HEADER PROTEIN TRANSPORT,STRUCTURAL PROTEIN 14-OCT-08 3EWE TITLE CRYSTAL STRUCTURE OF THE NUP85/SEH1 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOPORIN SEH1; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: NUCLEAR PORE PROTEIN SEH1, SEC13 HOMOLOG 1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NUCLEOPORIN NUP85; COMPND 8 CHAIN: B, D; COMPND 9 FRAGMENT: UNP RESIDUES 1-564; COMPND 10 SYNONYM: NUCLEAR PORE PROTEIN NUP85; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST,YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: SEH1, YGL100W; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCOLA-DUET; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST,YEAST; SOURCE 14 ORGANISM_TAXID: 4932; SOURCE 15 GENE: J1624, NUP85, RAT9, YJR042W; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCOLA-DUET KEYWDS NUCLEOPORIN, NUCLEAR PORE COMPLEX, MRNA TRANSPORT, NUCLEUS, KEYWDS 2 PROTEIN TRANSPORT, TRANSLOCATION, CELL MEMBRANE, MEMBRANE, KEYWDS 3 PHOSPHOPROTEIN, TRANSPORT, WD REPEAT, MEMBRANE PROTEIN, KEYWDS 4 PROTEIN TRANSPORT,STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.G.BROHAWN,N.C.LEKSA,K.R.RAJASHANKAR,T.U.SCHWARTZ REVDAT 5 09-JUN-09 3EWE 1 REVDAT REVDAT 4 24-FEB-09 3EWE 1 VERSN REVDAT 3 09-DEC-08 3EWE 1 JRNL REVDAT 2 25-NOV-08 3EWE 1 TITLE REVDAT 1 11-NOV-08 3EWE 0 JRNL AUTH S.G.BROHAWN,N.C.LEKSA,E.D.SPEAR,K.R.RAJASHANKAR, JRNL AUTH 2 T.U.SCHWARTZ JRNL TITL STRUCTURAL EVIDENCE FOR COMMON ANCESTRY OF THE JRNL TITL 2 NUCLEAR PORE COMPLEX AND VESICLE COATS. JRNL REF SCIENCE V. 322 1369 2008 JRNL REFN ISSN 0036-8075 JRNL PMID 18974315 JRNL DOI 10.1126/SCIENCE.1165886 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4 REMARK 3 NUMBER OF REFLECTIONS : 28300 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.328 REMARK 3 R VALUE (WORKING SET) : 0.326 REMARK 3 FREE R VALUE : 0.369 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 1405 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 29.7560 - 7.5042 0.90 2715 138 0.2961 0.3380 REMARK 3 2 7.5042 - 5.9721 0.96 2721 180 0.3260 0.3847 REMARK 3 3 5.9721 - 5.2218 0.96 2699 149 0.3236 0.3272 REMARK 3 4 5.2218 - 4.7464 0.96 2656 143 0.2979 0.3391 REMARK 3 5 4.7464 - 4.4074 0.97 2707 118 0.2953 0.3496 REMARK 3 6 4.4074 - 4.1483 0.97 2655 131 0.3143 0.3702 REMARK 3 7 4.1483 - 3.9410 0.98 2711 119 0.3133 0.3746 REMARK 3 8 3.9410 - 3.7698 0.98 2692 131 0.3356 0.3409 REMARK 3 9 3.7698 - 3.6249 0.98 2636 161 0.3323 0.4330 REMARK 3 10 3.6249 - 3.5000 0.99 2703 135 0.3965 0.4609 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.26 REMARK 3 B_SOL : 102.79 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.590 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.690 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 118.00 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 : 0.008 9889 REMARK 3 ANGLE : 1.200 13498 REMARK 3 CHIRALITY : 0.079 1623 REMARK 3 PLANARITY : 0.005 1664 REMARK 3 DIHEDRAL : 17.296 3172 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A OR (CHAIN B AND RESSEQ 1:95) REMARK 3 ORIGIN FOR THE GROUP (A): -43.0737 60.8201 62.3163 REMARK 3 T TENSOR REMARK 3 T11: 1.3263 T22: 2.0759 REMARK 3 T33: 1.5490 T12: 0.1302 REMARK 3 T13: 0.0737 T23: 0.1428 REMARK 3 L TENSOR REMARK 3 L11: 3.6136 L22: 3.1552 REMARK 3 L33: 3.6653 L12: -0.5829 REMARK 3 L13: 0.1282 L23: -1.1318 REMARK 3 S TENSOR REMARK 3 S11: 0.0826 S12: -0.5344 S13: -0.1600 REMARK 3 S21: 0.5757 S22: 0.5283 S23: 0.9671 REMARK 3 S31: 0.0152 S32: -0.9733 S33: -0.0004 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B AND NOT (RESSEQ 1:95) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8869 69.6900 58.8780 REMARK 3 T TENSOR REMARK 3 T11: 1.2592 T22: 1.8603 REMARK 3 T33: 0.9677 T12: -0.0203 REMARK 3 T13: -0.3073 T23: -0.0492 REMARK 3 L TENSOR REMARK 3 L11: 8.0699 L22: 2.1423 REMARK 3 L33: 1.9958 L12: -2.7281 REMARK 3 L13: -3.4013 L23: 0.1131 REMARK 3 S TENSOR REMARK 3 S11: -0.0823 S12: -0.4752 S13: -0.5083 REMARK 3 S21: 0.4230 S22: -0.2087 S23: 0.1177 REMARK 3 S31: -0.2740 S32: 0.6531 S33: 0.0009 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN C OR (CHAIN D AND RESSEQ 1:95) REMARK 3 ORIGIN FOR THE GROUP (A): 34.9924 62.9921 17.1784 REMARK 3 T TENSOR REMARK 3 T11: 1.4251 T22: 2.9936 REMARK 3 T33: 1.6856 T12: 0.2224 REMARK 3 T13: 0.1671 T23: 0.2188 REMARK 3 L TENSOR REMARK 3 L11: 5.1405 L22: 0.7777 REMARK 3 L33: 6.0106 L12: -0.2398 REMARK 3 L13: -0.1246 L23: 0.3634 REMARK 3 S TENSOR REMARK 3 S11: -0.1274 S12: 0.9238 S13: -0.4226 REMARK 3 S21: -0.6495 S22: 0.2766 S23: -0.5365 REMARK 3 S31: 0.3153 S32: 2.0529 S33: -0.0005 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN D AND NOT (RESSEQ 1:95) REMARK 3 ORIGIN FOR THE GROUP (A): -6.1574 71.7318 21.5158 REMARK 3 T TENSOR REMARK 3 T11: 1.1152 T22: 1.6004 REMARK 3 T33: 1.1455 T12: 0.1859 REMARK 3 T13: -0.2431 T23: 0.2117 REMARK 3 L TENSOR REMARK 3 L11: 6.3868 L22: 0.8945 REMARK 3 L33: 2.0895 L12: 2.6904 REMARK 3 L13: -2.7368 L23: -0.5629 REMARK 3 S TENSOR REMARK 3 S11: -0.2205 S12: 0.1342 S13: -0.2473 REMARK 3 S21: -0.2992 S22: 0.0752 S23: -0.2533 REMARK 3 S31: -0.4216 S32: -0.0878 S33: 0.0017 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN A OR (CHAIN B AND RESSEQ 1:99) REMARK 3 SELECTION : CHAIN C OR (CHAIN D AND RESSEQ 1:99) REMARK 3 ATOM PAIRS NUMBER : 2114 REMARK 3 RMSD : 0.090 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN B AND RESSEQ 216:370) REMARK 3 SELECTION : CHAIN D AND RESSEQ 216:370) REMARK 3 ATOM PAIRS NUMBER : 876 REMARK 3 RMSD : 0.109 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN B AND NOT (RESSEQ 1:99 OR RESSEQ REMARK 3 216:370 OR RESSEQ 531:556) REMARK 3 SELECTION : CHAIN D AND NOT (RESSEQ 1:99 OR RESSEQ REMARK 3 216:370 OR RESSEQ 531:556) REMARK 3 ATOM PAIRS NUMBER : 1663 REMARK 3 RMSD : 0.101 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3EWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-08. REMARK 100 THE RCSB ID CODE IS RCSB049850. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-APR-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29579 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.10700 REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELX C/D/E REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.1M BIS TRIS REMARK 280 PROPANE, 0.2M SODIUM CITRATE, PH 8.5, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 175.27450 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 56.27950 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 56.27950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.63725 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 56.27950 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 56.27950 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 262.91175 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 56.27950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.27950 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.63725 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 56.27950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.27950 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 262.91175 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 175.27450 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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 300 REMARK: HETEROTETRAMER IS NOT OBSERVED IN SOLUTION BY AUTHOR. REMARK 300 SEE CITATION FOR DETAILS. 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: 3250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 3160 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 60820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLN A 2 REMARK 465 PRO A 3 REMARK 465 PHE A 4 REMARK 465 ASP A 5 REMARK 465 SER A 6 REMARK 465 GLY A 7 REMARK 465 HIS A 8 REMARK 465 ASP A 9 REMARK 465 ASP A 10 REMARK 465 LEU A 11 REMARK 465 ASP A 87 REMARK 465 PRO A 88 REMARK 465 ASP A 89 REMARK 465 GLN A 90 REMARK 465 GLU A 91 REMARK 465 GLU A 92 REMARK 465 CYS A 93 REMARK 465 SER A 94 REMARK 465 GLY A 95 REMARK 465 ARG A 96 REMARK 465 ARG A 97 REMARK 465 LEU A 157 REMARK 465 SER A 158 REMARK 465 ILE A 159 REMARK 465 PRO A 160 REMARK 465 PRO A 161 REMARK 465 ALA A 162 REMARK 465 ASN A 163 REMARK 465 HIS A 164 REMARK 465 LEU A 165 REMARK 465 GLN A 166 REMARK 465 ARG A 177 REMARK 465 PHE A 178 REMARK 465 SER A 179 REMARK 465 GLY A 197 REMARK 465 LYS A 198 REMARK 465 ASP A 199 REMARK 465 GLY A 200 REMARK 465 LYS A 201 REMARK 465 ILE A 224 REMARK 465 GLY A 225 REMARK 465 ARG A 226 REMARK 465 TRP A 227 REMARK 465 LYS A 248 REMARK 465 LEU A 249 REMARK 465 SER A 250 REMARK 465 PRO A 251 REMARK 465 LEU A 252 REMARK 465 ALA A 253 REMARK 465 SER A 254 REMARK 465 GLU A 255 REMARK 465 GLU A 256 REMARK 465 SER A 257 REMARK 465 LEU A 258 REMARK 465 THR A 259 REMARK 465 ASN A 260 REMARK 465 SER A 261 REMARK 465 ASN A 262 REMARK 465 MET A 263 REMARK 465 PHE A 264 REMARK 465 ASP A 265 REMARK 465 ASN A 266 REMARK 465 SER A 267 REMARK 465 ALA A 268 REMARK 465 ASP A 269 REMARK 465 VAL A 270 REMARK 465 ASP A 271 REMARK 465 MET A 272 REMARK 465 ASP A 273 REMARK 465 ALA A 274 REMARK 465 GLN A 275 REMARK 465 GLY A 276 REMARK 465 ARG A 277 REMARK 465 SER A 278 REMARK 465 ASP A 279 REMARK 465 SER A 280 REMARK 465 ASN A 281 REMARK 465 THR A 282 REMARK 465 GLU A 283 REMARK 465 GLU A 284 REMARK 465 LYS A 285 REMARK 465 ALA A 286 REMARK 465 GLU A 287 REMARK 465 LEU A 288 REMARK 465 GLN A 289 REMARK 465 SER A 290 REMARK 465 GLU A 299 REMARK 465 HIS A 300 REMARK 465 ASP A 301 REMARK 465 ASP A 302 REMARK 465 HIS A 303 REMARK 465 ASN A 304 REMARK 465 GLN A 349 REMARK 465 MET B 1 REMARK 465 THR B 2 REMARK 465 ILE B 3 REMARK 465 ASP B 4 REMARK 465 ASP B 5 REMARK 465 SER B 6 REMARK 465 ASN B 7 REMARK 465 ARG B 8 REMARK 465 LEU B 9 REMARK 465 LEU B 10 REMARK 465 MET B 11 REMARK 465 ASP B 12 REMARK 465 VAL B 13 REMARK 465 ASP B 14 REMARK 465 GLN B 15 REMARK 465 PHE B 16 REMARK 465 ASP B 17 REMARK 465 PHE B 18 REMARK 465 LEU B 19 REMARK 465 ASP B 20 REMARK 465 ASP B 21 REMARK 465 GLY B 22 REMARK 465 THR B 23 REMARK 465 ALA B 24 REMARK 465 GLN B 25 REMARK 465 LEU B 26 REMARK 465 SER B 27 REMARK 465 ASN B 28 REMARK 465 ASN B 29 REMARK 465 LYS B 30 REMARK 465 THR B 31 REMARK 465 ASP B 32 REMARK 465 GLU B 33 REMARK 465 GLU B 34 REMARK 465 GLU B 35 REMARK 465 GLN B 36 REMARK 465 LEU B 37 REMARK 465 TYR B 38 REMARK 465 LYS B 39 REMARK 465 ARG B 40 REMARK 465 ASP B 41 REMARK 465 PRO B 42 REMARK 465 VAL B 43 REMARK 465 SER B 44 REMARK 465 GLY B 45 REMARK 465 ALA B 46 REMARK 465 ILE B 47 REMARK 465 LEU B 48 REMARK 465 VAL B 49 REMARK 465 PRO B 50 REMARK 465 MET B 51 REMARK 465 THR B 52 REMARK 465 VAL B 53 REMARK 465 ASN B 54 REMARK 465 ASP B 55 REMARK 465 GLN B 56 REMARK 465 PRO B 57 REMARK 465 ILE B 58 REMARK 465 GLU B 59 REMARK 465 LYS B 60 REMARK 465 ASN B 61 REMARK 465 GLY B 62 REMARK 465 ASP B 63 REMARK 465 LYS B 64 REMARK 465 ALA B 84 REMARK 465 LYS B 85 REMARK 465 ASP B 86 REMARK 465 ASP B 121 REMARK 465 ARG B 122 REMARK 465 VAL B 123 REMARK 465 PHE B 124 REMARK 465 ASN B 125 REMARK 465 VAL B 126 REMARK 465 PRO B 127 REMARK 465 THR B 128 REMARK 465 ILE B 129 REMARK 465 GLY B 130 REMARK 465 VAL B 131 REMARK 465 VAL B 132 REMARK 465 ASN B 133 REMARK 465 SER B 134 REMARK 465 ASN B 135 REMARK 465 PHE B 136 REMARK 465 ALA B 137 REMARK 465 GLN B 165 REMARK 465 ASP B 166 REMARK 465 GLY B 167 REMARK 465 ARG B 168 REMARK 465 ASP B 193 REMARK 465 GLY B 194 REMARK 465 GLN B 195 REMARK 465 ASP B 196 REMARK 465 VAL B 197 REMARK 465 GLU B 198 REMARK 465 GLU B 199 REMARK 465 PHE B 228 REMARK 465 SER B 229 REMARK 465 VAL B 230 REMARK 465 LYS B 231 REMARK 465 ASP B 232 REMARK 465 SER B 233 REMARK 465 THR B 234 REMARK 465 ALA B 235 REMARK 465 GLY B 236 REMARK 465 LYS B 237 REMARK 465 LYS B 238 REMARK 465 VAL B 239 REMARK 465 PHE B 240 REMARK 465 PRO B 272 REMARK 465 TYR B 273 REMARK 465 LEU B 274 REMARK 465 SER B 275 REMARK 465 ASP B 276 REMARK 465 THR B 277 REMARK 465 LYS B 293 REMARK 465 GLN B 294 REMARK 465 TYR B 295 REMARK 465 PRO B 296 REMARK 465 LYS B 297 REMARK 465 ASP B 298 REMARK 465 SER B 299 REMARK 465 SER B 300 REMARK 465 SER B 301 REMARK 465 GLY B 318 REMARK 465 SER B 319 REMARK 465 SER B 320 REMARK 465 ALA B 321 REMARK 465 THR B 322 REMARK 465 ASP B 323 REMARK 465 ILE B 324 REMARK 465 LEU B 429 REMARK 465 ILE B 430 REMARK 465 GLU B 431 REMARK 465 ASN B 432 REMARK 465 ILE B 433 REMARK 465 PHE B 434 REMARK 465 GLU B 435 REMARK 465 GLY B 436 REMARK 465 GLU B 437 REMARK 465 LYS B 438 REMARK 465 ASN B 439 REMARK 465 SER B 440 REMARK 465 ASP B 441 REMARK 465 ASP B 442 REMARK 465 TYR B 443 REMARK 465 SER B 444 REMARK 465 ASN B 445 REMARK 465 GLU B 446 REMARK 465 ASP B 447 REMARK 465 ASN B 448 REMARK 465 GLU B 449 REMARK 465 MET B 450 REMARK 465 LEU B 451 REMARK 465 GLU B 452 REMARK 465 ASP B 453 REMARK 465 LEU B 491 REMARK 465 SER B 492 REMARK 465 ALA B 493 REMARK 465 THR B 494 REMARK 465 GLY B 495 REMARK 465 ILE B 556 REMARK 465 ALA B 557 REMARK 465 ASN B 558 REMARK 465 PHE B 559 REMARK 465 SER B 560 REMARK 465 ARG B 561 REMARK 465 ALA B 562 REMARK 465 GLY B 563 REMARK 465 LYS B 564 REMARK 465 MET C 1 REMARK 465 GLN C 2 REMARK 465 PRO C 3 REMARK 465 PHE C 4 REMARK 465 ASP C 5 REMARK 465 SER C 6 REMARK 465 GLY C 7 REMARK 465 HIS C 8 REMARK 465 ASP C 9 REMARK 465 ASP C 10 REMARK 465 LEU C 11 REMARK 465 ASP C 87 REMARK 465 PRO C 88 REMARK 465 ASP C 89 REMARK 465 GLN C 90 REMARK 465 GLU C 91 REMARK 465 GLU C 92 REMARK 465 CYS C 93 REMARK 465 SER C 94 REMARK 465 GLY C 95 REMARK 465 ARG C 96 REMARK 465 ARG C 97 REMARK 465 LEU C 157 REMARK 465 SER C 158 REMARK 465 ILE C 159 REMARK 465 PRO C 160 REMARK 465 PRO C 161 REMARK 465 ALA C 162 REMARK 465 ASN C 163 REMARK 465 HIS C 164 REMARK 465 LEU C 165 REMARK 465 GLN C 166 REMARK 465 ARG C 177 REMARK 465 PHE C 178 REMARK 465 SER C 179 REMARK 465 GLY C 197 REMARK 465 LYS C 198 REMARK 465 ASP C 199 REMARK 465 GLY C 200 REMARK 465 LYS C 201 REMARK 465 ILE C 224 REMARK 465 GLY C 225 REMARK 465 ARG C 226 REMARK 465 TRP C 227 REMARK 465 LYS C 248 REMARK 465 LEU C 249 REMARK 465 SER C 250 REMARK 465 PRO C 251 REMARK 465 LEU C 252 REMARK 465 ALA C 253 REMARK 465 SER C 254 REMARK 465 GLU C 255 REMARK 465 GLU C 256 REMARK 465 SER C 257 REMARK 465 LEU C 258 REMARK 465 THR C 259 REMARK 465 ASN C 260 REMARK 465 SER C 261 REMARK 465 ASN C 262 REMARK 465 MET C 263 REMARK 465 PHE C 264 REMARK 465 ASP C 265 REMARK 465 ASN C 266 REMARK 465 SER C 267 REMARK 465 ALA C 268 REMARK 465 ASP C 269 REMARK 465 VAL C 270 REMARK 465 ASP C 271 REMARK 465 MET C 272 REMARK 465 ASP C 273 REMARK 465 ALA C 274 REMARK 465 GLN C 275 REMARK 465 GLY C 276 REMARK 465 ARG C 277 REMARK 465 SER C 278 REMARK 465 ASP C 279 REMARK 465 SER C 280 REMARK 465 ASN C 281 REMARK 465 THR C 282 REMARK 465 GLU C 283 REMARK 465 GLU C 284 REMARK 465 LYS C 285 REMARK 465 ALA C 286 REMARK 465 GLU C 287 REMARK 465 LEU C 288 REMARK 465 GLN C 289 REMARK 465 SER C 290 REMARK 465 GLU C 299 REMARK 465 HIS C 300 REMARK 465 ASP C 301 REMARK 465 ASP C 302 REMARK 465 HIS C 303 REMARK 465 ASN C 304 REMARK 465 GLN C 349 REMARK 465 MET D 1 REMARK 465 THR D 2 REMARK 465 ILE D 3 REMARK 465 ASP D 4 REMARK 465 ASP D 5 REMARK 465 SER D 6 REMARK 465 ASN D 7 REMARK 465 ARG D 8 REMARK 465 LEU D 9 REMARK 465 LEU D 10 REMARK 465 MET D 11 REMARK 465 ASP D 12 REMARK 465 VAL D 13 REMARK 465 ASP D 14 REMARK 465 GLN D 15 REMARK 465 PHE D 16 REMARK 465 ASP D 17 REMARK 465 PHE D 18 REMARK 465 LEU D 19 REMARK 465 ASP D 20 REMARK 465 ASP D 21 REMARK 465 GLY D 22 REMARK 465 THR D 23 REMARK 465 ALA D 24 REMARK 465 GLN D 25 REMARK 465 LEU D 26 REMARK 465 SER D 27 REMARK 465 ASN D 28 REMARK 465 ASN D 29 REMARK 465 LYS D 30 REMARK 465 THR D 31 REMARK 465 ASP D 32 REMARK 465 GLU D 33 REMARK 465 GLU D 34 REMARK 465 GLU D 35 REMARK 465 GLN D 36 REMARK 465 LEU D 37 REMARK 465 TYR D 38 REMARK 465 LYS D 39 REMARK 465 ARG D 40 REMARK 465 ASP D 41 REMARK 465 PRO D 42 REMARK 465 VAL D 43 REMARK 465 SER D 44 REMARK 465 GLY D 45 REMARK 465 ALA D 46 REMARK 465 ILE D 47 REMARK 465 LEU D 48 REMARK 465 VAL D 49 REMARK 465 PRO D 50 REMARK 465 MET D 51 REMARK 465 THR D 52 REMARK 465 VAL D 53 REMARK 465 ASN D 54 REMARK 465 ASP D 55 REMARK 465 GLN D 56 REMARK 465 PRO D 57 REMARK 465 ILE D 58 REMARK 465 GLU D 59 REMARK 465 LYS D 60 REMARK 465 ASN D 61 REMARK 465 GLY D 62 REMARK 465 ASP D 63 REMARK 465 LYS D 64 REMARK 465 ALA D 84 REMARK 465 LYS D 85 REMARK 465 ASP D 86 REMARK 465 ASP D 121 REMARK 465 ARG D 122 REMARK 465 VAL D 123 REMARK 465 PHE D 124 REMARK 465 ASN D 125 REMARK 465 VAL D 126 REMARK 465 PRO D 127 REMARK 465 THR D 128 REMARK 465 ILE D 129 REMARK 465 GLY D 130 REMARK 465 VAL D 131 REMARK 465 VAL D 132 REMARK 465 ASN D 133 REMARK 465 SER D 134 REMARK 465 ASN D 135 REMARK 465 PHE D 136 REMARK 465 ALA D 137 REMARK 465 GLN D 165 REMARK 465 ASP D 166 REMARK 465 GLY D 167 REMARK 465 ARG D 168 REMARK 465 ASP D 193 REMARK 465 GLY D 194 REMARK 465 GLN D 195 REMARK 465 ASP D 196 REMARK 465 VAL D 197 REMARK 465 GLU D 198 REMARK 465 GLU D 199 REMARK 465 PHE D 228 REMARK 465 SER D 229 REMARK 465 VAL D 230 REMARK 465 LYS D 231 REMARK 465 ASP D 232 REMARK 465 SER D 233 REMARK 465 THR D 234 REMARK 465 ALA D 235 REMARK 465 GLY D 236 REMARK 465 LYS D 237 REMARK 465 LYS D 238 REMARK 465 VAL D 239 REMARK 465 PHE D 240 REMARK 465 PRO D 272 REMARK 465 TYR D 273 REMARK 465 LEU D 274 REMARK 465 SER D 275 REMARK 465 ASP D 276 REMARK 465 THR D 277 REMARK 465 LYS D 293 REMARK 465 GLN D 294 REMARK 465 TYR D 295 REMARK 465 PRO D 296 REMARK 465 LYS D 297 REMARK 465 ASP D 298 REMARK 465 SER D 299 REMARK 465 SER D 300 REMARK 465 SER D 301 REMARK 465 GLY D 318 REMARK 465 SER D 319 REMARK 465 SER D 320 REMARK 465 ALA D 321 REMARK 465 THR D 322 REMARK 465 ASP D 323 REMARK 465 ILE D 324 REMARK 465 LEU D 429 REMARK 465 ILE D 430 REMARK 465 GLU D 431 REMARK 465 ASN D 432 REMARK 465 ILE D 433 REMARK 465 PHE D 434 REMARK 465 GLU D 435 REMARK 465 GLY D 436 REMARK 465 GLU D 437 REMARK 465 LYS D 438 REMARK 465 ASN D 439 REMARK 465 SER D 440 REMARK 465 ASP D 441 REMARK 465 ASP D 442 REMARK 465 TYR D 443 REMARK 465 SER D 444 REMARK 465 ASN D 445 REMARK 465 GLU D 446 REMARK 465 ASP D 447 REMARK 465 ASN D 448 REMARK 465 GLU D 449 REMARK 465 MET D 450 REMARK 465 LEU D 451 REMARK 465 GLU D 452 REMARK 465 ASP D 453 REMARK 465 LEU D 491 REMARK 465 SER D 492 REMARK 465 ALA D 493 REMARK 465 THR D 494 REMARK 465 GLY D 495 REMARK 465 ILE D 556 REMARK 465 ALA D 557 REMARK 465 ASN D 558 REMARK 465 PHE D 559 REMARK 465 SER D 560 REMARK 465 ARG D 561 REMARK 465 ALA D 562 REMARK 465 GLY D 563 REMARK 465 LYS D 564 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 34 CG CD CE NZ REMARK 470 ASP A 39 CG OD1 OD2 REMARK 470 LYS A 40 CG CD CE NZ REMARK 470 ASN A 44 CG OD1 ND2 REMARK 470 GLU A 46 CG CD OE1 OE2 REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 70 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 79 CG CD CE NZ REMARK 470 LYS A 82 CG CD CE NZ REMARK 470 LYS A 100 CG CD CE NZ REMARK 470 LYS A 108 CG CD CE NZ REMARK 470 LYS A 124 CG CD CE NZ REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 141 CG CD OE1 OE2 REMARK 470 ASP A 144 CG OD1 OD2 REMARK 470 ARG A 146 CG CD NE CZ NH1 NH2 REMARK 470 TRP A 148 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 148 CZ3 CH2 REMARK 470 GLU A 153 CG CD OE1 OE2 REMARK 470 LYS A 155 CG CD CE NZ REMARK 470 ASP A 168 CG OD1 OD2 REMARK 470 GLU A 181 CG CD OE1 OE2 REMARK 470 LYS A 182 CG CD CE NZ REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 202 CG CD1 CD2 REMARK 470 HIS A 203 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 207 CG CD CE NZ REMARK 470 LYS A 212 CG CD CE NZ REMARK 470 LYS A 236 CG CD CE NZ REMARK 470 ARG A 241 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 247 CG CD OE1 OE2 REMARK 470 ASP A 324 CG OD1 OD2 REMARK 470 LYS A 327 CG CD CE NZ REMARK 470 LYS A 332 CG CD CE NZ REMARK 470 GLN A 348 CG CD OE1 NE2 REMARK 470 LYS B 70 CG CD CE NZ REMARK 470 LYS B 87 CG CD CE NZ REMARK 470 TYR B 88 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 89 CG CD CE NZ REMARK 470 ARG B 94 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 102 CG CD CE NZ REMARK 470 GLU B 113 CG CD OE1 OE2 REMARK 470 ARG B 116 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 120 CG OD1 OD2 REMARK 470 LYS B 138 CG CD CE NZ REMARK 470 GLU B 139 CG CD OE1 OE2 REMARK 470 LYS B 163 CG CD CE NZ REMARK 470 ASP B 164 CG OD1 OD2 REMARK 470 ASN B 200 CG OD1 ND2 REMARK 470 ARG B 201 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 216 CG OD1 OD2 REMARK 470 GLU B 218 CG CD OE1 OE2 REMARK 470 GLU B 221 CG CD OE1 OE2 REMARK 470 GLU B 222 CG CD OE1 OE2 REMARK 470 GLU B 225 CG CD OE1 OE2 REMARK 470 GLN B 226 CG CD OE1 NE2 REMARK 470 GLU B 241 CG CD OE1 OE2 REMARK 470 GLN B 243 CG CD OE1 NE2 REMARK 470 LYS B 247 CG CD CE NZ REMARK 470 GLN B 251 CG CD OE1 NE2 REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 260 CG CD OE1 NE2 REMARK 470 GLU B 266 CG CD OE1 OE2 REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 304 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 305 CG CD OE1 OE2 REMARK 470 LYS B 307 CG CD CE NZ REMARK 470 LYS B 312 CG CD CE NZ REMARK 470 GLU B 327 CG CD OE1 OE2 REMARK 470 ARG B 329 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 333 CG CD OE1 OE2 REMARK 470 ARG B 344 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 345 CG CD CE NZ REMARK 470 GLN B 348 CG CD OE1 NE2 REMARK 470 ARG B 351 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 355 CG CD OE1 OE2 REMARK 470 GLU B 373 CG CD OE1 OE2 REMARK 470 LYS B 401 CG CD CE NZ REMARK 470 LEU B 454 CG CD1 CD2 REMARK 470 ARG B 458 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 479 CG CD CE NZ REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 500 CG CD CE NZ REMARK 470 LYS B 501 CG CD CE NZ REMARK 470 ARG B 530 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 536 CG CD CE NZ REMARK 470 LYS C 34 CG CD CE NZ REMARK 470 ASP C 39 CG OD1 OD2 REMARK 470 LYS C 40 CG CD CE NZ REMARK 470 ASN C 44 CG OD1 ND2 REMARK 470 GLU C 46 CG CD OE1 OE2 REMARK 470 ARG C 52 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 70 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 79 CG CD CE NZ REMARK 470 LYS C 82 CG CD CE NZ REMARK 470 LYS C 100 CG CD CE NZ REMARK 470 LYS C 108 CG CD CE NZ REMARK 470 LYS C 124 CG CD CE NZ REMARK 470 ARG C 135 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 141 CG CD OE1 OE2 REMARK 470 ASP C 144 CG OD1 OD2 REMARK 470 ARG C 146 CG CD NE CZ NH1 NH2 REMARK 470 TRP C 148 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 148 CZ3 CH2 REMARK 470 GLU C 153 CG CD OE1 OE2 REMARK 470 LYS C 155 CG CD CE NZ REMARK 470 ASP C 168 CG OD1 OD2 REMARK 470 GLU C 181 CG CD OE1 OE2 REMARK 470 LYS C 182 CG CD CE NZ REMARK 470 ARG C 196 CG CD NE CZ NH1 NH2 REMARK 470 HIS C 203 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 207 CG CD CE NZ REMARK 470 LYS C 212 CG CD CE NZ REMARK 470 LYS C 236 CG CD CE NZ REMARK 470 ARG C 241 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 247 CG CD OE1 OE2 REMARK 470 ASP C 324 CG OD1 OD2 REMARK 470 LYS C 327 CG CD CE NZ REMARK 470 LYS C 332 CG CD CE NZ REMARK 470 GLN C 348 CG CD OE1 NE2 REMARK 470 LYS D 70 CG CD CE NZ REMARK 470 LYS D 87 CG CD CE NZ REMARK 470 TYR D 88 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS D 89 CG CD CE NZ REMARK 470 ARG D 94 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 102 CG CD CE NZ REMARK 470 GLU D 113 CG CD OE1 OE2 REMARK 470 ARG D 116 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 120 CG OD1 OD2 REMARK 470 LYS D 138 CG CD CE NZ REMARK 470 GLU D 139 CG CD OE1 OE2 REMARK 470 LYS D 163 CG CD CE NZ REMARK 470 ASP D 164 CG OD1 OD2 REMARK 470 ASN D 200 CG OD1 ND2 REMARK 470 ARG D 201 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 216 CG OD1 OD2 REMARK 470 GLU D 218 CG CD OE1 OE2 REMARK 470 GLU D 221 CG CD OE1 OE2 REMARK 470 GLU D 222 CG CD OE1 OE2 REMARK 470 GLU D 225 CG CD OE1 OE2 REMARK 470 GLN D 226 CG CD OE1 NE2 REMARK 470 GLU D 241 CG CD OE1 OE2 REMARK 470 GLN D 243 CG CD OE1 NE2 REMARK 470 LYS D 247 CG CD CE NZ REMARK 470 GLN D 251 CG CD OE1 NE2 REMARK 470 ARG D 255 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 260 CG CD OE1 NE2 REMARK 470 GLU D 266 CG CD OE1 OE2 REMARK 470 ARG D 267 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 304 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 305 CG CD OE1 OE2 REMARK 470 LYS D 307 CG CD CE NZ REMARK 470 LYS D 312 CG CD CE NZ REMARK 470 GLU D 327 CG CD OE1 OE2 REMARK 470 ARG D 329 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 333 CG CD OE1 OE2 REMARK 470 ARG D 344 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 345 CG CD CE NZ REMARK 470 GLN D 348 CG CD OE1 NE2 REMARK 470 ARG D 351 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 355 CG CD OE1 OE2 REMARK 470 GLU D 373 CG CD OE1 OE2 REMARK 470 LYS D 401 CG CD CE NZ REMARK 470 LEU D 454 CG CD1 CD2 REMARK 470 ARG D 458 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 479 CG CD CE NZ REMARK 470 ARG D 497 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 500 CG CD CE NZ REMARK 470 LYS D 501 CG CD CE NZ REMARK 470 ARG D 530 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 536 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 28 -169.95 -61.31 REMARK 500 GLN A 31 -32.45 65.68 REMARK 500 LYS A 37 143.70 -172.73 REMARK 500 LYS A 40 7.42 -67.90 REMARK 500 THR A 42 -1.37 -155.88 REMARK 500 SER A 43 -12.86 84.34 REMARK 500 ALA A 53 -67.31 -100.35 REMARK 500 SER A 57 126.10 -38.27 REMARK 500 ASP A 78 36.28 -90.94 REMARK 500 LYS A 79 29.77 47.03 REMARK 500 ASN A 99 137.37 -172.94 REMARK 500 LEU A 101 -72.95 -110.93 REMARK 500 SER A 110 154.38 -40.86 REMARK 500 ASN A 130 -43.34 -20.55 REMARK 500 GLU A 141 140.82 163.70 REMARK 500 ASP A 144 -10.42 71.72 REMARK 500 GLU A 181 103.45 -44.61 REMARK 500 GLU A 189 -3.55 75.57 REMARK 500 GLN A 195 -156.98 -145.22 REMARK 500 ALA A 206 142.45 -174.65 REMARK 500 PRO A 222 -6.72 -56.44 REMARK 500 ASP A 237 4.92 -61.75 REMARK 500 TRP A 308 -61.33 -125.17 REMARK 500 ASN A 313 -163.22 -102.60 REMARK 500 LEU B 71 -137.94 -102.43 REMARK 500 LEU B 74 -87.97 -73.21 REMARK 500 TYR B 76 -5.86 102.01 REMARK 500 PRO B 96 141.19 -39.36 REMARK 500 THR B 100 36.54 -66.84 REMARK 500 SER B 101 -69.42 80.37 REMARK 500 LYS B 102 -140.21 51.01 REMARK 500 VAL B 108 -71.48 -41.94 REMARK 500 ASN B 141 -76.08 -47.93 REMARK 500 ARG B 161 -25.71 -39.80 REMARK 500 ASN B 210 -75.15 -38.79 REMARK 500 ASP B 216 29.75 49.23 REMARK 500 THR B 242 -166.40 -120.95 REMARK 500 ARG B 255 13.22 -66.10 REMARK 500 GLU B 266 -17.97 -46.72 REMARK 500 ARG B 267 -72.64 -49.89 REMARK 500 LEU B 270 -89.00 -29.03 REMARK 500 TYR B 331 -27.87 -39.63 REMARK 500 ILE B 346 0.17 -65.31 REMARK 500 TRP B 353 -33.29 -34.29 REMARK 500 PHE B 360 -71.02 -31.12 REMARK 500 TYR B 364 -104.03 -65.31 REMARK 500 ASP B 389 29.24 -74.18 REMARK 500 LYS B 401 82.60 -68.68 REMARK 500 ILE B 402 -72.86 -68.76 REMARK 500 HIS B 403 -42.30 -20.50 REMARK 500 SER B 404 3.06 -62.24 REMARK 500 LEU B 412 -60.60 -98.18 REMARK 500 ALA B 426 -74.23 -59.23 REMARK 500 SER B 463 4.99 -64.83 REMARK 500 ALA B 485 -71.51 -49.15 REMARK 500 LEU B 508 -37.58 -39.98 REMARK 500 VAL B 514 -66.00 -138.01 REMARK 500 LEU B 531 48.40 -109.59 REMARK 500 TYR B 539 -28.72 -37.57 REMARK 500 ASN B 551 -6.67 -59.33 REMARK 500 SER C 28 -169.66 -62.34 REMARK 500 GLN C 31 -29.29 69.47 REMARK 500 LYS C 37 142.69 -178.01 REMARK 500 LYS C 40 3.79 -67.03 REMARK 500 THR C 42 -5.28 -154.75 REMARK 500 SER C 43 -16.48 88.68 REMARK 500 ALA C 53 -67.11 -105.78 REMARK 500 SER C 57 128.62 -37.16 REMARK 500 TYR C 68 -38.26 -130.61 REMARK 500 ASP C 78 35.45 -86.05 REMARK 500 ASN C 99 138.49 -172.08 REMARK 500 LEU C 101 -73.30 -109.94 REMARK 500 SER C 110 155.88 -42.22 REMARK 500 ASN C 130 -41.78 -21.19 REMARK 500 GLU C 141 141.75 167.85 REMARK 500 ASP C 144 -8.49 70.61 REMARK 500 ASP C 168 117.70 -167.01 REMARK 500 GLU C 181 100.85 -40.85 REMARK 500 GLU C 189 -3.08 71.49 REMARK 500 GLN C 195 -159.57 -145.93 REMARK 500 HIS C 203 102.58 -168.95 REMARK 500 ALA C 206 144.51 179.96 REMARK 500 PRO C 222 -7.28 -51.62 REMARK 500 ASP C 237 4.17 -61.70 REMARK 500 TRP C 308 -65.26 -124.37 REMARK 500 ASN C 313 -167.02 -108.98 REMARK 500 THR C 317 63.40 37.71 REMARK 