 ASN A 244 1161 1404 1211 -53 -150 44 N ATOM 610 N TYR A 245 0.888 26.634 -11.863 1.00 12.28 N ANISOU 610 N TYR A 245 1433 1696 1534 -49 -120 66 N ATOM 611 CA TYR A 245 1.203 27.814 -12.648 1.00 15.50 C ANISOU 611 CA TYR A 245 1840 2123 1925 -41 -102 66 C ATOM 612 C TYR A 245 -0.077 28.497 -13.137 1.00 21.48 C ANISOU 612 C TYR A 245 2587 2866 2707 -44 -99 79 C ATOM 613 O TYR A 245 -0.168 29.729 -13.149 1.00 17.82 O ANISOU 613 O TYR A 245 2120 2408 2241 -49 -70 87 O ATOM 614 CB TYR A 245 2.090 27.463 -13.849 1.00 17.40 C ANISOU 614 CB TYR A 245 2090 2384 2137 -15 -124 50 C ATOM 615 CG TYR A 245 3.527 27.155 -13.498 1.00 23.44 C ANISOU 615 CG TYR A 245 2862 3171 2874 -10 -118 40 C ATOM 616 CD1 TYR A 245 4.495 28.155 -13.471 1.00 23.32 C ANISOU 616 CD1 TYR A 245 2843 3181 2835 -13 -90 44 C ATOM 617 CD2 TYR A 245 3.917 25.858 -13.196 1.00 22.39 C ANISOU 617 CD2 TYR A 245 2736 3033 2738 -2 -143 30 C ATOM 618 CE1 TYR A 245 5.816 27.861 -13.147 1.00 21.74 C ANISOU 618 CE1 TYR A 245 2646 3002 2613 -9 -87 38 C ATOM 619 CE2 TYR A 245 5.217 25.556 -12.881 1.00 19.06 C ANISOU 619 CE2 TYR A 245 2318 2632 2292 4 -140 22 C ATOM 620 CZ TYR A 245 6.159 26.547 -12.853 1.00 22.56 C ANISOU 620 CZ TYR A 245 2756 3101 2714 0 -112 26 C ATOM 621 OH TYR A 245 7.443 26.207 -12.521 1.00 22.27 O ANISOU 621 OH TYR A 245 2720 3085 2658 6 -110 21 O ATOM 622 N LEU A 246 -1.055 27.691 -13.545 1.00 17.74 N ANISOU 622 N LEU A 246 2110 2372 2259 -39 -130 82 N ATOM 623 CA LEU A 246 -2.306 28.225 -14.060 1.00 17.38 C ANISOU 623 CA LEU A 246 2051 2312 2240 -41 -132 95 C ATOM 624 C LEU A 246 -3.082 28.882 -12.925 1.00 17.81 C ANISOU 624 C LEU A 246 2092 2355 2320 -62 -97 115 C ATOM 625 O LEU A 246 -3.747 29.887 -13.124 1.00 17.06 O ANISOU 625 O LEU A 246 1988 2257 2237 -63 -78 126 O ATOM 626 CB LEU A 246 -3.154 27.131 -14.707 1.00 18.25 C ANISOU 626 CB LEU A 246 2159 2400 2374 -34 -179 95 C ATOM 627 CG LEU A 246 -4.463 27.665 -15.307 1.00 20.53 C ANISOU 627 CG LEU A 246 2433 2674 2695 -35 -186 111 C ATOM 628 CD1 LEU A 246 -4.166 28.570 -16.496 1.00 16.21 C ANISOU 628 CD1 LEU A 246 1894 2143 2124 -18 -184 104 C ATOM 629 CD2 LEU A 246 -5.394 26.535 -15.693 1.00 19.34 C ANISOU 629 CD2 LEU A 246 2277 2497 2574 -35 -234 116 C ATOM 630 N VAL A 247 -2.994 28.316 -11.729 1.00 10.56 N ANISOU 630 N VAL A 247 1173 1429 1408 -75 -88 119 N ATOM 631 CA VAL A 247 -3.634 28.941 -10.585 1.00 10.79 C ANISOU 631 CA VAL A 247 1195 1451 1456 -92 -51 136 C ATOM 632 C VAL A 247 -3.057 30.326 -10.320 1.00 14.96 C ANISOU 632 C VAL A 247 1731 1992 1960 -94 -12 135 C ATOM 633 O VAL A 247 -3.796 31.290 -10.105 1.00 14.80 O ANISOU 633 O VAL A 247 1703 1965 1953 -97 14 148 O ATOM 634 CB VAL A 247 -3.468 28.099 -9.322 1.00 15.13 C ANISOU 634 CB VAL A 247 1748 1993 2009 -105 -46 140 C ATOM 635 CG1 VAL A 247 -3.839 28.930 -8.091 1.00 9.56 C ANISOU 635 CG1 VAL A 247 1041 1284 1309 -118 0 155 C ATOM 636 CG2 VAL A 247 -4.319 26.819 -9.424 1.00 12.53 C ANISOU 636 CG2 VAL A 247 1406 1644 1711 -108 -82 149 C ATOM 637 N GLN A 248 -1.731 30.426 -10.336 1.00 14.03 N ANISOU 637 N GLN A 248 1629 1894 1809 -92 -10 120 N ATOM 638 CA GLN A 248 -1.082 31.704 -10.095 1.00 18.35 C ANISOU 638 CA GLN A 248 2185 2453 2334 -96 21 119 C ATOM 639 C GLN A 248 -1.436 32.748 -11.152 1.00 19.88 C ANISOU 639 C GLN A 248 2375 2651 2528 -87 25 122 C ATOM 640 O GLN A 248 -1.597 33.929 -10.827 1.00 20.18 O ANISOU 640 O GLN A 248 2417 2688 2565 -93 54 130 O ATOM 641 CB GLN A 248 0.435 31.527 -9.994 1.00 15.08 C ANISOU 641 CB GLN A 248 1784 2059 1886 -96 18 105 C ATOM 642 CG GLN A 248 0.848 30.577 -8.874 1.00 17.23 C ANISOU 642 CG GLN A 248 2063 2327 2156 -106 14 102 C ATOM 643 CD GLN A 248 2.342 30.386 -8.810 1.00 15.68 C ANISOU 643 CD GLN A 248 1876 2151 1930 -105 9 90 C ATOM 644 OE1 GLN A 248 3.091 31.340 -8.598 1.00 16.09 O ANISOU 644 OE1 GLN A 248 1935 2215 1963 -112 28 90 O ATOM 645 NE2 GLN A 248 2.790 29.151 -9.007 1.00 10.59 N ANISOU 645 NE2 GLN A 248 1233 1511 1282 -96 -19 79 N ATOM 646 N SER A 249 -1.545 32.309 -12.407 1.00 15.93 N ANISOU 646 N SER A 249 1869 2155 2028 -72 -5 117 N ATOM 647 CA SER A 249 -1.900 33.200 -13.512 1.00 17.78 C ANISOU 647 CA SER A 249 2100 2393 2261 -62 -5 120 C ATOM 648 C SER A 249 -3.324 33.694 -13.373 1.00 10.34 C ANISOU 648 C SER A 249 1145 1431 1354 -65 5 137 C ATOM 649 O SER A 249 -3.603 34.876 -13.583 1.00 16.46 O ANISOU 649 O SER A 249 1919 2205 2129 -65 25 144 O ATOM 650 CB SER A 249 -1.752 32.497 -14.859 1.00 21.61 C ANISOU 650 CB SER A 249 2586 2885 2738 -42 -43 110 C ATOM 651 OG SER A 249 -0.390 32.344 -15.195 1.00 35.15 O ANISOU 651 OG SER A 249 4313 4625 4418 -34 -46 97 O ATOM 652 N VAL A 250 -4.232 32.784 -13.032 1.00 6.09 N ANISOU 652 N VAL A 250 594 875 846 -68 -10 144 N ATOM 653 CA VAL A 250 -5.632 33.176 -12.846 1.00 11.82 C ANISOU 653 CA VAL A 250 1302 1582 1608 -71 0 164 C ATOM 654 C VAL A 250 -5.840 34.091 -11.626 1.00 10.88 C ANISOU 654 C VAL A 250 1184 1459 1492 -81 46 175 C ATOM 655 O VAL A 250 -6.629 35.027 -11.679 1.00 15.26 O ANISOU 655 O VAL A 250 1731 2005 2062 -78 66 187 O ATOM 656 CB VAL A 250 -6.557 31.957 -12.826 1.00 14.73 C ANISOU 656 CB VAL A 250 1654 1933 2011 -73 -29 173 C ATOM 657 CG1 VAL A 250 -8.005 32.366 -12.470 1.00 17.73 C ANISOU 657 CG1 VAL A 250 2010 2296 2432 -77 -13 199 C ATOM 658 CG2 VAL A 250 -6.500 31.257 -14.196 1.00 7.85 C ANISOU 658 CG2 VAL A 250 785 1062 1136 -60 -77 162 C ATOM 659 N ILE A 251 -5.128 33.830 -10.536 1.00 6.71 N ANISOU 659 N ILE A 251 669 934 947 -91 63 169 N ATOM 660 CA ILE A 251 -5.145 34.740 -9.390 1.00 12.02 C ANISOU 660 CA ILE A 251 1351 1603 1613 -98 105 176 C ATOM 661 C ILE A 251 -4.720 36.154 -9.824 1.00 16.72 C ANISOU 661 C ILE A 251 1960 2205 2189 -94 121 172 C ATOM 662 O ILE A 251 -5.361 37.146 -9.462 1.00 18.97 O ANISOU 662 O ILE A 251 2246 2480 2483 -92 149 183 O ATOM 663 CB ILE A 251 -4.230 34.233 -8.244 1.00 9.47 C ANISOU 663 CB ILE A 251 1045 1284 1269 -109 114 168 C ATOM 664 CG1 ILE A 251 -4.889 33.041 -7.528 1.00 13.22 C ANISOU 664 CG1 ILE A 251 1508 1747 1768 -115 107 178 C ATOM 665 CG2 ILE A 251 -3.910 35.355 -7.255 1.00 10.81 C ANISOU 665 CG2 ILE A 251 1236 1451 1421 -115 152 169 C ATOM 666 CD1 ILE A 251 -4.000 32.352 -6.511 1.00 11.31 C ANISOU 666 CD1 ILE A 251 1282 1509 1506 -126 108 170 C ATOM 667 N GLY A 252 -3.655 36.244 -10.617 1.00 13.06 N ANISOU 667 N GLY A 252 1505 1758 1698 -92 105 159 N ATOM 668 CA GLY A 252 -3.191 37.528 -11.118 1.00 7.31 C ANISOU 668 CA GLY A 252 788 1037 952 -91 117 157 C ATOM 669 C GLY A 252 -4.276 38.259 -11.899 1.00 15.13 C ANISOU 669 C GLY A 252 1766 2018 1964 -81 118 168 C ATOM 670 O GLY A 252 -4.481 39.464 -11.745 1.00 14.48 O ANISOU 670 O GLY A 252 1693 1930 1881 -81 141 174 O ATOM 671 N ILE A 253 -4.981 37.520 -12.747 1.00 16.98 N ANISOU 671 N ILE A 253 1983 2249 2219 -71 91 171 N ATOM 672 CA ILE A 253 -6.012 38.115 -13.584 1.00 12.03 C ANISOU 672 CA ILE A 253 1343 1613 1614 -61 86 182 C ATOM 673 C ILE A 253 -7.179 38.584 -12.707 1.00 14.42 C ANISOU 673 C ILE A 253 1635 1897 1946 -62 114 199 C ATOM 674 O ILE A 253 -7.707 39.693 -12.885 1.00 11.55 O ANISOU 674 O ILE A 253 1272 1527 1591 -56 131 208 O ATOM 675 CB ILE A 253 -6.419 37.134 -14.711 1.00 11.85 C ANISOU 675 CB ILE A 253 1307 1590 1605 -52 44 180 C ATOM 676 CG1 ILE A 253 -5.194 36.853 -15.594 1.00 15.37 C ANISOU 676 CG1 ILE A 253 1768 2057 2015 -46 23 163 C ATOM 677 CG2 ILE A 253 -7.532 37.690 -15.575 1.00 8.31 C ANISOU 677 CG2 ILE A 253 846 1131 1182 -42 34 193 C ATOM 678 CD1 ILE A 253 -5.398 35.737 -16.612 1.00 14.63 C ANISOU 678 CD1 ILE A 253 1670 1962 1926 -35 -21 156 C ATOM 679 N SER A 254 -7.538 37.755 -11.729 1.00 12.86 N ANISOU 679 N SER A 254 1430 1693 1765 -68 120 205 N ATOM 680 CA SER A 254 -8.600 38.078 -10.785 1.00 18.24 C ANISOU 680 CA SER A 254 2100 2359 2472 -67 151 223 C ATOM 681 C SER A 254 -8.332 39.392 -10.074 1.00 19.26 C ANISOU 681 C SER A 254 2250 2485 2581 -65 190 222 C ATOM 682 O SER A 254 -9.218 40.234 -9.943 1.00 18.45 O ANISOU 682 O SER A 254 2142 2372 2497 -56 212 235 O ATOM 683 CB SER A 254 -8.737 36.973 -9.738 1.00 17.87 C ANISOU 683 CB SER A 254 2046 2308 2435 -75 155 228 C ATOM 684 OG SER A 254 -9.883 37.194 -8.940 1.00 18.20 O ANISOU 684 OG SER A 254 2072 2337 2505 -71 184 250 O ATOM 685 N LEU A 255 -7.099 39.541 -9.606 1.00 19.29 N ANISOU 685 N LEU A 255 2281 2498 2551 -75 196 207 N ATOM 686 CA LEU A 255 -6.648 40.750 -8.929 1.00 19.03 C ANISOU 686 CA LEU A 255 2274 2460 2494 -76 226 204 C ATOM 687 C LEU A 255 -6.644 41.978 -9.844 1.00 20.02 C ANISOU 687 C LEU A 255 2406 2585 2614 -70 225 204 C ATOM 688 O LEU A 255 -6.751 43.114 -9.369 1.00 23.80 O ANISOU 688 O LEU A 255 2903 3053 3086 -67 251 207 O ATOM 689 CB LEU A 255 -5.248 40.521 -8.362 1.00 15.51 C ANISOU 689 CB LEU A 255 1853 2025 2014 -91 223 188 C ATOM 690 CG LEU A 255 -5.163 39.597 -7.143 1.00 17.36 C ANISOU 690 CG LEU A 255 2092 2257 2248 -98 232 188 C ATOM 691 CD1 LEU A 255 -3.711 39.270 -6.786 1.00 21.40 C ANISOU 691 CD1 LEU A 255 2623 2780 2727 -112 221 173 C ATOM 692 CD2 LEU A 255 -5.868 40.233 -5.961 1.00 20.49 C ANISOU 692 CD2 LEU A 255 2500 2636 2648 -93 271 198 C ATOM 693 N ALA A 256 -6.516 41.753 -11.151 1.00 12.75 N ANISOU 693 N ALA A 256 1473 1675 1696 -67 195 201 N ATOM 694 CA ALA A 256 -6.491 42.859 -12.113 1.00 18.54 C ANISOU 694 CA ALA A 256 2212 2409 2424 -61 192 203 C ATOM 695 C ALA A 256 -7.888 43.261 -12.585 1.00 20.49 C ANISOU 695 C ALA A 256 2439 2642 2704 -47 194 218 C ATOM 696 O ALA A 256 -8.051 44.293 -13.239 1.00 24.29 O ANISOU 696 O ALA A 256 2925 3119 3184 -40 196 222 O ATOM 697 CB ALA A 256 -5.598 42.515 -13.319 1.00 19.26 C ANISOU 697 CB ALA A 256 2302 2520 2495 -63 161 193 C ATOM 698 N THR A 257 -8.893 42.454 -12.245 1.00 15.09 N ANISOU 698 N THR A 257 1731 1950 2052 -42 194 228 N ATOM 699 CA THR A 257 -10.241 42.647 -12.782 1.00 17.63 C ANISOU 699 CA THR A 257 2028 2260 2411 -29 190 246 C ATOM 700 C THR A 257 -11.207 43.253 -11.761 1.00 17.88 C ANISOU 700 C THR A 257 2054 2277 2463 -19 229 261 C ATOM 701 O THR A 257 -11.815 42.541 -10.975 1.00 20.22 O ANISOU 701 O THR A 257 2334 2569 2780 -19 241 272 O ATOM 702 CB THR A 257 -10.807 41.318 -13.323 1.00 18.01 C ANISOU 702 CB THR A 257 2047 2310 2486 -30 157 251 C ATOM 703 OG1 THR A 257 -9.840 40.717 -14.195 1.00 16.59 O ANISOU 703 OG1 THR A 257 1877 2144 2282 -35 123 235 O ATOM 704 CG2 THR A 257 -12.099 41.550 -14.088 1.00 5.69 C ANISOU 704 CG2 THR A 257 461 738 964 -18 144 269 C ATOM 705 N ASN A 258 -11.354 44.574 -11.788 1.00 24.22 N ANISOU 705 N ASN A 258 2872 3071 3259 -10 249 263 N ATOM 706 CA ASN A 258 -12.149 45.266 -10.777 1.00 24.49 C ANISOU 706 CA ASN A 258 2909 3091 3307 4 290 275 C ATOM 707 C ASN A 258 -13.637 45.362 -11.087 1.00 23.06 C ANISOU 707 C ASN A 258 2693 2900 3169 21 294 298 C ATOM 708 O ASN A 258 -14.245 46.443 -11.019 1.00 21.89 O ANISOU 708 O ASN A 258 2548 2740 3029 38 316 307 O ATOM 709 CB ASN A 258 -11.558 46.644 -10.472 1.00 23.71 C ANISOU 709 CB ASN A 258 2848 2984 3178 7 311 266 C ATOM 710 CG ASN A 258 -10.174 46.547 -9.852 1.00 31.21 C ANISOU 710 CG ASN A 258 3831 3941 4087 -11 312 247 C ATOM 711 OD1 ASN A 258 -9.173 46.926 -10.468 1.00 35.96 O ANISOU 711 OD1 ASN A 258 4450 4550 4664 -22 293 236 O ATOM 712 ND2 ASN A 258 -10.109 46.017 -8.633 1.00 30.98 N ANISOU 712 ND2 ASN A 258 3809 3910 4051 -13 332 246 N ATOM 713 N ASP A 259 -14.230 44.222 -11.416 1.00 16.54 N ANISOU 713 N ASP A 259 1832 2078 2373 17 271 310 N ATOM 714 CA ASP A 259 -15.664 44.185 -11.607 1.00 18.99 C ANISOU 714 CA ASP A 259 2104 2379 2731 31 274 336 C ATOM 715 C ASP A 259 -16.353 43.934 -10.263 1.00 23.68 C ANISOU 715 C ASP A 259 2685 2970 3342 39 314 353 C ATOM 716 O ASP A 259 -15.687 43.834 -9.229 1.00 24.33 O ANISOU 716 O ASP A 259 2794 3056 3397 34 338 343 O ATOM 717 CB ASP A 259 -16.063 43.159 -12.675 1.00 19.68 C ANISOU 717 CB ASP A 259 2160 2470 2846 23 226 343 C ATOM 718 CG ASP A 259 -15.665 41.731 -12.316 1.00 30.24 C ANISOU 718 CG ASP A 259 3493 3815 4183 6 207 339 C ATOM 719 OD1 ASP A 259 -15.146 41.489 -11.198 1.00 27.73 O ANISOU 719 OD1 ASP A 259 3191 3501 3846 0 234 333 O ATOM 720 OD2 ASP A 259 -15.880 40.843 -13.174 1.00 36.35 O ANISOU 720 OD2 ASP A 259 4248 4589 4975 -1 164 341 O ATOM 721 N ASP A 260 -17.680 43.850 -10.282 1.00 16.70 N ANISOU 721 N ASP A 260 1762 2080 2503 52 322 382 N ATOM 722 CA ASP A 260 -18.461 43.721 -9.059 1.00 23.50 C ANISOU 722 CA ASP A 260 2608 2940 3383 63 365 403 C ATOM 723 C ASP A 260 -18.126 42.462 -8.260 1.00 22.99 C ANISOU 723 C ASP A 260 2539 2882 3314 46 365 405 C ATOM 724 O ASP A 260 -18.382 42.395 -7.052 1.00 23.08 O ANISOU 724 O ASP A 260 2552 2894 3323 53 405 416 O ATOM 725 CB ASP A 260 -19.960 43.735 -9.378 1.00 30.24 C ANISOU 725 CB ASP A 260 3410 3787 4291 78 367 438 C ATOM 726 CG ASP A 260 -20.806 43.925 -8.145 1.00 36.83 C ANISOU 726 CG ASP A 260 4231 4622 5143 98 422 463 C ATOM 727 OD1 ASP A 260 -20.707 45.015 -7.538 1.00 36.34 O ANISOU 727 OD1 ASP A 260 4198 4554 5056 119 462 456 O ATOM 728 OD2 ASP A 260 -21.557 42.987 -7.784 1.00 41.92 O ANISOU 728 OD2 ASP A 260 4835 5270 5823 93 423 490 O ATOM 729 N GLY A 261 -17.565 41.465 -8.930 1.00 19.46 N ANISOU 729 N GLY A 261 2088 2440 2865 24 319 393 N ATOM 730 CA GLY A 261 -17.234 40.218 -8.266 1.00 20.12 C ANISOU 730 CA GLY A 261 2168 2529 2946 7 312 394 C ATOM 731 C GLY A 261 -15.843 40.185 -7.648 1.00 18.35 C ANISOU 731 C GLY A 261 1990 2312 2671 -3 320 365 C ATOM 732 O GLY A 261 -15.469 39.190 -7.022 1.00 18.64 O ANISOU 732 O GLY A 261 2029 2353 2702 -17 316 363 O ATOM 733 N TYR A 262 -15.075 41.263 -7.819 1.00 14.53 N ANISOU 733 N TYR A 262 1542 1828 2152 2 329 343 N ATOM 734 CA TYR A 262 -13.705 41.306 -7.304 1.00 16.79 C ANISOU 734 CA TYR A 262 1870 2120 2390 -10 332 317 C ATOM 735 C TYR A 262 -13.655 40.924 -5.823 1.00 17.20 C ANISOU 735 C TYR A 262 1933 2171 2432 -11 367 322 C ATOM 736 O TYR A 262 -12.886 40.062 -5.419 1.00 18.33 O ANISOU 736 O TYR A 262 2088 2320 2558 -27 354 312 O ATOM 737 CB TYR A 262 -13.081 42.697 -7.521 1.00 10.38 C ANISOU 737 CB TYR A 262 1092 1304 1547 -2 344 300 C ATOM 738 CG TYR A 262 -11.685 42.884 -6.925 1.00 11.06 C ANISOU 738 CG TYR A 262 1222 1395 1587 -15 348 277 C ATOM 739 CD1 TYR A 262 -10.533 42.708 -7.701 1.00 14.67 C ANISOU 739 CD1 TYR A 262 1692 1862 2019 -30 315 257 C ATOM 740 CD2 TYR A 262 -11.523 43.255 -5.586 1.00 18.46 C ANISOU 740 CD2 TYR A 262 2187 2324 2503 -11 385 275 C ATOM 741 CE1 TYR A 262 -9.253 42.891 -7.154 1.00 14.17 C ANISOU 741 CE1 TYR A 262 1664 1803 1917 -43 317 239 C ATOM 742 CE2 TYR A 262 -10.258 43.448 -5.029 1.00 17.51 C ANISOU 742 CE2 TYR A 262 2106 2205 2340 -24 385 255 C ATOM 743 CZ TYR A 262 -9.131 43.265 -5.818 1.00 17.26 C ANISOU 743 CZ TYR A 262 2082 2185 2290 -41 351 238 C ATOM 744 OH TYR A 262 -7.901 43.456 -5.253 1.00 16.01 O ANISOU 744 OH TYR A 262 1959 2028 2094 -54 350 221 O ATOM 745 N THR A 263 -14.487 41.568 -5.014 1.00 22.73 N ANISOU 745 N THR A 263 2632 2864 3141 8 410 339 N ATOM 746 CA THR A 263 -14.403 41.398 -3.565 1.00 22.84 C ANISOU 746 CA THR A 263 2665 2876 3137 11 448 343 C ATOM 747 C THR A 263 -14.711 39.973 -3.134 1.00 24.29 C ANISOU 747 C THR A 263 2821 3066 3342 -2 440 359 C ATOM 748 O THR A 263 -13.993 39.401 -2.314 1.00 25.12 O ANISOU 748 O THR A 263 2949 3174 3423 -14 443 350 O ATOM 749 CB THR A 263 -15.300 42.406 -2.813 1.00 26.14 C ANISOU 749 CB THR A 263 3088 3285 3560 39 499 359 C ATOM 750 OG1 THR A 263 -14.797 43.733 -3.018 1.00 24.31 O ANISOU 750 OG1 THR A 263 2894 3044 3299 49 506 339 O ATOM 751 CG2 THR A 263 -15.310 42.113 -1.310 1.00 28.34 C ANISOU 751 CG2 THR A 263 3385 3563 3820 45 539 365 C ATOM 752 N LYS A 264 -15.768 39.396 -3.696 1.00 26.78 N ANISOU 752 N LYS A 264 3088 3381 3705 -1 425 384 N ATOM 753 CA LYS A 264 -16.125 38.019 -3.380 1.00 29.25 C ANISOU 753 CA LYS A 264 3373 3698 4043 -16 412 403 C ATOM 754 C LYS A 264 -15.063 37.005 -3.813 1.00 27.61 C ANISOU 754 C LYS A 264 3176 3494 3819 -41 364 381 C ATOM 755 O LYS A 264 -14.754 36.083 -3.055 1.00 25.93 O ANISOU 755 O LYS A 264 2968 3284 3599 -53 364 383 O ATOM 756 CB LYS A 264 -17.497 37.654 -3.953 1.00 37.94 C ANISOU 756 CB LYS A 264 4418 4797 5202 -12 401 438 C ATOM 757 CG LYS A 264 -18.662 38.221 -3.151 1.00 49.11 C ANISOU 757 CG LYS A 264 5811 6209 6638 11 454 470 C ATOM 758 CD LYS A 264 -19.997 38.024 -3.864 1.00 60.45 C ANISOU 758 CD LYS A 264 7190 7644 8134 16 441 504 C ATOM 759 CE LYS A 264 -21.151 38.592 -3.037 1.00 69.39 C ANISOU 759 CE LYS A 264 8298 8777 9289 42 498 539 C ATOM 760 NZ LYS A 264 -22.497 38.357 -3.654 1.00 73.18 N ANISOU 760 NZ LYS A 264 8717 9257 9833 46 485 579 N ATOM 761 N ARG A 265 -14.507 37.166 -5.018 1.00 18.41 N ANISOU 761 N ARG A 265 2017 2331 2647 -45 325 361 N ATOM 762 CA ARG A 265 -13.449 36.252 -5.493 1.00 20.03 C ANISOU 762 CA ARG A 265 2236 2542 2833 -64 282 338 C ATOM 763 C ARG A 265 -12.224 36.264 -4.567 1.00 18.95 C ANISOU 763 C ARG A 265 2139 2410 2650 -71 297 316 C ATOM 764 O ARG A 265 -11.586 35.230 -4.316 1.00 14.75 O ANISOU 764 O ARG A 265 1613 1881 2108 -86 276 308 O ATOM 765 CB ARG A 265 -12.987 36.628 -6.910 1.00 20.27 C ANISOU 765 CB ARG A 265 2271 2575 2856 -62 246 319 C ATOM 766 CG ARG A 265 -14.054 36.539 -7.991 1.00 25.50 C ANISOU 766 CG ARG A 265 2897 3231 3560 -57 219 337 C ATOM 767 CD ARG A 265 -13.430 36.605 -9.384 1.00 23.08 C ANISOU 767 CD ARG A 265 2601 2929 3240 -58 176 316 C ATOM 768 NE ARG A 265 -12.541 37.758 -9.536 1.00 20.56 N ANISOU 768 NE ARG A 265 2314 2616 2882 -52 193 295 N ATOM 769 CZ ARG A 265 -12.882 38.908 -10.114 1.00 17.24 C ANISOU 769 CZ ARG A 265 1894 2192 2463 -39 203 297 C ATOM 770 NH1 ARG A 265 -14.108 39.081 -10.601 1.00 16.84 N ANISOU 770 NH1 ARG A 265 1813 2134 2453 -30 198 319 N ATOM 771 NH2 ARG A 265 -11.993 39.891 -10.208 1.00 9.57 N ANISOU 771 NH2 ARG A 265 954 1226 1456 -37 215 279 N ATOM 772 N GLN A 266 -11.878 37.449 -4.084 1.00 19.72 N ANISOU 772 N GLN A 266 2267 2506 2720 -61 331 307 N ATOM 773 CA GLN A 266 -10.680 37.609 -3.267 1.00 26.21 C ANISOU 773 CA GLN A 266 3130 3331 3497 -69 342 286 C ATOM 774 C GLN A 266 -10.887 37.050 -1.874 1.00 24.12 C ANISOU 774 C GLN A 266 2872 3064 3230 -71 370 298 C ATOM 775 O GLN A 266 -9.967 36.488 -1.282 1.00 23.65 O ANISOU 775 O GLN A 266 2835 3007 3144 -84 363 285 O ATOM 776 CB GLN A 266 -10.269 39.080 -3.192 1.00 28.75 C ANISOU 776 CB GLN A 266 3484 3648 3791 -59 365 273 C ATOM 777 CG GLN A 266 -9.125 39.455 -4.136 1.00 35.31 C ANISOU 777 CG GLN A 266 4332 4487 4598 -68 334 249 C ATOM 778 CD GLN A 266 -9.264 38.849 -5.528 1.00 37.18 C ANISOU 778 CD GLN A 266 4540 4732 4857 -71 293 249 C ATOM 779 OE1 GLN A 266 -9.971 39.379 -6.400 1.00 28.27 O ANISOU 779 OE1 GLN A 266 3393 3599 3748 -60 288 257 O ATOM 780 NE2 GLN A 266 -8.573 37.735 -5.748 1.00 43.69 N ANISOU 780 NE2 GLN A 266 5362 5565 5675 -84 261 239 N ATOM 781 N GLU A 267 -12.100 37.204 -1.354 1.00 22.96 N ANISOU 781 N GLU A 267 2704 2911 3109 -57 403 325 N ATOM 782 CA GLU A 267 -12.422 36.704 -0.026 1.00 27.72 C ANISOU 782 CA GLU A 267 3311 3512 3708 -57 435 341 C ATOM 783 C GLU A 267 -12.411 35.189 -0.070 1.00 27.82 C ANISOU 783 C GLU A 267 3300 3529 3742 -76 403 350 C ATOM 784 O GLU A 267 -11.883 34.522 0.823 1.00 33.12 O ANISOU 784 O GLU A 267 3989 4201 4393 -87 407 347 O ATOM 785 CB GLU A 267 -13.798 37.198 0.414 1.00 35.20 C ANISOU 785 CB GLU A 267 4235 4455 4683 -35 478 372 C ATOM 786 CG GLU A 267 -14.333 36.516 1.658 1.00 40.67 C ANISOU 786 CG GLU A 267 4922 5150 5382 -33 511 397 C ATOM 787 CD GLU A 267 -13.729 37.073 2.935 1.00 45.39 C ANISOU 787 CD GLU A 267 5571 5744 5932 -24 548 384 C ATOM 788 OE1 GLU A 267 -12.985 38.080 2.857 1.00 47.00 O ANISOU 788 OE1 GLU A 267 5814 5943 6102 -19 551 358 O ATOM 789 OE2 GLU A 267 -14.008 36.506 4.015 1.00 44.24 O ANISOU 789 OE2 GLU A 267 5427 5599 5783 -24 575 402 O ATOM 790 N LYS A 268 -12.990 34.655 -1.135 1.00 23.08 N ANISOU 790 N LYS A 268 2662 2929 3180 -81 369 361 N ATOM 791 CA LYS A 268 -13.047 33.219 -1.347 1.00 24.77 C ANISOU 791 CA LYS A 268 2853 3143 3416 -99 331 369 C ATOM 792 C LYS A 268 -11.640 32.621 -1.472 1.00 23.08 C ANISOU 792 C LYS A 268 2668 2932 3168 -114 298 338 C ATOM 793 O LYS A 268 -11.377 31.520 -0.998 1.00 27.92 O ANISOU 793 O LYS A 268 3282 3545 3782 -127 282 341 O ATOM 794 CB LYS A 268 -13.876 32.925 -2.593 1.00 23.09 C ANISOU 794 CB LYS A 268 2600 2927 3247 -99 296 383 C ATOM 795 CG LYS A 268 -13.845 31.496 -3.012 1.00 30.09 C ANISOU 795 CG LYS A 268 3468 3810 4155 -117 247 387 C ATOM 796 CD LYS A 268 -14.502 31.315 -4.370 1.00 33.09 C ANISOU 796 CD LYS A 268 3817 4183 4571 -117 205 394 C ATOM 797 CE LYS A 268 -16.011 31.332 -4.282 1.00 27.61 C ANISOU 797 CE LYS A 268 3079 3484 3929 -113 219 435 C ATOM 798 NZ LYS A 268 -16.594 30.735 -5.521 1.00 28.22 N ANISOU 798 NZ LYS A 268 3125 3551 4044 -120 164 443 N ATOM 799 N LEU A 269 -10.732 33.356 -2.100 1.00 19.69 N ANISOU 799 N LEU A 269 2263 2508 2709 -110 287 310 N ATOM 800 CA LEU A 269 -9.364 32.873 -2.280 1.00 21.93 C ANISOU 800 CA LEU A 269 2573 2799 2962 -122 257 283 C ATOM 801 C LEU A 269 -8.645 32.873 -0.927 1.00 21.73 C ANISOU 801 C LEU A 269 2579 2773 2903 -128 283 276 C ATOM 802 O LEU A 269 -7.857 31.979 -0.615 1.00 22.80 O ANISOU 802 O LEU A 269 2726 2911 3024 -140 262 266 O ATOM 803 CB LEU A 269 -8.623 33.744 -3.301 1.00 20.39 C ANISOU 803 CB LEU A 269 2391 2610 2746 -117 243 260 C ATOM 804 CG LEU A 269 -7.253 33.270 -3.796 1.00 31.04 C ANISOU 804 CG LEU A 269 3758 3970 4067 -125 208 233 C ATOM 805 CD1 LEU A 269 -7.355 31.919 -4.515 1.00 24.09 C ANISOU 805 CD1 LEU A 269 2857 3088 3206 -130 163 234 C ATOM 806 CD2 LEU A 269 -6.612 34.331 -4.696 1.00 34.27 C ANISOU 806 CD2 LEU A 269 4180 4387 4455 -119 204 217 C ATOM 807 N LYS A 270 -8.931 33.887 -0.126 1.00 18.41 N ANISOU 807 N LYS A 270 2176 2349 2469 -117 327 282 N ATOM 808 CA LYS A 270 -8.441 33.945 1.241 1.00 20.11 C ANISOU 808 CA LYS A 270 2426 2562 2654 -120 355 279 C ATOM 809 C LYS A 270 -8.937 32.712 2.007 1.00 20.80 C ANISOU 809 C LYS A 270 2497 2647 2759 -128 357 300 C ATOM 810 O LYS A 270 -8.144 32.000 2.629 1.00 18.37 O ANISOU 810 O LYS A 270 2209 2340 2431 -141 345 291 O ATOM 811 CB LYS A 270 -8.919 35.244 1.902 1.00 25.58 C ANISOU 811 CB LYS A 270 3138 3248 3334 -102 403 285 C ATOM 812 CG LYS A 270 -8.467 35.441 3.334 1.00 27.12 C ANISOU 812 CG LYS A 270 3374 3437 3493 -101 433 281 C ATOM 813 CD LYS A 270 -9.515 34.947 4.318 1.00 25.03 C ANISOU 813 CD LYS A 270 3096 3170 3244 -94 468 311 C ATOM 814 CE LYS A 270 -10.656 35.949 4.447 1.00 33.56 C ANISOU 814 CE LYS A 270 4167 4245 4338 -68 511 329 C ATOM 815 NZ LYS A 270 -11.714 35.495 5.409 1.00 32.08 N ANISOU 815 NZ LYS A 270 3964 4058 4168 -58 550 362 N ATOM 816 N ASN A 271 -10.244 32.458 1.948 1.00 15.35 N ANISOU 816 N ASN A 271 1770 1953 2108 -122 369 329 N ATOM 817 CA ASN A 271 -10.840 31.298 2.633 1.00 18.41 C ANISOU 817 CA ASN A 271 2137 2339 2518 -131 371 355 C ATOM 818 C ASN A 271 -10.270 29.956 2.203 1.00 16.74 C ANISOU 818 C ASN A 271 1918 2127 2314 -151 320 347 C ATOM 819 O ASN A 271 -9.974 29.106 3.040 1.00 21.57 O ANISOU 819 O ASN A 271 2540 2737 2918 -162 318 352 O ATOM 820 CB ASN A 271 -12.354 31.267 2.446 1.00 22.89 C ANISOU 820 CB ASN A 271 2659 2904 3132 -123 388 392 C ATOM 821 CG ASN A 271 -13.051 32.384 3.182 1.00 27.60 C ANISOU 821 CG ASN A 271 3264 3501 3723 -100 447 407 C ATOM 822 OD1 ASN A 271 -12.498 32.967 4.112 1.00 30.57 O ANISOU 822 OD1 ASN A 271 3680 3876 4058 -93 477 394 O ATOM 823 ND2 ASN A 271 -14.270 32.700 2.760 1.00 27.72 N ANISOU 823 ND2 ASN A 271 3239 3516 3777 -88 461 433 N ATOM 824 N PHE A 272 -10.123 29.761 0.898 1.00 14.73 N ANISOU 824 N PHE A 272 1648 1875 2075 -153 278 335 N ATOM 825 CA PHE A 272 -9.612 28.501 0.381 1.00 19.80 C ANISOU 825 CA PHE A 272 2285 2515 2724 -168 226 326 C ATOM 826 C PHE A 272 -8.222 28.209 0.931 1.00 24.91 C ANISOU 826 C PHE A 272 2969 3166 3329 -175 218 300 C ATOM 827 O PHE A 272 -7.969 27.134 1.483 1.00 29.14 O ANISOU 827 O PHE A 272 3509 3699 3866 -188 202 304 O ATOM 828 CB PHE A 272 -9.573 28.521 -1.151 1.00 22.20 C ANISOU 828 CB PHE A 272 2574 2820 3042 -164 185 312 C ATOM 829 CG PHE A 272 -10.927 28.443 -1.793 1.00 24.97 C ANISOU 829 CG PHE A 272 2883 3163 3440 -161 178 339 C ATOM 830 CD1 PHE A 272 -12.072 28.308 -1.015 1.00 21.84 C ANISOU 830 CD1 PHE A 272 2462 2761 3074 -162 207 375 C ATOM 831 CD2 PHE A 272 -11.056 28.494 -3.180 1.00 21.09 C ANISOU 831 CD2 PHE A 272 2379 2670 2963 -156 140 330 C ATOM 832 CE1 PHE A 272 -13.333 28.233 -1.607 1.00 21.86 C ANISOU 832 CE1 PHE A 272 2423 2758 3124 -161 198 404 C ATOM 833 CE2 PHE A 272 -12.297 28.416 -3.776 1.00 23.66 C ANISOU 833 CE2 PHE A 272 2668 2988 3335 -155 129 356 C ATOM 834 CZ PHE A 272 -13.448 28.280 -2.983 1.00 25.42 C ANISOU 834 CZ PHE A 272 2862 3206 3591 -158 157 394 C ATOM 835 N ILE A 273 -7.324 29.175 0.781 1.00 22.60 N ANISOU 835 N ILE A 273 2704 2881 3002 -169 227 275 N ATOM 836 CA ILE A 273 -5.949 29.021 1.238 1.00 21.63 C ANISOU 836 CA ILE A 273 2615 2764 2841 -176 217 252 C ATOM 837 C ILE A 273 -5.871 28.901 2.764 1.00 24.23 C ANISOU 837 C ILE A 273 2966 3087 3151 -182 248 261 C ATOM 838 O ILE A 273 -5.192 28.018 3.286 1.00 26.37 O ANISOU 838 O ILE A 273 3251 3359 3411 -193 231 255 O ATOM 839 CB ILE A 273 -5.076 30.193 0.734 1.00 20.55 C ANISOU 839 CB ILE A 273 2498 2635 2674 -170 221 228 C ATOM 840 CG1 ILE A 273 -5.017 30.185 -0.805 1.00 22.79 C ANISOU 840 CG1 ILE A 273 2762 2925 2971 -164 187 218 C ATOM 841 CG2 ILE A 273 -3.692 30.134 1.352 1.00 20.91 C ANISOU 841 CG2 ILE A 273 2577 2686 2682 -178 215 208 C ATOM 842 CD1 ILE A 273 -4.163 31.279 -1.405 1.00 22.36 C ANISOU 842 CD1 ILE A 273 2724 2881 2890 -159 189 198 C ATOM 843 N SER A 274 -6.576 29.784 3.468 1.00 20.01 N ANISOU 843 N SER A 274 2438 2549 2615 -172 294 276 N ATOM 844 CA SER A 274 -6.541 29.818 4.932 1.00 26.11 C ANISOU 844 CA SER A 274 3238 3318 3366 -173 328 284 C ATOM 845 C SER A 274 -6.906 28.473 5.535 1.00 27.74 C ANISOU 845 C SER A 274 3431 3519 3589 -185 319 305 C ATOM 846 O SER A 274 -6.169 27.933 6.359 1.00 25.32 O ANISOU 846 O SER A 274 3150 3211 3258 -195 314 298 O ATOM 847 CB SER A 274 -7.506 30.876 5.488 1.00 26.76 C ANISOU 847 CB SER A 274 3323 3395 3448 -156 380 302 C ATOM 848 OG SER A 274 -7.120 32.180 5.102 1.00 36.11 O ANISOU 848 OG SER A 274 4527 4580 4612 -145 390 283 O ATOM 849 N SER A 275 -8.056 27.951 5.115 1.00 29.53 N ANISOU 849 N SER A 275 3617 3744 3859 -185 316 331 N ATOM 850 CA SER A 275 -8.624 26.721 5.663 1.00 26.06 C ANISOU 850 CA SER A 275 3159 3299 3443 -197 309 357 C ATOM 851 C SER A 275 -7.685 25.535 5.468 1.00 27.43 C ANISOU 851 C SER A 275 3340 3470 3611 -214 259 341 C ATOM 852 O SER A 275 -7.710 24.572 6.244 1.00 22.13 O ANISOU 852 O SER A 275 2672 2794 2942 -225 255 355 O ATOM 853 CB SER A 275 -9.970 26.417 4.986 1.00 24.68 C ANISOU 853 CB SER A 275 2935 3122 3321 -196 304 388 C ATOM 854 OG SER A 275 -9.770 25.910 3.671 1.00 21.43 O ANISOU 854 OG SER A 275 2504 2708 2929 -202 251 374 O ATOM 855 N GLN A 276 -6.858 25.608 4.431 1.00 25.48 N ANISOU 855 N GLN A 276 2990 3459 3234 50 -178 403 N ATOM 856 CA GLN A 276 -5.985 24.499 4.082 1.00 26.88 C ANISOU 856 CA GLN A 276 3193 3583 3436 24 -216 378 C ATOM 857 C GLN A 276 -4.520 24.920 4.159 1.00 24.33 C ANISOU 857 C GLN A 276 2912 3232 3099 41 -205 312 C ATOM 858 O GLN A 276 -3.663 24.354 3.494 1.00 28.50 O ANISOU 858 O GLN A 276 3470 3714 3643 28 -228 277 O ATOM 859 CB GLN A 276 -6.337 23.993 2.682 1.00 35.39 C ANISOU 859 CB GLN A 276 4277 4629 4540 0 -246 381 C ATOM 860 CG GLN A 276 -6.192 22.478 2.508 1.00 51.50 C ANISOU 860 CG GLN A 276 6324 6629 6614 -35 -297 394 C ATOM 861 CD GLN A 276 -7.155 21.671 3.383 1.00 57.70 C ANISOU 861 CD GLN A 276 7069 7440 7413 -55 -315 463 C ATOM 862 OE1 GLN A 276 -7.087 21.716 4.612 1.00 56.49 O ANISOU 862 OE1 GLN A 276 6901 7315 7246 -45 -300 478 O ATOM 863 NE2 GLN A 276 -8.049 20.917 2.743 1.00 59.50 N ANISOU 863 NE2 GLN A 276 7279 7658 7669 -84 -350 505 N ATOM 864 N MET A 277 -4.238 25.910 4.993 1.00 23.53 N ANISOU 864 N MET A 277 2813 3160 2969 71 -170 297 N ATOM 865 CA MET A 277 -2.915 26.524 5.043 1.00 22.69 C ANISOU 865 CA MET A 277 2744 3032 2848 89 -157 236 C ATOM 866 C MET A 277 -1.714 25.562 5.236 1.00 25.44 C ANISOU 866 C MET A 277 3118 3336 3212 75 -184 206 C ATOM 867 O MET A 277 -0.752 25.589 4.456 1.00 20.02 O ANISOU 867 O MET A 277 2463 2613 2531 75 -191 162 O ATOM 868 CB MET A 277 -2.891 27.641 6.086 1.00 16.39 C ANISOU 868 CB MET A 277 1941 2271 2016 124 -122 232 C ATOM 869 CG MET A 277 -1.629 28.525 6.022 1.00 22.79 C ANISOU 869 CG MET A 277 2788 3061 2809 144 -107 171 C ATOM 870 SD MET A 277 -1.386 29.349 4.419 1.00 28.68 S ANISOU 870 SD MET A 277 3555 3786 3556 145 -99 136 S ATOM 871 CE MET A 277 -0.146 30.578 4.823 1.00 33.31 C ANISOU 871 CE MET A 277 4173 4366 4116 174 -77 82 C ATOM 872 N THR A 278 -1.751 24.736 6.273 1.00 29.67 N ANISOU 872 N THR A 278 3642 3878 3754 66 -199 232 N ATOM 873 CA THR A 278 -0.624 23.841 6.545 1.00 32.17 C ANISOU 873 CA THR A 278 3983 4155 4084 56 -225 205 C ATOM 874 C THR A 278 -0.422 22.847 5.404 1.00 30.66 C ANISOU 874 C THR A 278 3808 3918 3924 31 -261 197 C ATOM 875 O THR A 278 0.680 22.724 4.859 1.00 33.22 O ANISOU 875 O THR A 278 4165 4205 4254 35 -269 152 O ATOM 876 CB THR A 278 -0.810 23.052 7.850 1.00 34.81 C ANISOU 876 CB THR A 278 4300 4505 4422 49 -238 240 C ATOM 877 OG1 THR A 278 -1.282 23.924 8.884 1.00 39.36 O ANISOU 877 OG1 THR A 278 4855 5130 4969 74 -206 258 O ATOM 878 CG2 THR A 278 0.522 22.408 8.271 1.00 30.29 C ANISOU 878 CG2 THR A 278 3757 3895 3857 47 -257 204 C ATOM 879 N ASP A 279 -1.495 22.147 5.046 1.00 27.17 N ANISOU 879 N ASP A 279 3342 3479 3500 8 -283 243 N ATOM 880 CA ASP A 279 -1.471 21.225 3.915 1.00 31.40 C ANISOU 880 CA ASP A 279 3892 3973 4065 -14 -320 239 C ATOM 881 C ASP A 279 -0.787 21.846 2.698 1.00 36.15 C ANISOU 881 C ASP A 279 4524 4550 4662 0 -310 188 C ATOM 882 O ASP A 279 0.093 21.233 2.095 1.00 39.94 O ANISOU 882 O ASP A 279 5033 4987 5156 -2 -333 155 O ATOM 883 CB ASP A 279 -2.887 20.767 3.558 1.00 37.57 C ANISOU 883 CB ASP A 279 4641 4769 4864 -38 -340 296 C ATOM 884 CG ASP A 279 -3.416 19.711 4.516 1.00 51.02 C ANISOU 884 CG ASP A 279 6321 6481 6584 -60 -367 347 C ATOM 885 OD1 ASP A 279 -2.599 19.111 5.257 1.00 53.44 O ANISOU 885 OD1 ASP A 279 6642 6770 6893 -61 -380 333 O ATOM 886 OD2 ASP A 279 -4.644 19.477 4.525 1.00 54.45 O ANISOU 886 OD2 ASP A 279 6721 6941 7029 -77 -376 404 O ATOM 887 N MET A 280 -1.179 23.071 2.352 1.00 30.11 N ANISOU 887 N MET A 280 3751 3814 3877 16 -276 183 N ATOM 888 CA MET A 280 -0.606 23.751 1.192 1.00 23.40 C ANISOU 888 CA MET A 280 2925 2945 3020 29 -264 140 C ATOM 889 C MET A 280 0.861 24.167 1.369 1.00 24.72 C ANISOU 889 C MET A 280 3123 3094 3175 49 -251 87 C ATOM 890 O MET A 280 1.641 24.115 0.424 1.00 18.34 O ANISOU 890 O MET A 280 2340 2256 2372 54 -258 51 O ATOM 891 CB MET A 280 -1.440 24.973 0.829 1.00 11.50 C ANISOU 891 CB MET A 280 1400 1474 1493 42 -233 151 C ATOM 892 CG MET A 280 -2.806 24.637 0.245 1.00 16.60 C ANISOU 892 CG MET A 280 2020 2132 2154 24 -248 198 C ATOM 893 SD MET A 280 -3.690 26.144 -0.179 1.00 20.75 S ANISOU 893 SD MET A 280 2528 2700 2656 44 -208 208 S ATOM 894 CE MET A 280 -3.199 26.355 -1.882 1.00 17.40 C ANISOU 894 CE MET A 280 2134 2241 2238 45 -217 166 C ATOM 895 N CYS A 281 1.232 24.608 2.565 1.00 30.81 N ANISOU 895 N CYS A 281 3891 3886 3929 61 -231 83 N ATOM 896 CA CYS A 281 2.586 25.127 2.765 1.00 34.41 C ANISOU 896 CA CYS A 281 4374 4328 4374 80 -218 36 C ATOM 897 C CYS A 281 3.594 24.034 2.481 1.00 36.62 C ANISOU 897 C CYS A 281 4678 4563 4675 73 -248 12 C ATOM 898 O CYS A 281 4.598 24.248 1.774 1.00 35.12 O ANISOU 898 O CYS A 281 4511 4349 4484 84 -246 -27 O ATOM 899 CB CYS A 281 2.774 25.654 4.192 1.00 26.66 C ANISOU 899 CB CYS A 281 3384 3372 3372 94 -198 39 C ATOM 900 SG CYS A 281 2.182 27.323 4.426 1.00 33.32 S ANISOU 900 SG CYS A 281 4216 4260 4183 118 -157 41 S ATOM 901 N LEU A 282 3.288 22.861 3.029 1.00 33.37 N ANISOU 901 N LEU A 282 4257 4142 4281 55 -277 40 N ATOM 902 CA LEU A 282 4.157 21.704 2.951 1.00 43.43 C ANISOU 902 CA LEU A 282 5552 5375 5575 49 -310 23 C ATOM 903 C LEU A 282 4.209 21.080 1.551 1.00 48.64 C ANISOU 903 C LEU A 282 6228 6001 6254 44 -335 11 C ATOM 904 O LEU A 282 5.206 20.448 1.197 1.00 54.30 O ANISOU 904 O LEU A 282 6968 6682 6981 51 -355 -18 O ATOM 905 CB LEU A 282 3.744 20.673 4.007 1.00 45.74 C ANISOU 905 CB LEU A 282 5830 5670 5880 31 -334 60 C ATOM 906 CG LEU A 282 3.901 21.145 5.464 1.00 41.23 C ANISOU 906 CG LEU A 282 5247 5128 5289 41 -313 67 C ATOM 907 CD1 LEU A 282 3.300 20.131 6.447 1.00 40.77 C ANISOU 907 CD1 LEU A 282 5170 5078 5243 22 -337 111 C ATOM 908 CD2 LEU A 282 5.364 21.450 5.812 1.00 29.57 C ANISOU 908 CD2 LEU A 282 3797 3634 3804 61 -304 21 C ATOM 909 N ASP A 283 3.155 21.267 0.754 1.00 42.48 N ANISOU 909 N ASP A 283 5433 5230 5476 34 -336 33 N ATOM 910 CA ASP A 283 3.173 20.816 -0.640 1.00 31.73 C ANISOU 910 CA ASP A 283 4088 3839 4129 33 -359 19 C ATOM 911 C ASP A 283 4.110 21.666 -1.511 1.00 28.04 C ANISOU 911 C ASP A 283 3641 3365 3647 57 -336 -28 C ATOM 912 O ASP A 283 3.966 22.883 -1.617 1.00 25.38 O ANISOU 912 O ASP A 283 3297 3055 3289 67 -302 -34 O ATOM 913 CB ASP A 283 1.768 20.793 -1.249 1.00 26.73 C ANISOU 913 CB ASP A 283 3433 3218 3503 15 -369 58 C ATOM 914 CG ASP A 283 1.761 20.259 -2.678 1.00 29.16 C ANISOU 914 CG ASP A 283 3760 3493 3827 14 -398 43 C ATOM 915 OD1 ASP A 283 1.819 21.070 -3.635 1.00 26.93 O ANISOU 915 OD1 ASP A 283 3485 3216 3533 28 -379 22 O ATOM 916 OD2 ASP A 283 1.715 19.021 -2.846 1.00 33.68 O ANISOU 916 OD2 ASP A 283 4341 4032 4423 1 -442 53 O ATOM 917 N LYS A 284 5.069 20.989 -2.124 1.00 28.80 N ANISOU 917 N LYS A 284 3764 3426 3754 67 -358 -58 N ATOM 918 CA LYS A 284 6.035 21.571 -3.057 1.00 26.55 C ANISOU 918 CA LYS A 284 3486 3151 3451 94 -342 -89 C ATOM 919 C LYS A 284 5.412 22.585 -4.030 1.00 27.57 C ANISOU 919 C LYS A 284 3611 3297 3569 96 -320 -90 C ATOM 920 O LYS A 284 5.961 23.663 -4.253 1.00 26.24 O ANISOU 920 O LYS A 284 3436 3156 3377 112 -288 -101 O ATOM 921 CB LYS A 284 6.664 20.405 -3.820 1.00 29.04 C ANISOU 921 CB LYS A 284 3813 3443 3777 103 -379 -99 C ATOM 922 CG LYS A 284 7.790 20.704 -4.777 1.00 40.82 C ANISOU 922 CG LYS A 284 5307 4951 5252 130 -370 -121 C ATOM 923 CD LYS A 284 8.224 19.370 -5.392 1.00 48.41 C ANISOU 923 CD LYS A 284 6283 5884 6227 139 -414 -130 C ATOM 924 CE LYS A 284 9.552 19.445 -6.121 1.00 58.13 C ANISOU 924 CE LYS A 284 7515 7129 7443 166 -411 -152 C ATOM 925 NZ LYS A 284 9.945 18.105 -6.668 1.00 64.14 N ANISOU 925 NZ LYS A 284 8292 7861 8218 178 -456 -164 N ATOM 926 N PHE A 285 4.258 22.251 -4.606 1.00 22.04 N ANISOU 926 N PHE A 285 2910 2581 2885 79 -339 -73 N ATOM 927 CA PHE A 285 3.649 23.127 -5.603 1.00 22.05 C ANISOU 927 CA PHE A 285 2904 2598 2874 83 -322 -72 C ATOM 928 C PHE A 285 2.686 24.174 -5.022 1.00 19.70 C ANISOU 928 C PHE A 285 2581 2342 2562 76 -290 -44 C ATOM 929 O PHE A 285 2.680 25.325 -5.462 1.00 20.23 O ANISOU 929 O PHE A 285 2647 2429 2610 88 -261 -56 O ATOM 930 CB PHE A 285 3.005 22.294 -6.719 1.00 21.20 C ANISOU 930 CB PHE A 285 2803 2467 2785 74 -359 -62 C ATOM 931 CG PHE A 285 3.929 21.252 -7.280 1.00 19.35 C ANISOU 931 CG PHE A 285 2590 2203 2560 88 -391 -85 C ATOM 932 CD1 PHE A 285 5.001 21.620 -8.077 1.00 20.53 C ANISOU 932 CD1 PHE A 285 2743 2371 2689 117 -378 -109 C ATOM 933 CD2 PHE A 285 3.762 19.916 -6.972 1.00 22.41 C ANISOU 933 CD2 PHE A 285 2985 2557 2973 73 -434 -72 C ATOM 934 CE1 PHE A 285 5.874 20.669 -8.582 1.00 20.43 C ANISOU 934 CE1 PHE A 285 2741 2342 2678 134 -407 -124 C ATOM 935 CE2 PHE A 285 4.633 18.955 -7.474 1.00 22.05 C ANISOU 935 CE2 PHE A 285 2954 2494 2929 92 -465 -89 C ATOM 936 CZ PHE A 285 5.686 19.334 -8.287 1.00 19.05 C ANISOU 936 CZ PHE A 285 2578 2133 2528 123 -451 -117 C ATOM 937 N ALA A 286 1.902 23.801 -4.016 1.00 21.31 N ANISOU 937 N ALA A 286 2763 2560 2772 59 -297 -6 N ATOM 938 CA ALA A 286 0.980 24.766 -3.407 1.00 20.23 C ANISOU 938 CA ALA A 286 2601 2467 2620 58 -267 22 C ATOM 939 C ALA A 286 1.734 25.885 -2.678 1.00 17.02 C ANISOU 939 C ALA A 286 2198 2081 2188 77 -229 -2 C ATOM 940 O ALA A 286 1.259 27.021 -2.609 1.00 13.17 O ANISOU 940 O ALA A 286 1699 1625 1681 86 -200 4 O ATOM 941 CB ALA A 286 0.007 24.070 -2.459 1.00 16.73 C ANISOU 941 CB ALA A 286 2131 2038 2188 38 -282 71 C ATOM 942 N CYS A 287 2.915 25.578 -2.144 1.00 8.29 N ANISOU 942 N CYS A 287 1110 956 1083 84 -233 -29 N ATOM 943 CA CYS A 287 3.657 26.607 -1.421 1.00 13.53 C ANISOU 943 CA CYS A 287 1779 1636 1724 101 -202 -51 C ATOM 944 C CYS A 287 4.010 27.759 -2.373 1.00 16.82 C ANISOU 944 C CYS A 287 2207 2059 2126 116 -179 -78 C ATOM 945 O CYS A 287 4.114 28.911 -1.956 1.00 19.09 O ANISOU 945 O CYS A 287 2492 2369 2393 128 -152 -85 O ATOM 946 CB CYS A 287 4.900 26.017 -0.728 1.00 20.83 C ANISOU 946 CB CYS A 287 2721 2538 2656 106 -213 -75 C ATOM 947 SG CYS A 287 6.276 25.640 -1.848 1.00 45.97 S ANISOU 947 SG CYS A 287 5918 5704 5843 118 -226 -100 S ATOM 948 N ARG A 288 4.164 27.444 -3.661 1.00 16.05 N ANISOU 948 N ARG A 288 2121 1940 2038 116 -193 -92 N ATOM 949 CA ARG A 288 4.437 28.473 -4.666 1.00 17.68 C ANISOU 949 CA ARG A 288 2324 2166 2229 127 -174 -97 C ATOM 950 C ARG A 288 3.232 29.386 -4.833 1.00 14.37 C ANISOU 950 C ARG A 288 1897 1765 1797 127 -155 -89 C ATOM 951 O ARG A 288 3.400 30.591 -4.941 1.00 15.62 O ANISOU 951 O ARG A 288 2051 1947 1938 137 -131 -90 O ATOM 952 CB ARG A 288 4.814 27.860 -6.021 1.00 19.61 C ANISOU 952 CB ARG A 288 2573 2395 2481 130 -195 -103 C ATOM 953 CG ARG A 288 6.082 27.023 -6.003 1.00 22.12 C ANISOU 953 CG ARG A 288 2896 2704 2806 136 -213 -110 C ATOM 954 CD ARG A 288 7.319 27.883 -5.807 1.00 21.82 C ANISOU 954 CD ARG A 288 2851 2687 2754 146 -194 -114 C ATOM 955 NE ARG A 288 8.531 27.078 -5.942 1.00 22.32 N ANISOU 955 NE ARG A 288 2918 2741 2822 154 -212 -123 N ATOM 956 CZ ARG A 288 9.695 27.554 -6.357 1.00 22.11 C ANISOU 956 CZ ARG A 288 2887 2726 2788 163 -206 -128 C ATOM 957 NH1 ARG A 288 9.812 28.838 -6.669 1.00 17.39 N ANISOU 957 NH1 ARG A 288 2282 2147 2179 162 -185 -123 N ATOM 958 NH2 ARG A 288 10.736 26.748 -6.462 1.00 28.69 N ANISOU 958 NH2 ARG A 288 3724 3551 3626 171 -224 -138 N ATOM 959 N VAL A 289 2.031 28.795 -4.870 1.00 13.95 N ANISOU 959 N VAL A 289 1826 1718 1756 113 -169 -54 N ATOM 960 CA VAL A 289 0.766 29.534 -4.884 1.00 19.53 C ANISOU 960 CA VAL A 289 2510 2458 2453 112 -153 -23 C ATOM 961 C VAL A 289 0.600 30.431 -3.645 1.00 18.60 C ANISOU 961 C VAL A 289 2379 2372 2314 124 -126 -14 C ATOM 962 O VAL A 289 0.142 31.566 -3.748 1.00 20.37 O ANISOU 962 O VAL A 289 2598 2623 2521 136 -101 -10 O ATOM 963 CB VAL A 289 -0.461 28.586 -4.974 1.00 17.20 C ANISOU 963 CB VAL A 289 2194 2164 2178 93 -178 20 C ATOM 964 CG1 VAL A 289 -1.753 29.399 -4.899 1.00 18.82 C ANISOU 964 CG1 VAL A 289 2371 2407 2371 95 -159 54 C ATOM 965 CG2 VAL A 289 -0.416 27.736 -6.258 1.00 9.97 C ANISOU 965 CG2 VAL A 289 1292 1215 1282 84 -210 11 C ATOM 966 N ILE A 290 0.971 29.902 -2.482 1.00 15.33 N ANISOU 966 N ILE A 290 1965 1957 1904 121 -131 -10 N ATOM 967 CA ILE A 290 0.976 30.665 -1.235 1.00 20.34 C ANISOU 967 CA ILE A 290 2591 2618 2519 135 -108 -6 C ATOM 968 C ILE A 290 1.865 31.907 -1.355 1.00 16.62 C ANISOU 968 C ILE A 290 2139 2148 2027 154 -86 -43 C ATOM 969 O ILE A 290 1.441 33.027 -1.068 1.00 19.08 O ANISOU 969 O ILE A 290 2445 2487 2318 170 -63 -38 O ATOM 970 CB ILE A 290 1.515 29.810 -0.064 1.00 18.45 C ANISOU 970 CB ILE A 290 2353 2369 2287 130 -121 -4 C ATOM 971 CG1 ILE A 290 0.651 28.570 0.140 1.00 22.37 C ANISOU 971 CG1 ILE A 290 2830 2865 2805 109 -146 36 C ATOM 972 CG2 ILE A 290 1.566 30.620 1.225 1.00 13.14 C ANISOU 972 CG2 ILE A 290 1676 1725 1593 148 -99 -3 C ATOM 973 CD1 ILE A 290 -0.777 28.899 0.481 1.00 26.00 C ANISOU 973 CD1 ILE A 290 3257 3364 3257 110 -134 81 C ATOM 974 N GLN A 291 3.095 31.691 -1.804 1.00 13.69 N ANISOU 974 N GLN A 291 1791 1747 1663 154 -94 -78 N ATOM 975 CA GLN A 291 4.097 32.746 -1.871 1.00 18.22 C ANISOU 975 CA GLN A 291 2365 2327 2232 158 -89 -79 C ATOM 976 C GLN A 291 3.735 33.880 -2.823 1.00 20.28 C ANISOU 976 C GLN A 291 2621 2599 2485 161 -79 -73 C ATOM 977 O GLN A 291 3.945 35.052 -2.509 1.00 24.15 O ANISOU 977 O GLN A 291 3110 3102 2966 168 -70 -69 O ATOM 978 CB GLN A 291 5.457 32.157 -2.241 1.00 13.30 C ANISOU 978 CB GLN A 291 1747 1683 1623 150 -107 -87 C ATOM 979 CG GLN A 291 6.004 31.243 -1.157 1.00 12.27 C ANISOU 979 CG GLN A 291 1620 1541 1500 149 -119 -91 C ATOM 980 CD GLN A 291 7.161 30.384 -1.626 1.00 18.37 C ANISOU 980 CD GLN A 291 2397 2296 2286 145 -138 -98 C ATOM 981 OE1 GLN A 291 7.234 29.202 -1.298 1.00 16.85 O ANISOU 981 OE1 GLN A 291 2211 2087 2106 142 -155 -101 O ATOM 982 NE2 GLN A 291 8.074 30.974 -2.394 1.00 22.87 N ANISOU 982 NE2 GLN A 291 2965 2871 2855 148 -136 -99 N ATOM 983 N SER A 292 3.196 33.555 -3.988 1.00 14.69 N ANISOU 983 N SER A 292 1915 1886 1781 157 -82 -74 N ATOM 984 CA SER A 292 2.826 34.630 -4.898 1.00 19.77 C ANISOU 984 CA SER A 292 2554 2541 2417 161 -72 -69 C ATOM 985 C SER A 292 1.575 35.349 -4.387 1.00 14.71 C ANISOU 985 C SER A 292 1904 1927 1758 174 -52 -55 C ATOM 986 O SER A 292 1.463 36.571 -4.526 1.00 17.57 O ANISOU 986 O SER A 292 2264 2302 2111 182 -44 -49 O ATOM 987 CB SER A 292 2.682 34.142 -6.353 1.00 22.83 C ANISOU 987 CB SER A 292 2946 2915 2813 156 -82 -74 C ATOM 988 OG SER A 292 1.819 33.026 -6.461 1.00 23.81 O ANISOU 988 OG SER A 292 3074 3029 2943 153 -90 -78 O ATOM 989 N SER A 293 0.658 34.602 -3.768 1.00 12.59 N ANISOU 989 N SER A 293 1627 1672 1483 178 -44 -47 N ATOM 990 CA SER A 293 -0.553 35.207 -3.190 1.00 17.08 C ANISOU 990 CA SER A 293 2175 2278 2039 189 -27 -14 C ATOM 991 C SER A 293 -0.194 36.228 -2.104 1.00 20.72 C ANISOU 991 C SER A 293 2639 2751 2481 208 -14 -19 C ATOM 992 O SER A 293 -0.806 37.296 -2.028 1.00 23.31 O ANISOU 992 O SER A 293 2961 3099 2796 224 -3 -4 O ATOM 993 CB SER A 293 -1.500 34.143 -2.615 1.00 15.97 C ANISOU 993 CB SER A 293 2008 2147 1912 176 -40 26 C ATOM 994 OG SER A 293 -1.913 33.226 -3.624 1.00 16.75 O ANISOU 994 OG SER A 293 2101 2228 2034 156 -63 39 O ATOM 995 N LEU A 294 0.790 35.887 -1.268 1.00 12.06 N ANISOU 995 N LEU A 294 1552 1639 1391 204 -26 -32 N ATOM 996 CA LEU A 294 1.260 36.784 -0.207 1.00 16.50 C ANISOU 996 CA LEU A 294 2118 2206 1944 218 -26 -32 C ATOM 997 C LEU A 294 1.734 38.145 -0.723 1.00 16.34 C ANISOU 997 C LEU A 294 2107 2179 1923 222 -30 -36 C ATOM 998 O LEU A 294 1.479 39.184 -0.101 1.00 16.19 O ANISOU 998 O LEU A 294 2089 2173 1889 241 -24 -29 O ATOM 999 CB LEU A 294 2.394 36.126 0.596 1.00 12.80 C ANISOU 999 CB LEU A 294 1660 1719 1487 209 -40 -46 C ATOM 1000 CG LEU A 294 1.941 35.014 1.539 1.00 16.22 C ANISOU 1000 CG LEU A 294 2085 2163 1914 212 -34 -41 C ATOM 1001 CD1 LEU A 294 3.124 34.098 1.941 1.00 9.71 C ANISOU 1001 CD1 LEU A 294 1273 1310 1107 199 -53 -59 C ATOM 1002 CD2 LEU A 294 1.197 35.632 2.762 1.00 11.17 C ANISOU 1002 CD2 LEU A 294 1434 1558 1252 238 -17 -22 C ATOM 1003 N GLN A 295 2.430 38.156 -1.853 1.00 13.91 N ANISOU 1003 N GLN A 295 1804 1851 1630 205 -41 -45 N ATOM 1004 CA GLN A 295 2.966 39.427 -2.343 1.00 20.69 C ANISOU 1004 CA GLN A 295 2669 2704 2488 208 -43 -47 C ATOM 1005 C GLN A 295 2.057 40.156 -3.337 1.00 15.75 C ANISOU 1005 C GLN A 295 2040 2089 1855 215 -35 -39 C ATOM 1006 O GLN A 295 2.206 41.358 -3.529 1.00 17.84 O ANISOU 1006 O GLN A 295 2310 2354 2113 224 -34 -38 O ATOM 1007 CB GLN A 295 4.379 39.252 -2.919 1.00 26.33 C ANISOU 1007 CB GLN A 295 3388 3398 3218 191 -56 -58 C ATOM 1008 CG GLN A 295 4.422 38.487 -4.210 1.00 29.60 C ANISOU 1008 CG GLN A 295 3800 3803 3644 178 -60 -61 C ATOM 1009 CD GLN A 295 5.828 38.077 -4.596 1.00 28.84 C ANISOU 1009 CD GLN A 295 3706 3691 3560 167 -71 -68 C ATOM 1010 OE1 GLN A 295 6.773 38.244 -3.826 1.00 26.67 O ANISOU 1010 OE1 GLN A 295 3433 3413 3288 167 -76 -71 O ATOM 1011 NE2 GLN A 295 5.970 37.528 -5.797 1.00 23.84 N ANISOU 1011 NE2 GLN A 295 3072 3052 2934 161 -75 -71 N ATOM 1012 N ASN A 296 1.118 39.437 -3.952 1.00 14.25 N ANISOU 1012 N ASN A 296 1842 1907 1664 212 -28 -33 N ATOM 1013 CA ASN A 296 0.211 40.045 -4.933 1.00 22.46 C ANISOU 1013 CA ASN A 296 2879 2959 2698 219 -20 -24 C ATOM 1014 C ASN A 296 -1.182 40.445 -4.411 1.00 26.50 C ANISOU 1014 C ASN A 296 3378 3501 3190 241 -2 -2 C ATOM 1015 O ASN A 296 -1.746 41.449 -4.868 1.00 25.47 O ANISOU 1015 O ASN A 296 3247 3380 3050 255 5 6 O ATOM 1016 CB ASN A 296 0.080 39.162 -6.184 1.00 21.42 C ANISOU 1016 CB ASN A 296 2746 2817 2577 204 -24 -29 C ATOM 1017 CG ASN A 296 1.408 38.999 -6.920 1.00 23.11 C ANISOU 1017 CG ASN A 296 2968 3006 2806 189 -39 -44 C ATOM 1018 OD1 ASN A 296 2.274 39.867 -6.856 1.00 29.17 O ANISOU 1018 OD1 ASN A 296 3741 3768 3575 189 -43 -46 O ATOM 1019 ND2 ASN A 296 1.573 37.879 -7.603 1.00 24.49 N ANISOU 1019 ND2 ASN A 296 3145 3168 2992 178 -48 -51 N ATOM 1020 N MET A 297 -1.732 39.665 -3.474 1.00 22.58 N ANISOU 1020 N MET A 297 2870 3022 2689 246 7 9 N ATOM 1021 CA MET A 297 -3.062 39.935 -2.939 1.00 21.36 C ANISOU 1021 CA MET A 297 2696 2903 2516 268 27 39 C ATOM 1022 C MET A 297 -3.075 41.286 -2.222 1.00 19.95 C ANISOU 1022 C MET A 297 2527 2733 2321 296 30 42 C ATOM 1023 O MET A 297 -2.032 41.758 -1.772 1.00 18.41 O ANISOU 1023 O MET A 297 2350 2518 2128 295 18 23 O ATOM 1024 CB MET A 297 -3.494 38.848 -1.951 1.00 24.42 C ANISOU 1024 CB MET A 297 3066 3311 2902 267 36 56 C ATOM 1025 CG MET A 297 -3.920 37.505 -2.555 1.00 32.16 C ANISOU 1025 CG MET A 297 4029 4290 3901 242 29 71 C ATOM 1026 SD MET A 297 -4.509 36.342 -1.274 1.00 40.46 S ANISOU 1026 SD MET A 297 5052 5357 4963 234 20 111 S ATOM 1027 CE MET A 297 -6.037 37.127 -0.776 1.00114.48 C ANISOU 1027 CE MET A 297 14397 14784 14318 263 46 159 C ATOM 1028 N ASP A 298 -4.248 41.905 -2.104 1.00 13.60 N ANISOU 1028 N ASP A 298 1710 1958 1500 321 47 68 N ATOM 1029 CA ASP A 298 -4.356 43.088 -1.261 1.00 22.14 C ANISOU 1029 CA ASP A 298 2802 3049 2561 354 52 73 C ATOM 1030 C ASP A 298 -3.744 42.756 0.104 1.00 22.03 C ANISOU 1030 C ASP A 298 2793 3033 2543 360 48 66 C ATOM 1031 O ASP A 298 -3.950 41.663 0.635 1.00 20.97 O ANISOU 1031 O ASP A 298 2643 2912 2413 351 52 76 O ATOM 1032 CB ASP A 298 -5.815 43.519 -1.105 1.00 25.93 C ANISOU 1032 CB ASP A 298 3263 3567 3022 384 74 108 C ATOM 1033 CG ASP A 298 -6.469 43.863 -2.437 1.00 26.34 C ANISOU 1033 CG ASP A 298 3309 3622 3078 380 78 117 C ATOM 1034 OD1 ASP A 298 -5.819 44.528 -3.274 1.00 21.51 O ANISOU 1034 OD1 ASP A 298 2716 2984 2472 372 66 94 O ATOM 1035 OD2 ASP A 298 -7.632 43.464 -2.638 1.00 23.46 O ANISOU 1035 OD2 ASP A 298 2916 3287 2710 385 94 149 O ATOM 1036 N LEU A 299 -2.992 43.697 0.664 1.00 16.90 N ANISOU 1036 N LEU A 299 2166 2369 1886 374 38 50 N ATOM 1037 CA LEU A 299 -2.279 43.460 1.919 1.00 16.57 C ANISOU 1037 CA LEU A 299 2133 2322 1840 379 32 40 C ATOM 1038 C LEU A 299 -3.181 42.954 3.058 1.00 15.40 C ANISOU 1038 C LEU A 299 1968 2210 1675 404 49 66 C ATOM 1039 O LEU A 299 -2.822 42.031 3.777 1.00 12.48 O ANISOU 1039 O LEU A 299 1592 1841 1310 395 46 63 O ATOM 1040 CB LEU A 299 -1.484 44.706 2.358 1.00 17.39 C ANISOU 1040 CB LEU A 299 2264 2410 1935 396 20 25 C ATOM 1041 CG LEU A 299 -0.643 44.482 3.619 1.00 20.90 C ANISOU 1041 CG LEU A 299 2719 2846 2377 401 11 13 C ATOM 1042 CD1 LEU A 299 0.320 43.324 3.390 1.00 17.68 C ANISOU 1042 CD1 LEU A 299 2305 2417 1995 362 -3 -3 C ATOM 1043 CD2 LEU A 299 0.093 45.741 4.071 1.00 11.92 C ANISOU 1043 CD2 LEU A 299 1608 1692 1229 419 -1 -1 C ATOM 1044 N SER A 300 -4.350 43.552 3.222 1.00 18.35 N ANISOU 1044 N SER A 300 2331 2614 2027 437 68 93 N ATOM 1045 CA SER A 300 -5.249 43.121 4.290 1.00 20.53 C ANISOU 1045 CA SER A 300 2585 2929 2285 464 87 124 C ATOM 1046 C SER A 300 -5.622 41.657 4.153 1.00 16.55 C ANISOU 1046 C SER A 300 2050 2441 1799 435 92 143 C ATOM 1047 O SER A 300 -5.740 40.956 5.147 1.00 18.99 O ANISOU 1047 O SER A 300 2345 2769 2103 441 99 158 O ATOM 1048 CB SER A 300 -6.510 43.977 4.304 1.00 25.78 C ANISOU 1048 CB SER A 300 3241 3628 2928 504 107 156 C ATOM 1049 OG SER A 300 -6.154 45.338 4.476 1.00 35.67 O ANISOU 1049 OG SER A 300 4526 4865 4163 533 102 139 O ATOM 1050 N LEU A 301 -5.814 41.198 2.920 1.00 18.07 N ANISOU 1050 N LEU A 301 2232 2625 2010 405 90 144 N ATOM 1051 CA LEU A 301 -6.120 39.786 2.683 1.00 17.90 C ANISOU 1051 CA LEU A 301 2182 2613 2006 375 93 161 C ATOM 1052 C LEU A 301 -4.890 38.888 2.843 1.00 15.20 C ANISOU 1052 C LEU A 301 1855 2239 1680 345 76 129 C ATOM 1053 O LEU A 301 -4.980 37.819 3.461 1.00 14.93 O ANISOU 1053 O LEU A 301 1802 2216 1653 333 77 146 O ATOM 1054 CB LEU A 301 -6.792 39.572 1.314 1.00 23.10 C ANISOU 1054 CB LEU A 301 2825 3274 2678 354 96 175 C ATOM 1055 CG LEU A 301 -8.269 39.994 1.241 1.00 33.45 C ANISOU 1055 CG LEU A 301 4106 4627 3977 378 117 222 C ATOM 1056 CD1 LEU A 301 -8.923 39.368 0.027 1.00 37.29 C ANISOU 1056 CD1 LEU A 301 4571 5112 4486 348 109 244 C ATOM 1057 CD2 LEU A 301 -9.035 39.601 2.511 1.00 33.49 C ANISOU 1057 CD2 LEU A 301 4081 4675 3970 398 133 266 C ATOM 1058 N ALA A 302 -3.753 39.313 2.289 1.00 5.90 N ANISOU 1058 N ALA A 302 709 1021 513 333 57 89 N ATOM 1059 CA ALA A 302 -2.499 38.597 2.525 1.00 13.71 C ANISOU 1059 CA ALA A 302 1713 1979 1516 310 39 59 C ATOM 1060 C ALA A 302 -2.247 38.427 4.027 1.00 16.29 C ANISOU 1060 C ALA A 302 2040 2317 1831 328 41 62 C ATOM 1061 O ALA A 302 -1.866 37.351 4.473 1.00 20.82 O ANISOU 1061 O ALA A 302 2610 2887 2414 313 38 59 O ATOM 1062 CB ALA A 302 -1.327 39.298 1.848 1.00 14.26 C ANISOU 1062 CB ALA A 302 1811 2010 1598 298 19 26 C ATOM 1063 N CYS A 303 -2.498 39.473 4.811 1.00 14.49 N ANISOU 1063 N CYS A 303 1820 2104 1582 362 47 69 N ATOM 1064 CA CYS A 303 -2.358 39.376 6.267 1.00 17.14 C ANISOU 1064 CA CYS A 303 2156 2454 1902 385 50 74 C ATOM 1065 C CYS A 303 -3.179 38.228 6.884 1.00 20.78 C ANISOU 1065 C CYS A 303 2584 2952 2361 384 68 108 C ATOM 1066 O CYS A 303 -2.711 37.540 7.801 1.00 23.55 O ANISOU 1066 O CYS A 303 2934 3303 2711 383 65 104 O ATOM 1067 CB CYS A 303 -2.697 40.710 6.943 1.00 16.85 C ANISOU 1067 CB CYS A 303 2133 2432 1839 429 57 80 C ATOM 1068 SG CYS A 303 -1.415 41.982 6.759 1.00 19.03 S ANISOU 1068 SG CYS A 303 2448 2665 2117 430 33 42 S ATOM 1069 N LYS A 304 -4.398 38.022 6.392 1.00 21.21 N ANISOU 1069 N LYS A 304 2607 3037 2414 384 85 146 N ATOM 1070 CA LYS A 304 -5.216 36.910 6.877 1.00 22.15 C ANISOU 1070 CA LYS A 304 2688 3183 2544 373 85 193 C ATOM 1071 C LYS A 304 -4.543 35.554 6.624 1.00 23.47 C ANISOU 1071 C LYS A 304 2855 3317 2744 327 55 185 C ATOM 1072 O LYS A 304 -4.685 34.633 7.429 1.00 22.11 O ANISOU 1072 O LYS A 304 2666 3155 2580 319 45 211 O ATOM 1073 CB LYS A 304 -6.614 36.934 6.250 1.00 30.41 C ANISOU 1073 CB LYS A 304 3701 4260 3593 374 95 240 C ATOM 1074 CG LYS A 304 -7.383 38.242 6.448 1.00 35.35 C ANISOU 1074 CG LYS A 304 4326 4920 4186 422 126 253 C ATOM 1075 CD LYS A 304 -8.272 38.201 7.684 1.00 42.45 C ANISOU 1075 CD LYS A 304 5197 5867 5066 456 143 299 C ATOM 1076 CE LYS A 304 -9.018 39.522 7.872 1.00 48.90 C ANISOU 1076 CE LYS A 304 6019 6710 5851 509 165 312 C ATOM 1077 NZ LYS A 304 -9.804 39.934 6.663 1.00 53.38 N ANISOU 1077 NZ LYS A 304 6575 7283 6426 502 170 327 N ATOM 1078 N LEU A 305 -3.809 35.423 5.515 1.00 22.08 N ANISOU 1078 N LEU A 305 2701 3103 2587 301 40 151 N ATOM 1079 CA LEU A 305 -3.132 34.156 5.219 1.00 21.27 C ANISOU 1079 CA LEU A 305 2602 2965 2513 262 12 142 C ATOM 1080 C LEU A 305 -2.117 33.837 6.304 1.00 21.00 C ANISOU 1080 C LEU A 305 2585 2918 2476 266 4 119 C ATOM 1081 O LEU A 305 -1.995 32.696 6.744 1.00 19.52 O ANISOU 1081 O LEU A 305 2388 2722 2306 246 -15 134 O ATOM 1082 CB LEU A 305 -2.420 34.201 3.870 1.00 20.88 C ANISOU 1082 CB LEU A 305 2577 2878 2480 242 0 106 C ATOM 1083 CG LEU A 305 -3.280 34.425 2.630 1.00 25.55 C ANISOU 1083 CG LEU A 305 3157 3475 3078 234 3 122 C ATOM 1084 CD1 LEU A 305 -2.478 34.094 1.381 1.00 28.46 C ANISOU 1084 CD1 LEU A 305 3547 3802 3465 210 -15 89 C ATOM 1085 CD2 LEU A 305 -4.545 33.584 2.694 1.00 18.16 C ANISOU 1085 CD2 LEU A 305 2184 2562 2156 220 -5 178 C ATOM 1086 N VAL A 306 -1.381 34.859 6.722 1.00 22.98 N ANISOU 1086 N VAL A 306 2861 3165 2705 292 16 84 N ATOM 1087 CA VAL A 306 -0.378 34.719 7.775 1.00 24.74 C ANISOU 1087 CA VAL A 306 3102 3375 2923 300 8 60 C ATOM 1088 C VAL A 306 -1.027 34.239 9.079 1.00 25.32 C ANISOU 1088 C VAL A 306 3153 3481 2987 314 12 98 C ATOM 1089 O VAL A 306 -0.501 33.377 9.779 1.00 22.19 O ANISOU 1089 O VAL A 306 2756 3073 2600 303 -4 98 O ATOM 1090 CB VAL A 306 0.347 36.054 8.012 1.00 17.75 C ANISOU 1090 CB VAL A 306 2246 2481 2017 328 17 24 C ATOM 1091 CG1 VAL A 306 1.364 35.911 9.130 1.00 17.91 C ANISOU 1091 CG1 VAL A 306 2284 2486 2036 334 3 4 C ATOM 1092 CG2 VAL A 306 1.008 36.519 6.715 1.00 13.58 C ANISOU 1092 CG2 VAL A 306 1736 1917 1508 306 0 0 C ATOM 1093 N GLN A 307 -2.195 34.788 9.373 1.00 24.18 N ANISOU 1093 N GLN A 307 2986 3378 2823 341 33 133 N ATOM 1094 CA GLN A 307 -2.953 34.417 10.548 1.00 22.65 C ANISOU 1094 CA GLN A 307 2766 3223 2617 360 40 176 C ATOM 1095 C GLN A 307 -3.327 32.929 10.545 1.00 23.47 C ANISOU 1095 C GLN A 307 2842 3327 2750 322 19 214 C ATOM 1096 O GLN A 307 -3.456 32.300 11.597 1.00 28.97 O ANISOU 1096 O GLN A 307 3523 4040 3444 326 14 239 O ATOM 1097 CB GLN A 307 -4.205 35.282 10.594 1.00 29.12 C ANISOU 1097 CB GLN A 307 3564 4086 3413 395 68 210 C ATOM 1098 CG GLN A 307 -5.048 35.116 11.826 1.00 40.56 C ANISOU 1098 CG GLN A 307 4986 5582 4843 425 82 257 C ATOM 1099 CD GLN A 307 -6.117 36.180 11.904 1.00 46.75 C ANISOU 1099 CD GLN A 307 5758 6407 5598 470 113 282 C ATOM 1100 OE1 GLN A 307 -6.223 37.038 11.019 1.00 44.25 O ANISOU 1100 OE1 GLN A 307 5454 6082 5277 476 122 264 O ATOM 1101 NE2 GLN A 307 -6.918 36.135 12.964 1.00 52.65 N ANISOU 1101 NE2 GLN A 307 6480 7200 6326 503 128 326 N ATOM 1102 N ALA A 308 -3.503 32.363 9.358 1.00 21.57 N ANISOU 1102 N ALA A 308 2594 3064 2536 286 4 218 N ATOM 1103 CA ALA A 308 -3.884 30.962 9.249 1.00 16.27 C ANISOU 1103 CA ALA A 308 1900 2389 1894 250 -21 254 C ATOM 1104 C ALA A 308 -2.710 30.011 9.525 1.00 18.39 C ANISOU 1104 C ALA A 308 2190 2617 2181 226 -48 226 C ATOM 1105 O ALA A 308 -2.896 28.802 9.603 1.00 22.97 O ANISOU 1105 O ALA A 308 2755 3188 2784 197 -72 253 O ATOM 1106 CB ALA A 308 -4.466 30.689 7.882 1.00 12.06 C ANISOU 1106 CB ALA A 308 1356 1843 1383 223 -31 267 C ATOM 1107 N LEU A 309 -1.500 30.547 9.641 1.00 18.94 N ANISOU 1107 N LEU A 309 2295 2661 2242 237 -46 174 N ATOM 1108 CA LEU A 309 -0.340 29.697 9.915 1.00 23.90 C ANISOU 1108 CA LEU A 309 2943 3251 2886 218 -71 147 C ATOM 1109 C LEU A 309 -0.532 29.006 11.263 1.00 24.00 C ANISOU 1109 C LEU A 309 2940 3285 2895 222 -78 177 C ATOM 1110 O LEU A 309 -1.021 29.621 12.201 1.00 23.29 O ANISOU 1110 O LEU A 309 2838 3232 2778 254 -57 195 O ATOM 1111 CB LEU A 309 0.965 30.512 9.905 1.00 14.51 C ANISOU 1111 CB LEU A 309 1792 2036 1686 233 -66 90 C ATOM 1112 CG LEU A 309 1.527 30.917 8.535 1.00 17.13 C ANISOU 1112 CG LEU A 309 2145 2336 2028 222 -67 54 C ATOM 1113 CD1 LEU A 309 2.672 31.905 8.697 1.00 18.46 C ANISOU 1113 CD1 LEU A 309 2344 2488 2183 242 -59 6 C ATOM 1114 CD2 LEU A 309 1.992 29.697 7.729 1.00 13.63 C ANISOU 1114 CD2 LEU A 309 1708 1855 1618 188 -95 48 C ATOM 1115 N PRO A 310 -0.155 27.722 11.356 1.00 24.74 N ANISOU 1115 N PRO A 310 3033 3353 3013 192 -107 184 N ATOM 1116 CA PRO A 310 -0.274 26.976 12.621 1.00 27.83 C ANISOU 1116 CA PRO A 310 3410 3763 3402 193 -117 214 C ATOM 1117 C PRO A 310 0.646 27.561 13.700 1.00 33.53 C ANISOU 1117 C PRO A 310 4154 4485 4101 223 -108 181 C ATOM 1118 O PRO A 310 1.639 28.209 13.365 1.00 30.39 O ANISOU 1118 O PRO A 310 3788 4060 3700 231 -105 132 O ATOM 1119 CB PRO A 310 0.198 25.568 12.245 1.00 24.89 C ANISOU 1119 CB PRO A 310 3043 3350 3064 154 -154 215 C ATOM 1120 CG PRO A 310 1.155 25.801 11.065 1.00 24.90 C ANISOU 1120 CG PRO A 310 3077 3305 3077 146 -160 163 C ATOM 1121 CD PRO A 310 0.522 26.944 10.298 1.00 21.55 C ANISOU 1121 CD PRO A 310 2648 2902 2640 161 -133 160 C ATOM 1122 N ARG A 311 0.326 27.323 14.972 1.00 37.99 N ANISOU 1122 N ARG A 311 4704 5081 4652 238 -106 211 N ATOM 1123 CA ARG A 311 1.109 27.870 16.078 1.00 36.03 C ANISOU 1123 CA ARG A 311 4476 4834 4379 269 -99 183 C ATOM 1124 C ARG A 311 1.715 26.778 16.939 1.00 39.09 C ANISOU 1124 C ARG A 311 4868 5209 4777 255 -124 188 C ATOM 1125 O ARG A 311 2.206 27.042 18.037 1.00 42.60 O ANISOU 1125 O ARG A 311 5324 5661 5202 280 -122 177 O ATOM 1126 CB ARG A 311 0.238 28.761 16.960 1.00 34.95 C ANISOU 1126 CB ARG A 311 4323 4750 4207 314 -70 210 C ATOM 1127 CG ARG A 311 -0.691 29.665 16.184 1.00 36.82 C ANISOU 1127 CG ARG A 311 4547 5009 4433 328 -45 222 C ATOM 1128 CD ARG A 311 0.073 30.456 15.158 1.00 34.71 C ANISOU 1128 CD ARG A 311 4311 4706 4170 325 -43 169 C ATOM 1129 NE ARG A 311 -0.799 31.326 14.371 1.00 34.25 N ANISOU 1129 NE ARG A 311 4242 4668 4102 338 -20 179 N ATOM 1130 CZ ARG A 311 -1.190 32.536 14.756 1.00 29.98 C ANISOU 1130 CZ ARG A 311 3706 4155 3530 382 6 177 C ATOM 1131 NH1 ARG A 311 -0.799 33.017 15.925 1.00 31.11 N ANISOU 1131 NH1 ARG A 311 3866 4308 3648 418 11 165 N ATOM 1132 NH2 ARG A 311 -1.969 33.269 13.973 1.00 31.01 N ANISOU 1132 NH2 ARG A 311 3828 4301 3654 391 24 187 N ATOM 1133 N ASP A 312 1.674 25.550 16.447 1.00 42.02 N ANISOU 1133 N ASP A 312 5229 5558 5179 215 -151 206 N ATOM 1134 CA ASP A 312 2.158 24.414 17.215 1.00 41.71 C ANISOU 1134 CA ASP A 312 5191 5504 5152 199 -178 216 C ATOM 1135 C ASP A 312 3.297 23.702 16.491 1.00 41.16 C ANISOU 1135 C ASP A 312 5150 5377 5112 171 -206 177 C ATOM 1136 O ASP A 312 3.960 24.285 15.635 1.00 44.01 O ANISOU 1136 O ASP A 312 5535 5711 5477 174 -200 134 O ATOM 1137 CB ASP A 312 1.007 23.454 17.516 1.00 45.34 C ANISOU 1137 CB ASP A 312 5613 5994 5623 180 -189 281 C ATOM 1138 CG ASP A 312 0.225 23.071 16.273 1.00 48.95 C ANISOU 1138 CG ASP A 312 6052 6443 6105 150 -197 305 C ATOM 1139 OD1 ASP A 312 0.827 23.025 15.173 1.00 48.51 O ANISOU 1139 OD1 ASP A 312 6020 6345 6068 133 -207 267 O ATOM 1140 OD2 ASP A 312 -0.992 22.808 16.399 1.00 48.37 O ANISOU 1140 OD2 ASP A 312 5940 6406 6032 144 -194 362 O ATOM 1141 N ALA A 313 3.522 22.441 16.840 1.00 37.92 N ANISOU 1141 N ALA A 313 4738 4950 4722 148 -236 194 N ATOM 1142 CA ALA A 313 4.647 21.690 16.303 1.00 38.51 C ANISOU 1142 CA ALA A 313 4840 4970 4821 128 -264 159 C ATOM 1143 C ALA A 313 4.699 21.739 14.776 1.00 37.99 C ANISOU 1143 C ALA A 313 4785 4875 4776 112 -266 139 C ATOM 1144 O ALA A 313 5.766 21.574 14.177 1.00 38.35 O ANISOU 1144 O ALA A 313 4858 4878 4834 109 -278 98 O ATOM 1145 CB ALA A 313 4.608 20.246 16.796 1.00 37.48 C ANISOU 1145 CB ALA A 313 4702 4827 4711 102 -298 190 C ATOM 1146 N ARG A 314 3.547 21.969 14.150 1.00 38.87 N ANISOU 1146 N ARG A 314 4873 5009 4888 105 -255 169 N ATOM 1147 CA ARG A 314 3.474 22.069 12.692 1.00 36.48 C ANISOU 1147 CA ARG A 314 4578 4682 4601 93 -257 154 C ATOM 1148 C ARG A 314 4.280 23.263 12.176 1.00 31.27 C ANISOU 1148 C ARG A 314 3943 4011 3926 115 -233 102 C ATOM 1149 O ARG A 314 4.866 23.200 11.094 1.00 24.52 O ANISOU 1149 O ARG A 314 3108 3122 3086 108 -241 72 O ATOM 1150 CB ARG A 314 2.022 22.157 12.214 1.00 35.61 C ANISOU 1150 CB ARG A 314 4435 4602 4492 83 -249 200 C ATOM 1151 CG ARG A 314 1.204 20.896 12.468 1.00 34.33 C ANISOU 1151 CG ARG A 314 4247 4445 4351 54 -279 254 C ATOM 1152 CD ARG A 314 -0.280 21.107 12.160 1.00 29.65 C ANISOU 1152 CD ARG A 314 3617 3890 3757 48 -268 306 C ATOM 1153 NE ARG A 314 -0.921 22.031 13.096 1.00 28.88 N ANISOU 1153 NE ARG A 314 3495 3848 3628 78 -233 329 N ATOM 1154 CZ ARG A 314 -2.099 22.622 12.883 1.00 32.79 C ANISOU 1154 CZ ARG A 314 3961 4385 4115 86 -212 365 C ATOM 1155 NH1 ARG A 314 -2.766 22.404 11.759 1.00 33.08 N ANISOU 1155 NH1 ARG A 314 3986 4411 4170 65 -223 382 N ATOM 1156 NH2 ARG A 314 -2.603 23.453 13.785 1.00 32.40 N ANISOU 1156 NH2 ARG A 314 3893 4384 4034 120 -180 384 N ATOM 1157 N LEU A 315 4.324 24.341 12.958 1.00 28.52 N ANISOU 1157 N LEU A 315 3595 3692 3549 144 -207 93 N ATOM 1158 CA LEU A 315 5.118 25.514 12.585 1.00 22.47 C ANISOU 1158 CA LEU A 315 2853 2916 2770 165 -187 47 C ATOM 1159 C LEU A 315 6.603 25.171 12.459 1.00 25.04 C ANISOU 1159 C LEU A 315 3208 3196 3109 162 -204 4 C ATOM 1160 O LEU A 315 7.270 25.601 11.513 1.00 28.13 O ANISOU 1160 O LEU A 315 3618 3563 3507 164 -201 -29 O ATOM 1161 CB LEU A 315 4.897 26.679 13.557 1.00 17.73 C ANISOU 1161 CB LEU A 315 2249 2352 2137 199 -161 46 C ATOM 1162 CG LEU A 315 5.488 28.022 13.101 1.00 18.65 C ANISOU 1162 CG LEU A 315 2387 2460 2239 220 -142 5 C ATOM 1163 CD1 LEU A 315 4.963 28.412 11.714 1.00 17.99 C ANISOU 1163 CD1 LEU A 315 2300 2375 2162 210 -132 5 C ATOM 1164 CD2 LEU A 315 5.228 29.135 14.102 1.00 16.71 C ANISOU 1164 CD2 LEU A 315 2142 2248 1961 256 -120 5 C ATOM 1165 N ILE A 316 7.118 24.394 13.405 1.00 27.76 N ANISOU 1165 N ILE A 316 3557 3531 3458 160 -223 7 N ATOM 1166 CA ILE A 316 8.482 23.866 13.313 1.00 27.16 C ANISOU 1166 CA ILE A 316 3506 3413 3399 156 -243 -27 C ATOM 1167 C ILE A 316 8.691 23.140 11.977 1.00 27.05 C ANISOU 1167 C ILE A 316 3501 3365 3412 137 -260 -36 C ATOM 1168 O ILE A 316 9.637 23.422 11.237 1.00 27.62 O ANISOU 1168 O ILE A 316 3594 3410 3491 144 -259 -72 O ATOM 1169 CB ILE A 316 8.759 22.853 14.447 1.00 30.03 C ANISOU 1169 CB ILE A 316 3869 3773 3768 151 -266 -12 C ATOM 1170 CG1 ILE A 316 8.460 23.468 15.811 1.00 29.08 C ANISOU 1170 CG1 ILE A 316 3740 3690 3620 172 -252 1 C ATOM 1171 CG2 ILE A 316 10.197 22.348 14.389 1.00 29.49 C ANISOU 1171 CG2 ILE A 316 3827 3662 3716 152 -286 -47 C ATOM 1172 CD1 ILE A 316 8.797 22.547 16.966 1.00 32.71 C ANISOU 1172 CD1 ILE A 316 4199 4146 4082 169 -274 15 C ATOM 1173 N ALA A 317 7.804 22.196 11.676 1.00 19.97 N ANISOU 1173 N ALA A 317 2588 2469 2530 115 -277 -1 N ATOM 1174 CA ALA A 317 7.911 21.417 10.450 1.00 25.48 C ANISOU 1174 CA ALA A 317 3296 3133 3253 98 -298 -7 C ATOM 1175 C ALA A 317 7.890 22.355 9.252 1.00 25.68 C ANISOU 1175 C ALA A 317 3328 3158 3273 106 -277 -30 C ATOM 1176 O ALA A 317 8.611 22.165 8.270 1.00 25.30 O ANISOU 1176 O ALA A 317 3298 3078 3238 108 -285 -57 O ATOM 1177 CB ALA A 317 6.779 20.384 10.355 1.00 24.67 C ANISOU 1177 CB ALA A 317 3172 3035 3166 73 -321 39 C ATOM 1178 N ILE A 318 7.070 23.386 9.331 1.00 23.58 N ANISOU 1178 N ILE A 318 3045 2927 2986 114 -249 -16 N ATOM 1179 CA ILE A 318 7.055 24.356 8.245 1.00 25.51 C ANISOU 1179 CA ILE A 318 3297 3173 3225 122 -229 -37 C ATOM 1180 C ILE A 318 8.407 25.063 8.121 1.00 21.83 C ANISOU 1180 C ILE A 318 2855 2688 2753 141 -219 -83 C ATOM 1181 O ILE A 318 8.947 25.173 7.017 1.00 19.00 O ANISOU 1181 O ILE A 318 2510 2307 2402 142 -220 -107 O ATOM 1182 CB ILE A 318 5.894 25.348 8.375 1.00 24.27 C ANISOU 1182 CB ILE A 318 3118 3059 3047 130 -202 -13 C ATOM 1183 CG1 ILE A 318 4.626 24.717 7.795 1.00 24.61 C ANISOU 1183 CG1 ILE A 318 3137 3110 3101 110 -213 27 C ATOM 1184 CG2 ILE A 318 6.202 26.627 7.648 1.00 21.36 C ANISOU 1184 CG2 ILE A 318 2760 2691 2663 146 -178 -43 C ATOM 1185 CD1 ILE A 318 3.369 25.481 8.118 1.00 22.45 C ANISOU 1185 CD1 ILE A 318 2837 2884 2810 118 -189 61 C ATOM 1186 N CYS A 319 8.962 25.509 9.250 1.00 17.59 N ANISOU 1186 N CYS A 319 2322 2159 2202 156 -212 -93 N ATOM 1187 CA CYS A 319 10.246 26.217 9.240 1.00 20.40 C ANISOU 1187 CA CYS A 319 2691 2505 2553 170 -207 -123 C ATOM 1188 C CYS A 319 11.405 25.401 8.674 1.00 21.40 C ANISOU 1188 C CYS A 319 2821 2613 2698 164 -229 -126 C ATOM 1189 O CYS A 319 12.319 25.976 8.070 1.00 24.38 O ANISOU 1189 O CYS A 319 3193 2998 3073 169 -225 -130 O ATOM 1190 CB CYS A 319 10.602 26.749 10.635 1.00 18.05 C ANISOU 1190 CB CYS A 319 2397 2221 2240 187 -201 -128 C ATOM 1191 SG CYS A 319 9.532 28.109 11.147 1.00 23.69 S ANISOU 1191 SG CYS A 319 3104 2973 2923 207 -171 -122 S ATOM 1192 N VAL A 320 11.360 24.075 8.849 1.00 20.52 N ANISOU 1192 N VAL A 320 2716 2477 2605 154 -253 -124 N ATOM 1193 CA VAL A 320 12.479 23.210 8.461 1.00 21.30 C ANISOU 1193 CA VAL A 320 2817 2559 2717 154 -275 -129 C ATOM 1194 C VAL A 320 12.196 22.367 7.223 1.00 25.72 C ANISOU 1194 C VAL A 320 3378 3103 3292 145 -291 -125 C ATOM 1195 O VAL A 320 13.045 21.569 6.790 1.00 21.53 O ANISOU 1195 O VAL A 320 2851 2559 2771 149 -312 -131 O ATOM 1196 CB VAL A 320 12.935 22.292 9.611 1.00 25.61 C ANISOU 1196 CB VAL A 320 3372 3088 3271 154 -297 -130 C ATOM 1197 CG1 VAL A 320 13.033 23.102 10.907 1.00 22.20 C ANISOU 1197 CG1 VAL A 320 2940 2671 2822 165 -283 -134 C ATOM 1198 CG2 VAL A 320 11.987 21.060 9.756 1.00 16.56 C ANISOU 1198 CG2 VAL A 320 2233 1915 2146 134 -321 -117 C ATOM 1199 N ASP A 321 11.014 22.555 6.640 1.00 24.40 N ANISOU 1199 N ASP A 321 3209 2937 3126 135 -284 -116 N ATOM 1200 CA ASP A 321 10.714 21.920 5.363 1.00 21.35 C ANISOU 1200 CA ASP A 321 2823 2535 2752 127 -299 -113 C ATOM 1201 C ASP A 321 11.463 22.599 4.224 1.00 23.00 C ANISOU 1201 C ASP A 321 3027 2762 2951 141 -286 -123 C ATOM 1202 O ASP A 321 11.518 23.839 4.146 1.00 23.29 O ANISOU 1202 O ASP A 321 3056 2822 2971 147 -259 -125 O ATOM 1203 CB ASP A 321 9.218 21.934 5.076 1.00 27.09 C ANISOU 1203 CB ASP A 321 3550 3256 3488 109 -297 -99 C ATOM 1204 CG ASP A 321 8.873 21.173 3.818 1.00 29.62 C ANISOU 1204 CG ASP A 321 3873 3558 3824 101 -319 -93 C ATOM 1205 OD1 ASP A 321 8.923 19.923 3.871 1.00 30.67 O ANISOU 1205 OD1 ASP A 321 4012 3663 3977 91 -354 -86 O ATOM 1206 OD2 ASP A 321 8.593 21.821 2.774 1.00 30.71 O ANISOU 1206 OD2 ASP A 321 4006 3707 3954 105 -305 -97 O ATOM 1207 N GLN A 322 12.026 21.788 3.333 1.00 19.62 N ANISOU 1207 N GLN A 322 2603 2320 2533 145 -307 -130 N ATOM 1208 CA GLN A 322 12.796 22.303 2.208 1.00 22.72 C ANISOU 1208 CA GLN A 322 2990 2726 2917 157 -299 -139 C ATOM 1209 C GLN A 322 11.995 23.204 1.267 1.00 23.08 C ANISOU 1209 C GLN A 322 3030 2785 2954 154 -278 -134 C ATOM 1210 O GLN A 322 12.571 24.064 0.600 1.00 25.61 O ANISOU 1210 O GLN A 322 3344 3123 3263 161 -263 -138 O ATOM 1211 CB GLN A 322 13.431 21.159 1.416 1.00 29.76 C ANISOU 1211 CB GLN A 322 3889 3599 3820 165 -328 -149 C ATOM 1212 CG GLN A 322 12.429 20.229 0.783 1.00 42.48 C ANISOU 1212 CG GLN A 322 5508 5186 5445 156 -352 -143 C ATOM 1213 CD GLN A 322 13.087 19.157 -0.081 1.00 51.09 C ANISOU 1213 CD GLN A 322 6607 6259 6545 168 -384 -155 C ATOM 1214 OE1 GLN A 322 14.074 19.416 -0.785 1.00 45.88 O ANISOU 1214 OE1 GLN A 322 5944 5612 5877 185 -380 -169 O ATOM 1215 NE2 GLN A 322 12.537 17.945 -0.030 1.00 54.42 N ANISOU 1215 NE2 GLN A 322 7040 6650 6986 160 -419 -150 N ATOM 1216 N ASN A 323 10.680 23.019 1.209 1.00 25.97 N ANISOU 1216 N ASN A 323 3399 3143 3327 141 -280 -124 N ATOM 1217 CA ASN A 323 9.839 23.903 0.394 1.00 27.32 C ANISOU 1217 CA ASN A 323 3565 3327 3489 138 -261 -119 C ATOM 1218 C ASN A 323 9.112 24.938 1.242 1.00 26.74 C ANISOU 1218 C ASN A 323 3486 3271 3404 134 -234 -113 C ATOM 1219 O ASN A 323 9.114 26.128 0.927 1.00 27.07 O ANISOU 1219 O ASN A 323 3520 3334 3430 139 -211 -113 O ATOM 1220 CB ASN A 323 8.835 23.104 -0.446 1.00 23.74 C ANISOU 1220 CB ASN A 323 3118 2852 3052 127 -282 -113 C ATOM 1221 CG ASN A 323 9.487 21.937 -1.181 1.00 26.04 C ANISOU 1221 CG ASN A 323 3417 3123 3355 134 -314 -121 C ATOM 1222 OD1 ASN A 323 10.448 22.115 -1.936 1.00 27.77 O ANISOU 1222 OD1 ASN A 323 3634 3351 3566 149 -312 -134 O ATOM 1223 ND2 ASN A 323 8.969 20.735 -0.954 1.00 28.10 N ANISOU 1223 ND2 ASN A 323 3686 3353 3636 121 -347 -113 N ATOM 1224 N ALA A 324 8.490 24.487 2.322 1.00 22.70 N ANISOU 1224 N ALA A 324 2977 2749 2899 125 -241 -106 N ATOM 1225 CA ALA A 324 7.715 25.388 3.164 1.00 19.62 C ANISOU 1225 CA ALA A 324 2584 2377 2495 125 -217 -102 C ATOM 1226 C ALA A 324 8.539 26.516 3.821 1.00 21.36 C ANISOU 1226 C ALA A 324 2798 2622 2694 141 -196 -109 C ATOM 1227 O ALA A 324 8.016 27.598 4.076 1.00 21.13 O ANISOU 1227 O ALA A 324 2764 2615 2649 148 -173 -107 O ATOM 1228 CB ALA A 324 6.960 24.609 4.208 1.00 19.51 C ANISOU 1228 CB ALA A 324 2558 2367 2488 112 -231 -74 C ATOM 1229 N ASN A 325 9.815 26.282 4.095 1.00 17.02 N ANISOU 1229 N ASN A 325 2250 2069 2148 147 -205 -115 N ATOM 1230 CA ASN A 325 10.621 27.343 4.697 1.00 22.02 C ANISOU 1230 CA ASN A 325 2879 2720 2768 157 -192 -118 C ATOM 1231 C ASN A 325 10.506 28.657 3.904 1.00 19.53 C ANISOU 1231 C ASN A 325 2557 2422 2441 159 -173 -115 C ATOM 1232 O ASN A 325 10.468 29.742 4.480 1.00 18.09 O ANISOU 1232 O ASN A 325 2372 2255 2247 166 -160 -113 O ATOM 1233 CB ASN A 325 12.091 26.905 4.911 1.00 20.14 C ANISOU 1233 CB ASN A 325 2643 2473 2536 162 -207 -125 C ATOM 1234 CG ASN A 325 12.958 27.059 3.655 1.00 22.99 C ANISOU 1234 CG ASN A 325 3000 2836 2900 164 -210 -129 C ATOM 1235 OD1 ASN A 325 13.584 28.098 3.441 1.00 17.93 O ANISOU 1235 OD1 ASN A 325 2353 2207 2252 167 -199 -130 O ATOM 1236 ND2 ASN A 325 13.011 25.997 2.828 1.00 19.50 N ANISOU 1236 ND2 ASN A 325 2561 2379 2469 162 -226 -133 N ATOM 1237 N HIS A 326 10.414 28.545 2.584 1.00 14.93 N ANISOU 1237 N HIS A 326 1973 1837 1864 155 -174 -114 N ATOM 1238 CA HIS A 326 10.291 29.714 1.710 1.00 15.88 C ANISOU 1238 CA HIS A 326 2087 1972 1976 156 -159 -110 C ATOM 1239 C HIS A 326 8.962 30.479 1.848 1.00 15.26 C ANISOU 1239 C HIS A 326 2006 1906 1886 156 -142 -104 C ATOM 1240 O HIS A 326 8.896 31.659 1.524 1.00 10.74 O ANISOU 1240 O HIS A 326 1429 1347 1304 159 -129 -100 O ATOM 1241 CB HIS A 326 10.535 29.319 0.249 1.00 18.26 C ANISOU 1241 CB HIS A 326 2388 2267 2284 153 -166 -113 C ATOM 1242 CG HIS A 326 11.883 28.719 0.015 1.00 21.64 C ANISOU 1242 CG HIS A 326 2817 2686 2719 158 -181 -121 C ATOM 1243 ND1 HIS A 326 13.026 29.484 -0.099 1.00 23.81 N ANISOU 1243 ND1 HIS A 326 3087 2968 2990 162 -177 -123 N ATOM 1244 CD2 HIS A 326 12.277 27.428 -0.111 1.00 18.78 C ANISOU 1244 CD2 HIS A 326 2460 2308 2367 160 -202 -127 C ATOM 1245 CE1 HIS A 326 14.064 28.690 -0.291 1.00 24.05 C ANISOU 1245 CE1 HIS A 326 3120 2991 3027 168 -192 -132 C ATOM 1246 NE2 HIS A 326 13.637 27.439 -0.298 1.00 21.07 N ANISOU 1246 NE2 HIS A 326 2748 2599 2658 167 -208 -135 N ATOM 1247 N VAL A 327 7.914 29.813 2.325 1.00 14.58 N ANISOU 1247 N VAL A 327 1922 1817 1801 154 -142 -102 N ATOM 1248 CA VAL A 327 6.697 30.520 2.710 1.00 13.91 C ANISOU 1248 CA VAL A 327 1834 1752 1700 161 -123 -96 C ATOM 1249 C VAL A 327 6.952 31.481 3.890 1.00 17.61 C ANISOU 1249 C VAL A 327 2301 2238 2153 175 -113 -95 C ATOM 1250 O VAL A 327 6.550 32.662 3.854 1.00 15.52 O ANISOU 1250 O VAL A 327 2031 1991 1874 184 -99 -89 O ATOM 1251 CB VAL A 327 5.549 29.548 3.063 1.00 17.58 C ANISOU 1251 CB VAL A 327 2298 2214 2169 157 -127 -90 C ATOM 1252 CG1 VAL A 327 4.326 30.338 3.517 1.00 20.50 C ANISOU 1252 CG1 VAL A 327 2646 2624 2519 165 -107 -61 C ATOM 1253 CG2 VAL A 327 5.210 28.631 1.855 1.00 12.39 C ANISOU 1253 CG2 VAL A 327 1640 1537 1533 139 -147 -82 C ATOM 1254 N ILE A 328 7.623 30.990 4.928 1.00 15.25 N ANISOU 1254 N ILE A 328 2006 1931 1856 178 -123 -100 N ATOM 1255 CA ILE A 328 7.936 31.846 6.081 1.00 17.01 C ANISOU 1255 CA ILE A 328 2230 2168 2066 192 -118 -100 C ATOM 1256 C ILE A 328 8.791 33.045 5.647 1.00 14.71 C ANISOU 1256 C ILE A 328 1938 1877 1773 194 -118 -101 C ATOM 1257 O ILE A 328 8.476 34.197 5.967 1.00 12.86 O ANISOU 1257 O ILE A 328 1704 1657 1525 206 -110 -98 O ATOM 1258 CB ILE A 328 8.631 31.067 7.241 1.00 15.63 C ANISOU 1258 CB ILE A 328 2061 1983 1895 195 -131 -107 C ATOM 1259 CG1 ILE A 328 7.739 29.929 7.743 1.00 14.69 C ANISOU 1259 CG1 ILE A 328 1944 1862 1776 194 -131 -106 C ATOM 1260 CG2 ILE A 328 8.972 32.013 8.394 1.00 15.60 C ANISOU 1260 CG2 ILE A 328 2061 1991 1875 213 -128 -109 C ATOM 1261 CD1 ILE A 328 6.277 30.359 8.052 1.00 10.45 C ANISOU 1261 CD1 ILE A 328 1391 1361 1219 205 -111 -83 C ATOM 1262 N GLN A 329 9.860 32.761 4.904 1.00 15.32 N ANISOU 1262 N GLN A 329 2015 1939 1865 183 -129 -105 N ATOM 1263 CA GLN A 329 10.719 33.804 4.336 1.00 17.39 C ANISOU 1263 CA GLN A 329 2277 2203 2129 182 -129 -106 C ATOM 1264 C GLN A 329 9.957 34.830 3.475 1.00 16.82 C ANISOU 1264 C GLN A 329 2201 2141 2049 183 -117 -99 C ATOM 1265 O GLN A 329 10.269 36.016 3.499 1.00 18.46 O ANISOU 1265 O GLN A 329 2411 2353 2251 188 -115 -99 O ATOM 1266 CB GLN A 329 11.866 33.176 3.523 1.00 19.92 C ANISOU 1266 CB GLN A 329 2596 2512 2463 174 -140 -110 C ATOM 1267 CG GLN A 329 12.813 32.259 4.334 1.00 14.54 C ANISOU 1267 CG GLN A 329 1917 1819 1788 176 -154 -117 C ATOM 1268 CD GLN A 329 14.159 32.066 3.648 1.00 19.29 C ANISOU 1268 CD GLN A 329 2517 2415 2400 174 -164 -123 C ATOM 1269 OE1 GLN A 329 15.008 32.954 3.667 1.00 18.28 O ANISOU 1269 OE1 GLN A 329 2387 2288 2269 177 -164 -124 O ATOM 1270 NE2 GLN A 329 14.359 30.902 3.039 1.00 19.08 N ANISOU 1270 NE2 GLN A 329 2489 2378 2381 171 -173 -126 N ATOM 1271 N LYS A 330 8.969 34.384 2.707 1.00 10.99 N ANISOU 1271 N LYS A 330 1460 1405 1312 177 -110 -95 N ATOM 1272 CA LYS A 330 8.147 35.331 1.957 1.00 14.24 C ANISOU 1272 CA LYS A 330 1869 1828 1716 180 -99 -88 C ATOM 1273 C LYS A 330 7.312 36.197 2.900 1.00 15.36 C ANISOU 1273 C LYS A 330 2011 1986 1839 197 -89 -83 C ATOM 1274 O LYS A 330 7.186 37.405 2.696 1.00 12.90 O ANISOU 1274 O LYS A 330 1701 1681 1519 205 -85 -80 O ATOM 1275 CB LYS A 330 7.211 34.618 0.982 1.00 10.44 C ANISOU 1275 CB LYS A 330 1383 1345 1237 173 -95 -85 C ATOM 1276 CG LYS A 330 6.247 35.579 0.287 1.00 11.01 C ANISOU 1276 CG LYS A 330 1452 1430 1300 177 -82 -78 C ATOM 1277 CD LYS A 330 6.996 36.411 -0.745 1.00 16.13 C ANISOU 1277 CD LYS A 330 2101 2074 1953 172 -85 -78 C ATOM 1278 CE LYS A 330 7.533 35.539 -1.878 1.00 14.15 C ANISOU 1278 CE LYS A 330 1850 1812 1716 161 -92 -82 C ATOM 1279 NZ LYS A 330 8.510 36.314 -2.712 1.00 19.06 N ANISOU 1279 NZ LYS A 330 2471 2431 2340 159 -94 -83 N ATOM 1280 N VAL A 331 6.727 35.576 3.920 1.00 12.99 N ANISOU 1280 N VAL A 331 1711 1693 1531 205 -86 -82 N ATOM 1281 CA VAL A 331 5.937 36.326 4.891 1.00 9.98 C ANISOU 1281 CA VAL A 331 1329 1333 1128 228 -75 -76 C ATOM 1282 C VAL A 331 6.803 37.453 5.438 1.00 13.13 C ANISOU 1282 C VAL A 331 1738 1728 1522 239 -83 -81 C ATOM 1283 O VAL A 331 6.396 38.612 5.472 1.00 14.10 O ANISOU 1283 O VAL A 331 1865 1862 1632 255 -78 -77 O ATOM 1284 CB VAL A 331 5.458 35.430 6.047 1.00 12.18 C ANISOU 1284 CB VAL A 331 1605 1623 1398 238 -70 -73 C ATOM 1285 CG1 VAL A 331 4.962 36.273 7.247 1.00 10.35 C ANISOU 1285 CG1 VAL A 331 1376 1416 1142 269 -61 -66 C ATOM 1286 CG2 VAL A 331 4.378 34.459 5.568 1.00 9.51 C ANISOU 1286 CG2 VAL A 331 1257 1297 1060 232 -59 -64 C ATOM 1287 N VAL A 332 8.016 37.097 5.847 1.00 11.57 N ANISOU 1287 N VAL A 332 1546 1515 1337 231 -97 -91 N ATOM 1288 CA VAL A 332 8.957 38.036 6.443 1.00 12.77 C ANISOU 1288 CA VAL A 332 1706 1661 1485 241 -107 -97 C ATOM 1289 C VAL A 332 9.292 39.194 5.491 1.00 16.80 C ANISOU 1289 C VAL A 332 2219 2168 1998 237 -107 -96 C ATOM 1290 O VAL A 332 9.534 40.331 5.922 1.00 14.98 O ANISOU 1290 O VAL A 332 1997 1938 1757 252 -111 -99 O ATOM 1291 CB VAL A 332 10.255 37.304 6.852 1.00 13.65 C ANISOU 1291 CB VAL A 332 1820 1757 1611 231 -121 -106 C ATOM 1292 CG1 VAL A 332 11.351 38.302 7.230 1.00 9.19 C ANISOU 1292 CG1 VAL A 332 1263 1184 1045 238 -132 -112 C ATOM 1293 CG2 VAL A 332 9.977 36.343 8.006 1.00 17.48 C ANISOU 1293 CG2 VAL A 332 2306 2244 2090 238 -123 -108 C ATOM 1294 N ALA A 333 9.282 38.900 4.197 1.00 13.44 N ANISOU 1294 N ALA A 333 1784 1737 1584 219 -103 -93 N ATOM 1295 CA ALA A 333 9.649 39.887 3.190 1.00 14.58 C ANISOU 1295 CA ALA A 333 1928 1878 1731 215 -103 -92 C ATOM 1296 C ALA A 333 8.524 40.858 2.835 1.00 12.56 C ANISOU 1296 C ALA A 333 1675 1635 1462 227 -93 -85 C ATOM 1297 O ALA A 333 8.783 42.021 2.571 1.00 16.00 O ANISOU 1297 O ALA A 333 2117 2069 1894 233 -95 -85 O ATOM 1298 CB ALA A 333 10.163 39.193 1.932 1.00 15.59 C ANISOU 1298 CB ALA A 333 2048 1999 1875 195 -103 -91 C ATOM 1299 N VAL A 334 7.274 40.405 2.844 1.00 12.84 N ANISOU 1299 N VAL A 334 1706 1683 1490 232 -82 -78 N ATOM 1300 CA VAL A 334 6.217 41.221 2.233 1.00 20.64 C ANISOU 1300 CA VAL A 334 2693 2682 2465 243 -71 -70 C ATOM 1301 C VAL A 334 5.047 41.574 3.143 1.00 18.21 C ANISOU 1301 C VAL A 334 2388 2395 2135 270 -61 -62 C ATOM 1302 O VAL A 334 4.109 42.268 2.712 1.00 13.56 O ANISOU 1302 O VAL A 334 1799 1820 1535 284 -51 -52 O ATOM 1303 CB VAL A 334 5.691 40.585 0.915 1.00 18.77 C ANISOU 1303 CB VAL A 334 2447 2446 2239 226 -65 -65 C ATOM 1304 CG1 VAL A 334 6.865 40.286 -0.022 1.00 18.27 C ANISOU 1304 CG1 VAL A 334 2381 2365 2194 205 -74 -71 C ATOM 1305 CG2 VAL A 334 4.916 39.310 1.211 1.00 12.33 C ANISOU 1305 CG2 VAL A 334 1623 1637 1423 223 -60 -62 C ATOM 1306 N ILE A 335 5.121 41.124 4.397 1.00 12.63 N ANISOU 1306 N ILE A 335 1684 1694 1422 282 -62 -64 N ATOM 1307 CA ILE A 335 4.070 41.361 5.394 1.00 10.65 C ANISOU 1307 CA ILE A 335 1433 1467 1145 313 -50 -53 C ATOM 1308 C ILE A 335 4.615 42.152 6.593 1.00 16.44 C ANISOU 1308 C ILE A 335 2184 2198 1864 337 -59 -60 C ATOM 1309 O ILE A 335 5.670 41.810 7.125 1.00 16.01 O ANISOU 1309 O ILE A 335 2135 2128 1819 328 -72 -72 O ATOM 1310 CB ILE A 335 3.485 40.027 5.892 1.00 10.60 C ANISOU 1310 CB ILE A 335 1414 1475 1138 311 -41 -46 C ATOM 1311 CG1 ILE A 335 3.019 39.173 4.709 1.00 13.71 C ANISOU 1311 CG1 ILE A 335 1794 1868 1548 286 -36 -41 C ATOM 1312 CG2 ILE A 335 2.326 40.259 6.851 1.00 10.73 C ANISOU 1312 CG2 ILE A 335 1425 1525 1128 346 -24 -28 C ATOM 1313 CD1 ILE A 335 1.771 39.727 4.041 1.00 14.01 C ANISOU 1313 CD1 ILE A 335 1823 1927 1573 299 -20 -24 C ATOM 1314 N PRO A 336 3.904 43.217 7.024 1.00 19.59 N ANISOU 1314 N PRO A 336 2593 2611 2237 372 -51 -52 N ATOM 1315 CA PRO A 336 4.436 43.984 8.163 1.00 15.82 C ANISOU 1315 CA PRO A 336 2138 2130 1745 398 -61 -60 C ATOM 1316 C PRO A 336 4.573 43.095 9.396 1.00 17.12 C ANISOU 1316 C PRO A 336 2301 2301 1904 407 -62 -62 C ATOM 1317 O PRO A 336 3.794 42.154 9.583 1.00 15.35 O ANISOU 1317 O PRO A 336 2060 2097 1676 408 -48 -50 O ATOM 1318 CB PRO A 336 3.390 45.083 8.392 1.00 11.95 C ANISOU 1318 CB PRO A 336 1658 1658 1224 439 -48 -48 C ATOM 1319 CG PRO A 336 2.608 45.158 7.107 1.00 18.72 C ANISOU 1319 CG PRO A 336 2502 2524 2089 426 -36 -37 C ATOM 1320 CD PRO A 336 2.628 43.764 6.526 1.00 19.07 C ANISOU 1320 CD PRO A 336 2522 2567 2157 391 -34 -36 C ATOM 1321 N LEU A 337 5.571 43.412 10.218 1.00 15.38 N ANISOU 1321 N LEU A 337 2098 2064 1681 414 -79 -76 N ATOM 1322 CA LEU A 337 6.007 42.576 11.334 1.00 10.86 C ANISOU 1322 CA LEU A 337 1526 1491 1107 418 -85 -82 C ATOM 1323 C LEU A 337 4.890 42.158 12.292 1.00 16.80 C ANISOU 1323 C LEU A 337 2273 2276 1834 450 -67 -67 C ATOM 1324 O LEU A 337 4.884 41.025 12.800 1.00 15.52 O ANISOU 1324 O LEU A 337 2099 2121 1676 443 -64 -65 O ATOM 1325 CB LEU A 337 7.106 43.307 12.111 1.00 11.64 C ANISOU 1325 CB LEU A 337 1650 1570 1202 430 -107 -98 C ATOM 1326 CG LEU A 337 7.471 42.809 13.520 1.00 19.73 C ANISOU 1326 CG LEU A 337 2684 2596 2216 448 -115 -104 C ATOM 1327 CD1 LEU A 337 7.919 41.333 13.533 1.00 17.98 C ANISOU 1327 CD1 LEU A 337 2444 2370 2017 418 -117 -107 C ATOM 1328 CD2 LEU A 337 8.557 43.709 14.114 1.00 19.16 C ANISOU 1328 CD2 LEU A 337 2639 2501 2140 460 -139 -120 C ATOM 1329 N LYS A 338 3.958 43.070 12.558 1.00 13.22 N ANISOU 1329 N LYS A 338 1829 1843 1353 489 -54 -55 N ATOM 1330 CA LYS A 338 2.939 42.820 13.578 1.00 12.64 C ANISOU 1330 CA LYS A 338 1750 1804 1250 528 -34 -36 C ATOM 1331 C LYS A 338 2.219 41.495 13.279 1.00 17.66 C ANISOU 1331 C LYS A 338 2351 2463 1897 508 -16 -18 C ATOM 1332 O LYS A 338 1.916 40.716 14.181 1.00 18.43 O ANISOU 1332 O LYS A 338 2437 2582 1983 522 -6 -7 O ATOM 1333 CB LYS A 338 1.948 43.995 13.653 1.00 12.25 C ANISOU 1333 CB LYS A 338 1710 1774 1169 573 -19 -21 C ATOM 1334 CG LYS A 338 0.797 43.806 14.664 1.00 19.27 C ANISOU 1334 CG LYS A 338 2590 2707 2025 620 6 6 C ATOM 1335 CD LYS A 338 1.322 43.618 16.094 1.00 20.31 C ANISOU 1335 CD LYS A 338 2739 2838 2140 647 -3 -3 C ATOM 1336 CE LYS A 338 0.233 43.190 17.068 1.00 18.28 C ANISOU 1336 CE LYS A 338 2465 2628 1853 690 25 28 C ATOM 1337 NZ LYS A 338 0.854 42.758 18.363 1.00 18.26 N ANISOU 1337 NZ LYS A 338 2476 2624 1840 707 16 17 N ATOM 1338 N ASN A 339 1.967 41.232 12.002 1.00 14.90 N ANISOU 1338 N ASN A 339 1986 2109 1568 476 -13 -14 N ATOM 1339 CA ASN A 339 1.254 40.024 11.624 1.00 16.83 C ANISOU 1339 CA ASN A 339 2199 2373 1821 457 3 4 C ATOM 1340 C ASN A 339 2.035 38.749 11.898 1.00 16.77 C ANISOU 1340 C ASN A 339 2187 2351 1833 428 -7 -9 C ATOM 1341 O ASN A 339 1.442 37.713 12.145 1.00 20.01 O ANISOU 1341 O ASN A 339 2575 2785 2243 424 7 9 O ATOM 1342 CB ASN A 339 0.858 40.076 10.160 1.00 16.13 C ANISOU 1342 CB ASN A 339 2100 2280 1750 431 7 8 C ATOM 1343 CG ASN A 339 -0.025 41.252 9.854 1.00 19.19 C ANISOU 1343 CG ASN A 339 2490 2684 2118 460 19 23 C ATOM 1344 OD1 ASN A 339 0.457 42.316 9.467 1.00 18.29 O ANISOU 1344 OD1 ASN A 339 2398 2549 2004 463 7 9 O ATOM 1345 ND2 ASN A 339 -1.324 41.080 10.048 1.00 15.21 N ANISOU 1345 ND2 ASN A 339 1962 2220 1596 483 43 56 N ATOM 1346 N TRP A 340 3.359 38.823 11.845 1.00 16.99 N ANISOU 1346 N TRP A 340 2235 2342 1879 408 -32 -36 N ATOM 1347 CA TRP A 340 4.175 37.628 12.043 1.00 20.51 C ANISOU 1347 CA TRP A 340 2678 2769 2344 382 -44 -49 C ATOM 1348 C TRP A 340 5.054 37.683 13.297 1.00 21.37 C ANISOU 1348 C TRP A 340 2805 2868 2447 398 -58 -63 C ATOM 1349 O TRP A 340 6.006 36.905 13.449 1.00 16.85 O ANISOU 1349 O TRP A 340 2237 2273 1893 377 -74 -78 O ATOM 1350 CB TRP A 340 4.999 37.294 10.788 1.00 15.91 C ANISOU 1350 CB TRP A 340 2097 2154 1794 341 -59 -64 C ATOM 1351 CG TRP A 340 