500 LEU D 71 -131.85 -106.23 REMARK 500 LEU D 74 -87.73 -70.11 REMARK 500 TYR D 76 -5.71 103.72 REMARK 500 PRO D 96 139.85 -39.37 REMARK 500 THR D 100 36.20 -71.54 REMARK 500 SER D 101 -69.63 79.85 REMARK 500 LYS D 102 -139.72 51.58 REMARK 500 VAL D 108 -70.79 -40.53 REMARK 500 ASN D 141 -80.82 -43.00 REMARK 500 ARG D 161 -29.97 -36.58 REMARK 500 LEU D 185 -33.67 -37.74 REMARK 500 SER D 215 47.42 -72.82 REMARK 500 THR D 242 -169.27 -118.33 REMARK 500 ARG D 255 25.29 -75.03 REMARK 500 GLU D 266 -17.66 -48.74 REMARK 500 LEU D 270 -87.61 -23.06 REMARK 500 TYR D 331 -32.52 -39.87 REMARK 500 TYR D 364 -103.81 -61.03 REMARK 500 SER D 371 -72.58 -25.53 REMARK 500 THR D 387 -71.09 -55.55 REMARK 500 ASP D 389 30.23 -69.75 REMARK 500 LYS D 401 80.53 -67.04 REMARK 500 ILE D 402 -75.60 -65.41 REMARK 500 HIS D 403 -39.98 -19.42 REMARK 500 SER D 404 5.45 -64.64 REMARK 500 ALA D 426 -74.00 -66.75 REMARK 500 SER D 463 5.33 -68.97 REMARK 500 CYS D 474 5.89 -68.88 REMARK 500 ASP D 478 101.93 -58.62 REMARK 500 ALA D 485 -71.49 -45.75 REMARK 500 VAL D 514 -67.68 -137.17 REMARK 500 SER D 524 -28.42 -39.53 REMARK 500 ARG D 530 70.84 42.28 REMARK 500 LEU D 531 68.72 -116.30 REMARK 500 GLU D 537 -15.18 -49.46 REMARK 500 ASN D 544 -51.00 -27.87 REMARK 500 REMARK 500 REMARK: NULL DBREF 3EWE A 1 349 UNP P53011 SEH1_YEAST 1 349 DBREF 3EWE B 1 564 UNP P46673 NUP85_YEAST 1 564 DBREF 3EWE C 1 349 UNP P53011 SEH1_YEAST 1 349 DBREF 3EWE D 1 564 UNP P46673 NUP85_YEAST 1 564 SEQRES 1 A 349 MET GLN PRO PHE ASP SER GLY HIS ASP ASP LEU VAL HIS SEQRES 2 A 349 ASP VAL VAL TYR ASP PHE TYR GLY ARG HIS VAL ALA THR SEQRES 3 A 349 CYS SER SER ASP GLN HIS ILE LYS VAL PHE LYS LEU ASP SEQRES 4 A 349 LYS ASP THR SER ASN TRP GLU LEU SER ASP SER TRP ARG SEQRES 5 A 349 ALA HIS ASP SER SER ILE VAL ALA ILE ASP TRP ALA SER SEQRES 6 A 349 PRO GLU TYR GLY ARG ILE ILE ALA SER ALA SER TYR ASP SEQRES 7 A 349 LYS THR VAL LYS LEU TRP GLU GLU ASP PRO ASP GLN GLU SEQRES 8 A 349 GLU CYS SER GLY ARG ARG TRP ASN LYS LEU CYS THR LEU SEQRES 9 A 349 ASN ASP SER LYS GLY SER LEU TYR SER VAL LYS PHE ALA SEQRES 10 A 349 PRO ALA HIS LEU GLY LEU LYS LEU ALA CYS LEU GLY ASN SEQRES 11 A 349 ASP GLY ILE LEU ARG LEU TYR ASP ALA LEU GLU PRO SER SEQRES 12 A 349 ASP LEU ARG SER TRP THR LEU THR SER GLU MET LYS VAL SEQRES 13 A 349 LEU SER ILE PRO PRO ALA ASN HIS LEU GLN SER ASP PHE SEQRES 14 A 349 CYS LEU SER TRP CYS PRO SER ARG PHE SER PRO GLU LYS SEQRES 15 A 349 LEU ALA VAL SER ALA LEU GLU GLN ALA ILE ILE TYR GLN SEQRES 16 A 349 ARG GLY LYS ASP GLY LYS LEU HIS VAL ALA ALA LYS LEU SEQRES 17 A 349 PRO GLY HIS LYS SER LEU ILE ARG SER ILE SER TRP ALA SEQRES 18 A 349 PRO SER ILE GLY ARG TRP TYR GLN LEU ILE ALA THR GLY SEQRES 19 A 349 CYS LYS ASP GLY ARG ILE ARG ILE PHE LYS ILE THR GLU SEQRES 20 A 349 LYS LEU SER PRO LEU ALA SER GLU GLU SER LEU THR ASN SEQRES 21 A 349 SER ASN MET PHE ASP ASN SER ALA ASP VAL ASP MET ASP SEQRES 22 A 349 ALA GLN GLY ARG SER ASP SER ASN THR GLU GLU LYS ALA SEQRES 23 A 349 GLU LEU GLN SER ASN LEU GLN VAL GLU LEU LEU SER GLU SEQRES 24 A 349 HIS ASP ASP HIS ASN GLY GLU VAL TRP SER VAL SER TRP SEQRES 25 A 349 ASN LEU THR GLY THR ILE LEU SER SER ALA GLY ASP ASP SEQRES 26 A 349 GLY LYS VAL ARG LEU TRP LYS ALA THR TYR SER ASN GLU SEQRES 27 A 349 PHE LYS CYS MET SER VAL ILE THR ALA GLN GLN SEQRES 1 B 564 MET THR ILE ASP ASP SER ASN ARG LEU LEU MET ASP VAL SEQRES 2 B 564 ASP GLN PHE ASP PHE LEU ASP ASP GLY THR ALA GLN LEU SEQRES 3 B 564 SER ASN ASN LYS THR ASP GLU GLU GLU GLN LEU TYR LYS SEQRES 4 B 564 ARG ASP PRO VAL SER GLY ALA ILE LEU VAL PRO MET THR SEQRES 5 B 564 VAL ASN ASP GLN PRO ILE GLU LYS ASN GLY ASP LYS MET SEQRES 6 B 564 PRO LEU LYS PHE LYS LEU GLY PRO LEU SER TYR GLN ASN SEQRES 7 B 564 MET ALA PHE ILE THR ALA LYS ASP LYS TYR LYS LEU TYR SEQRES 8 B 564 PRO VAL ARG ILE PRO ARG LEU ASP THR SER LYS GLU PHE SEQRES 9 B 564 SER ALA TYR VAL SER GLY LEU PHE GLU ILE TYR ARG ASP SEQRES 10 B 564 LEU GLY ASP ASP ARG VAL PHE ASN VAL PRO THR ILE GLY SEQRES 11 B 564 VAL VAL ASN SER ASN PHE ALA LYS GLU HIS ASN ALA THR SEQRES 12 B 564 VAL ASN LEU ALA MET GLU ALA ILE LEU ASN GLU LEU GLU SEQRES 13 B 564 VAL PHE ILE GLY ARG VAL LYS ASP GLN ASP GLY ARG VAL SEQRES 14 B 564 ASN ARG PHE TYR GLU LEU GLU GLU SER LEU THR VAL LEU SEQRES 15 B 564 ASN CYS LEU ARG THR MET TYR PHE ILE LEU ASP GLY GLN SEQRES 16 B 564 ASP VAL GLU GLU ASN ARG SER GLU PHE ILE GLU SER LEU SEQRES 17 B 564 LEU ASN TRP ILE ASN ARG SER ASP GLY GLU PRO ASP GLU SEQRES 18 B 564 GLU TYR ILE GLU GLN VAL PHE SER VAL LYS ASP SER THR SEQRES 19 B 564 ALA GLY LYS LYS VAL PHE GLU THR GLN TYR PHE TRP LYS SEQRES 20 B 564 LEU LEU ASN GLN LEU VAL LEU ARG GLY LEU LEU SER GLN SEQRES 21 B 564 ALA ILE GLY CYS ILE GLU ARG SER ASP LEU LEU PRO TYR SEQRES 22 B 564 LEU SER ASP THR CYS ALA VAL SER PHE ASP ALA VAL SER SEQRES 23 B 564 ASP SER ILE GLU LEU LEU LYS GLN TYR PRO LYS ASP SER SEQRES 24 B 564 SER SER THR PHE ARG GLU TRP LYS ASN LEU VAL LEU LYS SEQRES 25 B 564 LEU SER GLN ALA PHE GLY SER SER ALA THR ASP ILE SER SEQRES 26 B 564 GLY GLU LEU ARG ASP TYR ILE GLU ASP PHE LEU LEU VAL SEQRES 27 B 564 ILE GLY GLY ASN GLN ARG LYS ILE LEU GLN TYR SER ARG SEQRES 28 B 564 THR TRP TYR GLU SER PHE CYS GLY PHE LEU LEU TYR TYR SEQRES 29 B 564 ILE PRO SER LEU GLU LEU SER ALA GLU TYR LEU GLN MET SEQRES 30 B 564 SER LEU GLU ALA ASN VAL VAL ASP ILE THR ASN ASP TRP SEQRES 31 B 564 GLU GLN PRO CYS VAL ASP ILE ILE SER GLY LYS ILE HIS SEQRES 32 B 564 SER ILE LEU PRO VAL MET GLU SER LEU ASP SER CYS THR SEQRES 33 B 564 ALA ALA PHE THR ALA MET ILE CYS GLU ALA LYS GLY LEU SEQRES 34 B 564 ILE GLU ASN ILE PHE GLU GLY GLU LYS ASN SER ASP ASP SEQRES 35 B 564 TYR SER ASN GLU ASP ASN GLU MET LEU GLU ASP LEU PHE SEQRES 36 B 564 SER TYR ARG ASN GLY MET ALA SER TYR MET LEU ASN SER SEQRES 37 B 564 PHE ALA PHE GLU LEU CYS SER LEU GLY ASP LYS GLU LEU SEQRES 38 B 564 TRP PRO VAL ALA ILE GLY LEU ILE ALA LEU SER ALA THR SEQRES 39 B 564 GLY THR ARG SER ALA LYS LYS MET VAL ILE ALA GLU LEU SEQRES 40 B 564 LEU PRO HIS TYR PRO PHE VAL THR ASN ASP ASP ILE GLU SEQRES 41 B 564 TRP MET LEU SER ILE CYS VAL GLU TRP ARG LEU PRO GLU SEQRES 42 B 564 ILE ALA LYS GLU ILE TYR THR THR LEU GLY ASN GLN MET SEQRES 43 B 564 LEU SER ALA HIS ASN ILE ILE GLU SER ILE ALA ASN PHE SEQRES 44 B 564 SER ARG ALA GLY LYS SEQRES 1 C 349 MET GLN PRO PHE ASP SER GLY HIS ASP ASP LEU VAL HIS SEQRES 2 C 349 ASP VAL VAL TYR ASP PHE TYR GLY ARG HIS VAL ALA THR SEQRES 3 C 349 CYS SER SER ASP GLN HIS ILE LYS VAL PHE LYS LEU ASP SEQRES 4 C 349 LYS ASP THR SER ASN TRP GLU LEU SER ASP SER TRP ARG SEQRES 5 C 349 ALA HIS ASP SER SER ILE VAL ALA ILE ASP TRP ALA SER SEQRES 6 C 349 PRO GLU TYR GLY ARG ILE ILE ALA SER ALA SER TYR ASP SEQRES 7 C 349 LYS THR VAL LYS LEU TRP GLU GLU ASP PRO ASP GLN GLU SEQRES 8 C 349 GLU CYS SER GLY ARG ARG TRP ASN LYS LEU CYS THR LEU SEQRES 9 C 349 ASN ASP SER LYS GLY SER LEU TYR SER VAL LYS PHE ALA SEQRES 10 C 349 PRO ALA HIS LEU GLY LEU LYS LEU ALA CYS LEU GLY ASN SEQRES 11 C 349 ASP GLY ILE LEU ARG LEU TYR ASP ALA LEU GLU PRO SER SEQRES 12 C 349 ASP LEU ARG SER TRP THR LEU THR SER GLU MET LYS VAL SEQRES 13 C 349 LEU SER ILE PRO PRO ALA ASN HIS LEU GLN SER ASP PHE SEQRES 14 C 349 CYS LEU SER TRP CYS PRO SER ARG PHE SER PRO GLU LYS SEQRES 15 C 349 LEU ALA VAL SER ALA LEU GLU GLN ALA ILE ILE TYR GLN SEQRES 16 C 349 ARG GLY LYS ASP GLY LYS LEU HIS VAL ALA ALA LYS LEU SEQRES 17 C 349 PRO GLY HIS LYS SER LEU ILE ARG SER ILE SER TRP ALA SEQRES 18 C 349 PRO SER ILE GLY ARG TRP TYR GLN LEU ILE ALA THR GLY SEQRES 19 C 349 CYS LYS ASP GLY ARG ILE ARG ILE PHE LYS ILE THR GLU SEQRES 20 C 349 LYS LEU SER PRO LEU ALA SER GLU GLU SER LEU THR ASN SEQRES 21 C 349 SER ASN MET PHE ASP ASN SER ALA ASP VAL ASP MET ASP SEQRES 22 C 349 ALA GLN GLY ARG SER ASP SER ASN THR GLU GLU LYS ALA SEQRES 23 C 349 GLU LEU GLN SER ASN LEU GLN VAL GLU LEU LEU SER GLU SEQRES 24 C 349 HIS ASP ASP HIS ASN GLY GLU VAL TRP SER VAL SER TRP SEQRES 25 C 349 ASN LEU THR GLY THR ILE LEU SER SER ALA GLY ASP ASP SEQRES 26 C 349 GLY LYS VAL ARG LEU TRP LYS ALA THR TYR SER ASN GLU SEQRES 27 C 349 PHE LYS CYS MET SER VAL ILE THR ALA GLN GLN SEQRES 1 D 564 MET THR ILE ASP ASP SER ASN ARG LEU LEU MET ASP VAL SEQRES 2 D 564 ASP GLN PHE ASP PHE LEU ASP ASP GLY THR ALA GLN LEU SEQRES 3 D 564 SER ASN ASN LYS THR ASP GLU GLU GLU GLN LEU TYR LYS SEQRES 4 D 564 ARG ASP PRO VAL SER GLY ALA ILE LEU VAL PRO MET THR SEQRES 5 D 564 VAL ASN ASP GLN PRO ILE GLU LYS ASN GLY ASP LYS MET SEQRES 6 D 564 PRO LEU LYS PHE LYS LEU GLY PRO LEU SER TYR GLN ASN SEQRES 7 D 564 MET ALA PHE ILE THR ALA LYS ASP LYS TYR LYS LEU TYR SEQRES 8 D 564 PRO VAL ARG ILE PRO ARG LEU ASP THR SER LYS GLU PHE SEQRES 9 D 564 SER ALA TYR VAL SER GLY LEU PHE GLU ILE TYR ARG ASP SEQRES 10 D 564 LEU GLY ASP ASP ARG VAL PHE ASN VAL PRO THR ILE GLY SEQRES 11 D 564 VAL VAL ASN SER ASN PHE ALA LYS GLU HIS ASN ALA THR SEQRES 12 D 564 VAL ASN LEU ALA MET GLU ALA ILE LEU ASN GLU LEU GLU SEQRES 13 D 564 VAL PHE ILE GLY ARG VAL LYS ASP GLN ASP GLY ARG VAL SEQRES 14 D 564 ASN ARG PHE TYR GLU LEU GLU GLU SER LEU THR VAL LEU SEQRES 15 D 564 ASN CYS LEU ARG THR MET TYR PHE ILE LEU ASP GLY GLN SEQRES 16 D 564 ASP VAL GLU GLU ASN ARG SER GLU PHE ILE GLU SER LEU SEQRES 17 D 564 LEU ASN TRP ILE ASN ARG SER ASP GLY GLU PRO ASP GLU SEQRES 18 D 564 GLU TYR ILE GLU GLN VAL PHE SER VAL LYS ASP SER THR SEQRES 19 D 564 ALA GLY LYS LYS VAL PHE GLU THR GLN TYR PHE TRP LYS SEQRES 20 D 564 LEU LEU ASN GLN LEU VAL LEU ARG GLY LEU LEU SER GLN SEQRES 21 D 564 ALA ILE GLY CYS ILE GLU ARG SER ASP LEU LEU PRO TYR SEQRES 22 D 564 LEU SER ASP THR CYS ALA VAL SER PHE ASP ALA VAL SER SEQRES 23 D 564 ASP SER ILE GLU LEU LEU LYS GLN TYR PRO LYS ASP SER SEQRES 24 D 564 SER SER THR PHE ARG GLU TRP LYS ASN LEU VAL LEU LYS SEQRES 25 D 564 LEU SER GLN ALA PHE GLY SER SER ALA THR ASP ILE SER SEQRES 26 D 564 GLY GLU LEU ARG ASP TYR ILE GLU ASP PHE LEU LEU VAL SEQRES 27 D 564 ILE GLY GLY ASN GLN ARG LYS ILE LEU GLN TYR SER ARG SEQRES 28 D 564 THR TRP TYR GLU SER PHE CYS GLY PHE LEU LEU TYR TYR SEQRES 29 D 564 ILE PRO SER LEU GLU LEU SER ALA GLU TYR LEU GLN MET SEQRES 30 D 564 SER LEU GLU ALA ASN VAL VAL ASP ILE THR ASN ASP TRP SEQRES 31 D 564 GLU GLN PRO CYS VAL ASP ILE ILE SER GLY LYS ILE HIS SEQRES 32 D 564 SER ILE LEU PRO VAL MET GLU SER LEU ASP SER CYS THR SEQRES 33 D 564 ALA ALA PHE THR ALA MET ILE CYS GLU ALA LYS GLY LEU SEQRES 34 D 564 ILE GLU ASN ILE PHE GLU GLY GLU LYS ASN SER ASP ASP SEQRES 35 D 564 TYR SER ASN GLU ASP ASN GLU MET LEU GLU ASP LEU PHE SEQRES 36 D 564 SER TYR ARG ASN GLY MET ALA SER TYR MET LEU ASN SER SEQRES 37 D 564 PHE ALA PHE GLU LEU CYS SER LEU GLY ASP LYS GLU LEU SEQRES 38 D 564 TRP PRO VAL ALA ILE GLY LEU ILE ALA LEU SER ALA THR SEQRES 39 D 564 GLY THR ARG SER ALA LYS LYS MET VAL ILE ALA GLU LEU SEQRES 40 D 564 LEU PRO HIS TYR PRO PHE VAL THR ASN ASP ASP ILE GLU SEQRES 41 D 564 TRP MET LEU SER ILE CYS VAL GLU TRP ARG LEU PRO GLU SEQRES 42 D 564 ILE ALA LYS GLU ILE TYR THR THR LEU GLY ASN GLN MET SEQRES 43 D 564 LEU SER ALA HIS ASN ILE ILE GLU SER ILE ALA ASN PHE SEQRES 44 D 564 SER ARG ALA GLY LYS HELIX 28 28 GLU B 103 ASP B 117 1 15 HELIX 29 29 LYS B 138 PHE B 190 1 49 HELIX 30 30 ASN B 200 ARG B 214 1 15 HELIX 31 31 PRO B 219 GLU B 225 1 7 HELIX 32 32 THR B 242 ARG B 255 1 14 HELIX 33 33 LEU B 257 GLU B 266 1 10 HELIX 34 34 CYS B 278 GLU B 290 1 13 HELIX 35 35 PHE B 303 PHE B 317 1 15 HELIX 36 36 GLY B 326 LEU B 347 1 22 HELIX 37 37 THR B 352 TYR B 364 1 13 HELIX 38 38 LEU B 370 ASN B 382 1 13 HELIX 39 39 TRP B 390 GLY B 400 1 11 HELIX 40 40 ILE B 402 GLY B 428 1 27 HELIX 41 41 MET B 461 CYS B 474 1 14 HELIX 42 42 LEU B 481 TYR B 511 1 26 HELIX 43 43 THR B 515 GLU B 554 1 40 SHEET 28 28 1 ASN B 78 PHE B 81 0 SHEET 29 29 1 LEU B 90 VAL B 93 0 SSBOND 1 CYS B 184 CYS B 394 1555 1555 2.06 SSBOND 2 CYS D 184 CYS D 394 1555 1555 2.07 CISPEP 1 GLY B 72 PRO B 73 0 -0.82 CISPEP 2 GLY D 72 PRO D 73 0 -0.54 CRYST1 112.559 112.559 350.549 90.00 90.00 90.00 P 41 21 2 16 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 0.008884 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008884 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002853 0.00000 ATOM 1 N MET B 65 189.639 214.420 809.988 1.00207.75 N ANISOU 1 N MET B 65 25604 26673 26659 -744 -2195 1910 N ATOM 2 CA MET B 65 188.378 214.262 810.706 1.00206.49 C ANISOU 2 CA MET B 65 25205 26929 26324 -700 -1926 2121 C ATOM 3 C MET B 65 187.279 215.123 810.086 1.00202.81 C ANISOU 3 C MET B 65 24578 26804 25676 -561 -1854 1850 C ATOM 4 O MET B 65 187.532 216.261 809.693 1.00200.52 O ANISOU 4 O MET B 65 24410 26503 25274 -363 -1941 1527 O ATOM 5 CB MET B 65 188.562 214.591 812.193 1.00206.67 C ANISOU 5 CB MET B 65 25353 27028 26145 -475 -1779 2302 C ATOM 6 CG MET B 65 189.266 215.907 812.463 1.00204.89 C ANISOU 6 CG MET B 65 25357 26727 25765 -166 -1874 2032 C ATOM 7 SD MET B 65 189.526 216.277 814.215 1.00205.63 S ANISOU 7 SD MET B 65 25586 26931 25614 91 -1751 2260 S ATOM 8 CE MET B 65 187.847 216.474 814.809 1.00203.42 C ANISOU 8 CE MET B 65 25073 27187 25028 171 -1476 2303 C ATOM 9 N PRO B 66 186.057 214.569 809.982 1.00151.81 N ANISOU 9 N PRO B 66 17837 20643 19202 -658 -1683 2000 N ATOM 10 CA PRO B 66 184.902 215.252 809.385 1.00148.80 C ANISOU 10 CA PRO B 66 17288 20571 18680 -539 -1597 1793 C ATOM 11 C PRO B 66 184.062 216.028 810.398 1.00146.69 C ANISOU 11 C PRO B 66 17014 20598 18122 -269 -1365 1776 C ATOM 12 O PRO B 66 183.354 215.413 811.189 1.00147.80 O ANISOU 12 O PRO B 66 17031 20934 18191 -274 -1148 2029 O ATOM 13 CB PRO B 66 184.061 214.096 808.810 1.00150.47 C ANISOU 13 CB PRO B 66 17186 20925 19060 -784 -1532 2011 C ATOM 14 CG PRO B 66 184.869 212.835 809.032 1.00154.40 C ANISOU 14 CG PRO B 66 17690 21170 19806 -1066 -1609 2314 C ATOM 15 CD PRO B 66 185.784 213.141 810.185 1.00154.99 C ANISOU 15 CD PRO B 66 18044 21062 19785 -927 -1591 2383 C ATOM 16 N LEU B 67 184.125 217.356 810.373 1.00165.72 N ANISOU 16 N LEU B 67 19554 23048 20365 -42 -1408 1479 N ATOM 17 CA LEU B 67 183.289 218.169 811.254 1.00163.90 C ANISOU 17 CA LEU B 67 19320 23085 19868 188 -1224 1420 C ATOM 18 C LEU B 67 181.880 218.258 810.720 1.00162.43 C ANISOU 18 C LEU B 67 18922 23157 19638 206 -1077 1358 C ATOM 19 O LEU B 67 181.606 217.852 809.600 1.00162.49 O ANISOU 19 O LEU B 67 18780 23152 19807 68 -1140 1339 O ATOM 20 CB LEU B 67 183.835 219.587 811.398 1.00161.88 C ANISOU 20 CB LEU B 67 19244 22788 19476 402 -1330 1139 C ATOM 21 CG LEU B 67 185.314 219.758 811.727 1.00163.15 C ANISOU 21 CG LEU B 67 19625 22672 19692 446 -1502 1135 C ATOM 22 CD1 LEU B 67 185.534 221.082 812.453 1.00161.68 C ANISOU 22 CD1 LEU B 67 19552 22578 19301 703 -1515 965 C ATOM 23 CD2 LEU B 67 185.836 218.590 812.555 1.00166.26 C ANISOU 23 CD2 LEU B 67 20072 22935 20165 328 -1471 1479 C ATOM 24 N LYS B 68 180.986 218.810 811.525 1.00131.40 N ANISOU 24 N LYS B 68 14987 19453 15485 384 -894 1319 N ATOM 25 CA LYS B 68 179.628 219.066 811.085 1.00130.07 C ANISOU 25 CA LYS B 68 14655 19497 15267 450 -746 1230 C ATOM 26 C LYS B 68 179.068 220.189 811.932 1.00128.57 C ANISOU 26 C LYS B 68 14578 19449 14822 669 -649 1052 C ATOM 27 O LYS B 68 179.385 220.285 813.105 1.00129.42 O ANISOU 27 O LYS B 68 14821 19589 14766 749 -612 1114 O ATOM 28 CB LYS B 68 178.776 217.805 811.222 1.00132.17 C ANISOU 28 CB LYS B 68 14709 19916 15593 361 -542 1511 C ATOM 29 CG LYS B 68 179.499 216.533 810.807 1.00134.65 C ANISOU 29 CG LYS B 68 14924 20085 16153 106 -637 1765 C ATOM 30 CD LYS B 68 178.558 215.404 810.439 1.00136.52 C ANISOU 30 CD LYS B 68 14859 20494 16519 -7 -473 2006 C ATOM 31 CE LYS B 68 179.327 214.215 809.899 1.00139.17 C ANISOU 31 CE LYS B 68 15079 20664 17135 -307 -618 2238 C ATOM 32 NZ LYS B 68 178.437 213.056 809.664 1.00141.52 N ANISOU 32 NZ LYS B 68 15039 21164 17570 -423 -446 2523 N ATOM 33 N PHE B 69 178.243 221.050 811.363 1.00124.57 N ANISOU 33 N PHE B 69 14023 19027 14283 758 -619 839 N ATOM 34 CA PHE B 69 177.767 222.179 812.145 1.00123.45 C ANISOU 34 CA PHE B 69 13996 18985 13923 932 -561 650 C ATOM 35 C PHE B 69 176.296 222.512 811.899 1.00122.75 C ANISOU 35 C PHE B 69 13814 19037 13789 1020 -389 551 C ATOM 36 O PHE B 69 175.915 222.883 810.789 1.00121.47 O ANISOU 36 O PHE B 69 13557 18847 13748 1003 -428 450 O ATOM 37 CB PHE B 69 178.663 223.399 811.897 1.00121.82 C ANISOU 37 CB PHE B 69 13908 18665 13712 979 -765 430 C ATOM 38 CG PHE B 69 178.468 224.508 812.896 1.00121.29 C ANISOU 38 CG PHE B 69 13959 18692 13434 1121 -756 272 C ATOM 39 CD1 PHE B 69 179.337 224.668 813.959 1.00122.28 C ANISOU 39 CD1 PHE B 69 14219 18804 13436 1176 -839 317 C ATOM 40 CE1 PHE B 69 179.138 225.687 814.874 1.00122.13 C ANISOU 40 CE1 PHE B 69 14287 18895 13221 1290 -861 171 C ATOM 41 CZ PHE B 69 178.081 226.547 814.735 1.00121.04 C ANISOU 41 CZ PHE B 69 14118 18848 13025 1332 -796 -28 C ATOM 42 CE2 PHE B 69 177.213 226.400 813.691 1.00120.05 C ANISOU 42 CE2 PHE B 69 13877 18706 13031 1288 -696 -66 C ATOM 43 CD2 PHE B 69 177.403 225.390 812.774 1.00120.14 C ANISOU 43 CD2 PHE B 69 13786 18640 13222 1192 -678 88 C ATOM 44 N LYS B 70 175.482 222.379 812.947 1.00125.65 N ANISOU 44 N LYS B 70 14227 19548 13969 1127 -199 581 N ATOM 45 CA LYS B 70 174.050 222.685 812.885 1.00125.54 C ANISOU 45 CA LYS B 70 14166 19637 13895 1242 -15 473 C ATOM 46 C LYS B 70 173.744 224.028 813.559 1.00124.68 C ANISOU 46 C LYS B 70 14231 19540 13602 1354 -49 205 C ATOM 47 O LYS B 70 174.500 224.478 814.417 1.00124.84 O ANISOU 47 O LYS B 70 14393 19560 13480 1366 -162 157 O ATOM 48 CB LYS B 70 173.232 221.558 813.524 1.00127.98 C ANISOU 48 CB LYS B 70 14405 20101 14120 1300 247 673 C ATOM 49 N LEU B 71 172.633 224.659 813.184 1.00124.70 N ANISOU 49 N LEU B 71 14216 19546 13619 1430 41 45 N ATOM 50 CA LEU B 71 172.385 226.042 813.590 1.00123.91 C ANISOU 50 CA LEU B 71 14256 19416 13409 1485 -33 -220 C ATOM 51 C LEU B 71 171.393 226.295 814.742 1.00125.60 C ANISOU 51 C LEU B 71 14622 19712 13388 1606 111 -354 C ATOM 52 O LEU B 71 171.419 225.590 815.733 1.00127.45 O ANISOU 52 O LEU B 71 14930 20061 13433 1656 206 -255 O ATOM 53 CB LEU B 71 172.098 226.926 812.372 1.00122.10 C ANISOU 53 CB LEU B 71 13948 19083 13363 1456 -103 -346 C ATOM 54 CG LEU B 71 173.314 227.770 811.970 1.00120.51 C ANISOU 54 CG LEU B 71 13756 18811 13221 1377 -337 -420 C ATOM 55 CD1 LEU B 71 174.549 226.920 811.900 1.00120.67 C ANISOU 55 CD1 LEU B 71 13750 18814 13285 1307 -438 -250 C ATOM 56 CD2 LEU B 71 173.071 228.499 810.672 1.00119.05 C ANISOU 56 CD2 LEU B 71 13479 18553 13203 1349 -381 -495 C ATOM 57 N GLY B 72 170.535 227.308 814.607 1.00129.79 N ANISOU 57 N GLY B 72 15213 20177 13926 1648 123 -578 N ATOM 58 CA GLY B 72 169.862 227.932 815.747 1.00131.39 C ANISOU 58 CA GLY B 72 15613 20414 13895 1724 159 -791 C ATOM 59 C GLY B 72 168.486 227.441 816.206 1.00133.67 C ANISOU 59 C GLY B 72 15987 20740 14062 1874 420 -844 C ATOM 60 O GLY B 72 168.093 226.305 815.933 1.00134.55 O ANISOU 60 O GLY B 72 15989 20916 14219 1947 621 -651 O ATOM 61 N PRO B 73 167.733 228.295 816.929 1.00128.32 N ANISOU 61 N PRO B 73 15506 20022 13230 1926 420 -1113 N ATOM 62 CA PRO B 73 168.057 229.664 817.368 1.00127.95 C ANISOU 62 CA PRO B 73 15575 19916 13126 1827 182 -1350 C ATOM 63 C PRO B 73 169.184 229.728 818.393 1.00128.37 C ANISOU 63 C PRO B 73 15697 20118 12960 1779 -2 -1319 C ATOM 64 O PRO B 73 169.258 228.883 819.286 1.00130.19 O ANISOU 64 O PRO B 73 16017 20501 12951 1861 91 -1223 O ATOM 65 CB PRO B 73 166.746 230.157 817.995 1.00130.36 C ANISOU 65 CB PRO B 73 16089 20147 13293 1914 285 -1621 C ATOM 66 CG PRO B 73 165.690 229.272 817.410 1.00131.17 C ANISOU 66 CG PRO B 73 16139 20205 13495 2067 578 -1528 C ATOM 67 CD PRO B 73 166.337 227.939 817.227 1.00130.71 C ANISOU 67 CD PRO B 73 15912 20310 13440 2095 678 -1209 C ATOM 68 N LEU B 74 170.045 230.735 818.271 1.00168.92 N ANISOU 68 N LEU B 74 20785 25221 18176 1661 -252 -1385 N ATOM 69 CA LEU B 74 171.261 230.770 819.077 1.00169.21 C ANISOU 69 CA LEU B 74 20845 25389 18058 1633 -440 -1307 C ATOM 70 C LEU B 74 171.021 231.112 820.559 1.00171.95 C ANISOU 70 C LEU B 74 21400 25872 18061 1670 -520 -1470 C ATOM 71 O LEU B 74 170.825 230.199 821.376 1.00173.94 O ANISOU 71 O LEU B 74 21772 26258 18059 1772 -391 -1384 O ATOM 72 CB LEU B 74 172.329 231.681 818.457 1.00167.18 C ANISOU 72 CB LEU B 74 20445 25075 17998 1529 -666 -1303 C ATOM 73 CG LEU B 74 172.307 233.190 818.674 1.00167.38 C ANISOU 73 CG LEU B 74 20474 25079 18043 1442 -862 -1531 C ATOM 74 CD1 LEU B 74 173.676 233.720 818.434 1.00166.16 C ANISOU 74 CD1 LEU B 74 20182 24957 17993 1401 -1062 -1446 C ATOM 75 CD2 LEU B 74 171.296 233.875 817.798 1.00166.71 C ANISOU 75 CD2 LEU B 74 20352 24831 18160 1386 -783 -1673 C ATOM 76 N SER B 75 171.015 232.409 820.897 1.00130.02 N ANISOU 76 N SER B 75 16128 20542 12732 1584 -731 -1698 N ATOM 77 CA SER B 75 171.111 232.875 822.289 1.00132.66 C ANISOU 77 CA SER B 75 16628 21032 12746 1584 -904 -1842 C ATOM 78 C SER B 75 172.252 232.093 822.900 1.00133.05 C ANISOU 78 C SER B 75 16668 21254 12631 1651 -960 -1585 C ATOM 79 O SER B 75 172.219 231.735 824.076 1.00135.65 O ANISOU 79 O SER B 75 17164 21758 12619 1724 -977 -1583 O ATOM 80 CB SER B 75 169.786 232.714 823.063 1.00135.57 C ANISOU 80 CB SER B 75 17243 21417 12852 1658 -768 -2064 C ATOM 81 OG SER B 75 169.893 231.842 824.170 1.00137.98 O ANISOU 81 OG SER B 75 17707 21932 12787 1780 -704 -1976 O ATOM 82 N TYR B 76 173.246 231.823 822.051 1.00211.41 N ANISOU 82 N TYR B 76 26408 31113 22804 1628 -983 -1367 N ATOM 83 CA TYR B 76 174.512 231.216 822.446 1.00211.61 C ANISOU 83 CA TYR B 76 26405 31232 22764 1673 -1068 -1109 C ATOM 84 C TYR B 76 174.589 229.727 822.106 1.00211.39 C ANISOU 84 C TYR B 76 26361 31184 22773 1726 -839 -836 C ATOM 85 O TYR B 76 175.643 229.127 822.260 1.00211.53 O ANISOU 85 O TYR B 76 26351 31221 22799 1744 -890 -594 O ATOM 86 CB TYR B 76 174.786 231.456 823.937 1.00214.51 C ANISOU 86 CB TYR B 76 26925 31810 22771 1722 -1234 -1141 C ATOM 87 CG TYR B 76 176.113 230.939 824.479 1.00215.26 C ANISOU 87 CG TYR B 76 27008 31997 22783 1786 -1347 -859 C ATOM 88 CD1 TYR B 76 177.242 231.754 824.515 1.00214.84 C ANISOU 88 CD1 TYR B 76 26844 31952 22834 1775 -1606 -832 C ATOM 89 CE1 TYR B 76 178.461 231.280 825.035 1.00215.89 C ANISOU 89 CE1 TYR B 76 26984 32142 22902 1859 -1709 -564 C ATOM 90 CZ TYR B 76 178.538 229.980 825.529 1.00217.38 C ANISOU 90 CZ TYR B 76 27293 32381 22920 1926 -1552 -309 C ATOM 91 OH TYR B 76 179.720 229.486 826.041 1.00218.72 O ANISOU 91 OH TYR B 76 27486 32576 23041 2005 -1646 -19 O ATOM 92 CE2 TYR B 76 177.426 229.164 825.509 1.00217.83 C ANISOU 92 CE2 TYR B 76 27441 32461 22864 1924 -1286 -325 C ATOM 93 CD2 TYR B 76 176.225 229.645 824.998 1.00216.80 C ANISOU 93 CD2 TYR B 76 27303 32275 22795 1868 -1185 -606 C ATOM 94 N GLN B 77 173.502 229.129 821.621 1.00131.62 N ANISOU 94 N GLN B 77 16261 21031 12718 1748 -590 -858 N ATOM 95 CA GLN B 77 173.517 227.683 821.332 1.00131.88 C ANISOU 95 CA GLN B 77 16240 21074 12794 1784 -369 -580 C ATOM 96 C GLN B 77 173.378 227.266 819.885 1.00129.64 C ANISOU 96 C GLN B 77 15768 20633 12857 1725 -263 -493 C ATOM 97 O GLN B 77 172.292 227.243 819.334 1.00129.38 O ANISOU 97 O GLN B 77 15702 20551 12906 1750 -102 -592 O ATOM 98 CB GLN B 77 172.455 226.922 822.129 1.00134.59 C ANISOU 98 CB GLN B 77 16721 21564 12855 1900 -120 -576 C ATOM 99 CG GLN B 77 172.864 226.527 823.541 1.00137.48 C ANISOU 99 CG GLN B 77 17254 22140 12844 1975 -145 -464 C ATOM 100 CD GLN B 77 172.380 227.520 824.560 1.00139.34 C ANISOU 100 CD GLN B 77 17691 22482 12771 2016 -281 -765 C ATOM 101 OE1 GLN B 77 171.459 228.292 824.288 1.00139.02 O ANISOU 101 OE1 GLN B 77 17691 22351 12779 2002 -278 -1060 O ATOM 102 NE2 GLN B 77 172.999 227.519 825.740 1.00141.59 N ANISOU 102 NE2 GLN B 77 18107 22951 12739 2060 -418 -690 N ATOM 103 N ASN B 78 174.498 226.910 819.283 1.00131.10 N ANISOU 103 N ASN B 78 15839 20735 13238 1655 -362 -303 N ATOM 104 CA ASN B 78 174.494 226.090 818.079 1.00129.88 C ANISOU 104 CA ASN B 78 15519 20474 13356 1592 -257 -145 C ATOM 105 C ASN B 78 175.314 224.856 818.409 1.00131.25 C ANISOU 105 C ASN B 78 15678 20673 13518 1563 -222 168 C ATOM 106 O ASN B 78 176.202 224.926 819.264 1.00132.29 O ANISOU 106 O ASN B 78 15912 20842 13509 1582 -348 247 O ATOM 107 CB ASN B 78 175.126 226.816 816.888 1.00127.36 C ANISOU 107 CB ASN B 78 15088 19997 13306 1509 -428 -226 C ATOM 108 CG ASN B 78 174.740 228.279 816.818 1.00126.36 C ANISOU 108 CG ASN B 78 14990 19850 13170 1518 -531 -506 C ATOM 109 OD1 ASN B 78 175.281 229.111 817.560 1.00126.76 O ANISOU 109 OD1 ASN B 78 15115 19949 13099 1532 -696 -605 O ATOM 110 ND2 ASN B 78 173.801 228.603 815.924 1.00125.33 N ANISOU 110 ND2 ASN B 78 14788 19652 13181 1505 -440 -614 N ATOM 111 N MET B 79 175.012 223.728 817.775 1.00127.83 N ANISOU 111 N MET B 79 15110 20224 13235 1516 -57 366 N ATOM 112 CA MET B 79 175.742 222.512 818.086 1.00129.56 C ANISOU 112 CA MET B 79 15302 20454 13470 1456 -14 689 C ATOM 113 C MET B 79 176.827 222.232 817.060 1.00128.34 C ANISOU 113 C MET B 79 15045 20098 13619 1311 -181 795 C ATOM 114 O MET B 79 176.684 222.560 815.878 1.00126.43 O ANISOU 114 O MET B 79 14694 19753 13590 1255 -241 676 O ATOM 115 CB MET B 79 174.799 221.315 818.244 1.00131.65 C ANISOU 115 CB MET B 79 15474 20861 13687 1485 283 886 C ATOM 116 CG MET B 79 174.192 221.193 819.636 1.00134.21 C ANISOU 116 CG MET B 79 15959 21402 13634 1634 452 890 C ATOM 117 SD MET B 79 175.432 221.315 820.961 1.00135.84 S ANISOU 117 SD MET B 79 16369 21658 13585 1649 280 1018 S ATOM 118 CE MET B 79 176.536 219.982 820.493 1.00136.75 C ANISOU 118 CE MET B 79 16344 21641 13974 1479 274 1438 C ATOM 119 N ALA B 80 177.912 221.624 817.529 1.00131.28 N ANISOU 119 N ALA B 80 15474 20407 14000 1258 -259 1021 N ATOM 120 CA ALA B 80 179.035 221.256 816.674 1.00130.84 C ANISOU 120 CA ALA B 80 15366 20124 14222 1120 -424 1123 C ATOM 121 C ALA B 80 179.495 219.828 816.965 1.00133.49 C ANISOU 121 C ALA B 80 15665 20422 14632 1003 -343 1488 C ATOM 122 O ALA B 80 180.523 219.618 817.598 1.00134.94 O ANISOU 122 O ALA B 80 15970 20510 14791 995 -442 1646 O ATOM 123 CB ALA B 80 180.180 222.228 816.869 1.00130.00 C ANISOU 123 CB ALA B 80 15396 19894 14105 1176 -666 993 C ATOM 124 N PHE B 81 178.714 218.848 816.521 1.00164.30 N ANISOU 124 N PHE B 81 19388 24403 18637 917 -157 1643 N ATOM 125 CA PHE B 81 179.073 217.451 816.711 1.00167.13 C ANISOU 125 CA PHE B 81 19663 24737 19104 772 -65 2017 C ATOM 126 C PHE B 81 179.952 217.009 815.565 1.00166.92 C ANISOU 126 C PHE B 81 19554 24443 19426 560 -261 2069 C ATOM 127 O PHE B 81 179.744 217.408 814.424 1.00164.92 O ANISOU 127 O PHE B 81 19210 24124 19329 518 -361 1866 O ATOM 128 CB PHE B 81 177.833 216.571 816.769 1.00168.73 C ANISOU 128 CB PHE B 81 19673 25171 19266 781 234 2180 C ATOM 129 CG PHE B 81 177.279 216.224 815.430 1.00167.84 C ANISOU 129 CG PHE B 81 19314 25030 19426 669 240 2149 C ATOM 130 CD1 PHE B 81 177.640 215.046 814.801 1.00169.68 C ANISOU 130 CD1 PHE B 81 19351 25180 19937 440 223 2424 C ATOM 131 CE1 PHE B 81 177.131 214.721 813.566 1.00169.17 C ANISOU 131 CE1 PHE B 81 19046 25118 20113 334 200 2403 C ATOM 132 CZ PHE B 81 176.244 215.578 812.947 1.00166.76 C ANISOU 132 CZ PHE B 81 18704 24887 19768 475 213 2124 C ATOM 133 CE2 PHE B 81 175.877 216.757 813.571 1.00164.92 C ANISOU 133 CE2 PHE B 81 18677 24708 19276 695 245 1856 C ATOM 134 CD2 PHE B 81 176.393 217.075 814.801 1.00165.48 C ANISOU 134 CD2 PHE B 81 18976 24788 19112 782 250 1860 C ATOM 135 N ILE B 82 180.933 216.174 815.863 1.00138.14 N ANISOU 135 N ILE B 82 15954 20636 15897 422 -322 2344 N ATOM 136 CA ILE B 82 181.981 215.906 814.900 1.00138.26 C ANISOU 136 CA ILE B 82 15974 20337 16222 231 -560 2341 C ATOM 137 C ILE B 82 182.344 214.436 814.821 1.00141.62 C ANISOU 137 C ILE B 82 16280 20654 16876 -22 -522 2717 C ATOM 138 O ILE B 82 181.902 213.638 815.638 1.00143.99 O ANISOU 138 O ILE B 82 16502 21130 17079 -33 -297 3019 O ATOM 139 CB ILE B 82 183.213 216.767 815.227 1.00137.61 C ANISOU 139 CB ILE B 82 16149 20036 16101 334 -781 2200 C ATOM 140 CG1 ILE B 82 183.102 218.118 814.512 1.00134.25 C ANISOU 140 CG1 ILE B 82 15760 19611 15639 466 -911 1795 C ATOM 141 CD1 ILE B 82 182.113 219.086 815.127 