5.825 38.406 10.204 1.00 14.37 C ANISOU 1351 CG TRP A 340 1916 1936 1607 335 -73 -75 C ATOM 1352 CD1 TRP A 340 5.421 39.325 9.282 1.00 19.63 C ANISOU 1352 CD1 TRP A 340 2582 2605 2272 336 -68 -70 C ATOM 1353 CD2 TRP A 340 7.220 38.670 10.447 1.00 15.06 C ANISOU 1353 CD2 TRP A 340 2017 1999 1707 326 -94 -91 C ATOM 1354 NE1 TRP A 340 6.467 40.163 8.956 1.00 20.07 N ANISOU 1354 NE1 TRP A 340 2650 2638 2337 328 -83 -82 N ATOM 1355 CE2 TRP A 340 7.580 39.782 9.660 1.00 15.97 C ANISOU 1355 CE2 TRP A 340 2138 2104 1827 322 -99 -94 C ATOM 1356 CE3 TRP A 340 8.194 38.077 11.259 1.00 17.46 C ANISOU 1356 CE3 TRP A 340 2327 2289 2019 322 -108 -102 C ATOM 1357 CZ2 TRP A 340 8.872 40.325 9.667 1.00 15.80 C ANISOU 1357 CZ2 TRP A 340 2126 2062 1816 315 -116 -105 C ATOM 1358 CZ3 TRP A 340 9.487 38.621 11.263 1.00 16.75 C ANISOU 1358 CZ3 TRP A 340 2247 2177 1940 316 -127 -113 C ATOM 1359 CH2 TRP A 340 9.807 39.727 10.471 1.00 11.59 C ANISOU 1359 CH2 TRP A 340 1597 1517 1290 312 -130 -114 C ATOM 1360 N GLU A 341 4.716 38.588 14.204 1.00 17.87 N ANISOU 1360 N GLU A 341 2374 2441 1975 438 -54 -58 N ATOM 1361 CA GLU A 341 5.451 38.676 15.450 1.00 24.13 C ANISOU 1361 CA GLU A 341 3185 3226 2757 458 -67 -71 C ATOM 1362 C GLU A 341 5.392 37.345 16.220 1.00 21.46 C ANISOU 1362 C GLU A 341 2834 2899 2419 455 -62 -67 C ATOM 1363 O GLU A 341 6.356 36.960 16.875 1.00 21.84 O ANISOU 1363 O GLU A 341 2896 2928 2475 451 -80 -83 O ATOM 1364 CB GLU A 341 4.934 39.834 16.305 1.00 24.58 C ANISOU 1364 CB GLU A 341 3260 3301 2780 508 -61 -64 C ATOM 1365 CG GLU A 341 5.938 40.279 17.353 1.00 32.23 C ANISOU 1365 CG GLU A 341 4257 4249 3740 527 -83 -83 C ATOM 1366 CD GLU A 341 5.454 41.457 18.188 1.00 36.24 C ANISOU 1366 CD GLU A 341 4789 4770 4209 581 -79 -78 C ATOM 1367 OE1 GLU A 341 4.237 41.743 18.175 1.00 37.70 O ANISOU 1367 OE1 GLU A 341 4965 4988 4372 609 -55 -56 O ATOM 1368 OE2 GLU A 341 6.300 42.094 18.854 1.00 36.40 O ANISOU 1368 OE2 GLU A 341 4839 4768 4222 596 -101 -95 O ATOM 1369 N PHE A 342 4.268 36.643 16.129 1.00 10.80 N ANISOU 1369 N PHE A 342 1458 1583 1061 458 -37 -42 N ATOM 1370 CA PHE A 342 4.122 35.348 16.789 1.00 16.96 C ANISOU 1370 CA PHE A 342 2222 2380 1842 454 -29 -33 C ATOM 1371 C PHE A 342 5.194 34.338 16.370 1.00 23.11 C ANISOU 1371 C PHE A 342 3006 3119 2655 411 -54 -52 C ATOM 1372 O PHE A 342 5.612 33.498 17.165 1.00 25.36 O ANISOU 1372 O PHE A 342 3291 3399 2947 405 -70 -48 O ATOM 1373 CB PHE A 342 2.709 34.776 16.581 1.00 13.50 C ANISOU 1373 CB PHE A 342 1745 1982 1403 448 -14 19 C ATOM 1374 CG PHE A 342 2.445 34.263 15.191 1.00 20.03 C ANISOU 1374 CG PHE A 342 2557 2797 2258 407 -16 26 C ATOM 1375 CD1 PHE A 342 2.626 32.924 14.887 1.00 18.79 C ANISOU 1375 CD1 PHE A 342 2386 2624 2130 366 -36 38 C ATOM 1376 CD2 PHE A 342 1.981 35.109 14.200 1.00 20.21 C ANISOU 1376 CD2 PHE A 342 2580 2824 2276 412 -1 22 C ATOM 1377 CE1 PHE A 342 2.362 32.441 13.616 1.00 13.15 C ANISOU 1377 CE1 PHE A 342 1661 1897 1440 332 -40 45 C ATOM 1378 CE2 PHE A 342 1.711 34.632 12.931 1.00 16.70 C ANISOU 1378 CE2 PHE A 342 2122 2368 1855 376 -4 29 C ATOM 1379 CZ PHE A 342 1.916 33.299 12.637 1.00 14.75 C ANISOU 1379 CZ PHE A 342 1863 2104 1637 337 -25 40 C ATOM 1380 N ILE A 343 5.646 34.428 15.126 1.00 25.04 N ANISOU 1380 N ILE A 343 3256 3336 2923 382 -62 -69 N ATOM 1381 CA ILE A 343 6.730 33.567 14.646 1.00 21.72 C ANISOU 1381 CA ILE A 343 2842 2876 2533 347 -84 -88 C ATOM 1382 C ILE A 343 8.067 33.883 15.329 1.00 20.93 C ANISOU 1382 C ILE A 343 2763 2749 2440 350 -109 -107 C ATOM 1383 O ILE A 343 8.823 32.984 15.722 1.00 19.38 O ANISOU 1383 O ILE A 343 2572 2534 2258 338 -124 -118 O ATOM 1384 CB ILE A 343 6.891 33.695 13.126 1.00 22.17 C ANISOU 1384 CB ILE A 343 2897 2914 2613 317 -89 -91 C ATOM 1385 CG1 ILE A 343 5.562 33.371 12.435 1.00 18.00 C ANISOU 1385 CG1 ILE A 343 2348 2411 2078 315 -65 -72 C ATOM 1386 CG2 ILE A 343 7.988 32.766 12.636 1.00 25.19 C ANISOU 1386 CG2 ILE A 343 3286 3260 3026 287 -110 -106 C ATOM 1387 CD1 ILE A 343 5.682 33.213 10.929 1.00 19.88 C ANISOU 1387 CD1 ILE A 343 2586 2629 2340 286 -71 -77 C ATOM 1388 N VAL A 344 8.360 35.169 15.470 1.00 17.83 N ANISOU 1388 N VAL A 344 2382 2355 2037 366 -115 -111 N ATOM 1389 CA VAL A 344 9.564 35.584 16.157 1.00 18.15 C ANISOU 1389 CA VAL A 344 2440 2374 2081 371 -138 -126 C ATOM 1390 C VAL A 344 9.607 34.944 17.545 1.00 23.89 C ANISOU 1390 C VAL A 344 3174 3108 2794 392 -140 -129 C ATOM 1391 O VAL A 344 10.586 34.280 17.904 1.00 24.30 O ANISOU 1391 O VAL A 344 3232 3138 2861 380 -159 -140 O ATOM 1392 CB VAL A 344 9.622 37.104 16.288 1.00 20.27 C ANISOU 1392 CB VAL A 344 2724 2644 2334 394 -141 -128 C ATOM 1393 CG1 VAL A 344 10.824 37.508 17.105 1.00 24.94 C ANISOU 1393 CG1 VAL A 344 3334 3215 2926 403 -165 -142 C ATOM 1394 CG2 VAL A 344 9.659 37.752 14.892 1.00 14.07 C ANISOU 1394 CG2 VAL A 344 1932 1851 1563 373 -139 -125 C ATOM 1395 N ASP A 345 8.532 35.118 18.309 1.00 21.58 N ANISOU 1395 N ASP A 345 2879 2849 2470 426 -120 -116 N ATOM 1396 CA ASP A 345 8.450 34.582 19.677 1.00 26.70 C ANISOU 1396 CA ASP A 345 3533 3512 3100 453 -118 -116 C ATOM 1397 C ASP A 345 8.429 33.044 19.741 1.00 24.28 C ANISOU 1397 C ASP A 345 3210 3206 2811 427 -122 -105 C ATOM 1398 O ASP A 345 9.032 32.447 20.636 1.00 24.15 O ANISOU 1398 O ASP A 345 3200 3180 2796 427 -140 -107 O ATOM 1399 CB ASP A 345 7.248 35.178 20.411 1.00 27.66 C ANISOU 1399 CB ASP A 345 3650 3677 3182 499 -93 -95 C ATOM 1400 CG ASP A 345 7.376 36.687 20.605 1.00 36.51 C ANISOU 1400 CG ASP A 345 4795 4791 4285 528 -101 -101 C ATOM 1401 OD1 ASP A 345 6.407 37.413 20.305 1.00 37.32 O ANISOU 1401 OD1 ASP A 345 4892 4919 4370 548 -82 -84 O ATOM 1402 OD2 ASP A 345 8.450 37.154 21.047 1.00 38.81 O ANISOU 1402 OD2 ASP A 345 5111 5054 4581 530 -127 -121 O ATOM 1403 N PHE A 346 7.739 32.422 18.788 1.00 21.46 N ANISOU 1403 N PHE A 346 2828 2858 2469 398 -114 -83 N ATOM 1404 CA PHE A 346 7.707 30.965 18.643 1.00 24.96 C ANISOU 1404 CA PHE A 346 3253 3295 2935 363 -129 -62 C ATOM 1405 C PHE A 346 9.113 30.385 18.475 1.00 26.38 C ANISOU 1405 C PHE A 346 3453 3430 3142 341 -154 -93 C ATOM 1406 O PHE A 346 9.479 29.388 19.100 1.00 25.17 O ANISOU 1406 O PHE A 346 3297 3268 2997 330 -172 -85 O ATOM 1407 CB PHE A 346 6.871 30.580 17.419 1.00 22.72 C ANISOU 1407 CB PHE A 346 2947 3019 2667 336 -121 -40 C ATOM 1408 CG PHE A 346 6.738 29.091 17.216 1.00 22.96 C ANISOU 1408 CG PHE A 346 2961 3041 2723 300 -139 -16 C ATOM 1409 CD1 PHE A 346 5.723 28.376 17.850 1.00 17.13 C ANISOU 1409 CD1 PHE A 346 2194 2336 1978 298 -139 31 C ATOM 1410 CD2 PHE A 346 7.623 28.406 16.390 1.00 23.32 C ANISOU 1410 CD2 PHE A 346 3019 3045 2799 271 -158 -38 C ATOM 1411 CE1 PHE A 346 5.592 27.000 17.666 1.00 20.79 C ANISOU 1411 CE1 PHE A 346 2643 2788 2467 264 -160 56 C ATOM 1412 CE2 PHE A 346 7.502 27.029 16.195 1.00 28.03 C ANISOU 1412 CE2 PHE A 346 3603 3629 3418 241 -178 -17 C ATOM 1413 CZ PHE A 346 6.481 26.322 16.834 1.00 26.40 C ANISOU 1413 CZ PHE A 346 3370 3454 3208 236 -181 30 C ATOM 1414 N VAL A 347 9.880 31.024 17.605 1.00 25.55 N ANISOU 1414 N VAL A 347 3364 3295 3049 337 -153 -127 N ATOM 1415 CA VAL A 347 11.238 30.623 17.285 1.00 21.27 C ANISOU 1415 CA VAL A 347 2834 2714 2534 317 -177 -147 C ATOM 1416 C VAL A 347 12.175 30.893 18.449 1.00 16.31 C ANISOU 1416 C VAL A 347 2221 2077 1899 333 -195 -157 C ATOM 1417 O VAL A 347 13.152 30.177 18.654 1.00 17.99 O ANISOU 1417 O VAL A 347 2439 2266 2130 321 -215 -165 O ATOM 1418 CB VAL A 347 11.729 31.383 16.036 1.00 24.19 C ANISOU 1418 CB VAL A 347 3199 3074 2919 299 -179 -146 C ATOM 1419 CG1 VAL A 347 13.225 31.331 15.946 1.00 29.53 C ANISOU 1419 CG1 VAL A 347 3880 3726 3615 287 -202 -155 C ATOM 1420 CG2 VAL A 347 11.083 30.792 14.777 1.00 19.67 C ANISOU 1420 CG2 VAL A 347 2614 2499 2359 276 -170 -138 C ATOM 1421 N ALA A 348 11.843 31.913 19.231 1.00 14.71 N ANISOU 1421 N ALA A 348 2025 1893 1669 365 -187 -156 N ATOM 1422 CA ALA A 348 12.649 32.324 20.383 1.00 20.68 C ANISOU 1422 CA ALA A 348 2800 2641 2416 386 -205 -167 C ATOM 1423 C ALA A 348 12.561 31.365 21.570 1.00 25.08 C ANISOU 1423 C ALA A 348 3365 3203 2964 401 -208 -170 C ATOM 1424 O ALA A 348 13.430 31.373 22.434 1.00 27.68 O ANISOU 1424 O ALA A 348 3709 3517 3292 411 -229 -181 O ATOM 1425 CB ALA A 348 12.271 33.758 20.826 1.00 19.13 C ANISOU 1425 CB ALA A 348 2616 2462 2192 419 -199 -166 C ATOM 1426 N THR A 349 11.506 30.560 21.627 1.00 27.90 N ANISOU 1426 N THR A 349 3698 3588 3314 392 -198 -138 N ATOM 1427 CA THR A 349 11.392 29.528 22.658 1.00 28.61 C ANISOU 1427 CA THR A 349 3780 3692 3399 389 -212 -115 C ATOM 1428 C THR A 349 12.625 28.627 22.631 1.00 31.24 C ANISOU 1428 C THR A 349 4124 3985 3761 366 -239 -133 C ATOM 1429 O THR A 349 13.005 28.127 21.570 1.00 28.41 O ANISOU 1429 O THR A 349 3762 3601 3430 338 -243 -142 O ATOM 1430 CB THR A 349 10.139 28.678 22.429 1.00 35.56 C ANISOU 1430 CB THR A 349 4629 4604 4280 372 -202 -70 C ATOM 1431 OG1 THR A 349 8.977 29.445 22.785 1.00 37.55 O ANISOU 1431 OG1 THR A 349 4869 4899 4500 402 -178 -47 O ATOM 1432 CG2 THR A 349 10.186 27.425 23.264 1.00 39.07 C ANISOU 1432 CG2 THR A 349 5064 5053 4728 359 -222 -46 C ATOM 1433 N PRO A 350 13.264 28.427 23.800 1.00 30.58 N ANISOU 1433 N PRO A 350 4054 3895 3669 380 -257 -139 N ATOM 1434 CA PRO A 350 14.516 27.659 23.905 1.00 28.91 C ANISOU 1434 CA PRO A 350 3855 3647 3483 364 -284 -157 C ATOM 1435 C PRO A 350 14.518 26.359 23.097 1.00 26.49 C ANISOU 1435 C PRO A 350 3533 3325 3205 328 -293 -145 C ATOM 1436 O PRO A 350 15.493 26.063 22.404 1.00 26.17 O ANISOU 1436 O PRO A 350 3502 3249 3192 314 -304 -167 O ATOM 1437 CB PRO A 350 14.612 27.356 25.405 1.00 29.95 C ANISOU 1437 CB PRO A 350 3994 3792 3595 383 -299 -146 C ATOM 1438 CG PRO A 350 13.945 28.544 26.061 1.00 26.60 C ANISOU 1438 CG PRO A 350 3576 3397 3133 422 -282 -143 C ATOM 1439 CD PRO A 350 12.829 28.964 25.108 1.00 26.68 C ANISOU 1439 CD PRO A 350 3567 3431 3139 417 -254 -128 C ATOM 1440 N GLU A 351 13.440 25.592 23.178 1.00 26.39 N ANISOU 1440 N GLU A 351 3499 3339 3188 314 -289 -108 N ATOM 1441 CA GLU A 351 13.382 24.323 22.461 1.00 30.26 C ANISOU 1441 CA GLU A 351 3978 3813 3706 281 -303 -93 C ATOM 1442 C GLU A 351 13.186 24.496 20.949 1.00 30.64 C ANISOU 1442 C GLU A 351 4022 3848 3773 264 -291 -102 C ATOM 1443 O GLU A 351 13.704 23.704 20.148 1.00 31.84 O ANISOU 1443 O GLU A 351 4177 3969 3952 243 -305 -110 O ATOM 1444 CB GLU A 351 12.304 23.412 23.053 1.00 34.89 C ANISOU 1444 CB GLU A 351 4541 4431 4285 270 -307 -47 C ATOM 1445 CG GLU A 351 12.286 22.009 22.452 1.00 49.64 C ANISOU 1445 CG GLU A 351 6401 6277 6183 235 -329 -31 C ATOM 1446 CD GLU A 351 13.628 21.285 22.567 1.00 55.66 C ANISOU 1446 CD GLU A 351 7185 6997 6967 228 -357 -56 C ATOM 1447 OE1 GLU A 351 14.410 21.600 23.496 1.00 55.49 O ANISOU 1447 OE1 GLU A 351 7179 6972 6935 248 -364 -74 O ATOM 1448 OE2 GLU A 351 13.898 20.396 21.724 1.00 55.77 O ANISOU 1448 OE2 GLU A 351 7201 6982 7009 206 -373 -59 O ATOM 1449 N HIS A 352 12.440 25.520 20.549 1.00 22.11 N ANISOU 1449 N HIS A 352 2934 2791 2676 275 -265 -100 N ATOM 1450 CA HIS A 352 12.246 25.758 19.121 1.00 23.40 C ANISOU 1450 CA HIS A 352 3095 2943 2854 261 -253 -108 C ATOM 1451 C HIS A 352 13.515 26.321 18.509 1.00 22.51 C ANISOU 1451 C HIS A 352 3003 2794 2755 266 -256 -149 C ATOM 1452 O HIS A 352 13.911 25.945 17.402 1.00 23.46 O ANISOU 1452 O HIS A 352 3126 2889 2898 250 -260 -161 O ATOM 1453 CB HIS A 352 11.079 26.711 18.868 1.00 27.31 C ANISOU 1453 CB HIS A 352 3575 3474 3328 273 -226 -92 C ATOM 1454 CG HIS A 352 9.756 26.165 19.303 1.00 28.76 C ANISOU 1454 CG HIS A 352 3731 3695 3500 268 -221 -46 C ATOM 1455 ND1 HIS A 352 8.743 26.965 19.779 1.00 25.15 N ANISOU 1455 ND1 HIS A 352 3261 3280 3014 292 -198 -24 N ATOM 1456 CD2 HIS A 352 9.289 24.896 19.349 1.00 27.49 C ANISOU 1456 CD2 HIS A 352 3554 3537 3355 243 -237 -13 C ATOM 1457 CE1 HIS A 352 7.701 26.215 20.087 1.00 28.22 C ANISOU 1457 CE1 HIS A 352 3622 3698 3400 283 -199 22 C ATOM 1458 NE2 HIS A 352 8.009 24.956 19.840 1.00 31.29 N ANISOU 1458 NE2 HIS A 352 4009 4064 3817 251 -223 30 N ATOM 1459 N LEU A 353 14.142 27.237 19.232 1.00 22.17 N ANISOU 1459 N LEU A 353 2976 2750 2699 291 -254 -170 N ATOM 1460 CA LEU A 353 15.339 27.883 18.736 1.00 23.19 C ANISOU 1460 CA LEU A 353 3104 2868 2840 286 -264 -177 C ATOM 1461 C LEU A 353 16.368 26.803 18.423 1.00 27.11 C ANISOU 1461 C LEU A 353 3600 3340 3361 270 -286 -180 C ATOM 1462 O LEU A 353 16.980 26.806 17.352 1.00 20.07 O ANISOU 1462 O LEU A 353 2699 2442 2484 257 -289 -178 O ATOM 1463 CB LEU A 353 15.886 28.870 19.766 1.00 15.97 C ANISOU 1463 CB LEU A 353 2201 1959 1909 310 -271 -185 C ATOM 1464 CG LEU A 353 17.060 29.704 19.257 1.00 21.15 C ANISOU 1464 CG LEU A 353 2855 2608 2575 306 -281 -190 C ATOM 1465 CD1 LEU A 353 16.591 30.685 18.195 1.00 23.57 C ANISOU 1465 CD1 LEU A 353 3152 2927 2878 301 -263 -183 C ATOM 1466 CD2 LEU A 353 17.782 30.419 20.402 1.00 19.38 C ANISOU 1466 CD2 LEU A 353 2645 2379 2338 328 -297 -200 C ATOM 1467 N ARG A 354 16.525 25.868 19.358 1.00 34.57 N ANISOU 1467 N ARG A 354 4555 4271 4309 272 -302 -183 N ATOM 1468 CA ARG A 354 17.476 24.770 19.216 1.00 37.28 C ANISOU 1468 CA ARG A 354 4899 4590 4674 260 -326 -186 C ATOM 1469 C ARG A 354 17.234 23.972 17.935 1.00 31.37 C ANISOU 1469 C ARG A 354 4141 3832 3944 240 -327 -178 C ATOM 1470 O ARG A 354 18.145 23.811 17.124 1.00 29.25 O ANISOU 1470 O ARG A 354 3867 3558 3689 235 -335 -180 O ATOM 1471 CB ARG A 354 17.408 23.845 20.433 1.00 45.28 C ANISOU 1471 CB ARG A 354 5926 5589 5687 265 -343 -188 C ATOM 1472 CG ARG A 354 18.372 22.667 20.371 1.00 52.98 C ANISOU 1472 CG ARG A 354 6905 6540 6686 254 -370 -190 C ATOM 1473 CD ARG A 354 18.099 21.641 21.474 1.00 58.58 C ANISOU 1473 CD ARG A 354 7619 7247 7394 250 -390 -176 C ATOM 1474 NE ARG A 354 16.894 20.854 21.218 1.00 66.73 N ANISOU 1474 NE ARG A 354 8634 8295 8426 229 -390 -143 N ATOM 1475 CZ ARG A 354 16.786 19.943 20.253 1.00 72.55 C ANISOU 1475 CZ ARG A 354 9368 9012 9185 209 -401 -138 C ATOM 1476 NH1 ARG A 354 17.808 19.707 19.437 1.00 72.86 N ANISOU 1476 NH1 ARG A 354 9420 9017 9246 211 -410 -164 N ATOM 1477 NH2 ARG A 354 15.653 19.271 20.095 1.00 73.77 N ANISOU 1477 NH2 ARG A 354 9506 9181 9340 189 -405 -104 N ATOM 1478 N GLN A 355 16.006 23.484 17.761 1.00 27.13 N ANISOU 1478 N GLN A 355 3606 3295 3409 230 -319 -169 N ATOM 1479 CA GLN A 355 15.635 22.695 16.589 1.00 28.34 C ANISOU 1479 CA GLN A 355 3753 3436 3580 210 -324 -161 C ATOM 1480 C GLN A 355 15.796 23.452 15.279 1.00 24.28 C ANISOU 1480 C GLN A 355 3225 2934 3064 208 -308 -161 C ATOM 1481 O GLN A 355 16.406 22.959 14.335 1.00 27.25 O ANISOU 1481 O GLN A 355 3598 3302 3455 202 -318 -161 O ATOM 1482 CB GLN A 355 14.175 22.261 16.661 1.00 33.07 C ANISOU 1482 CB GLN A 355 4338 4054 4174 195 -320 -130 C ATOM 1483 CG GLN A 355 13.801 21.413 17.831 1.00 40.15 C ANISOU 1483 CG GLN A 355 5226 4963 5065 188 -338 -102 C ATOM 1484 CD GLN A 355 12.388 20.899 17.694 1.00 44.20 C ANISOU 1484 CD GLN A 355 5716 5501 5578 169 -337 -60 C ATOM 1485 OE1 GLN A 355 12.033 20.291 16.679 1.00 43.30 O ANISOU 1485 OE1 GLN A 355 5598 5372 5482 151 -346 -52 O ATOM 1486 NE2 GLN A 355 11.564 21.153 18.708 1.00 47.96 N ANISOU 1486 NE2 GLN A 355 6175 6015 6031 176 -328 -31 N ATOM 1487 N ILE A 356 15.211 24.638 15.213 1.00 22.50 N ANISOU 1487 N ILE A 356 2735 2840 2973 454 -517 -324 N ATOM 1488 CA ILE A 356 15.144 25.369 13.953 1.00 23.09 C ANISOU 1488 CA ILE A 356 2815 2924 3035 447 -490 -341 C ATOM 1489 C ILE A 356 16.532 25.873 13.523 1.00 24.84 C ANISOU 1489 C ILE A 356 3027 3138 3274 453 -499 -382 C ATOM 1490 O ILE A 356 16.929 25.698 12.369 1.00 27.15 O ANISOU 1490 O ILE A 356 3316 3422 3579 448 -500 -402 O ATOM 1491 CB ILE A 356 14.088 26.510 14.024 1.00 21.51 C ANISOU 1491 CB ILE A 356 2624 2755 2793 442 -450 -324 C ATOM 1492 CG1 ILE A 356 12.708 25.921 14.321 1.00 22.47 C ANISOU 1492 CG1 ILE A 356 2752 2885 2902 437 -440 -284 C ATOM 1493 CG2 ILE A 356 14.028 27.281 12.724 1.00 17.28 C ANISOU 1493 CG2 ILE A 356 2093 2227 2245 433 -425 -338 C ATOM 1494 CD1 ILE A 356 11.657 26.952 14.715 1.00 22.77 C ANISOU 1494 CD1 ILE A 356 2795 2954 2901 436 -406 -265 C ATOM 1495 N CYS A 357 17.268 26.479 14.451 1.00 21.53 N ANISOU 1495 N CYS A 357 2602 2723 2855 462 -508 -393 N ATOM 1496 CA CYS A 357 18.638 26.926 14.179 1.00 25.77 C ANISOU 1496 CA CYS A 357 3128 3253 3411 467 -520 -430 C ATOM 1497 C CYS A 357 19.580 25.781 13.823 1.00 26.98 C ANISOU 1497 C CYS A 357 3267 3378 3606 473 -554 -450 C ATOM 1498 O CYS A 357 20.522 25.968 13.062 1.00 30.45 O ANISOU 1498 O CYS A 357 3695 3812 4062 474 -559 -481 O ATOM 1499 CB CYS A 357 19.214 27.690 15.373 1.00 21.43 C ANISOU 1499 CB CYS A 357 2574 2713 2857 477 -525 -435 C ATOM 1500 SG CYS A 357 18.379 29.241 15.691 1.00 28.69 S ANISOU 1500 SG CYS A 357 3505 3665 3730 474 -487 -424 S ATOM 1501 N SER A 358 19.328 24.600 14.377 1.00 24.60 N ANISOU 1501 N SER A 358 2965 3058 3322 476 -580 -432 N ATOM 1502 CA SER A 358 20.192 23.452 14.120 1.00 25.58 C ANISOU 1502 CA SER A 358 3077 3154 3490 483 -618 -450 C ATOM 1503 C SER A 358 19.800 22.701 12.851 1.00 23.96 C ANISOU 1503 C SER A 358 2872 2938 3294 477 -617 -453 C ATOM 1504 O SER A 358 20.298 21.602 12.599 1.00 23.87 O ANISOU 1504 O SER A 358 2851 2901 3318 483 -649 -465 O ATOM 1505 CB SER A 358 20.205 22.507 15.324 1.00 27.43 C ANISOU 1505 CB SER A 358 3309 3371 3744 489 -653 -429 C ATOM 1506 OG SER A 358 20.730 23.181 16.458 1.00 34.83 O ANISOU 1506 OG SER A 358 4242 4317 4676 497 -657 -430 O ATOM 1507 N ASP A 359 18.917 23.306 12.059 1.00 24.52 N ANISOU 1507 N ASP A 359 2955 3029 3334 465 -581 -444 N ATOM 1508 CA ASP A 359 18.437 22.707 10.814 1.00 21.20 C ANISOU 1508 CA ASP A 359 2536 2601 2917 458 -575 -445 C ATOM 1509 C ASP A 359 18.927 23.441 9.565 1.00 19.86 C ANISOU 1509 C ASP A 359 2361 2444 2742 453 -556 -473 C ATOM 1510 O ASP A 359 18.955 24.671 9.513 1.00 18.61 O ANISOU 1510 O ASP A 359 2206 2307 2559 448 -531 -476 O ATOM 1511 CB ASP A 359 16.908 22.650 10.788 1.00 18.75 C ANISOU 1511 CB ASP A 359 2243 2303 2578 446 -551 -406 C ATOM 1512 CG ASP A 359 16.386 22.009 9.523 1.00 24.14 C ANISOU 1512 CG ASP A 359 2928 2978 3265 439 -547 -406 C ATOM 1513 OD1 ASP A 359 16.405 20.756 9.450 1.00 28.70 O ANISOU 1513 OD1 ASP A 359 3502 3532 3871 442 -577 -404 O ATOM 1514 OD2 ASP A 359 15.985 22.749 8.592 1.00 22.58 O ANISOU 1514 OD2 ASP A 359 2737 2799 3044 429 -516 -408 O ATOM 1515 N LYS A 360 19.295 22.664 8.558 1.00 19.19 N ANISOU 1515 N LYS A 360 2266 2345 2681 455 -571 -493 N ATOM 1516 CA LYS A 360 19.724 23.184 7.269 1.00 27.13 C ANISOU 1516 CA LYS A 360 3263 3361 3683 450 -556 -519 C ATOM 1517 C LYS A 360 18.864 24.359 6.794 1.00 24.64 C ANISOU 1517 C LYS A 360 2963 3074 3326 435 -515 -500 C ATOM 1518 O LYS A 360 19.376 25.433 6.494 1.00 28.55 O ANISOU 1518 O LYS A 360 3452 3585 3810 431 -499 -515 O ATOM 1519 CB LYS A 360 19.664 22.057 6.236 1.00 34.52 C ANISOU 1519 CB LYS A 360 4193 4282 4642 451 -571 -530 C ATOM 1520 CG LYS A 360 20.231 22.414 4.882 1.00 40.52 C ANISOU 1520 CG LYS A 360 4939 5053 5403 448 -561 -559 C ATOM 1521 CD LYS A 360 19.726 21.459 3.805 1.00 47.03 C ANISOU 1521 CD LYS A 360 5764 5869 6237 446 -566 -561 C ATOM 1522 CE LYS A 360 20.064 20.013 4.114 1.00 53.00 C ANISOU 1522 CE LYS A 360 6511 6594 7033 461 -608 -571 C ATOM 1523 NZ LYS A 360 19.631 19.115 3.003 1.00 56.18 N ANISOU 1523 NZ LYS A 360 6913 6988 7446 460 -615 -576 N ATOM 1524 N TYR A 361 17.553 24.159 6.729 1.00 20.38 N ANISOU 1524 N TYR A 361 2440 2539 2766 426 -498 -468 N ATOM 1525 CA TYR A 361 16.672 25.211 6.232 1.00 17.48 C ANISOU 1525 CA TYR A 361 2086 2195 2362 412 -460 -449 C ATOM 1526 C TYR A 361 16.280 26.217 7.297 1.00 19.76 C ANISOU 1526 C TYR A 361 2384 2500 2625 411 -443 -431 C ATOM 1527 O TYR A 361 16.255 27.416 7.037 1.00 24.83 O ANISOU 1527 O TYR A 361 3029 3161 3245 405 -421 -433 O ATOM 1528 CB TYR A 361 15.448 24.621 5.539 1.00 17.84 C ANISOU 1528 CB TYR A 361 2143 2239 2396 402 -448 -424 C ATOM 1529 CG TYR A 361 15.826 23.648 4.442 1.00 23.90 C ANISOU 1529 CG TYR A 361 2901 2992 3189 404 -465 -444 C ATOM 1530 CD1 TYR A 361 16.353 24.099 3.237 1.00 21.72 C ANISOU 1530 CD1 TYR A 361 2616 2725 2913 399 -457 -468 C ATOM 1531 CD2 TYR A 361 15.678 22.278 4.626 1.00 26.00 C ANISOU 1531 CD2 TYR A 361 3165 3233 3479 411 -493 -440 C ATOM 1532 CE1 TYR A 361 16.710 23.214 2.248 1.00 29.76 C ANISOU 1532 CE1 TYR A 361 3623 3732 3954 403 -473 -488 C ATOM 1533 CE2 TYR A 361 16.028 21.383 3.645 1.00 27.47 C ANISOU 1533 CE2 TYR A 361 3342 3406 3691 414 -511 -461 C ATOM 1534 CZ TYR A 361 16.548 21.852 2.456 1.00 34.76 C ANISOU 1534 CZ TYR A 361 4255 4340 4611 411 -500 -486 C ATOM 1535 OH TYR A 361 16.897 20.955 1.471 1.00 39.00 O ANISOU 1535 OH TYR A 361 4780 4865 5172 416 -519 -509 O ATOM 1536 N GLY A 362 15.988 25.728 8.497 1.00 18.38 N ANISOU 1536 N GLY A 362 2213 2318 2453 419 -455 -414 N ATOM 1537 CA GLY A 362 15.627 26.587 9.607 1.00 16.54 C ANISOU 1537 CA GLY A 362 1987 2102 2197 421 -442 -398 C ATOM 1538 C GLY A 362 16.627 27.689 9.926 1.00 16.73 C ANISOU 1538 C GLY A 362 2004 2135 2219 426 -441 -422 C ATOM 1539 O GLY A 362 16.228 28.799 10.266 1.00 17.32 O ANISOU 1539 O GLY A 362 2085 2228 2267 423 -419 -413 O ATOM 1540 N CYS A 363 17.925 27.402 9.814 1.00 16.04 N ANISOU 1540 N CYS A 363 1900 2032 2160 433 -466 -453 N ATOM 1541 CA CYS A 363 18.920 28.435 10.088 1.00 16.81 C ANISOU 1541 CA CYS A 363 1990 2138 2259 437 -466 -476 C ATOM 1542 C CYS A 363 18.849 29.570 9.065 1.00 16.60 C ANISOU 1542 C CYS A 363 1965 2129 2213 424 -441 -482 C ATOM 1543 O CYS A 363 19.079 30.725 9.410 1.00 24.80 O ANISOU 1543 O CYS A 363 3004 3180 3237 423 -431 -486 O ATOM 1544 CB CYS A 363 20.352 27.875 10.226 1.00 18.94 C ANISOU 1544 CB CYS A 363 2240 2390 2567 448 -499 -508 C ATOM 1545 SG CYS A 363 21.082 27.180 8.724 1.00 40.14 S ANISOU 1545 SG CYS A 363 4908 5064 5280 446 -510 -537 S ATOM 1546 N ARG A 364 18.528 29.256 7.816 1.00 15.82 N ANISOU 1546 N ARG A 364 1866 2030 2114 415 -432 -482 N ATOM 1547 CA ARG A 364 18.284 30.313 6.822 1.00 16.43 C ANISOU 1547 CA ARG A 364 1946 2124 2171 401 -408 -481 C ATOM 1548 C ARG A 364 17.054 31.145 7.214 1.00 19.64 C ANISOU 1548 C ARG A 364 2371 2547 2543 394 -382 -450 C ATOM 1549 O ARG A 364 17.073 32.381 7.134 1.00 21.09 O ANISOU 1549 O ARG A 364 2557 2745 2711 389 -367 -451 O ATOM 1550 CB ARG A 364 18.115 29.729 5.413 1.00 9.99 C ANISOU 1550 CB ARG A 364 1128 1306 1363 392 -404 -484 C ATOM 1551 CG ARG A 364 17.836 30.756 4.323 1.00 20.83 C ANISOU 1551 CG ARG A 364 2503 2695 2717 377 -380 -480 C ATOM 1552 CD ARG A 364 18.739 32.007 4.434 1.00 27.97 C ANISOU 1552 CD ARG A 364 3398 3609 3621 376 -379 -497 C ATOM 1553 NE ARG A 364 20.148 31.696 4.188 1.00 37.35 N ANISOU 1553 NE ARG A 364 4562 4789 4839 383 -399 -532 N ATOM 1554 CZ ARG A 364 21.100 32.609 3.988 1.00 39.65 C ANISOU 1554 CZ ARG A 364 4838 5088 5139 381 -399 -550 C ATOM 1555 NH1 ARG A 364 20.802 33.901 4.000 1.00 40.29 N ANISOU 1555 NH1 ARG A 364 4923 5182 5202 373 -380 -534 N ATOM 1556 NH2 ARG A 364 22.353 32.231 3.770 1.00 33.19 N ANISOU 1556 NH2 ARG A 364 3997 4263 4349 388 -417 -584 N ATOM 1557 N VAL A 365 15.992 30.467 7.653 1.00 15.00 N ANISOU 1557 N VAL A 365 1796 1958 1946 396 -377 -424 N ATOM 1558 CA VAL A 365 14.792 31.163 8.114 1.00 10.86 C ANISOU 1558 CA VAL A 365 1285 1450 1390 393 -352 -396 C ATOM 1559 C VAL A 365 15.092 32.130 9.284 1.00 15.08 C ANISOU 1559 C VAL A 365 1820 1996 1915 401 -352 -400 C ATOM 1560 O VAL A 365 14.613 33.272 9.311 1.00 12.46 O ANISOU 1560 O VAL A 365 1495 1680 1559 397 -334 -392 O ATOM 1561 CB VAL A 365 13.707 30.182 8.551 1.00 14.64 C ANISOU 1561 CB VAL A 365 1772 1926 1864 395 -350 -368 C ATOM 1562 CG1 VAL A 365 12.555 30.937 9.216 1.00 14.79 C ANISOU 1562 CG1 VAL A 365 1801 1965 1852 395 -326 -342 C ATOM 1563 CG2 VAL A 365 13.204 29.388 7.357 1.00 12.29 C ANISOU 1563 CG2 VAL A 365 1476 1620 1572 385 -346 -361 C ATOM 1564 N VAL A 366 15.893 31.682 10.244 1.00 14.10 N ANISOU 1564 N VAL A 366 1688 1861 1808 414 -375 -413 N ATOM 1565 CA VAL A 366 16.200 32.531 11.382 1.00 14.63 C ANISOU 1565 CA VAL A 366 1754 1937 1866 424 -377 -418 C ATOM 1566 C VAL A 366 17.035 33.719 10.920 1.00 16.21 C ANISOU 1566 C VAL A 366 1948 2143 2067 419 -375 -441 C ATOM 1567 O VAL A 366 16.818 34.850 11.365 1.00 15.17 O ANISOU 1567 O VAL A 366 1822 2026 1917 420 -364 -438 O ATOM 1568 CB VAL A 366 16.898 31.748 12.516 1.00 15.36 C ANISOU 1568 CB VAL A 366 1838 2016 1980 438 -404 -426 C ATOM 1569 CG1 VAL A 366 17.404 32.696 13.583 1.00 17.41 C ANISOU 1569 CG1 VAL A 366 2096 2286 2233 448 -408 -436 C ATOM 1570 CG2 VAL A 366 15.926 30.731 13.122 1.00 11.42 C ANISOU 1570 CG2 VAL A 366 1345 1515 1477 442 -406 -397 C ATOM 1571 N GLN A 367 17.974 33.477 10.005 1.00 11.66 N ANISOU 1571 N GLN A 367 1361 1557 1514 414 -386 -463 N ATOM 1572 CA GLN A 367 18.817 34.563 9.538 1.00 18.23 C ANISOU 1572 CA GLN A 367 2184 2394 2350 409 -385 -483 C ATOM 1573 C GLN A 367 17.973 35.619 8.816 1.00 17.92 C ANISOU 1573 C GLN A 367 2155 2370 2285 395 -359 -467 C ATOM 1574 O GLN A 367 18.107 36.820 9.050 1.00 19.97 O ANISOU 1574 O GLN A 367 2414 2639 2536 394 -353 -469 O ATOM 1575 CB GLN A 367 19.924 34.058 8.615 1.00 22.72 C ANISOU 1575 CB GLN A 367 2735 2951 2947 406 -399 -509 C ATOM 1576 CG GLN A 367 21.002 35.111 8.405 1.00 32.68 C ANISOU 1576 CG GLN A 367 3981 4216 4218 403 -402 -532 C ATOM 1577 CD GLN A 367 22.160 34.632 7.556 1.00 40.40 C ANISOU 1577 CD GLN A 367 4938 5186 5226 403 -415 -560 C ATOM 1578 OE1 GLN A 367 22.664 33.521 7.734 1.00 40.32 O ANISOU 1578 OE1 GLN A 367 4918 5162 5238 413 -435 -572 O ATOM 1579 NE2 GLN A 367 22.603 35.485 6.634 1.00 44.18 N ANISOU 1579 NE2 GLN A 367 5405 5674 5708 393 -405 -567 N ATOM 1580 N THR A 368 17.118 35.157 7.917 1.00 15.40 N ANISOU 1580 N THR A 368 1843 2051 1957 385 -346 -450 N ATOM 1581 CA THR A 368 16.193 36.040 7.225 1.00 14.02 C ANISOU 1581 CA THR A 368 1676 1889 1762 374 -322 -427 C ATOM 1582 C THR A 368 15.395 36.893 8.212 1.00 19.98 C ANISOU 1582 C THR A 368 2442 2657 2492 379 -311 -411 C ATOM 1583 O THR A 368 15.195 38.103 8.001 1.00 15.85 O ANISOU 1583 O THR A 368 1918 2143 1962 374 -299 -403 O ATOM 1584 CB THR A 368 15.248 35.215 6.359 1.00 14.33 C ANISOU 1584 CB THR A 368 1724 1927 1794 365 -311 -409 C ATOM 1585 OG1 THR A 368 16.030 34.593 5.335 1.00 16.94 O ANISOU 1585 OG1 THR A 368 2041 2247 2148 360 -321 -425 O ATOM 1586 CG2 THR A 368 14.168 36.102 5.704 1.00 11.58 C ANISOU 1586 CG2 THR A 368 1383 1591 1426 353 -285 -381 C ATOM 1587 N ILE A 369 14.950 36.262 9.296 1.00 16.22 N ANISOU 1587 N ILE A 369 1973 2181 2008 391 -315 -405 N ATOM 1588 CA ILE A 369 14.200 36.975 10.314 1.00 15.06 C ANISOU 1588 CA ILE A 369 1835 2050 1839 400 -305 -392 C ATOM 1589 C ILE A 369 15.075 38.054 10.950 1.00 19.15 C ANISOU 1589 C ILE A 369 2346 2570 2359 406 -315 -413 C ATOM 1590 O ILE A 369 14.677 39.224 11.044 1.00 15.40 O ANISOU 1590 O ILE A 369 1872 2107 1871 406 -304 -405 O ATOM 1591 CB ILE A 369 13.631 36.019 11.376 1.00 13.02 C ANISOU 1591 CB ILE A 369 1580 1793 1576 412 -307 -378 C ATOM 1592 CG1 ILE A 369 12.449 35.252 10.780 1.00 14.13 C ANISOU 1592 CG1 ILE A 369 1727 1935 1708 404 -291 -351 C ATOM 1593 CG2 ILE A 369 13.175 36.804 12.627 1.00 11.22 C ANISOU 1593 CG2 ILE A 369 1355 1581 1327 426 -302 -372 C ATOM 1594 CD1 ILE A 369 11.908 34.124 11.651 1.00 19.55 C ANISOU 1594 CD1 ILE A 369 2413 2619 2395 414 -296 -334 C ATOM 1595 N ILE A 370 16.283 37.666 11.354 1.00 18.97 N ANISOU 1595 N ILE A 370 2313 2537 2360 413 -336 -436 N ATOM 1596 CA ILE A 370 17.203 38.611 11.981 1.00 20.52 C ANISOU 1596 CA ILE A 370 2501 2734 2562 420 -348 -457 C ATOM 1597 C ILE A 370 17.457 39.812 11.082 1.00 19.99 C ANISOU 1597 C ILE A 370 2425 2670 2499 408 -339 -456 C ATOM 1598 O ILE A 370 17.409 40.961 11.538 1.00 13.88 O ANISOU 1598 O ILE A 370 1650 1904 1718 412 -337 -456 O ATOM 1599 CB ILE A 370 18.513 37.930 12.367 1.00 16.04 C ANISOU 1599 CB ILE A 370 1920 2152 2023 428 -372 -480 C ATOM 1600 CG1 ILE A 370 18.250 36.938 13.491 1.00 9.32 C ANISOU 1600 CG1 ILE A 370 1071 1297 1172 442 -381 -471 C ATOM 1601 CG2 ILE A 370 19.573 38.943 12.787 1.00 11.04 C ANISOU 1601 CG2 ILE A 370 1276 1518 1400 432 -383 -504 C ATOM 1602 CD1 ILE A 370 19.433 36.021 13.736 1.00 13.73 C ANISOU 1602 CD1 ILE A 370 1616 1837 1763 449 -407 -490 C ATOM 1603 N GLU A 371 17.684 39.542 9.799 1.00 16.88 N ANISOU 1603 N GLU A 371 2025 2270 2119 395 -335 -455 N ATOM 1604 CA GLU A 371 17.933 40.597 8.818 1.00 16.01 C ANISOU 1604 CA GLU A 371 1906 2162 2016 383 -326 -453 C ATOM 1605 C GLU A 371 16.767 41.577 8.714 1.00 21.11 C ANISOU 1605 C GLU A 371 2562 2818 2639 378 -308 -429 C ATOM 1606 O GLU A 371 16.971 42.796 8.665 1.00 21.97 O ANISOU 1606 O GLU A 371 2667 2930 2751 376 -306 -432 O ATOM 1607 CB GLU A 371 18.261 39.977 7.455 1.00 10.40 C ANISOU 1607 CB GLU A 371 1186 1444 1320 371 -324 -455 C ATOM 1608 CG GLU A 371 19.604 39.240 7.480 1.00 18.07 C ANISOU 1608 CG GLU A 371 2141 2405 2318 376 -344 -485 C ATOM 1609 CD GLU A 371 19.889 38.457 6.209 1.00 22.89 C ANISOU 1609 CD GLU A 371 2743 3011 2943 368 -343 -490 C ATOM 1610 OE1 GLU A 371 21.065 38.374 5.813 1.00 29.61 O ANISOU 1610 OE1 GLU A 371 3576 3858 3818 368 -354 -515 O ATOM 1611 OE2 GLU A 371 18.939 37.930 5.605 1.00 26.59 O ANISOU 1611 OE2 GLU A 371 3223 3481 3400 361 -332 -471 O ATOM 1612 N LYS A 372 15.548 41.044 8.700 1.00 13.33 N ANISOU 1612 N LYS A 372 1592 1839 1635 378 -295 -407 N ATOM 1613 CA LYS A 372 14.360 41.883 8.660 1.00 17.06 C ANISOU 1613 CA LYS A 372 2074 2322 2087 375 -277 -384 C ATOM 1614 C LYS A 372 14.236 42.741 9.914 1.00 21.64 C ANISOU 1614 C LYS A 372 2656 2911 2655 390 -282 -389 C ATOM 1615 O LYS A 372 13.737 43.866 9.858 1.00 26.18 O ANISOU 1615 O LYS A 372 3233 3492 3222 389 -275 -381 O ATOM 1616 CB LYS A 372 13.098 41.035 8.501 1.00 17.50 C ANISOU 1616 CB LYS A 372 2142 2382 2124 373 -263 -360 C ATOM 1617 CG LYS A 372 11.808 41.861 8.431 1.00 17.64 C ANISOU 1617 CG LYS A 372 2170 2412 2121 372 -244 -337 C ATOM 1618 CD LYS A 372 11.844 42.860 7.286 1.00 15.30 C ANISOU 1618 CD LYS A 372 1868 2111 1832 357 -237 -331 C ATOM 1619 CE LYS A 372 12.098 42.179 5.933 1.00 16.59 C ANISOU 1619 CE LYS A 372 2029 2266 2009 341 -233 -328 C ATOM 1620 NZ LYS A 372 12.258 43.173 4.814 1.00 20.54 N ANISOU 1620 NZ LYS A 372 2524 2762 2519 328 -227 -324 N ATOM 1621 N LEU A 373 14.683 42.202 11.046 1.00 18.55 N ANISOU 1621 N LEU A 373 2265 2521 2264 404 -295 -403 N ATOM 1622 CA LEU A 373 14.569 42.900 12.322 1.00 18.47 C ANISOU 1622 CA LEU A 373 2257 2520 2240 421 -301 -409 C ATOM 1623 C LEU A 373 15.729 43.871 12.578 1.00 18.10 C ANISOU 1623 C LEU A 373 2197 2468 2211 423 -316 -432 C ATOM 1624 O LEU A 373 15.838 44.451 13.665 1.00 21.26 O ANISOU 1624 O LEU A 373 2598 2875 2604 438 -324 -442 O ATOM 1625 CB LEU A 373 14.447 41.894 13.478 1.00 18.69 C ANISOU 1625 CB LEU A 373 2291 2553 2258 436 -307 -413 C ATOM 1626 CG LEU A 373 13.246 40.938 13.437 1.00 21.52 C ANISOU 1626 CG LEU A 373 2660 2918 2598 435 -292 -391 C ATOM 1627 CD1 LEU A 373 13.329 39.885 14.559 1.00 20.88 C ANISOU 1627 CD1 LEU A 373 2580 2838 2516 450 -301 -394 C ATOM 1628 CD2 LEU A 373 11.913 41.705 13.498 1.00 19.96 C ANISOU 1628 CD2 LEU A 373 2470 2738 2376 438 -273 -369 C ATOM 1629 N THR A 374 16.595 44.045 11.583 1.00 12.93 N ANISOU 1629 N THR A 374 1532 1802 1579 410 -319 -442 N ATOM 1630 CA THR A 374 17.793 44.865 11.767 1.00 16.41 C ANISOU 1630 CA THR A 374 1958 2236 2039 412 -334 -465 C ATOM 1631 C THR A 374 17.543 46.307 11.324 1.00 20.09 C ANISOU 1631 C THR A 374 2423 2705 2506 406 -327 -460 C ATOM 1632 O THR A 374 17.001 46.553 10.244 1.00 20.59 O ANISOU 1632 O THR A 374 2489 2767 2568 392 -314 -444 O ATOM 1633 CB THR A 374 19.007 44.279 11.005 1.00 19.45 C ANISOU 1633 CB THR A 374 2329 2609 2451 403 -343 -481 C ATOM 1634 OG1 THR A 374 19.282 42.955 11.477 1.00 19.07 O ANISOU 1634 OG1 THR A 374 2282 2556 2406 411 -352 -489 O ATOM 1635 CG2 THR A 374 20.244 45.147 11.207 1.00 15.11 C ANISOU 1635 CG2 THR A 374 1764 2054 1922 405 -356 -505 C ATOM 1636 N ALA A 375 17.916 47.262 12.169 1.00 19.57 N ANISOU 1636 N ALA A 375 2353 2640 2441 417 -338 -474 N ATOM 1637 CA ALA A 375 17.714 48.665 11.841 1.00 23.89 C ANISOU 1637 CA ALA A 375 2899 3187 2990 413 -336 -473 C ATOM 1638 C ALA A 375 18.801 49.090 10.873 1.00 23.31 C ANISOU 1638 C ALA A 375 2811 3102 2945 399 -339 -485 C ATOM 1639 O ALA A 375 19.721 49.832 11.234 1.00 24.19 O ANISOU 1639 O ALA A 375 2911 3208 3073 403 -352 -505 O ATOM 1640 CB ALA A 375 17.747 49.522 13.097 1.00 28.81 C ANISOU 1640 CB ALA A 375 3523 3817 3608 431 -348 -486 C ATOM 1641 N ASP A 376 18.712 48.585 9.648 1.00 17.79 N ANISOU 1641 N ASP A 376 2110 2398 2251 383 -328 -474 N ATOM 1642 CA ASP A 376 19.705 48.898 8.631 1.00 22.86 C ANISOU 1642 CA ASP A 376 2736 3031 2917 369 -329 -485 C ATOM 1643 C ASP A 376 19.115 49.827 7.576 1.00 22.21 C ANISOU 1643 C ASP A 376 2656 2946 2836 355 -316 -470 C ATOM 1644 O ASP A 376 18.002 50.337 7.743 1.00 26.70 O ANISOU 1644 O ASP A 376 3237 3519 3387 358 -309 -454 O ATOM 1645 CB ASP A 376 20.278 47.616 8.008 1.00 25.85 C ANISOU 1645 CB ASP A 376 3108 3408 3307 364 -328 -490 C ATOM 1646 CG ASP A 376 19.205 46.711 7.419 1.00 30.99 C ANISOU 1646 CG ASP A 376 3772 4062 3941 358 -314 -466 C ATOM 1647 OD1 ASP A 376 18.083 47.192 7.150 1.00 34.18 O ANISOU 1647 OD1 ASP A 376 4188 4470 4329 353 -301 -445 O ATOM 1648 OD2 ASP A 376 19.490 45.511 7.223 1.00 35.01 O ANISOU 1648 OD2 ASP A 376 4278 4569 4454 358 -316 -470 O ATOM 1649 N SER A 377 19.857 50.051 6.497 1.00 23.58 N ANISOU 1649 N SER A 377 2817 3114 3030 342 -313 -477 N ATOM 1650 CA SER A 377 19.456 51.029 5.488 1.00 30.75 C ANISOU 1650 CA SER A 377 3725 4016 3941 328 -303 -466 C ATOM 1651 C SER A 377 18.171 50.607 4.785 1.00 28.67 C ANISOU 1651 C SER A 377 3477 3758 3660 320 -286 -438 C ATOM 1652 O SER A 377 17.418 51.444 4.282 1.00 30.14 O ANISOU 1652 O SER A 377 3669 3941 3841 313 -278 -424 O ATOM 1653 CB SER A 377 20.574 51.250 4.465 1.00 33.26 C ANISOU 1653 CB SER A 377 4025 4328 4284 316 -302 -480 C ATOM 1654 OG SER A 377 21.045 50.012 3.966 1.00 41.17 O ANISOU 1654 OG SER A 377 5020 5333 5289 313 -299 -484 O ATOM 1655 N MET A 378 17.917 49.307 4.770 1.00 23.00 N ANISOU 1655 N MET A 378 2764 3045 2931 322 -282 -431 N ATOM 1656 CA MET A 378 16.719 48.792 4.131 1.00 29.53 C ANISOU 1656 CA MET A 378 3604 3875 3741 314 -267 -405 C ATOM 1657 C MET A 378 15.438 49.077 4.916 1.00 26.25 C ANISOU 1657 C MET A 378 3205 3467 3302 324 -262 -389 C ATOM 1658 O MET A 378 14.344 48.938 4.379 1.00 27.26 O ANISOU 1658 O MET A 378 3344 3597 3416 317 -248 -366 O ATOM 1659 CB MET A 378 16.861 47.293 3.854 1.00 32.93 C ANISOU 1659 CB MET A 378 4034 4308 4170 314 -265 -404 C ATOM 1660 CG MET A 378 18.012 46.974 2.904 1.00 43.28 C ANISOU 1660 CG MET A 378 5328 5614 5502 305 -267 -421 C ATOM 1661 SD MET A 378 17.883 45.334 2.176 1.00 95.82 S ANISOU 1661 SD MET A 378 11983 12271 12155 302 -262 -416 S ATOM 1662 CE MET A 378 16.295 45.470 1.356 1.00 98.72 C ANISOU 1662 CE MET A 378 12369 12641 12502 290 -242 -381 C ATOM 1663 N ASN A 379 15.567 49.481 6.176 1.00 20.60 N ANISOU 1663 N ASN A 379 2491 2755 2583 339 -274 -401 N ATOM 1664 CA ASN A 379 14.383 49.683 7.010 1.00 18.65 C ANISOU 1664 CA ASN A 379 2258 2518 2312 351 -270 -388 C ATOM 1665 C ASN A 379 14.078 51.140 7.340 1.00 17.42 C ANISOU 1665 C ASN A 379 2103 2361 2156 356 -275 -392 C ATOM 1666 O ASN A 379 13.261 51.421 8.218 1.00 18.08 O ANISOU 1666 O ASN A 379 2196 2454 2221 371 -276 -389 O ATOM 1667 CB ASN A 379 14.487 48.852 8.296 1.00 23.33 C ANISOU 1667 CB ASN A 379 2853 3118 2894 368 -278 -396 C ATOM 1668 CG ASN A 379 14.083 47.412 8.062 1.00 27.00 C ANISOU 1668 CG ASN A 379 3324 3586 3349 365 -269 -383 C ATOM 1669 OD1 ASN A 379 13.378 47.128 7.089 1.00 29.30 O ANISOU 1669 OD1 ASN A 379 3620 3876 3635 353 -255 -364 O ATOM 1670 ND2 ASN A 379 14.520 46.503 8.924 1.00 22.04 N ANISOU 1670 ND2 ASN A 379 2694 2959 2719 376 -279 -393 N ATOM 1671 N VAL A 380 14.714 52.069 6.630 1.00 18.73 N ANISOU 1671 N VAL A 380 2259 2515 2342 346 -279 -401 N ATOM 1672 CA VAL A 380 14.508 53.491 6.910 1.00 20.75 C ANISOU 1672 CA VAL A 380 2515 2767 2602 351 -287 -408 C ATOM 1673 C VAL A 380 13.082 53.969 6.597 1.00 17.71 C ANISOU 1673 C VAL A 380 2143 2385 2200 350 -277 -388 C ATOM 1674 O VAL A 380 12.673 55.045 7.030 1.00 20.10 O ANISOU 1674 O VAL A 380 2447 2687 2505 360 -283 -391 O ATOM 1675 CB VAL A 380 15.527 54.382 6.152 1.00 23.63 C ANISOU 1675 CB VAL A 380 2866 3117 2996 338 -294 -422 C ATOM 1676 CG1 VAL A 380 16.950 54.128 6.656 1.00 22.05 C ANISOU 1676 CG1 VAL A 380 2651 2914 2813 343 -306 -446 C ATOM 1677 CG2 VAL A 380 15.424 54.167 4.651 1.00 18.66 C ANISOU 1677 CG2 VAL A 380 2234 2481 2374 318 -279 -407 C ATOM 1678 N ASP A 381 12.334 53.178 5.835 1.00 17.68 N ANISOU 1678 N ASP A 381 2147 2385 2185 340 -260 -366 N ATOM 1679 CA ASP A 381 10.967 53.552 5.472 1.00 19.23 C ANISOU 1679 CA ASP A 381 2354 2585 2369 339 -246 -343 C ATOM 1680 C ASP A 381 9.952 53.204 6.561 1.00 17.18 C ANISOU 1680 C ASP A 381 2105 2341 2081 358 -244 -336 C ATOM 1681 O ASP A 381 8.770 53.522 6.440 1.00 20.15 O ANISOU 1681 O ASP A 381 2488 2722 2447 362 -233 -317 O ATOM 1682 CB ASP A 381 10.558 52.870 4.171 1.00 16.92 C ANISOU 1682 CB ASP A 381 2064 2289 2076 321 -229 -321 C ATOM 1683 CG ASP A 381 10.536 51.371 4.297 1.00 19.40 C ANISOU 1683 CG ASP A 381 2383 2612 2376 321 -222 -315 C ATOM 1684 OD1 ASP A 381 11.592 50.786 4.605 1.00 20.26 O ANISOU 1684 OD1 ASP A 381 2483 2719 2495 323 -231 -331 O ATOM 1685 OD2 ASP A 381 9.463 50.774 4.106 1.00 21.36 O ANISOU 1685 OD2 ASP A 381 2641 2867 2606 320 -208 -294 O ATOM 1686 N LEU A 382 10.402 52.530 7.611 1.00 17.82 N ANISOU 1686 N LEU A 382 2185 2431 2154 371 -252 -349 N ATOM 1687 CA LEU A 382 9.519 52.222 8.724 1.00 15.68 C ANISOU 1687 CA LEU A 382 1922 2177 1858 391 -249 -344 C ATOM 1688 C LEU A 382 9.160 53.497 9.468 1.00 16.03 C ANISOU 1688 C LEU A 382 1967 2226 1897 408 -261 -356 C ATOM 1689 O LEU A 382 9.994 54.390 9.629 1.00 16.92 O ANISOU 1689 O LEU A 382 2071 2328 2030 409 -276 -375 O ATOM 1690 CB LEU A 382 10.187 51.244 9.697 1.00 12.52 C ANISOU 1690 CB LEU A 382 1519 1784 1455 401 -256 -354 C ATOM 1691 CG LEU A 382 10.470 49.808 9.214 1.00 14.35 C ANISOU 1691 CG LEU A 382 1750 2012 1689 390 -248 -345 C ATOM 1692 CD1 LEU A 382 11.107 48.981 10.327 1.00 16.23 C ANISOU 1692 CD1 LEU A 382 1986 2257 1925 404 -258 -359 C ATOM 1693 CD2 LEU A 382 9.205 49.133 8.717 1.00 12.73 C ANISOU 1693 CD2 LEU A 382 1555 1814 1467 385 -228 -318 C ATOM 1694 N THR A 383 7.918 53.588 9.921 1.00 15.80 N ANISOU 1694 N THR A 383 1946 2211 1848 422 -252 -342 N ATOM 1695 CA THR A 383 7.567 54.622 10.878 1.00 17.71 C ANISOU 1695 CA THR A 383 2185 2458 2084 444 -263 -353 C ATOM 1696 C THR A 383 8.346 54.378 12.174 1.00 22.03 C ANISOU 1696 C THR A 383 2731 3017 2625 461 -279 -378 C ATOM 1697 O THR A 383 8.823 53.256 12.436 1.00 20.17 O ANISOU 1697 O THR A 383 2493 2783 2385 458 -276 -377 O ATOM 1698 CB THR A 383 6.054 54.619 11.204 1.00 22.61 C ANISOU 1698 CB THR A 383 2813 3097 2682 459 -249 -334 C ATOM 1699 OG1 THR A 383 5.690 53.384 11.842 1.00 19.82 O ANISOU 1699 OG1 THR A 383 2466 2762 2301 466 -240 -327 O ATOM 1700 CG2 THR A 383 5.220 54.825 9.936 1.00 18.82 C ANISOU 1700 CG2 THR A 383 2335 2607 2209 444 -232 -309 C ATOM 1701 N SER A 384 8.457 55.417 12.996 1.00 18.83 N ANISOU 1701 N SER A 384 2320 2612 2222 480 -295 -396 N ATOM 1702 CA SER A 384 9.110 55.287 14.291 1.00 19.29 C ANISOU 1702 CA SER A 384 2376 2682 2272 498 -311 -420 C ATOM 1703 C SER A 384 8.358 54.296 15.182 1.00 16.89 C ANISOU 1703 C SER A 384 2077 2401 1939 514 -300 -409 C ATOM 1704 O SER A 384 8.966 53.559 15.958 1.00 21.41 O ANISOU 1704 O SER A 384 2646 2979 2509 521 -304 -416 O ATOM 1705 CB SER A 384 9.265 56.660 14.969 1.00 22.38 C ANISOU 1705 CB SER A 384 2760 3070 2674 517 -329 -441 C ATOM 1706 OG SER A 384 8.151 57.487 14.672 1.00 33.92 O ANISOU 1706 OG SER A 384 4222 4531 4134 525 -323 -429 O ATOM 1707 N ALA A 385 7.040 54.249 15.063 1.00 16.48 N ANISOU 1707 N ALA A 385 2032 2363 1866 520 -285 -390 N ATOM 1708 CA ALA A 385 6.290 53.300 15.874 1.00 17.94 C ANISOU 1708 CA ALA A 385 2220 2571 2025 535 -273 -376 C ATOM 1709 C ALA A 385 6.654 51.879 15.438 1.00 21.99 C ANISOU 1709 C ALA A 385 2734 3078 2543 517 -261 -361 C ATOM 1710 O ALA A 385 6.859 50.990 16.272 1.00 20.15 O ANISOU 1710 O ALA A 385 2499 2856 2301 526 -260 -363 O ATOM 1711 CB ALA A 385 4.784 53.547 15.756 1.00 11.70 C ANISOU 1711 CB ALA A 385 1436 1797 1212 544 -258 -358 C ATOM 1712 N ALA A 386 6.752 51.674 14.128 1.00 17.96 N ANISOU 1712 N ALA A 386 2226 2551 