1.00132.47 C ANISOU 141 CD1 ILE B 82 15542 19662 15128 674 -784 1614 C ATOM 142 CG2 ILE B 82 184.512 216.068 814.856 1.00139.73 C ANISOU 142 CG2 ILE B 82 16499 19948 16646 147 -966 2354 C ATOM 143 N THR B 83 183.115 214.082 813.801 1.00168.07 N ANISOU 143 N THR B 83 19610 23721 20528 -233 -740 2692 N ATOM 144 CA THR B 83 183.695 212.748 813.680 1.00171.63 C ANISOU 144 CA THR B 83 19979 23985 21247 -520 -773 3032 C ATOM 145 C THR B 83 182.633 211.654 813.739 1.00173.65 C ANISOU 145 C THR B 83 19921 24512 21545 -642 -517 3334 C ATOM 146 O THR B 83 181.680 211.663 812.959 1.00172.41 O ANISOU 146 O THR B 83 19540 24539 21427 -647 -460 3223 O ATOM 147 CB THR B 83 184.806 212.505 814.746 1.00174.09 C ANISOU 147 CB THR B 83 20526 24086 21533 -511 -809 3268 C ATOM 148 OG1 THR B 83 184.357 212.929 816.040 1.00173.84 O ANISOU 148 OG1 THR B 83 20582 24321 21149 -261 -609 3338 O ATOM 149 CG2 THR B 83 186.084 213.280 814.392 1.00173.16 C ANISOU 149 CG2 THR B 83 20678 23607 21507 -457 -1102 3017 C ATOM 150 N LYS B 87 185.877 212.684 819.108 1.00158.68 N ANISOU 150 N LYS B 87 19127 22342 18820 -14 -513 3953 N ATOM 151 CA LYS B 87 185.245 211.478 818.596 1.00160.48 C ANISOU 151 CA LYS B 87 19086 22643 19245 -270 -347 4193 C ATOM 152 C LYS B 87 183.748 211.471 818.894 1.00159.63 C ANISOU 152 C LYS B 87 18790 22995 18867 -144 -51 4167 C ATOM 153 O LYS B 87 182.921 211.373 817.972 1.00158.13 O ANISOU 153 O LYS B 87 18375 22912 18797 -215 -1 4019 O ATOM 154 CB LYS B 87 185.905 210.223 819.183 1.00165.20 C ANISOU 154 CB LYS B 87 19692 23087 19991 -473 -275 4710 C ATOM 155 N TYR B 88 183.401 211.588 820.177 1.00171.00 N ANISOU 155 N TYR B 88 20335 24705 19932 60 139 4305 N ATOM 156 CA TYR B 88 182.010 211.427 820.607 1.00171.23 C ANISOU 156 CA TYR B 88 20220 25158 19682 192 457 4320 C ATOM 157 C TYR B 88 181.435 212.647 821.327 1.00169.04 C ANISOU 157 C TYR B 88 20121 25118 18988 507 478 3992 C ATOM 158 O TYR B 88 180.271 212.643 821.726 1.00169.29 O ANISOU 158 O TYR B 88 20087 25478 18757 650 729 3942 O ATOM 159 CB TYR B 88 181.877 210.186 821.494 1.00175.83 C ANISOU 159 CB TYR B 88 20723 25917 20168 123 740 4833 C ATOM 160 N LYS B 89 182.251 213.687 821.484 1.00152.72 N ANISOU 160 N LYS B 89 18276 22880 16871 612 212 3764 N ATOM 161 CA LYS B 89 181.846 214.876 822.237 1.00151.13 C ANISOU 161 CA LYS B 89 18244 22888 16291 878 183 3472 C ATOM 162 C LYS B 89 180.787 215.706 821.502 1.00147.72 C ANISOU 162 C LYS B 89 17715 22567 15844 954 202 3051 C ATOM 163 O LYS B 89 180.690 215.652 820.275 1.00145.83 O ANISOU 163 O LYS B 89 17318 22175 15914 822 138 2928 O ATOM 164 CB LYS B 89 183.069 215.736 822.572 1.00150.51 C ANISOU 164 CB LYS B 89 18383 22601 16203 964 -114 3380 C ATOM 165 N LEU B 90 179.982 216.450 822.261 1.00149.37 N ANISOU 165 N LEU B 90 18027 23037 15688 1162 284 2842 N ATOM 166 CA LEU B 90 179.039 217.417 821.693 1.00146.36 C ANISOU 166 CA LEU B 90 17604 22726 15279 1250 275 2429 C ATOM 167 C LEU B 90 179.469 218.838 822.039 1.00144.50 C ANISOU 167 C LEU B 90 17546 22455 14902 1375 24 2120 C ATOM 168 O LEU B 90 179.537 219.205 823.212 1.00146.05 O ANISOU 168 O LEU B 90 17912 22815 14764 1511 2 2126 O ATOM 169 CB LEU B 90 177.624 217.182 822.209 1.00147.66 C ANISOU 169 CB LEU B 90 17743 23198 15164 1383 578 2390 C ATOM 170 CG LEU B 90 176.745 216.242 821.396 1.00148.11 C ANISOU 170 CG LEU B 90 17543 23309 15423 1303 823 2508 C ATOM 171 CD1 LEU B 90 175.307 216.398 821.831 1.00148.88 C ANISOU 171 CD1 LEU B 90 17657 23674 15238 1501 1088 2342 C ATOM 172 CD2 LEU B 90 176.887 216.534 819.932 1.00145.09 C ANISOU 172 CD2 LEU B 90 17002 22697 15430 1166 654 2342 C ATOM 173 N TYR B 91 179.748 219.639 821.017 1.00140.04 N ANISOU 173 N TYR B 91 16928 21700 14581 1328 -167 1861 N ATOM 174 CA TYR B 91 180.283 220.978 821.224 1.00138.45 C ANISOU 174 CA TYR B 91 16844 21454 14306 1427 -411 1600 C ATOM 175 C TYR B 91 179.232 222.077 820.990 1.00136.32 C ANISOU 175 C TYR B 91 16558 21299 13939 1505 -402 1224 C ATOM 176 O TYR B 91 178.835 222.330 819.850 1.00134.08 O ANISOU 176 O TYR B 91 16148 20916 13880 1441 -399 1061 O ATOM 177 CB TYR B 91 181.465 221.208 820.284 1.00136.97 C ANISOU 177 CB TYR B 91 16627 20968 14447 1341 -635 1575 C ATOM 178 CG TYR B 91 182.594 220.204 820.386 1.00139.17 C ANISOU 178 CG TYR B 91 16945 21048 14885 1247 -681 1914 C ATOM 179 CD1 TYR B 91 183.722 220.481 821.145 1.00140.61 C ANISOU 179 CD1 TYR B 91 17280 21144 15001 1338 -848 2025 C ATOM 180 CE1 TYR B 91 184.765 219.583 821.226 1.00142.90 C ANISOU 180 CE1 TYR B 91 17629 21206 15462 1253 -895 2340 C ATOM 181 CZ TYR B 91 184.694 218.389 820.542 1.00143.83 C ANISOU 181 CZ TYR B 91 17639 21186 15825 1043 -785 2543 C ATOM 182 OH TYR B 91 185.733 217.500 820.629 1.00146.48 O ANISOU 182 OH TYR B 91 18042 21260 16353 931 -842 2859 O ATOM 183 CE2 TYR B 91 183.590 218.086 819.776 1.00142.44 C ANISOU 183 CE2 TYR B 91 17281 21125 15715 943 -630 2441 C ATOM 184 CD2 TYR B 91 182.546 218.996 819.698 1.00140.08 C ANISOU 184 CD2 TYR B 91 16937 21048 15240 1061 -573 2131 C ATOM 185 N PRO B 92 178.783 222.742 822.067 1.00135.56 N ANISOU 185 N PRO B 92 16596 21405 13507 1635 -410 1089 N ATOM 186 CA PRO B 92 177.873 223.878 821.927 1.00133.97 C ANISOU 186 CA PRO B 92 16404 21272 13228 1688 -437 725 C ATOM 187 C PRO B 92 178.728 225.100 821.680 1.00132.25 C ANISOU 187 C PRO B 92 16184 20945 13119 1689 -718 545 C ATOM 188 O PRO B 92 179.819 225.172 822.241 1.00133.31 O ANISOU 188 O PRO B 92 16382 21058 13210 1727 -879 680 O ATOM 189 CB PRO B 92 177.233 223.993 823.312 1.00136.55 C ANISOU 189 CB PRO B 92 16901 21853 13129 1810 -366 678 C ATOM 190 CG PRO B 92 177.813 222.868 824.133 1.00139.42 C ANISOU 190 CG PRO B 92 17331 22304 13339 1832 -279 1052 C ATOM 191 CD PRO B 92 179.087 222.476 823.474 1.00138.57 C ANISOU 191 CD PRO B 92 17137 21959 13553 1730 -408 1270 C ATOM 192 N VAL B 93 178.272 226.029 820.845 1.00130.49 N ANISOU 192 N VAL B 93 15880 20655 13045 1660 -768 274 N ATOM 193 CA VAL B 93 179.078 227.204 820.530 1.00129.04 C ANISOU 193 CA VAL B 93 15661 20389 12981 1664 -1007 120 C ATOM 194 C VAL B 93 178.262 228.411 820.070 1.00127.43 C ANISOU 194 C VAL B 93 15402 20199 12817 1646 -1038 -194 C ATOM 195 O VAL B 93 177.245 228.273 819.387 1.00126.46 O ANISOU 195 O VAL B 93 15227 20043 12778 1606 -882 -282 O ATOM 196 CB VAL B 93 180.129 226.915 819.445 1.00127.68 C ANISOU 196 CB VAL B 93 15398 19996 13121 1607 -1082 225 C ATOM 197 CG1 VAL B 93 181.239 227.947 819.521 1.00127.37 C ANISOU 197 CG1 VAL B 93 15354 19909 13132 1673 -1316 144 C ATOM 198 CG2 VAL B 93 180.704 225.514 819.587 1.00129.27 C ANISOU 198 CG2 VAL B 93 15632 20118 13369 1567 -1007 545 C ATOM 199 N ARG B 94 178.759 229.597 820.426 1.00126.82 N ANISOU 199 N ARG B 94 15320 20165 12702 1675 -1244 -336 N ATOM 200 CA ARG B 94 178.092 230.874 820.148 1.00125.85 C ANISOU 200 CA ARG B 94 15140 20062 12617 1636 -1304 -614 C ATOM 201 C ARG B 94 178.510 231.460 818.800 1.00123.51 C ANISOU 201 C ARG B 94 14690 19618 12621 1589 -1345 -676 C ATOM 202 O ARG B 94 179.570 231.116 818.278 1.00122.93 O ANISOU 202 O ARG B 94 14572 19444 12692 1610 -1396 -543 O ATOM 203 CB ARG B 94 178.404 231.887 821.262 1.00127.53 C ANISOU 203 CB ARG B 94 15392 20430 12635 1673 -1519 -722 C ATOM 204 N ILE B 95 177.690 232.354 818.245 1.00122.36 N ANISOU 204 N ILE B 95 14478 19452 12559 1529 -1322 -877 N ATOM 205 CA ILE B 95 178.029 233.041 816.994 1.00120.47 C ANISOU 205 CA ILE B 95 14095 19110 12567 1492 -1352 -936 C ATOM 206 C ILE B 95 179.031 234.175 817.232 1.00120.82 C ANISOU 206 C ILE B 95 14052 19215 12638 1527 -1553 -989 C ATOM 207 O ILE B 95 178.682 235.193 817.803 1.00121.71 O ANISOU 207 O ILE B 95 14135 19427 12682 1493 -1648 -1130 O ATOM 208 CB ILE B 95 176.776 233.651 816.341 1.00119.63 C ANISOU 208 CB ILE B 95 13947 18961 12547 1417 -1250 -1099 C ATOM 209 CG1 ILE B 95 175.696 232.597 816.124 1.00119.63 C ANISOU 209 CG1 ILE B 95 14012 18915 12527 1416 -1040 -1049 C ATOM 210 CD1 ILE B 95 174.509 233.114 815.348 1.00118.94 C ANISOU 210 CD1 ILE B 95 13886 18747 12560 1368 -931 -1176 C ATOM 211 CG2 ILE B 95 177.132 234.324 815.039 1.00117.97 C ANISOU 211 CG2 ILE B 95 13593 18671 12560 1385 -1266 -1126 C ATOM 212 N PRO B 96 180.275 234.021 816.768 1.00139.12 N ANISOU 212 N PRO B 96 13694 16027 23136 1566 2366 -501 N ATOM 213 CA PRO B 96 181.327 235.006 817.076 1.00139.19 C ANISOU 213 CA PRO B 96 13698 16183 23006 1614 2367 -302 C ATOM 214 C PRO B 96 180.848 236.452 817.049 1.00134.79 C ANISOU 214 C PRO B 96 13575 16295 21343 1521 1779 -307 C ATOM 215 O PRO B 96 180.022 236.814 816.218 1.00131.83 O ANISOU 215 O PRO B 96 13369 16217 20504 1328 1315 -755 O ATOM 216 CB PRO B 96 182.371 234.763 815.975 1.00141.52 C ANISOU 216 CB PRO B 96 13494 16122 24155 1432 2457 -967 C ATOM 217 CG PRO B 96 181.709 233.767 815.023 1.00142.21 C ANISOU 217 CG PRO B 96 13357 16010 24665 1267 2387 -1583 C ATOM 218 CD PRO B 96 180.787 232.979 815.875 1.00142.44 C ANISOU 218 CD PRO B 96 13584 15919 24618 1441 2624 -1066 C ATOM 219 N ARG B 97 181.345 237.254 817.982 1.00136.22 N ANISOU 219 N ARG B 97 13912 16718 21129 1681 1832 220 N ATOM 220 CA ARG B 97 180.995 238.669 818.061 1.00132.66 C ANISOU 220 CA ARG B 97 13826 16871 19709 1592 1325 238 C ATOM 221 C ARG B 97 179.521 238.891 818.372 1.00129.88 C ANISOU 221 C ARG B 97 13904 16893 18554 1560 1008 311 C ATOM 222 O ARG B 97 179.058 240.029 818.425 1.00127.14 O ANISOU 222 O ARG B 97 13858 17014 17436 1462 600 284 O ATOM 223 CB ARG B 97 181.356 239.380 816.761 1.00130.85 C ANISOU 223 CB ARG B 97 13490 16758 19470 1337 948 -404 C ATOM 224 CG ARG B 97 182.748 239.051 816.248 1.00133.91 C ANISOU 224 CG ARG B 97 13411 16732 20738 1326 1255 -652 C ATOM 225 CD ARG B 97 183.101 239.852 815.003 1.00132.32 C ANISOU 225 CD ARG B 97 13118 16751 20408 1113 856 -1283 C ATOM 226 NE ARG B 97 182.791 241.260 815.202 1.00128.98 N ANISOU 226 NE ARG B 97 13063 16880 19063 1077 436 -1101 N ATOM 227 CZ ARG B 97 181.642 241.824 814.841 1.00125.70 C ANISOU 227 CZ ARG B 97 12971 16865 17923 967 -3 -1249 C ATOM 228 NH1 ARG B 97 180.701 241.100 814.248 1.00125.18 N ANISOU 228 NH1 ARG B 97 12916 16746 17902 901 -93 -1559 N ATOM 229 NH2 ARG B 97 181.424 243.113 815.061 1.00123.23 N ANISOU 229 NH2 ARG B 97 12949 16994 16880 927 -326 -1084 N ATOM 230 N LEU B 98 178.791 237.800 818.563 1.00128.74 N ANISOU 230 N LEU B 98 13766 16509 18641 1637 1222 389 N ATOM 231 CA LEU B 98 177.384 237.866 818.950 1.00126.72 C ANISOU 231 CA LEU B 98 13901 16544 17701 1636 1007 488 C ATOM 232 C LEU B 98 177.231 238.561 820.299 1.00126.92 C ANISOU 232 C LEU B 98 14206 16991 17027 1826 1000 1032 C ATOM 233 O LEU B 98 177.999 238.322 821.225 1.00129.85 O ANISOU 233 O LEU B 98 14435 17312 17591 2093 1369 1533 O ATOM 234 CB LEU B 98 176.782 236.459 818.987 1.00128.40 C ANISOU 234 CB LEU B 98 14021 16375 18392 1727 1322 530 C ATOM 235 CG LEU B 98 175.414 236.145 819.581 1.00127.53 C ANISOU 235 CG LEU B 98 14254 16430 17773 1806 1283 735 C ATOM 236 CD1 LEU B 98 175.545 235.671 821.007 1.00130.47 C ANISOU 236 CD1 LEU B 98 14663 16802 18107 2153 1704 1413 C ATOM 237 CD2 LEU B 98 174.461 237.332 819.451 1.00124.00 C ANISOU 237 CD2 LEU B 98 14211 16488 16416 1633 772 548 C ATOM 238 N ASP B 99 176.236 239.435 820.396 1.00218.00 N ANISOU 238 N ASP B 99 26105 28963 27761 1699 594 919 N ATOM 239 CA ASP B 99 176.049 240.261 821.579 1.00218.34 C ANISOU 239 CA ASP B 99 26383 29499 27078 1827 499 1283 C ATOM 240 C ASP B 99 175.134 239.550 822.559 1.00219.89 C ANISOU 240 C ASP B 99 26759 29777 27013 2040 697 1602 C ATOM 241 O ASP B 99 173.924 239.487 822.345 1.00218.21 O ANISOU 241 O ASP B 99 26796 29619 26494 1913 512 1369 O ATOM 242 CB ASP B 99 175.444 241.618 821.203 1.00215.26 C ANISOU 242 CB ASP B 99 26257 29510 26020 1562 -9 948 C ATOM 243 CG ASP B 99 175.870 242.109 819.815 1.00213.08 C ANISOU 243 CG ASP B 99 25852 29103 26005 1314 -250 487 C ATOM 244 OD2 ASP B 99 175.532 243.267 819.485 1.00210.95 O ANISOU 244 OD2 ASP B 99 25753 29136 25261 1130 -610 275 O ATOM 245 OD1 ASP B 99 176.520 241.359 819.052 1.00213.84 O ANISOU 245 OD1 ASP B 99 25658 28814 26778 1311 -72 316 O ATOM 246 N THR B 100 175.720 239.028 823.633 1.00143.98 N ANISOU 246 N THR B 100 17007 20186 17513 2394 1098 2158 N ATOM 247 CA THR B 100 175.015 238.134 824.550 1.00146.27 C ANISOU 247 CA THR B 100 17396 20508 17673 2677 1389 2525 C ATOM 248 C THR B 100 173.880 238.802 825.336 1.00145.72 C ANISOU 248 C THR B 100 17690 21020 16655 2681 1095 2498 C ATOM 249 O THR B 100 173.658 238.480 826.497 1.00148.68 O ANISOU 249 O THR B 100 18114 21697 16679 3016 1311 2919 O ATOM 250 CB THR B 100 175.993 237.468 825.544 1.00150.84 C ANISOU 250 CB THR B 100 17702 21024 18586 3128 1940 3209 C ATOM 251 OG1 THR B 100 176.326 238.397 826.585 1.00152.38 O ANISOU 251 OG1 THR B 100 17955 21864 18079 3333 1837 3542 O ATOM 252 CG2 THR B 100 177.270 236.998 824.834 1.00151.99 C ANISOU 252 CG2 THR B 100 17446 20590 19712 3106 2257 3209 C ATOM 253 N SER B 101 173.169 239.721 824.690 1.00163.51 N ANISOU 253 N SER B 101 20170 23431 18524 2325 632 1994 N ATOM 254 CA SER B 101 172.040 240.441 825.291 1.00163.07 C ANISOU 254 CA SER B 101 20438 23855 17666 2251 348 1836 C ATOM 255 C SER B 101 172.472 241.604 826.189 1.00164.48 C ANISOU 255 C SER B 101 20619 24653 17221 2318 153 1951 C ATOM 256 O SER B 101 172.254 242.762 825.851 1.00162.51 O ANISOU 256 O SER B 101 20480 24621 16646 2031 -224 1591 O ATOM 257 CB SER B 101 171.082 239.495 826.022 1.00165.01 C ANISOU 257 CB SER B 101 20831 24119 17748 2478 586 2032 C ATOM 258 OG SER B 101 171.565 239.182 827.309 1.00169.03 O ANISOU 258 OG SER B 101 21231 24968 18025 2904 875 2570 O ATOM 259 N LYS B 102 173.068 241.296 827.331 1.00135.10 N ANISOU 259 N LYS B 102 16754 21238 13338 2718 427 2468 N ATOM 260 CA LYS B 102 173.738 242.310 828.154 1.00137.05 C ANISOU 260 CA LYS B 102 16904 22096 13071 2843 285 2645 C ATOM 261 C LYS B 102 172.931 243.581 828.494 1.00136.44 C ANISOU 261 C LYS B 102 17037 22584 12221 2601 -179 2217 C ATOM 262 O LYS B 102 171.741 243.538 828.812 1.00136.71 O ANISOU 262 O LYS B 102 17298 22780 11866 2536 -281 1967 O ATOM 263 CB LYS B 102 175.074 242.713 827.501 1.00136.02 C ANISOU 263 CB LYS B 102 16525 21733 13423 2764 299 2715 C ATOM 264 N GLU B 103 173.635 244.709 828.455 1.00151.24 N ANISOU 264 N GLU B 103 18802 24742 13919 2477 -424 2138 N ATOM 265 CA GLU B 103 173.047 246.041 828.594 1.00150.62 C ANISOU 265 CA GLU B 103 18853 25106 13271 2183 -859 1682 C ATOM 266 C GLU B 103 172.776 246.574 827.198 1.00146.19 C ANISOU 266 C GLU B 103 18406 24068 13073 1731 -1092 1222 C ATOM 267 O GLU B 103 172.260 247.675 827.014 1.00145.15 O ANISOU 267 O GLU B 103 18378 24120 12652 1429 -1413 817 O ATOM 268 CB GLU B 103 174.010 246.979 829.326 1.00153.02 C ANISOU 268 CB GLU B 103 18935 26005 13202 2322 -980 1885 C ATOM 269 CG GLU B 103 175.479 246.780 828.984 1.00152.92 C ANISOU 269 CG GLU B 103 18659 25739 13705 2489 -755 2314 C ATOM 270 CD GLU B 103 176.155 245.736 829.871 1.00156.90 C ANISOU 270 CD GLU B 103 18960 26345 14308 3033 -286 2997 C ATOM 271 OE1 GLU B 103 177.300 245.340 829.554 1.00157.20 O ANISOU 271 OE1 GLU B 103 18773 26032 14924 3188 11 3367 O ATOM 272 OE2 GLU B 103 175.545 245.315 830.886 1.00160.09 O ANISOU 272 OE2 GLU B 103 19414 27179 14233 3323 -184 3169 O ATOM 273 N PHE B 104 173.166 245.761 826.224 1.00128.51 N ANISOU 273 N PHE B 104 16107 21228 11494 1717 -899 1299 N ATOM 274 CA PHE B 104 172.868 245.964 824.814 1.00124.76 C ANISOU 274 CA PHE B 104 15711 20301 11391 1379 -1057 909 C ATOM 275 C PHE B 104 171.346 245.832 824.596 1.00123.67 C ANISOU 275 C PHE B 104 15853 20062 11074 1201 -1145 574 C ATOM 276 O PHE B 104 170.753 246.517 823.753 1.00121.35 O ANISOU 276 O PHE B 104 15681 19647 10781 906 -1364 206 O ATOM 277 CB PHE B 104 173.705 244.962 823.978 1.00123.94 C ANISOU 277 CB PHE B 104 15405 19661 12024 1470 -794 1060 C ATOM 278 CG PHE B 104 173.207 244.752 822.574 1.00120.89 C ANISOU 278 CG PHE B 104 15079 18847 12007 1219 -894 674 C ATOM 279 CD1 PHE B 104 173.207 243.487 822.011 1.00120.82 C ANISOU 279 CD1 PHE B 104 14969 18384 12554 1299 -644 694 C ATOM 280 CE1 PHE B 104 172.744 243.290 820.717 1.00118.51 C ANISOU 280 CE1 PHE B 104 14690 17797 12543 1103 -755 327 C ATOM 281 CZ PHE B 104 172.279 244.366 819.980 1.00116.27 C ANISOU 281 CZ PHE B 104 14536 17656 11986 859 -1081 2 C ATOM 282 CE2 PHE B 104 172.275 245.627 820.533 1.00116.27 C ANISOU 282 CE2 PHE B 104 14646 18034 11498 767 -1293 4 C ATOM 283 CD2 PHE B 104 172.737 245.817 821.817 1.00118.55 C ANISOU 283 CD2 PHE B 104 14906 18630 11506 929 -1219 305 C ATOM 284 N SER B 105 170.715 244.975 825.392 1.00124.64 N ANISOU 284 N SER B 105 16070 20250 11039 1412 -944 734 N ATOM 285 CA SER B 105 169.270 244.808 825.327 1.00124.15 C ANISOU 285 CA SER B 105 16270 20106 10796 1278 -983 445 C ATOM 286 C SER B 105 168.610 246.147 825.573 1.00124.35 C ANISOU 286 C SER B 105 16426 20478 10342 1016 -1287 61 C ATOM 287 O SER B 105 167.599 246.479 824.956 1.00122.82 O ANISOU 287 O SER B 105 16412 20079 10173 762 -1383 -285 O ATOM 288 CB SER B 105 168.798 243.805 826.373 1.00127.06 C ANISOU 288 CB SER B 105 16700 20613 10965 1591 -721 706 C ATOM 289 OG SER B 105 167.392 243.888 826.519 1.00127.20 O ANISOU 289 OG SER B 105 16977 20664 10691 1453 -787 384 O ATOM 290 N ALA B 106 169.203 246.915 826.481 1.00131.61 N ANISOU 290 N ALA B 106 17223 21923 10858 1093 -1411 132 N ATOM 291 CA ALA B 106 168.655 248.202 826.887 1.00132.73 C ANISOU 291 CA ALA B 106 17424 22453 10555 853 -1688 -263 C ATOM 292 C ALA B 106 168.923 249.298 825.855 1.00130.03 C ANISOU 292 C ALA B 106 17046 21917 10441 526 -1906 -501 C ATOM 293 O ALA B 106 168.096 250.183 825.637 1.00129.85 O ANISOU 293 O ALA B 106 17131 21889 10318 236 -2059 -899 O ATOM 294 CB ALA B 106 169.217 248.595 828.244 1.00136.68 C ANISOU 294 CB ALA B 106 17754 23662 10517 1083 -1751 -110 C ATOM 295 N TYR B 107 170.093 249.224 825.231 1.00144.80 N ANISOU 295 N TYR B 107 18749 23620 12649 591 -1884 -249 N ATOM 296 CA TYR B 107 170.511 250.186 824.216 1.00142.39 C ANISOU 296 CA TYR B 107 18383 23158 12561 346 -2065 -410 C ATOM 297 C TYR B 107 169.574 250.192 823.008 1.00139.80 C ANISOU 297 C TYR B 107 18221 22385 12510 125 -2074 -682 C ATOM 298 O TYR B 107 169.084 251.240 822.593 1.00139.26 O ANISOU 298 O TYR B 107 18208 22314 12390 -124 -2222 -954 O ATOM 299 CB TYR B 107 171.945 249.859 823.794 1.00141.46 C ANISOU 299 CB TYR B 107 18044 22916 12787 509 -1981 -88 C ATOM 300 CG TYR B 107 172.423 250.555 822.547 1.00138.81 C ANISOU 300 CG TYR B 107 17642 22355 12746 316 -2117 -232 C ATOM 301 CD1 TYR B 107 172.334 251.934 822.428 1.00138.61 C ANISOU 301 CD1 TYR B 107 17617 22533 12517 90 -2351 -444 C ATOM 302 CE1 TYR B 107 172.784 252.585 821.291 1.00136.48 C ANISOU 302 CE1 TYR B 107 17278 22090 12490 -41 -2453 -534 C ATOM 303 CZ TYR B 107 173.336 251.851 820.256 1.00134.68 C ANISOU 303 CZ TYR B 107 16967 21528 12678 49 -2349 -471 C ATOM 304 OH TYR B 107 173.779 252.501 819.127 1.00132.99 O ANISOU 304 OH TYR B 107 16669 21218 12645 -44 -2456 -580 O ATOM 305 CE2 TYR B 107 173.442 250.475 820.352 1.00134.98 C ANISOU 305 CE2 TYR B 107 16978 21350 12960 241 -2130 -321 C ATOM 306 CD2 TYR B 107 172.989 249.836 821.493 1.00136.96 C ANISOU 306 CD2 TYR B 107 17309 21727 13001 375 -2001 -173 C ATOM 307 N VAL B 108 169.343 249.004 822.457 1.00118.98 N ANISOU 307 N VAL B 108 15635 19386 10188 241 -1886 -580 N ATOM 308 CA VAL B 108 168.385 248.798 821.377 1.00117.05 C ANISOU 308 CA VAL B 108 15530 18773 10172 108 -1856 -779 C ATOM 309 C VAL B 108 167.110 249.589 821.624 1.00117.95 C ANISOU 309 C VAL B 108 15838 18949 10029 -103 -1918 -1074 C ATOM 310 O VAL B 108 166.839 250.579 820.956 1.00117.13 O ANISOU 310 O VAL B 108 15747 18783 9975 -302 -2022 -1257 O ATOM 311 CB VAL B 108 167.995 247.300 821.257 1.00116.91 C ANISOU 311 CB VAL B 108 15560 18469 10393 287 -1623 -648 C ATOM 312 CG1 VAL B 108 166.765 247.135 820.367 1.00115.63 C ANISOU 312 CG1 VAL B 108 15562 18018 10354 170 -1585 -849 C ATOM 313 CG2 VAL B 108 169.161 246.471 820.768 1.00116.22 C ANISOU 313 CG2 VAL B 108 15241 18197 10721 453 -1517 -438 C ATOM 314 N SER B 109 166.338 249.131 822.603 1.00118.96 N ANISOU 314 N SER B 109 16098 19191 9910 -41 -1819 -1118 N ATOM 315 CA SER B 109 165.068 249.740 822.954 1.00120.52 C ANISOU 315 CA SER B 109 16467 19418 9909 -236 -1825 -1453 C ATOM 316 C SER B 109 165.169 251.253 823.023 1.00121.36 C ANISOU 316 C SER B 109 16496 19722 9894 -485 -2017 -1705 C ATOM 317 O SER B 109 164.246 251.957 822.614 1.00121.64 O ANISOU 317 O SER B 109 16622 19566 10031 -709 -1992 -1975 O ATOM 318 CB SER B 109 164.588 249.173 824.286 1.00123.53 C ANISOU 318 CB SER B 109 16928 20080 9929 -93 -1738 -1476 C ATOM 319 OG SER B 109 165.684 248.625 825.000 1.00124.48 O ANISOU 319 OG SER B 109 16893 20497 9907 184 -1724 -1138 O ATOM 320 N GLY B 110 166.300 251.745 823.526 1.00121.27 N ANISOU 320 N GLY B 110 16295 20071 9710 -433 -2174 -1592 N ATOM 321 CA GLY B 110 166.527 253.172 823.682 1.00122.37 C ANISOU 321 CA GLY B 110 16317 20445 9733 -654 -2366 -1813 C ATOM 322 C GLY B 110 166.592 253.906 822.366 1.00119.95 C ANISOU 322 C GLY B 110 15990 19808 9777 -823 -2393 -1838 C ATOM 323 O GLY B 110 166.148 255.046 822.242 1.00120.96 O ANISOU 323 O GLY B 110 16096 19922 9943 -1064 -2447 -2096 O ATOM 324 N LEU B 111 167.169 253.243 821.379 1.00117.50 N ANISOU 324 N LEU B 111 15656 19251 9737 -676 -2338 -1576 N ATOM 325 CA LEU B 111 167.200 253.791 820.041 1.00115.45 C ANISOU 325 CA LEU B 111 15368 18733 9765 -760 -2346 -1573 C ATOM 326 C LEU B 111 165.808 253.667 819.451 1.00115.42 C ANISOU 326 C LEU B 111 15541 18398 9915 -840 -2175 -1713 C ATOM 327 O LEU B 111 165.326 254.579 818.779 1.00115.52 O ANISOU 327 O LEU B 111 15556 18263 10073 -980 -2139 -1808 O ATOM 328 CB LEU B 111 168.198 253.033 819.171 1.00113.10 C ANISOU 328 CB LEU B 111 14957 18327 9691 -562 -2340 -1328 C ATOM 329 CG LEU B 111 169.651 253.049 819.632 1.00113.20 C ANISOU 329 CG LEU B 111 14776 18586 9650 -449 -2439 -1141 C ATOM 330 CD1 LEU B 111 170.510 252.305 818.616 1.00111.28 C ANISOU 330 CD1 LEU B 111 14401 18153 9729 -290 -2394 -1000 C ATOM 331 CD2 LEU B 111 170.133 254.483 819.812 1.00113.92 C ANISOU 331 CD2 LEU B 111 14757 18921 9606 -605 -2611 -1210 C ATOM 332 N PHE B 112 165.165 252.530 819.713 1.00116.31 N ANISOU 332 N PHE B 112 15790 18384 10018 -728 -2033 -1687 N ATOM 333 CA PHE B 112 163.881 252.219 819.094 1.00116.22 C ANISOU 333 CA PHE B 112 15941 18041 10178 -752 -1836 -1758 C ATOM 334 C PHE B 112 162.827 253.215 819.540 1.00118.69 C ANISOU 334 C PHE B 112 16342 18297 10460 -994 -1761 -2053 C ATOM 335 O PHE B 112 161.854 253.456 818.828 1.00118.93 O ANISOU 335 O PHE B 112 16455 18022 10713 -1054 -1574 -2097 O ATOM 336 CB PHE B 112 163.452 250.783 819.405 1.00116.13 C ANISOU 336 CB PHE B 112 16044 17923 10157 -579 -1697 -1666 C ATOM 337 CG PHE B 112 162.091 250.445 818.898 1.00116.38 C ANISOU 337 CG PHE B 112 16244 17635 10341 -594 -1479 -1728 C ATOM 338 CD1 PHE B 112 161.762 250.665 817.586 1.00115.17 C ANISOU 338 CD1 PHE B 112 16063 17269 10428 -570 -1403 -1649 C ATOM 339 CE1 PHE B 112 160.503 250.364 817.121 1.00115.75 C ANISOU 339 CE1 PHE B 112 16271 17063 10645 -547 -1168 -1653 C ATOM 340 CZ PHE B 112 159.550 249.832 817.966 1.00117.38 C ANISOU 340 CZ PHE B 112 16661 17161 10779 -577 -1008 -1772 C ATOM 341 CE2 PHE B 112 159.863 249.607 819.285 1.00118.63 C ANISOU 341 CE2 PHE B 112 16854 17547 10672 -606 -1098 -1889 C ATOM 342 CD2 PHE B 112 161.130 249.914 819.746 1.00118.20 C ANISOU 342 CD2 PHE B 112 16647 17811 10453 -600 -1331 -1849 C ATOM 343 N GLU B 113 163.045 253.794 820.720 1.00119.81 N ANISOU 343 N GLU B 113 16431 18750 10343 -1119 -1888 -2262 N ATOM 344 CA GLU B 113 162.196 254.862 821.237 1.00122.87 C ANISOU 344 CA GLU B 113 16826 19128 10732 -1390 -1843 -2646 C ATOM 345 C GLU B 113 162.471 256.157 820.477 1.00122.64 C ANISOU 345 C GLU B 113 16658 18998 10943 -1551 -1875 -2657 C ATOM 346 O GLU B 113 161.562 256.915 820.178 1.00124.36 O ANISOU 346 O GLU B 113 16894 18937 11421 -1736 -1694 -2848 O ATOM 347 CB GLU B 113 162.415 255.052 822.745 1.00125.91 C ANISOU 347 CB GLU B 113 17138 19987 10716 -1444 -2003 -2907 C ATOM 348 N ILE B 114 163.731 256.417 820.165 1.00121.30 N ANISOU 348 N ILE B 114 16336 19033 10719 -1468 -2068 -2437 N ATOM 349 CA ILE B 114 164.055 257.560 819.331 1.00120.88 C ANISOU 349 CA ILE B 114 16152 18885 10890 -1567 -2081 -2382 C ATOM 350 C ILE B 114 163.388 257.333 817.994 1.00119.46 C ANISOU 350 C ILE B 114 16059 18316 11014 -1460 -1850 -2191 C ATOM 351 O ILE B 114 162.782 258.234 817.427 1.00120.71 O ANISOU 351 O ILE B 114 16187 18238 11439 -1570 -1675 -2225 O ATOM 352 CB ILE B 114 165.571 257.701 819.130 1.00118.94 C ANISOU 352 CB ILE B 114 15741 18918 10534 -1447 -2310 -2145 C ATOM 353 CG1 ILE B 114 166.307 257.565 820.466 1.00120.27 C ANISOU 353 CG1 ILE B 114 15823 19523 10351 -1437 -2509 -2213 C ATOM 354 CD1 ILE B 114 167.813 257.690 820.334 1.00118.74 C ANISOU 354 CD1 ILE B 114 15455 19575 10084 -1305 -2686 -1955 C ATOM 355 CG2 ILE B 114 165.904 259.032 818.493 1.00119.18 C ANISOU 355 CG2 ILE B 114 15621 18913 10747 -1567 -2333 -2127 C ATOM 356 N TYR B 115 163.492 256.104 817.509 1.00117.00 N ANISOU 356 N TYR B 115 15827 17953 10674 -1225 -1826 -1980 N ATOM 357 CA TYR B 115 162.833 255.704 816.277 1.00115.98 C ANISOU 357 CA TYR B 115 15756 17546 10764 -1069 -1621 -1797 C ATOM 358 C TYR B 115 161.330 255.952 816.353 1.00118.32 C ANISOU 358 C TYR B 115 16189 17515 11252 -1190 -1322 -1938 C ATOM 359 O TYR B 115 160.765 256.626 815.497 1.00119.16 O ANISOU 359 O TYR B 115 16264 17399 11613 -1180 -1109 -1834 O ATOM 360 CB TYR B 115 163.120 254.228 815.948 1.00113.88 C ANISOU 360 CB TYR B 115 15524 17304 10440 -825 -1653 -1633 C ATOM 361 CG TYR B 115 162.573 253.740 814.610 1.00112.99 C ANISOU 361 CG TYR B 115 15412 17020 10500 -618 -1490 -1448 C ATOM 362 CD1 TYR B 115 162.801 254.449 813.442 1.00112.70 C ANISOU 362 CD1 TYR B 115 15240 17020 10560 -515 -1470 -1296 C ATOM 363 CE1 TYR B 115 162.309 254.011 812.233 1.00112.46 C ANISOU 363 CE1 TYR B 115 15170 16940 10618 -273 -1327 -1115 C ATOM 364 CZ TYR B 115 161.597 252.841 812.171 1.00112.30 C ANISOU 364 CZ TYR B 115 15246 16800 10624 -159 -1212 -1094 C ATOM 365 OH TYR B 115 161.120 252.414 810.956 1.00112.42 O ANISOU 365 OH TYR B 115 15183 16836 10696 107 -1083 -912 O ATOM 366 CE2 TYR B 115 161.358 252.111 813.310 1.00112.35 C ANISOU 366 CE2 TYR B 115 15403 16710 10576 -279 -1218 -1239 C ATOM 367 CD2 TYR B 115 161.847 252.561 814.522 1.00112.78 C ANISOU 367 CD2 TYR B 115 15496 16846 10508 -493 -1353 -1409 C ATOM 368 N ARG B 116 160.678 255.407 817.371 1.00123.12 N ANISOU 368 N ARG B 116 16935 18092 11752 -1278 -1270 -2158 N ATOM 369 CA ARG B 116 159.228 255.495 817.449 1.00125.52 C ANISOU 369 CA ARG B 116 17373 18049 12269 -1381 -953 -2316 C ATOM 370 C ARG B 116 158.749 256.908 817.720 1.00128.69 C ANISOU 370 C ARG B 116 17690 18302 12904 -1664 -823 -2588 C ATOM 371 O ARG B 116 157.565 257.197 817.596 1.00131.13 O ANISOU 371 O ARG B 116 18064 18242 13518 -1761 -490 -2705 O ATOM 372 CB ARG B 116 158.699 254.560 818.525 1.00126.54 C ANISOU 372 CB ARG B 116 17661 18223 12197 -1393 -937 -2520 C ATOM 373 N ASP B 117 159.671 257.788 818.081 1.00169.31 N ANISOU 373 N ASP B 117 22667 23712 17950 -1797 -1059 -2690 N ATOM 374 CA ASP B 117 159.317 259.162 818.429 1.00172.71 C ANISOU 374 CA ASP B 117 22963 24027 18630 -2095 -960 -3000 C ATOM 375 C ASP B 117 159.323 260.075 817.209 1.00172.62 C ANISOU 375 C ASP B 117 22835 23758 18993 -2049 -759 -2714 C ATOM 376 O ASP B 117 158.844 261.209 817.278 1.00175.79 O ANISOU 376 O ASP B 117 23116 23925 19752 -2276 -557 -2909 O ATOM 377 CB ASP B 117 160.266 259.725 819.502 1.00173.66 C ANISOU 377 CB ASP B 117 22924 24605 18454 -2261 -1308 -3270 C ATOM 378 CG ASP B 117 159.920 259.250 820.913 1.00176.02 C ANISOU 378 CG ASP B 117 23278 25169 18434 -2364 -1416 -3684 C ATOM 379 OD1 ASP B 117 158.848 258.640 821.099 1.00177.29 O ANISOU 379 OD1 ASP B 117 23603 25093 18665 -2366 -1194 -3831 O ATOM 380 OD2 ASP B 117 160.723 259.496 821.839 1.00176.92 O ANISOU 380 OD2 ASP B 117 23254 25762 18204 -2416 -1712 -3851 