2048 492 -252 -348 N ATOM 1713 CA ALA A 386 7.172 50.377 13.592 1.00 19.35 C ANISOU 1713 CA ALA A 386 2401 2718 2231 475 -243 -337 C ATOM 1714 C ALA A 386 8.607 50.018 13.979 1.00 15.82 C ANISOU 1714 C ALA A 386 1948 2261 1802 473 -259 -359 C ATOM 1715 O ALA A 386 8.883 48.855 14.286 1.00 13.66 O ANISOU 1715 O ALA A 386 1674 1989 1527 473 -257 -356 O ATOM 1716 CB ALA A 386 6.984 50.309 12.060 1.00 14.49 C ANISOU 1716 CB ALA A 386 1790 2088 1630 450 -231 -320 C ATOM 1717 N GLN A 387 9.518 50.995 13.951 1.00 15.52 N ANISOU 1717 N GLN A 387 1903 2211 1782 472 -276 -380 N ATOM 1718 CA GLN A 387 10.900 50.743 14.384 1.00 17.25 C ANISOU 1718 CA GLN A 387 2114 2421 2019 473 -292 -402 C ATOM 1719 C GLN A 387 10.874 50.246 15.827 1.00 20.22 C ANISOU 1719 C GLN A 387 2491 2814 2378 495 -298 -410 C ATOM 1720 O GLN A 387 11.599 49.330 16.198 1.00 22.45 O ANISOU 1720 O GLN A 387 2771 3094 2667 495 -303 -417 O ATOM 1721 CB GLN A 387 11.771 52.002 14.301 1.00 19.44 C ANISOU 1721 CB GLN A 387 2383 2687 2317 471 -309 -424 C ATOM 1722 CG GLN A 387 12.137 52.456 12.904 1.00 23.97 C ANISOU 1722 CG GLN A 387 2953 3241 2912 448 -306 -420 C ATOM 1723 CD GLN A 387 13.243 51.618 12.262 1.00 25.49 C ANISOU 1723 CD GLN A 387 3138 3422 3126 432 -307 -423 C ATOM 1724 OE1 GLN A 387 13.648 50.581 12.796 1.00 26.43 O ANISOU 1724 OE1 GLN A 387 3257 3545 3242 437 -309 -427 O ATOM 1725 NE2 GLN A 387 13.733 52.071 11.105 1.00 18.69 N ANISOU 1725 NE2 GLN A 387 2271 2546 2286 413 -305 -424 N ATOM 1726 N ASN A 388 10.023 50.846 16.643 1.00 22.74 N ANISOU 1726 N ASN A 388 2812 3151 2676 515 -297 -410 N ATOM 1727 CA ASN A 388 9.946 50.427 18.027 1.00 25.04 C ANISOU 1727 CA ASN A 388 3103 3460 2949 538 -302 -418 C ATOM 1728 C ASN A 388 9.446 48.987 18.143 1.00 22.47 C ANISOU 1728 C ASN A 388 2782 3144 2610 536 -286 -399 C ATOM 1729 O ASN A 388 9.982 48.190 18.922 1.00 23.81 O ANISOU 1729 O ASN A 388 2950 3318 2779 544 -292 -407 O ATOM 1730 CB ASN A 388 9.073 51.374 18.843 1.00 32.21 C ANISOU 1730 CB ASN A 388 4012 4390 3837 562 -304 -423 C ATOM 1731 CG ASN A 388 9.411 51.329 20.318 1.00 47.09 C ANISOU 1731 CG ASN A 388 5892 6291 5710 587 -316 -441 C ATOM 1732 OD1 ASN A 388 8.609 50.874 21.136 1.00 52.22 O ANISOU 1732 OD1 ASN A 388 6543 6966 6334 604 -307 -433 O ATOM 1733 ND2 ASN A 388 10.623 51.772 20.665 1.00 50.41 N ANISOU 1733 ND2 ASN A 388 6306 6699 6149 588 -336 -466 N ATOM 1734 N LEU A 389 8.426 48.651 17.360 1.00 13.96 N ANISOU 1734 N LEU A 389 1711 2070 1524 526 -268 -374 N ATOM 1735 CA LEU A 389 7.937 47.292 17.330 1.00 17.56 C ANISOU 1735 CA LEU A 389 2171 2532 1971 522 -253 -355 C ATOM 1736 C LEU A 389 9.096 46.363 16.970 1.00 19.59 C ANISOU 1736 C LEU A 389 2425 2769 2248 508 -261 -364 C ATOM 1737 O LEU A 389 9.292 45.329 17.608 1.00 19.78 O ANISOU 1737 O LEU A 389 2451 2798 2269 514 -263 -366 O ATOM 1738 CB LEU A 389 6.787 47.142 16.326 1.00 18.48 C ANISOU 1738 CB LEU A 389 2292 2649 2079 510 -232 -328 C ATOM 1739 CG LEU A 389 6.065 45.789 16.350 1.00 15.62 C ANISOU 1739 CG LEU A 389 1933 2297 1705 508 -216 -306 C ATOM 1740 CD1 LEU A 389 5.300 45.604 17.661 1.00 12.78 C ANISOU 1740 CD1 LEU A 389 1571 1966 1319 533 -210 -302 C ATOM 1741 CD2 LEU A 389 5.125 45.627 15.147 1.00 15.49 C ANISOU 1741 CD2 LEU A 389 1921 2276 1688 491 -197 -280 C ATOM 1742 N ARG A 390 9.876 46.746 15.960 1.00 22.19 N ANISOU 1742 N ARG A 390 2751 3077 2601 490 -268 -371 N ATOM 1743 CA ARG A 390 10.990 45.915 15.498 1.00 22.65 C ANISOU 1743 CA ARG A 390 2807 3117 2682 476 -276 -381 C ATOM 1744 C ARG A 390 12.071 45.778 16.567 1.00 25.50 C ANISOU 1744 C ARG A 390 3162 3477 3050 489 -296 -406 C ATOM 1745 O ARG A 390 12.558 44.676 16.840 1.00 27.01 O ANISOU 1745 O ARG A 390 3354 3663 3247 490 -301 -411 O ATOM 1746 CB ARG A 390 11.606 46.497 14.221 1.00 14.06 C ANISOU 1746 CB ARG A 390 1713 2011 1617 456 -279 -384 C ATOM 1747 CG ARG A 390 12.795 45.719 13.692 1.00 14.89 C ANISOU 1747 CG ARG A 390 1813 2100 1746 444 -288 -396 C ATOM 1748 CD ARG A 390 13.672 46.595 12.785 1.00 20.26 C ANISOU 1748 CD ARG A 390 2483 2766 2450 430 -295 -407 C ATOM 1749 NE ARG A 390 14.023 47.853 13.445 1.00 24.39 N ANISOU 1749 NE ARG A 390 3001 3290 2975 441 -306 -423 N ATOM 1750 CZ ARG A 390 14.850 47.957 14.485 1.00 24.91 C ANISOU 1750 CZ ARG A 390 3062 3357 3047 455 -323 -444 C ATOM 1751 NH1 ARG A 390 15.434 46.874 14.990 1.00 22.17 N ANISOU 1751 NH1 ARG A 390 2713 3008 2703 459 -330 -453 N ATOM 1752 NH2 ARG A 390 15.096 49.148 15.020 1.00 22.76 N ANISOU 1752 NH2 ARG A 390 2784 3086 2776 464 -333 -459 N ATOM 1753 N GLU A 391 12.451 46.909 17.154 1.00 24.54 N ANISOU 1753 N GLU A 391 3035 3358 2930 500 -307 -422 N ATOM 1754 CA GLU A 391 13.524 46.944 18.141 1.00 21.83 C ANISOU 1754 CA GLU A 391 2686 3013 2596 513 -327 -447 C ATOM 1755 C GLU A 391 13.243 45.943 19.243 1.00 19.79 C ANISOU 1755 C GLU A 391 2431 2768 2320 529 -326 -446 C ATOM 1756 O GLU A 391 14.129 45.182 19.651 1.00 21.76 O ANISOU 1756 O GLU A 391 2678 3008 2581 530 -338 -459 O ATOM 1757 CB GLU A 391 13.680 48.346 18.734 1.00 21.40 C ANISOU 1757 CB GLU A 391 2626 2964 2540 526 -338 -463 C ATOM 1758 CG GLU A 391 15.088 48.640 19.246 1.00 25.58 C ANISOU 1758 CG GLU A 391 3147 3482 3091 530 -359 -490 C ATOM 1759 CD GLU A 391 16.123 48.578 18.134 1.00 34.40 C ANISOU 1759 CD GLU A 391 4255 4577 4238 509 -364 -496 C ATOM 1760 OE1 GLU A 391 16.804 47.535 18.019 1.00 36.31 O ANISOU 1760 OE1 GLU A 391 4495 4809 4491 503 -368 -500 O ATOM 1761 OE2 GLU A 391 16.250 49.562 17.366 1.00 32.26 O ANISOU 1761 OE2 GLU A 391 3980 4298 3979 498 -364 -498 O ATOM 1762 N ARG A 392 11.999 45.916 19.699 1.00 20.68 N ANISOU 1762 N ARG A 392 2550 2902 2406 540 -312 -429 N ATOM 1763 CA ARG A 392 11.625 45.011 20.782 1.00 30.39 C ANISOU 1763 CA ARG A 392 3782 4148 3616 557 -309 -426 C ATOM 1764 C ARG A 392 11.669 43.545 20.354 1.00 25.83 C ANISOU 1764 C ARG A 392 3206 3559 3048 545 -304 -412 C ATOM 1765 O ARG A 392 12.170 42.692 21.091 1.00 21.04 O ANISOU 1765 O ARG A 392 2594 2950 2452 552 -314 -413 O ATOM 1766 CB ARG A 392 10.249 45.366 21.360 1.00 35.64 C ANISOU 1766 CB ARG A 392 4449 4842 4250 573 -293 -411 C ATOM 1767 CG ARG A 392 10.257 46.578 22.284 1.00 50.48 C ANISOU 1767 CG ARG A 392 6323 6738 6119 594 -303 -427 C ATOM 1768 CD ARG A 392 9.038 46.607 23.220 1.00 62.45 C ANISOU 1768 CD ARG A 392 7838 8288 7602 617 -291 -416 C ATOM 1769 NE ARG A 392 7.761 46.718 22.510 1.00 72.39 N ANISOU 1769 NE ARG A 392 9101 9557 8849 612 -271 -390 N ATOM 1770 CZ ARG A 392 6.845 45.752 22.450 1.00 75.30 C ANISOU 1770 CZ ARG A 392 9470 9938 9202 610 -252 -366 C ATOM 1771 NH1 ARG A 392 7.060 44.593 23.063 1.00 77.78 N ANISOU 1771 NH1 ARG A 392 9780 10256 9516 613 -251 -360 N ATOM 1772 NH2 ARG A 392 5.712 45.944 21.782 1.00 70.41 N ANISOU 1772 NH2 ARG A 392 8853 9326 8573 605 -235 -344 N ATOM 1773 N ALA A 393 11.129 43.255 19.173 1.00 20.99 N ANISOU 1773 N ALA A 393 2599 2939 2437 527 -290 -395 N ATOM 1774 CA ALA A 393 11.141 41.894 18.649 1.00 19.37 C ANISOU 1774 CA ALA A 393 2393 2721 2245 515 -286 -380 C ATOM 1775 C ALA A 393 12.581 41.410 18.463 1.00 19.73 C ANISOU 1775 C ALA A 393 2433 2743 2321 507 -307 -400 C ATOM 1776 O ALA A 393 12.912 40.263 18.760 1.00 21.00 O ANISOU 1776 O ALA A 393 2589 2894 2495 509 -315 -396 O ATOM 1777 CB ALA A 393 10.374 41.817 17.329 1.00 15.08 C ANISOU 1777 CB ALA A 393 1857 2173 1699 496 -269 -362 C ATOM 1778 N LEU A 394 13.436 42.296 17.968 1.00 17.61 N ANISOU 1778 N LEU A 394 2163 2464 2066 500 -317 -422 N ATOM 1779 CA LEU A 394 14.833 41.939 17.775 1.00 20.71 C ANISOU 1779 CA LEU A 394 2547 2835 2486 494 -336 -442 C ATOM 1780 C LEU A 394 15.456 41.615 19.121 1.00 22.66 C ANISOU 1780 C LEU A 394 2787 3084 2740 512 -353 -453 C ATOM 1781 O LEU A 394 16.219 40.650 19.244 1.00 21.64 O ANISOU 1781 O LEU A 394 2651 2939 2631 512 -367 -457 O ATOM 1782 CB LEU A 394 15.599 43.081 17.108 1.00 16.18 C ANISOU 1782 CB LEU A 394 1966 2253 1927 485 -342 -458 C ATOM 1783 CG LEU A 394 17.114 42.890 17.059 1.00 16.76 C ANISOU 1783 CG LEU A 394 2028 2308 2030 482 -363 -483 C ATOM 1784 CD1 LEU A 394 17.475 41.664 16.229 1.00 11.75 C ANISOU 1784 CD1 LEU A 394 1393 1659 1413 470 -365 -482 C ATOM 1785 CD2 LEU A 394 17.795 44.148 16.517 1.00 16.37 C ANISOU 1785 CD2 LEU A 394 1968 2254 1997 475 -367 -494 C ATOM 1786 N GLN A 395 15.113 42.417 20.132 1.00 21.32 N ANISOU 1786 N GLN A 395 2619 2932 2551 529 -352 -457 N ATOM 1787 CA GLN A 395 15.704 42.260 21.457 1.00 26.78 C ANISOU 1787 CA GLN A 395 3303 3627 3246 547 -369 -467 C ATOM 1788 C GLN A 395 15.287 40.959 22.124 1.00 26.07 C ANISOU 1788 C GLN A 395 3210 3541 3155 554 -369 -445 C ATOM 1789 O GLN A 395 16.088 40.336 22.827 1.00 27.93 O ANISOU 1789 O GLN A 395 3437 3768 3408 560 -389 -451 O ATOM 1790 CB GLN A 395 15.368 43.430 22.377 1.00 38.11 C ANISOU 1790 CB GLN A 395 4739 5083 4660 565 -368 -476 C ATOM 1791 CG GLN A 395 15.847 43.193 23.797 1.00 53.63 C ANISOU 1791 CG GLN A 395 6696 7056 6626 585 -384 -483 C ATOM 1792 CD GLN A 395 15.569 44.362 24.708 1.00 71.22 C ANISOU 1792 CD GLN A 395 8922 9304 8832 604 -385 -496 C ATOM 1793 OE1 GLN A 395 14.697 45.193 24.429 1.00 76.22 O ANISOU 1793 OE1 GLN A 395 9562 9952 9445 606 -372 -494 O ATOM 1794 NE2 GLN A 395 16.311 44.439 25.811 1.00 75.07 N ANISOU 1794 NE2 GLN A 395 9403 9795 9327 619 -403 -510 N ATOM 1795 N ARG A 396 14.037 40.554 21.907 1.00 17.82 N ANISOU 1795 N ARG A 396 2170 2509 2091 552 -350 -420 N ATOM 1796 CA ARG A 396 13.558 39.287 22.436 1.00 23.26 C ANISOU 1796 CA ARG A 396 2855 3203 2780 555 -351 -395 C ATOM 1797 C ARG A 396 14.241 38.093 21.773 1.00 28.40 C ANISOU 1797 C ARG A 396 3504 3826 3462 541 -364 -393 C ATOM 1798 O ARG A 396 14.656 37.155 22.459 1.00 28.11 O ANISOU 1798 O ARG A 396 3459 3781 3439 545 -382 -386 O ATOM 1799 CB ARG A 396 12.044 39.183 22.304 1.00 25.46 C ANISOU 1799 CB ARG A 396 3138 3503 3032 556 -326 -368 C ATOM 1800 CG ARG A 396 11.330 40.300 23.057 1.00 34.78 C ANISOU 1800 CG ARG A 396 4318 4713 4182 573 -315 -370 C ATOM 1801 CD ARG A 396 9.885 39.962 23.327 1.00 32.67 C ANISOU 1801 CD ARG A 396 4050 4472 3891 579 -294 -340 C ATOM 1802 NE ARG A 396 9.157 39.697 22.091 1.00 37.39 N ANISOU 1802 NE ARG A 396 4655 5063 4488 562 -276 -324 N ATOM 1803 CZ ARG A 396 8.722 40.644 21.266 1.00 34.28 C ANISOU 1803 CZ ARG A 396 4270 4671 4083 556 -263 -329 C ATOM 1804 NH1 ARG A 396 8.963 41.922 21.541 1.00 32.09 N ANISOU 1804 NH1 ARG A 396 3996 4401 3797 566 -267 -351 N ATOM 1805 NH2 ARG A 396 8.055 40.312 20.165 1.00 25.15 N ANISOU 1805 NH2 ARG A 396 3120 3508 2928 540 -247 -312 N ATOM 1806 N LEU A 397 14.366 38.124 20.448 1.00 22.08 N ANISOU 1806 N LEU A 397 2708 3010 2671 524 -357 -398 N ATOM 1807 CA LEU A 397 15.010 37.015 19.740 1.00 19.42 C ANISOU 1807 CA LEU A 397 2367 2648 2362 512 -370 -400 C ATOM 1808 C LEU A 397 16.499 36.917 20.078 1.00 24.89 C ANISOU 1808 C LEU A 397 3051 3322 3083 516 -397 -425 C ATOM 1809 O LEU A 397 17.043 35.815 20.147 1.00 26.95 O ANISOU 1809 O LEU A 397 3306 3566 3369 515 -416 -423 O ATOM 1810 CB LEU A 397 14.810 37.129 18.228 1.00 12.64 C ANISOU 1810 CB LEU A 397 1516 1781 1507 494 -356 -401 C ATOM 1811 CG LEU A 397 15.542 36.136 17.313 1.00 18.21 C ANISOU 1811 CG LEU A 397 2217 2462 2242 483 -369 -408 C ATOM 1812 CD1 LEU A 397 15.222 34.671 17.649 1.00 19.59 C ANISOU 1812 CD1 LEU A 397 2388 2627 2428 485 -379 -388 C ATOM 1813 CD2 LEU A 397 15.237 36.434 15.840 1.00 17.38 C ANISOU 1813 CD2 LEU A 397 2116 2354 2133 465 -353 -407 C ATOM 1814 N MET A 398 17.151 38.063 20.288 1.00 23.56 N ANISOU 1814 N MET A 398 2881 3158 2913 521 -400 -448 N ATOM 1815 CA MET A 398 18.588 38.090 20.572 1.00 21.95 C ANISOU 1815 CA MET A 398 2665 2937 2736 525 -425 -473 C ATOM 1816 C MET A 398 18.869 37.590 21.989 1.00 22.07 C ANISOU 1816 C MET A 398 2674 2955 2756 541 -444 -468 C ATOM 1817 O MET A 398 19.873 36.917 22.243 1.00 13.54 O ANISOU 1817 O MET A 398 1584 1857 1704 542 -468 -477 O ATOM 1818 CB MET A 398 19.163 39.497 20.390 1.00 19.49 C ANISOU 1818 CB MET A 398 2354 2630 2423 524 -424 -497 C ATOM 1819 CG MET A 398 19.280 39.984 18.942 1.00 17.16 C ANISOU 1819 CG MET A 398 2060 2328 2133 506 -413 -504 C ATOM 1820 SD MET A 398 20.467 39.060 17.931 1.00 25.18 S ANISOU 1820 SD MET A 398 3063 3318 3187 494 -429 -519 S ATOM 1821 CE MET A 398 19.369 38.021 16.975 1.00 9.99 C ANISOU 1821 CE MET A 398 1149 1393 1255 482 -413 -494 C ATOM 1822 N THR A 399 17.972 37.916 22.910 1.00 19.40 N ANISOU 1822 N THR A 399 2339 2640 2390 552 -434 -452 N ATOM 1823 CA THR A 399 18.089 37.426 24.273 1.00 22.75 C ANISOU 1823 CA THR A 399 2757 3072 2815 566 -452 -442 C ATOM 1824 C THR A 399 18.158 35.905 24.238 1.00 24.24 C ANISOU 1824 C THR A 399 2941 3244 3025 559 -468 -423 C ATOM 1825 O THR A 399 18.993 35.288 24.899 1.00 21.25 O ANISOU 1825 O THR A 399 2554 2853 2668 563 -495 -425 O ATOM 1826 CB THR A 399 16.893 37.877 25.135 1.00 24.09 C ANISOU 1826 CB THR A 399 2930 3275 2949 578 -435 -424 C ATOM 1827 OG1 THR A 399 16.900 39.307 25.241 1.00 27.04 O ANISOU 1827 OG1 THR A 399 3306 3661 3306 586 -426 -444 O ATOM 1828 CG2 THR A 399 16.957 37.260 26.534 1.00 24.06 C ANISOU 1828 CG2 THR A 399 2916 3281 2944 589 -455 -408 C ATOM 1829 N SER A 400 17.284 35.308 23.442 1.00 21.47 N ANISOU 1829 N SER A 400 2597 2892 2668 549 -452 -404 N ATOM 1830 CA SER A 400 17.211 33.860 23.344 1.00 26.65 C ANISOU 1830 CA SER A 400 3250 3532 3344 542 -467 -385 C ATOM 1831 C SER A 400 18.438 33.267 22.636 1.00 29.80 C ANISOU 1831 C SER A 400 3642 3898 3780 535 -490 -406 C ATOM 1832 O SER A 400 18.971 32.229 23.054 1.00 23.81 O ANISOU 1832 O SER A 400 2877 3123 3048 536 -518 -400 O ATOM 1833 CB SER A 400 15.926 33.452 22.627 1.00 26.19 C ANISOU 1833 CB SER A 400 3199 3481 3270 532 -444 -360 C ATOM 1834 OG SER A 400 15.749 32.056 22.688 1.00 26.42 O ANISOU 1834 OG SER A 400 3225 3497 3317 526 -461 -338 O ATOM 1835 N VAL A 401 18.877 33.917 21.561 1.00 26.13 N ANISOU 1835 N VAL A 401 3180 3427 3321 528 -478 -430 N ATOM 1836 CA VAL A 401 20.070 33.474 20.858 1.00 22.23 C ANISOU 1836 CA VAL A 401 2678 2907 2862 523 -498 -453 C ATOM 1837 C VAL A 401 21.298 33.554 21.767 1.00 20.58 C ANISOU 1837 C VAL A 401 2457 2690 2675 534 -526 -470 C ATOM 1838 O VAL A 401 22.156 32.661 21.758 1.00 20.20 O ANISOU 1838 O VAL A 401 2397 2618 2658 535 -553 -477 O ATOM 1839 CB VAL A 401 20.306 34.281 19.577 1.00 21.67 C ANISOU 1839 CB VAL A 401 2609 2836 2789 512 -480 -473 C ATOM 1840 CG1 VAL A 401 21.729 34.065 19.071 1.00 17.07 C ANISOU 1840 CG1 VAL A 401 2013 2233 2242 511 -502 -502 C ATOM 1841 CG2 VAL A 401 19.275 33.886 18.517 1.00 16.76 C ANISOU 1841 CG2 VAL A 401 1996 2216 2155 500 -460 -456 C ATOM 1842 N THR A 402 21.362 34.615 22.564 1.00 19.87 N ANISOU 1842 N THR A 402 2367 2616 2566 543 -521 -476 N ATOM 1843 CA THR A 402 22.468 34.809 23.498 1.00 25.04 C ANISOU 1843 CA THR A 402 3010 3264 3238 553 -546 -491 C ATOM 1844 C THR A 402 22.501 33.759 24.614 1.00 28.65 C ANISOU 1844 C THR A 402 3462 3717 3706 560 -573 -470 C ATOM 1845 O THR A 402 23.573 33.287 24.985 1.00 35.94 O ANISOU 1845 O THR A 402 4374 4623 4659 564 -603 -480 O ATOM 1846 CB THR A 402 22.450 36.213 24.125 1.00 26.63 C ANISOU 1846 CB THR A 402 3214 3487 3417 562 -535 -503 C ATOM 1847 OG1 THR A 402 22.516 37.199 23.091 1.00 20.53 O ANISOU 1847 OG1 THR A 402 2446 2716 2638 554 -516 -521 O ATOM 1848 CG2 THR A 402 23.652 36.385 25.043 1.00 35.93 C ANISOU 1848 CG2 THR A 402 4380 4657 4615 572 -563 -519 C ATOM 1849 N ASN A 403 21.340 33.393 25.150 1.00 27.23 N ANISOU 1849 N ASN A 403 3289 3554 3502 561 -564 -439 N ATOM 1850 CA ASN A 403 21.288 32.353 26.181 1.00 34.69 C ANISOU 1850 CA ASN A 403 4229 4497 4455 563 -592 -414 C ATOM 1851 C ASN A 403 21.811 31.003 25.693 1.00 35.70 C ANISOU 1851 C ASN A 403 4350 4593 4620 556 -618 -410 C ATOM 1852 O ASN A 403 22.334 30.209 26.476 1.00 39.17 O ANISOU 1852 O ASN A 403 4782 5020 5080 558 -653 -400 O ATOM 1853 CB ASN A 403 19.867 32.177 26.718 1.00 36.68 C ANISOU 1853 CB ASN A 403 4487 4776 4675 563 -576 -379 C ATOM 1854 CG ASN A 403 19.375 33.393 27.463 1.00 43.45 C ANISOU 1854 CG ASN A 403 5347 5666 5497 574 -557 -381 C ATOM 1855 OD1 ASN A 403 20.148 34.306 27.770 1.00 47.89 O ANISOU 1855 OD1 ASN A 403 5906 6230 6061 582 -561 -406 O ATOM 1856 ND2 ASN A 403 18.081 33.421 27.755 1.00 41.73 N ANISOU 1856 ND2 ASN A 403 5133 5474 5247 574 -537 -355 N ATOM 1857 N ARG A 404 21.655 30.739 24.402 1.00 34.77 N ANISOU 1857 N ARG A 404 4237 4462 4511 548 -604 -419 N ATOM 1858 CA ARG A 404 22.087 29.467 23.840 1.00 36.95 C ANISOU 1858 CA ARG A 404 4507 4709 4822 542 -629 -419 C ATOM 1859 C ARG A 404 23.304 29.643 22.938 1.00 31.41 C ANISOU 1859 C ARG A 404 3796 3987 4150 543 -636 -456 C ATOM 1860 O ARG A 404 23.615 28.774 22.123 1.00 31.96 O ANISOU 1860 O ARG A 404 3862 4036 4247 538 -649 -464 O ATOM 1861 CB ARG A 404 20.941 28.788 23.085 1.00 44.45 C ANISOU 1861 CB ARG A 404 5467 5659 5762 532 -613 -397 C ATOM 1862 CG ARG A 404 19.919 28.099 23.986 1.00 56.80 C ANISOU 1862 CG ARG A 404 7034 7235 7311 529 -619 -356 C ATOM 1863 CD ARG A 404 19.296 26.892 23.287 1.00 66.28 C ANISOU 1863 CD ARG A 404 8239 8419 8525 519 -625 -337 C ATOM 1864 NE ARG A 404 18.464 26.083 24.181 1.00 74.46 N ANISOU 1864 NE ARG A 404 9275 9463 9553 514 -639 -296 N ATOM 1865 CZ ARG A 404 18.342 24.759 24.098 1.00 80.18 C ANISOU 1865 CZ ARG A 404 9997 10165 10302 507 -667 -276 C ATOM 1866 NH1 ARG A 404 19.003 24.084 23.170 1.00 81.45 N ANISOU 1866 NH1 ARG A 404 10156 10295 10498 506 -684 -297 N ATOM 1867 NH2 ARG A 404 17.562 24.103 24.947 1.00 83.05 N ANISOU 1867 NH2 ARG A 404 10361 10539 10656 500 -681 -236 N ATOM 1868 N CYS A 405 23.989 30.772 23.103 1.00 30.65 N ANISOU 1868 N CYS A 405 3697 3901 4050 548 -629 -480 N ATOM 1869 CA CYS A 405 25.133 31.144 22.265 1.00 36.65 C ANISOU 1869 CA CYS A 405 4445 4647 4832 547 -633 -515 C ATOM 1870 C CYS A 405 26.140 29.982 22.061 1.00 23.84 C ANISOU 1870 C CYS A 405 2808 2996 3256 550 -668 -527 C ATOM 1871 O CYS A 405 26.589 29.714 20.938 1.00 23.72 O ANISOU 1871 O CYS A 405 2785 2968 3260 546 -667 -547 O ATOM 1872 CB CYS A 405 25.814 32.424 22.833 1.00 12.41 C ANISOU 1872 CB CYS A 405 1370 1589 1755 554 -630 -534 C ATOM 1873 SG CYS A 405 27.424 32.820 22.118 1.00123.59 S ANISOU 1873 SG CYS A 405 15432 15655 15871 554 -642 -575 S ATOM 1874 N GLN A 406 26.473 29.288 23.146 1.00 24.49 N ANISOU 1874 N GLN A 406 2883 3067 3354 557 -701 -513 N ATOM 1875 CA GLN A 406 27.494 28.246 23.125 1.00 30.36 C ANISOU 1875 CA GLN A 406 3610 3781 4143 562 -740 -525 C ATOM 1876 C GLN A 406 27.077 27.103 22.203 1.00 32.11 C ANISOU 1876 C GLN A 406 3834 3986 4382 556 -745 -519 C ATOM 1877 O GLN A 406 27.847 26.641 21.355 1.00 29.52 O ANISOU 1877 O GLN A 406 3492 3639 4085 558 -757 -545 O ATOM 1878 CB GLN A 406 27.724 27.719 24.546 1.00 41.46 C ANISOU 1878 CB GLN A 406 5012 5181 5559 567 -775 -503 C ATOM 1879 CG GLN A 406 29.154 27.284 24.844 1.00 56.12 C ANISOU 1879 CG GLN A 406 6849 7014 7461 576 -815 -523 C ATOM 1880 CD GLN A 406 29.531 25.980 24.167 1.00 67.44 C ANISOU 1880 CD GLN A 406 8272 8417 8934 576 -842 -530 C ATOM 1881 OE1 GLN A 406 28.670 25.162 23.840 1.00 73.34 O ANISOU 1881 OE1 GLN A 406 9029 9158 9678 570 -842 -510 O ATOM 1882 NE2 GLN A 406 30.828 25.776 23.960 1.00 69.55 N ANISOU 1882 NE2 GLN A 406 8519 8666 9243 584 -867 -559 N ATOM 1883 N GLU A 407 25.844 26.652 22.372 1.00 30.87 N ANISOU 1883 N GLU A 407 3692 3836 4203 549 -736 -487 N ATOM 1884 CA GLU A 407 25.335 25.535 21.600 1.00 27.40 C ANISOU 1884 CA GLU A 407 3255 3380 3777 544 -742 -478 C ATOM 1885 C GLU A 407 25.263 25.918 20.119 1.00 27.19 C ANISOU 1885 C GLU A 407 3229 3357 3745 538 -713 -501 C ATOM 1886 O GLU A 407 25.655 25.149 19.243 1.00 31.06 O ANISOU 1886 O GLU A 407 3711 3828 4263 538 -727 -517 O ATOM 1887 CB GLU A 407 23.966 25.125 22.143 1.00 32.30 C ANISOU 1887 CB GLU A 407 3890 4011 4370 537 -735 -435 C ATOM 1888 CG GLU A 407 23.303 23.978 21.409 1.00 45.89 C ANISOU 1888 CG GLU A 407 5616 5717 6104 529 -742 -421 C ATOM 1889 CD GLU A 407 21.945 23.624 21.994 1.00 57.26 C ANISOU 1889 CD GLU A 407 7069 7170 7517 521 -734 -377 C ATOM 1890 OE1 GLU A 407 21.637 24.080 23.121 1.00 58.68 O ANISOU 1890 OE1 GLU A 407 7252 7371 7675 522 -732 -357 O ATOM 1891 OE2 GLU A 407 21.189 22.891 21.323 1.00 61.54 O ANISOU 1891 OE2 GLU A 407 7617 7705 8060 513 -730 -363 O ATOM 1892 N LEU A 408 24.794 27.128 19.843 1.00 22.51 N ANISOU 1892 N LEU A 408 2645 2789 3116 533 -676 -504 N ATOM 1893 CA LEU A 408 24.618 27.568 18.465 1.00 20.58 C ANISOU 1893 CA LEU A 408 2404 2553 2863 525 -648 -521 C ATOM 1894 C LEU A 408 25.954 27.778 17.736 1.00 23.54 C ANISOU 1894 C LEU A 408 2761 2918 3267 528 -658 -560 C ATOM 1895 O LEU A 408 26.107 27.360 16.582 1.00 20.96 O ANISOU 1895 O LEU A 408 2427 2583 2953 524 -656 -575 O ATOM 1896 CB LEU A 408 23.748 28.820 18.421 1.00 16.61 C ANISOU 1896 CB LEU A 408 1916 2078 2316 518 -609 -510 C ATOM 1897 CG LEU A 408 22.370 28.611 19.062 1.00 20.60 C ANISOU 1897 CG LEU A 408 2438 2597 2793 515 -596 -472 C ATOM 1898 CD1 LEU A 408 21.533 29.884 19.048 1.00 21.00 C ANISOU 1898 CD1 LEU A 408 2501 2677 2802 511 -559 -465 C ATOM 1899 CD2 LEU A 408 21.631 27.476 18.367 1.00 21.99 C ANISOU 1899 CD2 LEU A 408 2618 2761 2975 508 -599 -456 C ATOM 1900 N ALA A 409 26.912 28.410 18.416 1.00 19.17 N ANISOU 1900 N ALA A 409 2196 2365 2723 535 -668 -576 N ATOM 1901 CA ALA A 409 28.257 28.627 17.858 1.00 20.65 C ANISOU 1901 CA ALA A 409 2361 2544 2939 539 -679 -612 C ATOM 1902 C ALA A 409 28.946 27.352 17.380 1.00 21.19 C ANISOU 1902 C ALA A 409 2412 2587 3051 546 -710 -628 C ATOM 1903 O ALA A 409 29.604 27.366 16.345 1.00 22.34 O ANISOU 1903 O ALA A 409 2543 2732 3214 545 -708 -656 O ATOM 1904 CB ALA A 409 29.146 29.335 18.864 1.00 19.12 C ANISOU 1904 CB ALA A 409 2159 2354 2753 548 -692 -623 C ATOM 1905 N THR A 410 28.803 26.262 18.136 1.00 20.85 N ANISOU 1905 N THR A 410 2370 2525 3026 552 -741 -610 N ATOM 1906 CA THR A 410 29.473 24.998 17.811 1.00 24.07 C ANISOU 1906 CA THR A 410 2761 2906 3479 560 -776 -625 C ATOM 1907 C THR A 410 28.670 24.109 16.856 1.00 24.57 C ANISOU 1907 C THR A 410 2831 2960 3542 554 -772 -618 C ATOM 1908 O THR A 410 29.184 23.104 16.360 1.00 24.37 O ANISOU 1908 O THR A 410 2791 2914 3555 561 -799 -635 O ATOM 1909 CB THR A 410 29.765 24.173 19.079 1.00 25.90 C ANISOU 1909 CB THR A 410 2989 3116 3735 569 -818 -608 C ATOM 1910 OG1 THR A 410 28.564 24.053 19.848 1.00 31.83 O ANISOU 1910 OG1 THR A 410 3763 3876 4457 563 -811 -567 O ATOM 1911 CG2 THR A 410 30.827 24.841 19.927 1.00 22.89 C ANISOU 1911 CG2 THR A 410 2595 2738 3366 577 -831 -621 C ATOM 1912 N ASN A 411 27.411 24.472 16.619 1.00 22.21 N ANISOU 1912 N ASN A 411 2555 2680 3205 543 -740 -593 N ATOM 1913 CA ASN A 411 26.540 23.697 15.740 1.00 21.67 C ANISOU 1913 CA ASN A 411 2495 2606 3133 536 -734 -582 C ATOM 1914 C ASN A 411 26.876 23.819 14.257 1.00 18.59 C ANISOU 1914 C ASN A 411 2094 2220 2749 532 -719 -612 C ATOM 1915 O ASN A 411 27.177 24.901 13.771 1.00 18.52 O ANISOU 1915 O ASN A 411 2082 2231 2724 527 -694 -628 O ATOM 1916 CB ASN A 411 25.079 24.086 15.941 1.00 20.29 C ANISOU 1916 CB ASN A 411 2345 2450 2914 524 -703 -546 C ATOM 1917 CG ASN A 411 24.150 23.255 15.086 1.00 23.08 C ANISOU 1917 CG ASN A 411 2708 2797 3265 517 -698 -532 C ATOM 1918 OD1 ASN A 411 23.656 23.717 14.059 1.00 21.49 O ANISOU 1918 OD1 ASN A 411 2512 2610 3042 507 -668 -536 O ATOM 1919 ND2 ASN A 411 23.942 21.996 15.487 1.00 21.93 N ANISOU 1919 ND2 ASN A 411 2562 2628 3144 520 -731 -516 N ATOM 1920 N GLU A 412 26.779 22.704 13.543 1.00 17.48 N ANISOU 1920 N GLU A 412 1949 2061 2632 535 -737 -618 N ATOM 1921 CA GLU A 412 27.070 22.648 12.111 1.00 18.86 C ANISOU 1921 CA GLU A 412 2111 2240 2815 533 -726 -647 C ATOM 1922 C GLU A 412 26.249 23.621 11.244 1.00 20.73 C ANISOU 1922 C GLU A 412 2362 2504 3009 517 -682 -638 C ATOM 1923 O GLU A 412 26.643 23.933 10.117 1.00 21.93 O ANISOU 1923 O GLU A 412 2503 2667 3163 513 -669 -662 O ATOM 1924 CB GLU A 412 26.820 21.228 11.605 1.00 22.97 C ANISOU 1924 CB GLU A 412 2629 2737 3363 538 -752 -648 C ATOM 1925 CG GLU A 412 25.353 20.943 11.369 1.00 25.40 C ANISOU 1925 CG GLU A 412 2961 3048 3642 525 -734 -613 C ATOM 1926 CD GLU A 412 25.062 19.479 11.089 1.00 29.32 C ANISOU 1926 CD GLU A 412 3455 3516 4167 530 -766 -609 C ATOM 1927 OE1 GLU A 412 25.696 18.914 10.166 1.00 22.84 O ANISOU 1927 OE1 GLU A 412 2617 2686 3376 538 -781 -641 O ATOM 1928 OE2 GLU A 412 24.184 18.912 11.787 1.00 27.39 O ANISOU 1928 OE2 GLU A 412 3228 3262 3917 526 -775 -573 O ATOM 1929 N TYR A 413 25.100 24.074 11.747 1.00 17.47 N ANISOU 1929 N TYR A 413 1974 2104 2559 507 -659 -603 N ATOM 1930 CA TYR A 413 24.244 24.978 10.972 1.00 20.58 C ANISOU 1930 CA TYR A 413 2382 2523 2914 492 -619 -592 C ATOM 1931 C TYR A 413 24.087 26.345 11.626 1.00 22.99 C ANISOU 1931 C TYR A 413 2697 2850 3188 487 -595 -582 C ATOM 1932 O TYR A 413 24.198 27.377 10.969 1.00 23.01 O ANISOU 1932 O TYR A 413 2698 2870 3173 479 -571 -591 O ATOM 1933 CB TYR A 413 22.861 24.351 10.713 1.00 20.13 C ANISOU 1933 CB TYR A 413 2345 2465 2840 484 -609 -560 C ATOM 1934 CG TYR A 413 22.899 23.201 9.728 1.00 18.84 C ANISOU 1934 CG TYR A 413 2173 2284 2702 486 -625 -572 C ATOM 1935 CD1 TYR A 413 23.437 23.369 8.457 1.00 14.24 C ANISOU 1935 CD1 TYR A 413 1577 1709 2127 483 -618 -601 C ATOM 1936 CD2 TYR A 413 22.393 21.950 10.065 1.00 24.74 C ANISOU 1936 CD2 TYR A 413 2926 3010 3466 490 -650 -555 C ATOM 1937 CE1 TYR A 413 23.487 22.315 7.551 1.00 16.77 C ANISOU 1937 CE1 TYR A 413 1888 2014 2470 487 -634 -615 C ATOM 1938 CE2 TYR A 413 22.430 20.888 9.162 1.00 22.65 C ANISOU 1938 CE2 TYR A 413 2653 2727 3226 493 -668 -568 C ATOM 1939 CZ TYR A 413 22.976 21.078 7.904 1.00 25.05 C ANISOU 1939 CZ TYR A 413 2942 3038 3536 492 -659 -599 C ATOM 1940 OH TYR A 413 23.021 20.028 6.999 1.00 30.45 O ANISOU 1940 OH TYR A 413 3618 3707 4245 497 -678 -615 O ATOM 1941 N ALA A 414 23.838 26.347 12.928 1.00 23.72 N ANISOU 1941 N ALA A 414 2797 2940 3274 493 -603 -562 N ATOM 1942 CA ALA A 414 23.567 27.590 13.639 1.00 19.94 C ANISOU 1942 CA ALA A 414 2329 2483 2765 490 -582 -551 C ATOM 1943 C ALA A 414 24.805 28.485 13.737 1.00 20.46 C ANISOU 1943 C ALA A 414 2379 2553 2842 494 -586 -580 C ATOM 1944 O ALA A 414 24.698 29.675 14.035 1.00 17.56 O ANISOU 1944 O ALA A 414 2018 2204 2450 491 -566 -578 O ATOM 1945 CB ALA A 414 23.006 27.287 15.013 1.00 15.51 C ANISOU 1945 CB ALA A 414 1778 1920 2196 496 -592 -523 C ATOM 1946 N ASN A 415 25.985 27.935 13.471 1.00 17.99 N ANISOU 1946 N ASN A 415 2045 2224 2566 502 -611 -609 N ATOM 1947 CA ASN A 415 27.174 28.769 13.556 1.00 16.79 C ANISOU 1947 CA ASN A 415 1876 2077 2427 506 -614 -636 C ATOM 1948 C ASN A 415 27.097 29.921 12.550 1.00 16.04 C ANISOU 1948 C ASN A 415 1782 2003 2310 493 -583 -645 C ATOM 1949 O ASN A 415 27.684 30.977 12.755 1.00 15.49 O ANISOU 1949 O ASN A 415 1706 1944 2236 492 -577 -657 O ATOM 1950 CB ASN A 415 28.454 27.955 13.349 1.00 20.91 C ANISOU 1950 CB ASN A 415 2371 2579 2994 518 -646 -667 C ATOM 1951 CG ASN A 415 28.726 27.658 11.886 1.00 22.98 C ANISOU 1951 CG ASN A 415 2620 2843 3269 513 -640 -689 C ATOM 1952 OD1 ASN A 415 29.174 28.532 11.142 1.00 19.70 O ANISOU 1952 OD1 ASN A 415 2194 2443 2848 506 -622 -706 O ATOM 1953 ND2 ASN A 415 28.449 26.420 11.463 1.00 18.17 N ANISOU 1953 ND2 ASN A 415 2009 2218 2679 517 -656 -688 N ATOM 1954 N TYR A 416 26.364 29.725 11.461 1.00 15.94 N ANISOU 1954 N TYR A 416 1777 1996 2284 482 -566 -637 N ATOM 1955 CA TYR A 416 26.254 30.781 10.471 1.00 18.81 C ANISOU 1955 CA TYR A 416 2140 2379 2628 468 -539 -642 C ATOM 1956 C TYR A 416 25.457 31.954 11.052 1.00 20.43 C ANISOU 1956 C TYR A 416 2365 2601 2797 462 -517 -620 C ATOM 1957 O TYR A 416 25.696 33.108 10.717 1.00 20.69 O ANISOU 1957 O TYR A 416 2395 2647 2819 454 -502 -626 O ATOM 1958 CB TYR A 416 25.625 30.260 9.169 1.00 18.21 C ANISOU 1958 CB TYR A 416 2067 2305 2547 459 -527 -638 C ATOM 1959 CG TYR A 416 26.536 29.346 8.359 1.00 14.68 C ANISOU 1959 CG TYR A 416 1596 1847 2136 465 -546 -667 C ATOM 1960 CD1 TYR A 416 27.527 29.867 7.542 1.00 19.74 C ANISOU 1960 CD1 TYR A 416 2214 2497 2791 462 -543 -696 C ATOM 1961 CD2 TYR A 416 26.391 27.963 8.409 1.00 17.02 C ANISOU 1961 CD2 TYR A 416 1890 2123 2453 474 -568 -667 C ATOM 1962 CE1 TYR A 416 28.370 29.028 6.797 1.00 26.02 C ANISOU 1962 CE1 TYR A 416 2983 3283 3619 470 -560 -726 C ATOM 1963 CE2 TYR A 416 27.213 27.119 7.668 1.00 24.88 C ANISOU 1963 CE2 TYR A 416 2862 3108 3482 482 -587 -697 C ATOM 1964 CZ TYR A 416 28.204 27.656 6.861 1.00 28.79 C ANISOU 1964 CZ TYR A 416 3334 3616 3991 481 -582 -727 C ATOM 1965 OH TYR A 416 29.028 26.814 6.128 1.00 32.86 O ANISOU 1965 OH TYR A 416 3822 4123 4541 490 -600 -759 O ATOM 1966 N ILE A 417 24.517 31.646 11.934 1.00 17.98 N ANISOU 1966 N ILE A 417 2073 2289 2469 466 -515 -593 N ATOM 1967 CA ILE A 417 23.720 32.679 12.567 1.00 17.44 C ANISOU 1967 CA ILE A 417 2021 2237 2367 462 -496 -574 C ATOM 1968 C ILE A 417 24.594 33.523 13.492 1.00 17.36 C ANISOU 1968 C ILE A 417 2003 2230 2362 471 -505 -589 C ATOM 1969 O ILE A 417 24.599 34.766 13.418 1.00 16.49 O ANISOU 1969 O ILE A 417 1896 2134 2236 465 -490 -592 O ATOM 1970 CB ILE A 417 22.541 32.068 13.339 1.00 18.74 C ANISOU 1970 CB ILE A 417 2204 2403 2515 466 -493 -543 C ATOM 1971 CG1 ILE A 417 21.601 31.364 12.359 1.00 18.37 C ANISOU 1971 CG1 ILE A 417 2165 2354 2460 456 -480 -527 C ATOM 1972 CG2 ILE A 417 21.791 33.147 14.126 1.00 16.83 C ANISOU 1972 CG2 ILE A 417 1976 2180 2240 467 -474 -526 C ATOM 1973 CD1 ILE A 417 20.560 30.531 13.024 1.00 25.52 C ANISOU 1973 CD1 ILE A 417 3083 3256 3356 460 -481 -498 C ATOM 1974 N ILE A 418 25.355 32.850 14.344 1.00 12.51 N ANISOU 1974 N ILE A 418 1378 1601 1773 484 -531 -598 N ATOM 1975 CA ILE A 418 26.235 33.560 15.253 1.00 20.22 C ANISOU 1975 CA ILE A 418 2346 2579 2758 493 -543 -612 C ATOM 1976 C ILE A 418 27.223 34.408 14.455 1.00 20.84 C ANISOU 1976 C ILE A 418 2408 2661 2848 486 -539 -639 C ATOM 1977 O ILE A 418 27.539 35.532 14.841 1.00 20.55 O ANISOU 1977 O ILE A 418 2370 2633 2804 486 -533 -645 O ATOM 1978 CB ILE A 418 26.977 32.586 16.172 1.00 21.86 C ANISOU 1978 CB ILE A 418 2543 2767 2996 507 -575 -618 C ATOM 1979 CG1 ILE A 418 25.964 31.686 16.896 1.00 23.06 C ANISOU 1979 CG1 ILE A 418 2709 2915 3137 511 -581 -588 C ATOM 1980 CG2 ILE A 418 27.881 33.344 17.156 1.00 13.08 C ANISOU 1980 CG2 ILE A 418 1422 1657 1892 516 -588 -631 C ATOM 1981 CD1 ILE A 418 24.935 32.451 17.704 1.00 21.07 C ANISOU 1981 CD1 ILE A 418 2476 2683 2848 511 -561 -564 C ATOM 1982 N GLN A 419 27.704 33.866 13.338 1.00 16.40 N ANISOU 1982 N GLN A 419 1831 2092 2306 482 -542 -655 N ATOM 1983 CA GLN A 419 28.618 34.608 12.477 1.00 18.36 C ANISOU 1983 CA GLN A 419 2062 2348 2568 475 -536 -679 C ATOM 1984 C GLN A 419 27.920 35.829 11.909 1.00 20.60 C ANISOU 1984 C GLN A 419 2357 2648 2820 460 -508 -667 C ATOM 1985 O GLN A 419 28.517 36.912 11.813 1.00 16.11 O ANISOU 1985 O GLN A 419 1780 2087 2254 456 -503 -679 O ATOM 1986 CB GLN A 419 29.115 33.740 11.328 1.00 13.56 C ANISOU 1986 CB GLN A 419 1435 1732 1984 473 -542 -697 C ATOM 1987 CG GLN A 419 30.281 32.833 11.672 1.00 19.06 C ANISOU 1987 CG GLN A 419 2109 2412 2721 488 -572 -721 C ATOM 1988 CD GLN A 419 30.791 32.089 10.452 1.00 19.85 C ANISOU 1988 CD GLN A 419 2188 2508 2846 487 -576 -743 C ATOM 1989 OE1 GLN A 419 31.591 32.614 9.680 1.00 20.52 O ANISOU 1989 OE1 GLN A 419 2252 2602 2941 483 -570 -765 O ATOM 1990 NE2 GLN A 419 30.311 30.869 10.263 1.00 12.09 N ANISOU 1990 NE2 GLN A 419 1211 1514 1871 492 -587 -736 N ATOM 1991 N HIS A 420 26.665 35.650 11.505 1.00 14.70 N ANISOU 1991 N HIS A 420 1629 1907 2047 452 -491 -643 N ATOM 1992 CA HIS A 420 25.904 36.771 10.967 1.00 16.96 C ANISOU 1992 CA HIS A 420 1928 2209 2306 438 -466 -628 C ATOM 1993 C HIS A 420 25.760 37.903 11.986 1.00 18.10 C ANISOU 1993 C HIS A 420 2082 2362 2434 442 -463 -623 C ATOM 1994 O HIS A 420 25.934 39.078 11.653 1.00 22.62 O ANISOU 1994 O HIS A 420 2652 2943 3001 434 -453 -628 O ATOM 1995 CB HIS A 420 24.514 36.354 10.481 1.00 19.54 C ANISOU 1995 CB HIS A 420 2275 2541 2609 430 -450 -601 C ATOM 1996 CG HIS A 420 23.672 37.520 10.075 1.00 23.81 C ANISOU 1996 CG HIS A 420 2829 3097 3121 418 -426 -584 C ATOM 1997 ND1 HIS A 420 23.755 38.089 8.826 1.00 24.23 N ANISOU 1997 ND1 HIS A 420 2873 3157 3178 405 -412 -581 N ATOM 1998 CD2 HIS A 420 22.794 38.274 10.779 1.00 25.01 C ANISOU 1998 CD2 HIS A 420 2997 3259 3247 419 -415 -564 C ATOM 1999 CE1 HIS A 420 22.936 39.123 8.761 1.00 26.59 C ANISOU 1999 CE1 HIS A 420 3182 3467 3454 398 -394 -559 C ATOM 2000 NE2 HIS A 420 22.337 39.255 9.930 1.00 28.09 N ANISOU 2000 NE2 HIS A 420 3387 3660 3627 407 -395 -549 N ATOM 2001 N ILE A 421 25.430 37.551 13.222 1.00 15.41 N ANISOU 2001 N ILE A 421 1751 2018 2086 455 -472 -614 N ATOM 2002 CA ILE A 421 25.255 38.568 14.253 1.00 13.57 C ANISOU 2002 CA ILE A 421 1525 1794 1836 461 -470 -610 C ATOM 2003 C ILE A 421 26.582 39.240 14.582 1.00 18.99 C ANISOU 2003 C ILE A 421 2194 2476 2544 466 -484 -636 C ATOM 2004 O ILE A 421 26.658 40.468 14.683 1.00 17.83 O ANISOU 2004 O ILE A 421 2047 2337 2389 463 -477 -640 O ATOM 2005 CB ILE A 421 24.605 38.006 15.530 1.00 18.25 C ANISOU 2005 CB ILE A 421 2131 2387 2416 475 -476 -594 C ATOM 2006 CG1 ILE A 421 23.168 37.550 15.232 1.00 22.06 C ANISOU 2006 CG1 ILE A 421 2631 2878 2874 470 -458 -565 C ATOM 2007 CG2 ILE A 421 24.615 39.066 16.648 1.00 13.12 C ANISOU 2007 CG2 ILE A 421 1485 1748 1753 484 -477 -596 C ATOM 2008 CD1 ILE A 421 22.590 36.589 16.267 1.00 21.13 C ANISOU 2008 CD1 ILE A 421 2521 2757 2751 481 -466 -547 C ATOM 2009 N VAL A 422 27.634 38.437 14.740 1.00 18.93 N ANISOU 2009 N VAL A 422 2169 2455 2568 474 -505 -654 N ATOM 2010 CA VAL A 422 28.948 38.982 15.082 1.00 13.42 C ANISOU 2010 CA VAL A 422 1452 1753 1895 480 -519 -678 C ATOM 2011 C VAL A 422 29.525 39.851 13.957 1.00 15.88 C ANISOU 2011 C VAL A 422 1750 2070 2215 466 -508 -693 C ATOM 2012 O VAL A 422 30.236 40.803 14.219 1.00 18.32 O ANISOU 2012 O VAL A 422 2050 2381 2532 467 -511 -707 O ATOM 2013 CB VAL A 422 29.950 37.873 15.461 1.00 18.23 C ANISOU 2013 CB VAL A 422 2044 2346 2538 492 -545 -694 C ATOM 2014 CG1 VAL A 422 31.334 38.464 15.710 1.00 17.54 C ANISOU 2014 CG1 VAL A 422 1934 2254 2477 497 -559 -720 C ATOM 2015 CG2 VAL A 422 29.468 37.116 16.687 1.00 18.20 C ANISOU 2015 CG2 VAL A 422 2052 2336 2528 505 -559 -677 C ATOM 2016 N SER A 423 29.183 39.545 12.709 1.00 16.82 N ANISOU 2016 N SER A 423 1868 2192 2332 454 -495 -689 N ATOM 2017 CA SER A 423 29.777 40.235 11.559 1.00 21.52 C ANISOU 2017 CA SER A 423 2447 2793 2938 442 -485 -703 C ATOM 2018 C SER A 423 29.096 41.549 11.165 1.00 27.52 C ANISOU 2018 C SER A 423 3218 3564 3675 429 -465 -689 C ATOM 2019 O SER A 423 29.662 42.351 10.410 1.00 30.59 O ANISOU 2019 O SER A 423 3592 3957 4075 420 -457 -697 O ATOM 2020 CB SER A 423 29.805 39.299 10.340 1.00 19.60 C ANISOU 2020 CB SER A 423 2193 2547 2705 435 -481 -707 C ATOM 2021 OG SER A 423 30.753 38.253 10.520 1.00 27.74 O ANISOU 2021 OG SER A 423 3206 3568 3767 447 -501 -728 O ATOM 2022 N ASN A 424 27.876 41.757 11.650 1.00 23.70 N ANISOU 2022 N ASN A 424 2757 3087 3163 430 -455 -662 N ATOM 2023 CA ASN A 424 27.066 42.881 11.200 1.00 22.02 C ANISOU 2023 CA ASN A 424 2552 2884 2931 420 -435 -640 C ATOM 2024 C ASN A 424 27.152 44.064 12.177 1.00 20.40 C ANISOU 2024 C ASN A 424 2350 2682 2720 426 -440 -643 C ATOM 2025 O ASN A 424 26.773 43.948 13.343 1.00 18.07 O ANISOU 2025 O ASN A 424 2067 2387 2412 439 -447 -639 O ATOM 2026 CB ASN A 424 25.613 42.425 10.987 1.00 25.02 C ANISOU 2026 CB ASN A 424 2952 3269 3284 416 -421 -611 C ATOM 2027 CG ASN A 424 24.709 43.537 10.462 1.00 27.41 C ANISOU 2027 CG ASN A 424 3264 3582 3569 405 -401 -588 C ATOM 2028 OD1 ASN A 424 25.045 44.721 10.520 1.00 28.33 O ANISOU 2028 OD1 ASN A 424 3374 3700 3691 403 -400 -593 O ATOM 2029 ND2 ASN A 424 23.552 43.153 9.954 1.00 27.76 N ANISOU 2029 ND2 ASN A 424 3322 3630 3594 399 -386 -564 N ATOM 2030 N ASP A 425 27.672 45.190 11.696 1.00 20.08 N ANISOU 2030 N ASP A 425 2297 2643 2691 419 -435 -650 N ATOM 2031 CA ASP A 425 27.832 46.380 12.531 1.00 17.94 C ANISOU 2031 CA ASP A 425 2027 2373 2418 425 -441 -654 C ATOM 2032 C ASP A 425 26.494 46.875 13.057 1.00 17.76 C ANISOU 2032 C ASP A 425 2025 2358 2366 429 -432 -630 C ATOM 2033 O ASP A 425 26.411 47.445 14.154 1.00 17.36 O ANISOU 2033 O ASP A 425 1979 2309 2306 441 -440 -634 O ATOM 2034 CB ASP A 425 28.517 47.505 11.754 1.00 21.46 C ANISOU 2034 CB ASP A 425 2457 2817 2882 415 -435 -664 C ATOM 2035 CG ASP A 425 29.999 47.256 11.536 1.00 27.24 C ANISOU 2035 CG ASP A 425 3164 3541 3643 415 -447 -693 C ATOM 2036 OD1 ASP A 425 30.611 46.477 12.312 1.00 24.57 O ANISOU 2036 OD1 ASP A 425 2823 3197 3314 427 -463 -710 O ATOM 2037 OD2 ASP A 425 30.548 47.848 10.581 1.00 28.32 O ANISOU 2037 OD2 ASP A 425 3286 3678 3795 404 -439 -701 O ATOM 2038 N ASP A 426 25.446 46.659 12.276 1.00 15.15 N ANISOU 2038 N ASP A 426 1705 2032 2018 419 -415 -607 N ATOM 2039 CA ASP A 426 24.116 47.103 12.686 1.00 17.55 C ANISOU 2039 CA ASP A 426 2028 2346 2295 423 -405 -585 C ATOM 2040 C ASP A 426 23.573 46.277 13.846 1.00 18.34 C ANISOU 2040 C ASP A 426 2141 2450 2377 438 -411 -581 C ATOM 2041 O ASP A 426 22.541 46.609 14.429 1.00 18.68 O ANISOU 2041 O ASP A 426 2198 2502 2396 445 -405 -566 O ATOM 2042 CB ASP A 426 23.158 47.107 11.499 1.00 17.84 C ANISOU 2042 CB ASP A 426 2072 2386 2322 408 -385 -561 C ATOM 2043 CG ASP A 426 23.465 48.220 10.515 1.00 25.12 C ANISOU 2043 CG ASP A 426 2983 3304 3257 394 -378 -562 C ATOM 2044 OD1 ASP A 426 23.508 47.937 9.303 1.00 30.33 O ANISOU 2044 OD1 ASP A 426 3637 3962 3923 380 -367 -556 O ATOM 2045 OD2 ASP A 426 23.688 49.373 10.958 1.00 26.47 O ANISOU 2045 OD2 ASP A 426 3151 3474 3432 398 -384 -570 O ATOM 2046 N LEU A 427 24.290 45.216 14.207 1.00 14.83 N ANISOU 2046 N LEU A 427 1692 1999 1945 444 -424 -595 N ATOM 2047 CA LEU A 427 23.925 44.425 15.377 1.00 15.47 C ANISOU 2047 CA LEU A 427 1784 2081 2011 459 -432 -594 C ATOM 2048 C LEU A 427 25.008 44.532 16.454 1.00 16.03 C ANISOU 2048 C LEU A 427 1847 2146 2097 472 -454 -619 C ATOM 2049 O LEU A 427 25.121 43.658 17.314 1.00 18.28 O ANISOU 2049 O LEU A 427 2138 2428 2381 484 -466 -626 O ATOM 2050 CB LEU A 427 23.683 42.957 14.977 1.00 11.74 C ANISOU 2050 CB LEU A 427 1318 1604 1540 455 -431 -588 C ATOM 2051 CG LEU A 427 22.450 42.729 14.099 1.00 18.92 C ANISOU 2051 CG LEU A 427 2238 2520 2431 444 -410 -561 C ATOM 2052 CD1 LEU A 427 22.392 41.311 13.537 1.00 18.21 C ANISOU 2052 CD1 LEU A 427 2150 2422 2348 440 -412 -558 C ATOM 2053 CD2 LEU A 427 21.165 43.048 14.880 1.00 23.49 C ANISOU 2053 CD2 LEU A 427 2835 3113 2979 453 -400 -541 C ATOM 2054 N ALA A 428 25.791 45.612 16.415 1.00 16.84 N ANISOU 2054 N ALA A 428 1938 2247 2215 471 -459 -634 N ATOM 2055 CA ALA A 428 26.989 45.732 17.265 1.00 19.20 C ANISOU 2055 CA ALA A 428 2225 2537 2532 482 -480 -660 C ATOM 2056 C ALA A 428 26.759 45.392 18.738 1.00 20.99 C ANISOU 2056 C ALA A 428 2464 2767 2745 500 -492 -663 C ATOM 2057 O ALA A 428 27.549 44.644 19.339 1.00 25.28 O ANISOU 2057 O ALA A 428 2997 3301 3306 510 -508 -672 O ATOM 2058 CB ALA A 428 27.620 47.125 17.135 1.00 21.33 C ANISOU 2058 CB ALA A 428 2483 2806 2816 479 -482 -672 C ATOM 2059 N VAL A 429 25.691 45.933 19.324 1.00 14.74 N ANISOU 2059 N VAL A 429 1687 1990 1926 508 -483 -649 N ATOM 2060 CA VAL A 429 25.404 45.672 20.740 1.00 17.66 C ANISOU 2060 CA VAL A 429 2065 2367 2281 527 -492 -648 C ATOM 2061 C VAL A 429 25.242 44.165 21.012 1.00 23.50 C ANISOU 2061 C VAL A 429 2805 3101 3022 532 -495 -635 C ATOM 2062 O VAL A 429 25.624 43.660 22.069 1.00 28.35 O ANISOU 2062 O VAL A 429 3416 3714 3643 546 -511 -637 O ATOM 2063 CB VAL A 429 24.163 46.449 21.230 1.00 24.31 C ANISOU 2063 CB VAL A 429 2921 3227 3089 535 -480 -637 C ATOM 2064 CG1 VAL A 429 22.879 45.769 20.766 1.00 23.13 C ANISOU 2064 CG1 VAL A 429 2784 3086 2916 530 -461 -611 C ATOM 2065 CG2 VAL A 429 24.164 46.563 22.734 1.00 24.79 C ANISOU 2065 CG2 VAL A 429 2983 3296 3139 558 -492 -642 C ATOM 2066 N TYR A 430 24.702 43.439 20.041 1.00 23.67 N ANISOU 2066 N TYR A 430 2832 3122 3042 519 -483 -620 N ATOM 2067 CA TYR A 430 24.495 42.004 20.213 1.00 25.29 C ANISOU 2067 CA TYR A 430 3037 3320 3250 523 -487 -607 C ATOM 2068 C TYR A 430 25.793 41.253 19.982 1.00 24.37 C ANISOU 2068 C TYR A 430 2905 3185 3171 521 -506 -623 C ATOM 2069 O TYR A 430 26.051 40.222 20.609 1.00 19.92 O ANISOU 2069 O TYR A 430 2336 2612 2619 530 -522 -618 O ATOM 2070 CB TYR A 430 23.335 41.522 19.332 1.00 24.55 C ANISOU 2070 CB TYR A 430 2956 3232 3139 511 -466 -585 C ATOM 2071 CG TYR A 430 22.072 42.243 19.752 1.00 24.28 C ANISOU 2071 CG TYR A 430 2937 3218 3070 516 -449 -569 C ATOM 2072 CD1 TYR A 430 21.501 41.993 21.004 1.00 20.02 C ANISOU 2072 CD1 TYR A 430 2403 2690 2513 533 -451 -558 C ATOM 2073 CD2 TYR A 430 21.500 43.228 18.950 1.00 20.42 C ANISOU 2073 CD2 TYR A 430 2455 2738 2568 505 -433 -566 C ATOM 2074 CE1 TYR A 430 20.365 42.674 21.428 1.00 16.94 C ANISOU 2074 CE1 TYR A 430 2023 2321 2091 540 -436 -546 C ATOM 2075 CE2 TYR A 430 20.358 43.919 19.365 1.00 23.14 C ANISOU 2075 CE2 TYR A 430 2810 3100 2881 512 -420 -554 C ATOM 2076 CZ TYR A 430 19.800 43.641 20.614 1.00 24.70 C ANISOU 2076 CZ TYR A 430 3014 3311 3062 530 -421 -545 C ATOM 2077 OH TYR A 430 18.677 44.321 21.053 1.00 23.51 O ANISOU 2077 OH TYR A 430 2872 3181 2881 539 -408 -535 O ATOM 2078 N ARG A 431 26.632 41.812 19.116 1.00 24.49 N ANISOU 2078 N ARG A 431 2907 3194 3205 511 -507 -641 N ATOM 2079 CA ARG A 431 27.944 41.252 18.863 1.00 19.46 C ANISOU 2079 CA ARG A 431 2250 2541 2603 511 -525 -660 C ATOM 2080 C ARG A 431 28.762 41.182 20.144 1.00 24.73 C ANISOU 2080 C ARG A 431 2909 3202 3285 527 -548 -670 C ATOM 2081 O ARG A 431 29.450 40.187 20.404 1.00 23.88 O ANISOU 2081 O ARG A 431 2790 3081 3202 533 -567 -675 O ATOM 2082 CB ARG A 431 28.687 42.089 17.831 1.00 21.43 C ANISOU 2082 CB ARG A 431 2486 2788 2867 498 -520 -678 C ATOM 2083 CG ARG A 431 30.204 41.991 17.927 1.00 20.08 C ANISOU 2083 CG ARG A 431 2292 2606 2733 503 -539 -703 C ATOM 2084 CD ARG A 431 30.832 42.394 16.616 1.00 24.94 C ANISOU 2084 CD ARG A 431 2892 3221 3365 489 -531 -717 C ATOM 2085 NE ARG A 431 30.704 43.826 16.384 1.00 23.56 N ANISOU 2085 NE ARG A 431 2719 3054 3179 481 -519 -718 N ATOM 2086 CZ ARG A 431 30.503 44.391 15.198 1.00 20.04 C ANISOU 2086 CZ ARG A 431 2271 2613 2731 465 -502 -716 C ATOM 2087 NH1 ARG A 431 30.373 43.645 14.106 1.00 13.13 N ANISOU 2087 NH1 ARG A 431 1392 1738 1860 455 -494 -712 N ATOM 2088 NH2 ARG A 431 30.416 45.715 15.112 1.00 20.88 N ANISOU 2088 NH2 ARG A 431 2378 2724 2831 460 -495 -716 N ATOM 2089 N GLU A 432 28.702 42.242 20.940 1.00 22.89 N ANISOU 2089 N GLU A 432 2680 2978 3039 535 -548 -674 N ATOM 2090 CA GLU A 432 29.537 42.316 22.131 1.00 28.67 C ANISOU 2090 CA GLU A 432 3403 3706 3785 550 -571 -685 C ATOM 2091 C GLU A 432 29.040 41.339 23.189 1.00 31.56 C ANISOU 2091 C GLU A 432 3776 4073 4142 562 -581 -666 C ATOM 2092 O GLU A 432 29.837 40.638 23.825 1.00 31.91 O ANISOU 2092 O GLU A 432 3809 4106 4210 570 -605 -669 O ATOM 2093 CB GLU A 432 29.594 43.748 22.655 1.00 31.95 C ANISOU 2093 CB GLU A 432 3820 4130 4188 555 -569 -695 C ATOM 2094 CG GLU A 432 29.867 44.755 21.539 1.00 35.06 C ANISOU 2094 CG GLU A 432 4209 4523 4588 540 -556 -708 C ATOM 2095 CD GLU A 432 30.326 46.106 22.057 1.00 37.05 C ANISOU 2095 CD GLU A 432 4458 4779 4842 545 -563 -723 C ATOM 2096 OE1 GLU A 432 30.364 46.287 23.299 1.00 39.81 O ANISOU 2096 OE1 GLU A 432 4810 5133 5185 561 -575 -725 O ATOM 2097 OE2 GLU A 432 30.652 46.977 21.216 1.00 30.72 O ANISOU 2097 OE2 GLU A 432 3649 3975 4049 533 -556 -733 O ATOM 2098 N CYS A 433 27.720 41.277 23.348 1.00 28.87 N ANISOU 2098 N CYS A 433 3007 4868 3094 449 -185 -1027 N ATOM 2099 CA ACYS A 433 27.085 40.333 24.262 0.50 28.81 C ANISOU 2099 CA ACYS A 433 2967 4921 3056 411 -164 -1025 C ATOM 2100 CA BCYS A 433 27.118 40.342 24.282 0.50 28.49 C ANISOU 2100 CA BCYS A 433 2928 4881 3017 410 -164 -1024 C ATOM 2101 C CYS A 433 27.602 38.924 23.993 1.00 29.90 C ANISOU 2101 C CYS A 433 3112 5038 3210 365 -146 -972 C ATOM 2102 O CYS A 433 28.116 38.242 24.890 1.00 20.67 O ANISOU 2102 O CYS A 433 1941 3880 2034 327 -137 -941 O ATOM 2103 CB ACYS A 433 25.558 40.347 24.084 0.50 30.41 C ANISOU 2103 CB ACYS A 433 3135 5183 3237 423 -158 -1068 C ATOM 2104 CB BCYS A 433 25.589 40.410 24.199 0.50 30.08 C ANISOU 2104 CB BCYS A 433 3093 5144 3194 424 -158 -1070 C ATOM 2105 SG ACYS A 433 24.639 41.721 24.849 0.50 44.15 S ANISOU 2105 SG ACYS A 433 4849 6976 4949 466 -172 -1137 S ATOM 2106 SG BCYS A 433 24.708 39.601 25.564 0.50 36.29 S ANISOU 2106 SG BCYS A 433 3836 6019 3934 382 -136 -1079 S ATOM 2107 N ILE A 434 27.449 38.491 22.742 1.00 25.91 N ANISOU 2107 N ILE A 434 2614 4503 2728 368 -143 -964 N ATOM 2108 CA ILE A 434 27.796 37.131 22.350 1.00 26.77 C ANISOU 2108 CA ILE A 434 2725 4591 2855 327 -125 -922 C ATOM 2109 C ILE A 434 29.255 36.790 22.656 1.00 28.17 C ANISOU 2109 C ILE A 434 2930 4719 3056 305 -127 -874 C ATOM 2110 O ILE A 434 29.562 35.734 23.216 1.00 26.50 O ANISOU 2110 O ILE A 434 2711 4512 2847 263 -114 -839 O ATOM 2111 CB ILE A 434 27.527 36.914 20.858 1.00 29.00 C ANISOU 2111 CB ILE A 434 3014 4844 3160 340 -124 -925 C ATOM 2112 CG1 ILE A 434 26.032 36.691 20.627 1.00 34.33 C ANISOU 2112 CG1 ILE A 434 3656 5575 3813 343 -115 -959 C ATOM 2113 CG2 ILE A 434 28.366 35.754 20.332 1.00 23.86 C ANISOU 2113 CG2 ILE A 434 2378 4148 2541 305 -111 -879 C ATOM 2114 CD1 ILE A 434 25.640 36.659 19.167 1.00 33.87 C ANISOU 2114 CD1 ILE A 434 3601 5495 3771 359 -117 -969 C ATOM 2115 N ILE A 435 30.144 37.692 22.270 1.00 25.44 N ANISOU 2115 N ILE A 435 2614 4323 2730 334 -144 -873 N ATOM 2116 CA ILE A 435 31.555 37.514 22.517 1.00 35.77 C ANISOU 2116 CA ILE A 435 3948 5583 4061 318 -147 -831 C ATOM 2117 C ILE A 435 31.804 37.292 24.018 1.00 38.98 C ANISOU 2117 C ILE A 435 4343 6023 4445 291 -145 -816 C ATOM 2118 O ILE A 435 32.497 36.350 24.405 1.00 39.15 O ANISOU 2118 O ILE A 435 4367 6028 4478 253 -136 -774 O ATOM 2119 CB ILE A 435 32.363 38.713 21.951 1.00 19.16 C ANISOU 2119 CB ILE A 435 1875 3428 1975 356 -168 -838 C ATOM 2120 CG1 ILE A 435 32.248 38.747 20.424 1.00 19.02 C ANISOU 2120 CG1 ILE A 435 1870 3377 1982 373 -170 -843 C ATOM 2121 CG2 ILE A 435 33.817 38.633 22.363 1.00 21.98 C ANISOU 2121 CG2 ILE A 435 2258 3742 2353 340 -173 -799 C ATOM 2122 CD1 ILE A 435 32.852 39.978 19.763 1.00 17.02 C ANISOU 2122 CD1 ILE A 435 1645 3079 1744 411 -193 -852 C ATOM 2123 N GLU A 436 31.213 38.134 24.860 1.00 41.40 N ANISOU 2123 N GLU A 436 4636 6377 4718 308 -152 -852 N ATOM 2124 CA GLU A 436 31.409 38.024 26.312 1.00 46.50 C ANISOU 2124 CA GLU A 436 5270 7062 5337 282 -150 -842 C ATOM 2125 C GLU A 436 30.776 36.755 26.908 1.00 41.95 C ANISOU 2125 C GLU A 436 4663 6534 4742 235 -130 -823 C ATOM 2126 O GLU A 436 31.343 36.130 27.811 1.00 40.09 O ANISOU 2126 O GLU A 436 4426 6306 4501 198 -126 -786 O ATOM 2127 CB GLU A 436 30.890 39.283 27.027 1.00 53.57 C ANISOU 2127 CB GLU A 436 6155 7998 6202 313 -162 -892 C ATOM 2128 CG GLU A 436 31.629 40.569 26.619 1.00 64.16 C ANISOU 2128 CG GLU A 436 7526 9290 7563 356 -184 -907 C ATOM 2129 CD GLU A 436 31.123 41.825 27.329 1.00 73.24 C ANISOU 2129 CD GLU A 436 8665 10476 8687 388 -197 -960 C ATOM 2130 OE1 GLU A 436 29.896 42.067 27.324 1.00 76.77 O ANISOU 2130 OE1 GLU A 436 9085 10971 9113 404 -194 -1003 O ATOM 2131 OE2 GLU A 436 31.960 42.581 27.879 1.00 72.97 O ANISOU 2131 OE2 GLU A 436 8648 10422 8654 398 -211 -960 O ATOM 2132 N LYS A 437 29.617 36.374 26.378 1.00 33.58 N ANISOU 2132 N LYS A 437 3581 5505 3673 237 -119 -846 N ATOM 2133 CA LYS A 437 28.815 35.283 26.927 1.00 38.93 C ANISOU 2133 CA LYS A 437 4226 6236 4328 195 -101 -835 C ATOM 2134 C LYS A 437 29.386 33.904 26.661 1.00 42.40 C ANISOU 2134 C LYS A 437 4672 6641 4797 153 -91 -781 C ATOM 2135 O LYS A 437 29.368 33.042 27.542 1.00 44.21 O ANISOU 2135 O LYS A 437 4885 6899 5013 109 -82 -751 O ATOM 2136 CB LYS A 437 27.398 35.328 26.355 1.00 45.08 C ANISOU 2136 CB LYS A 437 4981 7058 5091 211 -94 -878 C ATOM 2137 CG LYS A 437 26.575 34.072 26.619 1.00 49.52 C ANISOU 2137 CG LYS A 437 5513 7665 5638 167 -74 -863 C ATOM 2138 CD LYS A 437 26.036 34.025 28.051 1.00 53.13 C ANISOU 2138 CD LYS A 437 5940 8199 6049 141 -69 -872 C ATOM 2139 CE LYS A 437 25.184 32.785 28.260 1.00 56.84 C ANISOU 2139 CE LYS A 437 6379 8713 6503 96 -51 -856 C ATOM 2140 NZ LYS A 437 24.747 32.601 29.666 1.00 58.85 N ANISOU 2140 NZ LYS A 437 6605 9042 6712 62 -44 -855 N ATOM 2141 N CYS A 438 29.859 33.671 25.440 1.00 38.60 N ANISOU 2141 N CYS A 438 4212 6098 4356 164 -91 -768 N ATOM 2142 CA CYS A 438 30.324 32.332 25.107 1.00 35.20 C ANISOU 2142 CA CYS A 438 3783 5633 3957 126 -80 -723 C ATOM 2143 C CYS A 438 31.728 32.259 24.512 1.00 29.50 C ANISOU 2143 C CYS A 438 3095 4834 3281 130 -87 -690 C ATOM 2144 O CYS A 438 32.295 31.170 24.424 1.00 29.37 O ANISOU 2144 O CYS A 438 3080 4785 3293 97 -80 -649 O ATOM 2145 CB CYS A 438 29.318 31.595 24.205 1.00 27.83 C ANISOU 2145 CB CYS A 438 2832 4712 3030 119 -66 -736 C ATOM 2146 SG CYS A 438 29.297 32.093 22.461 1.00 45.98 S ANISOU 2146 SG CYS A 438 5151 6963 5357 161 -69 -763 S ATOM 2147 N LEU A 439 32.289 33.390 24.096 1.00 21.68 N ANISOU 2147 N LEU A 439 2129 3812 2298 169 -101 -707 N ATOM 2148 CA LEU A 439 33.587 33.327 23.410 1.00 24.51 C ANISOU 2148 CA LEU A 439 2516 4097 2698 174 -107 -679 C ATOM 2149 C LEU A 439 34.768 33.593 24.337 1.00 27.69 C ANISOU 2149 C LEU A 439 2935 4480 3105 165 -118 -648 C ATOM 2150 O LEU A 439 35.710 32.797 24.391 1.00 31.37 O ANISOU 2150 O LEU A 439 3410 4907 3602 139 -115 -605 O ATOM 2151 CB LEU A 439 33.634 34.243 22.186 1.00 21.14 C ANISOU 2151 CB LEU A 439 2110 3639 2285 216 -115 -707 C ATOM 2152 CG LEU A 439 32.627 33.936 21.068 1.00 24.53 C ANISOU 2152 CG LEU A 439 2526 4079 2715 225 -105 -733 C ATOM 2153 CD1 LEU A 439 32.849 34.871 19.890 1.00 22.25 C ANISOU 2153 CD1 LEU A 439 2259 3755 2440 264 -117 -754 C ATOM 2154 CD2 LEU A 439 32.689 32.470 20.619 1.00 20.35 C ANISOU 2154 CD2 LEU A 439 1988 3531 2213 187 -88 -705 C ATOM 2155 N MET A 440 34.717 34.702 25.069 1.00 24.68 N ANISOU 2155 N MET A 440 2557 4126 2695 186 -130 -671 N ATOM 2156 CA MET A 440 35.819 35.059 25.951 1.00 18.72 C ANISOU 2156 CA MET A 440 1817 3354 1941 180 -142 -647 C ATOM 2157 C MET A 440 36.096 33.920 26.909 1.00 17.26 C ANISOU 2157 C MET A 440 1618 3185 1755 131 -135 -602 C ATOM 2158 O MET A 440 35.169 33.284 27.402 1.00 18.55 O ANISOU 2158 O MET A 440 1754 3399 1895 106 -124 -604 O ATOM 2159 CB MET A 440 35.511 36.334 26.729 1.00 22.72 C ANISOU 2159 CB MET A 440 2322 3899 2411 206 -155 -684 C ATOM 2160 CG MET A 440 35.439 37.571 25.868 1.00 29.33 C ANISOU 2160 CG MET A 440 3178 4712 3255 255 -167 -722 C ATOM 2161 SD MET A 440 36.877 37.857 24.812 1.00 36.43 S ANISOU 2161 SD MET A 440 4116 5525 4202 271 -178 -696 S ATOM 2162 CE MET A 440 38.226 38.007 25.992 1.00 12.65 C ANISOU 2162 CE MET A 440 1119 2496 1192 252 -188 -660 C ATOM 2163 N ARG A 441 37.376 33.668 27.164 1.00 17.54 N ANISOU 2163 N ARG A 441 1671 3176 1817 116 -141 -560 N ATOM 2164 CA ARG A 441 37.798 32.596 28.055 1.00 22.21 C ANISOU 2164 CA ARG A 441 2251 3774 2415 69 -138 -511 C ATOM 2165 C ARG A 441 37.648 31.214 27.421 1.00 27.03 C ANISOU 2165 C ARG A 441 2851 4360 3058 41 -125 -484 C ATOM 2166 O ARG A 441 38.076 30.215 27.996 1.00 25.05 O ANISOU 2166 O ARG A 441 2592 4102 2823 2 -124 -439 O ATOM 2167 CB ARG A 441 37.066 32.669 29.403 1.00 21.07 C ANISOU 2167 CB ARG A 441 2083 3706 2219 48 -138 -518 C ATOM 2168 CG ARG A 441 37.418 33.913 30.234 1.00 26.14 C ANISOU 2168 CG ARG A 441 2734 4369 2831 68 -152 -538 C ATOM 2169 CD ARG A 441 36.605 34.003 31.539 1.00 28.63 C ANISOU 2169 CD ARG A 441 3021 4766 3091 46 -150 -552 C ATOM 2170 NE ARG A 441 35.173 33.972 31.267 1.00 35.08 N ANISOU 2170 NE ARG A 441 3814 5633 3883 54 -138 -593 N ATOM 2171 CZ ARG A 441 34.484 35.007 30.797 1.00 39.33 C ANISOU 2171 CZ ARG A 441 4352 6185 4406 97 -140 -649 C ATOM 2172 NH1 ARG A 441 35.103 36.164 30.563 1.00 34.43 N ANISOU 2172 NH1 ARG A 441 3755 5532 3794 136 -154 -670 N ATOM 2173 NH2 ARG A 441 33.181 34.883 30.556 1.00 40.70 N ANISOU 2173 NH2 ARG A 441 4501 6405 4559 102 -128 -683 N ATOM 2174 N ASN A 442 37.044 31.155 26.236 1.00 23.30 N ANISOU 2174 N ASN A 442 2379 3876 2599 61 -115 -512 N ATOM 2175 CA ASN A 442 36.900 29.888 25.525 1.00 20.10 C ANISOU 2175 CA ASN A 442 1964 3445 2228 37 -102 -492 C ATOM 2176 C ASN A 442 37.606 29.915 24.175 1.00 21.43 C ANISOU 2176 C ASN A 442 2154 3547 2440 58 -101 -495 C ATOM 2177 O ASN A 442 37.404 29.018 23.343 1.00 22.77 O ANISOU 2177 O ASN A 442 2317 3695 2639 46 -89 -492 O ATOM 2178 CB ASN A 442 35.417 29.574 25.307 1.00 24.47 C ANISOU 2178 CB ASN A 442 2492 4050 2756 33 -89 -523 C ATOM 2179 CG ASN A 442 34.677 29.368 26.612 1.00 27.94 C ANISOU 2179 CG ASN A 442 2907 4559 3152 5 -88 -517 C ATOM 2180 OD1 ASN A 442 35.116 28.607 27.486 1.00 27.00 O ANISOU 2180 OD1 ASN A 442 2779 4441 3037 -34 -90 -473 O ATOM 2181 ND2 ASN A 442 33.561 30.040 26.756 1.00 25.44 N ANISOU 2181 ND2 ASN A 442 2574 4298 2792 23 -85 -562 N ATOM 2182 N LEU A 443 38.433 30.935 23.957 1.00 15.63 N ANISOU 2182 N LEU A 443 1445 2784 1711 88 -113 -503 N ATOM 2183 CA LEU A 443 39.015 31.159 22.633 1.00 18.18 C ANISOU 2183 CA LEU A 443 1788 3052 2068 111 -112 -512 C ATOM 2184 C LEU A 443 39.903 30.009 22.145 1.00 20.01 C ANISOU 2184 C LEU A 443 2022 3229 2352 87 -104 -476 C ATOM 2185 O LEU A 443 39.877 29.656 20.969 1.00 22.27 O ANISOU 2185 O LEU A 443 2310 3487 2663 92 -95 -487 O ATOM 2186 CB LEU A 443 39.775 32.490 22.590 1.00 11.75 C ANISOU 2186 CB LEU A 443 1000 2218 1248 145 -128 -523 C ATOM 2187 CG LEU A 443 38.926 33.735 22.812 1.00 13.87 C ANISOU 2187 CG LEU A 443 1268 2530 1473 177 -137 -566 C ATOM 2188 CD1 LEU A 443 39.751 35.017 22.660 1.00 12.32 C ANISOU 2188 CD1 LEU A 443 1099 2304 1279 209 -155 -575 C ATOM 2189 CD2 LEU A 443 37.710 33.754 21.870 1.00 12.78 C ANISOU 2189 CD2 LEU A 443 1118 2414 1325 193 -128 -603 C ATOM 2190 N LEU A 444 40.696 29.436 23.040 1.00 20.18 N ANISOU 2190 N LEU A 444 2042 3237 2390 59 -109 -433 N ATOM 2191 CA LEU A 444 41.585 28.342 22.659 1.00 19.25 C ANISOU 2191 CA LEU A 444 1924 3064 2325 37 -104 -399 C ATOM 2192 C LEU A 444 40.812 27.083 22.250 1.00 18.65 C ANISOU 2192 C LEU A 444 1826 2993 2267 11 -88 -397 C ATOM 2193 O LEU A 444 41.128 26.455 21.242 1.00 18.72 O ANISOU 2193 O LEU A 444 1836 2960 2318 9 -79 -398 O ATOM 2194 CB LEU A 444 42.548 28.013 23.794 1.00 17.13 C ANISOU 2194 CB LEU A 444 1656 2783 2070 12 -115 -351 C ATOM 2195 CG LEU A 444 43.483 26.817 23.564 1.00 17.77 C ANISOU 2195 CG LEU A 444 1734 2807 2211 -13 -113 -312 C ATOM 2196 CD1 LEU A 444 44.317 26.971 22.269 1.00 10.48 C ANISOU 2196 CD1 LEU A 444 828 1826 1327 9 -108 -325 C ATOM 2197 CD2 LEU A 444 44.383 26.574 24.792 1.00 9.02 C ANISOU 2197 CD2 LEU A 444 625 1691 1110 -37 -127 -263 C ATOM 2198 N SER A 445 39.800 26.715 23.026 1.00 13.64 N ANISOU 2198 N SER A 445 1169 2410 1602 -10 -85 -395 N ATOM 2199 CA SER A 445 39.061 25.502 22.729 1.00 18.81 C ANISOU 2199 CA SER A 445 1802 3070 2273 -38 -72 -391 C ATOM 2200 C SER A 445 38.188 25.687 21.500 1.00 16.03 C ANISOU 2200 C SER A 445 1449 2728 1915 -16 -59 -437 C ATOM 2201 O SER A 445 38.072 24.782 20.676 1.00 19.83 O ANISOU 2201 O SER A 445 1922 3182 2430 -29 -47 -438 O ATOM 2202 CB SER A 445 38.215 25.056 23.931 1.00 23.44 C ANISOU 2202 CB SER A 445 2366 3715 2826 -70 -72 -375 C ATOM 2203 OG SER A 445 37.284 26.056 24.277 1.00 29.55 O ANISOU 2203 OG SER A 445 3136 4550 3543 -49 -74 -411 O ATOM 2204 N LEU A 446 37.579 26.862 21.370 1.00 16.92 N ANISOU 2204 N LEU A 446 1567 2876 1985 16 -63 -475 N ATOM 2205 CA LEU A 446 36.653 27.112 20.260 1.00 17.22 C ANISOU 2205 CA LEU A 446 1602 2930 2013 37 -53 -518 C ATOM 2206 C LEU A 446 37.401 27.237 18.939 1.00 17.74 C ANISOU 2206 C LEU A 446 1686 2940 2113 56 -51 -528 C ATOM 2207 O LEU A 446 36.878 26.866 17.876 1.00 17.06 O ANISOU 2207 O LEU A 446 1594 2850 2037 58 -39 -551 O ATOM 2208 CB LEU A 446 35.803 28.361 20.523 1.00 16.04 C ANISOU 2208 CB LEU A 446 1452 2832 1810 68 -61 -555 C ATOM 2209 CG LEU A 446 34.721 28.202 21.598 1.00 17.66 C ANISOU 2209 CG LEU A 446 1632 3103 1974 50 -59 -559 C ATOM 2210 CD1 LEU A 446 33.965 29.485 21.744 1.00 18.60 C ANISOU 2210 CD1 LEU A 446 1752 3269 2048 85 -66 -601 C ATOM 2211 CD2 LEU A 446 33.750 27.044 21.268 1.00 18.32 C ANISOU 2211 CD2 LEU A 446 1690 3207 2063 22 -43 -562 C ATOM 2212 N SER A 447 38.627 27.755 19.012 1.00 11.60 N ANISOU 2212 N SER A 447 930 2123 1353 68 -61 -511 N ATOM 2213 CA SER A 447 39.473 27.870 17.830 1.00 16.99 C ANISOU 2213 CA SER A 447 1631 2755 2070 83 -59 -517 C ATOM 2214 C SER A 447 39.823 26.483 17.331 1.00 17.05 C ANISOU 2214 C SER A 447 1627 2725 2127 54 -45 -500 C ATOM 2215 O SER A 447 40.284 26.326 16.212 1.00 19.74 O ANISOU 2215 O SER A 447 1975 3030 2496 61 -37 -511 O ATOM 2216 CB SER A 447 40.760 28.652 18.135 1.00 18.02 C ANISOU 2216 CB SER A 447 1785 2852 2209 98 -73 -499 C ATOM 2217 OG SER A 447 40.471 29.992 18.498 1.00 22.79 O ANISOU 2217 OG SER A 447 2401 3486 2772 127 -87 -519 O ATOM 2218 N GLN A 448 39.593 25.475 18.170 1.00 17.27 N ANISOU 2218 N GLN A 448 1636 2762 2165 21 -42 -473 N ATOM 2219 CA GLN A 448 39.918 24.094 17.818 1.00 15.97 C ANISOU 2219 CA GLN A 448 1459 2559 2052 -9 -31 -454 C ATOM 2220 C GLN A 448 38.701 23.307 17.338 1.00 20.25 C ANISOU 2220 C GLN A 448 1978 3125 2589 -25 -16 -475 C ATOM 2221 O GLN A 448 38.790 22.105 17.075 1.00 25.85 O ANISOU 2221 O GLN A 448 2674 3807 3340 -51 -7 -462 O ATOM 2222 CB GLN A 448 40.566 23.381 19.005 1.00 15.49 C ANISOU 2222 CB GLN A 448 1391 2482 2013 -39 -39 -404 C ATOM 2223 CG GLN A 448 42.001 23.795 19.265 1.00 18.57 C ANISOU 2223 CG GLN A 448 1799 2829 2426 -29 -51 -379 C ATOM 2224 CD GLN A 448 42.523 23.180 20.547 1.00 22.03 C ANISOU 2224 CD GLN A 448 2231 3261 2880 -59 -62 -329 C ATOM 2225 OE1 GLN A 448 43.212 22.160 20.520 1.00 21.28 O ANISOU 2225 OE1 GLN A 448 2128 3120 2838 -81 -62 -300 O ATOM 2226 NE2 GLN A 448 42.174 23.783 21.682 1.00 17.12 N ANISOU 2226 NE2 GLN A 448 1609 2686 2212 -61 -73 -319 N ATOM 2227 N GLU A 449 37.571 23.996 17.216 1.00 19.28 N ANISOU 2227 N GLU A 449 1851 3055 2418 -8 -15 -508 N ATOM 2228 CA GLU A 449 36.320 23.383 16.784 1.00 21.10 C ANISOU 2228 CA GLU A 449 2061 3318 2638 -21 -2 -530 C ATOM 2229 C GLU A 449 36.095 23.602 15.294 1.00 21.81 C ANISOU 2229 C GLU A 449 2156 3397 2733 0 8 -569 C ATOM 2230 O GLU A 449 36.352 24.689 14.768 1.00 15.35 O ANISOU 2230 O GLU A 449 1356 2577 1898 32 1 -589 O ATOM 2231 CB GLU A 449 35.160 24.025 17.536 1.00 21.98 C ANISOU 2231 CB GLU A 449 2162 3497 2691 -14 -6 -546 C ATOM 2232 CG GLU A 449 35.191 23.783 19.013 1.00 30.23 C ANISOU 2232 CG GLU A 449 3197 4565 3723 -38 -14 -511 C ATOM 2233 CD GLU A 449 34.166 22.774 19.447 1.00 34.82 C ANISOU 2233 CD GLU A 449 3751 5183 4297 -73 -5 -504 C ATOM 2234 OE1 GLU A 449 34.210 22.367 20.622 1.00 41.50 O ANISOU 2234 OE1 GLU A 449 4586 6045 5135 -101 -11 -470 O ATOM 2235 OE2 GLU A 449 33.318 22.389 18.615 1.00 36.44 O ANISOU 2235 OE2 GLU A 449 3944 5400 4503 -75 7 -531 O ATOM 2236 N LYS A 450 35.589 22.583 14.615 1.00 22.07 N ANISOU 2236 N LYS A 450 2173 3425 2789 -21 23 -580 N ATOM 2237 CA LYS A 450 35.359 22.698 13.191 1.00 19.93 C ANISOU 2237 CA LYS A 450 1904 3147 2523 -6 33 -617 C ATOM 2238 C LYS A 450 34.456 23.897 12.888 1.00 21.45 C ANISOU 2238 C LYS A 450 2101 3389 2662 26 26 -651 C ATOM 2239 O LYS A 450 34.780 24.754 12.058 1.00 20.30 O ANISOU 2239 O LYS A 450 1972 3233 2508 53 22 -670 O ATOM 2240 CB LYS A 450 34.744 21.413 12.645 1.00 21.04 C ANISOU 2240 CB LYS A 450 2021 3283 2688 -35 49 -627 C ATOM 2241 CG LYS A 450 34.487 21.451 11.150 1.00 19.46 C ANISOU 2241 CG LYS A 450 1822 3080 2493 -24 61 -666 C ATOM 2242 CD LYS A 450 33.940 20.115 10.669 1.00 26.45 C ANISOU 2242 CD LYS A 450 2685 3959 3407 -56 77 -675 C ATOM 2243 CE LYS A 450 33.751 20.105 9.159 1.00 31.30 C ANISOU 2243 CE LYS A 450 3297 4569 4025 -48 89 -715 C ATOM 2244 NZ LYS A 450 35.052 20.370 8.448 1.00 39.26 N ANISOU 2244 NZ LYS A 450 4325 5529 5063 -35 90 -716 N ATOM 2245 N PHE A 451 33.327 23.962 13.577 1.00 18.61 N ANISOU 2245 N PHE A 451 1725 3082 2265 21 25 -657 N ATOM 2246 CA PHE A 451 32.337 24.985 13.298 1.00 15.23 C ANISOU 2246 CA PHE A 451 1296 2702 1790 50 20 -691 C ATOM 2247 C PHE A 451 32.575 26.302 14.056 1.00 19.62 C ANISOU 2247 C PHE A 451 1867 3273 2314 80 2 -689 C ATOM 2248 O PHE A 451 32.519 27.371 13.447 1.00 16.29 O ANISOU 2248 O PHE A 451 1459 2856 1874 113 -8 -712 O ATOM 2249 CB PHE A 451 30.932 24.431 13.529 1.00 10.93 C ANISOU 2249 CB PHE A 451 722 2209 1221 33 28 -706 C ATOM 2250 CG PHE A 451 30.648 23.181 12.728 1.00 18.63 C ANISOU 2250 CG PHE A 451 1683 3169 2228 4 45 -712 C ATOM 2251 CD1 PHE A 451 30.642 23.221 11.341 1.00 22.46 C ANISOU 2251 CD1 PHE A 451 2172 3639 2724 15 52 -739 C ATOM 2252 CD2 PHE A 451 30.410 21.968 13.358 1.00 20.01 C ANISOU 2252 CD2 PHE A 451 1837 3344 2421 -35 54 -690 C ATOM 2253 CE1 PHE A 451 30.396 22.073 10.595 1.00 26.62 C ANISOU 2253 CE1 PHE A 451 2684 4151 3279 -11 68 -748 C ATOM 2254 CE2 PHE A 451 30.163 20.819 12.619 1.00 23.58 C ANISOU 2254 CE2 PHE A 451 2275 3778 2905 -61 69 -697 C ATOM 2255 CZ PHE A 451 30.160 20.872 11.235 1.00 24.69 C ANISOU 2255 CZ PHE A 451 2420 3904 3057 -49 77 -728 C ATOM 2256 N ALA A 452 32.864 26.230 15.359 1.00 13.84 N ANISOU 2256 N ALA A 452 1132 2548 1576 67 -5 -662 N ATOM 2257 CA ALA A 452 33.082 27.443 16.155 1.00 13.06 C ANISOU 2257 CA ALA A 452 1048 2468 1448 92 -21 -662 C ATOM 2258 C ALA A 452 34.343 28.215 15.766 1.00 18.50 C ANISOU 2258 C ALA A 452 1766 3109 2156 115 -32 -654 C ATOM 2259 O ALA A 452 34.484 29.383 16.116 1.00 20.94 O ANISOU 2259 O ALA A 452 2088 3427 2441 143 -47 -662 O ATOM 2260 CB ALA A 452 33.110 27.123 17.663 1.00 12.80 C ANISOU 2260 CB ALA A 452 1004 2457 1403 68 -24 -633 C ATOM 2261 N SER A 453 35.276 27.567 15.073 1.00 20.83 N ANISOU 2261 N SER A 453 2070 3351 2494 103 -25 -638 N ATOM 2262 CA SER A 453 36.504 28.254 14.688 1.00 20.27 C ANISOU 2262 CA SER A 453 2026 3235 2440 123 -34 -630 C ATOM 2263 C SER A 453 36.189 29.403 13.737 1.00 17.27 C ANISOU 2263 C SER A 453 1659 2865 2038 158 -43 -662 C ATOM 2264 O SER A 453 36.852 30.439 13.760 1.00 16.52 O ANISOU 2264 O SER A 453 1586 2754 1938 182 -57 -661 O ATOM 2265 CB SER A 453 37.549 27.294 14.080 1.00 18.56 C ANISOU 2265 CB SER A 453 1813 2963 2276 102 -24 -610 C ATOM 2266 OG SER A 453 37.047 26.601 12.947 1.00 18.79 O ANISOU 2266 OG SER A 453 1830 2990 2320 93 -8 -632 O ATOM 2267 N HIS A 454 35.162 29.222 12.916 1.00 9.71 N ANISOU 2267 N HIS A 454 688 1933 1068 161 -34 -691 N ATOM 2268 CA HIS A 454 34.721 30.272 12.007 1.00 12.97 C ANISOU 2268 CA HIS A 454 1111 2360 1459 193 -44 -721 C ATOM 2269 C HIS A 454 34.104 31.463 12.760 1.00 18.64 C ANISOU 2269 C HIS A 454 1830 3115 2137 222 -62 -735 C ATOM 2270 O HIS A 454 34.248 32.620 12.350 1.00 17.33 O ANISOU 2270 O HIS A 454 1681 2944 1959 253 -78 -747 O ATOM 2271 CB HIS A 454 33.715 29.702 11.014 1.00 12.90 C ANISOU 2271 CB HIS A 454 1083 2373 1445 186 -31 -746 C ATOM 2272 CG HIS A 454 34.311 28.697 10.077 1.00 18.17 C ANISOU 2272 CG HIS A 454 1750 3003 2150 162 -14 -741 C ATOM 2273 ND1 HIS A 454 35.070 29.061 8.990 1.00 18.08 N ANISOU 2273 ND1 HIS A 454 1756 2961 2153 173 -16 -746 N ATOM 2274 CD2 HIS A 454 34.257 27.343 10.070 1.00 15.01 C ANISOU 2274 CD2 HIS A 454 1332 2593 1777 129 4 -733 C ATOM 2275 CE1 HIS A 454 35.464 27.972 8.349 1.00 18.52 C ANISOU 2275 CE1 HIS A 454 1804 2989 2242 147 2 -744 C ATOM 2276 NE2 HIS A 454 34.985 26.920 8.984 1.00 19.56 N ANISOU 2276 NE2 HIS A 454 1915 3131 2384 121 13 -736 N ATOM 2277 N VAL A 455 33.417 31.169 13.862 1.00 12.01 N ANISOU 2277 N VAL A 455 971 2313 1278 210 -59 -733 N ATOM 2278 CA VAL A 455 32.875 32.213 14.725 1.00 15.94 C ANISOU 2278 CA VAL A 455 1467 2849 1741 234 -74 -749 C ATOM 2279 C VAL A 455 33.983 32.978 15.438 1.00 18.25 C ANISOU 2279 C VAL A 455 1783 3114 2038 246 -89 -729 C ATOM 2280 O VAL A 455 33.906 34.196 15.602 1.00 15.13 O ANISOU 2280 O VAL A 455 1398 2727 1623 278 -106 -746 O ATOM 2281 CB VAL A 455 31.935 31.618 15.779 1.00 17.72 C ANISOU 2281 CB VAL A 455 1664 3124 1943 213 -65 -750 C ATOM 2282 CG1 VAL A 455 31.463 32.715 16.760 1.00 16.98 C ANISOU 2282 CG1 VAL A 455 1567 3070 1812 237 -80 -769 C ATOM 2283 CG2 VAL A 455 30.764 30.942 15.089 1.00 20.48 C ANISOU 2283 CG2 VAL A 455 1991 3504 2285 203 -52 -772 C ATOM 2284 N VAL A 456 35.015 32.258 15.869 1.00 17.98 N ANISOU 2284 N VAL A 456 1755 3046 2031 220 -83 -694 N ATOM 2285 CA VAL A 456 36.148 32.901 16.519 1.00 15.24 C ANISOU 2285 CA VAL A 456 1430 2671 1691 228 -97 -673 C ATOM 2286 C VAL A 456 36.811 33.903 15.571 1.00 11.65 C ANISOU 2286 C VAL A 456 1000 2180 1244 258 -109 -682 C ATOM 2287 O VAL A 456 37.096 35.027 15.959 1.00 12.71 O ANISOU 2287 O VAL A 456 1151 2314 1366 282 -127 -687 O ATOM 2288 CB VAL A 456 37.170 31.866 17.065 1.00 14.69 C ANISOU 2288 CB VAL A 456 1361 2569 1653 194 -89 -632 C ATOM 2289 CG1 VAL A 456 38.475 32.550 17.449 1.00 10.15 C ANISOU 2289 CG1 VAL A 456 810 1956 1090 204 -103 -611 C ATOM 2290 CG2 VAL A 456 36.586 31.127 18.289 1.00 6.60 C ANISOU 2290 CG2 VAL A 456 312 1582 613 165 -82 -618 C ATOM 2291 N GLU A 457 37.022 33.503 14.319 1.00 11.63 N ANISOU 2291 N GLU A 457 1003 2152 1265 254 -101 -684 N ATOM 2292 CA GLU A 457 37.565 34.406 13.306 1.00 17.83 C ANISOU 2292 CA GLU A 457 1811 2908 2055 279 -112 -692 C ATOM 2293 C GLU A 457 36.713 35.677 13.168 1.00 20.47 C ANISOU 2293 C GLU A 457 2148 3271 2357 315 -131 -722 C ATOM 2294 O GLU A 457 37.227 36.793 13.269 1.00 18.43 O ANISOU 2294 O GLU A 457 1910 2998 2095 339 -150 -722 O ATOM 2295 CB GLU A 457 37.675 33.707 11.946 1.00 14.75 C ANISOU 2295 CB GLU A 457 1419 2498 1687 267 -98 -696 C ATOM 2296 CG GLU A 457 38.623 32.499 11.916 1.00 22.75 C ANISOU 2296 CG GLU A 457 2429 3474 2739 234 -81 -669 C ATOM 2297 CD GLU A 457 38.788 31.946 10.506 1.00 26.71 C ANISOU 2297 CD GLU A 457 2930 3956 3262 225 -68 -679 C ATOM 2298 OE1 GLU A 457 38.957 32.756 9.572 1.00 31.08 O ANISOU 2298 OE1 GLU A 457 3499 4502 3808 244 -76 -691 O ATOM 2299 OE2 GLU A 457 38.746 30.715 10.325 1.00 21.27 O ANISOU 2299 OE2 GLU A 457 2225 3260 2597 198 -49 -675 O ATOM 2300 N LYS A 458 35.415 35.505 12.935 1.00 17.09 N ANISOU 2300 N LYS A 458 1699 2885 1909 318 -126 -748 N ATOM 2301 CA LYS A 458 34.509 36.649 12.836 1.00 21.97 C ANISOU 2301 CA LYS A 458 2316 3533 2499 353 -144 -778 C ATOM 2302 C LYS A 458 34.622 37.607 14.029 1.00 17.87 C ANISOU 2302 C LYS A 458 1802 3024 1963 372 -161 -781 C ATOM 2303 O LYS A 458 34.572 38.829 13.860 1.00 15.62 O ANISOU 2303 O LYS A 458 1531 2735 1670 405 -182 -797 O ATOM 2304 CB LYS A 458 33.060 36.191 12.646 1.00 21.82 C ANISOU 2304 CB LYS A 458 2268 3563 2460 350 -134 -804 C ATOM 2305 CG LYS A 458 32.811 35.468 11.316 1.00 26.12 C ANISOU 2305 CG LYS A 458 2807 4101 3016 337 -120 -809 C ATOM 2306 CD LYS A 458 33.411 36.241 10.137 1.00 25.30 C ANISOU 2306 CD LYS A 458 2726 3963 2922 356 -134 -808 C ATOM 2307 CE LYS A 458 32.825 35.778 8.810 1.00 27.17 C ANISOU 2307 CE LYS A 458 2954 4211 3159 349 -125 -823 C ATOM 2308 NZ LYS A 458 33.221 34.379 8.487 1.00 33.94 N ANISOU 2308 NZ LYS A 458 3803 5052 4040 312 -99 -810 N ATOM 2309 N ALA A 459 34.796 37.054 15.225 1.00 13.59 N ANISOU 2309 N ALA A 459 1250 2495 1418 351 -152 -767 N ATOM 2310 CA ALA A 459 34.890 37.888 16.423 1.00 16.81 C ANISOU 2310 CA ALA A 459 1661 2917 1808 365 -166 -772 C ATOM 2311 C ALA A 459 36.158 38.739 16.371 1.00 20.35 C ANISOU 2311 C ALA A 459 2140 3318 2272 380 -183 -756 C ATOM 2312 O ALA A 459 36.095 39.941 16.594 1.00 20.18 O ANISOU 2312 O ALA A 459 2129 3299 2240 410 -203 -774 O ATOM 2313 CB ALA A 459 34.855 37.042 17.688 1.00 11.59 C ANISOU 2313 CB ALA A 459 983 2283 1139 334 -153 -756 C ATOM 2314 N PHE A 460 37.298 38.107 16.074 1.00 15.45 N ANISOU 2314 N PHE A 460 1534 2655 1681 358 -175 -723 N ATOM 2315 CA PHE A 460 38.555 38.826 15.909 1.00 16.23 C ANISOU 2315 CA PHE A 460 1661 2707 1797 368 -189 -705 C ATOM 2316 C PHE A 460 38.423 39.945 14.873 1.00 22.16 C ANISOU 2316 C PHE A 460 2429 3445 2546 401 -208 -724 C ATOM 2317 O PHE A 460 38.836 41.078 15.127 1.00 17.29 O ANISOU 2317 O PHE A 460 1830 2813 1926 424 -229 -728 O ATOM 2318 CB PHE A 460 39.674 37.874 15.491 1.00 17.33 C ANISOU 2318 CB PHE A 460 1808 2805 1969 340 -176 -672 C ATOM 2319 CG PHE A 460 40.449 37.295 16.643 1.00 20.14 C ANISOU 2319 CG PHE A 460 2163 3153 2336 315 -171 -642 C ATOM 2320 CD1 PHE A 460 40.313 35.953 16.989 1.00 19.25 C ANISOU 2320 CD1 PHE A 460 2031 3049 2234 282 -152 -625 C ATOM 2321 CD2 PHE A 460 41.312 38.089 17.381 1.00 13.79 C ANISOU 2321 CD2 PHE A 460 1376 2333 1531 324 -187 -630 C ATOM 2322 CE1 PHE A 460 41.033 35.413 18.050 1.00 18.65 C ANISOU 2322 CE1 PHE A 460 1953 2966 2168 258 -150 -594 C ATOM 2323 CE2 PHE A 460 42.043 37.552 18.437 1.00 18.93 C ANISOU 2323 CE2 PHE A 460 2025 2977 2190 300 -184 -601 C ATOM 2324 CZ PHE A 460 41.902 36.213 18.772 1.00 19.31 C ANISOU 2324 CZ PHE A 460 2054 3035 2249 267 -166 -581 C ATOM 2325 N LEU A 461 37.845 39.618 13.715 1.00 20.00 N ANISOU 2325 N LEU A 461 2149 3175 2275 401 -200 -735 N ATOM 2326 CA LEU A 461 37.631 40.584 12.635 1.00 16.64 C ANISOU 2326 CA LEU A 461 1736 2739 1846 429 -218 -750 C ATOM 2327 C LEU A 461 36.740 41.766 13.002 1.00 19.37 C ANISOU 2327 C LEU A 461 2078 3111 2169 464 -240 -780 C ATOM 2328 O LEU A 461 36.938 42.861 12.494 1.00 21.43 O ANISOU 2328 O LEU A 461 2358 3352 2433 490 -263 -785 O ATOM 2329 CB LEU A 461 37.030 39.893 11.408 1.00 15.37 C ANISOU 2329 CB LEU A 461 1563 2588 1687 419 -204 -758 C ATOM 2330 CG LEU A 461 37.972 38.968 10.641 1.00 16.61 C ANISOU 2330 CG LEU A 461 1727 2712 1870 390 -186 -735 C ATOM 2331 CD1 LEU A 461 37.209 38.052 9.676 1.00 14.06 C ANISOU 2331 CD1 LEU A 461 1386 2408 1548 375 -168 -748 C ATOM 2332 CD2 LEU A 461 38.999 39.831 9.916 1.00 14.29 C ANISOU 2332 CD2 LEU A 461 1462 2378 1589 402 -203 -722 C ATOM 2333 N HIS A 462 35.759 41.553 13.872 1.00 23.24 N ANISOU 2333 N HIS A 462 2545 3646 2640 465 -234 -801 N ATOM 2334 CA HIS A 462 34.740 42.582 14.096 1.00 23.17 C ANISOU 2334 CA HIS A 462 2526 3666 2610 500 -253 -836 C ATOM 2335 C HIS A 462 34.606 43.103 15.537 1.00 26.35 C ANISOU 2335 C HIS A 462 2922 4093 2998 510 -261 -850 C ATOM 2336 O HIS A 462 33.855 44.046 15.799 1.00 31.74 O ANISOU 2336 O HIS A 462 3597 4796 3667 541 -278 -882 O ATOM 2337 CB HIS A 462 33.377 42.102 13.579 1.00 17.07 C ANISOU 2337 CB HIS A 462 1726 2936 1822 501 -244 -860 C ATOM 2338 CG HIS A 462 33.367 41.775 12.119 1.00 18.90 C ANISOU 2338 CG HIS A 462 1964 3151 2065 496 -240 -853 C ATOM 2339 ND1 HIS A 462 33.346 42.744 11.139 1.00 18.48 N ANISOU 2339 ND1 HIS A 462 1925 3079 2016 522 -263 -859 N ATOM 2340 CD2 HIS A 462 33.365 40.585 11.471 1.00 19.63 C ANISOU 2340 CD2 HIS A 462 2049 3245 2167 466 -217 -841 C ATOM 2341 CE1 HIS A 462 33.331 42.166 9.951 1.00 17.63 C ANISOU 2341 CE1 HIS A 462 1819 2966 1916 507 -253 -850 C ATOM 2342 NE2 HIS A 462 33.350 40.856 10.124 1.00 18.55 N ANISOU 2342 NE2 HIS A 462 1921 3092 2035 474 -225 -841 N ATOM 2343 N ALA A 463 35.319 42.502 16.476 1.00 22.47 N ANISOU 2343 N ALA A 463 2431 3597 2507 483 -248 -828 N ATOM 2344 CA ALA A 463 35.232 42.982 17.846 1.00 23.43 C ANISOU 2344 CA ALA A 463 2546 3745 2612 490 -255 -842 C ATOM 2345 C ALA A 463 35.589 44.460 17.894 1.00 25.32 C ANISOU 2345 C ALA A 463 2805 3959 2855 525 -284 -857 C ATOM 2346 O ALA A 463 36.409 44.921 17.100 1.00 23.72 O ANISOU 2346 O ALA A 463 2630 3710 2674 534 -296 -839 O ATOM 2347 CB ALA A 463 36.147 42.184 18.766 1.00 17.15 C ANISOU 2347 CB ALA A 463 1753 2942 1821 455 -241 -808 C ATOM 2348 N PRO A 464 34.971 45.208 18.824 1.00 26.35 N ANISOU 2348 N PRO A 464 2922 4122 2965 546 -294 -890 N ATOM 2349 CA PRO A 464 35.434 46.574 19.101 1.00 30.42 C ANISOU 2349 CA PRO A 464 3457 4613 3487 577 -322 -904 C ATOM 2350 C PRO A 464 36.853 46.481 19.638 1.00 27.45 C ANISOU 2350 C PRO A 464 3104 4202 3123 556 -321 -869 C ATOM 2351 O PRO A 464 37.189 45.460 20.238 1.00 24.33 O ANISOU 2351 O PRO A 464 2701 3820 2723 522 -301 -846 O ATOM 2352 CB PRO A 464 34.510 47.050 20.228 1.00 28.66 C ANISOU 2352 CB PRO A 464 3210 4442 3239 592 -325 -946 C ATOM 2353 CG PRO A 464 33.408 46.058 20.310 1.00 30.94 C ANISOU 2353 CG PRO A 464 3466 4783 3508 575 -302 -957 C ATOM 2354 CD PRO A 464 33.928 44.769 19.762 1.00 26.09 C ANISOU 2354 CD PRO A 464 2857 4152 2905 538 -280 -915 C ATOM 2355 N LEU A 465 37.660 47.521 19.455 1.00 31.08 N ANISOU 2355 N LEU A 465 3591 4619 3600 576 -344 -865 N ATOM 2356 CA LEU A 465 39.078 47.458 19.828 1.00 34.89 C ANISOU 2356 CA LEU A 465 4096 5064 4096 557 -345 -830 C ATOM 2357 C LEU A 465 39.364 47.036 21.281 1.00 35.00 C ANISOU 2357 C LEU A 465 4099 5107 4092 533 -334 -825 C ATOM 2358 O LEU A 465 40.257 46.227 21.531 1.00 36.28 O ANISOU 2358 O LEU A 465 4267 5255 4263 502 -321 -788 O ATOM 2359 CB LEU A 465 39.801 48.763 19.474 1.00 35.71 C ANISOU 2359 CB LEU A 465 4229 5121 4217 583 -374 -831 C ATOM 2360 CG LEU A 465 39.782 49.111 17.982 1.00 41.39 C ANISOU 2360 CG LEU A 465 4964 5807 4955 598 -386 -824 C ATOM 2361 CD1 LEU A 465 40.948 50.022 17.619 1.00 45.43 C ANISOU 2361 CD1 LEU A 465 5508 6264 5488 607 -409 -804 C ATOM 2362 CD2 LEU A 465 39.819 47.854 17.138 1.00 42.94 C ANISOU 2362 CD2 LEU A 465 5155 6004 5157 570 -361 -798 C ATOM 2363 N GLU A 466 38.609 47.577 22.231 1.00 32.68 N ANISOU 2363 N GLU A 466 3787 4855 3775 548 -340 -862 N ATOM 2364 CA GLU A 466 38.792 47.251 23.642 1.00 29.87 C ANISOU 2364 CA GLU A 466 3418 4534 3398 525 -331 -861 C ATOM 2365 C GLU A 466 38.597 45.756 23.862 1.00 26.98 C ANISOU 2365 C GLU A 466 3032 4196 3022 485 -303 -834 C ATOM 2366 O GLU A 466 39.377 45.103 24.562 1.00 31.41 O ANISOU 2366 O GLU A 466 3595 4755 3582 454 -294 -801 O ATOM 2367 CB GLU A 466 37.820 48.073 24.504 1.00 37.02 C ANISOU 2367 CB GLU A 466 4302 5486 4277 549 -340 -913 C ATOM 2368 CG GLU A 466 37.751 47.685 25.976 1.00 51.91 C ANISOU 2368 CG GLU A 466 6168 7424 6133 524 -328 -918 C ATOM 2369 CD GLU A 466 36.550 48.317 26.703 1.00 65.06 C ANISOU 2369 CD GLU A 466 7804 9146 7769 546 -331 -976 C ATOM 2370 OE1 GLU A 466 36.076 49.396 26.275 1.00 66.25 O ANISOU 2370 OE1 GLU A 466 7958 9285 7928 587 -350 -1015 O ATOM 2371 OE2 GLU A 466 36.075 47.729 27.702 1.00 68.74 O ANISOU 2371 OE2 GLU A 466 8244 9670 8203 521 -315 -984 O ATOM 2372 N LEU A 467 37.564 45.200 23.249 1.00 24.49 N ANISOU 2372 N LEU A 467 2698 3905 2702 486 -291 -846 N ATOM 2373 CA LEU A 467 37.323 43.767 23.373 1.00 29.86 C ANISOU 2373 CA LEU A 467 3360 4610 3376 448 -265 -822 C ATOM 2374 C LEU A 467 38.374 42.957 22.589 1.00 27.53 C ANISOU 2374 C LEU A 467 3084 4264 3113 425 -257 -774 C ATOM 2375 O LEU A 467 38.777 41.865 23.005 1.00 23.02 O ANISOU 2375 O LEU A 467 2506 3695 2546 389 -241 -741 O ATOM 2376 CB LEU A 467 35.907 43.436 22.902 1.00 34.27 C ANISOU 2376 CB LEU A 467 3893 5209 3921 456 -255 -851 C ATOM 2377 CG LEU A 467 35.117 42.376 23.667 1.00 46.79 C ANISOU 2377 CG LEU A 467 5445 6851 5480 424 -233 -850 C ATOM 2378 CD1 LEU A 467 35.367 42.469 25.167 1.00 49.34 C ANISOU 2378 CD1 LEU A 467 5759 7208 5778 407 -233 -849 C ATOM 2379 CD2 LEU A 467 33.622 42.513 23.356 1.00 47.39 C ANISOU 2379 CD2 LEU A 467 5495 6974 5537 443 -230 -893 C ATOM 2380 N LEU A 468 38.817 43.495 21.454 1.00 23.70 N ANISOU 2380 N LEU A 468 2622 3731 2652 446 -269 -772 N ATOM 2381 CA LEU A 468 39.810 42.803 20.636 1.00 21.02 C ANISOU 2381 CA LEU A 468 2299 3344 2343 427 -261 -732 C ATOM 2382 C LEU A 468 41.114 42.677 21.413 1.00 21.59 C ANISOU 2382 C LEU A 468 2386 3391 2426 407 -263 -699 C ATOM 2383 O LEU A 468 41.813 41.668 21.319 1.00 23.82 O ANISOU 2383 O LEU A 468 2669 3654 2728 377 -249 -663 O ATOM 2384 CB LEU A 468 40.029 43.524 19.301 1.00 16.58 C ANISOU 2384 CB LEU A 468 1758 2741 1799 452 -274 -737 C ATOM 2385 CG LEU A 468 41.181 43.007 18.437 1.00 19.73 C ANISOU 2385 CG LEU A 468 2176 3090 2229 435 -268 -701 C ATOM 2386 CD1 LEU A 468 40.950 41.556 18.040 1.00 17.89 C ANISOU 2386 CD1 LEU A 468 1927 2866 2005 405 -242 -685 C ATOM 2387 CD2 LEU A 468 41.405 43.872 17.203 1.00 21.16 C ANISOU 2387 CD2 LEU A 468 2379 3238 2424 459 -284 -706 C ATOM 2388 N ALA A 469 41.424 43.694 22.211 1.00 21.09 N ANISOU 2388 N ALA A 469 2332 3331 2352 422 -281 -711 N ATOM 2389 CA ALA A 469 42.615 43.653 23.042 1.00 22.52 C ANISOU 2389 CA ALA A 469 2524 3492 2539 404 -285 -681 C ATOM 2390 C ALA A 469 42.530 42.513 24.048 1.00 21.37 C ANISOU 2390 C ALA A 469 2357 3381 2380 366 -267 -660 C ATOM 2391 O ALA A 469 43.517 41.803 24.282 1.00 19.09 O ANISOU 2391 O ALA A 469 2075 3069 2111 339 -262 -620 O ATOM 2392 CB ALA A 469 42.832 44.988 23.748 1.00 17.77 C ANISOU 2392 CB ALA A 469 1934 2892 1924 428 -307 -705 C ATOM 2393 N GLU A 470 41.349 42.327 24.633 1.00 19.82 N ANISOU 2393 N GLU A 470 2135 3241 2154 364 -260 -686 N ATOM 2394 CA GLU A 470 41.146 41.225 25.575 1.00 22.04 C ANISOU 2394 CA GLU A 470 2393 3560 2421 326 -244 -665 C ATOM 2395 C GLU A 470 41.326 39.880 24.892 1.00 20.24 C ANISOU 2395 C GLU A 470 2161 3311 2220 299 -226 -630 C ATOM 2396 O GLU A 470 41.954 38.968 25.452 1.00 23.40 O ANISOU 2396 O GLU A 470 2555 3705 2629 265 -219 -591 O ATOM 2397 CB GLU A 470 39.763 41.296 26.229 1.00 25.82 C ANISOU 2397 CB GLU A 470 2842 4107 2860 329 -238 -702 C ATOM 2398 CG GLU A 470 39.633 42.384 27.266 1.00 33.77 C ANISOU 2398 CG GLU A 470 3847 5146 3839 345 -252 -733 C ATOM 2399 CD GLU A 470 38.260 42.379 27.916 1.00 45.62 C ANISOU 2399 CD GLU A 470 5315 6717 5300 346 -244 -772 C ATOM 2400 OE1 GLU A 470 37.716 43.479 28.178 1.00 50.97 O ANISOU 2400 OE1 GLU A 470 5988 7417 5960 377 -256 -819 O ATOM 2401 OE2 GLU A 470 37.723 41.272 28.150 1.00 44.30 O ANISOU 2401 OE2 GLU A 470 5125 6584 5122 315 -227 -756 O ATOM 2402 N MET A 471 40.775 39.760 23.685 1.00 16.83 N ANISOU 2402 N MET A 471 1729 2866 1800 313 -220 -645 N ATOM 2403 CA MET A 471 40.909 38.528 22.899 1.00 18.76 C ANISOU 2403 CA MET A 471 1968 3088 2071 290 -203 -619 C ATOM 2404 C MET A 471 42.379 38.245 22.616 1.00 19.28 C ANISOU 2404 C MET A 471 2055 3096 2174 278 -206 -580 C ATOM 2405 O MET A 471 42.852 37.137 22.857 1.00 21.49 O ANISOU 2405 O MET A 471 2327 3364 2472 246 -195 -545 O ATOM 2406 CB MET A 471 40.128 38.610 21.582 1.00 14.22 C ANISOU 2406 CB MET A 471 1393 2510 1503 310 -199 -645 C ATOM 2407 CG MET A 471 38.611 38.701 21.760 1.00 17.69 C ANISOU 2407 CG MET A 471 1807 3006 1909 320 -194 -682 C ATOM 2408 SD MET A 471 37.731 38.881 20.191 1.00 21.18 S ANISOU 2408 SD MET A 471 2247 3443 2357 345 -192 -712 S ATOM 2409 CE MET A 471 38.006 37.272 19.450 1.00 20.77 C ANISOU 2409 CE MET A 471 2189 3368 2336 308 -169 -680 C ATOM 2410 N MET A 472 43.096 39.257 22.127 1.00 15.12 N ANISOU 2410 N MET A 472 1554 2534 1658 303 -221 -585 N ATOM 2411 CA MET A 472 44.525 39.124 21.828 1.00 12.89 C ANISOU 2411 CA MET A 472 1291 2198 1409 294 -224 -551 C ATOM 2412 C MET A 472 45.284 38.730 23.088 1.00 18.25 C ANISOU 2412 C MET A 472 1966 2879 2087 268 -226 -519 C ATOM 2413 O MET A 472 46.157 37.857 23.054 1.00 20.11 O ANISOU 2413 O MET A 472 2203 3085 2353 243 -220 -482 O ATOM 2414 CB MET A 472 45.090 40.428 21.261 1.00 10.55 C ANISOU 2414 CB MET A 472 1022 1870 1118 325 -243 -564 C ATOM 2415 CG MET A 472 44.611 40.763 19.858 1.00 17.09 C ANISOU 2415 CG MET A 472 1856 2684 1951 347 -243 -586 C ATOM 2416 SD MET A 472 45.443 39.782 18.571 1.00 21.59 S ANISOU 2416 SD MET A 472 2433 3208 2563 328 -227 -559 S ATOM 2417 CE MET A 472 44.426 40.180 17.153 1.00 13.72 C ANISOU 2417 CE MET A 472 1436 2219 1558 352 -226 -592 C ATOM 2418 N ASP A 473 44.925 39.355 24.206 1.00 17.66 N ANISOU 2418 N ASP A 473 1887 2844 1980 272 -236 -533 N ATOM 2419 CA ASP A 473 45.596 39.081 25.470 1.00 24.10 C ANISOU 2419 CA ASP A 473 2698 3669 2789 247 -240 -504 C ATOM 2420 C ASP A 473 45.296 37.664 25.963 1.00 23.68 C ANISOU 2420 C ASP A 473 2621 3638 2739 209 -225 -476 C ATOM 2421 O ASP A 473 46.150 37.035 26.602 1.00 17.20 O ANISOU 2421 O ASP A 473 1799 2804 1932 181 -226 -435 O ATOM 2422 CB ASP A 473 45.200 40.109 26.538 1.00 31.33 C ANISOU 2422 CB ASP A 473 3612 4628 3666 260 -253 -532 C ATOM 2423 CG ASP A 473 45.879 41.471 26.344 1.00 39.29 C ANISOU 2423 CG ASP A 473 4647 5605 4678 290 -273 -548 C ATOM 2424 OD1 ASP A 473 45.699 42.335 27.228 1.00 43.08 O ANISOU 2424 OD1 ASP A 473 5126 6113 5130 301 -285 -571 O ATOM 2425 OD2 ASP A 473 46.584 41.690 25.328 1.00 40.77 O ANISOU 2425 OD2 ASP A 473 4855 5742 4896 303 -277 -539 O ATOM 2426 N GLU A 474 44.089 37.168 25.667 1.00 17.90 N ANISOU 2426 N GLU A 474 1869 2939 1994 206 -211 -495 N ATOM 2427 CA GLU A 474 43.714 35.809 26.049 1.00 13.76 C ANISOU 2427 CA GLU A 474 1321 2434 1472 169 -197 -469 C ATOM 2428 C GLU A 474 44.572 34.782 25.310 1.00 16.94 C ANISOU 2428 C GLU A 474 1729 2782 1925 152 -189 -433 C ATOM 2429 O GLU A 474 44.994 33.798 25.888 1.00 21.86 O ANISOU 2429 O GLU A 474 2342 3400 2565 119 -186 -394 O ATOM 2430 CB GLU A 474 42.230 35.533 25.777 1.00 16.89 C ANISOU 2430 CB GLU A 474 1696 2875 1846 172 -184 -501 C ATOM 2431 CG GLU A 474 41.833 34.073 26.025 1.00 20.05 C ANISOU 2431 CG GLU A 474 2073 3291 2256 132 -169 -473 C ATOM 2432 CD GLU A 474 40.321 33.835 26.058 1.00 22.75 C ANISOU 2432 