O ATOM 381 N LEU B 118 159.858 259.577 816.096 1.00153.23 N ANISOU 381 N LEU B 118 20389 21361 16470 -1742 -797 -2267 N ATOM 382 CA LEU B 118 160.072 260.397 814.900 1.00153.09 C ANISOU 382 CA LEU B 118 20234 21239 16695 -1613 -651 -1939 C ATOM 383 C LEU B 118 159.004 260.269 813.802 1.00154.07 C ANISOU 383 C LEU B 118 20408 21003 17126 -1401 -224 -1633 C ATOM 384 O LEU B 118 159.103 260.938 812.770 1.00154.48 O ANISOU 384 O LEU B 118 20333 21002 17360 -1229 -55 -1306 O ATOM 385 CB LEU B 118 161.434 260.087 814.285 1.00149.67 C ANISOU 385 CB LEU B 118 19715 21179 15972 -1379 -965 -1665 C ATOM 386 CG LEU B 118 162.683 260.572 815.001 1.00148.96 C ANISOU 386 CG LEU B 118 19499 21434 15663 -1519 -1319 -1804 C ATOM 387 CD1 LEU B 118 163.885 259.908 814.375 1.00145.65 C ANISOU 387 CD1 LEU B 118 19028 21312 14999 -1254 -1566 -1553 C ATOM 388 CD2 LEU B 118 162.792 262.086 814.935 1.00151.20 C ANISOU 388 CD2 LEU B 118 19605 21643 16200 -1700 -1236 -1847 C ATOM 389 N GLY B 119 157.993 259.428 814.019 1.00154.33 N ANISOU 389 N GLY B 119 20612 20819 17206 -1378 -31 -1706 N ATOM 390 CA GLY B 119 156.965 259.156 813.018 1.00155.35 C ANISOU 390 CA GLY B 119 20788 20646 17592 -1132 382 -1377 C ATOM 391 C GLY B 119 156.608 260.328 812.119 1.00157.91 C ANISOU 391 C GLY B 119 20952 20723 18323 -1048 759 -1087 C ATOM 392 O GLY B 119 156.292 260.152 810.944 1.00157.98 O ANISOU 392 O GLY B 119 20917 20711 18395 -689 998 -635 O ATOM 393 N ASP B 120 156.648 261.530 812.681 1.00169.90 N ANISOU 393 N ASP B 120 22353 22077 20123 -1358 830 -1338 N ATOM 394 CA ASP B 120 156.422 262.749 811.913 1.00172.68 C ANISOU 394 CA ASP B 120 22518 22174 20920 -1295 1206 -1056 C ATOM 395 C ASP B 120 157.321 262.814 810.673 1.00170.39 C ANISOU 395 C ASP B 120 22109 22248 20385 -893 1081 -543 C ATOM 396 O ASP B 120 158.554 262.809 810.769 1.00167.63 O ANISOU 396 O ASP B 120 21705 22314 19675 -897 638 -597 O ATOM 397 CB ASP B 120 156.639 263.982 812.794 1.00175.34 C ANISOU 397 CB ASP B 120 22701 22381 21540 -1718 1180 -1469 C ATOM 398 N LYS B 138 162.282 272.691 807.492 1.00161.02 N ANISOU 398 N LYS B 138 19104 21288 20789 -609 1793 1221 N ATOM 399 CA LYS B 138 162.789 273.472 808.614 1.00161.72 C ANISOU 399 CA LYS B 138 19069 21298 21081 -1127 1553 731 C ATOM 400 C LYS B 138 162.498 272.778 809.945 1.00160.65 C ANISOU 400 C LYS B 138 19087 21127 20826 -1586 1227 44 C ATOM 401 O LYS B 138 163.418 272.447 810.695 1.00157.70 O ANISOU 401 O LYS B 138 18763 21157 20000 -1773 677 -292 O ATOM 402 CB LYS B 138 162.182 274.875 808.603 1.00167.33 C ANISOU 402 CB LYS B 138 19501 21443 22632 -1295 2127 827 C ATOM 403 N GLU B 139 161.216 272.563 810.231 1.00165.01 N ANISOU 403 N GLU B 139 19702 21209 21786 -1735 1598 -137 N ATOM 404 CA GLU B 139 160.796 271.831 811.425 1.00164.47 C ANISOU 404 CA GLU B 139 19788 21121 21583 -2108 1344 -767 C ATOM 405 C GLU B 139 161.408 270.435 811.437 1.00159.15 C ANISOU 405 C GLU B 139 19374 20962 20135 -1903 840 -758 C ATOM 406 O GLU B 139 161.812 269.932 812.485 1.00157.42 O ANISOU 406 O GLU B 139 19237 21008 19568 -2160 405 -1215 O ATOM 407 CB GLU B 139 159.268 271.728 811.494 1.00168.31 C ANISOU 407 CB GLU B 139 20316 21003 22632 -2204 1895 -874 C ATOM 408 N HIS B 140 161.470 269.811 810.267 1.00197.64 N ANISOU 408 N HIS B 140 24344 25996 24755 -1419 923 -235 N ATOM 409 CA HIS B 140 162.085 268.498 810.144 1.00193.02 C ANISOU 409 CA HIS B 140 23952 25870 23516 -1206 488 -220 C ATOM 410 C HIS B 140 163.574 268.600 810.464 1.00190.10 C ANISOU 410 C HIS B 140 23520 25977 22731 -1261 -33 -328 C ATOM 411 O HIS B 140 164.129 267.762 811.170 1.00187.33 O ANISOU 411 O HIS B 140 23286 25908 21981 -1367 -447 -607 O ATOM 412 CB HIS B 140 161.859 267.936 808.739 1.00192.21 C ANISOU 412 CB HIS B 140 23886 25889 23256 -664 697 328 C ATOM 413 CG HIS B 140 162.458 266.581 808.524 1.00188.03 C ANISOU 413 CG HIS B 140 23503 25805 22136 -448 284 303 C ATOM 414 ND1 HIS B 140 161.870 265.425 808.995 1.00186.79 N ANISOU 414 ND1 HIS B 140 23544 25583 21847 -518 209 78 N ATOM 415 CE1 HIS B 140 162.616 264.390 808.656 1.00183.41 C ANISOU 415 CE1 HIS B 140 23170 25567 20951 -299 -143 99 C ATOM 416 NE2 HIS B 140 163.664 264.828 807.983 1.00182.47 N ANISOU 416 NE2 HIS B 140 22898 25786 20646 -95 -306 296 N ATOM 417 CD2 HIS B 140 163.585 266.198 807.885 1.00185.20 C ANISOU 417 CD2 HIS B 140 23096 25936 21336 -170 -48 450 C ATOM 418 N ASN B 141 164.213 269.642 809.946 1.00178.07 N ANISOU 418 N ASN B 141 21800 24527 21332 -1169 30 -72 N ATOM 419 CA ASN B 141 165.616 269.888 810.246 1.00175.83 C ANISOU 419 CA ASN B 141 21430 24652 20725 -1226 -408 -152 C ATOM 420 C ASN B 141 165.881 269.792 811.729 1.00175.57 C ANISOU 420 C ASN B 141 21417 24704 20589 -1661 -746 -685 C ATOM 421 O ASN B 141 166.434 268.811 812.218 1.00172.66 O ANISOU 421 O ASN B 141 21177 24638 19789 -1655 -1111 -848 O ATOM 422 CB ASN B 141 166.028 271.277 809.766 1.00178.09 C ANISOU 422 CB ASN B 141 21474 24882 21310 -1184 -214 114 C ATOM 423 CG ASN B 141 166.672 271.253 808.401 1.00176.76 C ANISOU 423 CG ASN B 141 21256 25015 20889 -674 -180 626 C ATOM 424 OD1 ASN B 141 166.931 270.190 807.838 1.00174.05 O ANISOU 424 OD1 ASN B 141 21036 24971 20126 -377 -357 717 O ATOM 425 ND2 ASN B 141 166.939 272.431 807.859 1.00179.02 N ANISOU 425 ND2 ASN B 141 21336 25248 21435 -562 55 938 N ATOM 426 N ALA B 142 165.474 270.838 812.433 1.00176.80 N ANISOU 426 N ALA B 142 21408 24604 21162 -2018 -595 -954 N ATOM 427 CA ALA B 142 165.702 270.954 813.858 1.00177.66 C ANISOU 427 CA ALA B 142 21459 24873 21171 -2421 -904 -1490 C ATOM 428 C ALA B 142 165.414 269.651 814.587 1.00175.86 C ANISOU 428 C ALA B 142 21458 24790 20569 -2459 -1125 -1770 C ATOM 429 O ALA B 142 166.254 269.168 815.348 1.00173.95 O ANISOU 429 O ALA B 142 21239 24962 19892 -2502 -1531 -1932 O ATOM 430 CB ALA B 142 164.861 272.085 814.432 1.00182.82 C ANISOU 430 CB ALA B 142 21901 25136 22428 -2806 -606 -1839 C ATOM 431 N THR B 143 164.234 269.082 814.357 1.00157.41 N ANISOU 431 N THR B 143 19279 22113 18416 -2417 -826 -1788 N ATOM 432 CA THR B 143 163.852 267.863 815.062 1.00156.09 C ANISOU 432 CA THR B 143 19326 22047 17935 -2451 -989 -2049 C ATOM 433 C THR B 143 164.821 266.713 814.780 1.00151.49 C ANISOU 433 C THR B 143 18884 21859 16815 -2151 -1326 -1807 C ATOM 434 O THR B 143 165.153 265.950 815.690 1.00150.31 O ANISOU 434 O THR B 143 18817 21980 16314 -2216 -1613 -2033 O ATOM 435 CB THR B 143 162.401 267.436 814.767 1.00157.84 C ANISOU 435 CB THR B 143 19692 21807 18471 -2428 -572 -2064 C ATOM 436 OG1 THR B 143 162.229 267.233 813.360 1.00156.55 O ANISOU 436 OG1 THR B 143 19580 21503 18398 -2040 -307 -1519 O ATOM 437 CG2 THR B 143 161.432 268.499 815.247 1.00163.03 C ANISOU 437 CG2 THR B 143 20186 22033 19724 -2781 -221 -2418 C ATOM 438 N VAL B 144 165.288 266.595 813.536 1.00139.82 N ANISOU 438 N VAL B 144 17406 20431 15290 -1810 -1272 -1362 N ATOM 439 CA VAL B 144 166.252 265.547 813.203 1.00136.01 C ANISOU 439 CA VAL B 144 17002 20294 14381 -1544 -1567 -1196 C ATOM 440 C VAL B 144 167.542 265.740 813.985 1.00134.92 C ANISOU 440 C VAL B 144 16759 20526 13980 -1654 -1941 -1316 C ATOM 441 O VAL B 144 167.937 264.865 814.749 1.00133.54 O ANISOU 441 O VAL B 144 16662 20560 13518 -1672 -2174 -1459 O ATOM 442 CB VAL B 144 166.565 265.465 811.701 1.00134.62 C ANISOU 442 CB VAL B 144 16787 20182 14181 -1151 -1460 -774 C ATOM 443 CG1 VAL B 144 167.815 264.640 811.478 1.00131.38 C ANISOU 443 CG1 VAL B 144 16371 20149 13400 -952 -1796 -717 C ATOM 444 CG2 VAL B 144 165.398 264.844 810.957 1.00135.19 C ANISOU 444 CG2 VAL B 144 16977 20015 14373 -947 -1148 -616 C ATOM 445 N ASN B 145 168.192 266.887 813.811 1.00124.19 N ANISOU 445 N ASN B 145 15208 19246 12733 -1705 -1966 -1222 N ATOM 446 CA ASN B 145 169.440 267.166 814.528 1.00123.49 C ANISOU 446 CA ASN B 145 14991 19518 12411 -1791 -2294 -1292 C ATOM 447 C ASN B 145 169.316 266.854 816.018 1.00124.67 C ANISOU 447 C ASN B 145 15158 19836 12375 -2040 -2484 -1663 C ATOM 448 O ASN B 145 170.281 266.484 816.688 1.00123.59 O ANISOU 448 O ASN B 145 14979 20050 11930 -2006 -2756 -1673 O ATOM 449 CB ASN B 145 169.856 268.627 814.352 1.00125.38 C ANISOU 449 CB ASN B 145 15003 19757 12879 -1896 -2243 -1213 C ATOM 450 CG ASN B 145 169.996 269.024 812.901 1.00124.79 C ANISOU 450 CG ASN B 145 14886 19578 12951 -1604 -2033 -814 C ATOM 451 OD1 ASN B 145 169.817 270.194 812.555 1.00127.10 O ANISOU 451 OD1 ASN B 145 15023 19708 13562 -1659 -1823 -700 O ATOM 452 ND2 ASN B 145 170.310 268.051 812.040 1.00122.13 N ANISOU 452 ND2 ASN B 145 14658 19355 12388 -1273 -2075 -610 N ATOM 453 N LEU B 146 168.108 267.013 816.535 1.00180.89 N ANISOU 453 N LEU B 146 22320 26722 19689 -2266 -2312 -1964 N ATOM 454 CA LEU B 146 167.854 266.694 817.925 1.00182.63 C ANISOU 454 CA LEU B 146 22545 27153 19692 -2471 -2477 -2360 C ATOM 455 C LEU B 146 167.939 265.179 818.146 1.00180.11 C ANISOU 455 C LEU B 146 22439 26962 19035 -2262 -2581 -2285 C ATOM 456 O LEU B 146 168.620 264.711 819.055 1.00179.87 O ANISOU 456 O LEU B 146 22379 27310 18654 -2229 -2822 -2341 O ATOM 457 CB LEU B 146 166.492 267.227 818.352 1.00186.55 C ANISOU 457 CB LEU B 146 23019 27336 20526 -2765 -2233 -2761 C ATOM 458 CG LEU B 146 165.958 266.554 819.614 1.00188.27 C ANISOU 458 CG LEU B 146 23309 27752 20475 -2898 -2351 -3183 C ATOM 459 CD1 LEU B 146 166.769 266.963 820.841 1.00190.15 C ANISOU 459 CD1 LEU B 146 23328 28554 20365 -3026 -2695 -3443 C ATOM 460 CD2 LEU B 146 164.477 266.847 819.794 1.00191.90 C ANISOU 460 CD2 LEU B 146 23791 27796 21324 -3144 -2035 -3571 C ATOM 461 N ALA B 147 167.249 264.417 817.301 1.00142.32 N ANISOU 461 N ALA B 147 17841 21866 14369 -2098 -2372 -2127 N ATOM 462 CA ALA B 147 167.252 262.957 817.398 1.00140.11 C ANISOU 462 CA ALA B 147 17744 21644 13846 -1900 -2428 -2049 C ATOM 463 C ALA B 147 168.659 262.416 817.259 1.00137.43 C ANISOU 463 C ALA B 147 17347 21598 13272 -1682 -2653 -1800 C ATOM 464 O ALA B 147 168.977 261.341 817.760 1.00136.36 O ANISOU 464 O ALA B 147 17284 21605 12922 -1560 -2746 -1772 O ATOM 465 CB ALA B 147 166.358 262.337 816.341 1.00139.04 C ANISOU 465 CB ALA B 147 17769 21154 13906 -1738 -2166 -1889 C ATOM 466 N MET B 148 169.505 263.165 816.572 1.00134.71 N ANISOU 466 N MET B 148 16858 21321 13007 -1621 -2706 -1611 N ATOM 467 CA MET B 148 170.894 262.772 816.454 1.00132.67 C ANISOU 467 CA MET B 148 16512 21314 12582 -1434 -2891 -1410 C ATOM 468 C MET B 148 171.536 262.867 817.828 1.00133.99 C ANISOU 468 C MET B 148 16581 21828 12502 -1531 -3088 -1510 C ATOM 469 O MET B 148 172.318 262.005 818.214 1.00132.94 O ANISOU 469 O MET B 148 16441 21871 12201 -1368 -3177 -1385 O ATOM 470 CB MET B 148 171.649 263.659 815.471 1.00132.00 C ANISOU 470 CB MET B 148 16282 21253 12621 -1350 -2896 -1212 C ATOM 471 CG MET B 148 173.094 263.297 815.386 1.00130.32 C ANISOU 471 CG MET B 148 15962 21273 12280 -1176 -3061 -1050 C ATOM 472 SD MET B 148 173.261 261.611 814.842 1.00128.04 S ANISOU 472 SD MET B 148 15777 20899 11972 -917 -3029 -992 S ATOM 473 CE MET B 148 173.458 261.890 813.075 1.00126.97 C ANISOU 473 CE MET B 148 15568 20706 11968 -694 -2949 -860 C ATOM 474 N GLU B 149 171.223 263.933 818.558 1.00147.05 N ANISOU 474 N GLU B 149 18121 23598 14154 -1779 -3134 -1731 N ATOM 475 CA GLU B 149 171.660 264.046 819.938 1.00149.14 C ANISOU 475 CA GLU B 149 18261 24286 14120 -1854 -3326 -1870 C ATOM 476 C GLU B 149 171.291 262.740 820.624 1.00149.05 C ANISOU 476 C GLU B 149 18403 24347 13880 -1733 -3312 -1910 C ATOM 477 O GLU B 149 172.150 262.007 821.121 1.00148.44 O ANISOU 477 O GLU B 149 18292 24527 13581 -1529 -3396 -1708 O ATOM 478 CB GLU B 149 170.943 265.206 820.631 1.00152.90 C ANISOU 478 CB GLU B 149 18599 24838 14658 -2175 -3344 -2255 C ATOM 479 CG GLU B 149 170.954 266.522 819.851 1.00153.51 C ANISOU 479 CG GLU B 149 18537 24701 15088 -2323 -3258 -2235 C ATOM 480 CD GLU B 149 171.996 267.511 820.357 1.00154.94 C ANISOU 480 CD GLU B 149 18440 25262 15166 -2395 -3463 -2215 C ATOM 481 OE1 GLU B 149 171.870 267.987 821.513 1.00158.34 O ANISOU 481 OE1 GLU B 149 18695 26038 15430 -2583 -3608 -2546 O ATOM 482 OE2 GLU B 149 172.928 267.833 819.587 1.00152.95 O ANISOU 482 OE2 GLU B 149 18128 24994 14994 -2254 -3477 -1889 O ATOM 483 N ALA B 150 169.992 262.454 820.610 1.00134.31 N ANISOU 483 N ALA B 150 16700 22221 12112 -1841 -3162 -2140 N ATOM 484 CA ALA B 150 169.429 261.259 821.229 1.00134.53 C ANISOU 484 CA ALA B 150 16891 22276 11949 -1739 -3112 -2204 C ATOM 485 C ALA B 150 170.273 260.044 820.928 1.00131.76 C ANISOU 485 C ALA B 150 16598 21930 11537 -1434 -3108 -1845 C ATOM 486 O ALA B 150 170.814 259.408 821.819 1.00132.50 O ANISOU 486 O ALA B 150 16648 22327 11368 -1281 -3174 -1740 O ATOM 487 CB ALA B 150 168.003 261.030 820.738 1.00134.74 C ANISOU 487 CB ALA B 150 17111 21872 12212 -1842 -2885 -2385 C ATOM 488 N ILE B 151 170.388 259.731 819.652 1.00118.73 N ANISOU 488 N ILE B 151 15011 19954 10148 -1329 -3009 -1661 N ATOM 489 CA ILE B 151 171.160 258.575 819.221 1.00116.45 C ANISOU 489 CA ILE B 151 14734 19610 9902 -1069 -2981 -1400 C ATOM 490 C ILE B 151 172.599 258.628 819.732 1.00116.58 C ANISOU 490 C ILE B 151 14562 19932 9799 -944 -3101 -1194 C ATOM 491 O ILE B 151 173.119 257.629 820.233 1.00116.57 O ANISOU 491 O ILE B 151 14544 20011 9736 -752 -3057 -1025 O ATOM 492 CB ILE B 151 171.163 258.450 817.688 1.00114.13 C ANISOU 492 CB ILE B 151 14461 19021 9881 -979 -2896 -1305 C ATOM 493 CG1 ILE B 151 169.739 258.229 817.197 1.00114.24 C ANISOU 493 CG1 ILE B 151 14652 18743 10012 -1035 -2729 -1428 C ATOM 494 CD1 ILE B 151 169.670 257.677 815.820 1.00112.35 C ANISOU 494 CD1 ILE B 151 14426 18306 9957 -855 -2637 -1313 C ATOM 495 CG2 ILE B 151 172.115 257.356 817.243 1.00112.36 C ANISOU 495 CG2 ILE B 151 14173 18766 9752 -742 -2885 -1126 C ATOM 496 N LEU B 152 173.233 259.794 819.606 1.00114.45 N ANISOU 496 N LEU B 152 14138 19815 9532 -1037 -3216 -1177 N ATOM 497 CA LEU B 152 174.640 259.925 819.943 1.00114.56 C ANISOU 497 CA LEU B 152 13960 20091 9477 -904 -3303 -947 C ATOM 498 C LEU B 152 174.798 259.622 821.385 1.00116.99 C ANISOU 498 C LEU B 152 14208 20775 9469 -833 -3347 -903 C ATOM 499 O LEU B 152 175.647 258.833 821.779 1.00117.09 O ANISOU 499 O LEU B 152 14146 20892 9452 -597 -3283 -635 O ATOM 500 CB LEU B 152 175.151 261.327 819.672 1.00114.99 C ANISOU 500 CB LEU B 152 13859 20271 9562 -1035 -3418 -955 C ATOM 501 CG LEU B 152 175.785 261.459 818.293 1.00112.68 C ANISOU 501 CG LEU B 152 13528 19754 9530 -940 -3375 -824 C ATOM 502 CD1 LEU B 152 176.530 262.770 818.187 1.00113.33 C ANISOU 502 CD1 LEU B 152 13429 20013 9617 -1016 -3479 -758 C ATOM 503 CD2 LEU B 152 176.731 260.304 818.066 1.00111.36 C ANISOU 503 CD2 LEU B 152 13321 19522 9468 -693 -3304 -636 C ATOM 504 N ASN B 153 173.968 260.283 822.173 1.00129.21 N ANISOU 504 N ASN B 153 15758 22541 10794 -1024 -3436 -1178 N ATOM 505 CA ASN B 153 173.929 260.059 823.604 1.00132.31 C ANISOU 505 CA ASN B 153 16076 23405 10792 -944 -3500 -1209 C ATOM 506 C ASN B 153 173.774 258.556 823.927 1.00131.96 C ANISOU 506 C ASN B 153 16164 23284 10692 -689 -3335 -1027 C ATOM 507 O ASN B 153 174.636 257.942 824.562 1.00132.91 O ANISOU 507 O ASN B 153 16172 23652 10675 -414 -3281 -702 O ATOM 508 CB ASN B 153 172.796 260.900 824.216 1.00135.22 C ANISOU 508 CB ASN B 153 16440 23941 10997 -1227 -3597 -1675 C ATOM 509 CG ASN B 153 172.412 260.435 825.587 1.00138.64 C ANISOU 509 CG ASN B 153 16841 24845 10991 -1125 -3640 -1806 C ATOM 510 OD1 ASN B 153 173.145 260.660 826.542 1.00141.20 O ANISOU 510 OD1 ASN B 153 16949 25738 10964 -981 -3765 -1694 O ATOM 511 ND2 ASN B 153 171.250 259.795 825.700 1.00139.03 N ANISOU 511 ND2 ASN B 153 17093 24702 11031 -1171 -3528 -2033 N ATOM 512 N GLU B 154 172.677 257.971 823.459 1.00129.35 N ANISOU 512 N GLU B 154 16055 22584 10506 -765 -3221 -1201 N ATOM 513 CA GLU B 154 172.359 256.576 823.724 1.00129.14 C ANISOU 513 CA GLU B 154 16162 22443 10463 -554 -3051 -1065 C ATOM 514 C GLU B 154 173.543 255.664 823.502 1.00127.86 C ANISOU 514 C GLU B 154 15905 22189 10489 -266 -2922 -649 C ATOM 515 O GLU B 154 173.625 254.606 824.105 1.00128.87 O ANISOU 515 O GLU B 154 16045 22368 10552 -28 -2769 -439 O ATOM 516 CB GLU B 154 171.199 256.111 822.839 1.00127.26 C ANISOU 516 CB GLU B 154 16156 21718 10480 -670 -2928 -1250 C ATOM 517 CG GLU B 154 169.882 256.814 823.131 1.00129.10 C ANISOU 517 CG GLU B 154 16492 21954 10606 -934 -2960 -1662 C ATOM 518 CD GLU B 154 169.151 256.246 824.328 1.00131.94 C ANISOU 518 CD GLU B 154 16926 22576 10629 -870 -2922 -1812 C ATOM 519 OE1 GLU B 154 169.580 255.192 824.852 1.00132.20 O ANISOU 519 OE1 GLU B 154 16960 22748 10524 -587 -2839 -1533 O ATOM 520 OE2 GLU B 154 168.142 256.859 824.737 1.00134.25 O ANISOU 520 OE2 GLU B 154 17260 22927 10823 -1094 -2949 -2217 O ATOM 521 N LEU B 155 174.455 256.058 822.628 1.00122.50 N ANISOU 521 N LEU B 155 15115 21351 10078 -279 -2951 -535 N ATOM 522 CA LEU B 155 175.618 255.224 822.341 1.00121.66 C ANISOU 522 CA LEU B 155 14883 21094 10247 -34 -2795 -204 C ATOM 523 C LEU B 155 176.769 255.544 823.280 1.00123.93 C ANISOU 523 C LEU B 155 14945 21794 10349 148 -2802 101 C ATOM 524 O LEU B 155 177.544 254.666 823.656 1.00124.90 O ANISOU 524 O LEU B 155 14956 21901 10600 425 -2594 443 O ATOM 525 CB LEU B 155 176.074 255.403 820.890 1.00118.91 C ANISOU 525 CB LEU B 155 14502 20392 10288 -106 -2803 -269 C ATOM 526 CG LEU B 155 177.389 254.699 820.550 1.00118.57 C ANISOU 526 CG LEU B 155 14273 20185 10592 108 -2642 -19 C ATOM 527 CD1 LEU B 155 177.237 253.210 820.757 1.00118.99 C ANISOU 527 CD1 LEU B 155 14353 20002 10856 294 -2400 102 C ATOM 528 CD2 LEU B 155 177.837 254.982 819.127 1.00116.42 C ANISOU 528 CD2 LEU B 155 13938 19662 10635 41 -2684 -166 C ATOM 529 N GLU B 156 176.884 256.814 823.642 1.00132.88 N ANISOU 529 N GLU B 156 15985 23287 11215 3 -3014 -4 N ATOM 530 CA GLU B 156 177.929 257.225 824.556 1.00135.39 C ANISOU 530 CA GLU B 156 16064 24075 11304 185 -3041 288 C ATOM 531 C GLU B 156 177.721 256.469 825.847 1.00138.55 C ANISOU 531 C GLU B 156 16436 24852 11354 449 -2935 480 C ATOM 532 O GLU B 156 178.669 255.970 826.449 1.00140.40 O ANISOU 532 O GLU B 156 16498 25280 11569 778 -2759 918 O ATOM 533 CB GLU B 156 177.866 258.728 824.813 1.00136.61 C ANISOU 533 CB GLU B 156 16111 24600 11196 -45 -3311 66 C ATOM 534 CG GLU B 156 177.860 259.566 823.549 1.00133.87 C ANISOU 534 CG GLU B 156 15806 23898 11161 -302 -3400 -130 C ATOM 535 CD GLU B 156 178.290 260.980 823.799 1.00135.30 C ANISOU 535 CD GLU B 156 15795 24423 11188 -446 -3599 -191 C ATOM 536 OE1 GLU B 156 177.515 261.905 823.468 1.00135.24 O ANISOU 536 OE1 GLU B 156 15833 24350 11203 -736 -3722 -527 O ATOM 537 OE2 GLU B 156 179.406 261.161 824.321 1.00136.72 O ANISOU 537 OE2 GLU B 156 15762 24923 11264 -257 -3600 118 O ATOM 538 N VAL B 157 176.453 256.369 826.235 1.00143.62 N ANISOU 538 N VAL B 157 17246 25583 11742 325 -3007 162 N ATOM 539 CA VAL B 157 176.042 255.753 827.487 1.00147.04 C ANISOU 539 CA VAL B 157 17667 26453 11749 566 -2938 257 C ATOM 540 C VAL B 157 176.304 254.241 827.512 1.00146.78 C ANISOU 540 C VAL B 157 17681 26133 11956 897 -2601 657 C ATOM 541 O VAL B 157 176.925 253.721 828.437 1.00149.75 O ANISOU 541 O VAL B 157 17897 26865 12137 1274 -2430 1082 O ATOM 542 CB VAL B 157 174.557 256.022 827.741 1.00147.92 C ANISOU 542 CB VAL B 157 17957 26640 11607 313 -3078 -261 C ATOM 543 CG1 VAL B 157 174.171 255.518 829.111 1.00152.12 C ANISOU 543 CG1 VAL B 157 18441 27751 11606 580 -3041 -213 C ATOM 544 CG2 VAL B 157 174.280 257.504 827.619 1.00148.43 C ANISOU 544 CG2 VAL B 157 17944 26875 11578 -44 -3354 -682 C ATOM 545 N PHE B 158 175.830 253.543 826.489 1.00127.47 N ANISOU 545 N PHE B 158 15427 23055 9952 775 -2485 536 N ATOM 546 CA PHE B 158 176.065 252.113 826.343 1.00127.11 C ANISOU 546 CA PHE B 158 15399 22639 10258 1036 -2155 854 C ATOM 547 C PHE B 158 177.561 251.788 826.365 1.00127.90 C ANISOU 547 C PHE B 158 15245 22680 10671 1311 -1930 1333 C ATOM 548 O PHE B 158 177.975 250.780 826.929 1.00129.99 O ANISOU 548 O PHE B 158 15411 22926 11053 1656 -1612 1746 O ATOM 549 CB PHE B 158 175.383 251.619 825.058 1.00123.52 C ANISOU 549 CB PHE B 158 15138 21549 10246 813 -2125 572 C ATOM 550 CG PHE B 158 175.788 250.236 824.628 1.00122.89 C ANISOU 550 CG PHE B 158 15013 21003 10675 1018 -1803 823 C ATOM 551 CD1 PHE B 158 175.957 249.941 823.289 1.00120.02 C ANISOU 551 CD1 PHE B 158 14647 20127 10827 878 -1776 653 C ATOM 552 CE1 PHE B 158 176.334 248.676 822.880 1.00119.93 C ANISOU 552 CE1 PHE B 158 14541 19687 11338 1038 -1483 802 C ATOM 553 CZ PHE B 158 176.544 247.688 823.810 1.00122.60 C ANISOU 553 CZ PHE B 158 14803 20049 11731 1350 -1172 1188 C ATOM 554 CE2 PHE B 158 176.378 247.966 825.149 1.00125.43 C ANISOU 554 CE2 PHE B 158 15181 20938 11539 1536 -1178 1430 C ATOM 555 CD2 PHE B 158 175.997 249.233 825.553 1.00125.61 C ANISOU 555 CD2 PHE B 158 15284 21445 10998 1365 -1513 1214 C ATOM 556 N ILE B 159 178.368 252.658 825.771 1.00129.50 N ANISOU 556 N ILE B 159 15328 22843 11032 1173 -2060 1293 N ATOM 557 CA ILE B 159 179.817 252.465 825.727 1.00130.37 C ANISOU 557 CA ILE B 159 15187 22862 11487 1407 -1834 1708 C ATOM 558 C ILE B 159 180.433 252.506 827.128 1.00134.70 C ANISOU 558 C ILE B 159 15528 24009 11644 1783 -1708 2192 C ATOM 559 O ILE B 159 181.425 251.826 827.407 1.00136.64 O ANISOU 559 O ILE B 159 15573 24147 12197 2119 -1350 2684 O ATOM 560 CB ILE B 159 180.498 253.510 824.809 1.00128.20 C ANISOU 560 CB ILE B 159 14836 22474 11402 1177 -2023 1532 C ATOM 561 CG1 ILE B 159 180.138 253.230 823.356 1.00124.61 C ANISOU 561 CG1 ILE B 159 14513 21439 11394 935 -2054 1165 C ATOM 562 CD1 ILE B 159 180.487 254.345 822.428 1.00122.56 C ANISOU 562 CD1 ILE B 159 14226 21139 11201 701 -2280 930 C ATOM 563 CG2 ILE B 159 182.010 253.501 824.978 1.00129.85 C ANISOU 563 CG2 ILE B 159 14764 22692 11880 1429 -1798 1967 C ATOM 564 N GLY B 160 179.846 253.308 828.012 1.00135.04 N ANISOU 564 N GLY B 160 15587 24699 11023 1744 -1979 2048 N ATOM 565 CA GLY B 160 180.270 253.331 829.397 1.00139.77 C ANISOU 565 CA GLY B 160 15973 26008 11125 2141 -1893 2470 C ATOM 566 C GLY B 160 179.929 251.990 829.998 1.00141.86 C ANISOU 566 C GLY B 160 16279 26229 11391 2492 -1555 2786 C ATOM 567 O GLY B 160 180.805 251.243 830.410 1.00144.28 O ANISOU 567 O GLY B 160 16393 26508 11918 2909 -1163 3378 O ATOM 568 N ARG B 161 178.637 251.679 830.006 1.00143.49 N ANISOU 568 N ARG B 161 16731 26383 11406 2327 -1668 2405 N ATOM 569 CA ARG B 161 178.149 250.445 830.590 1.00145.50 C ANISOU 569 CA ARG B 161 17051 26621 11612 2644 -1370 2659 C ATOM 570 C ARG B 161 179.083 249.304 830.269 1.00145.58 C ANISOU 570 C ARG B 161 16930 26080 12302 2938 -884 3197 C ATOM 571 O ARG B 161 179.147 248.324 830.996 1.00148.69 O ANISOU 571 O ARG B 161 17248 26565 12681 3358 -524 3658 O ATOM 572 CB ARG B 161 176.757 250.116 830.068 1.00142.91 C ANISOU 572 CB ARG B 161 17040 25936 11322 2330 -1492 2146 C ATOM 573 CG ARG B 161 175.811 251.287 830.033 1.00142.15 C ANISOU 573 CG ARG B 161 17080 26128 10804 1926 -1928 1515 C ATOM 574 CD ARG B 161 175.024 251.442 831.318 1.00146.43 C ANISOU 574 CD ARG B 161 17616 27419 10601 2079 -2046 1372 C ATOM 575 NE ARG B 161 173.802 252.202 831.076 1.00145.39 N ANISOU 575 NE ARG B 161 17674 27282 10287 1636 -2355 672 N ATOM 576 CZ ARG B 161 172.619 251.652 830.826 1.00144.28 C ANISOU 576 CZ ARG B 161 17791 26810 10219 1494 -2305 373 C ATOM 577 NH1 ARG B 161 172.494 250.331 830.807 1.00143.98 N ANISOU 577 NH1 ARG B 161 17853 26457 10396 1757 -1987 703 N ATOM 578 NH2 ARG B 161 171.562 252.420 830.604 1.00143.78 N ANISOU 578 NH2 ARG B 161 17868 26709 10053 1096 -2539 -244 N ATOM 579 N VAL B 162 179.809 249.430 829.174 1.00142.55 N ANISOU 579 N VAL B 162 16497 25122 12542 2728 -849 3125 N ATOM 580 CA VAL B 162 180.679 248.361 828.746 1.00142.78 C ANISOU 580 CA VAL B 162 16372 24542 13338 2939 -380 3509 C ATOM 581 C VAL B 162 182.058 248.471 829.359 1.00146.26 C ANISOU 581 C VAL B 162 16485 25206 13882 3325 -83 4126 C ATOM 582 O VAL B 162 182.611 247.483 829.821 1.00149.37 O ANISOU 582 O VAL B 162 16698 25435 14619 3736 418 4683 O ATOM 583 CB VAL B 162 180.837 248.346 827.230 1.00138.47 C ANISOU 583 CB VAL B 162 15885 23276 13452 2553 -453 3087 C ATOM 584 CG1 VAL B 162 181.919 247.349 826.826 1.00139.56 C ANISOU 584 CG1 VAL B 162 15778 22811 14436 2760 42 3424 C ATOM 585 CG2 VAL B 162 179.499 248.036 826.553 1.00135.40 C ANISOU 585 CG2 VAL B 162 15790 22604 13051 2240 -654 2568 C ATOM 586 N LYS B 163 182.632 249.666 829.347 1.00143.92 N ANISOU 586 N LYS B 163 16091 25256 13335 3209 -351 4060 N ATOM 587 CA LYS B 163 183.967 249.842 829.900 1.00147.31 C ANISOU 587 CA LYS B 163 16196 25911 13863 3581 -64 4665 C ATOM 588 C LYS B 163 183.972 249.285 831.320 1.00152.70 C ANISOU 588 C LYS B 163 16730 27190 14098 4153 234 5292 C ATOM 589 O LYS B 163 184.897 248.575 831.711 1.00156.09 O ANISOU 589 O LYS B 163 16908 27476 14924 4600 769 5958 O ATOM 590 CB LYS B 163 184.400 251.313 829.873 1.00146.69 C ANISOU 590 CB LYS B 163 16042 26285 13407 3390 -456 4496 C ATOM 591 N ASP B 164 182.908 249.581 832.067 1.00153.02 N ANISOU 591 N ASP B 164 16913 27888 13338 4152 -82 5065 N ATOM 592 CA ASP B 164 182.742 249.132 833.452 1.00158.48 C ANISOU 592 CA ASP B 164 17473 29309 13434 4708 126 5575 C ATOM 593 C ASP B 164 181.899 247.855 833.582 1.00158.89 C ANISOU 593 C ASP B 164 17692 29055 13625 4856 401 5635 C ATOM 594 O ASP B 164 182.276 246.777 833.110 1.00158.46 O ANISOU 594 O ASP B 164 17600 28255 14353 4972 869 5930 O ATOM 595 CB ASP B 164 182.102 250.250 834.277 1.00160.39 C ANISOU 595 CB ASP B 164 17717 30558 12665 4644 -393 5230 C ATOM 596 N VAL B 169 186.724 243.695 825.927 1.00157.15 N ANISOU 596 N VAL B 169 16641 22553 20515 3669 2455 4795 N ATOM 597 CA VAL B 169 187.191 244.970 825.396 1.00154.66 C ANISOU 597 CA VAL B 169 16359 22476 19930 3409 2041 4480 C ATOM 598 C VAL B 169 187.013 245.061 823.889 1.00150.74 C ANISOU 598 C VAL B 169 15925 21544 19805 2934 1735 3665 C ATOM 599 O VAL B 169 186.811 246.156 823.359 1.00147.49 O ANISOU 599 O VAL B 169 15679 21435 18925 2649 1227 3271 O ATOM 600 CB VAL B 169 188.683 245.236 825.710 1.00158.12 C ANISOU 600 CB VAL B 169 16459 22834 20787 3683 2453 4974 C ATOM 601 CG1 VAL B 169 188.842 245.941 827.059 1.00160.79 C ANISOU 601 CG1 VAL B 169 16787 23978 20327 4064 2432 5642 C ATOM 602 CG2 VAL B 169 189.486 243.936 825.639 1.00162.13 C ANISOU 602 CG2 VAL B 169 16618 22570 22415 3924 3214 5273 C ATOM 603 N ASN B 170 187.117 243.924 823.198 1.00140.93 N ANISOU 603 N ASN B 170 14515 19618 19413 2872 2060 3419 N ATOM 604 CA ASN B 170 186.909 243.897 821.756 1.00137.88 C ANISOU 604 CA ASN B 170 14141 18894 19353 2469 1776 2621 C ATOM 605 C ASN B 170 185.672 244.692 821.439 1.00133.49 C ANISOU 605 C ASN B 170 13972 18816 17932 2194 1127 2230 C ATOM 606 O ASN B 170 185.702 245.656 820.675 1.00130.77 O ANISOU 606 O ASN B 170 13713 18656 17318 1943 720 1826 O ATOM 607 CB ASN B 170 186.736 242.466 821.263 1.00139.39 C ANISOU 607 CB ASN B 170 14149 18441 20374 2449 2135 2392 C ATOM 608 CG ASN B 170 188.027 241.869 820.746 1.00142.76 C ANISOU 608 CG ASN B 170 14128 18215 21897 2483 2638 2288 C ATOM 609 OD1 ASN B 170 188.116 240.669 820.509 1.00145.26 O ANISOU 609 OD1 ASN B 170 14199 17954 23040 2513 3055 2182 O ATOM 610 ND2 ASN B 170 189.036 242.711 820.553 1.00143.09 N ANISOU 610 ND2 ASN B 170 14045 18329 21995 2467 2618 2286 N ATOM 611 N ARG B 171 184.587 244.281 822.074 1.00132.81 N ANISOU 611 N ARG B 171 14109 18922 17432 2270 1077 2387 N ATOM 612 CA ARG B 171 183.294 244.915 821.908 1.00129.30 C ANISOU 612 CA ARG B 171 14028 18878 16224 2036 549 2060 C ATOM 613 C ARG B 171 183.315 246.405 822.251 1.00127.94 C ANISOU 613 C ARG B 171 14006 19299 15308 1956 150 2101 C ATOM 614 O ARG B 171 182.456 247.167 821.801 1.00124.93 O ANISOU 614 O ARG B 171 13869 19163 14437 1691 -295 1721 O ATOM 615 CB ARG B 171 182.275 244.184 822.772 1.00130.29 C ANISOU 615 CB ARG B 171 14325 19118 16060 2203 661 2321 C ATOM 616 CG ARG B 171 180.881 244.680 822.618 1.00127.22 C ANISOU 616 CG ARG B 171 14293 19049 14997 1968 201 1972 C ATOM 617 CD ARG B 171 180.334 244.292 821.271 1.00124.56 C ANISOU 617 CD ARG B 171 13996 18334 14997 1685 45 1395 C ATOM 618 NE ARG B 171 178.988 244.808 821.121 1.00121.92 N ANISOU 618 NE ARG B 171 13996 18281 14049 1484 -344 1113 N ATOM 619 CZ ARG B 171 178.377 244.960 819.961 1.00119.25 C ANISOU 619 CZ ARG B 171 13747 17826 13738 1232 -604 627 C ATOM 620 NH1 ARG B 171 179.002 244.640 818.836 1.00118.89 N ANISOU 620 NH1 ARG B 171 13471 17457 14245 1147 -564 314 N ATOM 621 NH2 ARG B 171 177.142 245.432 819.934 1.00117.41 N ANISOU 621 NH2 ARG B 171 13807 17822 12981 1084 -882 448 N ATOM 622 N PHE B 172 184.296 246.808 823.052 1.00131.52 N ANISOU 622 N PHE B 172 14286 19972 15713 2200 343 2582 N ATOM 623 CA PHE B 172 184.479 248.209 823.409 1.00130.83 C ANISOU 623 CA PHE B 172 14269 20446 14995 2142 1 2640 C ATOM 624 C PHE B 172 185.214 248.912 822.289 1.00128.90 C ANISOU 624 C PHE B 172 13927 20011 15039 1912 -160 2284 C ATOM 625 O PHE B 172 184.778 249.961 821.836 1.00126.25 O ANISOU 625 O PHE B 172 13758 19947 14265 1659 -593 1957 O ATOM 626 CB PHE B 172 185.251 248.332 824.725 1.00134.83 C ANISOU 626 CB PHE B 172 14593 21329 15308 2542 282 3331 C ATOM 627 CG PHE B 172 185.660 249.748 825.075 1.00134.76 C ANISOU 627 CG PHE B 172 14568 21886 14748 2505 -27 3409 C ATOM 628 CD1 PHE B 172 184.709 250.708 825.396 1.00133.26 C ANISOU 628 CD1 PHE B 172 14605 22253 13775 2315 -508 3166 C ATOM 629 CE1 PHE B 172 185.096 252.004 825.731 1.00133.59 C ANISOU 629 CE1 PHE B 172 14589 22809 13361 2271 -781 3217 C ATOM 630 CZ PHE B 172 186.435 252.346 825.753 1.00135.21 C ANISOU 630 CZ PHE B 172 14532 22994 13847 2438 -580 3551 C ATOM 631 CE2 PHE B 172 187.393 251.404 825.452 1.00136.72 C ANISOU 631 CE2 PHE B 172 14512 22628 14808 2641 -83 3815 C ATOM 632 CD2 PHE B 172 187.009 250.110 825.122 1.00136.63 C ANISOU 632 CD2 PHE B 172 14535 22084 15293 2667 197 3728 C ATOM 633 N TYR B 173 186.322 248.324 821.837 1.00196.94 N ANISOU 633 N TYR B 173 22257 28147 24424 2008 218 2334 N ATOM 634 CA TYR B 173 187.132 248.913 820.772 1.00195.73 C ANISOU 634 CA TYR B 173 21972 27812 24587 1828 113 1979 C ATOM 635 C TYR B 173 186.295 249.260 819.548 1.00192.00 C ANISOU 635 C TYR B 173 21687 27330 23933 1488 -323 1318 C ATOM 636 O TYR B 173 186.249 250.411 819.114 1.00189.94 O ANISOU 636 O TYR B 173 21529 27364 23277 1322 -682 1123 O ATOM 637 CB TYR B 173 188.266 247.968 820.366 1.00198.53 C ANISOU 637 CB TYR B 173 21971 27548 25914 1951 628 1990 C ATOM 638 CG TYR B 173 188.950 248.344 819.064 1.00197.45 C ANISOU 638 CG TYR B 173 21686 27175 26162 1738 514 1445 C ATOM 639 CD1 TYR B 173 189.787 249.456 818.988 1.00197.33 C ANISOU 639 CD1 TYR B 173 21609 27386 25981 1734 402 1528 C ATOM 640 CE1 TYR B 173 190.420 249.803 817.796 1.00196.65 C ANISOU 640 CE1 TYR B 173 21382 27120 26214 1571 308 1023 C ATOM 641 CZ TYR B 173 190.220 249.028 816.662 1.00196.35 C ANISOU 641 CZ TYR B 173 21238 26720 26645 1414 308 394 C ATOM 642 OH TYR B 173 190.846 249.365 815.474 1.00196.20 O ANISOU 642 OH TYR B 173 21051 26608 26888 1285 203 -150 O ATOM 643 CE2 TYR B 173 189.394 247.916 816.716 1.00196.51 C ANISOU 643 CE2 TYR B 173 21297 26518 26850 1405 408 294 C ATOM 644 CD2 TYR B 173 188.767 247.580 817.910 1.00196.94 C ANISOU 644 CD2 TYR B 173 21517 26702 26608 1563 521 834 C ATOM 645 N GLU B 174 185.627 248.255 819.001 1.00123.48 N ANISOU 645 N GLU B 174 13036 18328 15552 1414 -265 1008 N ATOM 646 CA GLU B 174 184.894 248.436 817.760 1.00120.59 C ANISOU 646 CA GLU B 174 12790 17951 15078 1156 -614 411 C ATOM 647 C GLU B 174 183.578 249.174 817.981 1.00118.02 C ANISOU 647 C GLU B 174 12819 18041 13980 1020 -1010 375 C ATOM 648 O GLU B 174 182.843 249.454 817.037 1.00115.75 O ANISOU 648 O GLU B 174 12658 17805 13516 839 -1292 -30 O ATOM 649 CB GLU B 174 184.677 247.088 817.061 1.00121.36 C ANISOU 649 CB GLU B 174 12737 17585 15787 1135 -409 72 C ATOM 650 CG GLU B 174 183.569 246.230 817.648 1.00121.33 C ANISOU 650 CG GLU B 174 12909 17533 15659 1188 -331 223 C ATOM 651 CD GLU B 174 183.730 244.748 817.324 1.00123.50 C ANISOU 651 CD GLU B 174 12930 17274 16719 1248 42 71 C ATOM 652 OE1 GLU B 174 184.800 244.336 816.812 1.00125.65 O ANISOU 652 OE1 GLU B 174 12858 17184 17701 1266 305 -114 O ATOM 653 OE2 GLU B 174 182.771 243.995 817.599 1.00123.32 O ANISOU 653 OE2 GLU B 174 13040 17182 16633 1273 90 122 O ATOM 654 N LEU B 175 183.283 249.498 819.229 1.00120.42 N ANISOU 654 N LEU B 175 13257 18663 13834 1126 -1011 791 N ATOM 655 CA LEU B 175 182.103 250.293 819.532 1.00118.66 C ANISOU 655 CA LEU B 175 13331 18830 12923 980 -1360 716 C ATOM 656 C LEU B 175 182.499 251.766 819.492 1.00117.90 C ANISOU 656 C LEU B 175 13243 19086 12466 873 -1629 712 C ATOM 657 O LEU B 175 181.886 252.580 818.798 1.00115.76 O ANISOU 657 O LEU B 175 13114 18932 11938 663 -1928 409 O ATOM 658 CB LEU B 175 181.561 249.919 820.914 1.00120.53 C ANISOU 658 CB LEU B 175 13672 19299 12824 1151 -1243 1086 C ATOM 659 CG LEU B 175 180.047 249.941 821.167 1.00119.38 C ANISOU 659 CG LEU B 175 13822 19326 12213 1025 -1447 911 C ATOM 660 CD1 LEU B 175 179.236 249.878 819.873 1.00116.58 C ANISOU 660 CD1 LEU B 175 13597 18719 11978 790 -1625 440 C ATOM 661 CD2 LEU B 175 179.652 248.802 822.087 1.00121.50 C ANISOU 661 CD2 LEU B 175 14115 19546 12504 1255 -1165 1197 C ATOM 662 N GLU B 176 183.543 252.086 820.248 1.00153.69 N ANISOU 662 N GLU B 176 17600 23782 17013 1045 -1485 1090 N ATOM 663 CA GLU B 176 184.117 253.418 820.281 1.00153.48 C ANISOU 663 CA GLU B 176 17522 24076 16716 978 -1690 1144 C ATOM 664 C GLU B 176 184.332 253.915 818.861 1.00151.24 C ANISOU 664 C GLU B 176 17220 23609 16636 794 -1854 741 C ATOM 665 O GLU B 176 184.095 255.082 818.555 1.00149.91 O ANISOU 665 O GLU B 176 17135 23688 16134 635 -2137 610 O ATOM 666 CB GLU B 176 185.452 253.354 821.009 1.00156.35 C ANISOU 666 CB GLU B 176 17624 24489 17293 1243 -1397 1611 C ATOM 667 CG GLU B 176 185.814 254.597 821.761 1.00157.35 C ANISOU 667 CG GLU B 176 17705 25142 16940 1269 -1578 1858 C ATOM 668 CD GLU B 176 186.992 254.375 822.686 1.00160.86 C ANISOU 668 CD GLU B 176 17887 25698 17536 1610 -1235 2427 C ATOM 669 OE1 GLU B 176 187.463 255.352 823.309 1.00162.18 O ANISOU 669 OE1 GLU B 176 17956 26321 17346 1676 -1351 2673 O ATOM 670 OE2 GLU B 176 187.453 253.219 822.790 1.00162.63 O ANISOU 670 OE2 GLU B 176 17977 25548 18266 1827 -821 2646 O ATOM 671 N GLU B 177 184.777 253.006 817.997 1.00136.00 N ANISOU 671 N GLU B 177 15150 21259 15266 832 -1657 533 N ATOM 672 CA GLU B 177 185.120 253.316 816.611 1.00134.67 C ANISOU 672 CA GLU B 177 14898 20959 15311 723 -1775 124 C ATOM 673 C GLU B 177 183.893 253.735 815.817 1.00132.22 C ANISOU 673 C GLU B 177 14810 20778 14650 544 -2087 -214 C ATOM 674 O GLU B 177 183.929 254.678 815.047 1.00131.06 O ANISOU 674 O GLU B 177 14678 20790 14329 459 -2294 -386 O ATOM 675 CB GLU B 177 185.771 252.098 815.966 1.00136.05 C ANISOU 675 CB GLU B 177 14830 20683 16179 806 -1481 -94 C ATOM 676 CG GLU B 177 186.770 252.436 814.896 1.00136.37 C ANISOU 676 CG GLU B 177 14648 20630 16534 790 -1483 -405 C ATOM 677 CD GLU B 177 187.744 251.295 814.613 1.00139.04 C ANISOU 677 CD GLU B 177 14659 20502 17669 891 -1094 -558 C ATOM 678 OE1 GLU B 177 187.526 250.188 815.174 1.00140.43 O ANISOU 678 OE1 GLU B 177 14792 20401 18165 969 -822 -416 O ATOM 679 OE2 GLU B 177 188.719 251.510 813.837 1.00140.06 O ANISOU 679 OE2 GLU B 177 14558 20531 18128 895 -1038 -833 O ATOM 680 N SER B 178 182.801 253.010 815.997 1.00120.05 N ANISOU 680 N SER B 178 13429 19158 13026 514 -2084 -274 N ATOM 681 CA SER B 178 181.527 253.451 815.467 1.00118.15 C ANISOU 681 CA SER B 178 13415 19048 12428 369 -2329 -494 C ATOM 682 C SER B 178 181.270 254.866 815.936 1.00117.68 C ANISOU 682 C SER B 178 13482 19325 11904 257 -2541 -355 C ATOM 683 O SER B 178 180.936 255.727 815.139 1.00116.52 O ANISOU 683 O SER B 178 13389 19286 11596 161 -2717 -520 O ATOM 684 CB SER B 178 180.391 252.543 815.943 1.00118.08 C ANISOU 684 CB SER B 178 13578 18931 12355 365 -2260 -482 C ATOM 685 OG SER B 178 180.216 251.422 815.093 1.00117.98 O ANISOU 685 OG SER B 178 13478 18637 12713 406 -2155 -745 O ATOM 686 N LEU B 179 181.428 255.110 817.232 1.00111.54 N ANISOU 686 N LEU B 179 12721 18739 10920 289 -2507 -51 N ATOM 687 CA LEU B 179 181.167 256.435 817.763 1.00111.67 C ANISOU 687 CA LEU B 179 12810 19101 10518 164 -2714 24 C ATOM 688 C LEU B 179 181.892 257.525 816.992 1.00111.03 C ANISOU 688 C LEU B 179 12618 19103 10465 114 -2832 -28 C ATOM 689 O LEU B 179 181.259 258.489 816.580 1.00110.19 O ANISOU 689 O LEU B 179 12607 19109 10152 -36 -3005 -159 O ATOM 690 CB LEU B 179 181.520 256.549 819.242 1.00113.92 C ANISOU 690 CB LEU B 179 13033 19680 10571 261 -2665 352 C ATOM 691 CG LEU B 179 181.211 257.949 819.782 1.00114.52 C ANISOU 691 CG LEU B 179 13135 20152 10226 103 -2905 341 C ATOM 692 CD1 LEU B 179 179.730 258.277 819.697 1.00113.82 C ANISOU 692 CD1 LEU B 179 13265 20074 9909 -113 -3052 53 C ATOM 693 CD2 LEU B 179 181.682 258.073 821.197 1.00117.29 C ANISOU 693 CD2 LEU B 179 13360 20901 10304 246 -2876 651 C ATOM 694 N THR B 180 183.205 257.402 816.792 1.00121.23 N ANISOU 694 N THR B 180 13698 20323 12041 247 -2707 84 N ATOM 695 CA THR B 180 183.937 258.491 816.129 1.00120.86 C ANISOU 695 CA THR B 180 13543 20387 11991 218 -2812 55 C ATOM 696 C THR B 180 183.457 258.732 814.682 1.00119.24 C ANISOU 696 C THR B 180 13392 20098 11815 161 -2922 -272 C ATOM 697 O THR B 180 183.266 259.870 814.267 1.00118.72 O ANISOU 697 O THR B 180 13359 20199 11552 81 -3069 -292 O ATOM 698 CB THR B 180 185.493 258.356 816.229 1.00122.27 C ANISOU 698 CB THR B 180 13470 20499 12489 383 -2624 244 C ATOM 699 OG1 THR B 180 186.024 257.621 815.117 1.00122.08 O ANISOU 699 OG1 THR B 180 13319 20177 12889 458 -2496 -29 O ATOM 700 CG2 THR B 180 185.890 257.692 817.529 1.00124.32 C ANISOU 700 CG2 THR B 180 13653 20780 12804 531 -2415 601 C ATOM 701 N VAL B 181 183.245 257.656 813.932 1.00109.12 N ANISOU 701 N VAL B 181 12095 18587 10778 227 -2834 -512 N ATOM 702 CA VAL B 181 182.660 257.741 812.596 1.00108.09 C ANISOU 702 CA VAL B 181 11997 18463 10611 230 -2932 -809 C ATOM 703 C VAL B 181 181.345 258.493 812.664 1.00107.24 C ANISOU 703 C VAL B 181 12112 18479 10155 101 -3065 -771 C ATOM 704 O VAL B 181 181.095 259.428 811.918 1.00106.89 O ANISOU 704 O VAL B 181 12082 18570 9963 93 -3156 -804 O ATOM 705 CB VAL B 181 182.397 256.345 812.024 1.00108.20 C ANISOU 705 CB VAL B 181 11958 18256 10897 307 -2829 -1075 C ATOM 706 CG1 VAL B 181 181.255 256.392 811.035 1.00107.30 C ANISOU 706 CG1 VAL B 181 11952 18226 10590 309 -2941 -1281 C ATOM 707 CG2 VAL B 181 183.666 255.800 811.380 1.00109.43 C ANISOU 707 CG2 VAL B 181 11827 18290 11463 428 -2709 -1287 C ATOM 708 N LEU B 182 180.504 258.069 813.584 1.00123.23 N ANISOU 708 N LEU B 182 14297 20448 12079 15 -3039 -694 N ATOM 709 CA LEU B 182 179.219 258.692 813.780 1.00122.94 C ANISOU 709 CA LEU B 182 14457 20471 11784 -129 -3116 -698 C ATOM 710 C LEU B 182 179.329 260.059 814.453 1.00123.68 C ANISOU 710 C LEU B 182 14545 20772 11675 -267 -3218 -554 C ATOM 711 O LEU B 182 178.445 260.899 814.312 1.00123.80 O ANISOU 711 O LEU B 182 14656 20818 11566 -394 -3264 -595 O ATOM 712 CB LEU B 182 178.339 257.754 814.600 1.00123.14 C ANISOU 712 CB LEU B 182 14635 20381 11773 -169 -3045 -703 C ATOM 713 CG LEU B 182 177.019 258.303 815.127 1.00123.48 C ANISOU 713 CG LEU B 182 14874 20463 11579 -341 -3089 -734 C ATOM 714 CD1 LEU B 182 176.214 258.939 813.994 1.00122.89 C ANISOU 714 CD1 LEU B 182 14862 20333 11499 -372 -3098 -837 C ATOM 715 CD2 LEU B 182 176.231 257.189 815.786 1.00123.73 C ANISOU 715 CD2 LEU B 182 15044 20372 11594 -333 -2996 -764 C ATOM 716 N ASN B 183 180.407 260.289 815.187 1.00126.27 N ANISOU 716 N ASN B 183 14735 21235 12006 -235 -3226 -383 N ATOM 717 CA ASN B 183 180.609 261.573 815.847 1.00127.32 C ANISOU 717 CA ASN B 183 14811 21614 11951 -357 -3337 -261 C ATOM 718 C ASN B 183 180.954 262.602 814.793 1.00126.82 C ANISOU 718 C ASN B 183 14669 21578 11938 -354 -3385 -275 C ATOM 719 O ASN B 183 180.835 263.809 815.007 1.00127.60 O ANISOU 719 O ASN B 183 14731 21820 11930 -482 -3464 -223 O ATOM 720 CB ASN B 183 181.748 261.453 816.848 1.00128.64 C ANISOU 720 CB ASN B 183 14819 21955 12103 -261 -3308 -26 C ATOM 721 CG ASN B 183 181.584 262.369 818.031 1.00130.47 C ANISOU 721 CG ASN B 183 15006 22524 12044 -386 -3431 66 C ATOM 722 OD1 ASN B 183 180.593 263.094 818.148 1.00130.88 O ANISOU 722 OD1 ASN B 183 15141 22636 11951 -585 -3534 -101 O ATOM 723 ND2 ASN B 183 182.567 262.345 818.925 1.00132.06 N ANISOU 723 ND2 ASN B 183 15040 22958 12178 -260 -3403 322 N ATOM 724 N CYS B 184 181.384 262.085 813.648 1.00126.97 N ANISOU 724 N CYS B 184 14637 21476 12130 -192 -3324 -365 N ATOM 725 CA CYS B 184 181.667 262.856 812.443 1.00126.68 C ANISOU 725 CA CYS B 184 14523 21497 12114 -109 -3346 -398 C ATOM 726 CB CYS B 184 182.509 261.995 811.506 1.00126.39 C ANISOU 726 CB CYS B 184 14354 21398 12270 97 -3284 -551 C ATOM 727 SG CYS B 184 183.308 262.862 810.164 1.00126.72 S ANISOU 727 SG CYS B 184 14229 21613 12305 270 -3308 -596 S ATOM 728 C CYS B 184 180.396 263.252 811.722 1.00126.45 C ANISOU 728 C CYS B 184 14621 21429 11996 -142 -3336 -467 C ATOM 729 O CYS B 184 180.109 264.432 811.559 1.00127.06 O ANISOU 729 O CYS B 184 14690 21576 12011 -210 -3346 -369 O ATOM 730 C LEU B 185 177.521 263.531 811.114 1.00107.87 C ANISOU 730 C LEU B 185 12568 18857 9560 -257 -3192 -538 C ATOM 731 CA LEU B 185 178.415 262.437 810.537 1.00106.97 C ANISOU 731 CA LEU B 185 12358 18788 9495 -50 -3223 -646 C ATOM 732 N LEU B 185 179.649 262.243 811.293 1.00106.92 N ANISOU 732 N LEU B 185 12244 18829 9553 -77 -3283 -615 N ATOM 733 CB LEU B 185 177.623 261.124 810.424 1.00106.42 C ANISOU 733 CB LEU B 185 12397 18575 9463 -5 -3169 -795 C ATOM 734 CG LEU B 185 176.603 260.967 809.281 1.00106.60 C ANISOU 734 CG LEU B 185 12464 18601 9437 150 -3085 -833 C ATOM 735 CD1 LEU B 185 176.363 259.521 809.002 1.00106.13 C ANISOU 735 CD1 LEU B 185 12409 18469 9445 252 -3068 -1019 C ATOM 736 CD2 LEU B 185 175.283 261.603 809.604 1.00107.25 C ANISOU 736 CD2 LEU B 185 12713 18548 9491 8 -2977 -722 C ATOM 737 O LEU B 185 176.780 264.186 810.379 1.00108.53 O ANISOU 737 O LEU B 185 12673 18911 9651 -211 -3091 -469 O ATOM 738 C ARG B 186 177.514 266.192 812.678 1.00119.98 C ANISOU 738 C ARG B 186 13987 20501 11098 -702 -3257 -375 C ATOM 739 CA ARG B 186 176.843 264.852 813.008 1.00119.17 C ANISOU 739 CA ARG B 186 14048 20276 10953 -696 -3238 -519 C ATOM 740 N ARG B 186 177.571 263.729 812.424 1.00117.66 N ANISOU 740 N ARG B 186 13836 20104 10767 -469 -3254 -532 N ATOM 741 CB ARG B 186 176.680 264.706 814.525 1.00120.16 C ANISOU 741 CB ARG B 186 14205 20477 10974 -903 -3324 -613 C ATOM 742 CG ARG B 186 176.339 266.029 815.223 1.00122.37 C ANISOU 742 CG ARG B 186 14397 20836 11261 -1154 -3358 -668 C ATOM 743 CD ARG B 186 175.994 265.778 816.655 1.00123.90 C ANISOU 743 CD ARG B 186 14608 21177 11290 -1324 -3449 -835 C ATOM 744 NE ARG B 186 176.671 266.707 817.550 1.00125.80 N ANISOU 744 NE ARG B 186 14644 21729 11424 -1447 -3595 -830 N ATOM 745 CZ ARG B 186 176.123 267.822 818.018 1.00128.34 C ANISOU 745 CZ ARG B 186 14854 22102 11806 -1700 -3617 -1014 C ATOM 746 NH1 ARG B 186 176.818 268.618 818.832 1.00130.27 N ANISOU 746 NH1 ARG B 186 14873 22691 11933 -1791 -3772 -1018 N ATOM 747 NH2 ARG B 186 174.880 268.140 817.657 1.00129.29 N ANISOU 747 NH2 ARG B 186 15061 21921 12140 -1856 -3460 -1197 N ATOM 748 O ARG B 186 176.887 267.084 812.093 1.00121.00 O ANISOU 748 O ARG B 186 14102 20541 11331 -722 -3136 -310 O ATOM 749 C THR B 187 179.393 268.097 811.378 1.00133.94 C ANISOU 749 C THR B 187 15423 22541 12925 -470 -3270 -38 C ATOM 750 CA THR B 187 179.532 267.560 812.807 1.00133.96 C ANISOU 750 CA THR B 187 15456 22587 12857 -660 -3394 -142 C ATOM 751 N THR B 187 178.786 266.324 813.045 1.00133.17 N ANISOU 751 N THR B 187 15522 22355 12720 -663 -3370 -293 N ATOM 752 CB THR B 187 181.027 267.392 813.149 1.00133.58 C ANISOU 752 CB THR B 187 15267 22721 12766 -561 -3490 -41 C ATOM 753 OG1 THR B 187 181.225 267.632 814.548 1.00134.82 O ANISOU 753 OG1 THR B 187 15359 23038 12828 -734 -3591 -20 O ATOM 754 CG2 THR B 187 181.876 268.373 812.357 1.00133.85 C ANISOU 754 CG2 THR B 187 15150 22857 12852 -441 -3473 115 C ATOM 755 O THR B 187 179.586 269.284 811.131 1.00135.08 O ANISOU 755 O THR B 187 15453 22734 13137 -488 -3227 106 O ATOM 756 C MET B 188 177.701 267.790 808.348 1.00112.43 C ANISOU 756 C MET B 188 12796 19722 10199 86 -2899 89 C ATOM 757 CA MET B 188 179.061 267.556 809.019 1.00111.40 C ANISOU 757 CA MET B 188 12585 19718 10026 16 -3097 5 C ATOM 758 N MET B 188 179.028 267.226 810.446 1.00111.10 N ANISOU 758 N MET B 188 12613 19593 10008 -265 -3201 -100 N ATOM 759 CB MET B 188 179.829 266.472 808.268 1.00110.36 C ANISOU 759 CB MET B 188 12397 19721 9813 269 -3163 -144 C ATOM 760 CG MET B 188 181.237 266.281 808.799 1.00109.85 C ANISOU 760 CG MET B 188 12219 19733 9787 243 -3278 -190 C ATOM 761 SD MET B 188 182.278 267.725 808.484 1.00110.84 S ANISOU 761 SD MET B 188 12168 20043 9905 315 -3280 26 S ATOM 762 CE MET B 188 183.117 267.236 806.973 1.00111.06 C ANISOU 762 CE MET B 188 12048 20294 9857 698 -3268 -131 C ATOM 763 O MET B 188 177.600 268.578 807.418 1.00113.66 O ANISOU 763 O MET B 188 12866 19957 10361 285 -2758 291 O ATOM 764 C TYR B 189 174.234 267.521 809.292 1.00120.84 C ANISOU 764 C TYR B 189 14209 20136 11570 -314 -2526 -22 C ATOM 765 CA TYR B 189 175.325 267.316 808.244 1.00119.84 C ANISOU 765 CA TYR B 189 13964 20304 11265 21 -2617 77 C ATOM 766 N TYR B 189 176.659 267.108 808.807 1.00118.55 N ANISOU 766 N TYR B 189 13727 20304 11012 -45 -2854 -30 N ATOM 767 CB TYR B 189 174.905 266.147 807.354 1.00119.13 C ANISOU 767 CB TYR B 189 13930 20288 11047 295 -2583 21 C ATOM 768 CG TYR B 189 175.850 265.823 806.233 1.00118.79 C ANISOU 768 CG TYR B 189 13735 20582 10818 642 -2670 12 C ATOM 769 CD1 TYR B 189 175.527 266.121 804.922 1.00120.32 C ANISOU 769 CD1 TYR B 189 13830 20988 10896 1010 -2516 201 C ATOM 770 CE1 TYR B 189 176.397 265.818 803.877 1.00120.55 C ANISOU 770 CE1 TYR B 189 13687 21409 10708 1348 -2616 120 C ATOM 771 CZ TYR B 189 177.599 265.193 804.145 1.00119.21 C ANISOU 771 CZ TYR B 189 13445 21332 10519 1284 -2842 -169 C ATOM 772 OH TYR B 189 178.462 264.892 803.110 1.00119.95 O ANISOU 772 OH TYR B 189 13336 21803 10435 1600 -2930 -334 O ATOM 773 CE2 TYR B 189 177.939 264.878 805.448 1.00117.63 C ANISOU 773 CE2 TYR B 189 13347 20863 10485 928 -2954 -295 C ATOM 774 CD2 TYR B 189 177.062 265.192 806.481 1.00117.44 C ANISOU 774 CD2 TYR B 189 13492 20536 10593 627 -2883 -196 C ATOM 775 O TYR B 189 173.061 267.565 808.935 1.00122.07 O ANISOU 775 O TYR B 189 14436 20089 11856 -282 -2292 45 O ATOM 776 C PHE B 190 173.759 268.997 812.561 1.00123.21 C ANISOU 776 C PHE B 190 14444 20246 12125 -1229 -2684 -461 C ATOM 777 CA PHE B 190 173.562 267.808 811.607 1.00121.16 C ANISOU 777 CA PHE B 190 14330 19961 11744 -927 -2629 -372 C ATOM 778 N PHE B 190 174.590 267.636 810.570 1.00119.67 N ANISOU 778 N PHE B 190 14061 19986 11423 -611 -2692 -188 N ATOM 779 CB PHE B 190 173.378 266.516 812.400 1.00119.88 C ANISOU 779 CB PHE B 190 14318 19809 11420 -993 -2759 -582 C ATOM 780 CG PHE B 190 172.930 265.364 811.566 1.00118.46 C ANISOU 780 CG PHE B 190 14263 19557 11187 -754 -2678 -551 C ATOM 781 CD1 PHE B 190 173.820 264.721 810.726 1.00116.78 C ANISOU 781 CD1 PHE B 190 13993 19526 10854 -478 -2767 -477 C ATOM 782 CE1 PHE B 190 173.412 263.658 809.944 1.00115.92 C ANISOU 782 CE1 PHE B 190 13948 19399 10698 -259 -2711 -498 C ATOM 783 CZ PHE B 190 172.114 263.222 809.999 1.00116.46 C ANISOU 783 CZ PHE B 190 14165 19255 10830 -298 -2552 -534 C ATOM 784 CE2 PHE B 190 171.211 263.865 810.832 1.00118.04 C ANISOU 784 CE2 PHE B 190 14448 19234 11166 -570 -2435 -587 C ATOM 785 CD2 PHE B 190 171.619 264.929 811.610 1.00119.15 C ANISOU 785 CD2 PHE B 190 14500 19407 11364 -804 -2504 -626 C ATOM 786 O PHE B 190 173.220 268.997 813.678 1.00124.56 O ANISOU 786 O PHE B 190 14638 20373 12316 -1506 -2733 -721 O ATOM 787 C ILE B 191 174.339 272.475 812.004 1.00145.25 C ANISOU 787 C ILE B 191 16742 22960 15488 -1384 -2415 -108 C ATOM 788 CA ILE B 191 174.667 271.255 812.867 1.00143.16 C ANISOU 788 CA ILE B 191 16612 22892 14892 -1439 -2700 -339 C ATOM 789 N ILE B 191 174.504 270.011 812.109 1.00140.79 N ANISOU 789 N ILE B 191 16499 22571 14424 -1164 -2674 -268 N ATOM 790 CB ILE B 191 176.099 271.394 813.437 1.00142.27 C ANISOU 790 CB ILE B 191 16367 23129 14560 -1438 -2979 -305 C ATOM 791 CG1 ILE B 191 176.496 270.143 814.225 1.00140.55 C ANISOU 791 CG1 ILE B 191 16259 23096 14047 -1419 -3192 -440 C ATOM 792 CD1 ILE B 191 177.915 270.185 814.768 1.00139.98 C ANISOU 792 CD1 ILE B 191 16049 23349 13789 -1365 -3403 -342 C ATOM 793 CG2 ILE B 191 176.218 272.626 814.312 1.00145.06 C ANISOU 793 CG2 ILE B 191 16496 23562 15058 -1731 -3035 -417 C ATOM 794 O ILE B 191 173.975 273.533 812.507 1.00148.11 O ANISOU 794 O ILE B 191 16945 23183 16148 -1648 -2314 -208 O ATOM 795 C LEU B 192 175.333 274.481 810.057 1.00136.08 C ANISOU 795 C LEU B 192 15264 21845 14594 -952 -2083 591 C ATOM 796 CA LEU B 192 174.279 273.418 809.777 1.00135.33 C ANISOU 796 CA LEU B 192 15381 21587 14451 -866 -1970 509 C ATOM 797 N LEU B 192 174.454 272.308 810.694 1.00133.21 N ANISOU 797 N LEU B 192 15254 21441 13918 -1020 -2268 192 N ATOM 798 CB LEU B 192 172.870 274.010 809.897 1.00138.56 C ANISOU 798 CB LEU B 192 15766 21567 15313 -1053 -1607 478 C ATOM 799 CG LEU B 192 171.710 273.285 809.201 1.00138.75 C ANISOU 799 CG LEU B 192 15953 21376 15390 -851 -1333 579 C ATOM 800 CD1 LEU B 192 170.390 274.051 809.370 1.00142.67 C ANISOU 800 CD1 LEU B 192 16379 21382 16447 -1055 -904 565 C ATOM 801 CD2 LEU B 192 172.013 273.049 807.716 1.00137.92 C ANISOU 801 CD2 LEU B 192 15849 21489 15067 -321 -1212 992 C ATOM 802 O LEU B 192 176.478 274.163 810.377 1.00134.13 O ANISOU 802 O LEU B 192 15000 21896 14067 -924 -2377 544 O ATOM 803 C ASN B 200 177.014 277.820 814.812 1.00150.65 C ANISOU 803 C ASN B 200 16195 24245 16800 -2348 -2811 -300 C ATOM 804 CA ASN B 200 175.595 277.849 814.224 1.00152.14 C ANISOU 804 CA ASN B 200 16483 23945 17377 -2389 -2441 -348 C ATOM 805 N ASN B 200 174.550 277.609 815.211 1.00154.34 N ANISOU 805 N ASN B 200 16765 24111 17764 -2727 -2458 -836 N ATOM 806 CB ASN B 200 175.349 279.162 813.469 1.00155.02 C ANISOU 806 CB ASN B 200 16638 23993 18271 -2379 -2075 -96 C ATOM 807 O ASN B 200 177.510 276.755 815.188 1.00148.06 O ANISOU 807 O ASN B 200 16024 24182 16049 -2235 -3055 -338 O ATOM 808 C ARG B 201 179.652 278.469 816.403 1.00135.05 C ANISOU 808 C ARG B 201 13807 23222 14284 -2393 -3436 -227 C ATOM 809 CA ARG B 201 179.097 279.107 815.134 1.00135.45 C ANISOU 809 CA ARG B 201 13886 22829 14751 -2298 -3075 -1 C ATOM 810 N ARG B 201 177.650 278.992 814.901 1.00136.84 N ANISOU 810 N ARG B 201 14167 22589 15236 -2429 -2815 -194 N ATOM 811 CB ARG B 201 179.538 280.571 815.074 1.00138.25 C ANISOU 811 CB ARG B 201 13914 23183 15433 -2402 -2988 133 C ATOM 812 O ARG B 201 180.814 278.088 816.442 1.00133.02 O ANISOU 812 O ARG B 201 13563 23258 13719 -2180 -3602 -1 O ATOM 813 C SER B 202 179.322 276.258 818.661 1.00154.86 C ANISOU 813 C SER B 202 16519 26323 15998 -2497 -3907 -780 C ATOM 814 CA SER B 202 179.337 277.788 818.689 1.00158.16 C ANISOU 814 CA SER B 202 16612 26718 16763 -2723 -3854 -843 C ATOM 815 N SER B 202 178.841 278.358 817.443 1.00157.85 N ANISOU 815 N SER B 202 16634 26175 17165 -2687 -3531 -663 N ATOM 816 CB SER B 202 178.532 278.308 819.881 1.00162.70 C ANISOU 816 CB SER B 202 16941 27466 17410 -3104 -3961 -1385 C ATOM 817 OG SER B 202 177.141 278.117 819.672 1.00163.67 O ANISOU 817 OG SER B 202 17204 27160 17825 -3279 -3747 -1688 O ATOM 818 O SER B 202 180.365 275.604 818.775 1.00152.76 O ANISOU 818 O SER B 202 16302 26319 15421 -2252 -4035 -529 O ATOM 819 C GLU B 203 178.844 273.482 817.631 1.00157.83 C ANISOU 819 C GLU B 203 17555 26338 16075 -2048 -3775 -603 C ATOM 820 CA GLU B 203 177.941 274.256 818.592 1.00161.76 C ANISOU 820 CA GLU B 203 17876 26897 16688 -2409 -3812 -1004 C ATOM 821 N GLU B 203 178.130 275.696 818.499 1.00164.29 N ANISOU 821 N GLU B 203 17916 27208 17298 -2578 -3771 -1002 N ATOM 822 CB GLU B 203 176.470 273.919 818.368 1.00162.32 C ANISOU 822 CB GLU B 203 18128 26578 16969 -2546 -3619 -1268 C ATOM 823 CG GLU B 203 176.020 272.619 818.989 1.00161.38 C ANISOU 823 CG GLU B 203 18216 26554 16549 -2498 -3702 -1437 C ATOM 824 CD GLU B 203 174.526 272.399 818.817 1.00162.42 C ANISOU 824 CD GLU B 203 18501 26290 16920 -2655 -3490 -1714 C ATOM 825 OE1 GLU B 203 173.759 273.362 819.042 1.00165.86 O ANISOU 825 OE1 GLU B 203 18771 26561 17687 -2945 -3375 -2008 O ATOM 826 OE2 GLU B 203 174.121 271.273 818.443 1.00160.05 O ANISOU 826 OE2 GLU B 203 18467 25822 16524 -2491 -3414 -1643 O ATOM 827 O GLU B 203 179.333 272.407 817.968 1.00156.13 O ANISOU 827 O GLU B 203 17449 26290 15582 -1876 -3875 -531 O ATOM 828 C PHE B 204 181.311 273.120 815.834 1.00124.53 C ANISOU 828 C PHE B 204 13363 22175 11778 -1430 -3733 111 C ATOM 829 CA PHE B 204 179.870 273.388 815.409 1.00125.43 C ANISOU 829 CA PHE B 204 13578 21966 12115 -1582 -3565 -64 C ATOM 830 N PHE B 204 179.077 274.048 816.449 1.00128.56 N ANISOU 830 N PHE B 204 13844 22405 12599 -1923 -3611 -358 N ATOM 831 CB PHE B 204 179.862 274.196 814.108 1.00125.42 C ANISOU 831 CB PHE B 204 13541 21758 12355 -1446 -3357 162 C ATOM 832 CG PHE B 204 180.615 273.535 812.971 1.00122.81 C ANISOU 832 CG PHE B 204 13312 21446 11907 -1082 -3318 379 C ATOM 833 CD1 PHE B 204 179.948 273.021 811.869 1.00121.82 C ANISOU 833 CD1 PHE B 204 13340 21129 11814 -883 -3149 416 C ATOM 834 CE1 PHE B 204 180.648 272.418 810.839 1.00120.04 C ANISOU 834 CE1 PHE B 204 13156 20997 11457 -550 -3140 529 C ATOM 835 CZ PHE B 204 182.033 272.326 810.893 1.00119.20 C ANISOU 835 CZ PHE B 204 12949 21100 11242 -431 -3266 601 C ATOM 836 CE2 PHE B 204 182.700 272.831 811.956 1.00120.00 C ANISOU 836 CE2 PHE B 204 12918 21339 11338 -611 -3396 629 C ATOM 837 CD2 PHE B 204 181.996 273.432 813.002 1.00121.82 C ANISOU 837 CD2 PHE B 204 13094 21551 11642 -927 -3438 522 C ATOM 838 O PHE B 204 181.765 271.982 815.829 1.00122.64 O ANISOU 838 O PHE B 204 13242 21973 11381 -1247 -3767 159 O ATOM 839 C ILE B 205 183.522 272.975 817.757 1.00122.93 C ANISOU 839 C ILE B 205 12832 22721 11155 -1318 -4047 355 C ATOM 840 CA ILE B 205 183.418 274.020 816.641 1.00122.80 C ANISOU 840 CA ILE B 205 12777 22475 11407 -1343 -3926 429 C ATOM 841 N ILE B 205 182.038 274.175 816.182 1.00123.14 N ANISOU 841 N ILE B 205 12947 22209 11634 -1497 -3804 221 N ATOM 842 CB ILE B 205 184.011 275.342 817.141 1.00125.28 C ANISOU 842 CB ILE B 205 12791 23042 11766 -1464 -4009 522 C ATOM 843 CG1 ILE B 205 183.275 276.506 816.496 1.00126.69 C ANISOU 843 CG1 ILE B 205 12897 22973 12265 -1630 -3874 465 C ATOM 844 CD1 ILE B 205 183.577 277.842 817.115 1.00129.83 C ANISOU 844 CD1 ILE B 205 12966 23588 12775 -1830 -3951 458 C ATOM 845 CG2 ILE B 205 185.514 275.390 816.873 1.00124.32 C ANISOU 845 CG2 ILE B 205 12570 23077 11590 -1211 -4011 857 C ATOM 846 O ILE B 205 184.388 272.103 817.717 1.00121.47 O ANISOU 846 O ILE B 205 12691 22580 10882 -1084 -4025 536 O ATOM 847 C GLU B 206 182.683 270.625 819.236 1.00157.21 C ANISOU 847 C GLU B 206 17432 27198 15103 -1251 -4111 128 C ATOM 848 CA GLU B 206 182.648 272.043 819.808 1.00160.17 C ANISOU 848 CA GLU B 206 17547 27844 15464 -1474 -4237 35 C ATOM 849 N GLU B 206 182.631 273.040 818.744 1.00159.62 N ANISOU 849 N GLU B 206 17446 27511 15693 -1542 -4143 83 N ATOM 850 CB GLU B 206 181.442 272.216 820.723 1.00162.84 C ANISOU 850 CB GLU B 206 17857 28319 15696 -1740 -4330 -361 C ATOM 851 CG GLU B 206 181.297 273.627 821.254 1.00166.35 C ANISOU 851 CG GLU B 206 18001 29003 16203 -2007 -4444 -561 C ATOM 852 CD GLU B 206 180.422 273.707 822.499 1.00170.06 C ANISOU 852 CD GLU B 206 18342 29808 16463 -2230 -4592 -1001 C ATOM 853 OE1 GLU B 206 179.846 272.664 822.875 1.00169.59 O ANISOU 853 OE1 GLU B 206 18473 29753 16211 -2168 -4584 -1122 O ATOM 854 OE2 GLU B 206 180.314 274.808 823.100 1.00173.71 O ANISOU 854 OE2 GLU B 206 18496 30549 16958 -2463 -4715 -1253 O ATOM 855 