CD GLU A 474 2390 3690 2566 130 -158 -503 C ATOM 2433 OE1 GLU A 474 39.557 34.791 26.321 1.00 19.75 O ANISOU 2433 OE1 GLU A 474 2005 3350 2149 154 -163 -543 O ATOM 2434 OE2 GLU A 474 39.900 32.677 25.828 1.00 26.65 O ANISOU 2434 OE2 GLU A 474 2867 4186 3074 104 -144 -487 O ATOM 2435 N ILE A 475 44.831 35.005 24.027 1.00 18.52 N ANISOU 2435 N ILE A 475 1943 2941 2151 173 -186 -446 N ATOM 2436 CA ILE A 475 45.654 34.062 23.280 1.00 17.15 C ANISOU 2436 CA ILE A 475 1773 2717 2025 157 -177 -417 C ATOM 2437 C ILE A 475 47.114 34.122 23.744 1.00 25.03 C ANISOU 2437 C ILE A 475 2785 3677 3048 148 -188 -381 C ATOM 2438 O ILE A 475 47.729 33.086 24.016 1.00 25.56 O ANISOU 2438 O ILE A 475 2843 3722 3145 120 -184 -344 O ATOM 2439 CB ILE A 475 45.574 34.304 21.770 1.00 15.99 C ANISOU 2439 CB ILE A 475 1637 2542 1896 180 -171 -442 C ATOM 2440 CG1 ILE A 475 44.118 34.181 21.281 1.00 19.84 C ANISOU 2440 CG1 ILE A 475 2109 3067 2361 188 -161 -476 C ATOM 2441 CG2 ILE A 475 46.528 33.360 21.036 1.00 16.43 C ANISOU 2441 CG2 ILE A 475 1695 2545 2002 164 -162 -415 C ATOM 2442 CD1 ILE A 475 43.435 32.849 21.619 1.00 11.52 C ANISOU 2442 CD1 ILE A 475 1029 2037 1312 155 -145 -463 C ATOM 2443 N PHE A 476 47.652 35.337 23.860 1.00 19.00 N ANISOU 2443 N PHE A 476 2042 2905 2271 172 -204 -392 N ATOM 2444 CA PHE A 476 49.063 35.517 24.198 1.00 22.32 C ANISOU 2444 CA PHE A 476 2478 3288 2715 166 -215 -361 C ATOM 2445 C PHE A 476 49.423 35.187 25.655 1.00 24.30 C ANISOU 2445 C PHE A 476 2718 3560 2954 139 -223 -329 C ATOM 2446 O PHE A 476 50.519 34.685 25.922 1.00 21.13 O ANISOU 2446 O PHE A 476 2320 3126 2584 121 -227 -290 O ATOM 2447 CB PHE A 476 49.513 36.942 23.866 1.00 18.47 C ANISOU 2447 CB PHE A 476 2016 2785 2217 198 -230 -383 C ATOM 2448 CG PHE A 476 49.481 37.264 22.396 1.00 19.01 C ANISOU 2448 CG PHE A 476 2097 2824 2301 220 -225 -405 C ATOM 2449 CD1 PHE A 476 50.175 36.474 21.483 1.00 13.91 C ANISOU 2449 CD1 PHE A 476 1452 2137 1698 209 -213 -387 C ATOM 2450 CD2 PHE A 476 48.787 38.374 21.927 1.00 15.78 C ANISOU 2450 CD2 PHE A 476 1698 2430 1868 251 -232 -443 C ATOM 2451 CE1 PHE A 476 50.159 36.778 20.121 1.00 12.94 C ANISOU 2451 CE1 PHE A 476 1340 1992 1586 227 -209 -407 C ATOM 2452 CE2 PHE A 476 48.765 38.682 20.568 1.00 14.67 C ANISOU 2452 CE2 PHE A 476 1569 2265 1740 269 -230 -460 C ATOM 2453 CZ PHE A 476 49.454 37.885 19.668 1.00 12.41 C ANISOU 2453 CZ PHE A 476 1284 1941 1491 256 -217 -441 C ATOM 2454 N ASP A 477 48.504 35.461 26.584 1.00 25.81 N ANISOU 2454 N ASP A 477 2898 3807 3102 136 -226 -344 N ATOM 2455 CA ASP A 477 48.817 35.421 28.019 1.00 32.65 C ANISOU 2455 CA ASP A 477 3757 4703 3948 113 -236 -319 C ATOM 2456 C ASP A 477 47.791 34.659 28.845 1.00 32.41 C ANISOU 2456 C ASP A 477 3698 4726 3888 85 -228 -313 C ATOM 2457 O ASP A 477 47.985 34.458 30.043 1.00 29.48 O ANISOU 2457 O ASP A 477 3318 4384 3499 60 -236 -288 O ATOM 2458 CB ASP A 477 48.900 36.842 28.595 1.00 36.78 C ANISOU 2458 CB ASP A 477 4294 5247 4436 136 -252 -346 C ATOM 2459 CG ASP A 477 50.183 37.559 28.228 1.00 44.03 C ANISOU 2459 CG ASP A 477 5237 6113 5377 151 -264 -337 C ATOM 2460 OD1 ASP A 477 51.265 36.962 28.377 1.00 47.68 O ANISOU 2460 OD1 ASP A 477 5703 6542 5872 132 -267 -295 O ATOM 2461 OD2 ASP A 477 50.109 38.734 27.808 1.00 50.24 O ANISOU 2461 OD2 ASP A 477 6041 6894 6153 183 -272 -371 O ATOM 2462 N GLY A 478 46.700 34.250 28.207 1.00 31.17 N ANISOU 2462 N GLY A 478 3529 4587 3728 89 -214 -336 N ATOM 2463 CA GLY A 478 45.543 33.731 28.918 1.00 28.38 C ANISOU 2463 CA GLY A 478 3150 4293 3341 68 -206 -341 C ATOM 2464 C GLY A 478 45.630 32.305 29.425 1.00 26.72 C ANISOU 2464 C GLY A 478 2920 4084 3149 24 -201 -294 C ATOM 2465 O GLY A 478 44.835 31.903 30.266 1.00 24.78 O ANISOU 2465 O GLY A 478 2653 3892 2872 -1 -197 -289 O ATOM 2466 N TYR A 479 46.594 31.542 28.923 1.00 27.42 N ANISOU 2466 N TYR A 479 3014 4114 3289 13 -200 -258 N ATOM 2467 CA TYR A 479 46.666 30.114 29.224 1.00 29.86 C ANISOU 2467 CA TYR A 479 3305 4415 3626 -27 -196 -214 C ATOM 2468 C TYR A 479 48.027 29.674 29.751 1.00 29.11 C ANISOU 2468 C TYR A 479 3214 4280 3566 -48 -209 -161 C ATOM 2469 O TYR A 479 49.073 30.184 29.339 1.00 24.97 O ANISOU 2469 O TYR A 479 2710 3712 3066 -28 -216 -159 O ATOM 2470 CB TYR A 479 46.310 29.285 27.983 1.00 25.78 C ANISOU 2470 CB TYR A 479 2782 3864 3148 -25 -180 -223 C ATOM 2471 CG TYR A 479 44.918 29.540 27.462 1.00 17.54 C ANISOU 2471 CG TYR A 479 1730 2860 2073 -9 -167 -269 C ATOM 2472 CD1 TYR A 479 43.837 28.815 27.933 1.00 14.93 C ANISOU 2472 CD1 TYR A 479 1375 2576 1721 -35 -159 -266 C ATOM 2473 CD2 TYR A 479 44.691 30.510 26.496 1.00 18.74 C ANISOU 2473 CD2 TYR A 479 1898 3005 2217 31 -164 -315 C ATOM 2474 CE1 TYR A 479 42.558 29.049 27.452 1.00 22.76 C ANISOU 2474 CE1 TYR A 479 2358 3606 2685 -21 -147 -310 C ATOM 2475 CE2 TYR A 479 43.433 30.751 26.012 1.00 22.58 C ANISOU 2475 CE2 TYR A 479 2376 3527 2677 46 -154 -356 C ATOM 2476 CZ TYR A 479 42.367 30.020 26.488 1.00 22.70 C ANISOU 2476 CZ TYR A 479 2366 3589 2671 21 -145 -355 C ATOM 2477 OH TYR A 479 41.114 30.276 25.993 1.00 17.81 O ANISOU 2477 OH TYR A 479 1736 3005 2025 36 -135 -397 O ATOM 2478 N ILE A 480 48.011 28.715 30.668 1.00 31.26 N ANISOU 2478 N ILE A 480 3467 4569 3840 -88 -214 -117 N ATOM 2479 CA ILE A 480 49.259 28.198 31.215 1.00 26.69 C ANISOU 2479 CA ILE A 480 2889 3954 3296 -110 -228 -63 C ATOM 2480 C ILE A 480 49.847 27.199 30.220 1.00 20.69 C ANISOU 2480 C ILE A 480 2129 3126 2606 -112 -221 -44 C ATOM 2481 O ILE A 480 49.138 26.311 29.736 1.00 24.72 O ANISOU 2481 O ILE A 480 2625 3633 3135 -124 -209 -47 O ATOM 2482 CB ILE A 480 49.054 27.533 32.611 1.00 45.93 C ANISOU 2482 CB ILE A 480 5306 6435 5711 -155 -238 -18 C ATOM 2483 CG1 ILE A 480 48.612 28.565 33.656 1.00 43.78 C ANISOU 2483 CG1 ILE A 480 5033 6231 5369 -154 -245 -38 C ATOM 2484 CG2 ILE A 480 50.336 26.835 33.076 1.00 45.84 C ANISOU 2484 CG2 ILE A 480 5293 6379 5745 -180 -255 43 C ATOM 2485 CD1 ILE A 480 47.157 28.969 33.569 1.00 47.75 C ANISOU 2485 CD1 ILE A 480 5526 6793 5823 -143 -231 -88 C ATOM 2486 N PRO A 481 51.137 27.354 29.896 1.00 24.98 N ANISOU 2486 N PRO A 481 2686 3614 3189 -101 -229 -29 N ATOM 2487 CA PRO A 481 51.847 26.426 29.008 1.00 26.17 C ANISOU 2487 CA PRO A 481 2835 3699 3410 -103 -224 -11 C ATOM 2488 C PRO A 481 51.869 25.006 29.568 1.00 30.32 C ANISOU 2488 C PRO A 481 3337 4214 3970 -144 -229 39 C ATOM 2489 O PRO A 481 51.782 24.827 30.787 1.00 26.13 O ANISOU 2489 O PRO A 481 2796 3718 3413 -173 -242 75 O ATOM 2490 CB PRO A 481 53.268 26.994 28.968 1.00 25.42 C ANISOU 2490 CB PRO A 481 2758 3563 3339 -89 -236 2 C ATOM 2491 CG PRO A 481 53.109 28.444 29.310 1.00 30.91 C ANISOU 2491 CG PRO A 481 3471 4296 3976 -65 -242 -29 C ATOM 2492 CD PRO A 481 51.989 28.484 30.308 1.00 32.21 C ANISOU 2492 CD PRO A 481 3623 4531 4087 -84 -243 -31 C ATOM 2493 N HIS A 482 51.978 24.013 28.686 1.00 31.12 N ANISOU 2493 N HIS A 482 3429 4267 4128 -148 -219 43 N ATOM 2494 CA HIS A 482 52.030 22.614 29.114 1.00 34.18 C ANISOU 2494 CA HIS A 482 3794 4635 4558 -186 -225 91 C ATOM 2495 C HIS A 482 53.178 22.390 30.102 1.00 31.65 C ANISOU 2495 C HIS A 482 3471 4295 4259 -206 -248 148 C ATOM 2496 O HIS A 482 54.311 22.813 29.861 1.00 30.04 O ANISOU 2496 O HIS A 482 3280 4052 4080 -188 -254 151 O ATOM 2497 CB HIS A 482 52.169 21.670 27.913 1.00 31.93 C ANISOU 2497 CB HIS A 482 3502 4291 4339 -182 -211 80 C ATOM 2498 CG HIS A 482 52.102 20.220 28.276 1.00 39.02 C ANISOU 2498 CG HIS A 482 4376 5167 5284 -219 -217 125 C ATOM 2499 ND1 HIS A 482 53.170 19.538 28.819 1.00 41.72 N ANISOU 2499 ND1 HIS A 482 4709 5466 5677 -239 -235 178 N ATOM 2500 CD2 HIS A 482 51.093 19.319 28.175 1.00 41.00 C ANISOU 2500 CD2 HIS A 482 4608 5429 5540 -241 -208 125 C ATOM 2501 CE1 HIS A 482 52.824 18.282 29.038 1.00 40.45 C ANISOU 2501 CE1 HIS A 482 4526 5290 5553 -271 -239 211 C ATOM 2502 NE2 HIS A 482 51.569 18.122 28.653 1.00 42.12 N ANISOU 2502 NE2 HIS A 482 4732 5535 5738 -274 -222 179 N ATOM 2503 N PRO A 483 52.873 21.731 31.228 1.00 34.73 N ANISOU 2503 N PRO A 483 3844 4714 4637 -245 -261 194 N ATOM 2504 CA PRO A 483 53.788 21.504 32.359 1.00 32.87 C ANISOU 2504 CA PRO A 483 3603 4473 4412 -271 -287 254 C ATOM 2505 C PRO A 483 55.099 20.832 31.950 1.00 32.67 C ANISOU 2505 C PRO A 483 3576 4371 4468 -269 -296 285 C ATOM 2506 O PRO A 483 56.150 21.085 32.558 1.00 33.83 O ANISOU 2506 O PRO A 483 3728 4504 4624 -273 -315 318 O ATOM 2507 CB PRO A 483 52.998 20.555 33.263 1.00 35.45 C ANISOU 2507 CB PRO A 483 3907 4836 4726 -316 -294 295 C ATOM 2508 CG PRO A 483 51.561 20.779 32.899 1.00 39.22 C ANISOU 2508 CG PRO A 483 4382 5363 5158 -310 -274 247 C ATOM 2509 CD PRO A 483 51.549 21.118 31.442 1.00 35.08 C ANISOU 2509 CD PRO A 483 3871 4800 4657 -269 -253 192 C ATOM 2510 N ASP A 484 55.037 19.978 30.935 1.00 30.34 N ANISOU 2510 N ASP A 484 3272 4026 4230 -264 -283 273 N ATOM 2511 CA ASP A 484 56.219 19.240 30.506 1.00 30.88 C ANISOU 2511 CA ASP A 484 3334 4019 4380 -263 -291 298 C ATOM 2512 C ASP A 484 56.931 19.895 29.328 1.00 24.17 C ANISOU 2512 C ASP A 484 2500 3129 3552 -223 -276 253 C ATOM 2513 O ASP A 484 58.142 20.078 29.368 1.00 25.52 O ANISOU 2513 O ASP A 484 2676 3264 3755 -214 -288 270 O ATOM 2514 CB ASP A 484 55.865 17.791 30.152 1.00 35.27 C ANISOU 2514 CB ASP A 484 3867 4537 4996 -286 -287 316 C ATOM 2515 CG ASP A 484 55.256 17.030 31.321 1.00 41.04 C ANISOU 2515 CG ASP A 484 4579 5301 5713 -331 -304 369 C ATOM 2516 OD1 ASP A 484 55.590 17.331 32.495 1.00 37.25 O ANISOU 2516 OD1 ASP A 484 4100 4853 5202 -350 -325 411 O ATOM 2517 OD2 ASP A 484 54.440 16.119 31.053 1.00 46.94 O ANISOU 2517 OD2 ASP A 484 5311 6044 6480 -349 -296 369 O ATOM 2518 N THR A 485 56.187 20.257 28.288 1.00 18.35 N ANISOU 2518 N THR A 485 1772 2402 2797 -199 -253 196 N ATOM 2519 CA THR A 485 56.818 20.648 27.020 1.00 26.50 C ANISOU 2519 CA THR A 485 2816 3393 3860 -166 -238 154 C ATOM 2520 C THR A 485 57.043 22.147 26.867 1.00 25.82 C ANISOU 2520 C THR A 485 2756 3333 3722 -135 -236 122 C ATOM 2521 O THR A 485 57.942 22.571 26.146 1.00 24.52 O ANISOU 2521 O THR A 485 2602 3133 3581 -113 -232 105 O ATOM 2522 CB THR A 485 55.999 20.162 25.806 1.00 29.51 C ANISOU 2522 CB THR A 485 3191 3763 4258 -157 -213 109 C ATOM 2523 OG1 THR A 485 54.727 20.809 25.816 1.00 27.10 O ANISOU 2523 OG1 THR A 485 2894 3519 3885 -151 -203 76 O ATOM 2524 CG2 THR A 485 55.784 18.638 25.860 1.00 32.39 C ANISOU 2524 CG2 THR A 485 3530 4096 4681 -186 -215 138 C ATOM 2525 N GLY A 486 56.218 22.949 27.530 1.00 26.28 N ANISOU 2525 N GLY A 486 2823 3453 3709 -135 -238 111 N ATOM 2526 CA GLY A 486 56.280 24.392 27.368 1.00 25.21 C ANISOU 2526 CA GLY A 486 2712 3343 3523 -106 -237 76 C ATOM 2527 C GLY A 486 55.440 24.926 26.209 1.00 26.17 C ANISOU 2527 C GLY A 486 2844 3477 3623 -78 -216 17 C ATOM 2528 O GLY A 486 55.419 26.141 25.961 1.00 19.41 O ANISOU 2528 O GLY A 486 2008 2639 2727 -52 -215 -15 O ATOM 2529 N LYS A 487 54.763 24.030 25.487 1.00 26.82 N ANISOU 2529 N LYS A 487 2912 3548 3731 -85 -200 3 N ATOM 2530 CA LYS A 487 53.820 24.447 24.446 1.00 27.50 C ANISOU 2530 CA LYS A 487 3004 3652 3792 -63 -180 -51 C ATOM 2531 C LYS A 487 52.780 25.372 25.047 1.00 25.05 C ANISOU 2531 C LYS A 487 2701 3407 3408 -57 -183 -71 C ATOM 2532 O LYS A 487 52.234 25.089 26.108 1.00 26.04 O ANISOU 2532 O LYS A 487 2816 3571 3508 -80 -191 -47 O ATOM 2533 CB LYS A 487 53.082 23.253 23.838 1.00 31.89 C ANISOU 2533 CB LYS A 487 3540 4196 4380 -79 -165 -59 C ATOM 2534 CG LYS A 487 53.833 22.508 22.762 1.00 38.88 C ANISOU 2534 CG LYS A 487 4419 5020 5333 -75 -155 -66 C ATOM 2535 CD LYS A 487 52.907 21.525 22.065 1.00 39.26 C ANISOU 2535 CD LYS A 487 4450 5065 5402 -86 -137 -86 C ATOM 2536 CE LYS A 487 53.632 20.763 20.971 1.00 35.66 C ANISOU 2536 CE LYS A 487 3985 4550 5015 -83 -125 -98 C ATOM 2537 NZ LYS A 487 52.772 19.676 20.425 1.00 32.95 N ANISOU 2537 NZ LYS A 487 3623 4201 4698 -99 -111 -113 N ATOM 2538 N ASP A 488 52.496 26.473 24.365 1.00 16.26 N ANISOU 2538 N ASP A 488 1606 2309 2262 -25 -177 -115 N ATOM 2539 CA ASP A 488 51.447 27.363 24.816 1.00 13.78 C ANISOU 2539 CA ASP A 488 1298 2054 1883 -15 -178 -140 C ATOM 2540 C ASP A 488 50.272 27.375 23.821 1.00 19.34 C ANISOU 2540 C ASP A 488 1999 2778 2572 -1 -160 -186 C ATOM 2541 O ASP A 488 50.248 26.612 22.846 1.00 21.23 O ANISOU 2541 O ASP A 488 2231 2986 2850 -3 -146 -195 O ATOM 2542 CB ASP A 488 52.002 28.775 25.087 1.00 14.71 C ANISOU 2542 CB ASP A 488 1439 2181 1968 9 -191 -152 C ATOM 2543 CG ASP A 488 52.680 29.390 23.867 1.00 20.13 C ANISOU 2543 CG ASP A 488 2144 2828 2676 38 -186 -177 C ATOM 2544 OD1 ASP A 488 52.380 28.948 22.728 1.00 16.79 O ANISOU 2544 OD1 ASP A 488 1717 2385 2275 44 -170 -199 O ATOM 2545 OD2 ASP A 488 53.506 30.324 24.050 1.00 18.98 O ANISOU 2545 OD2 ASP A 488 2017 2672 2523 52 -198 -175 O ATOM 2546 N ALA A 489 49.290 28.223 24.086 1.00 17.90 N ANISOU 2546 N ALA A 489 1821 2647 2334 13 -161 -215 N ATOM 2547 CA ALA A 489 48.110 28.305 23.245 1.00 20.89 C ANISOU 2547 CA ALA A 489 2194 3049 2693 26 -146 -257 C ATOM 2548 C ALA A 489 48.495 28.615 21.797 1.00 21.94 C ANISOU 2548 C ALA A 489 2342 3144 2851 51 -138 -285 C ATOM 2549 O ALA A 489 47.968 28.029 20.849 1.00 23.18 O ANISOU 2549 O ALA A 489 2490 3294 3025 50 -122 -304 O ATOM 2550 CB ALA A 489 47.174 29.354 23.784 1.00 19.70 C ANISOU 2550 CB ALA A 489 2048 2957 2482 42 -152 -285 C ATOM 2551 N LEU A 490 49.437 29.524 21.629 1.00 19.57 N ANISOU 2551 N LEU A 490 2062 2821 2552 71 -147 -286 N ATOM 2552 CA LEU A 490 49.854 29.922 20.293 1.00 18.94 C ANISOU 2552 CA LEU A 490 1997 2709 2491 92 -140 -310 C ATOM 2553 C LEU A 490 50.485 28.751 19.515 1.00 16.07 C ANISOU 2553 C LEU A 490 1623 2299 2186 77 -127 -299 C ATOM 2554 O LEU A 490 50.179 28.547 18.336 1.00 19.41 O ANISOU 2554 O LEU A 490 2043 2712 2620 84 -113 -326 O ATOM 2555 CB LEU A 490 50.788 31.121 20.394 1.00 18.11 C ANISOU 2555 CB LEU A 490 1915 2589 2375 113 -156 -309 C ATOM 2556 CG LEU A 490 51.184 31.845 19.121 1.00 24.87 C ANISOU 2556 CG LEU A 490 2790 3421 3238 137 -153 -335 C ATOM 2557 CD1 LEU A 490 49.943 32.262 18.333 1.00 28.88 C ANISOU 2557 CD1 LEU A 490 3297 3960 3715 155 -145 -375 C ATOM 2558 CD2 LEU A 490 52.037 33.053 19.493 1.00 19.32 C ANISOU 2558 CD2 LEU A 490 2110 2710 2521 154 -171 -329 C ATOM 2559 N ASP A 491 51.331 27.960 20.173 1.00 9.66 N ANISOU 2559 N ASP A 491 801 1459 1411 55 -132 -259 N ATOM 2560 CA ASP A 491 51.886 26.771 19.532 1.00 11.72 C ANISOU 2560 CA ASP A 491 1048 1674 1731 39 -121 -248 C ATOM 2561 C ASP A 491 50.767 25.810 19.106 1.00 19.40 C ANISOU 2561 C ASP A 491 2000 2660 2709 25 -105 -264 C ATOM 2562 O ASP A 491 50.783 25.236 18.005 1.00 19.94 O ANISOU 2562 O ASP A 491 2063 2704 2811 25 -89 -285 O ATOM 2563 CB ASP A 491 52.833 26.024 20.475 1.00 15.69 C ANISOU 2563 CB ASP A 491 1541 2148 2273 16 -132 -200 C ATOM 2564 CG ASP A 491 54.102 26.809 20.790 1.00 24.97 C ANISOU 2564 CG ASP A 491 2734 3302 3453 27 -146 -182 C ATOM 2565 OD1 ASP A 491 54.822 27.200 19.840 1.00 21.71 O ANISOU 2565 OD1 ASP A 491 2331 2859 3057 44 -141 -200 O ATOM 2566 OD2 ASP A 491 54.388 27.006 21.997 1.00 24.38 O ANISOU 2566 OD2 ASP A 491 2660 3240 3363 17 -163 -150 O ATOM 2567 N ILE A 492 49.810 25.608 20.004 1.00 12.18 N ANISOU 2567 N ILE A 492 1076 1787 1765 11 -109 -255 N ATOM 2568 CA ILE A 492 48.741 24.659 19.747 1.00 11.85 C ANISOU 2568 CA ILE A 492 1013 1760 1727 -6 -95 -265 C ATOM 2569 C ILE A 492 47.917 25.126 18.560 1.00 13.61 C ANISOU 2569 C ILE A 492 1241 2002 1927 15 -81 -315 C ATOM 2570 O ILE A 492 47.647 24.358 17.639 1.00 18.07 O ANISOU 2570 O ILE A 492 1795 2550 2521 9 -66 -332 O ATOM 2571 CB ILE A 492 47.855 24.469 20.994 1.00 12.64 C ANISOU 2571 CB ILE A 492 1101 1909 1792 -26 -103 -246 C ATOM 2572 CG1 ILE A 492 48.637 23.691 22.067 1.00 14.13 C ANISOU 2572 CG1 ILE A 492 1280 2075 2013 -55 -116 -191 C ATOM 2573 CG2 ILE A 492 46.556 23.723 20.633 1.00 12.48 C ANISOU 2573 CG2 ILE A 492 1062 1915 1765 -40 -88 -265 C ATOM 2574 CD1 ILE A 492 47.867 23.534 23.374 1.00 23.37 C ANISOU 2574 CD1 ILE A 492 2438 3296 3144 -79 -125 -167 C ATOM 2575 N MET A 493 47.537 26.400 18.577 1.00 13.47 N ANISOU 2575 N MET A 493 1241 2018 1861 41 -88 -338 N ATOM 2576 CA MET A 493 46.682 26.956 17.540 1.00 14.88 C ANISOU 2576 CA MET A 493 1424 2219 2012 62 -79 -382 C ATOM 2577 C MET A 493 47.364 27.020 16.171 1.00 18.79 C ANISOU 2577 C MET A 493 1927 2675 2536 74 -69 -401 C ATOM 2578 O MET A 493 46.751 26.661 15.180 1.00 18.80 O ANISOU 2578 O MET A 493 1921 2681 2541 75 -55 -429 O ATOM 2579 CB MET A 493 46.163 28.324 17.966 1.00 12.76 C ANISOU 2579 CB MET A 493 1170 1992 1687 87 -91 -399 C ATOM 2580 CG MET A 493 45.107 28.251 19.076 1.00 8.55 C ANISOU 2580 CG MET A 493 622 1510 1115 75 -95 -395 C ATOM 2581 SD MET A 493 44.848 29.887 19.773 1.00 19.78 S ANISOU 2581 SD MET A 493 2062 2973 2482 104 -113 -412 S ATOM 2582 CE MET A 493 43.856 30.636 18.457 1.00 8.64 C ANISOU 2582 CE MET A 493 657 1581 1047 136 -107 -464 C ATOM 2583 N MET A 494 48.629 27.449 16.130 1.00 17.00 N ANISOU 2583 N MET A 494 1716 2413 2329 82 -77 -387 N ATOM 2584 CA MET A 494 49.387 27.516 14.879 1.00 15.91 C ANISOU 2584 CA MET A 494 1585 2240 2218 91 -68 -403 C ATOM 2585 C MET A 494 49.433 26.210 14.109 1.00 19.41 C ANISOU 2585 C MET A 494 2008 2656 2709 72 -49 -410 C ATOM 2586 O MET A 494 49.512 26.233 12.882 1.00 23.18 O ANISOU 2586 O MET A 494 2487 3124 3195 79 -37 -439 O ATOM 2587 CB MET A 494 50.840 27.945 15.122 1.00 14.88 C ANISOU 2587 CB MET A 494 1470 2074 2110 96 -79 -380 C ATOM 2588 CG MET A 494 51.019 29.414 15.405 1.00 21.62 C ANISOU 2588 CG MET A 494 2347 2944 2922 120 -96 -383 C ATOM 2589 SD MET A 494 52.768 29.815 15.469 1.00 26.04 S ANISOU 2589 SD MET A 494 2923 3459 3514 123 -105 -358 S ATOM 2590 CE MET A 494 53.388 28.551 16.578 1.00 32.33 C ANISOU 2590 CE MET A 494 3699 4230 4355 94 -108 -314 C ATOM 2591 N PHE A 495 49.426 25.082 14.816 1.00 12.68 N ANISOU 2591 N PHE A 495 1137 1791 1888 47 -48 -385 N ATOM 2592 CA PHE A 495 49.592 23.780 14.161 1.00 16.79 C ANISOU 2592 CA PHE A 495 1638 2279 2463 28 -31 -389 C ATOM 2593 C PHE A 495 48.328 22.926 14.183 1.00 18.92 C ANISOU 2593 C PHE A 495 1887 2572 2728 11 -22 -400 C ATOM 2594 O PHE A 495 48.343 21.751 13.792 1.00 19.11 O ANISOU 2594 O PHE A 495 1893 2570 2799 -8 -10 -402 O ATOM 2595 CB PHE A 495 50.766 22.997 14.772 1.00 11.76 C ANISOU 2595 CB PHE A 495 992 1594 1882 12 -38 -351 C ATOM 2596 CG PHE A 495 52.103 23.607 14.493 1.00 15.50 C ANISOU 2596 CG PHE A 495 1480 2036 2372 26 -43 -346 C ATOM 2597 CD1 PHE A 495 52.718 23.423 13.266 1.00 18.22 C ANISOU 2597 CD1 PHE A 495 1823 2352 2749 31 -28 -372 C ATOM 2598 CD2 PHE A 495 52.750 24.372 15.453 1.00 16.50 C ANISOU 2598 CD2 PHE A 495 1623 2165 2483 33 -62 -316 C ATOM 2599 CE1 PHE A 495 53.964 23.996 13.003 1.00 17.39 C ANISOU 2599 CE1 PHE A 495 1729 2219 2657 42 -33 -367 C ATOM 2600 CE2 PHE A 495 53.998 24.944 15.193 1.00 19.11 C ANISOU 2600 CE2 PHE A 495 1966 2467 2828 45 -67 -311 C ATOM 2601 CZ PHE A 495 54.597 24.759 13.964 1.00 13.73 C ANISOU 2601 CZ PHE A 495 1282 1757 2178 49 -52 -336 C ATOM 2602 N HIS A 496 47.231 23.519 14.624 1.00 13.50 N ANISOU 2602 N HIS A 496 1205 1937 1987 17 -27 -408 N ATOM 2603 CA HIS A 496 45.975 22.782 14.713 1.00 13.72 C ANISOU 2603 CA HIS A 496 1213 1994 2005 0 -18 -417 C ATOM 2604 C HIS A 496 45.180 22.860 13.403 1.00 16.67 C ANISOU 2604 C HIS A 496 1585 2385 2365 10 -2 -464 C ATOM 2605 O HIS A 496 45.168 23.896 12.732 1.00 14.26 O ANISOU 2605 O HIS A 496 1296 2094 2030 35 -3 -488 O ATOM 2606 CB HIS A 496 45.134 23.310 15.871 1.00 9.31 C ANISOU 2606 CB HIS A 496 656 1487 1396 0 -30 -405 C ATOM 2607 CG HIS A 496 43.947 22.459 16.165 1.00 15.24 C ANISOU 2607 CG HIS A 496 1385 2267 2140 -23 -23 -406 C ATOM 2608 ND1 HIS A 496 42.726 22.657 15.559 1.00 13.89 N ANISOU 2608 ND1 HIS A 496 1209 2136 1934 -15 -13 -443 N ATOM 2609 CD2 HIS A 496 43.805 21.372 16.963 1.00 8.76 C ANISOU 2609 CD2 HIS A 496 546 1440 1343 -55 -25 -374 C ATOM 2610 CE1 HIS A 496 41.871 21.747 15.996 1.00 14.16 C ANISOU 2610 CE1 HIS A 496 1221 2189 1970 -41 -8 -434 C ATOM 2611 NE2 HIS A 496 42.502 20.955 16.845 1.00 12.12 N ANISOU 2611 NE2 HIS A 496 956 1904 1747 -66 -15 -392 N ATOM 2612 N GLN A 497 44.518 21.766 13.040 1.00 17.32 N ANISOU 2612 N GLN A 497 1646 2466 2470 -10 12 -474 N ATOM 2613 CA GLN A 497 43.858 21.688 11.739 1.00 16.34 C ANISOU 2613 CA GLN A 497 1516 2354 2337 -5 28 -518 C ATOM 2614 C GLN A 497 42.841 22.813 11.547 1.00 15.69 C ANISOU 2614 C GLN A 497 1444 2326 2191 18 24 -544 C ATOM 2615 O GLN A 497 42.586 23.216 10.423 1.00 17.51 O ANISOU 2615 O GLN A 497 1680 2567 2408 31 31 -577 O ATOM 2616 CB GLN A 497 43.179 20.331 11.545 1.00 10.56 C ANISOU 2616 CB GLN A 497 759 1618 1637 -33 42 -525 C ATOM 2617 CG GLN A 497 42.183 20.029 12.635 1.00 19.19 C ANISOU 2617 CG GLN A 497 1839 2746 2705 -50 35 -505 C ATOM 2618 CD GLN A 497 41.524 18.667 12.479 1.00 26.75 C ANISOU 2618 CD GLN A 497 2772 3697 3695 -80 47 -508 C ATOM 2619 OE1 GLN A 497 41.392 18.146 11.368 1.00 25.21 O ANISOU 2619 OE1 GLN A 497 2568 3487 3522 -84 63 -540 O ATOM 2620 NE2 GLN A 497 41.087 18.094 13.597 1.00 26.85 N ANISOU 2620 NE2 GLN A 497 2772 3722 3707 -103 40 -476 N ATOM 2621 N PHE A 498 42.259 23.308 12.640 1.00 11.88 N ANISOU 2621 N PHE A 498 963 1879 1670 21 11 -528 N ATOM 2622 CA PHE A 498 41.307 24.411 12.569 1.00 15.45 C ANISOU 2622 CA PHE A 498 1423 2382 2064 44 5 -552 C ATOM 2623 C PHE A 498 41.889 25.687 13.196 1.00 19.03 C ANISOU 2623 C PHE A 498 1900 2839 2491 69 -14 -540 C ATOM 2624 O PHE A 498 41.636 26.802 12.729 1.00 15.59 O ANISOU 2624 O PHE A 498 1479 2424 2022 96 -21 -562 O ATOM 2625 CB PHE A 498 39.957 24.050 13.231 1.00 16.36 C ANISOU 2625 CB PHE A 498 1521 2546 2151 31 6 -555 C ATOM 2626 CG PHE A 498 39.340 22.764 12.728 1.00 18.63 C ANISOU 2626 CG PHE A 498 1784 2829 2464 5 23 -565 C ATOM 2627 CD1 PHE A 498 39.303 22.469 11.367 1.00 17.64 C ANISOU 2627 CD1 PHE A 498 1656 2689 2356 7 37 -596 C ATOM 2628 CD2 PHE A 498 38.776 21.857 13.619 1.00 22.91 C ANISOU 2628 CD2 PHE A 498 2306 3385 3012 -24 25 -544 C ATOM 2629 CE1 PHE A 498 38.736 21.280 10.907 1.00 19.28 C ANISOU 2629 CE1 PHE A 498 1843 2894 2590 -19 53 -608 C ATOM 2630 CE2 PHE A 498 38.198 20.669 13.171 1.00 17.89 C ANISOU 2630 CE2 PHE A 498 1650 2745 2403 -50 39 -553 C ATOM 2631 CZ PHE A 498 38.179 20.379 11.816 1.00 18.93 C ANISOU 2631 CZ PHE A 498 1780 2860 2554 -47 53 -586 C ATOM 2632 N GLY A 499 42.668 25.521 14.259 1.00 18.74 N ANISOU 2632 N GLY A 499 1866 2784 2470 58 -23 -503 N ATOM 2633 CA GLY A 499 43.277 26.650 14.942 1.00 15.99 C ANISOU 2633 CA GLY A 499 1537 2437 2099 77 -41 -490 C ATOM 2634 C GLY A 499 44.220 27.487 14.083 1.00 19.21 C ANISOU 2634 C GLY A 499 1968 2817 2515 100 -45 -500 C ATOM 2635 O GLY A 499 44.364 28.693 14.315 1.00 15.80 O ANISOU 2635 O GLY A 499 1554 2396 2053 124 -60 -503 O ATOM 2636 N ASN A 500 44.870 26.864 13.097 1.00 12.58 N ANISOU 2636 N ASN A 500 1126 1939 1716 93 -33 -505 N ATOM 2637 CA ASN A 500 45.813 27.598 12.254 1.00 11.48 C ANISOU 2637 CA ASN A 500 1005 1772 1583 110 -35 -513 C ATOM 2638 C ASN A 500 45.158 28.778 11.513 1.00 15.66 C ANISOU 2638 C ASN A 500 1549 2332 2069 137 -41 -544 C ATOM 2639 O ASN A 500 45.800 29.806 11.269 1.00 11.61 O ANISOU 2639 O ASN A 500 1057 1809 1546 156 -52 -544 O ATOM 2640 CB ASN A 500 46.511 26.662 11.266 1.00 11.59 C ANISOU 2640 CB ASN A 500 1010 1747 1647 95 -18 -519 C ATOM 2641 CG ASN A 500 45.649 26.347 10.054 1.00 13.82 C ANISOU 2641 CG ASN A 500 1282 2047 1922 94 -2 -556 C ATOM 2642 OD1 ASN A 500 45.650 27.099 9.070 1.00 12.82 O ANISOU 2642 OD1 ASN A 500 1168 1928 1776 110 -2 -579 O ATOM 2643 ND2 ASN A 500 44.902 25.230 10.116 1.00 8.72 N ANISOU 2643 ND2 ASN A 500 614 1408 1291 73 10 -561 N ATOM 2644 N TYR A 501 43.878 28.630 11.175 1.00 13.38 N ANISOU 2644 N TYR A 501 1248 2081 1756 138 -34 -569 N ATOM 2645 CA TYR A 501 43.139 29.672 10.456 1.00 14.42 C ANISOU 2645 CA TYR A 501 1389 2242 1848 163 -41 -597 C ATOM 2646 C TYR A 501 42.874 30.895 11.335 1.00 17.48 C ANISOU 2646 C TYR A 501 1790 2654 2197 186 -62 -594 C ATOM 2647 O TYR A 501 42.824 32.033 10.850 1.00 14.93 O ANISOU 2647 O TYR A 501 1484 2338 1852 211 -75 -608 O ATOM 2648 CB TYR A 501 41.814 29.108 9.939 1.00 10.94 C ANISOU 2648 CB TYR A 501 928 1835 1392 155 -29 -624 C ATOM 2649 CG TYR A 501 41.993 28.093 8.836 1.00 12.43 C ANISOU 2649 CG TYR A 501 1105 2004 1614 136 -8 -637 C ATOM 2650 CD1 TYR A 501 42.394 28.494 7.562 1.00 16.51 C ANISOU 2650 CD1 TYR A 501 1631 2509 2131 145 -5 -655 C ATOM 2651 CD2 TYR A 501 41.774 26.740 9.064 1.00 13.13 C ANISOU 2651 CD2 TYR A 501 1172 2085 1733 108 7 -632 C ATOM 2652 CE1 TYR A 501 42.573 27.578 6.537 1.00 17.41 C ANISOU 2652 CE1 TYR A 501 1732 2607 2274 126 14 -671 C ATOM 2653 CE2 TYR A 501 41.942 25.805 8.038 1.00 17.48 C ANISOU 2653 CE2 TYR A 501 1709 2615 2316 91 26 -648 C ATOM 2654 CZ TYR A 501 42.344 26.236 6.780 1.00 16.92 C ANISOU 2654 CZ TYR A 501 1648 2536 2244 100 30 -670 C ATOM 2655 OH TYR A 501 42.514 25.339 5.759 1.00 14.61 O ANISOU 2655 OH TYR A 501 1342 2227 1981 83 50 -690 O ATOM 2656 N VAL A 502 42.727 30.655 12.634 1.00 16.99 N ANISOU 2656 N VAL A 502 1721 2604 2130 177 -67 -575 N ATOM 2657 CA VAL A 502 42.474 31.729 13.587 1.00 17.06 C ANISOU 2657 CA VAL A 502 1739 2638 2104 197 -86 -574 C ATOM 2658 C VAL A 502 43.723 32.576 13.746 1.00 20.76 C ANISOU 2658 C VAL A 502 2232 3073 2581 209 -100 -557 C ATOM 2659 O VAL A 502 43.671 33.804 13.663 1.00 23.27 O ANISOU 2659 O VAL A 502 2567 3399 2874 236 -116 -569 O ATOM 2660 CB VAL A 502 42.009 31.182 14.943 1.00 12.94 C ANISOU 2660 CB VAL A 502 1202 2143 1573 179 -85 -558 C ATOM 2661 CG1 VAL A 502 41.953 32.300 15.989 1.00 12.37 C ANISOU 2661 CG1 VAL A 502 1139 2094 1467 197 -104 -557 C ATOM 2662 CG2 VAL A 502 40.632 30.518 14.788 1.00 16.37 C ANISOU 2662 CG2 VAL A 502 1612 2617 1992 168 -73 -578 C ATOM 2663 N VAL A 503 44.852 31.915 13.962 1.00 18.69 N ANISOU 2663 N VAL A 503 1972 2774 2357 191 -95 -529 N ATOM 2664 CA VAL A 503 46.128 32.621 14.032 1.00 16.50 C ANISOU 2664 CA VAL A 503 1716 2463 2091 200 -108 -512 C ATOM 2665 C VAL A 503 46.410 33.398 12.736 1.00 17.00 C ANISOU 2665 C VAL A 503 1796 2512 2152 219 -110 -531 C ATOM 2666 O VAL A 503 46.916 34.512 12.795 1.00 15.30 O ANISOU 2666 O VAL A 503 1602 2288 1924 238 -127 -528 O ATOM 2667 CB VAL A 503 47.300 31.670 14.346 1.00 10.82 C ANISOU 2667 CB VAL A 503 992 1702 1417 176 -101 -480 C ATOM 2668 CG1 VAL A 503 48.609 32.469 14.552 1.00 9.16 C ANISOU 2668 CG1 VAL A 503 803 1461 1215 186 -115 -461 C ATOM 2669 CG2 VAL A 503 46.974 30.838 15.578 1.00 7.91 C ANISOU 2669 CG2 VAL A 503 605 1349 1051 154 -99 -457 C ATOM 2670 N GLN A 504 46.083 32.827 11.574 1.00 15.52 N ANISOU 2670 N GLN A 504 1599 2323 1975 212 -95 -549 N ATOM 2671 CA GLN A 504 46.248 33.566 10.321 1.00 18.58 C ANISOU 2671 CA GLN A 504 2001 2704 2355 227 -98 -566 C ATOM 2672 C GLN A 504 45.397 34.839 10.370 1.00 19.34 C ANISOU 2672 C GLN A 504 2109 2832 2409 255 -117 -584 C ATOM 2673 O GLN A 504 45.824 35.908 9.937 1.00 16.67 O ANISOU 2673 O GLN A 504 1790 2482 2060 273 -132 -585 O ATOM 2674 CB GLN A 504 45.863 32.716 9.092 1.00 20.32 C ANISOU 2674 CB GLN A 504 2207 2927 2588 214 -77 -587 C ATOM 2675 CG GLN A 504 46.862 31.607 8.746 1.00 27.88 C ANISOU 2675 CG GLN A 504 3154 3846 3592 189 -59 -576 C ATOM 2676 CD GLN A 504 46.409 30.730 7.580 1.00 28.75 C ANISOU 2676 CD GLN A 504 3248 3962 3715 175 -38 -601 C ATOM 2677 OE1 GLN A 504 46.494 31.137 6.424 1.00 34.76 O ANISOU 2677 OE1 GLN A 504 4015 4725 4467 180 -35 -619 O ATOM 2678 NE2 GLN A 504 45.927 29.519 7.884 1.00 18.39 N ANISOU 2678 NE2 GLN A 504 1913 2652 2423 155 -23 -602 N ATOM 2679 N CYS A 505 44.185 34.698 10.895 1.00 16.38 N ANISOU 2679 N CYS A 505 1720 2494 2011 259 -116 -597 N ATOM 2680 CA CYS A 505 43.256 35.797 11.013 1.00 12.01 C ANISOU 2680 CA CYS A 505 1171 1972 1420 286 -134 -617 C ATOM 2681 C CYS A 505 43.832 36.900 11.907 1.00 15.24 C ANISOU 2681 C CYS A 505 1600 2373 1820 304 -156 -606 C ATOM 2682 O CYS A 505 43.800 38.079 11.543 1.00 17.84 O ANISOU 2682 O CYS A 505 1946 2701 2133 328 -174 -616 O ATOM 2683 CB CYS A 505 41.927 35.284 11.585 1.00 15.94 C ANISOU 2683 CB CYS A 505 1646 2513 1898 282 -126 -633 C ATOM 2684 SG CYS A 505 40.621 36.534 11.771 1.00 21.22 S ANISOU 2684 SG CYS A 505 2314 3226 2523 316 -146 -663 S ATOM 2685 N MET A 506 44.374 36.519 13.064 1.00 11.94 N ANISOU 2685 N MET A 506 1179 1947 1412 290 -155 -584 N ATOM 2686 CA MET A 506 44.968 37.492 13.982 1.00 8.68 C ANISOU 2686 CA MET A 506 783 1527 989 304 -175 -573 C ATOM 2687 C MET A 506 46.094 38.225 13.277 1.00 15.12 C ANISOU 2687 C MET A 506 1623 2303 1819 313 -185 -563 C ATOM 2688 O MET A 506 46.225 39.434 13.402 1.00 16.82 O ANISOU 2688 O MET A 506 1856 2515 2019 335 -206 -568 O ATOM 2689 CB MET A 506 45.540 36.790 15.229 1.00 8.50 C ANISOU 2689 CB MET A 506 752 1499 979 282 -170 -545 C ATOM 2690 CG MET A 506 44.498 36.118 16.130 1.00 11.95 C ANISOU 2690 CG MET A 506 1165 1977 1398 269 -162 -550 C ATOM 2691 SD MET A 506 45.262 34.960 17.291 1.00 20.50 S ANISOU 2691 SD MET A 506 2236 3048 2505 234 -154 -510 S ATOM 2692 CE MET A 506 46.320 36.056 18.248 1.00 18.34 C ANISOU 2692 CE MET A 506 1985 2760 2225 246 -176 -493 C ATOM 2693 N LEU A 507 46.923 37.480 12.545 1.00 15.75 N ANISOU 2693 N LEU A 507 1702 2353 1929 294 -171 -549 N ATOM 2694 CA LEU A 507 48.088 38.069 11.885 1.00 17.40 C ANISOU 2694 CA LEU A 507 1932 2525 2153 298 -178 -537 C ATOM 2695 C LEU A 507 47.639 39.126 10.893 1.00 20.70 C ANISOU 2695 C LEU A 507 2363 2950 2550 320 -192 -557 C ATOM 2696 O LEU A 507 48.110 40.259 10.915 1.00 22.02 O ANISOU 2696 O LEU A 507 2552 3104 2710 337 -213 -553 O ATOM 2697 CB LEU A 507 48.905 36.995 11.163 1.00 14.79 C ANISOU 2697 CB LEU A 507 1594 2167 1858 274 -158 -526 C ATOM 2698 CG LEU A 507 50.143 37.518 10.432 1.00 17.69 C ANISOU 2698 CG LEU A 507 1980 2501 2241 274 -163 -515 C ATOM 2699 CD1 LEU A 507 50.965 38.405 11.370 1.00 16.28 C ANISOU 2699 CD1 LEU A 507 1820 2306 2060 284 -183 -495 C ATOM 2700 CD2 LEU A 507 50.998 36.358 9.880 1.00 15.06 C ANISOU 2700 CD2 LEU A 507 1634 2141 1947 249 -141 -506 C ATOM 2701 N THR A 508 46.698 38.743 10.039 1.00 20.36 N ANISOU 2701 N THR A 508 2308 2929 2498 320 -182 -578 N ATOM 2702 CA THR A 508 46.220 39.601 8.960 1.00 21.69 C ANISOU 2702 CA THR A 508 2486 3106 2648 337 -194 -595 C ATOM 2703 C THR A 508 45.577 40.882 9.493 1.00 20.12 C ANISOU 2703 C THR A 508 2298 2923 2423 367 -221 -606 C ATOM 2704 O THR A 508 45.765 41.962 8.928 1.00 20.22 O ANISOU 2704 O THR A 508 2329 2925 2428 384 -241 -607 O ATOM 2705 CB THR A 508 45.239 38.835 8.034 1.00 24.95 C ANISOU 2705 CB THR A 508 2879 3545 3055 329 -177 -616 C ATOM 2706 OG1 THR A 508 45.935 37.735 7.428 1.00 26.66 O ANISOU 2706 OG1 THR A 508 3087 3743 3299 302 -153 -608 O ATOM 2707 CG2 THR A 508 44.674 39.754 6.935 1.00 21.11 C ANISOU 2707 CG2 THR A 508 2403 3071 2548 347 -192 -631 C ATOM 2708 N ILE A 509 44.826 40.756 10.583 1.00 17.03 N ANISOU 2708 N ILE A 509 1894 2558 2019 373 -221 -615 N ATOM 2709 CA ILE A 509 44.273 41.918 11.251 1.00 16.88 C ANISOU 2709 CA ILE A 509 1883 2554 1978 402 -245 -629 C ATOM 2710 C ILE A 509 45.400 42.874 11.631 1.00 19.04 C ANISOU 2710 C ILE A 509 2180 2793 2259 410 -265 -611 C ATOM 2711 O ILE A 509 45.322 44.063 11.356 1.00 21.06 O ANISOU 2711 O ILE A 509 2452 3042 2506 434 -289 -619 O ATOM 2712 CB ILE A 509 43.519 41.523 12.524 1.00 20.66 C ANISOU 2712 CB ILE A 509 2342 3065 2443 400 -239 -638 C ATOM 2713 CG1 ILE A 509 42.181 40.864 12.168 1.00 25.13 C ANISOU 2713 CG1 ILE A 509 2884 3670 2995 398 -226 -661 C ATOM 2714 CG2 ILE A 509 43.313 42.750 13.425 1.00 17.07 C ANISOU 2714 CG2 ILE A 509 1896 2619 1971 427 -264 -650 C ATOM 2715 CD1 ILE A 509 41.545 40.138 13.343 1.00 24.70 C ANISOU 2715 CD1 ILE A 509 2806 3648 2930 386 -213 -665 C ATOM 2716 N CYS A 510 46.450 42.345 12.255 1.00 15.23 N ANISOU 2716 N CYS A 510 1701 2290 1795 391 -256 -587 N ATOM 2717 CA CYS A 510 47.560 43.183 12.705 1.00 22.67 C ANISOU 2717 CA CYS A 510 2665 3202 2745 396 -273 -570 C ATOM 2718 C CYS A 510 48.311 43.833 11.546 1.00 24.23 C ANISOU 2718 C CYS A 510 2885 3370 2954 400 -284 -561 C ATOM 2719 O CYS A 510 48.654 45.013 11.606 1.00 26.03 O ANISOU 2719 O CYS A 510 3132 3581 3176 417 -308 -559 O ATOM 2720 CB CYS A 510 48.523 42.393 13.592 1.00 20.90 C ANISOU 2720 CB CYS A 510 2437 2963 2540 372 -261 -544 C ATOM 2721 SG CYS A 510 47.793 41.888 15.162 1.00 18.92 S ANISOU 2721 SG CYS A 510 2166 2749 2273 367 -256 -549 S ATOM 2722 N CYS A 511 48.564 43.061 10.495 1.00 20.49 N ANISOU 2722 N CYS A 511 2405 2889 2493 381 -265 -556 N ATOM 2723 CA CYS A 511 49.202 43.598 9.298 1.00 20.39 C ANISOU 2723 CA CYS A 511 2409 2854 2486 381 -273 -548 C ATOM 2724 C CYS A 511 48.329 44.667 8.632 1.00 22.37 C ANISOU 2724 C CYS A 511 2668 3117 2714 405 -295 -565 C ATOM 2725 O CYS A 511 48.835 45.682 8.183 1.00 21.63 O ANISOU 2725 O CYS A 511 2596 3004 2621 415 -316 -556 O ATOM 2726 CB CYS A 511 49.562 42.476 8.313 1.00 14.50 C ANISOU 2726 CB CYS A 511 1651 2103 1756 355 -246 -544 C ATOM 2727 SG CYS A 511 50.906 41.405 8.908 1.00 24.00 S ANISOU 2727 SG CYS A 511 2847 3277 2993 327 -226 -519 S ATOM 2728 N ASP A 512 47.020 44.446 8.581 1.00 23.74 N ANISOU 2728 N ASP A 512 2825 3323 2871 415 -292 -588 N ATOM 2729 CA ASP A 512 46.118 45.458 8.038 1.00 24.52 C ANISOU 2729 CA ASP A 512 2930 3436 2952 441 -315 -605 C ATOM 2730 C ASP A 512 46.218 46.746 8.853 1.00 30.28 C ANISOU 2730 C ASP A 512 3675 4152 3676 467 -345 -606 C ATOM 2731 O ASP A 512 46.324 47.839 8.296 1.00 29.61 O ANISOU 2731 O ASP A 512 3609 4052 3590 483 -371 -603 O ATOM 2732 CB ASP A 512 44.669 44.961 8.016 1.00 25.31 C ANISOU 2732 CB ASP A 512 3006 3576 3036 448 -306 -631 C ATOM 2733 CG ASP A 512 44.407 43.975 6.892 1.00 29.68 C ANISOU 2733 CG ASP A 512 3545 4142 3590 427 -283 -634 C ATOM 2734 OD1 ASP A 512 45.314 43.766 6.062 1.00 27.32 O ANISOU 2734 OD1 ASP A 512 3255 3822 3303 409 -276 -618 O ATOM 2735 OD2 ASP A 512 43.294 43.410 6.839 1.00 32.68 O ANISOU 2735 OD2 ASP A 512 3903 4554 3958 428 -272 -654 O ATOM 2736 N ALA A 513 46.199 46.608 10.174 1.00 29.54 N ANISOU 2736 N ALA A 513 3576 4066 3582 470 -343 -610 N ATOM 2737 CA ALA A 513 46.240 47.765 11.059 1.00 27.66 C ANISOU 2737 CA ALA A 513 3351 3820 3340 494 -369 -617 C ATOM 2738 C ALA A 513 47.488 48.623 10.861 1.00 29.28 C ANISOU 2738 C ALA A 513 3583 3983 3559 493 -388 -595 C ATOM 2739 O ALA A 513 47.381 49.836 10.706 1.00 32.73 O ANISOU 2739 O ALA A 513 4037 4407 3994 516 -417 -600 O ATOM 2740 CB ALA A 513 46.100 47.336 12.515 1.00 26.99 C ANISOU 2740 CB ALA A 513 3252 3753 3249 490 -359 -624 C ATOM 2741 N VAL A 514 48.670 48.008 10.861 1.00 31.87 N ANISOU 2741 N VAL A 514 3916 4289 3902 468 -373 -569 N ATOM 2742 CA VAL A 514 49.911 48.781 10.760 1.00 27.89 C ANISOU 2742 CA VAL A 514 3438 3748 3412 465 -389 -547 C ATOM 2743 C VAL A 514 50.222 49.200 9.320 1.00 30.41 C ANISOU 2743 C VAL A 514 3771 4051 3734 461 -398 -535 C ATOM 2744 O VAL A 514 51.138 49.978 9.067 1.00 31.41 O ANISOU 2744 O VAL A 514 3919 4148 3869 460 -415 -517 O ATOM 2745 CB VAL A 514 51.122 48.021 11.325 1.00 26.97 C ANISOU 2745 CB VAL A 514 3320 3614 3312 439 -371 -523 C ATOM 2746 CG1 VAL A 514 50.855 47.574 12.747 1.00 23.65 C ANISOU 2746 CG1 VAL A 514 2887 3213 2887 439 -364 -530 C ATOM 2747 CG2 VAL A 514 51.483 46.848 10.417 1.00 29.76 C ANISOU 2747 CG2 VAL A 514 3663 3967 3677 413 -343 -512 C ATOM 2748 N SER A 515 49.450 48.678 8.380 1.00 29.46 N ANISOU 2748 N SER A 515 3637 3952 3605 457 -386 -545 N ATOM 2749 CA SER A 515 49.663 48.968 6.976 1.00 37.90 C ANISOU 2749 CA SER A 515 4716 5013 4673 450 -392 -535 C ATOM 2750 C SER A 515 48.770 50.113 6.504 1.00 39.00 C ANISOU 2750 C SER A 515 4863 5156 4798 477 -424 -546 C ATOM 2751 O SER A 515 48.851 50.528 5.351 1.00 38.92 O ANISOU 2751 O SER A 515 4862 5141 4784 473 -435 -536 O ATOM 2752 CB SER A 515 49.376 47.719 6.146 1.00 46.80 C ANISOU 2752 CB SER A 515 5822 6161 5798 428 -361 -540 C ATOM 2753 OG SER A 515 49.939 47.834 4.857 1.00 56.46 O ANISOU 2753 OG SER A 515 7055 7375 7022 412 -361 -526 O ATOM 2754 N GLY A 516 47.911 50.606 7.393 1.00 34.25 N ANISOU 2754 N GLY A 516 4256 4566 4190 504 -438 -568 N ATOM 2755 CA GLY A 516 46.981 51.667 7.051 1.00 38.93 C ANISOU 2755 CA GLY A 516 4854 5164 4775 533 -469 -582 C ATOM 2756 C GLY A 516 45.691 51.157 6.437 1.00 40.61 C ANISOU 2756 C GLY A 516 5045 5413 4973 538 -460 -602 C ATOM 2757 O GLY A 516 44.779 51.929 6.145 1.00 42.67 O ANISOU 2757 O GLY A 516 5305 5681 5227 563 -485 -616 O ATOM 2758 N ARG A 517 45.609 49.847 6.244 1.00 39.45 N ANISOU 2758 N ARG A 517 5867 4208 4912 -54 -1083 36 N ATOM 2759 CA ARG A 517 44.433 49.246 5.630 1.00 38.75 C ANISOU 2759 CA ARG A 517 5775 4100 4847 -2 -1119 1 C ATOM 2760 C ARG A 517 43.265 49.113 6.602 1.00 42.29 C ANISOU 2760 C ARG A 517 6144 4558 5365 54 -1133 -38 C ATOM 2761 O ARG A 517 42.144 48.792 6.196 1.00 46.09 O ANISOU 2761 O ARG A 517 6617 5020 5877 100 -1176 -73 O ATOM 2762 CB ARG A 517 44.784 47.889 5.022 1.00 33.79 C ANISOU 2762 CB ARG A 517 5137 3505 4198 -12 -1064 8 C ATOM 2763 CG ARG A 517 45.832 47.982 3.924 1.00 34.72 C ANISOU 2763 CG ARG A 517 5328 3625 4239 -54 -1050 51 C ATOM 2764 CD ARG A 517 45.985 46.650 3.187 1.00 39.24 C ANISOU 2764 CD ARG A 517 5894 4229 4787 -48 -1008 53 C ATOM 2765 NE ARG A 517 46.509 45.604 4.060 1.00 42.18 N ANISOU 2765 NE ARG A 517 6187 4658 5183 -63 -928 50 N ATOM 2766 CZ ARG A 517 47.788 45.248 4.113 1.00 49.61 C ANISOU 2766 CZ ARG A 517 7116 5647 6086 -105 -861 84 C ATOM 2767 NH1 ARG A 517 48.674 45.851 3.331 1.00 51.96 N ANISOU 2767 NH1 ARG A 517 7476 5944 6324 -136 -858 128 N ATOM 2768 NH2 ARG A 517 48.183 44.284 4.942 1.00 49.13 N ANISOU 2768 NH2 ARG A 517 6982 5634 6051 -114 -796 79 N ATOM 2769 N ARG A 518 43.526 49.371 7.880 1.00 40.82 N ANISOU 2769 N ARG A 518 5901 4402 5205 49 -1098 -36 N ATOM 2770 CA ARG A 518 42.495 49.254 8.903 1.00 40.40 C ANISOU 2770 CA ARG A 518 5771 4363 5216 97 -1103 -76 C ATOM 2771 C ARG A 518 42.590 50.377 9.942 1.00 40.61 C ANISOU 2771 C ARG A 518 5789 4381 5261 99 -1120 -78 C ATOM 2772 O ARG A 518 43.656 50.640 10.498 1.00 38.47 O ANISOU 2772 O ARG A 518 5520 4131 4964 54 -1077 -47 O ATOM 2773 CB ARG A 518 42.570 47.886 9.579 1.00 44.28 C ANISOU 2773 CB ARG A 518 6181 4915 5727 98 -1022 -79 C ATOM 2774 CG ARG A 518 41.503 47.667 10.624 1.00 48.86 C ANISOU 2774 CG ARG A 518 6681 5513 6372 143 -1020 -123 C ATOM 2775 CD ARG A 518 41.803 46.454 11.476 1.00 50.26 C ANISOU 2775 CD ARG A 518 6786 5749 6561 133 -934 -118 C ATOM 2776 NE ARG A 518 41.034 46.509 12.714 1.00 49.78 N ANISOU 2776 NE ARG A 518 6654 5706 6553 164 -924 -156 N ATOM 2777 CZ ARG A 518 40.149 45.596 13.093 1.00 48.35 C ANISOU 2777 CZ ARG A 518 6410 5549 6413 191 -903 -191 C ATOM 2778 NH1 ARG A 518 39.911 44.522 12.338 1.00 48.75 N ANISOU 2778 NH1 ARG A 518 6459 5607 6458 192 -893 -192 N ATOM 2779 NH2 ARG A 518 39.503 45.762 14.236 1.00 45.58 N ANISOU 2779 NH2 ARG A 518 5998 5216 6105 210 -891 -231 N ATOM 2780 N GLN A 519 41.456 51.032 10.185 1.00 42.78 N ANISOU 2780 N GLN A 519 6051 4624 5580 145 -1182 -125 N ATOM 2781 CA GLN A 519 41.359 52.144 11.122 1.00 41.65 C ANISOU 2781 CA GLN A 519 5902 4465 5460 146 -1200 -149 C ATOM 2782 C GLN A 519 41.747 51.704 12.538 1.00 36.93 C ANISOU 2782 C GLN A 519 5227 3924 4880 131 -1120 -152 C ATOM 2783 O GLN A 519 41.232 50.714 13.054 1.00 38.00 O ANISOU 2783 O GLN A 519 5290 4102 5048 153 -1078 -174 O ATOM 2784 CB GLN A 519 39.933 52.715 11.087 1.00 45.03 C ANISOU 2784 CB GLN A 519 6319 4850 5939 205 -1276 -209 C ATOM 2785 CG GLN A 519 39.667 53.837 12.071 1.00 50.64 C ANISOU 2785 CG GLN A 519 7022 5536 6682 215 -1295 -245 C ATOM 2786 CD GLN A 519 40.596 55.018 11.880 1.00 53.16 C ANISOU 2786 CD GLN A 519 7428 5810 6962 174 -1317 -211 C ATOM 2787 OE1 GLN A 519 41.640 55.113 12.529 1.00 55.11 O ANISOU 2787 OE1 GLN A 519 7673 6083 7183 128 -1263 -180 O ATOM 2788 NE2 GLN A 519 40.225 55.923 10.983 1.00 50.66 N ANISOU 2788 NE2 GLN A 519 7189 5420 6641 191 -1398 -216 N ATOM 2789 N THR A 520 42.667 52.435 13.159 1.00 34.78 N ANISOU 2789 N THR A 520 4976 3652 4586 90 -1099 -131 N ATOM 2790 CA THR A 520 43.163 52.077 14.493 1.00 32.30 C ANISOU 2790 CA THR A 520 4602 3391 4281 70 -1026 -131 C ATOM 2791 C THR A 520 42.570 52.963 15.591 1.00 35.58 C ANISOU 2791 C THR A 520 4994 3789 4735 91 -1045 -179 C ATOM 2792 O THR A 520 42.678 52.650 16.774 1.00 38.75 O ANISOU 2792 O THR A 520 5340 4232 5152 86 -992 -193 O ATOM 2793 CB THR A 520 44.706 52.146 14.561 1.00 28.19 C ANISOU 2793 CB THR A 520 4112 2889 3710 4 -982 -74 C ATOM 2794 OG1 THR A 520 45.139 53.451 14.180 1.00 