O GLU B 206 183.645 269.886 819.459 1.00156.56 O ANISOU 855 O GLU B 206 17324 27226 14934 -1017 -4083 365 O ATOM 856 C SER B 207 182.751 268.583 817.056 1.00129.61 C ANISOU 856 C SER B 207 14341 23004 11900 -873 -3823 213 C ATOM 857 CA SER B 207 181.511 268.952 817.843 1.00131.38 C ANISOU 857 CA SER B 207 14603 23295 12022 -1131 -3894 -27 C ATOM 858 N SER B 207 181.637 270.268 818.484 1.00133.93 N ANISOU 858 N SER B 207 14701 23884 12302 -1317 -4008 -53 N ATOM 859 CB SER B 207 180.305 268.906 816.903 1.00130.39 C ANISOU 859 CB SER B 207 14664 22813 12067 -1209 -3777 -200 C ATOM 860 OG SER B 207 179.096 268.857 817.621 1.00131.91 O ANISOU 860 OG SER B 207 14931 22984 12205 -1421 -3791 -462 O ATOM 861 O SER B 207 183.145 267.413 817.030 1.00128.50 O ANISOU 861 O SER B 207 14267 22785 11773 -697 -3754 267 O ATOM 862 C LEU B 208 185.622 268.857 816.617 1.00117.74 C ANISOU 862 C LEU B 208 12524 21678 10535 -497 -3751 700 C ATOM 863 CA LEU B 208 184.566 269.340 815.649 1.00116.90 C ANISOU 863 CA LEU B 208 12546 21369 10501 -612 -3743 511 C ATOM 864 N LEU B 208 183.348 269.574 816.397 1.00118.09 N ANISOU 864 N LEU B 208 12760 21557 10550 -851 -3814 333 N ATOM 865 CB LEU B 208 185.040 270.617 814.960 1.00117.34 C ANISOU 865 CB LEU B 208 12470 21467 10647 -604 -3734 633 C ATOM 866 CG LEU B 208 186.370 270.409 814.235 1.00116.52 C ANISOU 866 CG LEU B 208 12280 21356 10638 -352 -3657 780 C ATOM 867 CD1 LEU B 208 186.159 269.445 813.066 1.00114.85 C ANISOU 867 CD1 LEU B 208 12203 20926 10510 -180 -3562 610 C ATOM 868 CD2 LEU B 208 186.987 271.697 813.760 1.00117.32 C ANISOU 868 CD2 LEU B 208 12226 21558 10792 -323 -3649 948 C ATOM 869 O LEU B 208 186.042 267.701 816.582 1.00116.97 O ANISOU 869 O LEU B 208 12470 21460 10515 -331 -3649 729 O ATOM 870 C LEU B 209 186.679 268.094 819.062 1.00118.98 C ANISOU 870 C LEU B 209 12445 22367 10395 -333 -3767 1064 C ATOM 871 CA LEU B 209 187.039 269.431 818.472 1.00119.06 C ANISOU 871 CA LEU B 209 12340 22422 10476 -422 -3835 1093 C ATOM 872 CB LEU B 209 187.063 270.509 819.534 1.00121.82 C ANISOU 872 CB LEU B 209 12473 23211 10602 -555 -4000 1154 C ATOM 873 CG LEU B 209 187.441 271.829 818.870 1.00121.94 C ANISOU 873 CG LEU B 209 12362 23216 10752 -638 -4032 1204 C ATOM 874 CD2 LEU B 209 188.957 271.942 818.736 1.00122.10 C ANISOU 874 CD2 LEU B 209 12218 23315 10860 -401 -3934 1550 C ATOM 875 CD1 LEU B 209 186.826 272.998 819.610 1.00124.55 C ANISOU 875 CD1 LEU B 209 12523 23843 10958 -902 -4209 1054 C ATOM 876 N LEU B 209 186.040 269.756 817.490 1.00117.62 N ANISOU 876 N LEU B 209 12319 21975 10395 -573 -3849 839 N ATOM 877 O LEU B 209 187.452 267.142 818.986 1.00118.58 O ANISOU 877 O LEU B 209 12380 22180 10495 -112 -3597 1228 O ATOM 878 C ASN B 210 185.322 265.545 819.186 1.00116.72 C ANISOU 878 C ASN B 210 12522 21677 10148 -244 -3598 820 C ATOM 879 CA ASN B 210 184.970 266.726 820.086 1.00118.92 C ANISOU 879 CA ASN B 210 12682 22370 10133 -421 -3796 793 C ATOM 880 N ASN B 210 185.481 268.007 819.613 1.00119.07 N ANISOU 880 N ASN B 210 12563 22458 10223 -504 -3870 840 N ATOM 881 CB ASN B 210 183.461 266.797 820.252 1.00119.06 C ANISOU 881 CB ASN B 210 12863 22350 10025 -657 -3895 452 C ATOM 882 CG ASN B 210 182.882 265.500 820.687 1.00118.88 C ANISOU 882 CG ASN B 210 12995 22246 9926 -568 -3813 403 C ATOM 883 OD1 ASN B 210 183.444 264.822 821.539 1.00120.25 O ANISOU 883 OD1 ASN B 210 13083 22632 9975 -364 -3745 634 O ATOM 884 ND2 ASN B 210 181.753 265.129 820.100 1.00117.41 N ANISOU 884 ND2 ASN B 210 13027 21754 9829 -692 -3787 141 N ATOM 885 O ASN B 210 186.193 264.747 819.520 1.00117.31 O ANISOU 885 O ASN B 210 12509 21734 10329 -22 -3437 1055 O ATOM 886 C TRP B 211 186.348 264.072 816.878 1.00119.21 C ANISOU 886 C TRP B 211 12897 21271 11126 27 -3288 694 C ATOM 887 CA TRP B 211 184.867 264.409 817.046 1.00118.80 C ANISOU 887 CA TRP B 211 13027 21277 10835 -186 -3441 497 C ATOM 888 N TRP B 211 184.631 265.448 818.053 1.00120.58 N ANISOU 888 N TRP B 211 13177 21849 10788 -332 -3592 575 N ATOM 889 CB TRP B 211 184.251 264.808 815.682 1.00117.18 C ANISOU 889 CB TRP B 211 12926 20887 10709 -252 -3476 272 C ATOM 890 CG TRP B 211 184.781 263.985 814.509 1.00116.00 C ANISOU 890 CG TRP B 211 12756 20506 10812 -72 -3359 153 C ATOM 891 CD1 TRP B 211 184.473 262.689 814.214 1.00115.34 C ANISOU 891 CD1 TRP B 211 12743 20207 10873 4 -3264 -7 C ATOM 892 NE1 TRP B 211 185.160 262.277 813.101 1.00114.98 N ANISOU 892 NE1 TRP B 211 12592 20041 11056 154 -3189 -164 N ATOM 893 CE2 TRP B 211 185.930 263.313 812.648 1.00115.31 C ANISOU 893 CE2 TRP B 211 12514 20221 11078 195 -3227 -87 C ATOM 894 CZ2 TRP B 211 186.785 263.377 811.563 1.00115.50 C ANISOU 894 CZ2 TRP B 211 12393 20238 11254 348 -3181 -227 C ATOM 895 CH2 TRP B 211 187.435 264.555 811.342 1.00115.95 C ANISOU 895 CH2 TRP B 211 12356 20464 11237 374 -3221 -81 C ATOM 896 CZ3 TRP B 211 187.252 265.656 812.180 1.00116.28 C ANISOU 896 CZ3 TRP B 211 12422 20667 11090 235 -3308 190 C ATOM 897 CE3 TRP B 211 186.401 265.596 813.260 1.00116.35 C ANISOU 897 CE3 TRP B 211 12547 20705 10955 67 -3370 274 C ATOM 898 CD2 TRP B 211 185.721 264.404 813.509 1.00115.84 C ANISOU 898 CD2 TRP B 211 12602 20483 10928 55 -3327 139 C ATOM 899 O TRP B 211 186.724 262.904 816.761 1.00119.13 O ANISOU 899 O TRP B 211 12871 21036 11357 172 -3111 690 O ATOM 900 C ILE B 212 189.305 264.165 817.716 1.00125.22 C ANISOU 900 C ILE B 212 13194 22178 12205 411 -2974 1334 C ATOM 901 CA ILE B 212 188.602 264.928 816.607 1.00123.30 C ANISOU 901 CA ILE B 212 13077 21883 11887 236 -3160 1027 C ATOM 902 N ILE B 212 187.183 265.103 816.862 1.00122.70 N ANISOU 902 N ILE B 212 13183 21887 11549 41 -3329 855 N ATOM 903 CB ILE B 212 189.308 266.274 816.399 1.00123.83 C ANISOU 903 CB ILE B 212 13005 22146 11898 220 -3238 1166 C ATOM 904 CG1 ILE B 212 188.776 266.933 815.135 1.00122.30 C ANISOU 904 CG1 ILE B 212 12906 21865 11697 133 -3337 921 C ATOM 905 CD1 ILE B 212 188.849 268.432 815.172 1.00122.97 C ANISOU 905 CD1 ILE B 212 12905 22179 11638 32 -3461 1047 C ATOM 906 CG2 ILE B 212 190.813 266.079 816.263 1.00124.85 C ANISOU 906 CG2 ILE B 212 12935 22189 12313 432 -3029 1363 C ATOM 907 O ILE B 212 189.789 263.056 817.501 1.00125.42 O ANISOU 907 O ILE B 212 13178 21910 12566 559 -2740 1329 O ATOM 908 C ASN B 213 189.601 262.980 820.685 1.00152.68 C ANISOU 908 C ASN B 213 16485 26147 15380 756 -2724 2056 C ATOM 909 CA ASN B 213 190.180 264.218 819.987 1.00151.95 C ANISOU 909 CA ASN B 213 16309 26108 15316 655 -2853 2007 C ATOM 910 N ASN B 213 189.357 264.755 818.903 1.00149.41 N ANISOU 910 N ASN B 213 16164 25633 14971 411 -3058 1601 N ATOM 911 CB ASN B 213 190.479 265.315 821.013 1.00154.27 C ANISOU 911 CB ASN B 213 16423 26951 15242 668 -3000 2284 C ATOM 912 CG ASN B 213 191.123 266.539 820.389 1.00153.84 C ANISOU 912 CG ASN B 213 16261 26945 15245 589 -3095 2291 C ATOM 913 OD1 ASN B 213 191.893 266.434 819.415 1.00152.75 O ANISOU 913 OD1 ASN B 213 16101 26473 15465 661 -2940 2263 O ATOM 914 ND2 ASN B 213 190.803 267.720 820.941 1.00155.01 N ANISOU 914 ND2 ASN B 213 16321 27523 15054 441 -3345 2295 N ATOM 915 O ASN B 213 190.337 262.131 821.188 1.00154.52 O ANISOU 915 O ASN B 213 16586 26293 15832 1016 -2424 2376 O ATOM 916 C ARG B 214 187.976 260.440 820.557 1.00163.85 C ANISOU 916 C ARG B 214 18230 26997 17027 775 -2512 1728 C ATOM 917 CA ARG B 214 187.630 261.712 821.319 1.00164.85 C ANISOU 917 CA ARG B 214 18334 27664 16638 658 -2798 1784 C ATOM 918 N ARG B 214 188.278 262.869 820.704 1.00164.23 N ANISOU 918 N ARG B 214 18156 27636 16607 567 -2912 1760 N ATOM 919 CB ARG B 214 186.104 261.890 821.386 1.00163.80 C ANISOU 919 CB ARG B 214 18426 27622 16189 412 -3042 1432 C ATOM 920 CG ARG B 214 185.396 260.799 822.191 1.00164.88 C ANISOU 920 CG ARG B 214 18658 27796 16191 519 -2941 1478 C ATOM 921 CD ARG B 214 183.894 261.042 822.327 1.00164.27 C ANISOU 921 CD ARG B 214 18790 27818 15809 272 -3164 1113 C ATOM 922 NE ARG B 214 183.580 262.306 822.999 1.00166.02 N ANISOU 922 NE ARG B 214 18924 28519 15635 111 -3422 1016 N ATOM 923 CZ ARG B 214 183.245 262.424 824.283 1.00169.08 C ANISOU 923 CZ ARG B 214 19225 29426 15593 168 -3514 1059 C ATOM 924 NH1 ARG B 214 183.171 261.349 825.055 1.00170.66 N ANISOU 924 NH1 ARG B 214 19436 29740 15667 418 -3351 1263 N ATOM 925 NH2 ARG B 214 182.978 263.622 824.794 1.00170.97 N ANISOU 925 NH2 ARG B 214 19338 30094 15528 -14 -3761 879 N ATOM 926 O ARG B 214 187.739 259.340 821.047 1.00164.77 O ANISOU 926 O ARG B 214 18373 26998 17234 913 -2321 1838 O ATOM 927 C SER B 215 190.100 258.708 818.993 1.00146.04 C ANISOU 927 C SER B 215 15670 23752 16068 1070 -1838 1702 C ATOM 928 CA SER B 215 188.868 259.467 818.497 1.00143.40 C ANISOU 928 CA SER B 215 15577 23610 15299 800 -2240 1349 C ATOM 929 N SER B 215 188.542 260.597 819.363 1.00143.99 N ANISOU 929 N SER B 215 15679 24176 14855 727 -2478 1535 N ATOM 930 CB SER B 215 189.097 259.943 817.067 1.00141.62 C ANISOU 930 CB SER B 215 15348 23217 15243 693 -2346 985 C ATOM 931 OG SER B 215 190.359 260.568 816.958 1.00142.75 O ANISOU 931 OG SER B 215 15291 23398 15551 792 -2247 1161 O ATOM 932 O SER B 215 191.065 258.521 818.247 1.00146.45 O ANISOU 932 O SER B 215 15560 23496 16587 1130 -1645 1605 O ATOM 933 C ASP B 216 192.518 257.866 820.712 1.00227.11 C ANISOU 933 C ASP B 216 25404 33929 26960 1705 -999 2780 C ATOM 934 CA ASP B 216 191.065 257.437 820.914 1.00225.48 C ANISOU 934 CA ASP B 216 25453 33829 26390 1567 -1228 2557 C ATOM 935 N ASP B 216 190.059 258.302 820.269 1.00222.31 N ANISOU 935 N ASP B 216 25285 33614 25571 1251 -1691 2114 N ATOM 936 CB ASP B 216 190.881 255.973 820.488 1.00225.60 C ANISOU 936 CB ASP B 216 25467 33301 26951 1610 -934 2379 C ATOM 937 O ASP B 216 193.424 257.029 820.703 1.00229.40 O ANISOU 937 O ASP B 216 25484 33817 27858 1910 -547 2969 O ATOM 938 C GLY B 217 194.672 260.437 821.486 1.00133.08 C ANISOU 938 C GLY B 217 13098 22777 14691 1925 -1051 3539 C ATOM 939 CA GLY B 217 194.065 259.694 820.301 1.00130.36 C ANISOU 939 CA GLY B 217 12927 21927 14678 1709 -1093 2945 C ATOM 940 N GLY B 217 192.736 259.168 820.559 1.00129.02 N ANISOU 940 N GLY B 217 12980 21836 14204 1596 -1278 2761 N ATOM 941 O GLY B 217 194.343 261.593 821.765 1.00132.44 O ANISOU 941 O GLY B 217 13061 23185 14075 1803 -1411 3544 O ATOM 942 C GLU B 218 197.667 260.384 823.417 1.00279.47 C ANISOU 942 C GLU B 218 30902 41536 33747 2826 -44 5125 C ATOM 943 CA GLU B 218 196.136 260.338 823.404 1.00276.53 C ANISOU 943 CA GLU B 218 30831 41385 32854 2550 -503 4689 C ATOM 944 N GLU B 218 195.585 259.772 822.179 1.00273.25 N ANISOU 944 N GLU B 218 30616 40414 32791 2265 -582 4052 N ATOM 945 CB GLU B 218 195.611 259.566 824.617 1.00279.10 C ANISOU 945 CB GLU B 218 31136 42012 32898 2813 -361 5081 C ATOM 946 O GLU B 218 198.324 259.359 823.602 1.00282.20 O ANISOU 946 O GLU B 218 31077 41461 34685 3094 497 5429 O ATOM 947 C PRO B 219 200.201 261.594 824.773 1.00210.86 C ANISOU 947 C PRO B 219 21575 33410 25130 3509 527 6463 C ATOM 948 CA PRO B 219 199.703 261.640 823.321 1.00206.17 C ANISOU 948 CA PRO B 219 21241 32317 24777 3055 241 5629 C ATOM 949 N PRO B 219 198.245 261.576 823.201 1.00202.97 N ANISOU 949 N PRO B 219 21133 32091 23894 2762 -224 5158 N ATOM 950 CD PRO B 219 197.694 262.756 822.506 1.00199.53 C ANISOU 950 CD PRO B 219 20874 31878 23060 2401 -759 4686 C ATOM 951 CG PRO B 219 198.877 263.293 821.765 1.00199.81 C ANISOU 951 CG PRO B 219 20758 31650 23509 2427 -586 4697 C ATOM 952 CB PRO B 219 200.040 262.988 822.662 1.00204.27 C ANISOU 952 CB PRO B 219 21013 32247 24351 2844 -84 5405 C ATOM 953 O PRO B 219 201.402 261.774 824.983 1.00213.90 O ANISOU 953 O PRO B 219 21693 33729 25850 3788 918 6943 O ATOM 954 C ASP B 220 200.998 261.013 827.704 1.00194.49 C ANISOU 954 C ASP B 220 18948 32394 22554 4587 1220 8199 C ATOM 955 CA ASP B 220 199.637 261.527 827.167 1.00189.41 C ANISOU 955 CA ASP B 220 18660 31927 21381 4055 500 7388 C ATOM 956 N ASP B 220 199.323 261.317 825.739 1.00184.77 N ANISOU 956 N ASP B 220 18329 30602 21272 3614 370 6638 N ATOM 957 CB ASP B 220 198.500 261.044 828.085 1.00190.30 C ANISOU 957 CB ASP B 220 18872 32541 20892 4144 312 7425 C ATOM 958 CG ASP B 220 198.661 261.544 829.531 1.00195.10 C ANISOU 958 CG ASP B 220 19205 34150 20772 4560 270 8059 C ATOM 959 OD1 ASP B 220 199.293 262.607 829.739 1.00196.40 O ANISOU 959 OD1 ASP B 220 19173 34756 20696 4612 134 8264 O ATOM 960 OD2 ASP B 220 198.155 260.876 830.459 1.00197.84 O ANISOU 960 OD2 ASP B 220 19513 34890 20768 4856 370 8350 O ATOM 961 O ASP B 220 201.702 261.746 828.411 1.00197.68 O ANISOU 961 O ASP B 220 19093 33354 22664 4876 1278 8747 O ATOM 962 C GLU B 221 203.789 259.941 827.194 1.00165.02 C ANISOU 962 C GLU B 221 14672 27313 20713 5174 2716 9054 C ATOM 963 CA GLU B 221 202.626 259.212 827.857 1.00164.92 C ANISOU 963 CA GLU B 221 14809 27605 20247 5232 2564 9060 C ATOM 964 N GLU B 221 201.356 259.766 827.396 1.00159.68 N ANISOU 964 N GLU B 221 14499 27227 18946 4728 1789 8290 N ATOM 965 CB GLU B 221 202.710 257.713 827.560 1.00166.21 C ANISOU 965 CB GLU B 221 14946 26912 21294 5329 3158 9050 C ATOM 966 O GLU B 221 204.896 259.992 827.739 1.00169.61 O ANISOU 966 O GLU B 221 14930 27927 21586 5607 3240 9781 O ATOM 967 C GLU B 222 204.680 262.686 825.521 1.00162.75 C ANISOU 967 C GLU B 222 14474 27173 20191 4535 1935 8285 C ATOM 968 CA GLU B 222 204.531 261.197 825.213 1.00163.25 C ANISOU 968 CA GLU B 222 14577 26491 20959 4566 2376 8117 C ATOM 969 N GLU B 222 203.517 260.511 826.019 1.00163.63 N ANISOU 969 N GLU B 222 14727 26865 20580 4669 2276 8258 N ATOM 970 CB GLU B 222 204.264 261.000 823.722 1.00159.03 C ANISOU 970 CB GLU B 222 14264 25290 20868 4100 2189 7189 C ATOM 971 O GLU B 222 205.699 263.283 825.192 1.00163.83 O ANISOU 971 O GLU B 222 14447 27169 20630 4599 2124 8435 O ATOM 972 C TYR B 223 205.021 264.661 827.616 1.00206.89 C ANISOU 972 C TYR B 223 19667 34604 24337 5020 1524 9401 C ATOM 973 CA TYR B 223 203.851 264.645 826.644 1.00201.14 C ANISOU 973 CA TYR B 223 19336 33579 23507 4453 1001 8464 C ATOM 974 N TYR B 223 203.679 263.289 826.148 1.00200.44 N ANISOU 974 N TYR B 223 19371 32723 24063 4431 1365 8234 N ATOM 975 CB TYR B 223 202.589 265.145 827.337 1.00200.09 C ANISOU 975 CB TYR B 223 19326 34251 22449 4296 384 8268 C ATOM 976 CG TYR B 223 201.429 265.331 826.396 1.00194.71 C ANISOU 976 CG TYR B 223 19015 33329 21636 3746 -132 7398 C ATOM 977 CD1 TYR B 223 201.438 266.344 825.447 1.00191.47 C ANISOU 977 CD1 TYR B 223 18716 32800 21233 3385 -467 6939 C ATOM 978 CE1 TYR B 223 200.361 266.519 824.568 1.00186.96 C ANISOU 978 CE1 TYR B 223 18465 32023 20549 2932 -892 6206 C ATOM 979 CZ TYR B 223 199.254 265.668 824.645 1.00185.51 C ANISOU 979 CZ TYR B 223 18500 31739 20246 2815 -1000 5902 C ATOM 980 OH TYR B 223 198.189 265.830 823.768 1.00181.37 O ANISOU 980 OH TYR B 223 18277 31008 19627 2401 -1378 5226 O ATOM 981 CE2 TYR B 223 199.230 264.654 825.598 1.00188.51 C ANISOU 981 CE2 TYR B 223 18784 32232 20609 3149 -693 6322 C ATOM 982 CD2 TYR B 223 200.319 264.496 826.463 1.00193.15 C ANISOU 982 CD2 TYR B 223 19045 33037 21308 3621 -256 7076 C ATOM 983 O TYR B 223 205.887 265.526 827.541 1.00208.04 O ANISOU 983 O TYR B 223 19633 34887 24527 5098 1573 9647 O ATOM 984 C ILE B 224 207.392 262.936 828.961 1.00235.53 C ANISOU 984 C ILE B 224 22567 37696 29227 6283 3326 11255 C ATOM 985 CA ILE B 224 206.104 263.561 829.521 1.00233.28 C ANISOU 985 CA ILE B 224 22458 38354 27824 6080 2527 10962 C ATOM 986 N ILE B 224 205.047 263.677 828.513 1.00227.03 N ANISOU 986 N ILE B 224 22072 37246 26943 5447 1950 9960 N ATOM 987 CB ILE B 224 205.633 262.768 830.766 1.00237.35 C ANISOU 987 CB ILE B 224 22847 39415 27920 6542 2720 11535 C ATOM 988 CG1 ILE B 224 204.390 263.411 831.383 1.00235.92 C ANISOU 988 CG1 ILE B 224 22794 40215 26629 6355 1946 11200 C ATOM 989 CD1 ILE B 224 203.073 262.904 830.822 1.00231.07 C ANISOU 989 CD1 ILE B 224 22584 39276 25935 5880 1549 10382 C ATOM 990 CG2 ILE B 224 206.743 262.700 831.805 1.00244.34 C ANISOU 990 CG2 ILE B 224 23280 40702 28855 7263 3344 12646 C ATOM 991 O ILE B 224 208.480 263.125 829.518 1.00240.30 O ANISOU 991 O ILE B 224 22829 38444 30032 6745 3818 12036 O ATOM 992 C GLU B 225 209.134 262.654 826.307 1.00173.77 C ANISOU 992 C GLU B 225 14782 27800 23441 5789 4017 10334 C ATOM 993 CA GLU B 225 208.425 261.620 827.179 1.00175.67 C ANISOU 993 CA GLU B 225 15023 28205 23519 6038 4180 10667 C ATOM 994 N GLU B 225 207.267 262.200 827.858 1.00173.60 N ANISOU 994 N GLU B 225 14932 28904 22124 5941 3462 10605 N ATOM 995 CB GLU B 225 208.018 260.410 826.335 1.00173.77 C ANISOU 995 CB GLU B 225 14948 27064 24011 5769 4379 10027 C ATOM 996 O GLU B 225 210.138 262.341 825.672 1.00175.51 O ANISOU 996 O GLU B 225 14853 27264 24570 5833 4563 10292 O ATOM 997 C GLN B 226 209.976 265.946 826.590 1.00175.08 C ANISOU 997 C GLN B 226 14768 29408 22348 5744 3177 10717 C ATOM 998 CA GLN B 226 209.233 265.018 825.609 1.00171.18 C ANISOU 998 CA GLN B 226 14587 28183 22271 5350 3095 9881 C ATOM 999 N GLN B 226 208.594 263.875 826.272 1.00172.62 N ANISOU 999 N GLN B 226 14790 28352 22446 5528 3285 10074 N ATOM 1000 CB GLN B 226 208.203 265.815 824.803 1.00165.27 C ANISOU 1000 CB GLN B 226 14184 27647 20964 4796 2285 9038 C ATOM 1001 O GLN B 226 210.957 266.593 826.211 1.00176.06 O ANISOU 1001 O GLN B 226 14747 29366 22782 5795 3370 10854 O ATOM 1002 C VAL B 227 211.412 266.015 829.439 1.00239.75 C ANISOU 1002 C VAL B 227 22112 38918 30066 7115 4075 13032 C ATOM 1003 CA VAL B 227 210.175 266.744 828.908 1.00233.55 C ANISOU 1003 CA VAL B 227 21690 38467 28584 6495 3134 12108 C ATOM 1004 N VAL B 227 209.496 266.010 827.834 1.00228.82 N ANISOU 1004 N VAL B 227 21453 37060 28427 6032 3020 11248 N ATOM 1005 CB VAL B 227 209.219 267.060 830.101 1.00234.88 C ANISOU 1005 CB VAL B 227 21799 39775 27668 6628 2626 12317 C ATOM 1006 CG1 VAL B 227 209.188 268.549 830.417 1.00234.82 C ANISOU 1006 CG1 VAL B 227 21661 40650 26909 6522 2052 12315 C ATOM 1007 CG2 VAL B 227 207.828 266.492 829.862 1.00230.83 C ANISOU 1007 CG2 VAL B 227 21646 39170 26888 6245 2191 11605 C ATOM 1008 O VAL B 227 211.345 265.337 830.460 1.00244.02 O ANISOU 1008 O VAL B 227 22462 39811 30444 7588 4406 13693 O ATOM 1009 C GLU B 241 214.696 273.398 821.783 1.00167.11 C ANISOU 1009 C GLU B 241 13533 28095 21867 4931 2526 9806 C ATOM 1010 CA GLU B 241 214.171 274.029 823.083 1.00168.32 C ANISOU 1010 CA GLU B 241 13539 29200 21215 5048 2153 10373 C ATOM 1011 N GLU B 241 213.168 275.065 822.844 1.00164.54 N ANISOU 1011 N GLU B 241 13239 29229 20048 4662 1403 9937 N ATOM 1012 CB GLU B 241 213.619 272.945 824.024 1.00169.97 C ANISOU 1012 CB GLU B 241 13718 29552 21313 5228 2279 10635 C ATOM 1013 O GLU B 241 215.553 273.977 821.106 1.00167.59 O ANISOU 1013 O GLU B 241 13531 27901 22247 4952 2709 9754 O ATOM 1014 C THR B 242 213.575 271.128 819.280 1.00183.23 C ANISOU 1014 C THR B 242 16165 28583 24873 4300 2552 7830 C ATOM 1015 CA THR B 242 214.647 271.397 820.333 1.00188.02 C ANISOU 1015 CA THR B 242 16426 29377 25637 4727 3028 8780 C ATOM 1016 N THR B 242 214.162 272.220 821.444 1.00188.14 N ANISOU 1016 N THR B 242 16371 30275 24837 4809 2625 9353 N ATOM 1017 CB THR B 242 215.089 270.035 820.853 1.00191.87 C ANISOU 1017 CB THR B 242 16735 29354 26812 5010 3708 9096 C ATOM 1018 OG1 THR B 242 213.933 269.243 821.141 1.00189.84 O ANISOU 1018 OG1 THR B 242 16664 29187 26280 4865 3441 8861 O ATOM 1019 CG2 THR B 242 215.879 270.199 822.129 1.00196.85 C ANISOU 1019 CG2 THR B 242 17023 30330 27442 5495 4145 10166 C ATOM 1020 O THR B 242 212.512 271.751 819.289 1.00179.73 O ANISOU 1020 O THR B 242 15927 28646 23716 4050 1918 7618 O ATOM 1021 C GLN B 243 211.608 269.198 817.932 1.00157.56 C ANISOU 1021 C GLN B 243 13409 24677 21779 3746 2156 6322 C ATOM 1022 CA GLN B 243 212.914 269.747 817.350 1.00159.86 C ANISOU 1022 CA GLN B 243 13513 24699 22529 3883 2511 6352 C ATOM 1023 N GLN B 243 213.855 270.167 818.397 1.00163.68 N ANISOU 1023 N GLN B 243 13716 25378 23096 4232 2890 7259 N ATOM 1024 CB GLN B 243 213.565 268.703 816.434 1.00161.89 C ANISOU 1024 CB GLN B 243 13671 24149 23691 3879 3008 5763 C ATOM 1025 O GLN B 243 210.544 269.815 817.793 1.00153.85 O ANISOU 1025 O GLN B 243 13173 24664 20619 3501 1543 6081 O ATOM 1026 C TYR B 244 209.479 268.281 819.765 1.00223.91 C ANISOU 1026 C TYR B 244 22026 33776 29275 3698 1675 6733 C ATOM 1027 CA TYR B 244 210.515 267.362 819.112 1.00226.59 C ANISOU 1027 CA TYR B 244 22202 33299 30594 3821 2324 6535 C ATOM 1028 N TYR B 244 211.698 268.047 818.595 1.00228.34 N ANISOU 1028 N TYR B 244 22256 33341 31163 3922 2582 6589 N ATOM 1029 CB TYR B 244 210.899 266.208 820.057 1.00230.72 C ANISOU 1029 CB TYR B 244 22510 33532 31623 4145 2935 7086 C ATOM 1030 CG TYR B 244 211.935 266.526 821.139 1.00235.45 C ANISOU 1030 CG TYR B 244 22785 34345 32331 4589 3407 8065 C ATOM 1031 CD1 TYR B 244 211.607 267.313 822.245 1.00235.84 C ANISOU 1031 CD1 TYR B 244 22789 35243 31575 4746 3093 8700 C ATOM 1032 CE1 TYR B 244 212.548 267.586 823.245 1.00240.61 C ANISOU 1032 CE1 TYR B 244 23063 36128 32232 5201 3525 9626 C ATOM 1033 CZ TYR B 244 213.827 267.055 823.155 1.00245.02 C ANISOU 1033 CZ TYR B 244 23347 36038 33712 5505 4330 9968 C ATOM 1034 OH TYR B 244 214.764 267.326 824.143 1.00250.09 O ANISOU 1034 OH TYR B 244 23644 36967 34413 5999 4801 10951 O ATOM 1035 CE2 TYR B 244 214.167 266.252 822.073 1.00244.79 C ANISOU 1035 CE2 TYR B 244 23358 35089 34563 5325 4680 9309 C ATOM 1036 CD2 TYR B 244 213.223 265.986 821.081 1.00240.08 C ANISOU 1036 CD2 TYR B 244 23075 34293 33853 4872 4198 8348 C ATOM 1037 O TYR B 244 208.276 268.084 819.600 1.00220.69 O ANISOU 1037 O TYR B 244 21866 33515 28471 3443 1241 6318 O ATOM 1038 C PHE B 245 208.202 270.964 820.150 1.00163.78 C ANISOU 1038 C PHE B 245 14600 27543 20087 3344 470 6801 C ATOM 1039 CA PHE B 245 209.030 270.205 821.174 1.00168.29 C ANISOU 1039 CA PHE B 245 14897 28046 21000 3750 1033 7488 C ATOM 1040 N PHE B 245 209.941 269.288 820.495 1.00169.96 N ANISOU 1040 N PHE B 245 15028 27466 22082 3872 1622 7337 N ATOM 1041 CB PHE B 245 209.802 271.194 822.050 1.00171.44 C ANISOU 1041 CB PHE B 245 15007 28998 21133 4018 1098 8217 C ATOM 1042 CG PHE B 245 208.916 272.140 822.841 1.00170.67 C ANISOU 1042 CG PHE B 245 14913 29759 20177 3897 509 8338 C ATOM 1043 CD1 PHE B 245 208.061 271.658 823.830 1.00171.44 C ANISOU 1043 CD1 PHE B 245 15017 30289 19833 3948 339 8482 C ATOM 1044 CE1 PHE B 245 207.257 272.527 824.563 1.00171.37 C ANISOU 1044 CE1 PHE B 245 14967 31081 19067 3823 -195 8502 C ATOM 1045 CZ PHE B 245 207.308 273.893 824.321 1.00170.55 C ANISOU 1045 CZ PHE B 245 14801 31312 18687 3635 -546 8409 C ATOM 1046 CE2 PHE B 245 208.155 274.387 823.353 1.00169.61 C ANISOU 1046 CE2 PHE B 245 14688 30762 18995 3602 -369 8338 C ATOM 1047 CD2 PHE B 245 208.957 273.514 822.614 1.00169.68 C ANISOU 1047 CD2 PHE B 245 14749 30008 19712 3738 148 8290 C ATOM 1048 O PHE B 245 206.987 271.107 820.281 1.00161.23 O ANISOU 1048 O PHE B 245 14472 27535 19254 3105 1 6531 O ATOM 1049 C TRP B 246 207.147 271.451 817.355 1.00154.20 C ANISOU 1049 C TRP B 246 13881 25851 18858 2743 -120 5300 C ATOM 1050 CA TRP B 246 208.231 272.225 818.098 1.00157.31 C ANISOU 1050 CA TRP B 246 13997 26501 19272 2990 101 5977 C ATOM 1051 N TRP B 246 208.876 271.433 819.115 1.00160.90 N ANISOU 1051 N TRP B 246 14234 26871 20029 3294 559 6531 N ATOM 1052 CB TRP B 246 209.285 272.789 817.158 1.00158.01 C ANISOU 1052 CB TRP B 246 13998 26329 19709 3063 311 5862 C ATOM 1053 CG TRP B 246 209.950 273.978 817.761 1.00159.83 C ANISOU 1053 CG TRP B 246 14024 26985 19720 3203 301 6450 C ATOM 1054 CD1 TRP B 246 211.289 274.221 817.857 1.00162.99 C ANISOU 1054 CD1 TRP B 246 14178 27241 20511 3473 738 6860 C ATOM 1055 NE1 TRP B 246 211.503 275.427 818.476 1.00163.96 N ANISOU 1055 NE1 TRP B 246 14146 27910 20239 3533 556 7356 N ATOM 1056 CE2 TRP B 246 210.294 275.980 818.800 1.00161.62 C ANISOU 1056 CE2 TRP B 246 13979 28108 19320 3283 -1 7230 C ATOM 1057 CZ2 TRP B 246 209.996 277.180 819.432 1.00161.96 C ANISOU 1057 CZ2 TRP B 246 13903 28784 18851 3213 -361 7524 C ATOM 1058 CH2 TRP B 246 208.679 277.480 819.629 1.00159.75 C ANISOU 1058 CH2 TRP B 246 13769 28844 18085 2921 -860 7233 C ATOM 1059 CZ3 TRP B 246 207.667 276.618 819.209 1.00157.03 C ANISOU 1059 CZ3 TRP B 246 13706 28233 17725 2723 -1003 6712 C ATOM 1060 CE3 TRP B 246 207.959 275.427 818.583 1.00156.53 C ANISOU 1060 CE3 TRP B 246 13764 27581 18127 2804 -671 6448 C ATOM 1061 CD2 TRP B 246 209.295 275.092 818.371 1.00158.97 C ANISOU 1061 CD2 TRP B 246 13906 27521 18973 3078 -159 6682 C ATOM 1062 O TRP B 246 206.000 271.905 817.265 1.00151.47 O ANISOU 1062 O TRP B 246 13729 25811 18010 2502 -590 5061 O ATOM 1063 C LYS B 247 205.287 269.303 817.107 1.00140.63 C ANISOU 1063 C LYS B 247 12519 23715 17199 2485 -268 4539 C ATOM 1064 CA LYS B 247 206.510 269.436 816.185 1.00142.09 C ANISOU 1064 CA LYS B 247 12559 23522 17906 2598 59 4373 C ATOM 1065 N LYS B 247 207.505 270.292 816.812 1.00144.54 N ANISOU 1065 N LYS B 247 12649 24057 18211 2801 237 4981 N ATOM 1066 CB LYS B 247 207.107 268.071 815.846 1.00144.20 C ANISOU 1066 CB LYS B 247 12711 23151 18926 2706 554 4119 C ATOM 1067 O LYS B 247 204.171 269.642 816.707 1.00137.61 O ANISOU 1067 O LYS B 247 12361 23532 16392 2242 -705 4180 O ATOM 1068 C LEU B 248 203.621 269.957 819.592 1.00140.17 C ANISOU 1068 C LEU B 248 12499 24804 15957 2425 -854 5262 C ATOM 1069 CA LEU B 248 204.392 268.675 819.304 1.00141.80 C ANISOU 1069 CA LEU B 248 12626 24395 16857 2622 -320 5249 C ATOM 1070 N LEU B 248 205.499 268.857 818.348 1.00142.50 N ANISOU 1070 N LEU B 248 12609 24079 17455 2688 -38 5100 N ATOM 1071 CB LEU B 248 204.869 268.047 820.622 1.00145.62 C ANISOU 1071 CB LEU B 248 12888 25009 17432 2958 54 5924 C ATOM 1072 CG LEU B 248 204.027 268.193 821.906 1.00146.40 C ANISOU 1072 CG LEU B 248 12982 25769 16873 3002 -222 6261 C ATOM 1073 CD1 LEU B 248 202.523 268.089 821.675 1.00142.93 C ANISOU 1073 CD1 LEU B 248 12842 25443 16021 2667 -697 5721 C ATOM 1074 CD2 LEU B 248 204.463 267.187 822.967 1.00150.35 C ANISOU 1074 CD2 LEU B 248 13282 26266 17576 3393 252 6856 C ATOM 1075 O LEU B 248 202.385 269.966 819.525 1.00137.76 O ANISOU 1075 O LEU B 248 12407 24648 15289 2183 -1225 4921 O ATOM 1076 C LEU B 249 202.558 272.559 819.202 1.00172.32 C ANISOU 1076 C LEU B 249 16678 29632 19166 1984 -1703 5009 C ATOM 1077 CA LEU B 249 203.702 272.311 820.177 1.00176.10 C ANISOU 1077 CA LEU B 249 16866 30238 19805 2329 -1334 5637 C ATOM 1078 N LEU B 249 204.338 271.024 819.942 1.00177.07 N ANISOU 1078 N LEU B 249 16976 29816 20489 2529 -864 5654 N ATOM 1079 CB LEU B 249 204.718 273.429 820.049 1.00177.53 C ANISOU 1079 CB LEU B 249 16842 30574 20038 2431 -1267 5940 C ATOM 1080 CG LEU B 249 205.387 273.701 821.377 1.00181.48 C ANISOU 1080 CG LEU B 249 17023 31570 20361 2714 -1128 6629 C ATOM 1081 CD1 LEU B 249 205.959 275.100 821.372 1.00182.48 C ANISOU 1081 CD1 LEU B 249 16960 32038 20336 2713 -1255 6863 C ATOM 1082 CD2 LEU B 249 204.364 273.531 822.487 1.00182.24 C ANISOU 1082 CD2 LEU B 249 17113 32199 19931 2663 -1416 6686 C ATOM 1083 O LEU B 249 201.449 272.922 819.612 1.00171.38 O ANISOU 1083 O LEU B 249 16650 29845 18621 1774 -2064 4865 O ATOM 1084 C ASN B 250 200.760 271.657 816.728 1.00148.27 C ANISOU 1084 C ASN B 250 14209 25860 16266 1561 -1991 3725 C ATOM 1085 CA ASN B 250 201.888 272.676 816.851 1.00150.14 C ANISOU 1085 CA ASN B 250 14221 26269 16554 1699 -1884 4102 C ATOM 1086 N ASN B 250 202.830 272.344 817.915 1.00153.21 N ANISOU 1086 N ASN B 250 14375 26746 17092 1948 -1587 4629 N ATOM 1087 CB ASN B 250 202.632 272.857 815.529 1.00149.66 C ANISOU 1087 CB ASN B 250 14162 25894 16806 1771 -1728 3843 C ATOM 1088 CG ASN B 250 203.671 273.980 815.587 1.00151.35 C ANISOU 1088 CG ASN B 250 14174 26288 17046 1895 -1641 4210 C ATOM 1089 OD1 ASN B 250 204.744 273.889 814.986 1.00152.53 O ANISOU 1089 OD1 ASN B 250 14219 26177 17557 2067 -1349 4193 O ATOM 1090 ND2 ASN B 250 203.348 275.045 816.316 1.00151.79 N ANISOU 1090 ND2 ASN B 250 14148 26791 16734 1802 -1889 4511 N ATOM 1091 O ASN B 250 199.606 272.038 816.568 1.00146.42 O ANISOU 1091 O ASN B 