27.40 O ANISOU 2794 OG1 THR A 520 4089 2735 3587 -23 -1034 -59 O ATOM 2795 CG2 THR A 520 45.338 51.134 13.609 1.00 28.31 C ANISOU 2795 CG2 THR A 520 4138 2929 3689 -18 -950 -31 C ATOM 2796 N LYS A 521 41.945 54.066 15.186 1.00 41.42 N ANISOU 2796 N LYS A 521 5782 4465 5489 116 -1122 -207 N ATOM 2797 CA LYS A 521 41.286 54.983 16.115 1.00 43.60 C ANISOU 2797 CA LYS A 521 6046 4716 5805 144 -1148 -260 C ATOM 2798 C LYS A 521 39.886 54.500 16.483 1.00 46.19 C ANISOU 2798 C LYS A 521 6300 5059 6190 202 -1155 -324 C ATOM 2799 O LYS A 521 39.092 54.152 15.610 1.00 46.76 O ANISOU 2799 O LYS A 521 6370 5116 6280 236 -1196 -339 O ATOM 2800 CB LYS A 521 41.158 56.368 15.493 1.00 43.77 C ANISOU 2800 CB LYS A 521 6154 4655 5823 150 -1230 -265 C ATOM 2801 CG LYS A 521 42.455 57.083 15.196 1.00 46.29 C ANISOU 2801 CG LYS A 521 6550 4947 6090 90 -1231 -209 C ATOM 2802 CD LYS A 521 42.119 58.449 14.620 1.00 53.03 C ANISOU 2802 CD LYS A 521 7489 5712 6949 105 -1316 -221 C ATOM 2803 CE LYS A 521 43.327 59.350 14.519 1.00 57.75 C ANISOU 2803 CE LYS A 521 8164 6274 7504 43 -1321 -173 C ATOM 2804 NZ LYS A 521 42.929 60.687 13.992 1.00 59.97 N ANISOU 2804 NZ LYS A 521 8532 6461 7794 62 -1406 -185 N ATOM 2805 N GLU A 522 39.584 54.509 17.778 1.00 46.57 N ANISOU 2805 N GLU A 522 6292 5135 6268 211 -1118 -364 N ATOM 2806 CA GLU A 522 38.277 54.093 18.287 1.00 47.51 C ANISOU 2806 CA GLU A 522 6336 5273 6444 260 -1118 -431 C ATOM 2807 C GLU A 522 38.257 54.312 19.797 1.00 47.72 C ANISOU 2807 C GLU A 522 6320 5326 6487 255 -1070 -468 C ATOM 2808 O GLU A 522 39.305 54.292 20.443 1.00 44.04 O ANISOU 2808 O GLU A 522 5863 4885 5985 211 -1021 -432 O ATOM 2809 CB GLU A 522 38.001 52.621 17.948 1.00 45.19 C ANISOU 2809 CB GLU A 522 5984 5030 6156 265 -1079 -420 C ATOM 2810 CG GLU A 522 36.662 52.083 18.441 1.00 46.91 C ANISOU 2810 CG GLU A 522 6120 5271 6433 308 -1075 -487 C ATOM 2811 CD GLU A 522 36.449 50.613 18.087 1.00 53.75 C ANISOU 2811 CD GLU A 522 6937 6182 7305 309 -1036 -472 C ATOM 2812 OE1 GLU A 522 36.509 50.266 16.885 1.00 58.65 O ANISOU 2812 OE1 GLU A 522 7592 6783 7910 312 -1068 -441 O ATOM 2813 OE2 GLU A 522 36.211 49.804 19.010 1.00 52.14 O ANISOU 2813 OE2 GLU A 522 6664 6028 7119 304 -974 -492 O ATOM 2814 N GLY A 523 37.072 54.532 20.358 1.00 49.04 N ANISOU 2814 N GLY A 523 6441 5487 6706 300 -1087 -541 N ATOM 2815 CA GLY A 523 36.949 54.828 21.776 1.00 49.89 C ANISOU 2815 CA GLY A 523 6513 5613 6828 299 -1046 -585 C ATOM 2816 C GLY A 523 37.750 56.041 22.224 1.00 49.61 C ANISOU 2816 C GLY A 523 6546 5537 6765 276 -1061 -573 C ATOM 2817 O GLY A 523 38.203 56.105 23.368 1.00 48.23 O ANISOU 2817 O GLY A 523 6358 5390 6578 251 -1012 -580 O ATOM 2818 N GLY A 524 37.931 57.002 21.321 1.00 50.86 N ANISOU 2818 N GLY A 524 6782 5628 6913 281 -1130 -554 N ATOM 2819 CA GLY A 524 38.631 58.236 21.635 1.00 52.30 C ANISOU 2819 CA GLY A 524 7038 5761 7073 260 -1154 -544 C ATOM 2820 C GLY A 524 40.133 58.082 21.779 1.00 58.98 C ANISOU 2820 C GLY A 524 7915 6631 7862 190 -1112 -472 C ATOM 2821 O GLY A 524 40.770 58.840 22.516 1.00 59.64 O ANISOU 2821 O GLY A 524 8034 6698 7928 163 -1106 -469 O ATOM 2822 N TYR A 525 40.706 57.107 21.075 1.00 62.54 N ANISOU 2822 N TYR A 525 8356 7123 8286 162 -1083 -416 N ATOM 2823 CA TYR A 525 42.146 56.862 21.139 1.00 63.66 C ANISOU 2823 CA TYR A 525 8521 7291 8376 98 -1040 -348 C ATOM 2824 C TYR A 525 42.654 56.052 19.943 1.00 54.18 C ANISOU 2824 C TYR A 525 7331 6108 7146 78 -1033 -289 C ATOM 2825 O TYR A 525 41.900 55.300 19.324 1.00 53.71 O ANISOU 2825 O TYR A 525 7239 6063 7106 111 -1039 -302 O ATOM 2826 CB TYR A 525 42.511 56.165 22.455 1.00 75.42 C ANISOU 2826 CB TYR A 525 9949 8845 9861 76 -963 -353 C ATOM 2827 CG TYR A 525 43.999 56.081 22.737 1.00 88.98 C ANISOU 2827 CG TYR A 525 11692 10586 11531 11 -923 -291 C ATOM 2828 CD1 TYR A 525 44.724 57.212 23.106 1.00 95.45 C ANISOU 2828 CD1 TYR A 525 12570 11366 12331 -23 -948 -280 C ATOM 2829 CD2 TYR A 525 44.677 54.869 22.653 1.00 94.44 C ANISOU 2829 CD2 TYR A 525 12346 11337 12199 -17 -863 -246 C ATOM 2830 CE1 TYR A 525 46.088 57.140 23.372 1.00 98.39 C ANISOU 2830 CE1 TYR A 525 12960 11761 12663 -85 -915 -226 C ATOM 2831 CE2 TYR A 525 46.041 54.786 22.917 1.00 97.88 C ANISOU 2831 CE2 TYR A 525 12800 11795 12595 -75 -829 -193 C ATOM 2832 CZ TYR A 525 46.740 55.925 23.277 1.00 98.35 C ANISOU 2832 CZ TYR A 525 12913 11818 12637 -110 -856 -183 C ATOM 2833 OH TYR A 525 48.091 55.848 23.541 1.00 96.69 O ANISOU 2833 OH TYR A 525 12717 11631 12390 -170 -825 -132 O ATOM 2834 N ASP A 526 43.938 56.227 19.630 1.00 47.38 N ANISOU 2834 N ASP A 526 6518 5247 6239 21 -1020 -229 N ATOM 2835 CA ASP A 526 44.613 55.514 18.545 1.00 43.57 C ANISOU 2835 CA ASP A 526 6052 4781 5721 -6 -1007 -172 C ATOM 2836 C ASP A 526 45.330 54.269 19.077 1.00 44.53 C ANISOU 2836 C ASP A 526 6116 4978 5827 -34 -924 -142 C ATOM 2837 O ASP A 526 46.363 54.370 19.750 1.00 47.04 O ANISOU 2837 O ASP A 526 6436 5318 6120 -80 -887 -114 O ATOM 2838 CB ASP A 526 45.622 56.439 17.860 1.00 38.80 C ANISOU 2838 CB ASP A 526 5534 4133 5077 -56 -1041 -125 C ATOM 2839 CG ASP A 526 46.094 55.906 16.518 1.00 38.60 C ANISOU 2839 CG ASP A 526 5540 4111 5016 -77 -1043 -77 C ATOM 2840 OD1 ASP A 526 46.035 54.680 16.295 1.00 43.05 O ANISOU 2840 OD1 ASP A 526 6055 4724 5577 -68 -1000 -67 O ATOM 2841 OD2 ASP A 526 46.523 56.721 15.681 1.00 40.57 O ANISOU 2841 OD2 ASP A 526 5866 4309 5239 -105 -1088 -50 O ATOM 2842 N HIS A 527 44.784 53.099 18.758 1.00 36.75 N ANISOU 2842 N HIS A 527 5080 4028 4854 -6 -897 -148 N ATOM 2843 CA HIS A 527 45.288 51.835 19.292 1.00 30.45 C ANISOU 2843 CA HIS A 527 4226 3296 4047 -23 -820 -127 C ATOM 2844 C HIS A 527 46.441 51.269 18.479 1.00 28.60 C ANISOU 2844 C HIS A 527 4018 3081 3769 -65 -793 -65 C ATOM 2845 O HIS A 527 46.802 50.106 18.642 1.00 34.16 O ANISOU 2845 O HIS A 527 4680 3833 4465 -73 -736 -47 O ATOM 2846 CB HIS A 527 44.172 50.791 19.361 1.00 29.40 C ANISOU 2846 CB HIS A 527 4029 3190 3950 24 -801 -163 C ATOM 2847 CG HIS A 527 43.002 51.213 20.194 1.00 35.81 C ANISOU 2847 CG HIS A 527 4805 3994 4809 64 -820 -230 C ATOM 2848 ND1 HIS A 527 42.561 50.482 21.279 1.00 41.47 N ANISOU 2848 ND1 HIS A 527 5454 4756 5549 75 -768 -261 N ATOM 2849 CD2 HIS A 527 42.188 52.288 20.103 1.00 35.33 C ANISOU 2849 CD2 HIS A 527 4767 3882 4774 95 -884 -273 C ATOM 2850 CE1 HIS A 527 41.519 51.092 21.815 1.00 45.07 C ANISOU 2850 CE1 HIS A 527 5888 5193 6043 109 -797 -323 C ATOM 2851 NE2 HIS A 527 41.273 52.191 21.124 1.00 38.13 N ANISOU 2851 NE2 HIS A 527 5063 4255 5168 125 -868 -332 N ATOM 2852 N ALA A 528 46.988 52.083 17.584 1.00 22.56 N ANISOU 2852 N ALA A 528 3322 2275 2975 -92 -837 -36 N ATOM 2853 CA ALA A 528 48.091 51.669 16.725 1.00 26.21 C ANISOU 2853 CA ALA A 528 3814 2753 3393 -137 -817 19 C ATOM 2854 C ALA A 528 49.178 50.918 17.509 1.00 26.76 C ANISOU 2854 C ALA A 528 3841 2882 3444 -175 -744 50 C ATOM 2855 O ALA A 528 49.683 49.884 17.070 1.00 27.84 O ANISOU 2855 O ALA A 528 3960 3055 3563 -187 -704 77 O ATOM 2856 CB ALA A 528 48.689 52.893 16.031 1.00 24.29 C ANISOU 2856 CB ALA A 528 3650 2459 3120 -175 -868 44 C ATOM 2857 N ILE A 529 49.531 51.472 18.663 1.00 25.54 N ANISOU 2857 N ILE A 529 3675 2735 3295 -194 -733 42 N ATOM 2858 CA ILE A 529 50.516 50.906 19.566 1.00 28.47 C ANISOU 2858 CA ILE A 529 4009 3159 3651 -229 -674 66 C ATOM 2859 C ILE A 529 50.177 49.464 19.927 1.00 28.65 C ANISOU 2859 C ILE A 529 3969 3231 3687 -201 -617 57 C ATOM 2860 O ILE A 529 51.067 48.616 20.070 1.00 26.37 O ANISOU 2860 O ILE A 529 3657 2986 3376 -227 -568 88 O ATOM 2861 CB ILE A 529 50.578 51.734 20.865 1.00 33.66 C ANISOU 2861 CB ILE A 529 4663 3808 4319 -240 -678 44 C ATOM 2862 CG1 ILE A 529 50.917 53.188 20.536 1.00 50.23 C ANISOU 2862 CG1 ILE A 529 6829 5851 6405 -269 -737 52 C ATOM 2863 CG2 ILE A 529 51.579 51.137 21.831 1.00 29.73 C ANISOU 2863 CG2 ILE A 529 4129 3364 3803 -274 -622 67 C ATOM 2864 CD1 ILE A 529 50.803 54.146 21.717 1.00 59.03 C ANISOU 2864 CD1 ILE A 529 7952 6944 7534 -274 -754 23 C ATOM 2865 N SER A 530 48.887 49.196 20.099 1.00 24.89 N ANISOU 2865 N SER A 530 3464 2746 3247 -150 -625 11 N ATOM 2866 CA SER A 530 48.439 47.855 20.437 1.00 28.59 C ANISOU 2866 CA SER A 530 3876 3255 3731 -124 -575 -2 C ATOM 2867 C SER A 530 48.651 46.877 19.279 1.00 23.32 C ANISOU 2867 C SER A 530 3214 2598 3049 -122 -562 26 C ATOM 2868 O SER A 530 49.185 45.778 19.463 1.00 22.91 O ANISOU 2868 O SER A 530 3133 2587 2984 -133 -509 45 O ATOM 2869 CB SER A 530 46.978 47.877 20.881 1.00 32.55 C ANISOU 2869 CB SER A 530 4345 3746 4278 -73 -592 -60 C ATOM 2870 OG SER A 530 46.864 48.479 22.159 1.00 36.15 O ANISOU 2870 OG SER A 530 4784 4206 4744 -77 -585 -89 O ATOM 2871 N PHE A 531 48.251 47.278 18.085 1.00 19.81 N ANISOU 2871 N PHE A 531 2810 2113 2603 -109 -611 26 N ATOM 2872 CA PHE A 531 48.427 46.399 16.936 1.00 23.11 C ANISOU 2872 CA PHE A 531 3241 2536 3005 -109 -602 49 C ATOM 2873 C PHE A 531 49.909 46.088 16.708 1.00 23.40 C ANISOU 2873 C PHE A 531 3290 2601 2999 -161 -565 99 C ATOM 2874 O PHE A 531 50.272 44.975 16.327 1.00 17.72 O ANISOU 2874 O PHE A 531 2555 1909 2268 -165 -526 115 O ATOM 2875 CB PHE A 531 47.789 47.010 15.689 1.00 18.45 C ANISOU 2875 CB PHE A 531 2703 1892 2414 -89 -669 41 C ATOM 2876 CG PHE A 531 46.284 46.959 15.700 1.00 21.60 C ANISOU 2876 CG PHE A 531 3080 2270 2858 -32 -703 -9 C ATOM 2877 CD1 PHE A 531 45.617 45.786 15.385 1.00 20.47 C ANISOU 2877 CD1 PHE A 531 2903 2141 2733 -2 -684 -24 C ATOM 2878 CD2 PHE A 531 45.536 48.085 16.029 1.00 23.95 C ANISOU 2878 CD2 PHE A 531 3387 2532 3180 -10 -756 -43 C ATOM 2879 CE1 PHE A 531 44.230 45.735 15.396 1.00 21.64 C ANISOU 2879 CE1 PHE A 531 3025 2272 2925 47 -718 -71 C ATOM 2880 CE2 PHE A 531 44.149 48.043 16.040 1.00 20.65 C ANISOU 2880 CE2 PHE A 531 2942 2098 2807 42 -790 -93 C ATOM 2881 CZ PHE A 531 43.496 46.866 15.718 1.00 23.40 C ANISOU 2881 CZ PHE A 531 3254 2464 3175 69 -771 -106 C ATOM 2882 N GLN A 532 50.761 47.074 16.962 1.00 23.60 N ANISOU 2882 N GLN A 532 3344 2622 3002 -202 -579 121 N ATOM 2883 CA GLN A 532 52.197 46.912 16.808 1.00 25.83 C ANISOU 2883 CA GLN A 532 3632 2937 3245 -255 -550 166 C ATOM 2884 C GLN A 532 52.749 45.917 17.817 1.00 19.13 C ANISOU 2884 C GLN A 532 2727 2144 2396 -260 -488 174 C ATOM 2885 O GLN A 532 53.593 45.086 17.486 1.00 20.49 O ANISOU 2885 O GLN A 532 2884 2355 2547 -282 -452 196 O ATOM 2886 CB GLN A 532 52.893 48.260 16.959 1.00 32.57 C ANISOU 2886 CB GLN A 532 4525 3771 4079 -298 -585 183 C ATOM 2887 CG GLN A 532 52.577 49.205 15.824 1.00 46.74 C ANISOU 2887 CG GLN A 532 6387 5510 5861 -302 -647 184 C ATOM 2888 CD GLN A 532 53.219 50.568 15.988 1.00 59.73 C ANISOU 2888 CD GLN A 532 8075 7129 7491 -348 -682 198 C ATOM 2889 OE1 GLN A 532 53.936 50.817 16.960 1.00 62.24 O ANISOU 2889 OE1 GLN A 532 8371 7471 7806 -378 -662 208 O ATOM 2890 NE2 GLN A 532 52.962 51.465 15.034 1.00 63.30 N ANISOU 2890 NE2 GLN A 532 8593 7526 7931 -355 -738 198 N ATOM 2891 N ASP A 533 52.258 45.997 19.045 1.00 10.81 N ANISOU 2891 N ASP A 533 1643 1098 1368 -242 -476 146 N ATOM 2892 CA ASP A 533 52.667 45.055 20.063 1.00 14.28 C ANISOU 2892 CA ASP A 533 2035 1585 1804 -244 -421 149 C ATOM 2893 C ASP A 533 52.256 43.642 19.653 1.00 18.45 C ANISOU 2893 C ASP A 533 2538 2133 2341 -215 -387 143 C ATOM 2894 O ASP A 533 53.089 42.733 19.609 1.00 20.80 O ANISOU 2894 O ASP A 533 2820 2468 2617 -230 -350 169 O ATOM 2895 CB ASP A 533 52.042 45.432 21.403 1.00 27.74 C ANISOU 2895 CB ASP A 533 3718 3289 3532 -228 -419 114 C ATOM 2896 CG ASP A 533 52.581 44.603 22.553 1.00 38.32 C ANISOU 2896 CG ASP A 533 5022 4677 4863 -237 -368 119 C ATOM 2897 OD1 ASP A 533 53.525 43.811 22.333 1.00 43.86 O ANISOU 2897 OD1 ASP A 533 5714 5413 5537 -256 -339 152 O ATOM 2898 OD2 ASP A 533 52.058 44.746 23.677 1.00 39.40 O ANISOU 2898 OD2 ASP A 533 5139 4818 5015 -226 -359 88 O ATOM 2899 N TRP A 534 50.977 43.456 19.332 1.00 16.09 N ANISOU 2899 N TRP A 534 2234 1808 2074 -173 -405 109 N ATOM 2900 CA TRP A 534 50.497 42.128 18.933 1.00 19.90 C ANISOU 2900 CA TRP A 534 2693 2303 2566 -147 -378 100 C ATOM 2901 C TRP A 534 51.281 41.595 17.737 1.00 16.49 C ANISOU 2901 C TRP A 534 2283 1874 2107 -167 -370 132 C ATOM 2902 O TRP A 534 51.640 40.416 17.683 1.00 16.46 O ANISOU 2902 O TRP A 534 2254 1904 2095 -170 -329 134 O ATOM 2903 CB TRP A 534 48.989 42.135 18.625 1.00 20.14 C ANISOU 2903 CB TRP A 534 2717 2302 2634 -100 -409 57 C ATOM 2904 CG TRP A 534 48.151 42.638 19.766 1.00 23.10 C ANISOU 2904 CG TRP A 534 3063 2675 3037 -80 -415 18 C ATOM 2905 CD1 TRP A 534 48.395 42.469 21.100 1.00 22.62 C ANISOU 2905 CD1 TRP A 534 2972 2647 2976 -91 -378 11 C ATOM 2906 CD2 TRP A 534 46.934 43.395 19.673 1.00 23.82 C ANISOU 2906 CD2 TRP A 534 3155 2733 3164 -47 -463 -23 C ATOM 2907 NE1 TRP A 534 47.406 43.077 21.843 1.00 20.71 N ANISOU 2907 NE1 TRP A 534 2711 2393 2764 -69 -396 -33 N ATOM 2908 CE2 TRP A 534 46.503 43.655 20.994 1.00 20.66 C ANISOU 2908 CE2 TRP A 534 2720 2347 2782 -40 -449 -55 C ATOM 2909 CE3 TRP A 534 46.170 43.878 18.603 1.00 18.91 C ANISOU 2909 CE3 TRP A 534 2560 2067 2556 -21 -520 -37 C ATOM 2910 CZ2 TRP A 534 45.342 44.373 21.271 1.00 21.66 C ANISOU 2910 CZ2 TRP A 534 2834 2450 2946 -9 -486 -104 C ATOM 2911 CZ3 TRP A 534 45.014 44.598 18.880 1.00 19.62 C ANISOU 2911 CZ3 TRP A 534 2639 2133 2684 12 -562 -84 C ATOM 2912 CH2 TRP A 534 44.611 44.839 20.202 1.00 19.80 C ANISOU 2912 CH2 TRP A 534 2622 2173 2727 18 -544 -117 C ATOM 2913 N LEU A 535 51.548 42.471 16.780 1.00 13.59 N ANISOU 2913 N LEU A 535 1958 1481 1725 -187 -409 141 N ATOM 2914 CA LEU A 535 52.249 42.067 15.573 1.00 16.36 C ANISOU 2914 CA LEU A 535 2325 1841 2049 -213 -403 152 C ATOM 2915 C LEU A 535 53.675 41.626 15.891 1.00 18.43 C ANISOU 2915 C LEU A 535 2558 2158 2285 -253 -361 174 C ATOM 2916 O LEU A 535 54.138 40.607 15.378 1.00 21.68 O ANISOU 2916 O LEU A 535 2951 2598 2688 -257 -332 174 O ATOM 2917 CB LEU A 535 52.251 43.192 14.539 1.00 17.48 C ANISOU 2917 CB LEU A 535 2526 1941 2175 -230 -456 158 C ATOM 2918 CG LEU A 535 53.054 42.952 13.252 1.00 22.95 C ANISOU 2918 CG LEU A 535 3246 2640 2834 -264 -454 170 C ATOM 2919 CD1 LEU A 535 52.594 41.673 12.538 1.00 24.54 C ANISOU 2919 CD1 LEU A 535 3439 2845 3042 -237 -435 152 C ATOM 2920 CD2 LEU A 535 52.916 44.154 12.336 1.00 19.92 C ANISOU 2920 CD2 LEU A 535 2931 2206 2431 -279 -512 174 C ATOM 2921 N LYS A 536 54.364 42.386 16.741 1.00 19.05 N ANISOU 2921 N LYS A 536 2633 2252 2353 -279 -362 191 N ATOM 2922 CA LYS A 536 55.701 42.001 17.187 1.00 22.84 C ANISOU 2922 CA LYS A 536 3080 2787 2813 -310 -330 209 C ATOM 2923 C LYS A 536 55.716 40.618 17.844 1.00 23.09 C ANISOU 2923 C LYS A 536 3065 2855 2853 -285 -284 198 C ATOM 2924 O LYS A 536 56.619 39.809 17.603 1.00 25.02 O ANISOU 2924 O LYS A 536 3284 3138 3086 -295 -260 203 O ATOM 2925 CB LYS A 536 56.290 43.042 18.142 1.00 27.29 C ANISOU 2925 CB LYS A 536 3649 3356 3366 -337 -345 226 C ATOM 2926 CG LYS A 536 57.772 42.823 18.442 1.00 41.42 C ANISOU 2926 CG LYS A 536 5408 5197 5132 -373 -327 248 C ATOM 2927 CD LYS A 536 58.386 44.029 19.149 1.00 55.12 C ANISOU 2927 CD LYS A 536 7160 6931 6854 -408 -354 269 C ATOM 2928 CE LYS A 536 57.893 45.342 18.528 1.00 65.12 C ANISOU 2928 CE LYS A 536 8482 8144 8118 -423 -403 273 C ATOM 2929 NZ LYS A 536 58.087 45.415 17.046 1.00 68.09 N ANISOU 2929 NZ LYS A 536 8881 8509 8479 -442 -419 278 N ATOM 2930 N LYS A 537 54.722 40.345 18.679 1.00 17.50 N ANISOU 2930 N LYS A 537 2350 2134 2166 -252 -274 181 N ATOM 2931 CA LYS A 537 54.615 39.018 19.268 1.00 19.89 C ANISOU 2931 CA LYS A 537 2618 2465 2473 -229 -234 169 C ATOM 2932 C LYS A 537 54.532 37.924 18.191 1.00 17.48 C ANISOU 2932 C LYS A 537 2307 2165 2171 -217 -221 160 C ATOM 2933 O LYS A 537 55.333 36.983 18.176 1.00 16.31 O ANISOU 2933 O LYS A 537 2134 2051 2012 -221 -196 162 O ATOM 2934 CB LYS A 537 53.411 38.930 20.213 1.00 18.81 C ANISOU 2934 CB LYS A 537 2478 2310 2358 -197 -231 152 C ATOM 2935 CG LYS A 537 53.482 39.833 21.455 1.00 16.77 C ANISOU 2935 CG LYS A 537 2224 2051 2097 -207 -239 159 C ATOM 2936 CD LYS A 537 52.315 39.489 22.383 1.00 21.19 C ANISOU 2936 CD LYS A 537 2762 2606 2683 -176 -226 122 C ATOM 2937 CE LYS A 537 52.175 40.463 23.529 1.00 22.82 C ANISOU 2937 CE LYS A 537 2965 2810 2895 -185 -237 106 C ATOM 2938 NZ LYS A 537 52.875 39.996 24.740 1.00 24.24 N ANISOU 2938 NZ LYS A 537 3131 3027 3051 -202 -206 114 N ATOM 2939 N LEU A 538 53.562 38.044 17.293 1.00 16.25 N ANISOU 2939 N LEU A 538 2176 1970 2030 -200 -244 149 N ATOM 2940 CA LEU A 538 53.397 37.057 16.230 1.00 14.70 C ANISOU 2940 CA LEU A 538 1981 1771 1834 -190 -237 140 C ATOM 2941 C LEU A 538 54.662 36.895 15.376 1.00 22.02 C ANISOU 2941 C LEU A 538 2907 2723 2736 -221 -231 154 C ATOM 2942 O LEU A 538 55.071 35.771 15.056 1.00 23.11 O ANISOU 2942 O LEU A 538 3025 2885 2871 -216 -207 150 O ATOM 2943 CB LEU A 538 52.199 37.427 15.348 1.00 12.85 C ANISOU 2943 CB LEU A 538 1782 1485 1617 -167 -277 125 C ATOM 2944 CG LEU A 538 50.811 37.398 16.003 1.00 16.21 C ANISOU 2944 CG LEU A 538 2199 1886 2076 -127 -290 103 C ATOM 2945 CD1 LEU A 538 49.742 37.845 15.011 1.00 18.79 C ANISOU 2945 CD1 LEU A 538 2557 2163 2417 -102 -341 83 C ATOM 2946 CD2 LEU A 538 50.488 36.011 16.540 1.00 13.99 C ANISOU 2946 CD2 LEU A 538 1885 1627 1805 -107 -253 92 C ATOM 2947 N HIS A 539 55.268 38.022 15.003 1.00 18.64 N ANISOU 2947 N HIS A 539 2501 2289 2292 -253 -256 170 N ATOM 2948 CA HIS A 539 56.469 38.022 14.167 1.00 20.29 C ANISOU 2948 CA HIS A 539 2709 2523 2477 -288 -255 185 C ATOM 2949 C HIS A 539 57.591 37.276 14.873 1.00 19.55 C ANISOU 2949 C HIS A 539 2564 2485 2378 -293 -223 195 C ATOM 2950 O HIS A 539 58.331 36.500 14.267 1.00 19.00 O ANISOU 2950 O HIS A 539 2474 2444 2300 -298 -209 199 O ATOM 2951 CB HIS A 539 56.898 39.468 13.873 1.00 27.55 C ANISOU 2951 CB HIS A 539 3662 3427 3379 -326 -289 203 C ATOM 2952 CG HIS A 539 58.238 39.590 13.212 1.00 35.86 C ANISOU 2952 CG HIS A 539 4707 4515 4405 -369 -289 223 C ATOM 2953 ND1 HIS A 539 58.386 39.789 11.856 1.00 35.86 N ANISOU 2953 ND1 HIS A 539 4751 4495 4380 -381 -297 232 N ATOM 2954 CD2 HIS A 539 59.492 39.547 13.725 1.00 36.22 C ANISOU 2954 CD2 HIS A 539 4710 4612 4439 -392 -277 244 C ATOM 2955 CE1 HIS A 539 59.670 39.860 11.559 1.00 32.73 C ANISOU 2955 CE1 HIS A 539 4341 4135 3959 -399 -269 269 C ATOM 2956 NE2 HIS A 539 60.363 39.716 12.675 1.00 35.99 N ANISOU 2956 NE2 HIS A 539 4697 4592 4386 -411 -262 273 N ATOM 2957 N SER A 540 57.721 37.530 16.164 1.00 14.39 N ANISOU 2957 N SER A 540 1892 1845 1728 -289 -216 199 N ATOM 2958 CA SER A 540 58.766 36.901 16.933 1.00 15.92 C ANISOU 2958 CA SER A 540 2048 2085 1917 -290 -196 209 C ATOM 2959 C SER A 540 58.500 35.394 16.992 1.00 17.27 C ANISOU 2959 C SER A 540 2198 2266 2099 -257 -168 192 C ATOM 2960 O SER A 540 59.416 34.596 16.838 1.00 16.15 O ANISOU 2960 O SER A 540 2030 2156 1951 -256 -156 200 O ATOM 2961 CB SER A 540 58.826 37.513 18.327 1.00 17.28 C ANISOU 2961 CB SER A 540 2217 2259 2088 -294 -199 214 C ATOM 2962 OG SER A 540 59.711 36.782 19.148 1.00 24.72 O ANISOU 2962 OG SER A 540 3127 3238 3025 -291 -183 221 O ATOM 2963 N ARG A 541 57.243 35.006 17.194 1.00 12.70 N ANISOU 2963 N ARG A 541 1631 1657 1535 -229 -161 170 N ATOM 2964 CA ARG A 541 56.917 33.583 17.255 1.00 12.41 C ANISOU 2964 CA ARG A 541 1581 1626 1508 -201 -138 154 C ATOM 2965 C ARG A 541 57.224 32.899 15.927 1.00 18.08 C ANISOU 2965 C ARG A 541 2299 2348 2223 -202 -136 154 C ATOM 2966 O ARG A 541 57.857 31.845 15.895 1.00 15.87 O ANISOU 2966 O ARG A 541 1996 2092 1941 -193 -120 154 O ATOM 2967 CB ARG A 541 55.451 33.343 17.629 1.00 5.83 C ANISOU 2967 CB ARG A 541 761 763 692 -174 -134 135 C ATOM 2968 CG ARG A 541 55.074 31.845 17.659 1.00 12.47 C ANISOU 2968 CG ARG A 541 1591 1607 1539 -150 -114 120 C ATOM 2969 CD ARG A 541 55.959 31.074 18.656 1.00 15.31 C ANISOU 2969 CD ARG A 541 1929 1998 1892 -148 -97 122 C ATOM 2970 NE ARG A 541 55.784 31.613 19.995 1.00 13.20 N ANISOU 2970 NE ARG A 541 1660 1732 1622 -150 -97 123 N ATOM 2971 CZ ARG A 541 54.926 31.141 20.902 1.00 20.48 C ANISOU 2971 CZ ARG A 541 2585 2648 2550 -134 -87 110 C ATOM 2972 NH1 ARG A 541 54.174 30.076 20.634 1.00 17.41 N ANISOU 2972 NH1 ARG A 541 2197 2249 2170 -115 -77 96 N ATOM 2973 NH2 ARG A 541 54.823 31.736 22.090 1.00 19.03 N ANISOU 2973 NH2 ARG A 541 2401 2469 2361 -139 -87 111 N ATOM 2974 N VAL A 542 56.778 33.516 14.837 1.00 15.73 N ANISOU 2974 N VAL A 542 2030 2022 1923 -214 -156 153 N ATOM 2975 CA VAL A 542 56.943 32.946 13.506 1.00 16.38 C ANISOU 2975 CA VAL A 542 2124 2101 1999 -220 -158 150 C ATOM 2976 C VAL A 542 58.415 32.890 13.093 1.00 19.80 C ANISOU 2976 C VAL A 542 2530 2579 2416 -244 -153 169 C ATOM 2977 O VAL A 542 58.855 31.915 12.480 1.00 16.21 O ANISOU 2977 O VAL A 542 2060 2143 1956 -235 -139 170 O ATOM 2978 CB VAL A 542 56.088 33.707 12.478 1.00 15.06 C ANISOU 2978 CB VAL A 542 2011 1882 1829 -227 -189 142 C ATOM 2979 CG1 VAL A 542 56.403 33.267 11.054 1.00 15.12 C ANISOU 2979 CG1 VAL A 542 2050 1883 1810 -225 -192 142 C ATOM 2980 CG2 VAL A 542 54.601 33.517 12.792 1.00 15.16 C ANISOU 2980 CG2 VAL A 542 2041 1856 1864 -192 -198 124 C ATOM 2981 N THR A 543 59.174 33.928 13.439 1.00 19.68 N ANISOU 2981 N THR A 543 2507 2583 2388 -270 -165 190 N ATOM 2982 CA THR A 543 60.619 33.919 13.242 1.00 19.18 C ANISOU 2982 CA THR A 543 2411 2568 2308 -286 -159 218 C ATOM 2983 C THR A 543 61.253 32.743 13.982 1.00 18.71 C ANISOU 2983 C THR A 543 2305 2546 2257 -261 -141 221 C ATOM 2984 O THR A 543 62.010 31.977 13.409 1.00 21.68 O ANISOU 2984 O THR A 543 2668 2945 2625 -245 -114 238 O ATOM 2985 CB THR A 543 61.271 35.205 13.773 1.00 25.39 C ANISOU 2985 CB THR A 543 3196 3367 3083 -320 -179 241 C ATOM 2986 OG1 THR A 543 60.898 36.304 12.945 1.00 25.17 O ANISOU 2986 OG1 THR A 543 3222 3300 3040 -341 -190 249 O ATOM 2987 CG2 THR A 543 62.794 35.086 13.764 1.00 27.72 C ANISOU 2987 CG2 THR A 543 3462 3706 3366 -325 -153 281 C ATOM 2988 N LYS A 544 60.936 32.606 15.262 1.00 19.39 N ANISOU 2988 N LYS A 544 2390 2623 2353 -245 -135 213 N ATOM 2989 CA LYS A 544 61.505 31.534 16.075 1.00 24.46 C ANISOU 2989 CA LYS A 544 3005 3289 3000 -222 -119 217 C ATOM 2990 C LYS A 544 61.153 30.143 15.554 1.00 22.61 C ANISOU 2990 C LYS A 544 2767 3050 2775 -194 -102 201 C ATOM 2991 O LYS A 544 61.969 29.229 15.605 1.00 20.62 O ANISOU 2991 O LYS A 544 2488 2826 2521 -179 -92 215 O ATOM 2992 CB LYS A 544 61.014 31.644 17.516 1.00 25.72 C ANISOU 2992 CB LYS A 544 3175 3432 3165 -215 -117 206 C ATOM 2993 CG LYS A 544 61.674 32.722 18.333 1.00 24.36 C ANISOU 2993 CG LYS A 544 2999 3274 2983 -241 -132 227 C ATOM 2994 CD LYS A 544 61.021 32.763 19.695 1.00 22.06 C ANISOU 2994 CD LYS A 544 2720 2965 2698 -232 -128 213 C ATOM 2995 CE LYS A 544 61.556 33.904 20.518 1.00 25.59 C ANISOU 2995 CE LYS A 544 3167 3421 3134 -260 -144 231 C ATOM 2996 NZ LYS A 544 60.804 34.002 21.802 1.00 27.27 N ANISOU 2996 NZ LYS A 544 3393 3617 3350 -251 -140 216 N ATOM 2997 N GLU A 545 59.932 29.978 15.057 1.00 18.21 N ANISOU 2997 N GLU A 545 2237 2456 2226 -185 -100 176 N ATOM 2998 CA GLU A 545 59.472 28.651 14.675 1.00 12.96 C ANISOU 2998 CA GLU A 545 1572 1782 1569 -161 -86 159 C ATOM 2999 C GLU A 545 59.399 28.452 13.148 1.00 12.52 C ANISOU 2999 C GLU A 545 1523 1725 1511 -167 -88 157 C ATOM 3000 O GLU A 545 58.672 27.587 12.654 1.00 12.16 O ANISOU 3000 O GLU A 545 1497 1656 1469 -150 -81 140 O ATOM 3001 CB GLU A 545 58.130 28.346 15.360 1.00 12.13 C ANISOU 3001 CB GLU A 545 1490 1639 1478 -145 -82 134 C ATOM 3002 CG GLU A 545 58.281 27.799 16.784 1.00 15.73 C ANISOU 3002 CG GLU A 545 1937 2104 1937 -133 -74 133 C ATOM 3003 CD GLU A 545 58.753 26.350 16.795 1.00 24.80 C ANISOU 3003 CD GLU A 545 3071 3265 3087 -117 -63 133 C ATOM 3004 OE1 GLU A 545 59.981 26.117 16.645 1.00 22.40 O ANISOU 3004 OE1 GLU A 545 2743 2993 2776 -119 -62 155 O ATOM 3005 OE2 GLU A 545 57.895 25.442 16.934 1.00 20.67 O ANISOU 3005 OE2 GLU A 545 2560 2721 2573 -103 -56 115 O ATOM 3006 N ARG A 546 60.171 29.234 12.404 1.00 11.89 N ANISOU 3006 N ARG A 546 1457 1656 1404 -175 -85 182 N ATOM 3007 CA ARG A 546 60.035 29.228 10.943 1.00 14.47 C ANISOU 3007 CA ARG A 546 1843 1960 1696 -156 -70 188 C ATOM 3008 C ARG A 546 60.232 27.840 10.334 1.00 18.30 C ANISOU 3008 C ARG A 546 2337 2451 2166 -114 -44 187 C ATOM 3009 O ARG A 546 59.572 27.485 9.361 1.00 17.23 O ANISOU 3009 O ARG A 546 2254 2285 2008 -91 -46 174 O ATOM 3010 CB ARG A 546 60.962 30.256 10.282 1.00 12.85 C ANISOU 3010 CB ARG A 546 1655 1767 1458 -172 -59 222 C ATOM 3011 CG ARG A 546 62.432 29.984 10.484 1.00 21.33 C ANISOU 3011 CG ARG A 546 2687 2889 2526 -170 -28 256 C ATOM 3012 CD ARG A 546 63.291 31.137 9.990 1.00 31.09 C ANISOU 3012 CD ARG A 546 3937 4138 3738 -199 -16 292 C ATOM 3013 NE ARG A 546 64.709 30.872 10.246 1.00 43.55 N ANISOU 3013 NE ARG A 546 5470 5763 5316 -199 14 326 N ATOM 3014 CZ ARG A 546 65.328 31.148 11.393 1.00 50.51 C ANISOU 3014 CZ ARG A 546 6301 6671 6220 -219 -1 337 C ATOM 3015 NH1 ARG A 546 64.663 31.712 12.396 1.00 45.62 N ANISOU 3015 NH1 ARG A 546 5674 6039 5622 -239 -44 316 N ATOM 3016 NH2 ARG A 546 66.618 30.864 11.537 1.00 53.67 N ANISOU 3016 NH2 ARG A 546 6663 7112 6619 -217 27 371 N ATOM 3017 N HIS A 547 61.114 27.036 10.913 1.00 16.04 N ANISOU 3017 N HIS A 547 2004 2201 1891 -102 -25 200 N ATOM 3018 CA HIS A 547 61.380 25.741 10.311 1.00 22.15 C ANISOU 3018 CA HIS A 547 2790 2979 2648 -61 2 202 C ATOM 3019 C HIS A 547 60.178 24.807 10.424 1.00 22.82 C ANISOU 3019 C HIS A 547 2892 3031 2746 -45 -14 167 C ATOM 3020 O HIS A 547 59.758 24.228 9.420 1.00 19.55 O ANISOU 3020 O HIS A 547 2529 2594 2305 -15 -10 157 O ATOM 3021 CB HIS A 547 62.644 25.103 10.884 1.00 23.61 C ANISOU 3021 CB HIS A 547 2924 3206 2839 -49 25 229 C ATOM 3022 CG HIS A 547 63.904 25.777 10.439 1.00 26.93 C ANISOU 3022 CG HIS A 547 3338 3658 3238 -57 53 268 C ATOM 3023 ND1 HIS A 547 64.592 26.669 11.233 1.00 30.42 N ANISOU 3023 ND1 HIS A 547 3740 4124 3694 -90 41 288 N ATOM 3024 CD2 HIS A 547 64.593 25.699 9.277 1.00 25.92 C ANISOU 3024 CD2 HIS A 547 3238 3540 3071 -38 93 291 C ATOM 3025 CE1 HIS A 547 65.656 27.106 10.582 1.00 26.45 C ANISOU 3025 CE1 HIS A 547 3237 3645 3167 -94 74 323 C ATOM 3026 NE2 HIS A 547 65.678 26.534 9.393 1.00 27.81 N ANISOU 3026 NE2 HIS A 547 3449 3810 3307 -63 109 326 N ATOM 3027 N ARG A 548 59.619 24.659 11.626 1.00 15.00 N ANISOU 3027 N ARG A 548 1864 2039 1796 -65 -32 149 N ATOM 3028 CA ARG A 548 58.419 23.827 11.764 1.00 16.48 C ANISOU 3028 CA ARG A 548 2070 2194 1999 -58 -42 118 C ATOM 3029 C ARG A 548 57.256 24.404 10.972 1.00 17.75 C ANISOU 3029 C ARG A 548 2286 2308 2149 -58 -66 99 C ATOM 3030 O ARG A 548 56.550 23.670 10.265 1.00 11.78 O ANISOU 3030 O ARG A 548 1573 1523 1381 -30 -77 80 O ATOM 3031 CB ARG A 548 58.040 23.587 13.230 1.00 19.11 C ANISOU 3031 CB ARG A 548 2356 2531 2374 -86 -45 109 C ATOM 3032 CG ARG A 548 58.586 22.258 13.802 1.00 21.31 C ANISOU 3032 CG ARG A 548 2616 2828 2654 -63 -31 114 C ATOM 3033 CD ARG A 548 58.279 22.080 15.311 1.00 17.66 C ANISOU 3033 CD ARG A 548 2163 2349 2197 -67 -35 107 C ATOM 3034 NE ARG A 548 59.127 22.949 16.119 1.00 23.13 N ANISOU 3034 NE ARG A 548 2843 3063 2883 -77 -40 126 N ATOM 3035 CZ ARG A 548 60.321 22.603 16.613 1.00 23.87 C ANISOU 3035 CZ ARG A 548 2912 3185 2971 -72 -37 150 C ATOM 3036 NH1 ARG A 548 60.814 21.384 16.405 1.00 16.31 N ANISOU 3036 NH1 ARG A 548 1942 2241 2014 -53 -27 158 N ATOM 3037 NH2 ARG A 548 61.018 23.478 17.333 1.00 16.29 N ANISOU 3037 NH2 ARG A 548 1942 2243 2006 -86 -45 168 N ATOM 3038 N LEU A 549 57.084 25.723 11.054 1.00 17.78 N ANISOU 3038 N LEU A 549 2294 2303 2158 -86 -80 103 N ATOM 3039 CA LEU A 549 56.004 26.398 10.343 1.00 19.39 C ANISOU 3039 CA LEU A 549 2551 2461 2354 -83 -109 88 C ATOM 3040 C LEU A 549 56.069 26.201 8.823 1.00 17.46 C ANISOU 3040 C LEU A 549 2368 2203 2063 -50 -115 89 C ATOM 3041 O LEU A 549 55.042 26.078 8.166 1.00 12.52 O ANISOU 3041 O LEU A 549 1788 1536 1432 -33 -144 68 O ATOM 3042 CB LEU A 549 55.989 27.895 10.681 1.00 17.89 C ANISOU 3042 CB LEU A 549 2358 2266 2174 -117 -122 97 C ATOM 3043 CG LEU A 549 55.476 28.254 12.082 1.00 14.59 C ANISOU 3043 CG LEU A 549 1906 1839 1800 -146 -120 95 C ATOM 3044 CD1 LEU A 549 55.919 29.658 12.493 1.00 12.49 C ANISOU 3044 CD1 LEU A 549 1632 1588 1527 -167 -127 111 C ATOM 3045 CD2 LEU A 549 53.952 28.095 12.162 1.00 8.42 C ANISOU 3045 CD2 LEU A 549 1154 1012 1034 -120 -137 78 C ATOM 3046 N SER A 550 57.269 26.164 8.261 1.00 15.73 N ANISOU 3046 N SER A 550 2152 2015 1810 -40 -86 116 N ATOM 3047 CA SER A 550 57.400 26.120 6.805 1.00 19.72 C ANISOU 3047 CA SER A 550 2722 2506 2263 -12 -83 123 C ATOM 3048 C SER A 550 57.070 24.735 6.207 1.00 21.93 C ANISOU 3048 C SER A 550 3033 2773 2526 30 -82 106 C ATOM 3049 O SER A 550 57.018 24.563 4.990 1.00 20.36 O ANISOU 3049 O SER A 550 2897 2556 2281 57 -84 106 O ATOM 3050 CB SER A 550 58.777 26.643 6.363 1.00 24.14 C ANISOU 3050 CB SER A 550 3280 3103 2791 -18 -45 162 C ATOM 3051 OG SER A 550 59.836 25.949 6.995 1.00 31.22 O ANISOU 3051 OG SER A 550 4120 4042 3699 -13 -9 180 O ATOM 3052 N ARG A 551 56.813 23.766 7.081 1.00 22.99 N ANISOU 3052 N ARG A 551 3129 2912 2694 34 -82 90 N ATOM 3053 CA ARG A 551 56.333 22.447 6.679 1.00 19.08 C ANISOU 3053 CA ARG A 551 2662 2397 2189 69 -90 70 C ATOM 3054 C ARG A 551 54.863 22.508 6.266 1.00 21.44 C ANISOU 3054 C ARG A 551 3003 2645 2497 73 -140 39 C ATOM 3055 O ARG A 551 54.356 21.617 5.579 1.00 17.13 O ANISOU 3055 O ARG A 551 2501 2074 1934 103 -159 21 O ATOM 3056 CB ARG A 551 56.487 21.467 7.851 1.00 17.66 C ANISOU 3056 CB ARG A 551 2427 2237 2046 65 -77 65 C ATOM 3057 CG ARG A 551 57.941 21.198 8.253 1.00 17.43 C ANISOU 3057 CG ARG A 551 2355 2257 2011 70 -34 96 C ATOM 3058 CD ARG A 551 58.017 20.296 9.472 1.00 19.81 C ANISOU 3058 CD ARG A 551 2605 2574 2349 63 -28 92 C ATOM 3059 NE ARG A 551 57.172 19.106 9.345 1.00 18.51 N ANISOU 3059 NE ARG A 551 2469 2378 2185 85 -47 65 N ATOM 3060 CZ ARG A 551 56.768 18.377 10.384 1.00 19.68 C ANISOU 3060 CZ ARG A 551 2587 2524 2367 71 -53 53 C ATOM 3061 NH1 ARG A 551 57.142 18.730 11.615 1.00 14.88 N ANISOU 3061 NH1 ARG A 551 1921 1943 1791 37 -39 66 N ATOM 3062 NH2 ARG A 551 55.981 17.307 10.202 1.00 14.06 N ANISOU 3062 NH2 ARG A 551 1906 1782 1655 88 -74 30 N ATOM 3063 N PHE A 552 54.171 23.560 6.688 1.00 20.62 N ANISOU 3063 N PHE A 552 2888 2523 2422 44 -164 33 N ATOM 3064 CA PHE A 552 52.732 23.650 6.461 1.00 16.00 C ANISOU 3064 CA PHE A 552 2332 1890 1858 50 -211 7 C ATOM 3065 C PHE A 552 52.329 24.855 5.612 1.00 13.43 C ANISOU 3065 C PHE A 552 2055 1537 1512 48 -243 9 C ATOM 3066 O PHE A 552 52.922 25.928 5.716 1.00 17.47 O ANISOU 3066 O PHE A 552 2558 2064 2014 25 -230 28 O ATOM 3067 CB PHE A 552 51.997 23.675 7.801 1.00 18.63 C ANISOU 3067 CB PHE A 552 2612 2216 2251 27 -215 -1 C ATOM 3068 CG PHE A 552 52.324 22.503 8.685 1.00 23.67 C ANISOU 3068 CG PHE A 552 3209 2877 2907 25 -187 -2 C ATOM 3069 CD1 PHE A 552 51.604 21.319 8.583 1.00 22.74 C ANISOU 3069 CD1 PHE A 552 3104 2737 2800 46 -205 -19 C ATOM 3070 CD2 PHE A 552 53.365 22.578 9.609 1.00 19.06 C ANISOU 3070 CD2 PHE A 552 2575 2336 2330 2 -148 17 C ATOM 3071 CE1 PHE A 552 51.905 20.228 9.395 1.00 23.33 C ANISOU 3071 CE1 PHE A 552 3146 2829 2889 44 -183 -19 C ATOM 3072 CE2 PHE A 552 53.674 21.488 10.419 1.00 18.31 C ANISOU 3072 CE2 PHE A 552 2446 2260 2250 1 -127 17 C ATOM 3073 CZ PHE A 552 52.938 20.310 10.308 1.00 20.39 C ANISOU 3073 CZ PHE A 552 2727 2499 2521 22 -144 -1 C ATOM 3074 N SER A 553 51.306 24.672 4.782 1.00 13.04 N ANISOU 3074 N SER A 553 2055 1444 1455 71 -288 -10 N ATOM 3075 CA SER A 553 50.754 25.761 3.989 1.00 13.73 C ANISOU 3075 CA SER A 553 2191 1498 1526 72 -328 -11 C ATOM 3076 C SER A 553 50.418 26.962 4.867 1.00 10.63 C ANISOU 3076 C SER A 553 1764 1102 1175 43 -336 -7 C ATOM 3077 O SER A 553 50.735 28.096 4.523 1.00 17.07 O ANISOU 3077 O SER A 553 2602 1914 1968 29 -342 7 O ATOM 3078 CB SER A 553 49.498 25.300 3.247 1.00 18.14 C ANISOU 3078 CB SER A 553 2794 2009 2089 101 -384 -35 C ATOM 3079 OG SER A 553 49.790 24.285 2.301 1.00 22.09 O ANISOU 3079 OG SER A 553 3342 2508 2543 130 -382 -40 O ATOM 3080 N SER A 554 49.767 26.710 5.999 1.00 9.59 N ANISOU 3080 N SER A 554 1578 966 1098 37 -334 -15 N ATOM 3081 CA SER A 554 49.420 27.776 6.939 1.00 11.01 C ANISOU 3081 CA SER A 554 1726 1142 1317 17 -337 -9 C ATOM 3082 C SER A 554 50.651 28.571 7.410 1.00 14.06 C ANISOU 3082 C SER A 554 2090 1564 1689 -18 -300 14 C ATOM 3083 O SER A 554 50.622 29.803 7.469 1.00 12.77 O ANISOU 3083 O SER A 554 1936 1389 1525 -34 -315 23 O ATOM 3084 CB SER A 554 48.684 27.197 8.152 1.00 11.31 C ANISOU 3084 CB SER A 554 1704 1194 1401 21 -326 -13 C ATOM 3085 OG SER A 554 49.553 26.382 8.938 1.00 15.33 O ANISOU 3085 OG SER A 554 2174 1737 1913 5 -277 -3 O ATOM 3086 N GLY A 555 51.728 27.856 7.734 1.00 17.26 N ANISOU 3086 N GLY A 555 2464 2012 2080 -29 -256 25 N ATOM 3087 CA GLY A 555 52.976 28.470 8.165 1.00 13.93 C ANISOU 3087 CA GLY A 555 2014 1631 1646 -59 -223 49 C ATOM 3088 C GLY A 555 53.624 29.276 7.059 1.00 17.70 C ANISOU 3088 C GLY A 555 2539 2112 2073 -60 -228 67 C ATOM 3089 O GLY A 555 53.992 30.443 7.257 1.00 17.75 O ANISOU 3089 O GLY A 555 2545 2123 2077 -87 -231 84 O ATOM 3090 N LYS A 556 53.745 28.668 5.882 1.00 16.67 N ANISOU 3090 N LYS A 556 2457 1976 1901 -31 -229 67 N ATOM 3091 CA LYS A 556 54.226 29.400 4.702 1.00 23.47 C ANISOU 3091 CA LYS A 556 3378 2831 2707 -29 -232 88 C ATOM 3092 C LYS A 556 53.411 30.665 4.384 1.00 20.07 C ANISOU 3092 C LYS A 556 2989 2359 2278 -39 -282 83 C ATOM 3093 O LYS A 556 53.989 31.689 4.008 1.00 20.70 O ANISOU 3093 O LYS A 556 3093 2441 2328 -59 -279 108 O ATOM 3094 CB LYS A 556 54.323 28.485 3.470 1.00 24.78 C ANISOU 3094 CB LYS A 556 3599 2990 2824 9 -227 86 C ATOM 3095 CG LYS A 556 55.587 27.608 3.464 1.00 30.56 C ANISOU 3095 CG LYS A 556 4306 3769 3534 20 -169 107 C ATOM 3096 CD LYS A 556 55.664 26.698 2.242 1.00 35.30 C ANISOU 3096 CD LYS A 556 4969 4361 4084 61 -162 104 C ATOM 3097 CE LYS A 556 54.537 25.672 2.250 1.00 42.85 C ANISOU 3097 CE LYS A 556 5936 5284 5060 87 -199 67 C ATOM 3098 NZ LYS A 556 54.840 24.485 1.397 1.00 48.48 N ANISOU 3098 NZ LYS A 556 6690 5999 5729 127 -182 64 N ATOM 3099 N LYS A 557 52.086 30.598 4.526 1.00 14.53 N ANISOU 3099 N LYS A 557 2294 1615 1610 -25 -327 54 N ATOM 3100 CA LYS A 557 51.241 31.798 4.363 1.00 21.30 C ANISOU 3100 CA LYS A 557 3184 2430 2478 -30 -378 47 C ATOM 3101 C LYS A 557 51.613 32.911 5.353 1.00 19.12 C ANISOU 3101 C LYS A 557 2872 2167 2228 -66 -369 62 C ATOM 3102 O LYS A 557 51.745 34.080 4.980 1.00 20.60 O ANISOU 3102 O LYS A 557 3095 2338 2394 -81 -391 76 O ATOM 3103 CB LYS A 557 49.751 31.469 4.539 1.00 22.97 C ANISOU 3103 CB LYS A 557 3393 2600 2735 -4 -423 16 C ATOM 3104 CG LYS A 557 49.098 30.701 3.395 1.00 33.06 C ANISOU 3104 CG LYS A 557 4723 3850 3989 31 -456 -1 C ATOM 3105 CD LYS A 557 47.605 30.471 3.695 1.00 43.35 C ANISOU 3105 CD LYS A 557 6011 5114 5346 56 -503 -27 C ATOM 3106 CE LYS A 557 46.967 29.474 2.728 1.00 52.86 C ANISOU 3106 CE LYS A 557 7256 6295 6534 89 -536 -45 C ATOM 3107 NZ LYS A 557 45.494 29.276 2.961 1.00 53.84 N ANISOU 3107 NZ LYS A 557 7361 6385 6710 114 -586 -68 N ATOM 3108 N MET A 558 51.763 32.555 6.626 1.00 13.97 N ANISOU 3108 N MET A 558 2151 1538 1617 -80 -339 60 N ATOM 3109 CA MET A 558 52.105 33.562 7.628 1.00 14.74 C ANISOU 3109 CA MET A 558 2217 1645 1738 -114 -331 73 C ATOM 3110 C MET A 558 53.480 34.170 7.358 1.00 17.06 C ANISOU 3110 C MET A 558 2516 1976 1992 -144 -308 105 C ATOM 3111 O MET A 558 53.656 35.386 7.403 1.00 17.29 O ANISOU 3111 O MET A 558 2563 1994 2013 -168 -326 119 O ATOM 3112 CB MET A 558 52.046 32.982 9.039 1.00 8.76 C ANISOU 3112 CB MET A 558 1394 908 1028 -120 -299 71 C ATOM 3113 CG MET A 558 50.633 32.637 9.504 1.00 7.56 C ANISOU 3113 CG MET A 558 1229 730 914 -84 -319 52 C ATOM 3114 SD MET A 558 50.571 32.330 11.295 1.00 19.41 S ANISOU 3114 SD MET A 558 2656 2272 2447 -86 -278 59 S ATOM 3115 CE MET A 558 51.702 30.954 11.463 1.00 15.21 C ANISOU 3115 CE MET A 558 2094 1782 1904 -101 -227 67 C ATOM 3116 N ILE A 559 54.455 33.315 7.076 1.00 20.11 N ANISOU 3116 N ILE A 559 2885 2403 2351 -140 -266 119 N ATOM 3117 CA ILE A 559 55.800 33.772 6.750 1.00 17.38 C ANISOU 3117 CA ILE A 559 2541 2094 1970 -162 -235 155 C ATOM 3118 C ILE A 559 55.715 34.773 5.611 1.00 25.39 C ANISOU 3118 C ILE A 559 3630 3076 2940 -165 -261 172 C ATOM 3119 O ILE A 559 56.271 35.876 5.694 1.00 29.65 O ANISOU 3119 O ILE A 559 4177 3619 3469 -196 -264 197 O ATOM 3120 CB ILE A 559 56.687 32.589 6.351 1.00 16.17 C ANISOU 3120 CB ILE A 559 2371 1979 1793 -142 -188 167 C ATOM 3121 CG1 ILE A 559 56.979 31.740 7.588 1.00 15.66 C ANISOU 3121 CG1 ILE A 559 2230 1949 1770 -146 -164 158 C ATOM 3122 CG2 ILE A 559 57.970 33.075 5.643 1.00 11.74 C ANISOU 3122 CG2 ILE A 559 1828 1445 1187 -156 -155 209 C ATOM 3123 CD1 ILE A 559 57.679 30.423 7.306 1.00 17.98 C ANISOU 3123 CD1 ILE A 559 2506 2274 2049 -118 -125 164 C ATOM 3124 N GLU A 560 54.979 34.394 4.565 1.00 23.99 N ANISOU 3124 N GLU A 560 3510 2866 2739 -132 -285 157 N ATOM 3125 CA GLU A 560 54.755 35.265 3.411 1.00 24.28 C ANISOU 3125 CA GLU A 560 3628 2867 2732 -130 -317 171 C ATOM 3126 C GLU A 560 54.074 36.594 3.788 1.00 25.27 C ANISOU 3126 C GLU A 560 3770 2953 2879 -149 -369 166 C ATOM 3127 O GLU A 560 54.497 37.662 3.346 1.00 20.90 O ANISOU 3127 O GLU A 560 3258 2389 2295 -172 -379 194 O ATOM 3128 CB GLU A 560 53.926 34.542 2.351 1.00 31.44 C ANISOU 3128 CB GLU A 560 4590 3740 3614 -89 -344 149 C ATOM 3129 CG GLU A 560 53.526 35.432 1.178 1.00 49.29 C ANISOU 3129 CG GLU A 560 6941 5958 5830 -85 -388 160 C ATOM 3130 CD GLU A 560 52.545 34.765 0.222 1.00 61.24 C ANISOU 3130 CD GLU A 560 8510 7434 7325 -44 -428 134 C ATOM 3131 OE1 GLU A 560 52.414 35.254 -0.923 1.00 65.08 O ANISOU 3131 OE1 GLU A 560 9077 7890 7761 -36 -456 147 O ATOM 3132 OE2 GLU A 560 51.907 33.760 0.613 1.00 64.31 O ANISOU 3132 OE2 GLU A 560 8863 7821 7749 -21 -434 102 O ATOM 3133 N THR A 561 53.010 36.511 4.586 1.00 19.30 N ANISOU 3133 N THR A 561 2983 2173 2175 -138 -401 131 N ATOM 3134 CA THR A 561 52.286 37.687 5.042 1.00 18.48 C ANISOU 3134 CA THR A 561 2891 2032 2099 -148 -449 123 C ATOM 3135 C THR A 561 53.255 38.680 5.689 1.00 21.42 C ANISOU 3135 C THR A 561 3245 2427 2469 -192 -432 152 C ATOM 3136 O THR A 561 53.205 39.885 5.424 1.00 20.96 O ANISOU 3136 O THR A 561 3231 2339 2395 -207 -467 166 O ATOM 3137 CB THR A 561 51.197 37.309 6.075 1.00 25.42 C ANISOU 3137 CB THR A 561 3722 2892 3044 -129 -464 88 C ATOM 3138 OG1 THR A 561 50.174 36.530 5.441 1.00 24.07 O ANISOU 3138 OG1 THR A 561 3572 2693 2880 -88 -490 63 O ATOM 3139 CG2 THR A 561 50.572 38.560 6.693 1.00 28.13 C ANISOU 3139 CG2 THR A 561 4070 3199 3419 -135 -505 84 C ATOM 3140 N LEU A 562 54.147 38.168 6.529 1.00 13.87 N ANISOU 3140 N LEU A 562 2223 1520 1525 -212 -381 162 N ATOM 3141 CA LEU A 562 55.093 39.028 7.231 1.00 18.69 C ANISOU 3141 CA LEU A 562 2809 2156 2137 -255 -367 189 C ATOM 3142 C LEU A 562 56.125 39.635 6.292 1.00 30.35 C ANISOU 3142 C LEU A 562 4328 3643 3560 -277 -351 232 C ATOM 3143 O LEU A 562 56.469 40.815 6.421 1.00 30.50 O ANISOU 3143 O LEU A 562 4368 3650 3570 -309 -368 255 O ATOM 3144 CB LEU A 562 55.780 38.268 8.366 1.00 18.09 C ANISOU 3144 CB LEU A 562 2651 2132 2089 -269 -323 188 C ATOM 3145 CG LEU A 562 54.944 38.191 9.651 1.00 17.71 C ANISOU 3145 CG LEU A 562 2562 2069 2097 -267 -335 160 C ATOM 3146 CD1 LEU A 562 55.519 37.136 10.594 1.00 16.38 C ANISOU 3146 CD1 LEU A 562 2322 1950 1953 -273 -290 158 C ATOM 3147 CD2 LEU A 562 54.881 39.554 10.318 1.00 11.92 C ANISOU 3147 CD2 LEU A 562 1839 1314 1377 -296 -365 166 C ATOM 3148 N ALA A 563 56.608 38.826 5.347 1.00 29.63 N ANISOU 3148 N ALA A 563 4254 3572 3433 -260 -317 245 N ATOM 3149 CA ALA A 563 57.580 39.290 4.362 1.00 30.94 C ANISOU 3149 CA ALA A 563 4464 3748 3546 -278 -291 289 C ATOM 3150 C ALA A 563 56.985 40.351 3.430 1.00 34.07 C ANISOU 3150 C ALA A 563 4948 4087 3908 -280 -340 298 C ATOM 3151 O ALA A 563 57.667 41.307 3.055 1.00 38.39 O ANISOU 3151 O ALA A 563 5529 4631 4426 -314 -336 337 O ATOM 3152 CB ALA A 563 58.142 38.117 3.556 1.00 28.32 C ANISOU 3152 CB ALA A 563 4134 3446 3182 -252 -242 297 C ATOM 3153 N ASN A 564 55.719 40.181 3.060 1.00 30.44 N ANISOU 3153 N ASN A 564 4527 3584 3456 -245 -389 264 N ATOM 3154 CA ASN A 564 55.025 41.180 2.248 1.00 39.31 C ANISOU 3154 CA ASN A 564 5733 4649 4554 -241 -448 269 C ATOM 3155 C ASN A 564 54.870 42.508 2.977 1.00 42.18 C ANISOU 3155 C ASN A 564 6098 4986 4942 -271 -487 275 C ATOM 3156 O ASN A 564 54.799 43.563 2.350 1.00 41.56 O ANISOU 3156 O ASN A 564 6088 4868 4834 -284 -522 297 O ATOM 3157 CB ASN A 564 53.640 40.685 1.813 1.00 42.08 C ANISOU 3157 CB ASN A 564 6114 4959 4917 -194 -499 227 C ATOM 3158 CG ASN A 564 53.712 39.614 0.748 1.00 50.48 C ANISOU 3158 CG ASN A 564 7210 6032 5940 -165 -477 226 C ATOM 3159 OD1 ASN A 564 54.788 39.316 0.221 1.00 53.56 O ANISOU 3159 OD1 ASN A 564 7608 6456 6286 -177 -422 259 O ATOM 3160 ND2 ASN A 564 52.562 39.023 0.424 1.00 49.93 N ANISOU 3160 ND2 ASN A 564 7157 5931 5883 -125 -519 189 N ATOM 3161 N LEU A 565 54.795 42.449 4.301 1.00 42.68 N ANISOU 3161 N LEU A 565 6090 5068 5057 -280 -482 255 N ATOM 3162 CA LEU A 565 54.629 43.657 5.095 1.00 42.93 C ANISOU 3162 CA LEU A 565 6122 5075 5113 -304 -519 257 C ATOM 3163 C LEU A 565 55.898 44.513 5.070 1.00 45.30 C ANISOU 3163 C LEU A 565 6433 5394 5386 -356 -493 307 C ATOM 3164 O LEU A 565 55.814 45.726 4.914 1.00 37.89 O ANISOU 3164 O LEU A 565 5545 4414 4435 -376 -533 324 O ATOM 3165 CB LEU A 565 54.209 43.322 6.531 1.00 35.21 C ANISOU 3165 CB LEU A 565 5069 4113 4195 -300 -517 222 C ATOM 3166 CG LEU A 565 53.797 44.494 7.420 1.00 30.52 C ANISOU 3166 CG LEU A 565 4478 3487 3630 -314 -562 214 C ATOM 3167 CD1 LEU A 565 52.702 45.301 6.766 1.00 31.60 C ANISOU 3167 CD1 LEU A 565 4684 3557 3765 -286 -632 200 C ATOM 3168 CD2 LEU A 565 53.352 44.001 8.792 1.00 28.84 C ANISOU 3168 CD2 LEU A 565 4194 3288 3474 -305 -550 182 C ATOM 3169 N ARG A 566 57.064 43.879 5.211 1.00 58.19 N ANISOU 3169 N ARG A 566 8016 7084 7007 -376 -429 329 N ATOM 3170 CA ARG A 566 58.346 44.593 5.200 1.00 70.98 C ANISOU 3170 CA ARG A 566 9637 8728 8606 -427 -399 378 C ATOM 3171 C ARG A 566 58.419 45.550 4.014 1.00 75.70 C ANISOU 3171 C ARG A 566 10326 9283 9154 -443 -421 413 C ATOM 3172 O ARG A 566 58.601 46.759 4.184 1.00 79.30 O ANISOU 3172 O ARG A 566 10814 9711 9607 -479 -449 436 O ATOM 3173 CB ARG A 566 59.527 43.619 5.126 1.00 79.81 C ANISOU 3173 CB ARG A 566 10700 9912 9712 -434 -326 398 C ATOM 3174 CG ARG A 566 59.309 42.285 5.820 1.00 88.26 C ANISOU 3174 CG ARG A 566 11699 11019 10818 -401 -303 362 C ATOM 3175 CD ARG A 566 59.670 42.330 7.298 1.00 94.88 C ANISOU 3175 CD ARG A 566 12461 11889 11700 -422 -299 353 C ATOM 3176 NE ARG A 566 59.467 41.033 7.941 1.00 98.44 N ANISOU 3176 NE ARG A 566 12849 12373 12182 -392 -277 321 N ATOM 3177 CZ ARG A 566 60.265 39.982 7.771 1.00100.43 C ANISOU 3177 CZ ARG A 566 13061 12671 12427 -380 -227 331 C ATOM 3178 NH1 ARG A 566 61.320 40.073 6.972 1.00101.47 N ANISOU 3178 NH1 ARG A 566 13206 12826 12523 -395 -189 371 N ATOM 3179 NH2 ARG A 566 60.008 38.839 8.393 1.00100.09 N ANISOU 3179 NH2 ARG A 566 12965 12650 12413 -354 -214 302 N ATOM 3180 N SER A 567 58.269 45.000 2.813 1.00 75.35 N ANISOU 3180 N SER A 567 10329 9233 9069 -417 -409 418 N ATOM 3181 CA SER A 567 58.322 45.797 1.593 1.00 76.34 C ANISOU 3181 CA SER A 567 10549 9318 9139 -430 -428 452 C ATOM 3182 C SER A 567 56.987 46.473 1.275 1.00 76.72 C ANISOU 3182 C SER A 567 10665 9293 9190 -403 -510 428 C ATOM 3183 O SER A 567 56.680 46.721 0.110 1.00 77.92 O ANISOU 3183 O SER A 567 10900 9410 9297 -392 -534 442 O ATOM 3184 CB SER A 567 58.772 44.934 0.413 1.00 77.01 C ANISOU 3184 CB SER A 567 10661 9428 9172 -413 -379 469 C ATOM 3185 OG SER A 567 57.878 43.857 0.198 1.00 75.23 O ANISOU 3185 OG SER A 567 10431 9198 8955 -358 -392 426 O TER 3186 SER A 567 ATOM 3187 O5' U B 1 45.919 21.205 1.375 1.00 29.12 O ANISOU 3187 O5' U B 1 2676 3760 4629 -34 -388 -851 O ATOM 3188 C5' U B 1 44.727 21.805 1.803 1.00 19.86 C ANISOU 3188 C5' U B 1 1512 2763 3271 3 -444 -875 C ATOM 3189 C4' U B 1 44.459 21.405 3.243 1.00 17.15 C ANISOU 3189 C4' U B 1 1222 2429 2864 1 -532 -891 C ATOM 3190 O4' U B 1 45.570 21.815 4.080 1.00 15.99 O ANISOU 3190 O4' U B 1 1074 2100 2903 46 -619 -877 O ATOM 3191 C3' U B 1 43.237 22.079 3.833 1.00 20.73 C ANISOU 3191 C3' U B 1 1704 3041 3132 52 -570 -913 C ATOM 3192 O3' U B 1 42.113 21.268 3.569 1.00 16.70 O ANISOU 3192 O3' U B 1 1208 2698 2441 -10 -512 -933 O ATOM 3193 C2' U B 1 43.577 22.129 5.323 1.00 18.64 C ANISOU 3193 C2' U B 1 1482 2690 2911 82 -671 -914 C ATOM 3194 O2' U B 1 43.279 20.931 5.998 1.00 14.83 O ANISOU 3194 O2' U B 1 1041 2237 2356 16 -671 -922 O ATOM 3195 C1' U B 1 45.083 22.355 5.292 1.00 21.07 C ANISOU 3195 C1' U B 1 1762 2780 3463 101 -712 -891 C ATOM 3196 N1 U B 1 45.368 23.803 5.334 1.00 22.36 N ANISOU 3196 N1 U B 1 1908 2891 3698 192 -759 -885 N ATOM 3197 C2 U B 1 45.317 24.410 6.567 1.00 19.92 C ANISOU 3197 C2 U B 1 1643 2548 3376 249 -863 -895 C ATOM 3198 O2 U B 1 45.063 23.786 7.584 1.00 20.35 O ANISOU 3198 O2 U B 1 1749 2615 3369 229 -913 -904 O ATOM 3199 N3 U B 1 45.576 25.756 6.553 1.00 21.49 N ANISOU 3199 N3 U B 1 1833 2696 3638 327 -901 -891 N ATOM 3200 C4 U B 1 45.879 26.534 5.442 1.00 26.00 C ANISOU 3200 C4 U B 1 2355 3243 4279 356 -841 -876 C ATOM 3201 O4 U B 1 46.090 27.737 5.581 1.00 27.07 O ANISOU 3201 O4 U B 1 2496 3328 4460 423 -881 -875 O ATOM 3202 C5 U B 1 45.915 25.822 4.183 1.00 23.12 C ANISOU 3202 C5 U B 1 1944 2915 3925 300 -729 -863 C ATOM 3203 C6 U B 1 45.653 24.504 4.179 1.00 20.29 C ANISOU 3203 C6 U B 1 1594 2611 3506 219 -695 -870 C ATOM 3204 P G B 2 40.702 21.885 3.136 1.00 21.14 P ANISOU 3204 P G B 2 1758 3462 2814 22 -482 -954 P ATOM 3205 OP1 G B 2 39.963 20.744 2.534 1.00 18.99 O ANISOU 3205 OP1 G B 2 1486 3305 2423 -68 -410 -969 O ATOM 3206 OP2 G B 2 40.935 23.145 2.397 1.00 24.43 O ANISOU 3206 OP2 G B 2 2143 3858 3283 98 -486 -944 O ATOM 3207 O5' G B 2 39.998 22.290 4.521 1.00 23.46 O ANISOU 3207 O5' G B 2 2081 3815 3018 69 -541 -969 O ATOM 3208 C5' G B 2 39.844 21.308 5.529 1.00 18.62 C ANISOU 3208 C5' G B 2 1504 3201 2369 17 -554 -974 C ATOM 3209 C4' G B 2 38.943 21.812 6.629 1.00 18.35 C ANISOU 3209 C4' G B 2 1488 3255 2230 63 -589 -991 C ATOM 3210 O4' G B 2 39.613 22.907 7.298 1.00 23.87 O ANISOU 3210 O4' G B 2 2208 3839 3023 150 -674 -982 O ATOM 3211 C3' G B 2 37.613 22.399 6.176 1.00 22.29 C ANISOU 3211 C3' G B 2 1946 3938 2586 91 -543 -1013 C ATOM 3212 O3' G B 2 36.648 21.370 5.989 1.00 24.55 O ANISOU 3212 O3' G B 2 2214 4358 2756 11 -477 -1029 O ATOM 3213 C2' G B 2 37.274 23.263 7.384 1.00 18.62 C ANISOU 3213 C2' G B 2 1503 3478 2092 165 -604 -1021 C ATOM 3214 O2' G B 2 36.773 22.515 8.477 1.00 19.07 O ANISOU 3214 O2' G B 2 1591 3573 2083 122 -609 -1032 O ATOM 3215 C1' G B 2 38.645 23.828 7.762 1.00 23.12 C ANISOU 3215 C1' G B 2 2109 3852 2821 215 -685 -1000 C ATOM 3216 N9 G B 2 38.875 25.152 7.191 1.00 24.05 N ANISOU 3216 N9 G B 2 2207 3947 2985 298 -702 -995 N ATOM 3217 C8 G B 2 39.210 25.456 5.892 1.00 23.98 C ANISOU 3217 C8 G B 2 2161 3928 3023 302 -663 -985 C ATOM 3218 N7 G B 2 39.327 26.739 5.688 1.00 26.21 N ANISOU 3218 N7 G B 2 2438 4188 3333 385 -689 -983 N ATOM 3219 C5 G B 2 39.044 27.318 6.923 1.00 23.95 C ANISOU 3219 C5 G B 2 2186 3898 3014 438 -749 -994 C ATOM 3220 C6 G B 2 39.019 28.682 7.320 1.00 22.14 C ANISOU 3220 C6 G B 2 1975 3646 2792 532 -797 -998 C ATOM 3221 O6 G B 2 39.244 29.678 6.625 1.00 24.03 O ANISOU 3221 O6 G B 2 2201 3864 3067 585 -795 -992 O ATOM 3222 N1 G B 2 38.690 28.842 8.662 1.00 18.31 N ANISOU 3222 N1 G B 2 1531 3163 2264 560 -852 -1010 N ATOM 3223 C2 G B 2 38.417 27.798 9.518 1.00 19.12 C ANISOU 3223 C2 G B 2 1659 3286 2321 504 -858 -1016 C ATOM 3224 N2 G B 2 38.111 28.131 10.778 1.00 19.40 N ANISOU 3224 N2 G B 2 1742 3316 2313 543 -916 -1026 N ATOM 3225 N3 G B 2 38.429 26.516 9.157 1.00 18.18 N ANISOU 3225 N3 G B 2 1525 3190 2194 414 -811 -1011 N ATOM 3226 C4 G B 2 38.750 26.351 7.853 1.00 20.48 C ANISOU 3226 C4 G B 2 1773 3481 2528 387 -758 -1001 C ATOM 3227 P U B 3 35.484 21.489 4.891 1.00 26.52 P ANISOU 3227 P U B 3 2404 4783 2891 1 -413 -1049 P ATOM 3228 OP1 U B 3 34.717 20.230 4.918 1.00 29.17 O ANISOU 3228 OP1 U B 3 2727 5217 3140 -97 -358 -1065 O ATOM 3229 OP2 U B 3 36.019 21.968 3.596 1.00 24.70 O ANISOU 3229 OP2 U B 3 2161 4512 2713 25 -403 -1038 O ATOM 3230 O5' U B 3 34.600 22.673 5.493 1.00 27.37 O ANISOU 3230 O5' U B 3 2488 4982 2931 91 -441 -1067 O ATOM 3231 C5' U B 3 33.518 23.194 4.734 1.00 23.16 C ANISOU 3231 C5' U B 3 1897 4597 2306 119 -410 -1088 C ATOM 3232 C4' U B 3 32.241 23.026 5.529 1.00 27.06 C ANISOU 3232 C4' U B 3 2353 5231 2697 106 -395 -1117 C ATOM 3233 O4' U B 3 32.400 23.681 6.800 1.00 29.87 O ANISOU 3233 O4' U B 3 2743 5536 3072 166 -446 -1116 O ATOM 3234 C3' U B 3 31.000 23.653 4.929 1.00 32.74 C ANISOU 3234 C3' U B 3 3001 6111 3327 145 -377 -1145 C ATOM 3235 O3' U B 3 30.424 22.718 4.035 1.00 38.74 O ANISOU 3235 O3' U B 3 3724 6961 4036 63 -328 -1159 O ATOM 3236 C2' U B 3 30.132 23.818 6.166 1.00 32.81 C ANISOU 3236 C2' U B 3 2990 6199 3276 159 -386 -1170 C ATOM 3237 O2' U B 3 29.531 22.596 6.535 1.00 34.99 O ANISOU 3237 O2' U B 3 3248 6546 3501 58 -347 -1189 O ATOM 3238 C1' U B 3 31.154 24.190 7.233 1.00 32.06 C ANISOU 3238 C1' U B 3 2971 5953 3256 201 -440 -1147 C ATOM 3239 N1 U B 3 31.301 25.652 7.519 1.00 27.83 N ANISOU 3239 N1 U B 3 2448 5385 2742 318 -489 -1143 N ATOM 3240 C2 U B 3 30.530 26.189 8.520 1.00 26.08 C ANISOU 3240 C2 U B 3 2216 5231 2461 362 -507 -1165 C ATOM 3241 O2 U B 3 29.735 25.525 9.167 1.00 24.87 O ANISOU 3241 O2 U B 3 2045 5164 2241 308 -484 -1187 O ATOM 3242 N3 U B 3 30.723 27.537 8.729 1.00 28.04 N ANISOU 3242 N3 U B 3 2483 5441 2731 470 -552 -1161 N ATOM 3243 C4 U B 3 31.593 28.368 8.048 1.00 26.34 C ANISOU 3243 C4 U B 3 2292 5126 2589 531 -579 -1139 C ATOM 3244 O4 U B 3 31.661 29.550 8.355 1.00 25.08 O ANISOU 3244 O4 U B 3 2151 4939 2439 622 -617 -1140 O ATOM 3245 C5 U B 3 32.360 27.730 7.011 1.00 24.40 C ANISOU 3245 C5 U B 3 2053 4815 2404 476 -556 -1119 C ATOM 3246 C6 U B 3 32.196 26.422 6.793 1.00 24.27 C ANISOU 3246 C6 U B 3 2021 4835 2367 375 -514 -1121 C ATOM 3247 P G B 4 29.696 23.203 2.697 1.00 39.22 P ANISOU 3247 P G B 4 3732 7126 4043 93 -319 -1174 P ATOM 3248 OP1 G B 4 29.561 22.017 1.829 1.00 37.62 O ANISOU 3248 OP1 G B 4 3522 6955 3817 -7 -279 -1178 O ATOM 3249 OP2 G B 4 30.362 24.417 2.173 1.00 39.84 O ANISOU 3249 OP2 G B 4 3838 7128 4171 191 -354 -1154 O ATOM 3250 O5' G B 4 28.260 23.631 3.263 1.00 44.90 O ANISOU 3250 O5' G B 4 4379 8004 4677 124 -323 -1215 O ATOM 3251 C5' G B 4 27.479 22.687 3.965 1.00 45.17 C ANISOU 3251 C5' G B 4 4379 8124 4661 42 -295 -1242 C ATOM 3252 C4' G B 4 26.121 23.264 4.318 1.00 46.08 C ANISOU 3252 C4' G B 4 4415 8391 4702 82 -303 -1286 C ATOM 3253 O4' G B 4 26.321 24.401 5.195 1.00 47.27 O ANISOU 3253 O4' G B 4 4588 8502 4871 180 -340 -1280 O ATOM 3254 C3' G B 4 25.280 23.822 3.173 1.00 44.32 C ANISOU 3254 C3' G B 4 4129 8277 4434 124 -316 -1310 C ATOM 3255 O3' G B 4 24.534 22.799 2.529 1.00 48.85 O ANISOU 3255 O3' G B 4 4654 8944 4961 32 -291 -1338 O ATOM 3256 C2' G B 4 24.316 24.685 3.957 1.00 41.28 C ANISOU 3256 C2' G B 4 3688 7992 4005 192 -337 -1345 C ATOM 3257 O2' G B 4 23.340 23.889 4.586 1.00 39.78 O ANISOU 3257 O2' G B 4 3439 7912 3762 114 -312 -1386 O ATOM 3258 C1' G B 4 25.227 25.278 5.024 1.00 43.53 C ANISOU 3258 C1' G B 4 4043 8156 4340 248 -356 -1314 C ATOM 3259 N9 G B 4 25.730 26.578 4.640 1.00 39.49 N ANISOU 3259 N9 G B 4 3561 7582 3861 361 -392 -1293 N ATOM 3260 C8 G B 4 26.835 26.866 3.884 1.00 39.74 C ANISOU 3260 C8 G B 4 3652 7491 3955 388 -403 -1255 C ATOM 3261 N7 G B 4 27.003 28.151 3.714 1.00 43.50 N ANISOU 3261 N7 G B 4 4144 7940 4444 494 -436 -1248 N ATOM 3262 C5 G B 4 25.942 28.735 4.394 1.00 39.16 C ANISOU 3262 C5 G B 4 3540 7503 3835 542 -447 -1282 C ATOM 3263 C6 G B 4 25.594 30.092 4.570 1.00 39.16 C ANISOU 3263 C6 G B 4 3532 7530 3817 655 -480 -1291 C ATOM 3264 O6 G B 4 26.177 31.092 4.140 1.00 44.38 O ANISOU 3264 O6 G B 4 4236 8117 4509 736 -505 -1271 O ATOM 3265 N1 G B 4 24.436 30.238 5.330 1.00 36.47 N ANISOU 3265 N1 G B 4 3127 7317 3414 668 -480 -1331 N ATOM 3266 C2 G B 4 23.713 29.197 5.859 1.00 37.06 C ANISOU 3266 C2 G B 4 3151 7481 3450 579 -453 -1359 C ATOM 3267 N2 G B 4 22.622 29.517 6.561 1.00 37.58 N ANISOU 3267 N2 G B 4 3152 7666 3459 603 -458 -1399 N ATOM 3268 N3 G B 4 24.028 27.920 5.704 1.00 39.82 N ANISOU 3268 N3 G B 4 3512 7804 3814 469 -421 -1351 N ATOM 3269 C4 G B 4 25.148 27.772 4.964 1.00 39.33 C ANISOU 3269 C4 G B 4 3513 7619 3812 460 -421 -1311 C ATOM 3270 P C B 5 23.933 22.974 1.048 1.00 55.34 P ANISOU 3270 P C B 5 5437 9843 5747 46 -311 -1355 P ATOM 3271 OP1 C B 5 23.326 21.668 0.721 1.00 60.82 O ANISOU 3271 OP1 C B 5 6097 10610 6403 -72 -283 -1382 O ATOM 3272 OP2 C B 5 24.926 23.577 0.131 1.00 51.26 O ANISOU 3272 OP2 C B 5 4985 9216 5273 105 -330 -1314 O ATOM 3273 O5' C B 5 22.770 24.036 1.250 1.00 39.15 O ANISOU 3273 O5' C B 5 3308 7917 3649 133 -348 -1396 O ATOM 3274 C5' C B 5 21.588 23.573 1.857 1.00 45.72 C ANISOU 3274 C5' C B 5 4057 8882 4433 82 -339 -1447 C ATOM 3275 C4' C B 5 20.634 24.719 2.125 1.00 49.12 C ANISOU 3275 C4' C B 5 4418 9414 4832 179 -378 -1483 C ATOM 3276 O4' C B 5 21.261 25.711 2.976 1.00 41.61 O ANISOU 3276 O4' C B 5 3515 8386 3910 268 -386 -1455 O ATOM 3277 C3' C B 5 20.198 25.464 0.873 1.00 56.73 C ANISOU 3277 C3' C B 5 5354 10423 5777 251 -428 -1493 C ATOM 3278 O3' C B 5 19.047 24.842 0.322 1.00 62.23 O ANISOU 3278 O3' C B 5 5964 11247 6435 192 -445 -1543 O ATOM 3279 C2' C B 5 19.825 26.826 1.432 1.00 55.31 C ANISOU 3279 C2' C B 5 5148 10277 5591 370 -459 -1504 C ATOM 3280 O2' C B 5 18.487 26.828 1.896 1.00 54.95 O ANISOU 3280 O2' C B 5 4993 10379 5508 362 -472 -1562 O ATOM 3281 C1' C B 5 20.826 26.997 2.582 1.00 49.02 C ANISOU 3281 C1' C B 5 4426 9367 4833 384 -430 -1466 C ATOM 3282 N1 C B 5 21.994 27.830 2.189 1.00 48.96 N ANISOU 3282 N1 C B 5 4507 9223 4872 463 -445 -1415 N ATOM 3283 C2 C B 5 21.873 29.210 2.301 1.00 48.93 C ANISOU 3283 C2 C B 5 4505 9222 4864 584 -480 -1416 C ATOM 3284 O2 C B 5 20.809 29.654 2.733 1.00 55.35 O ANISOU 3284 O2 C B 5 5244 10150 5634 621 -497 -1456 O ATOM 3285 N3 C B 5 22.912 30.004 1.941 1.00 45.09 N ANISOU 3285 N3 C B 5 4098 8613 4421 654 -495 -1374 N ATOM 3286 C4 C B 5 24.042 29.463 1.480 1.00 40.77 C ANISOU 3286 C4 C B 5 3620 7944 3925 607 -477 -1334 C ATOM 3287 N4 C B 5 25.044 30.287 1.142 1.00 32.06 N ANISOU 3287 N4 C B 5 2589 6723 2870 675 -493 -1298 N ATOM 3288 C5 C B 5 24.182 28.050 1.349 1.00 43.84 C ANISOU 3288 C5 C B 5 4008 8330 4320 487 -442 -1332 C ATOM 3289 C6 C B 5 23.147 27.277 1.709 1.00 46.77 C ANISOU 3289 C6 C B 5 4306 8822 4643 418 -426 -1372 C ATOM 3290 P C B 6 18.838 24.848 -1.261 1.00 56.04 P ANISOU 3290 P C B 6 6383 9555 5354 65 -56 -1285 P ATOM 3291 OP1 C B 6 17.573 24.132 -1.545 1.00 60.15 O ANISOU 3291 OP1 C B 6 6770 10252 5832 39 17 -1282 O ATOM 3292 OP2 C B 6 20.113 24.403 -1.882 1.00 49.14 O ANISOU 3292 OP2 C B 6 5572 8483 4614 -82 -34 -1242 O ATOM 3293 O5' C B 6 18.642 26.399 -1.600 1.00 44.28 O ANISOU 3293 O5' C B 6 5001 8028 3798 213 -177 -1367 O ATOM 3294 C5' C B 6 17.413 27.064 -1.369 1.00 47.10 C ANISOU 3294 C5' C B 6 5317 8544 4033 359 -216 -1424 C ATOM 3295 C4' C B 6 17.529 28.531 -1.748 1.00 49.01 C ANISOU 3295 C4' C B 6 5678 8699 4245 482 -330 -1492 C ATOM 3296 O4' C B 6 18.580 29.149 -0.969 1.00 50.29 O ANISOU 3296 O4' C B 6 5940 8740 4427 533 -388 -1502 O ATOM 3297 C3' C B 6 17.932 28.834 -3.184 1.00 54.09 C ANISOU 3297 C3' C B 6 6393 9199 4959 411 -357 -1496 C ATOM 3298 O3' C B 6 16.805 28.722 -4.044 1.00 57.08 O ANISOU 3298 O3' C B 6 6699 9695 5293 410 -338 -1512 O ATOM 3299 C2' C B 6 18.387 30.283 -3.029 1.00 58.48 C ANISOU 3299 C2' C B 6 7079 9645 5495 545 -471 -1552 C ATOM 3300 O2' C B 6 17.298 31.179 -2.901 1.00 63.05 O ANISOU 3300 O2' C B 6 7641 10344 5969 704 -526 -1612 O ATOM 3301 C1' C B 6 19.151 30.213 -1.708 1.00 55.37 C ANISOU 3301 C1' C B 6 6709 9222 5106 570 -473 -1541 C ATOM 3302 N1 C B 6 20.610 29.937 -1.852 1.00 60.29 N ANISOU 3302 N1 C B 6 7415 9650 5843 456 -468 -1501 N ATOM 3303 C2 C B 6 21.502 30.989 -2.106 1.00 65.50 C ANISOU 3303 C2 C B 6 8210 10132 6543 500 -553 -1535 C ATOM 3304 O2 C B 6 21.068 32.145 -2.211 1.00 70.68 O ANISOU 3304 O2 C B 6 8917 10793 7144 635 -632 -1597 O ATOM 3305 N3 C B 6 22.825 30.710 -2.229 1.00 61.71 N ANISOU 3305 N3 C B 6 7803 9477 6167 394 -546 -1499 N ATOM 3306 C4 C B 6 23.260 29.454 -2.108 1.00 59.52 C ANISOU 3306 C4 C B 6 7466 9197 5954 251 -458 -1430 C ATOM 3307 N4 C B 6 24.572 29.230 -2.240 1.00 57.20 N ANISOU 3307 N4 C B 6 7244 8726 5762 151 -455 -1397 N ATOM 3308 C5 C B 6 22.368 28.369 -1.851 1.00 58.76 C ANISOU 3308 C5 C B 6 7229 9275 5822 204 -369 -1392 C ATOM 3309 C6 C B 6 21.066 28.656 -1.728 1.00 58.92 C ANISOU 3309 C6 C B 6 7180 9468 5738 309 -377 -1430 C ATOM 3310 P U B 7 16.979 28.589 -5.629 1.00 63.57 P ANISOU 3310 P U B 7 7544 10426 6183 297 -329 -1502 P ATOM 3311 OP1 U B 7 18.429 28.501 -5.921 1.00 64.59 O ANISOU 3311 OP1 U B 7 7773 10343 6427 193 -336 -1471 O ATOM 3312 OP2 U B 7 16.150 29.634 -6.273 1.00 60.55 O ANISOU 3312 OP2 U B 7 7184 10095 5726 415 -402 -1554 O ATOM 3313 O5' U B 7 16.310 27.170 -5.937 1.00 50.09 O ANISOU 3313 O5' U B 7 5691 8850 4490 164 -212 -1465 O ATOM 3314 C5' U B 7 16.867 25.997 -5.352 1.00 52.55 C ANISOU 3314 C5' U B 7 5950 9146 4871 45 -124 -1408 C ATOM 3315 C4' U B 7 15.766 25.054 -4.901 1.00 54.94 C ANISOU 3315 C4' U B 7 6101 9652 5123 30 -37 -1393 C ATOM 3316 O4' U B 7 15.192 25.541 -3.664 1.00 54.52 O ANISOU 3316 O4' U B 7 6028 9721 4966 184 -70 -1417 O ATOM 3317 C3' U B 7 14.567 24.964 -5.837 1.00 54.51 C ANISOU 3317 C3' U B 7 5965 9732 5017 27 -17 -1425 C ATOM 3318 O3' U B 7 14.783 24.053 -6.890 1.00 53.31 O ANISOU 3318 O3' U B 7 5768 9534 4952 -144 57 -1399 O ATOM 3319 C2' U B 7 13.493 24.431 -4.908 1.00 55.64 C ANISOU 3319 C2' U B 7 5982 10081 5079 81 39 -1423 C ATOM 3320 O2' U B 7 13.610 23.038 -4.697 1.00 58.45 O ANISOU 3320 O2' U B 7 6239 10466 5505 -61 154 -1367 O ATOM 3321 C1' U B 7 13.811 25.208 -3.637 1.00 53.09 C ANISOU 3321 C1' U B 7 5725 9745 4702 222 -28 -1435 C ATOM 3322 N1 U B 7 12.987 26.440 -3.542 1.00 46.92 N ANISOU 3322 N1 U B 7 4974 9046 3807 400 -119 -1503 N ATOM 3323 C2 U B 7 11.691 26.297 -3.105 1.00 47.40 C ANISOU 3323 C2 U B 7 4926 9314 3769 478 -94 -1526 C ATOM 3324 O2 U B 7 11.221 25.212 -2.805 1.00 46.62 O ANISOU 3324 O2 U B 7 4711 9329 3672 404 0 -1492 O ATOM 3325 N3 U B 7 10.972 27.467 -3.034 1.00 47.09 N ANISOU 3325 N3 U B 7 4918 9341 3633 644 -180 -1589 N ATOM 3326 C4 U B 7 11.418 28.736 -3.357 1.00 43.47 C ANISOU 3326 C4 U B 7 4585 8760 3173 738 -285 -1629 C ATOM 3327 O4 U B 7 10.654 29.689 -3.244 1.00 42.88 O ANISOU 3327 O4 U B 7 4519 8762 3012 886 -350 -1683 O ATOM 3328 C5 U B 7 12.787 28.800 -3.812 1.00 42.25 C ANISOU 3328 C5 U B 7 4539 8389 3125 646 -304 -1600 C ATOM 3329 C6 U B 7 13.506 27.673 -3.888 1.00 42.41 C ANISOU 3329 C6 U B 7 4532 8344 3237 484 -223 -1540 C ATOM 3330 P U B 8 14.491 24.550 -8.378 1.00 57.01 P ANISOU 3330 P U B 8 6264 9982 5417 -165 18 -1435 P ATOM 3331 OP1 U B 8 15.128 23.584 -9.299 1.00 59.76 O ANISOU 3331 OP1 U B 8 6589 10238 5881 -359 93 -1404 O ATOM 3332 OP2 U B 8 14.845 25.987 -8.461 1.00 61.36 O ANISOU 3332 OP2 U B 8 6949 10435 5930 -33 -103 -1468 O ATOM 3333 O5' U B 8 12.897 24.443 -8.480 1.00 39.10 O ANISOU 3333 O5' U B 8 3872 7944 3040 -99 43 -1470 O ATOM 3334 C5' U B 8 12.231 24.797 -9.699 1.00 33.13 C ANISOU 3334 C5' U B 8 3099 7242 2248 -98 19 -1505 C ATOM 3335 C4' U B 8 10.947 24.001 -9.802 1.00 30.17 C ANISOU 3335 C4' U B 8 2568 7077 1819 -125 98 -1519 C ATOM 3336 O4' U B 8 9.934 24.616 -8.972 1.00 29.50 O ANISOU 3336 O4' U B 8 2453 7143 1614 46 56 -1551 O ATOM 3337 C3' U B 8 10.332 23.953 -11.182 1.00 29.93 C ANISOU 3337 C3' U B 8 2489 7110 1772 -181 107 -1547 C ATOM 3338 O3' U B 8 10.904 22.861 -11.890 1.00 34.66 O ANISOU 3338 O3' U B 8 3046 7642 2482 -377 195 -1521 O ATOM 3339 C2' U B 8 8.851 23.717 -10.885 1.00 29.07 C ANISOU 3339 C2' U B 8 2251 7234 1562 -112 141 -1577 C ATOM 3340 O2' U B 8 8.500 22.349 -10.846 1.00 32.48 O ANISOU 3340 O2' U B 8 2549 7755 2036 -245 263 -1561 O ATOM 3341 C1' U B 8 8.657 24.330 -9.501 1.00 28.42 C ANISOU 3341 C1' U B 8 2199 7190 1408 50 92 -1581 C ATOM 3342 N1 U B 8 7.847 25.582 -9.523 1.00 32.61 N ANISOU 3342 N1 U B 8 2762 7802 1825 232 -6 -1628 N ATOM 3343 C2 U B 8 6.480 25.484 -9.679 1.00 34.79 C ANISOU 3343 C2 U B 8 2928 8282 2010 285 14 -1662 C ATOM 3344 O2 U B 8 5.896 24.427 -9.805 1.00 33.68 O ANISOU 3344 O2 U B 8 2662 8258 1875 189 109 -1657 O ATOM 3345 N3 U B 8 5.803 26.678 -9.684 1.00 37.05 N ANISOU 3345 N3 U B 8 3250 8629 2199 456 -79 -1702 N ATOM 3346 C4 U B 8 6.341 27.941 -9.563 1.00 36.43 C ANISOU 3346 C4 U B 8 3304 8428 2111 576 -187 -1714 C ATOM 3347 O4 U B 8 5.594 28.913 -9.597 1.00 35.07 O ANISOU 3347 O4 U B 8 3143 8330 1853 725 -259 -1751 O ATOM 3348 C5 U B 8 7.776 27.967 -9.402 1.00 34.86 C ANISOU 3348 C5 U B 8 3217 8019 2011 510 -201 -1680 C ATOM 3349 C6 U B 8 8.462 26.814 -9.390 1.00 32.92 C ANISOU 3349 C6 U B 8 2939 7713 1856 345 -113 -1639 C ATOM 3350 P A B 9 11.137 22.920 -13.477 1.00 48.44 P ANISOU 3350 P A B 9 4811 9329 4267 -481 187 -1537 P ATOM 3351 OP1 A B 9 12.211 21.960 -13.792 1.00 53.65 O ANISOU 3351 OP1 A B 9 5474 9848 5063 -666 261 -1502 O ATOM 3352 OP2 A B 9 11.267 24.329 -13.910 1.00 48.12 O ANISOU 3352 OP2 A B 9 4889 9224 4171 -355 64 -1556 O ATOM 3353 O5' A B 9 9.756 22.362 -14.059 1.00 54.47 O ANISOU 3353 O5' A B 9 5422 10310 4964 -508 247 -1572 O ATOM 3354 C5' A B 9 9.171 21.142 -13.600 1.00 51.71 C ANISOU 3354 C5' A B 9 4932 10083 4632 -588 361 -1567 C ATOM 3355 C4' A B 9 8.117 20.687 -14.592 1.00 50.65 C ANISOU 3355 C4' A B 9 4675 10113 4458 -648 411 -1608 C ATOM 3356 O4' A B 9 7.090 21.710 -14.716 1.00 47.65 O ANISOU 3356 O4' A B 9 4297 9866 3944 -484 328 -1646 O ATOM 3357 C3' A B 9 8.659 20.484 -15.999 1.00 52.86 C ANISOU 3357 C3' A B 9 4969 10311 4805 -789 423 -1618 C ATOM 3358 O3' A B 9 7.919 19.465 -16.664 1.00 54.46 O ANISOU 3358 O3' A B 9 5024 10650 5019 -912 523 -1647 O ATOM 3359 C2' A B 9 8.437 21.864 -16.618 1.00 50.41 C ANISOU 3359 C2' A B 9 4749 10002 4404 -657 300 -1640 C ATOM 3360 O2' A B 9 8.424 21.862 -18.034 1.00 46.26 O ANISOU 3360 O2' A B 9 4207 9483 3885 -746 299 -1661 O ATOM 3361 C1' A B 9 7.063 22.196 -16.043 1.00 48.28 C ANISOU 3361 C1' A B 9 4403 9935 4007 -509 283 -1669 C ATOM 3362 N9 A B 9 6.773 23.630 -16.078 1.00 48.82 N ANISOU 3362 N9 A B 9 4562 10008 3980 -328 158 -1682 N ATOM 3363 C8 A B 9 7.644 24.664 -15.857 1.00 51.40 C ANISOU 3363 C8 A B 9 5039 10169 4320 -241 62 -1662 C ATOM 3364 N7 A B 9 7.105 25.856 -15.977 1.00 48.76 N ANISOU 3364 N7 A B 9 4753 9879 3894 -80 -36 -1681 N ATOM 3365 C5 A B 9 5.792 25.582 -16.305 1.00 45.06 C ANISOU 3365 C5 A B 9 4157 9624 3341 -60 -3 -1714 C ATOM 3366 C6 A B 9 4.687 26.410 -16.565 1.00 45.96 C ANISOU 3366 C6 A B 9 4243 9881 3339 83 -66 -1744 C ATOM 3367 N6 A B 9 4.744 27.746 -16.536 1.00 42.79 N ANISOU 3367 N6 A B 9 3946 9422 2890 239 -178 -1744 N ATOM 3368 N1 A B 9 3.515 25.808 -16.859 1.00 48.74 N ANISOU 3368 N1 A B 9 4451 10438 3629 58 -7 -1774 N ATOM 3369 C2 A B 9 3.446 24.478 -16.888 1.00 51.04 C ANISOU 3369 C2 A B 9 4635 10784 3974 -98 108 -1777 C ATOM 3370 N3 A B 9 4.417 23.599 -16.661 1.00 52.29 N ANISOU 3370 N3 A B 9 4805 10815 4246 -240 178 -1749 N ATOM 3371 C4 A B 9 5.571 24.220 -16.372 1.00 46.98 C ANISOU 3371 C4 A B 9 4277 9944 3629 -212 116 -1717 C TER 3372 A B 9 HETATM 3373 C1 EDO A 576 48.436 23.050 10.419 1.00 26.28 C HETATM 3374 O1 EDO A 576 48.088 24.066 9.452 1.00 23.05 O HETATM 3375 C2 EDO A 576 47.755 21.725 10.070 1.00 25.52 C HETATM 3376 O2 EDO A 576 46.491 22.001 9.437 1.00 24.59 O HETATM 3377 O HOH A 1 32.097 23.557 16.314 1.00 15.99 O HETATM 3378 O HOH A 2 39.601 28.023 25.889 1.00 17.87 O HETATM 3379 O HOH A 3 -15.812 31.700 -23.595 1.00 20.40 O HETATM 3380 O HOH A 4 54.992 30.609 26.414 1.00 13.04 O HETATM 3381 O HOH A 6 -13.792 23.461 -19.168 1.00 19.18 O HETATM 3382 O HOH A 8 48.300 24.155 6.537 1.00 15.46 O HETATM 3383 O HOH A 9 6.698 55.797 6.810 1.00 14.14 O HETATM 3384 O HOH A 10 48.538 29.865 11.392 1.00 15.87 O HETATM 3385 O HOH A 12 8.308 42.543 6.865 1.00 19.52 O HETATM 3386 O HOH A 13 55.407 25.421 18.169 1.00 21.79 O HETATM 3387 O HOH A 14 57.102 18.220 6.651 1.00 9.13 O HETATM 3388 O HOH A 15 4.032 43.397 -2.628 1.00 13.79 O HETATM 3389 O HOH A 16 1.596 15.440 -18.973 1.00 30.46 O HETATM 3390 O HOH A 17 -12.050 33.205 -6.054 1.00 25.29 O HETATM 3391 O HOH A 18 4.203 45.743 11.724 1.00 24.11 O HETATM 3392 O HOH A 19 13.084 36.863 2.661 1.00 23.49 O HETATM 3393 O HOH A 20 38.347 43.829 15.463 1.00 15.67 O HETATM 3394 O HOH A 21 14.854 25.041 -0.088 1.00 35.42 O HETATM 3395 O HOH A 23 56.555 27.442 30.113 1.00 16.87 O HETATM 3396 O HOH A 24 -12.466 25.771 -9.217 1.00 26.94 O HETATM 3397 O HOH A 25 49.580 29.150 26.994 1.00 18.39 O HETATM 3398 O HOH A 26 14.898 19.792 7.616 1.00 20.93 O HETATM 3399 O HOH A 27 -1.651 36.681 -14.651 1.00 27.96 O HETATM 3400 O HOH A 28 -16.427 35.102 -1.144 1.00 29.76 O HETATM 3401 O HOH A 29 42.387 32.615 8.069 1.00 16.12 O HETATM 3402 O HOH A 31 -4.374 38.162 -19.892 1.00 17.12 O HETATM 3403 O HOH A 32 22.497 20.084 13.409 1.00 18.70 O HETATM 3404 O HOH A 33 24.607 48.722 15.845 1.00 30.98 O HETATM 3405 O HOH A 34 41.152 19.272 8.731 1.00 22.61 O HETATM 3406 O HOH A 35 48.131 32.028 26.573 1.00 15.31 O HETATM 3407 O HOH A 36 13.155 39.482 3.668 1.00 24.90 O HETATM 3408 O HOH A 37 62.587 27.207 13.330 1.00 18.10 O HETATM 3409 O HOH A 38 13.380 41.508 2.384 1.00 26.57 O HETATM 3410 O HOH A 40 16.535 30.618 1.006 1.00 20.56 O HETATM 3411 O HOH A 41 18.942 47.787 16.779 1.00 23.27 O HETATM 3412 O HOH A 43 54.435 50.275 19.270 1.00 23.97 O HETATM 3413 O HOH A 44 42.202 25.634 3.344 1.00 26.97 O HETATM 3414 O HOH A 45 -5.329 45.973 1.538 1.00 18.87 O HETATM 3415 O HOH A 46 -0.616 35.405 -8.616 1.00 19.67 O HETATM 3416 O HOH A 47 8.188 46.736 12.248 1.00 26.60 O HETATM 3417 O HOH A 48 -13.049 23.345 -12.717 1.00 23.64 O HETATM 3418 O HOH A 49 16.927 45.586 19.672 1.00 21.93 O HETATM 3419 O HOH A 51 45.042 19.241 14.309 1.00 28.59 O HETATM 3420 O HOH A 52 -6.568 45.932 -9.200 1.00 27.16 O HETATM 3421 O HOH A 53 53.297 48.843 4.385 1.00 32.30 O HETATM 3422 O HOH A 54 14.925 39.662 5.810 1.00 19.14 O HETATM 3423 O HOH A 55 -6.145 41.088 -16.911 1.00 20.14 O HETATM 3424 O HOH A 57 61.819 27.689 17.715 1.00 25.61 O HETATM 3425 O HOH A 58 10.341 56.919 8.865 1.00 19.33 O HETATM 3426 O HOH A 59 -17.868 40.949 -4.908 1.00 21.52 O HETATM 3427 O HOH A 60 -18.218 24.620 -18.864 1.00 33.57 O HETATM 3428 O HOH A 61 6.249 46.895 10.299 1.00 19.15 O HETATM 3429 O HOH A 62 -6.275 46.224 -13.480 1.00 17.97 O HETATM 3430 O HOH A 63 19.469 46.557 14.354 1.00 23.36 O HETATM 3431 O HOH A 64 4.051 32.800 19.441 1.00 28.98 O HETATM 3432 O HOH A 65 -6.546 39.506 -19.000 1.00 35.20 O HETATM 3433 O HOH A 66 9.366 44.238 4.933 1.00 24.60 O HETATM 3434 O HOH A 67 10.597 33.115 -0.482 1.00 30.45 O HETATM 3435 O HOH A 69 56.197 27.738 23.599 1.00 32.80 O HETATM 3436 O HOH A 70 -3.730 40.615 -15.931 1.00 27.34 O HETATM 3437 O HOH A 71 54.273 22.596 18.226 1.00 21.16 O HETATM 3438 O HOH A 73 12.660 54.496 10.086 1.00 26.60 O HETATM 3439 O HOH A 74 24.218 47.887 18.259 1.00 29.50 O HETATM 3440 O HOH A 75 14.066 45.098 5.506 1.00 20.83 O HETATM 3441 O HOH A 76 -16.298 37.020 -10.818 1.00 22.33 O HETATM 3442 O HOH A 77 -14.731 46.112 -7.089 1.00 22.83 O HETATM 3443 O HOH A 78 33.177 45.473 11.640 1.00 29.23 O HETATM 3444 O HOH A 81 -7.136 46.522 -4.411 1.00 24.63 O HETATM 3445 O HOH A 82 3.892 44.774 3.809 1.00 16.03 O HETATM 3446 O HOH A 83 61.462 22.699 7.560 1.00 34.83 O HETATM 3447 O HOH A 84 -12.389 42.481 -18.040 1.00 34.64 O HETATM 3448 O HOH A 85 -7.700 41.184 -21.161 1.00 28.81 O HETATM 3449 O HOH A 86 40.078 36.259 28.301 1.00 20.14 O HETATM 3450 O HOH A 87 26.926 33.846 8.087 1.00 25.08 O HETATM 3451 O HOH A 88 50.506 32.598 31.083 1.00 24.68 O HETATM 3452 O HOH A 89 56.190 28.337 27.065 1.00 19.73 O HETATM 3453 O HOH A 91 50.218 27.714 10.882 1.00 16.73 O HETATM 3454 O HOH A 92 -13.856 23.121 -15.251 1.00 17.11 O HETATM 3455 O HOH A 93 12.963 32.246 -0.247 1.00 30.43 O HETATM 3456 O HOH A 94 27.728 17.970 13.559 1.00 45.04 O HETATM 3457 O HOH A 95 48.195 21.581 17.673 1.00 22.82 O HETATM 3458 O HOH A 96 -11.088 31.616 -27.298 1.00 18.32 O HETATM 3459 O HOH A 97 32.352 33.212 27.657 1.00 28.97 O HETATM 3460 O HOH A 98 -2.157 25.652 15.566 1.00 29.51 O HETATM 3461 O HOH A 99 -6.970 33.812 8.124 1.00 31.92 O HETATM 3462 O HOH A 100 16.109 51.336 9.846 1.00 23.66 O HETATM 3463 O HOH A 101 7.977 44.176 19.618 1.00 28.27 O HETATM 3464 O HOH A 102 4.227 43.696 20.355 1.00 16.77 O HETATM 3465 O HOH A 103 22.731 45.544 8.433 1.00 29.48 O HETATM 3466 O HOH A 105 50.559 42.949 24.851 1.00 24.42 O HETATM 3467 O HOH A 106 28.373 45.325 8.934 1.00 35.30 O HETATM 3468 O HOH A 107 62.448 36.564 17.507 1.00 34.13 O HETATM 3469 O HOH A 108 55.709 19.470 4.531 1.00 20.07 O HETATM 3470 O HOH A 109 41.755 38.589 28.077 1.00 27.32 O HETATM 3471 O HOH A 111 4.481 37.170 -8.160 1.00 29.75 O HETATM 3472 O HOH A 112 -11.744 41.302 -0.868 1.00 28.41 O HETATM 3473 O HOH A 113 9.218 28.051 -13.194 1.00 28.01 O HETATM 3474 O HOH A 114 22.664 49.547 6.868 1.00 26.70 O HETATM 3475 O HOH A 115 50.400 31.624 23.744 1.00 24.29 O HETATM 3476 O HOH A 116 33.360 39.146 7.889 1.00 25.60 O HETATM 3477 O HOH A 117 -16.782 35.104 -6.274 1.00 35.58 O HETATM 3478 O HOH A 118 51.751 33.839 -3.112 1.00 29.79 O HETATM 3479 O HOH A 119 -17.659 28.108 -16.195 1.00 20.29 O HETATM 3480 O HOH A 120 16.762 44.528 6.727 1.00 31.99 O HETATM 3481 O HOH A 121 1.721 16.992 -9.356 1.00 25.18 O HETATM 3482 O HOH A 123 57.702 27.295 20.542 1.00 28.73 O HETATM 3483 O HOH A 124 10.043 44.974 10.926 1.00 33.10 O HETATM 3484 O HOH A 125 19.041 20.012 8.569 1.00 28.52 O HETATM 3485 O HOH A 126 5.262 18.058 -1.416 1.00 42.29 O HETATM 3486 O HOH A 127 -16.203 38.475 -13.618 1.00 27.35 O HETATM 3487 O HOH A 128 40.706 43.789 9.526 1.00 43.93 O HETATM 3488 O HOH A 129 1.597 34.275 -12.807 1.00 37.26 O HETATM 3489 O HOH A 130 8.138 44.514 8.974 1.00 24.80 O HETATM 3490 O HOH A 131 9.272 19.459 7.648 1.00 31.28 O HETATM 3491 O HOH A 132 -15.977 32.798 -7.774 1.00 29.31 O HETATM 3492 O HOH A 133 18.935 35.514 5.079 1.00 21.95 O HETATM 3493 O HOH A 134 5.610 23.258 19.542 1.00 40.07 O HETATM 3494 O HOH A 135 -1.447 36.684 12.010 1.00 41.07 O HETATM 3495 O HOH A 136 39.991 30.777 30.020 1.00 32.32 O HETATM 3496 O HOH A 137 -0.675 40.309 -9.412 1.00 34.44 O HETATM 3497 O HOH A 138 -0.420 15.857 -13.702 1.00 29.92 O HETATM 3498 O HOH A 139 48.427 26.507 26.988 1.00 34.84 O HETATM 3499 O HOH A 140 -8.937 18.407 -4.005 1.00 34.27 O HETATM 3500 O HOH A 141 33.925 46.619 15.487 1.00 32.76 O HETATM 3501 O HOH A 142 -13.239 27.830 2.465 1.00 43.63 O HETATM 3502 O HOH A 143 37.745 22.107 21.369 1.00 28.48 O HETATM 3503 O HOH A 145 43.003 35.193 7.457 1.00 26.94 O HETATM 3504 O HOH A 146 26.893 20.163 14.817 1.00 31.21 O HETATM 3505 O HOH A 147 2.055 31.432 -13.741 1.00 31.58 O HETATM 3506 O HOH A 148 -17.671 36.794 0.299 1.00 28.77 O HETATM 3507 O HOH A 149 -16.525 34.368 -11.818 1.00 34.08 O HETATM 3508 O HOH A 150 52.542 21.146 2.641 1.00 40.98 O HETATM 3509 O HOH A 152 25.293 50.714 9.194 1.00 31.18 O HETATM 3510 O HOH A 153 9.460 20.991 20.421 1.00 45.06 O HETATM 3511 O HOH A 154 -2.560 41.401 -11.115 1.00 22.52 O HETATM 3512 O HOH A 155 -10.224 42.507 -22.987 1.00 22.87 O HETATM 3513 O HOH A 156 30.987 46.331 18.170 1.00 34.51 O HETATM 3514 O HOH A 157 9.431 33.313 23.255 1.00 35.69 O HETATM 3515 O HOH A 158 -12.811 20.374 -16.001 1.00 20.27 O HETATM 3516 O HOH A 159 21.991 46.670 17.159 1.00 37.64 O HETATM 3517 O HOH A 160 -7.663 30.633 -27.810 1.00 28.00 O HETATM 3518 O HOH A 161 41.533 54.127 24.025 1.00 41.83 O HETATM 3519 O HOH A 162 55.943 24.983 31.018 1.00 20.02 O HETATM 3520 O HOH A 577 42.007 32.863 29.569 1.00 33.87 O HETATM 3521 O HOH A 578 26.553 24.270 25.336 1.00 40.99 O HETATM 3522 O HOH A 579 21.123 41.619 9.952 1.00 14.07 O HETATM 3523 O HOH A 580 -5.771 47.712 -11.146 1.00 40.18 O HETATM 3524 O HOH A 581 30.430 28.434 4.158 1.00 39.34 O HETATM 3525 O HOH A 582 -16.055 44.144 -5.625 1.00 31.58 O HETATM 3526 O HOH A 583 -10.298 42.250 8.759 1.00 42.53 O HETATM 3527 O HOH A 584 -17.130 39.380 0.283 1.00 37.34 O HETATM 3528 O HOH A 585 31.935 49.287 22.226 1.00 47.30 O HETATM 3529 O HOH A 586 4.006 41.681 22.528 1.00 34.59 O HETATM 3530 O HOH A 587 2.729 34.998 20.716 1.00 31.09 O HETATM 3531 O HOH A 588 34.715 55.140 19.113 1.00 26.41 O HETATM 3532 O HOH A 589 -12.223 46.596 -7.064 1.00 32.86 O HETATM 3533 O HOH A 590 17.049 30.480 24.356 1.00 39.35 O HETATM 3534 O HOH A 591 -17.186 19.699 -15.455 1.00 39.30 O HETATM 3535 O HOH A 592 13.215 36.024 24.361 1.00 23.54 O HETATM 3536 O HOH A 593 -11.047 17.966 -7.387 1.00 32.88 O HETATM 3537 O HOH A 594 59.021 29.762 19.917 1.00 26.12 O HETATM 3538 O HOH A 595 54.408 30.754 0.520 1.00 34.55 O HETATM 3539 O HOH A 596 60.623 45.091 8.257 1.00 45.05 O HETATM 3540 O HOH A 597 1.863 38.362 15.827 1.00 31.49 O HETATM 3541 O HOH A 598 -2.755 39.627 -18.464 1.00 34.72 O HETATM 3542 O HOH A 599 4.075 37.799 19.742 1.00 36.11 O HETATM 3543 O HOH A 600 -15.476 40.337 2.059 1.00 34.65 O HETATM 3544 O HOH A 601 -20.415 28.628 -22.123 1.00 34.83 O HETATM 3545 O HOH A 602 36.291 49.716 21.919 1.00 33.01 O HETATM 3546 O HOH A 603 6.735 32.602 23.941 1.00 40.77 O HETATM 3547 O HOH A 604 -3.876 29.445 12.896 1.00 51.23 O HETATM 3548 O HOH A 605 1.955 30.967 -16.483 1.00 31.41 O HETATM 3549 O HOH A 606 56.789 31.401 2.742 1.00 42.02 O HETATM 3550 O HOH A 607 46.638 34.539 32.525 1.00 52.81 O HETATM 3551 O HOH A 608 -16.116 25.411 -2.925 1.00 26.80 O HETATM 3552 O HOH A 609 -12.635 40.557 1.640 1.00 41.20 O HETATM 3553 O HOH A 610 41.061 36.774 7.858 1.00 39.06 O HETATM 3554 O HOH A 611 61.342 31.350 23.233 1.00 18.37 O HETATM 3555 O HOH A 612 -0.344 36.693 16.262 1.00 30.38 O HETATM 3556 O HOH A 613 10.093 23.852 -5.819 1.00 41.10 O HETATM 3557 O HOH A 614 59.834 43.760 10.297 1.00 40.36 O HETATM 3558 O HOH A 615 41.740 23.498 24.481 1.00 31.40 O HETATM 3559 O HOH A 616 55.024 20.735 16.041 1.00 30.21 O HETATM 3560 O HOH A 617 61.403 28.984 20.107 1.00 28.10 O HETATM 3561 O HOH A 618 5.779 31.253 21.386 1.00 24.83 O HETATM 3562 O HOH A 619 -7.962 46.466 -7.177 1.00 22.70 O HETATM 3563 O HOH A 620 37.301 58.234 18.960 1.00 35.83 O HETATM 3564 O HOH A 621 -6.868 40.395 -2.659 1.00 18.25 O HETATM 3565 O HOH A 622 6.833 18.725 6.340 1.00 44.86 O HETATM 3566 O HOH A 623 31.420 31.012 28.963 1.00 38.64 O HETATM 3567 O HOH A 624 56.101 24.330 33.445 1.00 36.68 O HETATM 3568 O HOH A 625 12.189 18.803 4.100 1.00 32.89 O HETATM 3569 O HOH A 626 -9.528 44.879 -16.211 1.00 37.09 O HETATM 3570 O HOH A 627 13.310 51.500 19.923 1.00 30.93 O HETATM 3571 O HOH A 628 51.759 22.058 18.134 1.00 25.75 O HETATM 3572 O HOH A 629 -2.645 39.026 10.682 1.00 43.34 O HETATM 3573 O HOH A 630 56.913 43.811 11.137 1.00 32.25 O HETATM 3574 O HOH A 631 5.529 31.501 -6.395 1.00 26.36 O HETATM 3575 O HOH A 632 32.423 48.511 17.016 1.00 33.86 O HETATM 3576 O HOH A 633 -17.324 24.055 -16.413 1.00 27.09 O HETATM 3577 O HOH A 634 7.989 48.688 5.291 1.00 19.98 O HETATM 3578 O HOH A 635 11.180 36.179 -0.151 1.00 37.14 O HETATM 3579 O HOH A 636 -18.965 30.461 -15.552 1.00 41.00 O HETATM 3580 O HOH A 637 16.177 18.457 5.840 1.00 33.86 O HETATM 3581 O HOH A 638 1.816 17.605 -5.131 1.00 29.52 O HETATM 3582 O HOH A 639 -16.012 20.864 -7.411 1.00 43.08 O HETATM 3583 O HOH A 640 55.713 50.458 11.200 1.00 40.03 O HETATM 3584 O HOH A 641 -18.934 27.956 -18.474 1.00 38.59 O HETATM 3585 O HOH A 642 25.673 29.762 25.801 1.00 42.79 O HETATM 3586 O HOH A 643 50.909 41.518 4.261 1.00 35.52 O HETATM 3587 O HOH A 644 -0.850 14.199 -16.708 1.00 36.40 O HETATM 3588 O HOH A 645 -15.237 22.120 -3.355 1.00 41.73 O HETATM 3589 O HOH A 646 -0.629 15.931 -9.392 1.00 32.95 O HETATM 3590 O HOH A 647 26.357 22.255 19.343 1.00 43.83 O HETATM 3591 O HOH A 648 24.918 20.812 17.836 1.00 46.14 O HETATM 3592 O HOH A 649 -17.166 27.212 -12.016 1.00 37.74 O HETATM 3593 O HOH A 650 45.241 27.486 31.512 1.00 30.09 O HETATM 3594 O HOH A 651 7.982 60.067 15.254 1.00 45.42 O HETATM 3595 O HOH A 652 2.171 38.565 18.426 1.00 38.10 O HETATM 3596 O HOH A 653 57.607 50.050 12.756 1.00 39.66 O HETATM 3597 O HOH A 654 60.084 22.853 5.053 1.00 36.20 O HETATM 3598 O HOH A 655 -11.770 47.104 -4.291 1.00 38.50 O HETATM 3599 O HOH A 656 10.265 42.857 0.556 1.00 34.43 O HETATM 3600 O HOH A 657 6.598 34.393 -5.432 1.00 31.12 O HETATM 3601 O HOH A 658 -15.585 30.233 0.474 1.00 45.07 O HETATM 3602 O HOH A 659 -15.759 32.841 0.606 1.00 44.40 O HETATM 3603 O HOH A 660 41.160 25.375 26.646 1.00 41.27 O HETATM 3604 O HOH A 661 56.341 44.821 21.689 1.00 33.94 O HETATM 3605 O HOH A 662 28.921 20.292 16.603 1.00 39.22 O HETATM 3606 O HOH A 663 -9.966 18.540 -1.406 1.00 32.84 O HETATM 3607 O HOH A 664 -7.113 47.927 5.569 1.00 43.26 O HETATM 3608 O HOH A 665 52.556 19.177 24.719 1.00 34.24 O HETATM 3609 O HOH A 666 -6.128 17.944 -4.259 1.00 30.18 O HETATM 3610 O HOH A 667 56.640 45.992 9.764 1.00 38.28 O HETATM 3611 O HOH A 668 36.730 47.107 15.617 1.00 43.42 O HETATM 3612 O HOH A 669 -13.534 32.919 -8.242 1.00 29.12 O HETATM 3613 O HOH A 670 62.756 28.540 7.141 1.00 39.31 O HETATM 3614 O HOH A 671 3.035 28.769 -22.385 1.00 37.21 O HETATM 3615 O HOH A 672 1.188 18.757 1.787 1.00 36.35 O HETATM 3616 O HOH A 673 17.321 20.312 14.330 1.00 48.06 O HETATM 3617 O HOH A 674 48.337 35.143 7.389 1.00 26.00 O HETATM 3618 O HOH A 675 58.701 29.375 3.918 1.00 36.48 O HETATM 3619 O HOH A 676 -2.740 17.378 -8.540 1.00 30.78 O HETATM 3620 O HOH A 677 49.783 32.940 34.164 1.00 45.52 O HETATM 3621 O HOH A 678 5.881 45.245 5.275 1.00 26.66 O HETATM 3622 O HOH A 679 3.618 18.644 12.749 1.00 49.45 O HETATM 3623 O HOH A 680 -2.292 14.388 -12.568 1.00 44.27 O HETATM 3624 O HOH A 681 40.156 18.924 16.485 1.00 40.49 O HETATM 3625 O HOH A 682 11.483 25.469 25.206 1.00 34.71 O HETATM 3626 O HOH A 683 26.645 40.642 8.430 1.00 46.10 O HETATM 3627 O HOH A 684 8.309 30.974 -5.903 1.00 38.77 O HETATM 3628 O HOH A 685 57.034 30.139 23.795 1.00 30.39 O HETATM 3629 O HOH A 686 6.865 46.852 7.156 1.00 30.20 O HETATM 3630 O HOH A 687 3.836 18.727 9.546 1.00 42.82 O HETATM 3631 O HOH A 688 8.677 17.271 -9.102 1.00 48.38 O HETATM 3632 O HOH A 689 -8.101 29.096 -32.427 1.00 41.32 O HETATM 3633 O HOH A 690 39.032 20.038 19.978 1.00 40.70 O HETATM 3634 O HOH A 691 48.102 23.683 30.953 1.00 35.99 O HETATM 3635 O HOH A 692 -12.306 17.526 -16.041 1.00 43.24 O HETATM 3636 O HOH A 693 35.235 19.847 15.941 1.00 26.59 O HETATM 3637 O HOH A 694 6.780 50.152 23.240 1.00 31.98 O HETATM 3638 O HOH A 695 -1.794 43.371 -13.536 1.00 38.97 O HETATM 3639 O HOH A 696 -14.618 14.473 -21.144 1.00 45.54 O HETATM 3640 O HOH A 697 34.047 48.754 23.812 1.00 42.16 O HETATM 3641 O HOH A 698 26.569 47.985 8.465 1.00 53.97 O HETATM 3642 O HOH A 699 33.033 38.441 29.045 1.00 29.19 O HETATM 3643 O HOH A 700 35.759 31.594 8.124 1.00 31.63 O HETATM 3644 O HOH A 701 5.787 28.606 21.412 1.00 51.20 O HETATM 3645 O HOH A 702 26.804 19.835 7.832 1.00 32.53 O HETATM 3646 O HOH A 703 36.812 18.196 9.075 1.00 46.86 O HETATM 3647 O HOH A 704 42.299 21.613 8.336 1.00 20.95 O HETATM 3648 O HOH B 11 6.366 22.041 -12.241 1.00 29.00 O HETATM 3649 O HOH B 30 22.300 25.655 6.103 1.00 27.97 O HETATM 3650 O HOH B 39 35.910 29.142 5.032 1.00 33.89 O HETATM 3651 O HOH B 42 36.639 24.679 3.305 1.00 24.63 O HETATM 3652 O HOH B 50 48.296 21.938 2.440 1.00 23.92 O HETATM 3653 O HOH B 56 49.034 21.847 5.126 1.00 26.44 O HETATM 3654 O HOH B 68 27.338 22.671 7.921 1.00 29.72 O HETATM 3655 O HOH B 79 35.597 26.266 5.513 1.00 20.42 O HETATM 3656 O HOH B 90 36.822 24.623 10.261 1.00 23.05 O HETATM 3657 O HOH B 104 26.316 25.848 0.346 1.00 40.11 O HETATM 3658 O HOH B 110 40.287 27.733 3.108 1.00 25.38 O HETATM 3659 O HOH B 122 16.285 27.664 2.262 1.00 33.89 O HETATM 3660 O HOH B 170 39.969 31.865 7.389 1.00 23.46 O HETATM 3661 O HOH B 183 28.866 30.743 3.137 1.00 36.75 O HETATM 3662 O HOH B 199 8.848 27.127 -1.729 1.00 38.90 O HETATM 3663 O HOH B 206 38.958 24.917 1.992 1.00 36.49 O HETATM 3664 O HOH B 236 44.843 21.738 -1.264 1.00 28.23 O HETATM 3665 O HOH B 252 21.556 25.629 -4.875 1.00 32.69 O HETATM 3666 O HOH B 297 21.736 31.043 8.408 1.00 37.99 O CONECT 1873 2146 CONECT 2146 1873 CONECT 3373 3374 3375 CONECT 3374 3373 CONECT 3375 3373 3376 CONECT 3376 3375 MASTER 260 0 1 29 2 0 2 6 3661 2 6 33 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3qgc
RCSB PDB
PDBbind
RNA (5-UGUGCCUUA-3)
Entry Information
PDB ID
3qg9
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
RNA-binding domain of FBF-2 (amino acids 164-575)
Ligand Name
RNA (5-UGUGCCUUA-3)
EC.Number
E.C.-.-.-.-
Resolution
2.25(Å)
Affinity (Kd/Ki/IC50)
Kd=18nM
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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