250 14141 25776 15714 1339 -2310 3482 O ATOM 1092 C GLN B 251 198.997 269.501 817.823 1.00130.11 C ANISOU 1092 C GLN B 251 12163 23447 13824 1462 -2040 3513 C ATOM 1093 CA GLN B 251 200.105 269.278 816.800 1.00130.44 C ANISOU 1093 CA GLN B 251 12121 23082 14358 1597 -1746 3384 C ATOM 1094 N GLN B 251 201.095 270.368 816.821 1.00131.84 N ANISOU 1094 N GLN B 251 12114 23440 14540 1697 -1692 3693 N ATOM 1095 CB GLN B 251 200.773 267.916 817.033 1.00132.32 C ANISOU 1095 CB GLN B 251 12251 22920 15105 1797 -1314 3465 C ATOM 1096 O GLN B 251 197.862 269.095 817.616 1.00128.21 O ANISOU 1096 O GLN B 251 12130 23156 13428 1291 -2228 3183 O ATOM 1097 C LEU B 252 197.472 271.647 819.496 1.00130.12 C ANISOU 1097 C LEU B 252 12103 24545 12791 1124 -2752 3734 C ATOM 1098 CA LEU B 252 198.359 270.497 819.952 1.00131.87 C ANISOU 1098 CA LEU B 252 12221 24587 13299 1428 -2371 4045 C ATOM 1099 N LEU B 252 199.337 270.158 818.925 1.00131.39 N ANISOU 1099 N LEU B 252 12141 24043 13736 1551 -2074 3974 N ATOM 1100 CB LEU B 252 199.066 270.877 821.255 1.00135.50 C ANISOU 1100 CB LEU B 252 12386 25547 13552 1655 -2294 4615 C ATOM 1101 CG LEU B 252 199.532 269.708 822.116 1.00138.04 C ANISOU 1101 CG LEU B 252 12594 25845 14009 1975 -1942 5007 C ATOM 1102 CD1 LEU B 252 199.849 270.199 823.506 1.00141.86 C ANISOU 1102 CD1 LEU B 252 12793 27025 14082 2193 -1976 5534 C ATOM 1103 CD2 LEU B 252 198.449 268.646 822.164 1.00136.59 C ANISOU 1103 CD2 LEU B 252 12639 25484 13776 1878 -1992 4704 C ATOM 1104 O LEU B 252 196.249 271.631 819.672 1.00129.09 O ANISOU 1104 O LEU B 252 12124 24519 12407 912 -2994 3459 O ATOM 1105 C VAL B 253 196.464 273.404 817.284 1.00160.14 C ANISOU 1105 C VAL B 253 16147 28115 16583 724 -3104 3109 C ATOM 1106 CA VAL B 253 197.385 273.814 818.428 1.00163.03 C ANISOU 1106 CA VAL B 253 16233 28848 16862 867 -3046 3571 C ATOM 1107 N VAL B 253 198.104 272.655 818.916 1.00164.19 N ANISOU 1107 N VAL B 253 16322 28873 17189 1118 -2763 3797 N ATOM 1108 CB VAL B 253 198.358 274.924 817.985 1.00163.81 C ANISOU 1108 CB VAL B 253 16160 29011 17070 940 -2991 3783 C ATOM 1109 CG1 VAL B 253 197.605 276.174 817.588 1.00163.22 C ANISOU 1109 CG1 VAL B 253 16101 29066 16849 695 -3241 3613 C ATOM 1110 CG2 VAL B 253 199.334 275.248 819.111 1.00166.95 C ANISOU 1110 CG2 VAL B 253 16257 29786 17392 1126 -2901 4284 C ATOM 1111 O VAL B 253 195.409 274.004 817.085 1.00159.27 O ANISOU 1111 O VAL B 253 16136 28073 16306 498 -3320 2886 O ATOM 1112 C LEU B 254 194.759 271.197 815.955 1.00121.20 C ANISOU 1112 C LEU B 254 11712 22523 11816 624 -3072 2340 C ATOM 1113 CA LEU B 254 196.029 271.867 815.442 1.00122.06 C ANISOU 1113 CA LEU B 254 11650 22623 12103 780 -2936 2520 C ATOM 1114 N LEU B 254 196.856 272.373 816.542 1.00124.39 N ANISOU 1114 N LEU B 254 11716 23206 12342 866 -2888 2958 N ATOM 1115 CB LEU B 254 196.814 270.907 814.537 1.00121.79 C ANISOU 1115 CB LEU B 254 11614 22224 12435 968 -2681 2330 C ATOM 1116 CG LEU B 254 197.993 271.493 813.748 1.00122.60 C ANISOU 1116 CG LEU B 254 11575 22270 12736 1126 -2533 2376 C ATOM 1117 CD1 LEU B 254 198.542 270.512 812.731 1.00122.62 C ANISOU 1117 CD1 LEU B 254 11570 21929 13093 1268 -2319 2011 C ATOM 1118 CD2 LEU B 254 197.568 272.760 813.058 1.00121.80 C ANISOU 1118 CD2 LEU B 254 11517 22356 12407 1044 -2726 2335 C ATOM 1119 O LEU B 254 193.658 271.601 815.590 1.00120.00 O ANISOU 1119 O LEU B 254 11703 22389 11504 441 -3253 2116 O ATOM 1120 C ARG B 255 192.901 270.331 818.275 1.00121.90 C ANISOU 1120 C ARG B 255 11911 23012 11393 407 -3316 2350 C ATOM 1121 CA ARG B 255 193.781 269.456 817.366 1.00120.99 C ANISOU 1121 CA ARG B 255 11813 22490 11668 607 -3046 2320 C ATOM 1122 N ARG B 255 194.921 270.193 816.816 1.00121.53 N ANISOU 1122 N ARG B 255 11726 22545 11907 719 -2948 2471 N ATOM 1123 CB ARG B 255 194.241 268.177 818.088 1.00122.28 C ANISOU 1123 CB ARG B 255 11920 22544 11996 805 -2800 2510 C ATOM 1124 O ARG B 255 192.031 269.830 818.990 1.00122.20 O ANISOU 1124 O ARG B 255 12035 23159 11238 328 -3401 2262 O ATOM 1125 C GLY B 256 192.658 272.535 820.526 1.00127.55 C ANISOU 1125 C GLY B 256 12199 24810 11454 192 -3736 2654 C ATOM 1126 CA GLY B 256 192.359 272.579 819.035 1.00124.54 C ANISOU 1126 CA GLY B 256 12033 23942 11345 103 -3684 2395 C ATOM 1127 N GLY B 256 193.115 271.642 818.220 1.00123.04 N ANISOU 1127 N GLY B 256 11927 23374 11448 319 -3440 2436 N ATOM 1128 O GLY B 256 191.997 273.214 821.317 1.00129.43 O ANISOU 1128 O GLY B 256 12327 25433 11418 12 -3959 2542 O ATOM 1129 C LEU B 257 194.837 272.670 822.846 1.00135.58 C ANISOU 1129 C LEU B 257 12589 26783 12142 746 -3561 3639 C ATOM 1130 CA LEU B 257 193.962 271.532 822.320 1.00132.92 C ANISOU 1130 CA LEU B 257 12575 25995 11935 669 -3501 3317 C ATOM 1131 N LEU B 257 193.644 271.730 820.912 1.00129.63 N ANISOU 1131 N LEU B 257 12375 25075 11804 486 -3509 2990 N ATOM 1132 CB LEU B 257 194.671 270.191 822.534 1.00133.42 C ANISOU 1132 CB LEU B 257 12643 25846 12206 997 -3155 3622 C ATOM 1133 CG LEU B 257 193.919 268.880 822.265 1.00131.62 C ANISOU 1133 CG LEU B 257 12671 25234 12106 983 -3054 3383 C ATOM 1134 CD1 LEU B 257 194.778 267.680 822.677 1.00133.26 C ANISOU 1134 CD1 LEU B 257 12786 25278 12571 1340 -2658 3775 C ATOM 1135 CD2 LEU B 257 192.572 268.836 822.982 1.00132.07 C ANISOU 1135 CD2 LEU B 257 12828 25601 11750 805 -3316 3122 C ATOM 1136 O LEU B 257 196.047 272.501 823.023 1.00136.98 O ANISOU 1136 O LEU B 257 12598 26988 12461 1039 -3317 4075 O ATOM 1137 C LEU B 258 195.472 275.156 824.837 1.00161.66 C ANISOU 1137 C LEU B 258 15125 31538 14760 731 -3993 4009 C ATOM 1138 CA LEU B 258 194.947 275.049 823.414 1.00157.27 C ANISOU 1138 CA LEU B 258 14917 30254 14585 497 -3948 3648 C ATOM 1139 N LEU B 258 194.212 273.818 823.109 1.00154.97 N ANISOU 1139 N LEU B 258 14937 29577 14367 484 -3861 3420 N ATOM 1140 CB LEU B 258 194.106 276.280 823.076 1.00157.12 C ANISOU 1140 CB LEU B 258 14871 30266 14561 117 -4212 3260 C ATOM 1141 CG LEU B 258 194.236 276.803 821.640 1.00154.18 C ANISOU 1141 CG LEU B 258 14658 29354 14570 13 -4116 3171 C ATOM 1142 CD1 LEU B 258 193.722 278.230 821.579 1.00155.53 C ANISOU 1142 CD1 LEU B 258 14661 29673 14758 -285 -4314 2968 C ATOM 1143 CD2 LEU B 258 195.676 276.731 821.108 1.00153.63 C ANISOU 1143 CD2 LEU B 258 14531 29111 14732 305 -3861 3578 C ATOM 1144 O LEU B 258 196.614 275.565 825.055 1.00163.47 O ANISOU 1144 O LEU B 258 15110 31978 15024 961 -3868 4447 O ATOM 1145 C SER B 259 196.265 273.913 827.367 1.00152.51 C ANISOU 1145 C SER B 259 13526 31521 12901 1461 -3811 4813 C ATOM 1146 CA SER B 259 195.068 274.846 827.192 1.00151.82 C ANISOU 1146 CA SER B 259 13481 31526 12675 980 -4217 4169 C ATOM 1147 N SER B 259 194.636 274.811 825.806 1.00147.07 N ANISOU 1147 N SER B 259 13235 30118 12525 698 -4166 3831 N ATOM 1148 CB SER B 259 193.933 274.446 828.127 1.00153.92 C ANISOU 1148 CB SER B 259 13744 32247 12493 907 -4436 3832 C ATOM 1149 OG SER B 259 194.342 274.536 829.480 1.00159.15 O ANISOU 1149 OG SER B 259 14019 33814 12638 1222 -4507 4148 O ATOM 1150 O SER B 259 197.258 274.272 827.999 1.00155.81 O ANISOU 1150 O SER B 259 13616 32400 13184 1761 -3714 5309 O ATOM 1151 C GLN B 260 198.542 272.461 826.200 1.00155.77 C ANISOU 1151 C GLN B 260 14062 30845 14281 2047 -2904 5666 C ATOM 1152 CA GLN B 260 197.293 271.783 826.779 1.00155.87 C ANISOU 1152 CA GLN B 260 14219 31055 13948 1954 -3086 5360 C ATOM 1153 N GLN B 260 196.171 272.720 826.783 1.00155.23 N ANISOU 1153 N GLN B 260 14176 31244 13561 1537 -3547 4806 N ATOM 1154 CB GLN B 260 196.946 270.510 825.995 1.00152.56 C ANISOU 1154 CB GLN B 260 14144 29885 13935 1924 -2851 5160 C ATOM 1155 O GLN B 260 199.579 272.533 826.853 1.00159.14 O ANISOU 1155 O GLN B 260 14195 31600 14671 2409 -2679 6242 O ATOM 1156 C ALA B 261 200.218 274.585 825.353 1.00206.48 C ANISOU 1156 C ALA B 261 20158 37282 21012 2005 -2900 5976 C ATOM 1157 CA ALA B 261 199.511 273.702 824.341 1.00202.31 C ANISOU 1157 CA ALA B 261 20032 36042 20795 1808 -2843 5516 C ATOM 1158 N ALA B 261 198.423 272.971 824.979 1.00202.52 N ANISOU 1158 N ALA B 261 20175 36254 20517 1748 -2986 5299 N ATOM 1159 CB ALA B 261 198.983 274.535 823.176 1.00198.99 C ANISOU 1159 CB ALA B 261 19799 35292 20517 1434 -3069 5035 C ATOM 1160 O ALA B 261 201.377 274.343 825.680 1.00208.83 O ANISOU 1160 O ALA B 261 20254 37627 21467 2376 -2557 6533 O ATOM 1161 C ILE B 262 200.802 275.844 827.947 1.00157.03 C ANISOU 1161 C ILE B 262 13067 32831 13767 2416 -3181 6705 C ATOM 1162 CA ILE B 262 200.087 276.553 826.810 1.00152.88 C ANISOU 1162 CA ILE B 262 12797 31814 13477 1913 -3435 6085 C ATOM 1163 N ILE B 262 199.508 275.600 825.854 1.00148.57 N ANISOU 1163 N ILE B 262 12680 30501 13268 1762 -3313 5732 N ATOM 1164 CB ILE B 262 199.042 277.496 827.433 1.00154.75 C ANISOU 1164 CB ILE B 262 12864 32665 13269 1587 -3921 5641 C ATOM 1165 CG1 ILE B 262 198.018 277.962 826.407 1.00150.96 C ANISOU 1165 CG1 ILE B 262 12671 31659 13027 1098 -4126 5003 C ATOM 1166 CD1 ILE B 262 197.187 279.120 826.914 1.00153.40 C ANISOU 1166 CD1 ILE B 262 12738 32479 13067 754 -4533 4580 C ATOM 1167 CG2 ILE B 262 199.725 278.699 828.019 1.00158.54 C ANISOU 1167 CG2 ILE B 262 12900 33790 13547 1660 -4056 5909 C ATOM 1168 O ILE B 262 201.977 276.080 828.191 1.00159.46 O ANISOU 1168 O ILE B 262 13118 33304 14167 2743 -2929 7273 O ATOM 1169 C GLY B 263 202.052 273.701 829.397 1.00178.11 C ANISOU 1169 C GLY B 263 15506 35754 16413 3427 -2369 7897 C ATOM 1170 CA GLY B 263 200.655 274.199 829.719 1.00177.62 C ANISOU 1170 CA GLY B 263 15503 36149 15835 3035 -2934 7248 C ATOM 1171 N GLY B 263 200.076 274.982 828.648 1.00173.41 N ANISOU 1171 N GLY B 263 15201 35150 15536 2505 -3221 6625 N ATOM 1172 O GLY B 263 202.940 273.777 830.237 1.00182.63 O ANISOU 1172 O GLY B 263 15722 36852 16817 3875 -2145 8559 O ATOM 1173 C CYS B 264 204.545 273.669 827.349 1.00224.15 C ANISOU 1173 C CYS B 264 21431 40045 23691 3613 -1485 8401 C ATOM 1174 CA CYS B 264 203.540 272.621 827.784 1.00223.78 C ANISOU 1174 CA CYS B 264 21560 40031 23436 3604 -1543 8195 C ATOM 1175 N CYS B 264 202.251 273.197 828.180 1.00223.17 N ANISOU 1175 N CYS B 264 21533 40505 22757 3272 -2123 7695 N ATOM 1176 CB CYS B 264 203.344 271.603 826.668 1.00219.77 C ANISOU 1176 CB CYS B 264 21418 38559 23527 3439 -1309 7811 C ATOM 1177 SG CYS B 264 202.106 270.375 827.084 1.00219.01 S ANISOU 1177 SG CYS B 264 21549 38439 23224 3398 -1380 7541 S ATOM 1178 O CYS B 264 205.729 273.375 827.193 1.00225.74 O ANISOU 1178 O CYS B 264 21505 39916 24350 3929 -993 8882 O ATOM 1179 C ILE B 265 205.599 276.537 828.077 1.00191.89 C ANISOU 1179 C ILE B 265 16664 37214 19033 3642 -1923 8876 C ATOM 1180 CA ILE B 265 204.921 276.022 826.807 1.00186.34 C ANISOU 1180 CA ILE B 265 16434 35629 18738 3259 -1954 8225 C ATOM 1181 N ILE B 265 204.063 274.887 827.136 1.00185.72 N ANISOU 1181 N ILE B 265 16548 35483 18535 3263 -1956 8030 N ATOM 1182 CB ILE B 265 204.114 277.177 826.163 1.00183.53 C ANISOU 1182 CB ILE B 265 16192 35293 18248 2760 -2443 7623 C ATOM 1183 CG1 ILE B 265 203.324 276.667 824.960 1.00178.51 C ANISOU 1183 CG1 ILE B 265 16001 33901 17923 2426 -2491 7005 C ATOM 1184 CD1 ILE B 265 202.216 277.596 824.501 1.00176.26 C ANISOU 1184 CD1 ILE B 265 15839 33671 17461 1961 -2947 6420 C ATOM 1185 CG2 ILE B 265 205.029 278.320 825.771 1.00184.18 C ANISOU 1185 CG2 ILE B 265 16080 35403 18498 2774 -2405 7848 C ATOM 1186 O ILE B 265 206.752 276.976 828.056 1.00193.88 O ANISOU 1186 O ILE B 265 16688 37478 19498 3894 -1648 9371 O ATOM 1187 C GLU B 266 206.743 276.420 830.787 1.00179.66 C ANISOU 1187 C GLU B 266 14240 37378 16646 4681 -1622 10306 C ATOM 1188 CA GLU B 266 205.331 276.919 830.479 1.00176.31 C ANISOU 1188 CA GLU B 266 14041 37024 15924 4089 -2244 9414 C ATOM 1189 N GLU B 266 204.862 276.464 829.183 1.00170.42 N ANISOU 1189 N GLU B 266 13782 35266 15705 3704 -2203 8860 N ATOM 1190 CB GLU B 266 204.361 276.468 831.574 1.00179.06 C ANISOU 1190 CB GLU B 266 14294 38118 15621 4173 -2510 9277 C ATOM 1191 O GLU B 266 207.427 276.971 831.658 1.00184.58 O ANISOU 1191 O GLU B 266 14426 38770 16937 5046 -1578 10879 O ATOM 1192 C ARG B 267 209.662 275.926 830.262 1.00205.76 C ANISOU 1192 C ARG B 267 17285 39760 21133 5488 -325 11684 C ATOM 1193 CA ARG B 267 208.538 274.863 830.269 1.00203.45 C ANISOU 1193 CA ARG B 267 17308 39243 20752 5323 -440 11231 C ATOM 1194 N ARG B 267 207.191 275.395 830.072 1.00200.11 N ANISOU 1194 N ARG B 267 17094 39050 19890 4784 -1121 10418 N ATOM 1195 CB ARG B 267 208.832 273.768 829.240 1.00200.27 C ANISOU 1195 CB ARG B 267 17238 37677 21180 5269 44 11068 C ATOM 1196 O ARG B 267 210.227 276.258 831.307 1.00211.11 O ANISOU 1196 O ARG B 267 17534 41247 21431 5931 -227 12357 O ATOM 1197 C SER B 268 210.992 278.692 828.401 1.00264.59 C ANISOU 1197 C SER B 268 24674 46729 29130 4953 -572 11393 C ATOM 1198 CA SER B 268 211.194 277.257 828.913 1.00266.70 C ANISOU 1198 CA SER B 268 24952 46799 29583 5355 -81 11793 C ATOM 1199 N SER B 268 209.973 276.467 829.088 1.00264.74 N ANISOU 1199 N SER B 268 24954 46564 29073 5159 -339 11325 N ATOM 1200 CB SER B 268 212.145 276.514 827.969 1.00265.48 C ANISOU 1200 CB SER B 268 24966 45588 30317 5475 564 11900 C ATOM 1201 OG SER B 268 211.439 275.929 826.882 1.00260.31 O ANISOU 1201 OG SER B 268 24755 44159 29994 5061 456 11127 O ATOM 1202 O SER B 268 211.892 279.261 827.776 1.00264.32 O ANISOU 1202 O SER B 268 24591 46354 29483 4982 -354 11558 O ATOM 1203 C ASP B 269 210.575 281.620 828.305 1.00198.71 C ANISOU 1203 C ASP B 269 15987 39339 20175 4376 -1524 10956 C ATOM 1204 CA ASP B 269 209.476 280.581 828.120 1.00195.61 C ANISOU 1204 CA ASP B 269 15968 38604 19750 4159 -1641 10426 C ATOM 1205 N ASP B 269 209.830 279.276 828.677 1.00197.71 N ANISOU 1205 N ASP B 269 16225 38788 20107 4590 -1196 10877 N ATOM 1206 CB ASP B 269 208.159 281.087 828.720 1.00195.94 C ANISOU 1206 CB ASP B 269 15941 39321 19185 3821 -2265 9907 C ATOM 1207 CG ASP B 269 207.766 282.462 828.202 1.00194.46 C ANISOU 1207 CG ASP B 269 15711 39198 18978 3377 -2676 9463 C ATOM 1208 OD1 ASP B 269 208.593 283.395 828.267 1.00196.64 O ANISOU 1208 OD1 ASP B 269 15689 39729 19297 3492 -2630 9820 O ATOM 1209 OD2 ASP B 269 206.620 282.617 827.739 1.00191.39 O ANISOU 1209 OD2 ASP B 269 15569 38594 18556 2926 -3018 8780 O ATOM 1210 O ASP B 269 211.066 282.185 827.329 1.00196.40 O ANISOU 1210 O ASP B 269 15810 38523 20291 4229 -1424 10858 O ATOM 1211 C LEU B 270 212.861 283.409 828.847 1.00214.87 C ANISOU 1211 C LEU B 270 17252 42095 22294 4941 -1172 12176 C ATOM 1212 CA LEU B 270 211.854 282.959 829.934 1.00216.98 C ANISOU 1212 CA LEU B 270 17404 43113 21925 4956 -1518 12024 C ATOM 1213 N LEU B 270 210.961 281.852 829.560 1.00213.29 N ANISOU 1213 N LEU B 270 17371 42102 21566 4756 -1529 11530 N ATOM 1214 CB LEU B 270 212.532 282.656 831.272 1.00223.49 C ANISOU 1214 CB LEU B 270 17759 44792 22366 5584 -1269 12859 C ATOM 1215 CG LEU B 270 211.490 282.167 832.287 1.00225.66 C ANISOU 1215 CG LEU B 270 17938 45828 21974 5616 -1615 12648 C ATOM 1216 CD1 LEU B 270 212.047 282.170 833.704 1.00233.06 C ANISOU 1216 CD1 LEU B 270 18308 47904 22339 6244 -1502 13435 C ATOM 1217 CD2 LEU B 270 210.216 282.999 832.221 1.00223.77 C ANISOU 1217 CD2 LEU B 270 17738 45923 21361 5014 -2338 11765 C ATOM 1218 O LEU B 270 212.544 284.307 828.050 1.00211.89 O ANISOU 1218 O LEU B 270 17002 41476 22032 4528 -1461 11707 O ATOM 1219 C LEU B 271 215.948 281.917 827.378 1.00190.85 C ANISOU 1219 C LEU B 271 14409 37113 20991 5753 590 13261 C ATOM 1220 CA LEU B 271 214.994 283.074 827.704 1.00190.17 C ANISOU 1220 CA LEU B 271 14210 37798 20247 5386 -157 12882 C ATOM 1221 N LEU B 271 214.050 282.801 828.803 1.00192.12 N ANISOU 1221 N LEU B 271 14314 38838 19845 5397 -532 12821 N ATOM 1222 CB LEU B 271 215.786 284.371 827.946 1.00193.19 C ANISOU 1222 CB LEU B 271 14200 38681 20521 5516 -197 13326 C ATOM 1223 CG LEU B 271 215.180 285.674 827.408 1.00190.70 C ANISOU 1223 CG LEU B 271 13914 38502 20040 5025 -746 12783 C ATOM 1224 CD1 LEU B 271 216.258 286.743 827.176 1.00192.63 C ANISOU 1224 CD1 LEU B 271 13894 38805 20491 5175 -566 13224 C ATOM 1225 CD2 LEU B 271 214.406 285.372 826.120 1.00184.64 C ANISOU 1225 CD2 LEU B 271 13683 36887 19586 4568 -874 11983 C ATOM 1226 O LEU B 271 216.583 281.894 826.315 1.00188.75 O ANISOU 1226 O LEU B 271 14339 36054 21323 5689 909 13111 O ATOM 1227 C CYS B 278 210.077 288.297 822.768 1.00219.96 C ANISOU 1227 C CYS B 278 19059 40473 24043 2515 -2516 9208 C ATOM 1228 CA CYS B 278 211.309 288.816 822.032 1.00220.13 C ANISOU 1228 CA CYS B 278 19043 40184 24413 2747 -2164 9590 C ATOM 1229 N CYS B 278 212.540 288.258 822.579 1.00222.74 N ANISOU 1229 N CYS B 278 19204 40610 24820 3193 -1775 10193 N ATOM 1230 CB CYS B 278 211.209 288.524 820.533 1.00215.96 C ANISOU 1230 CB CYS B 278 18956 38873 24226 2669 -1987 9220 C ATOM 1231 SG CYS B 278 212.510 289.319 819.526 1.00216.29 S ANISOU 1231 SG CYS B 278 18958 38578 24642 2904 -1620 9547 S ATOM 1232 O CYS B 278 209.024 288.099 822.170 1.00216.87 O ANISOU 1232 O CYS B 278 18970 39754 23677 2210 -2696 8661 O ATOM 1233 C ALA B 279 207.854 288.461 824.682 1.00228.64 C ANISOU 1233 C ALA B 279 19822 42708 24342 2015 -3363 8551 C ATOM 1234 CA ALA B 279 209.125 287.652 824.933 1.00229.76 C ANISOU 1234 CA ALA B 279 19938 42818 24542 2520 -2937 9184 C ATOM 1235 N ALA B 279 210.225 288.084 824.073 1.00228.96 N ANISOU 1235 N ALA B 279 19873 42280 24841 2694 -2595 9518 N ATOM 1236 CB ALA B 279 209.536 287.733 826.412 1.00235.19 C ANISOU 1236 CB ALA B 279 20133 44438 24791 2810 -3017 9642 C ATOM 1237 O ALA B 279 206.738 287.957 824.831 1.00227.36 O ANISOU 1237 O ALA B 279 19837 42528 24021 1777 -3585 8073 O ATOM 1238 C VAL B 280 205.865 290.032 823.166 1.00200.18 C ANISOU 1238 C VAL B 280 16461 38470 21129 1143 -3778 7501 C ATOM 1239 CA VAL B 280 206.923 290.635 824.086 1.00204.64 C ANISOU 1239 CA VAL B 280 16532 39695 21526 1399 -3767 8033 C ATOM 1240 N VAL B 280 208.036 289.719 824.292 1.00204.76 N ANISOU 1240 N VAL B 280 16607 39698 21493 1863 -3435 8567 N ATOM 1241 CB VAL B 280 207.409 291.986 823.515 1.00205.54 C ANISOU 1241 CB VAL B 280 16439 39714 21943 1328 -3711 8204 C ATOM 1242 CG1 VAL B 280 206.316 293.036 823.627 1.00207.16 C ANISOU 1242 CG1 VAL B 280 16419 40072 22220 865 -4040 7713 C ATOM 1243 CG2 VAL B 280 208.669 292.449 824.242 1.00209.47 C ANISOU 1243 CG2 VAL B 280 16503 40762 22323 1665 -3606 8831 C ATOM 1244 O VAL B 280 204.671 290.280 823.331 1.00200.37 O ANISOU 1244 O VAL B 280 16474 38560 21098 781 -4057 6995 O ATOM 1245 C SER B 281 204.886 287.223 821.884 1.00205.29 C ANISOU 1245 C SER B 281 18149 37969 21881 1203 -3502 6959 C ATOM 1246 CA SER B 281 205.394 288.542 821.297 1.00206.07 C ANISOU 1246 CA SER B 281 18070 38009 22218 1166 -3449 7134 C ATOM 1247 N SER B 281 206.309 289.230 822.204 1.00210.13 N ANISOU 1247 N SER B 281 18126 39109 22606 1341 -3462 7598 N ATOM 1248 CB SER B 281 206.075 288.276 819.953 1.00203.03 C ANISOU 1248 CB SER B 281 17999 36991 22153 1365 -3107 7237 C ATOM 1249 OG SER B 281 206.935 287.150 820.036 1.00202.55 O ANISOU 1249 OG SER B 281 18056 36785 22120 1695 -2829 7481 O ATOM 1250 O SER B 281 203.685 286.958 821.889 1.00204.06 O ANISOU 1250 O SER B 281 18155 37737 21640 926 -3708 6491 O ATOM 1251 C PHE B 282 204.324 285.410 824.004 1.00264.26 C ANISOU 1251 C PHE B 282 25513 46210 28682 1397 -3678 6970 C ATOM 1252 CA PHE B 282 205.423 285.141 823.000 1.00262.08 C ANISOU 1252 CA PHE B 282 25430 45354 28796 1654 -3273 7289 C ATOM 1253 N PHE B 282 205.803 286.395 822.368 1.00262.25 N ANISOU 1253 N PHE B 282 25324 45292 29025 1562 -3274 7362 N ATOM 1254 CB PHE B 282 206.614 284.524 823.726 1.00264.71 C ANISOU 1254 CB PHE B 282 25570 45924 29083 2107 -2969 7898 C ATOM 1255 CG PHE B 282 207.852 284.445 822.890 1.00263.80 C ANISOU 1255 CG PHE B 282 25535 45313 29386 2370 -2546 8234 C ATOM 1256 CD1 PHE B 282 207.975 283.477 821.903 1.00260.59 C ANISOU 1256 CD1 PHE B 282 25499 44192 29322 2425 -2268 8035 C ATOM 1257 CE1 PHE B 282 209.124 283.401 821.127 1.00260.30 C ANISOU 1257 CE1 PHE B 282 25504 43710 29688 2659 -1871 8260 C ATOM 1258 CZ PHE B 282 210.164 284.302 821.340 1.00262.99 C ANISOU 1258 CZ PHE B 282 25539 44293 30092 2853 -1731 8746 C ATOM 1259 CE2 PHE B 282 210.048 285.268 822.322 1.00266.01 C ANISOU 1259 CE2 PHE B 282 25555 45389 30127 2810 -2007 8999 C ATOM 1260 CD2 PHE B 282 208.898 285.334 823.089 1.00266.53 C ANISOU 1260 CD2 PHE B 282 25556 45921 29791 2565 -2420 8716 C ATOM 1261 O PHE B 282 203.206 284.911 823.869 1.00262.32 O ANISOU 1261 O PHE B 282 25514 45778 28376 1157 -3833 6497 O ATOM 1262 C ASP B 283 202.388 286.965 825.329 1.00218.79 C ANISOU 1262 C ASP B 283 19238 41418 22475 728 -4454 6178 C ATOM 1263 CA ASP B 283 203.686 286.603 826.021 1.00221.28 C ANISOU 1263 CA ASP B 283 19326 42157 22595 1210 -4253 6846 C ATOM 1264 N ASP B 283 204.654 286.207 825.013 1.00218.18 N ANISOU 1264 N ASP B 283 19210 41106 22583 1455 -3846 7209 N ATOM 1265 CB ASP B 283 204.203 287.801 826.825 1.00226.24 C ANISOU 1265 CB ASP B 283 19384 43536 23039 1243 -4430 7076 C ATOM 1266 CG ASP B 283 205.367 287.437 827.736 1.00229.78 C ANISOU 1266 CG ASP B 283 19533 44572 23201 1759 -4251 7765 C ATOM 1267 OD1 ASP B 283 205.761 286.253 827.744 1.00228.46 O ANISOU 1267 OD1 ASP B 283 19603 44171 23031 2080 -3957 8065 O ATOM 1268 OD2 ASP B 283 205.888 288.332 828.444 1.00234.20 O ANISOU 1268 OD2 ASP B 283 19598 45823 23566 1858 -4377 8024 O ATOM 1269 O ASP B 283 201.322 286.453 825.669 1.00218.54 O ANISOU 1269 O ASP B 283 19325 41448 22261 534 -4640 5738 O ATOM 1270 C ALA B 284 200.533 287.134 822.970 1.00226.82 C ANISOU 1270 C ALA B 284 20996 41009 24176 107 -4406 5297 C ATOM 1271 CA ALA B 284 201.327 288.290 823.589 1.00230.88 C ANISOU 1271 CA ALA B 284 21012 42064 24649 158 -4485 5605 C ATOM 1272 N ALA B 284 202.493 287.839 824.333 1.00232.79 N ANISOU 1272 N ALA B 284 21069 42746 24634 567 -4375 6140 N ATOM 1273 CB ALA B 284 201.728 289.303 822.528 1.00229.84 C ANISOU 1273 CB ALA B 284 20883 41520 24926 111 -4321 5750 C ATOM 1274 O ALA B 284 199.319 287.051 823.149 1.00226.85 O ANISOU 1274 O ALA B 284 21067 40992 24133 -194 -4595 4807 O ATOM 1275 C VAL B 285 199.636 284.370 822.587 1.00164.11 C ANISOU 1275 C VAL B 285 13830 32441 16082 260 -4241 4983 C ATOM 1276 CA VAL B 285 200.553 285.101 821.608 1.00163.09 C ANISOU 1276 CA VAL B 285 13693 31998 16275 374 -4030 5273 C ATOM 1277 N VAL B 285 201.213 286.254 822.238 1.00166.78 N ANISOU 1277 N VAL B 285 13714 32964 16689 393 -4117 5555 N ATOM 1278 CB VAL B 285 201.584 284.105 821.026 1.00160.89 C ANISOU 1278 CB VAL B 285 13642 31355 16132 738 -3695 5587 C ATOM 1279 CG1 VAL B 285 201.029 282.688 821.019 1.00158.73 C ANISOU 1279 CG1 VAL B 285 13681 30838 15792 774 -3647 5364 C ATOM 1280 CG2 VAL B 285 202.007 284.533 819.632 1.00158.59 C ANISOU 1280 CG2 VAL B 285 13521 30559 16176 786 -3494 5612 C ATOM 1281 O VAL B 285 198.470 284.110 822.293 1.00162.48 O ANISOU 1281 O VAL B 285 13847 31980 15908 5 -4343 4535 O ATOM 1282 C SER B 286 198.166 284.224 825.181 1.00171.64 C ANISOU 1282 C SER B 286 14310 34662 16243 8 -4823 4470 C ATOM 1283 CA SER B 286 199.404 283.404 824.806 1.00169.69 C ANISOU 1283 CA SER B 286 14228 34160 16085 440 -4480 5040 C ATOM 1284 N SER B 286 200.174 284.055 823.760 1.00167.91 N ANISOU 1284 N SER B 286 14051 33506 16241 481 -4284 5266 N ATOM 1285 CB SER B 286 200.294 283.159 826.023 1.00173.67 C ANISOU 1285 CB SER B 286 14386 35376 16224 815 -4453 5526 C ATOM 1286 OG SER B 286 201.580 282.724 825.619 1.00172.65 O ANISOU 1286 OG SER B 286 14321 34966 16312 1191 -4081 6088 O ATOM 1287 O SER B 286 197.106 283.665 825.460 1.00171.32 O ANISOU 1287 O SER B 286 14418 34617 16059 -164 -4956 4055 O ATOM 1288 C ASP B 287 196.093 286.196 824.327 1.00181.46 C ANISOU 1288 C ASP B 287 15461 35441 18044 -886 -5102 3468 C ATOM 1289 CA ASP B 287 197.168 286.433 825.389 1.00185.23 C ANISOU 1289 CA ASP B 287 15519 36686 18175 -620 -5198 3860 C ATOM 1290 N ASP B 287 198.307 285.545 825.192 1.00183.09 N ANISOU 1290 N ASP B 287 15435 36309 17821 -171 -4940 4438 N ATOM 1291 CB ASP B 287 197.620 287.893 825.319 1.00187.93 C ANISOU 1291 CB ASP B 287 15465 37195 18747 -750 -5247 3953 C ATOM 1292 CG ASP B 287 197.769 288.528 826.678 1.00193.86 C ANISOU 1292 CG ASP B 287 15634 38882 19141 -778 -5542 3873 C ATOM 1293 OD1 ASP B 287 198.267 287.856 827.614 1.00195.80 O ANISOU 1293 OD1 ASP B 287 15750 39739 18905 -456 -5603 4132 O ATOM 1294 OD2 ASP B 287 197.381 289.711 826.794 1.00196.95 O ANISOU 1294 OD2 ASP B 287 15672 39408 19752 -1107 -5695 3550 O ATOM 1295 O ASP B 287 194.910 286.437 824.565 1.00182.84 O ANISOU 1295 O ASP B 287 15590 35613 18267 -1233 -5264 2929 O ATOM 1296 C SER B 288 195.063 284.129 821.968 1.00146.80 C ANISOU 1296 C SER B 288 12203 29524 14049 -807 -4668 3280 C ATOM 1297 CA SER B 288 195.606 285.563 822.016 1.00149.55 C ANISOU 1297 CA SER B 288 12172 30087 14564 -887 -4704 3440 C ATOM 1298 N SER B 288 196.518 285.750 823.145 1.00152.94 N ANISOU 1298 N SER B 288 12225 31201 14683 -711 -4825 3727 N ATOM 1299 CB SER B 288 196.293 285.948 820.692 1.00146.97 C ANISOU 1299 CB SER B 288 12004 29270 14567 -729 -4440 3751 C ATOM 1300 OG SER B 288 196.202 287.343 820.440 1.00149.09 O ANISOU 1300 OG SER B 288 12007 29519 15121 -923 -4443 3739 O ATOM 1301 O SER B 288 193.884 283.895 821.665 1.00145.68 O ANISOU 1301 O SER B 288 12266 29082 14004 -1037 -4696 2879 O ATOM 1302 C ILE B 289 194.566 281.579 823.437 1.00163.67 C ANISOU 1302 C ILE B 289 14610 32053 15525 -544 -4760 3164 C ATOM 1303 CA ILE B 289 195.562 281.768 822.308 1.00161.11 C ANISOU 1303 CA ILE B 289 14402 31294 15519 -356 -4510 3522 C ATOM 1304 N ILE B 289 195.935 283.174 822.266 1.00163.28 N ANISOU 1304 N ILE B 289 14365 31746 15929 -469 -4571 3617 N ATOM 1305 CB ILE B 289 196.796 280.880 822.522 1.00160.78 C ANISOU 1305 CB ILE B 289 14374 31320 15394 57 -4302 4000 C ATOM 1306 CG1 ILE B 289 197.485 280.620 821.178 1.00157.45 C ANISOU 1306 CG1 ILE B 289 14199 30297 15326 219 -4021 4157 C ATOM 1307 CD1 ILE B 289 198.816 279.901 821.285 1.00157.66 C ANISOU 1307 CD1 ILE B 289 14188 30302 15414 605 -3749 4609 C ATOM 1308 CG2 ILE B 289 196.421 279.579 823.193 1.00160.71 C ANISOU 1308 CG2 ILE B 289 14502 31416 15146 178 -4293 3948 C ATOM 1309 O ILE B 289 193.622 280.786 823.331 1.00162.03 O ANISOU 1309 O ILE B 289 14671 31607 15285 -646 -4773 2854 O ATOM 1310 C GLU B 290 192.536 282.999 825.161 1.00164.47 C ANISOU 1310 C GLU B 290 14148 32992 15350 -1235 -5329 2170 C ATOM 1311 CA GLU B 290 193.839 282.356 825.617 1.00164.58 C ANISOU 1311 CA GLU B 290 14102 33364 15068 -778 -5238 2759 C ATOM 1312 N GLU B 290 194.778 282.333 824.512 1.00161.15 N ANISOU 1312 N GLU B 290 13863 32406 14960 -582 -4964 3185 N ATOM 1313 CB GLU B 290 194.416 283.122 826.817 1.00169.93 C ANISOU 1313 CB GLU B 290 14239 34920 15407 -699 -5449 2882 C ATOM 1314 CG GLU B 290 193.471 283.282 828.000 1.00174.50 C ANISOU 1314 CG GLU B 290 14527 36165 15610 -904 -5770 2351 C ATOM 1315 CD GLU B 290 193.913 284.372 828.982 1.00180.30 C ANISOU 1315 CD GLU B 290 14652 37758 16096 -922 -6019 2330 C ATOM 1316 OE1 GLU B 290 194.927 285.055 828.701 1.00180.47 O ANISOU 1316 OE1 GLU B 290 14496 37798 16278 -795 -5930 2758 O ATOM 1317 OE2 GLU B 290 193.247 284.546 830.034 1.00184.97 O ANISOU 1317 OE2 GLU B 290 14922 39034 16323 -1057 -6308 1861 O ATOM 1318 O GLU B 290 191.500 282.809 825.795 1.00166.37 O ANISOU 1318 O GLU B 290 14353 33434 15426 -1446 -5498 1694 O ATOM 1319 C LEU B 291 190.339 283.711 822.879 1.00177.89 C ANISOU 1319 C LEU B 291 16359 33201 18030 -1867 -5063 1478 C ATOM 1320 CA LEU B 291 191.408 284.510 823.630 1.00181.22 C ANISOU 1320 CA LEU B 291 16340 34224 18289 -1772 -5198 1736 C ATOM 1321 N LEU B 291 192.582 283.750 824.062 1.00180.52 N ANISOU 1321 N LEU B 291 16262 34492 17836 -1364 -5182 2215 N ATOM 1322 CB LEU B 291 191.785 285.790 822.876 1.00181.70 C ANISOU 1322 CB LEU B 291 16228 34030 18780 -1868 -5077 1897 C ATOM 1323 CG LEU B 291 191.620 287.094 823.676 1.00187.08 C ANISOU 1323 CG LEU B 291 16369 35151 19562 -2165 -5270 1620 C ATOM 1324 CD1 LEU B 291 192.049 288.301 822.841 1.00187.34 C ANISOU 1324 CD1 LEU B 291 16252 34863 20067 -2220 -5094 1858 C ATOM 1325 CD2 LEU B 291 190.183 287.251 824.188 1.00189.97 C ANISOU 1325 CD2 LEU B 291 16626 35514 20039 -2576 -5398 918 C ATOM 1326 O LEU B 291 189.180 283.731 823.289 1.00179.68 O ANISOU 1326 O LEU B 291 16559 33428 18285 -2155 -5160 979 O ATOM 1327 C LEU B 292 189.423 280.956 822.013 1.00200.89 C ANISOU 1327 C LEU B 292 20160 35404 20765 -1599 -4844 1414 C ATOM 1328 CA LEU B 292 189.673 282.180 821.154 1.00201.03 C ANISOU 1328 CA LEU B 292 20057 35156 21171 -1690 -4730 1535 C ATOM 1329 N LEU B 292 190.686 283.019 821.795 1.00203.86 N ANISOU 1329 N LEU B 292 20027 35999 21432 -1632 -4839 1773 N ATOM 1330 CB LEU B 292 190.016 281.807 819.700 1.00196.92 C ANISOU 1330 CB LEU B 292 19865 34091 20865 -1466 -4476 1806 C ATOM 1331 CG LEU B 292 190.745 280.542 819.213 1.00193.48 C ANISOU 1331 CG LEU B 292 19715 33508 20291 -1121 -4357 2061 C ATOM 1332 CD1 LEU B 292 190.426 279.256 819.971 1.00192.99 C ANISOU 1332 CD1 LEU B 292 19797 33586 19945 -1063 -4433 1934 C ATOM 1333 CD2 LEU B 292 190.523 280.336 817.714 1.00190.41 C ANISOU 1333 CD2 LEU B 292 19613 32592 20141 -1014 -4145 2086 C ATOM 1334 O LEU B 292 188.380 280.330 821.911 1.00199.86 O ANISOU 1334 O LEU B 292 20262 35030 20648 -1721 -4828 1105 O ATOM 1335 C THR B 302 184.857 287.829 816.149 1.00155.18 C ANISOU 1335 C THR B 302 13958 26441 18562 -2705 -3182 1178 C ATOM 1336 CA THR B 302 183.412 288.337 816.071 1.00158.55 C ANISOU 1336 CA THR B 302 14280 26385 19577 -3015 -2901 858 C ATOM 1337 N THR B 302 183.068 289.179 817.216 1.00163.60 N ANISOU 1337 N THR B 302 14469 27173 20517 -3472 -3032 366 N ATOM 1338 CB THR B 302 183.188 289.069 814.726 1.00159.11 C ANISOU 1338 CB THR B 302 14366 25957 20131 -2799 -2423 1310 C ATOM 1339 OG1 THR B 302 183.517 288.195 813.640 1.00154.66 O ANISOU 1339 OG1 THR B 302 14207 25359 19196 -2336 -2339 1711 O ATOM 1340 CG2 THR B 302 184.054 290.309 814.638 1.00161.41 C ANISOU 1340 CG2 THR B 302 14309 26342 20678 -2781 -2355 1601 C ATOM 1341 O THR B 302 185.775 288.571 816.511 1.00156.66 O ANISOU 1341 O THR B 302 13860 26924 18741 -2716 -3298 1323 O ATOM 1342 C PHE B 303 187.305 286.524 814.808 1.00187.38 C ANISOU 1342 C PHE B 303 18522 30884 21791 -1816 -3281 2052 C ATOM 1343 CA PHE B 303 186.375 285.965 815.870 1.00188.42 C ANISOU 1343 CA PHE B 303 18658 31089 21843 -2139 -3472 1556 C ATOM 1344 CB PHE B 303 186.282 284.470 815.658 1.00184.59 C ANISOU 1344 CB PHE B 303 18565 30596 20973 -1936 -3543 1517 C ATOM 1345 CG PHE B 303 186.245 284.088 814.224 1.00181.88 C ANISOU 1345 CG PHE B 303 18505 29943 20660 -1602 -3293 1793 C ATOM 1346 CD2 PHE B 303 187.307 283.415 813.638 1.00178.90 C ANISOU 1346 CD2 PHE B 303 18294 29700 19981 -1243 -3324 2049 C ATOM 1347 CE2 PHE B 303 187.272 283.071 812.315 1.00177.01 C ANISOU 1347 CE2 PHE B 303 18267 29265 19723 -921 -3120 2234 C ATOM 1348 CZ PHE B 303 186.167 283.407 811.546 1.00178.03 C ANISOU 1348 CZ PHE B 303 18454 29071 20117 -913 -2858 2254 C ATOM 1349 CE1 PHE B 303 185.105 284.092 812.120 1.00180.94 C ANISOU 1349 CE1 PHE B 303 18670 29233 20848 -1266 -2775 2059 C ATOM 1350 CD1 PHE B 303 185.151 284.427 813.453 1.00182.88 C ANISOU 1350 CD1 PHE B 303 18693 29664 21129 -1628 -3003 1787 C ATOM 1351 N PHE B 303 185.054 286.564 815.792 1.00191.31 N ANISOU 1351 N PHE B 303 18925 31072 22693 -2428 -3261 1289 N ATOM 1352 O PHE B 303 188.508 286.598 815.019 1.00186.75 O ANISOU 1352 O PHE B 303 18351 31118 21489 -1661 -3413 2277 O ATOM 1353 C ARG B 304 188.517 288.457 813.087 1.00177.79 C ANISOU 1353 C ARG B 304 17051 29476 21024 -1399 -2823 2874 C ATOM 1354 CA ARG B 304 187.559 287.397 812.551 1.00175.55 C ANISOU 1354 CA ARG B 304 17120 28951 20630 -1315 -2740 2713 C ATOM 1355 N ARG B 304 186.751 286.872 813.649 1.00176.17 N ANISOU 1355 N ARG B 304 17201 29068 20668 -1673 -2948 2243 N ATOM 1356 CB ARG B 304 186.672 287.978 811.444 1.00177.06 C ANISOU 1356 CB ARG B 304 17333 28725 21217 -1192 -2326 2914 C ATOM 1357 O ARG B 304 189.701 288.476 812.739 1.00176.40 O ANISOU 1357 O ARG B 304 16886 29505 20634 -1116 -2851 3182 O ATOM 1358 C GLU B 305 189.994 289.670 815.320 1.00159.38 C ANISOU 1358 C GLU B 305 14019 27917 18621 -1794 -3306 2772 C ATOM 1359 CA GLU B 305 188.808 290.332 814.614 1.00161.35 C ANISOU 1359 CA GLU B 305 14241 27659 19405 -1926 -2974 2713 C ATOM 1360 N GLU B 305 187.993 289.327 813.949 1.00158.66 N ANISOU 1360 N GLU B 305 14293 27036 18953 -1796 -2857 2629 N ATOM 1361 CB GLU B 305 187.968 291.129 815.613 1.00166.03 C ANISOU 1361 CB GLU B 305 14447 28232 20403 -2420 -3032 2269 C ATOM 1362 O GLU B 305 191.067 290.264 815.449 1.00160.16 O ANISOU 1362 O GLU B 305 13909 28265 18679 -1684 -3349 3053 O ATOM 1363 C TRP B 306 192.016 287.472 815.428 1.00140.73 C ANISOU 1363 C TRP B 306 12110 26067 15295 -1197 -3596 3084 C ATOM 1364 CA TRP B 306 190.868 287.692 816.401 1.00143.44 C ANISOU 1364 CA TRP B 306 12283 26458 15758 -1615 -3740 2645 C ATOM 1365 N TRP B 306 189.796 288.435 815.765 1.00145.06 N ANISOU 1365 N TRP B 306 12453 26237 16427 -1785 -3501 2541 N ATOM 1366 CB TRP B 306 190.372 286.350 816.937 1.00141.55 C ANISOU 1366 CB TRP B 306 12297 26299 15189 -1643 -3904 2355 C ATOM 1367 CG TRP B 306 191.453 285.557 817.593 1.00140.36 C ANISOU 1367 CG TRP B 306 12162 26545 14623 -1434 -4077 2517 C ATOM 1368 CD1 TRP B 306 192.016 285.797 818.809 1.00142.93 C ANISOU 1368 CD1 TRP B 306 12177 27390 14739 -1499 -4295 2525 C ATOM 1369 NE1 TRP B 306 192.984 284.858 819.077 1.00141.22 N ANISOU 1369 NE1 TRP B 306 12068 27389 14200 -1204 -4328 2775 N ATOM 1370 CE2 TRP B 306 193.057 283.985 818.025 1.00137.50 C ANISOU 1370 CE2 TRP B 306 11971 26517 13755 -981 -4147 2862 C ATOM 1371 CZ2 TRP B 306 193.878 282.874 817.838 1.00135.12 C ANISOU 1371 CZ2 TRP B 306 11867 26189 13284 -675 -4071 3053 C ATOM 1372 CH2 TRP B 306 193.730 282.171 816.673 1.00132.05 C ANISOU 1372 CH2 TRP B 306 11801 25390 12982 -517 -3904 3013 C ATOM 1373 CZ3 TRP B 306 192.800 282.556 815.704 1.00131.30 C ANISOU 1373 CZ3 TRP B 306 11843 24962 13084 -610 -3805 2857 C ATOM 1374 CE3 TRP B 306 191.981 283.662 815.893 1.00133.66 C ANISOU 1374 CE3 TRP B 306 11961 25244 13581 -890 -3832 2739 C ATOM 1375 CD2 TRP B 306 192.106 284.395 817.071 1.00136.84 C ANISOU 1375 CD2 TRP B 306 12024 26015 13956 -1104 -4009 2704 C ATOM 1376 O TRP B 306 193.165 287.779 815.737 1.00141.28 O ANISOU 1376 O TRP B 306 12005 26421 15256 -1066 -3656 3345 O ATOM 1377 C LYS B 307 193.591 287.796 812.876 1.00140.93 C ANISOU 1377 C LYS B 307 12379 25803 15367 -437 -3132 3816 C ATOM 1378 CA LYS B 307 192.742 286.597 813.279 1.00139.20 C ANISOU 1378 CA LYS B 307 12396 25526 14969 -570 -3272 3451 C ATOM 1379 N LYS B 307 191.706 286.946 814.248 1.00141.51 N ANISOU 1379 N LYS B 307 12525 25833 15408 -976 -3397 3147 N ATOM 1380 CB LYS B 307 192.128 285.953 812.046 1.00137.05 C ANISOU 1380 CB LYS B 307 12439 24962 14672 -355 -3092 3405 C ATOM 1381 O LYS B 307 194.755 287.633 812.515 1.00139.87 O ANISOU 1381 O LYS B 307 12271 25787 15086 -149 -3092 4054 O ATOM 1382 C ASN B 308 194.869 290.374 813.719 1.00216.40 C ANISOU 1382 C ASN B 308 21178 35712 25334 -602 -3117 4294 C ATOM 1383 CA ASN B 308 193.742 290.241 812.717 1.00215.60 C ANISOU 1383 CA ASN B 308 21307 35206 25405 -570 -2900 4195 C ATOM 1384 N ASN B 308 193.007 288.994 812.941 1.00213.37 N ANISOU 1384 N ASN B 308 21306 34866 24899 -649 -3032 3848 N ATOM 1385 CB ASN B 308 192.824 291.457 812.870 1.00219.32 C ANISOU 1385 CB ASN B 308 21486 35472 26373 -875 -2763 4136 C ATOM 1386 CG ASN B 308 191.988 291.732 811.632 1.00219.54 C ANISOU 1386 CG ASN B 308 21656 35083 26676 -712 -2400 4278 C ATOM 1387 OD1 ASN B 308 192.148 291.087 810.592 1.00217.02 O ANISOU 1387 OD1 ASN B 308 21636 34703 26119 -339 -2273 4433 O ATOM 1388 ND2 ASN B 308 191.090 292.701 811.736 1.00223.07 N ANISOU 1388 ND2 ASN B 308 21852 35258 27645 -976 -2208 4223 N ATOM 1389 O ASN B 308 196.037 290.519 813.355 1.00215.83 O ANISOU 1389 O ASN B 308 21085 35757 25166 -318 -3045 4620 O ATOM 1390 C LEU B 309 196.519 289.379 815.963 1.00176.26 C ANISOU 1390 C LEU B 309 15862 31466 19644 -599 -3593 4320 C ATOM 1391 CA LEU B 309 195.432 290.437 816.094 1.00179.15 C ANISOU 1391 CA LEU B 309 15999 31713 20359 -952 -3591 4100 C ATOM 1392 N LEU B 309 194.489 290.333 814.991 1.00177.69 N ANISOU 1392 N LEU B 309 16081 31050 20383 -931 -3370 4007 N ATOM 1393 CB LEU B 309 194.696 290.263 817.421 1.00181.38 C ANISOU 1393 CB LEU B 309 16091 32295 20529 -1302 -3875 3682 C ATOM 1394 CG LEU B 309 193.274 290.831 817.426 1.00183.60 C ANISOU 1394 CG LEU B 309 16274 32302 21183 -1676 -3834 3283 C ATOM 1395 CD1 LEU B 309 192.521 290.448 818.688 1.00185.65 C ANISOU 1395 CD1 LEU B 309 16395 32877 21267 -1991 -4121 2785 C ATOM 1396 CD2 LEU B 309 193.317 292.333 817.246 1.00187.14 C ANISOU 1396 CD2 LEU B 309 16342 32659 22102 -1822 -3692 3404 C ATOM 1397 O LEU B 309 197.679 289.621 816.303 1.00177.10 O ANISOU 1397 O LEU B 309 15788 31845 19657 -433 -3605 4626 O ATOM 1398 C VAL B 310 198.100 287.426 814.200 1.00148.40 C ANISOU 1398 C VAL B 310 12959 27610 15817 157 -3281 4606 C ATOM 1399 CA VAL B 310 197.081 287.108 815.290 1.00149.20 C ANISOU 1399 CA VAL B 310 13014 27846 15828 -174 -3514 4292 C ATOM 1400 N VAL B 310 196.137 288.209 815.460 1.00151.62 N ANISOU 1400 N VAL B 310 13115 28120 16374 -484 -3554 4158 N ATOM 1401 CB VAL B 310 196.370 285.776 814.960 1.00146.39 C ANISOU 1401 CB VAL B 310 13019 27264 15340 -148 -3520 3997 C ATOM 1402 CG1 VAL B 310 197.386 284.642 814.839 1.00144.51 C ANISOU 1402 CG1 VAL B 310 12934 27025 14949 149 -3447 4102 C ATOM 1403 CG2 VAL B 310 195.321 285.455 816.019 1.00147.33 C ANISOU 1403 CG2 VAL B 310 13103 27517 15358 -462 -3736 3671 C ATOM 1404 O VAL B 310 199.257 287.013 814.284 1.00147.98 O ANISOU 1404 O VAL B 310 12895 27662 15670 394 -3221 4810 O ATOM 1405 C LEU B 311 199.352 289.764 812.374 1.00170.95 C ANISOU 1405 C LEU B 311 15556 30328 19070 550 -2840 5280 C ATOM 1406 CA LEU B 311 198.570 288.493 812.089 1.00168.35 C ANISOU 1406 CA LEU B 311 15559 29825 18580 542 -2892 4926 C ATOM 1407 N LEU B 311 197.674 288.167 813.185 1.00168.75 N ANISOU 1407 N LEU B 311 15569 29958 18589 195 -3118 4655 N ATOM 1408 CB LEU B 311 197.797 288.617 810.787 1.00167.64 C ANISOU 1408 CB LEU B 311 15660 29474 18563 678 -2707 4870 C ATOM 1409 CG LEU B 311 197.211 287.268 810.377 1.00165.04 C ANISOU 1409 CG LEU B 311 15654 29010 18042 741 -2746 4540 C ATOM 1410 CD1 LEU B 311 196.543 287.351 808.999 1.00164.70 C ANISOU 1410 CD1 LEU B 311 15776 28797 18006 967 -2546 4530 C ATOM 1411 CD2 LEU B 311 198.309 286.209 810.399 1.00163.44 C ANISOU 1411 CD2 LEU B 311 15557 28884 17659 954 -2765 4486 C ATOM 1412 O LEU B 311 200.544 289.845 812.074 1.00170.96 O ANISOU 1412 O LEU B 311 15518 30405 19034 822 -2723 5537 O ATOM 1413 C LYS B 312 200.681 291.518 814.000 1.00145.74 C ANISOU 1413 C LYS B 312 11656 27682 16036 386 -2967 5772 C ATOM 1414 CA LYS B 312 199.376 291.967 813.381 1.00145.98 C ANISOU 1414 CA LYS B 312 11757 27416 16291 206 -2896 5570 C ATOM 1415 N LYS B 312 198.686 290.756 812.961 1.00143.09 N ANISOU 1415 N LYS B 312 11764 26851 15752 244 -2914 5267 N ATOM 1416 CB LYS B 312 198.550 292.736 814.412 1.00149.09 C ANISOU 1416 CB LYS B 312 11817 27946 16885 -225 -3073 5374 C ATOM 1417 O LYS B 312 201.744 292.013 813.674 1.00146.41 O ANISOU 1417 O LYS B 312 11634 27827 16169 622 -2820 6115 O ATOM 1418 C LEU B 313 202.702 289.236 814.684 1.00146.39 C ANISOU 1418 C LEU B 313 11968 27983 15671 862 -2943 5937 C ATOM 1419 CA LEU B 313 201.735 290.004 815.586 1.00148.62 C ANISOU 1419 CA LEU B 313 11997 28495 15979 486 -3184 5801 C ATOM 1420 N LEU B 313 200.584 290.526 814.866 1.00148.35 N ANISOU 1420 N LEU B 313 12052 28180 16133 302 -3156 5578 N ATOM 1421 CB LEU B 313 201.245 289.167 816.785 1.00148.92 C ANISOU 1421 CB LEU B 313 12013 28794 15775 317 -3422 5574 C ATOM 1422 CG LEU B 313 201.997 288.034 817.497 1.00148.53 C ANISOU 1422 CG LEU B 313 12004 28936 15494 525 -3418 5704 C ATOM 1423 CD1 LEU B 313 203.436 288.352 817.834 1.00150.35 C ANISOU 1423 CD1 LEU B 313 11993 29403 15731 797 -3280 6185 C ATOM 1424 CD2 LEU B 313 201.222 287.676 818.758 1.00150.05 C ANISOU 1424 CD2 LEU B 313 12073 29495 15444 302 -3690 5476 C ATOM 1425 O LEU B 313 203.909 289.343 814.823 1.00147.32 O ANISOU 1425 O LEU B 313 11954 28219 15803 1088 -2817 6260 O ATOM 1426 C SER B 314 203.982 288.472 812.094 1.00140.85 C ANISOU 1426 C SER B 314 11716 26743 15057 1521 -2440 5946 C ATOM 1427 CA SER B 314 203.034 287.610 812.931 1.00139.82 C ANISOU 1427 CA SER B 314 11681 26641 14804 1262 -2661 5661 C ATOM 1428 N SER B 314 202.176 288.467 813.747 1.00141.49 N ANISOU 1428 N SER B 314 11683 27044 15031 934 -2866 5665 N ATOM 1429 CB SER B 314 202.206 286.690 812.012 1.00137.32 C ANISOU 1429 CB SER B 314 11700 26051 14423 1291 -2644 5267 C ATOM 1430 OG SER B 314 200.969 286.309 812.591 1.00136.63 O ANISOU 1430 OG SER B 314 11695 25962 14258 1002 -2846 5007 O ATOM 1431 O SER B 314 205.137 288.105 811.872 1.00140.98 O ANISOU 1431 O SER B 314 11731 26725 15111 1784 -2260 6072 O ATOM 1432 C GLN B 315 205.165 291.478 811.507 1.00157.77 C ANISOU 1432 C GLN B 315 13339 29088 17519 1715 -2176 6750 C ATOM 1433 CA GLN B 315 204.204 290.536 810.755 1.00155.29 C ANISOU 1433 CA GLN B 315 13366 28546 17090 1712 -2200 6333 C ATOM 1434 N GLN B 315 203.481 289.627 811.653 1.00154.14 N ANISOU 1434 N GLN B 315 13302 28424 16839 1450 -2424 6052 N ATOM 1435 CB GLN B 315 203.208 291.357 809.930 1.00155.77 C ANISOU 1435 CB GLN B 315 13455 28485 17245 1676 -2133 6326 C ATOM 1436 CG GLN B 315 203.735 292.690 809.470 1.00158.05 C ANISOU 1436 CG GLN B 315 13528 28820 17705 1832 -1941 6722 C ATOM 1437 CD GLN B 315 202.629 293.710 809.289 1.00159.68 C ANISOU 1437 CD GLN B 315 13611 28922 18140 1648 -1898 6796 C ATOM 1438 OE1 GLN B 315 201.581 293.635 809.932 1.00159.78 O ANISOU 1438 OE1 GLN B 315 13592 28879 18237 1300 -2061 6572 O ATOM 1439 NE2 GLN B 315 202.857 294.673 808.408 1.00161.34 N ANISOU 1439 NE2 GLN B 315 13734 29087 18481 1893 -1642 7110 N ATOM 1440 O GLN B 315 206.332 291.641 811.118 1.00158.42 O ANISOU 1440 O GLN B 315 13373 29180 17638 2002 -1977 6988 O ATOM 1441 C ALA B 316 206.821 292.186 813.564 1.00185.73 C ANISOU 1441 C ALA B 316 16290 33179 21099 1686 -2255 7368 C ATOM 1442 CA ALA B 316 205.500 292.920 813.430 1.00186.10 C ANISOU 1442 CA ALA B 316 16298 33177 21234 1384 -2400 7172 C ATOM 1443 N ALA B 316 204.658 292.135 812.549 1.00183.44 N ANISOU 1443 N ALA B 316 16328 32537 20832 1400 -2371 6812 N ATOM 1444 CB ALA B 316 204.836 293.053 814.791 1.00187.80 C ANISOU 1444 CB ALA B 316 16264 33702 21389 1028 -2700 7045 C ATOM 1445 O ALA B 316 207.887 292.722 813.258 1.00186.94 O ANISOU 1445 O ALA B 316 16322 33356 21352 1928 -2053 7705 O ATOM 1446 C PHE B 317 208.714 290.036 812.830 1.00167.47 C ANISOU 1446 C PHE B 317 14342 30511 18776 2278 -1822 7318 C ATOM 1447 CA PHE B 317 207.857 290.035 814.106 1.00168.04 C ANISOU 1447 CA PHE B 317 14271 30863 18712 1957 -2129 7290 C ATOM 1448 N PHE B 317 206.726 290.942 814.023 1.00168.29 N ANISOU 1448 N PHE B 317 14244 30955 18745 1676 -2327 7160 N ATOM 1449 CB PHE B 317 207.329 288.631 814.382 1.00166.13 C ANISOU 1449 CB PHE B 317 14262 30501 18357 1894 -2205 6954 C ATOM 1450 CG PHE B 317 208.277 287.766 815.147 1.00167.10 C ANISOU 1450 CG PHE B 317 14304 30685 18500 2083 -2056 7169 C ATOM 1451 CD1 PHE B 317 209.271 287.057 814.494 1.00166.74 C ANISOU 1451 CD1 PHE B 317 14376 30329 18650 2372 -1729 7172 C ATOM 1452 CE1 PHE B 317 210.145 286.253 815.193 1.00168.12 C ANISOU 1452 CE1 PHE B 317 14451 30491 18935 2561 -1516 7405 C ATOM 1453 CZ PHE B 317 210.030 286.144 816.560 1.00169.84 C ANISOU 1453 CZ PHE B 317 14459 31083 18990 2508 -1643 7684 C ATOM 1454 CE2 PHE B 317 209.040 286.843 817.227 1.00170.24 C ANISOU 1454 CE2 PHE B 317 14388 31527 18767 2229 -2017 7640 C ATOM 1455 CD2 PHE B 317 208.166 287.648 816.519 1.00168.87 C ANISOU 1455 CD2 PHE B 317 14309 31289 18563 1994 -2214 7358 C ATOM 1456 O PHE B 317 208.223 290.162 811.703 1.00166.18 O ANISOU 1456 O PHE B 317 14375 30158 18608 2322 -1780 7085 O ATOM 1457 C SER B 325 219.098 283.361 817.674 1.00177.01 C ANISOU 1457 C SER B 325 14268 30470 22519 4806 1782 10281 C ATOM 1458 CA SER B 325 218.232 284.483 818.267 1.00175.89 C ANISOU 1458 CA SER B 325 14049 31056 21725 4603 1190 10462 C ATOM 1459 N SER B 325 217.568 284.043 819.487 1.00176.66 N ANISOU 1459 N SER B 325 14041 31596 21488 4584 986 10706 N ATOM 1460 CB SER B 325 219.070 285.738 818.557 1.00178.52 C ANISOU 1460 CB SER B 325 14079 31744 22005 4778 1263 11047 C ATOM 1461 OG SER B 325 219.267 286.533 817.400 1.00177.01 O ANISOU 1461 OG SER B 325 14013 31341 21901 4696 1228 10748 O ATOM 1462 O SER B 325 220.200 283.103 818.147 1.00180.74 O ANISOU 1462 O SER B 325 14499 30794 23381 5136 2304 10805 O ATOM 1463 C GLY B 326 218.442 280.706 815.107 1.00166.75 C ANISOU 1463 C GLY B 326 13628 27690 22039 4506 2054 8341 C ATOM 1464 CA GLY B 326 219.315 281.625 815.967 1.00169.79 C ANISOU 1464 CA GLY B 326 13710 28412 22392 4750 2239 9185 C ATOM 1465 N GLY B 326 218.590 282.698 816.636 1.00168.54 N ANISOU 1465 N GLY B 326 13500 28950 21587 4615 1718 9527 N ATOM 1466 O GLY B 326 217.570 281.152 814.348 1.00163.47 O ANISOU 1466 O GLY B 326 13437 27435 21240 4271 1604 7861 O ATOM 1467 C GLU B 327 216.553 278.244 815.315 1.00161.07 C ANISOU 1467 C GLU B 327 13265 26606 21330 4165 1809 7508 C ATOM 1468 CA GLU B 327 217.861 278.385 814.556 1.00163.72 C ANISOU 1468 CA GLU B 327 13467 26527 22214 4368 2291 7420 C ATOM 1469 N GLU B 327 218.694 279.402 815.212 1.00166.14 N ANISOU 1469 N GLU B 327 13532 27134 22459 4585 2443 8179 N ATOM 1470 CB GLU B 327 218.571 277.028 814.507 1.00166.70 C ANISOU 1470 CB GLU B 327 13730 26233 23377 4510 2900 7239 C ATOM 1471 O GLU B 327 215.538 277.869 814.753 1.00157.99 O ANISOU 1471 O GLU B 327 13119 26189 20722 3924 1467 6923 O ATOM 1472 C LEU B 328 214.518 279.747 817.046 1.00173.13 C ANISOU 1472 C LEU B 328 14824 29479 21476 3838 731 8111 C ATOM 1473 CA LEU B 328 215.399 278.569 817.436 1.00176.19 C ANISOU 1473 CA LEU B 328 15072 29434 22439 4114 1325 8344 C ATOM 1474 N LEU B 328 216.595 278.559 816.604 1.00178.03 N ANISOU 1474 N LEU B 328 15227 29175 23242 4287 1792 8239 N ATOM 1475 CB LEU B 328 215.775 278.696 818.917 1.00179.60 C ANISOU 1475 CB LEU B 328 15203 30316 22722 4371 1469 9189 C ATOM 1476 CG LEU B 328 214.620 278.733 819.923 1.00178.67 C ANISOU 1476 CG LEU B 328 15100 30806 21979 4236 1001 9313 C ATOM 1477 CD1 LEU B 328 214.190 277.310 820.297 1.00178.81 C ANISOU 1477 CD1 LEU B 328 15208 30562 22171 4278 1179 9206 C ATOM 1478 CD2 LEU B 328 214.993 279.536 821.154 1.00182.03 C ANISOU 1478 CD2 LEU B 328 15180 31939 22045 4457 956 10077 C ATOM 1479 O LEU B 328 213.299 279.695 817.182 1.00170.58 O ANISOU 1479 O LEU B 328 14672 29389 20751 3586 296 7839 O ATOM 1480 C ARG B 329 213.515 281.847 815.061 1.00152.72 C ANISOU 1480 C ARG B 329 12544 27145 18338 3445 18 7396 C ATOM 1481 CA ARG B 329 214.451 282.058 816.233 1.00156.23 C ANISOU 1481 CA ARG B 329 12667 27809 18885 3680 279 8129 C ATOM 1482 N ARG B 329 215.149 280.810 816.552 1.00158.31 N ANISOU 1482 N ARG B 329 12863 27678 19609 3897 756 8232 N ATOM 1483 CB ARG B 329 215.457 283.165 815.909 1.00158.02 C ANISOU 1483 CB ARG B 329 12715 28105 19219 3847 449 8455 C ATOM 1484 O ARG B 329 212.504 282.543 814.912 1.00150.61 O ANISOU 1484 O ARG B 329 12384 27162 17679 3212 -406 7236 O ATOM 1485 C ASP B 330 211.928 279.596 813.359 1.00173.81 C ANISOU 1485 C ASP B 330 15782 29105 21152 3160 -132 5939 C ATOM 1486 CA ASP B 330 213.162 280.465 813.033 1.00176.07 C ANISOU 1486 CA ASP B 330 15884 29381 21632 3378 135 6226 C ATOM 1487 N ASP B 330 213.876 280.854 814.250 1.00178.68 N ANISOU 1487 N ASP B 330 15949 29925 22014 3523 307 6954 N ATOM 1488 CB ASP B 330 214.156 279.759 812.094 1.00177.76 C ANISOU 1488 CB ASP B 330 16073 29100 22366 3564 568 5830 C ATOM 1489 CG ASP B 330 213.491 279.025 810.963 1.00175.89 C ANISOU 1489 CG ASP B 330 16052 28662 22117 3457 438 5039 C ATOM 1490 OD1 ASP B 330 212.311 279.307 810.679 1.00173.10 O ANISOU 1490 OD1 ASP B 330 15889 28561 21318 3272 19 4833 O ATOM 1491 OD2 ASP B 330 214.165 278.163 810.357 1.00177.64 O ANISOU 1491 OD2 ASP B 330 16221 28472 22801 3567 778 4609 O ATOM 1492 O ASP B 330 210.811 279.951 812.993 1.00171.25 O ANISOU 1492 O ASP B 330 15639 28973 20455 2952 -521 5670 O ATOM 1493 C TYR B 331 209.901 278.527 815.131 1.00200.76 C ANISOU 1493 C TYR B 331 19345 32863 24073 2831 -607 6017 C ATOM 1494 CA TYR B 331 211.036 277.659 814.581 1.00202.58 C ANISOU 1494 CA TYR B 331 19509 32575 24888 3055 -106 5879 C ATOM 1495 N TYR B 331 212.134 278.475 814.053 1.00204.26 N ANISOU 1495 N TYR B 331 19580 32741 25288 3228 114 6033 N ATOM 1496 CB TYR B 331 211.518 276.767 815.733 1.00205.15 C ANISOU 1496 CB TYR B 331 19663 32803 25483 3227 230 6315 C ATOM 1497 CG TYR B 331 212.394 275.587 815.373 1.00207.26 C ANISOU 1497 CG TYR B 331 19855 32460 26434 3403 769 6132 C ATOM 1498 CD1 TYR B 331 211.856 274.432 814.816 1.00206.00 C ANISOU 1498 CD1 TYR B 331 19853 31924 26493 3287 791 5542 C ATOM 1499 CE1 TYR B 331 212.660 273.337 814.509 1.00208.50 C ANISOU 1499 CE1 TYR B 331 20050 31650 27520 3423 1311 5323 C ATOM 1500 CZ TYR B 331 214.013 273.385 814.775 1.00212.34 C ANISOU 1500 CZ TYR B 331 20270 31884 28525 3690 1848 5726 C ATOM 1501 OH TYR B 331 214.812 272.303 814.469 1.00215.35 O ANISOU 1501 OH TYR B 331 20499 31616 29708 3809 2416 5475 O ATOM 1502 CE2 TYR B 331 214.568 274.516 815.347 1.00213.50 C ANISOU 1502 CE2 TYR B 331 20277 32413 28432 3834 1842 6370 C ATOM 1503 CD2 TYR B 331 213.757 275.603 815.650 1.00210.96 C ANISOU 1503 CD2 TYR B 331 20062 32713 27378 3687 1288 6561 C ATOM 1504 O TYR B 331 208.746 278.102 815.165 1.00198.60 O ANISOU 1504 O TYR B 331 19258 32636 23565 2627 -886 5712 O ATOM 1505 C ILE B 332 208.332 281.261 815.240 1.00141.54 C ANISOU 1505 C ILE B 332 11844 26229 15706 2420 -1439 6161 C ATOM 1506 CA ILE B 332 209.274 280.605 816.250 1.00144.21 C ANISOU 1506 CA ILE B 332 11977 26576 16240 2648 -1133 6594 C ATOM 1507 N ILE B 332 210.241 279.730 815.588 1.00144.94 N ANISOU 1507 N ILE B 332 12094 26168 16807 2866 -698 6463 N ATOM 1508 CB ILE B 332 209.963 281.678 817.133 1.00147.04 C ANISOU 1508 CB ILE B 332 12011 27377 16479 2761 -1126 7206 C ATOM 1509 CG1 ILE B 332 210.642 281.009 818.327 1.00150.05 C ANISOU 1509 CG1 ILE B 332 12169 27897 16948 3010 -858 7707 C ATOM 1510 CD1 ILE B 332 211.433 281.950 819.219 1.00153.44 C ANISOU 1510 CD1 ILE B 332 12235 28806 17258 3192 -806 8353 C ATOM 1511 CG2 ILE B 332 208.953 282.692 817.633 1.00146.65 C ANISOU 1511 CG2 ILE B 332 11899 27816 16006 2493 -1582 7202 C ATOM 1512 O ILE B 332 207.118 281.323 815.458 1.00139.99 O ANISOU 1512 O ILE B 332 11765 26194 15232 2175 -1764 5953 O ATOM 1513 C GLU B 333 207.097 281.325 812.509 1.00188.16 C ANISOU 1513 C GLU B 333 18224 31733 21536 2284 -1630 5155 C ATOM 1514 CA GLU B 333 208.090 282.344 813.079 1.00190.52 C ANISOU 1514 CA GLU B 333 18254 32247 21890 2400 -1517 5694 C ATOM 1515 N GLU B 333 208.897 281.739 814.135 1.00192.51 N ANISOU 1515 N GLU B 333 18331 32500 22315 2528 -1303 6039 N ATOM 1516 CB GLU B 333 208.988 282.914 811.975 1.00191.31 C ANISOU 1516 CB GLU B 333 18321 32223 22143 2618 -1301 5669 C ATOM 1517 O GLU B 333 205.943 281.656 812.232 1.00186.52 O ANISOU 1517 O GLU B 333 18153 31623 21092 2095 -1894 4957 O ATOM 1518 C ASP B 334 205.456 278.904 812.693 1.00154.53 C ANISOU 1518 C ASP B 334 14327 27144 17243 2056 -1783 4450 C ATOM 1519 CA ASP B 334 206.725 278.987 811.871 1.00155.97 C ANISOU 1519 CA ASP B 334 14412 27136 17713 2307 -1477 4419 C ATOM 1520 N ASP B 334 207.561 280.086 812.342 1.00157.84 N ANISOU 1520 N ASP B 334 14432 27581 17958 2401 -1398 4926 N ATOM 1521 CB ASP B 334 207.473 277.659 812.006 1.00157.18 C ANISOU 1521 CB ASP B 334 14516 26932 18272 2441 -1149 4284 C ATOM 1522 CG ASP B 334 208.323 277.338 810.796 1.00158.21 C ANISOU 1522 CG ASP B 334 14622 26781 18711 2628 -886 3886 C ATOM 1523 OD1 ASP B 334 209.006 278.244 810.269 1.00159.26 O ANISOU 1523 OD1 ASP B 334 14666 27006 18839 2763 -808 3995 O ATOM 1524 OD2 ASP B 334 208.309 276.164 810.373 1.00158.29 O ANISOU 1524 OD2 ASP B 334 14678 26488 18978 2642 -754 3432 O ATOM 1525 O ASP B 334 204.350 279.097 812.195 1.00152.71 O ANISOU 1525 O ASP B 334 14265 26967 16790 1901 -2020 4182 O ATOM 1526 C PHE B 335 203.531 279.605 814.781 1.00146.05 C ANISOU 1526 C PHE B 335 13218 26678 15597 1601 -2348 4749 C ATOM 1527 CA PHE B 335 204.573 278.488 814.931 1.00147.07 C ANISOU 1527 CA PHE B 335 13298 26559 16025 1840 -2015 4833 C ATOM 1528 N PHE B 335 205.644 278.595 813.963 1.00147.67 N ANISOU 1528 N PHE B 335 13332 26391 16385 2048 -1746 4789 N ATOM 1529 CB PHE B 335 205.214 278.486 816.321 1.00149.73 C ANISOU 1529 CB PHE B 335 13384 27166 16340 1954 -1916 5353 C ATOM 1530 CG PHE B 335 204.239 278.463 817.448 1.00150.01 C ANISOU 1530 CG PHE B 335 13397 27571 16029 1783 -2194 5415 C ATOM 1531 CD1 PHE B 335 203.772 277.260 817.951 1.00149.71 C ANISOU 1531 CD1 PHE B 335 13461 27443 15977 1790 -2157 5312 C ATOM 1532 CE1 PHE B 335 202.875 277.244 818.998 1.00150.32 C ANISOU 1532 CE1 PHE B 335 13508 27908 15699 1654 -2413 5341 C ATOM 1533 CZ PHE B 335 202.440 278.448 819.562 1.00151.49 C ANISOU 1533 CZ PHE B 335 13493 28537 15530 1483 -2718 5421 C ATOM 1534 CE2 PHE B 335 202.911 279.651 819.071 1.00151.86 C ANISOU 1534 CE2 PHE B 335 13417 28640 15641 1457 -2745 5527 C ATOM 1535 CD2 PHE B 335 203.805 279.652 818.022 1.00151.01 C ANISOU 1535 CD2 PHE B 335 13369 28149 15860 1619 -2481 5553 C ATOM 1536 O PHE B 335 202.337 279.373 814.908 1.00144.67 O ANISOU 1536 O PHE B 335 13191 26535 15243 1393 -2567 4499 O ATOM 1537 C LEU B 336 202.292 281.814 813.017 1.00142.73 C ANISOU 1537 C LEU B 336 12907 26333 14992 1396 -2617 4521 C ATOM 1538 CA LEU B 336 203.105 281.956 814.297 1.00144.86 C ANISOU 1538 CA LEU B 336 12925 26844 15273 1428 -2588 4916 C ATOM 1539 N LEU B 336 203.995 280.815 814.497 1.00145.22 N ANISOU 1539 N LEU B 336 12973 26715 15489 1637 -2349 4963 N ATOM 1540 CB LEU B 336 203.912 283.248 814.227 1.00146.69 C ANISOU 1540 CB LEU B 336 12925 27248 15563 1515 -2524 5273 C ATOM 1541 CG LEU B 336 204.329 283.785 815.593 1.00149.26 C ANISOU 1541 CG LEU B 336 12943 27969 15801 1477 -2602 5673 C ATOM 1542 CD1 LEU B 336 205.343 284.898 815.428 1.00151.12 C ANISOU 1542 CD1 LEU B 336 12947 28327 16147 1621 -2476 6047 C ATOM 1543 CD2 LEU B 336 203.118 284.273 816.364 1.00149.77 C ANISOU 1543 CD2 LEU B 336 12935 28315 15655 1156 -2924 5544 C ATOM 1544 O LEU B 336 201.135 282.235 812.934 1.00142.06 O ANISOU 1544 O LEU B 336 12897 26289 14788 1189 -2798 4376 O ATOM 1545 C LEU B 337 201.172 279.865 810.921 1.00150.32 C ANISOU 1545 C LEU B 337 14370 26794 15951 1515 -2557 3624 C ATOM 1546 CA LEU B 337 202.233 280.951 810.755 1.00152.03 C ANISOU 1546 CA LEU B 337 14391 27129 16245 1667 -2432 3955 C ATOM 1547 N LEU B 337 202.918 281.229 812.006 1.00153.58 N ANISOU 1547 N LEU B 337 14380 27472 16501 1623 -2416 4339 N ATOM 1548 CB LEU B 337 203.237 280.573 809.670 1.00152.52 C ANISOU 1548 CB LEU B 337 14455 27050 16448 1963 -2200 3773 C ATOM 1549 CG LEU B 337 203.797 281.811 808.978 1.00153.79 C ANISOU 1549 CG LEU B 337 14504 27345 16584 2132 -2112 3992 C ATOM 1550 CD1 LEU B 337 204.779 281.419 807.890 1.00154.72 C ANISOU 1550 CD1 LEU B 337 14608 27367 16810 2437 -1888 3737 C ATOM 1551 CD2 LEU B 337 202.653 282.666 808.425 1.00153.23 C ANISOU 1551 CD2 LEU B 337 14512 27393 16314 2057 -2252 4005 C ATOM 1552 O LEU B 337 200.132 279.913 810.271 1.00149.18 O ANISOU 1552 O LEU B 337 14376 26625 15679 1450 -2659 3403 O ATOM 1553 C VAL B 338 199.199 278.343 812.741 1.00131.46 C ANISOU 1553 C VAL B 338 12186 24398 13365 1072 -2875 3383 C ATOM 1554 CA VAL B 338 200.474 277.822 812.076 1.00131.91 C ANISOU 1554 CA VAL B 338 12195 24280 13646 1347 -2621 3355 C ATOM 1555 N VAL B 338 201.428 278.901 811.805 1.00133.35 N ANISOU 1555 N VAL B 338 12204 24575 13887 1482 -2521 3634 N ATOM 1556 CB VAL B 338 201.090 276.734 812.972 1.00132.69 C ANISOU 1556 CB VAL B 338 12229 24275 13911 1410 -2476 3447 C ATOM 1557 CG1 VAL B 338 200.208 275.506 812.988 1.00131.22 C ANISOU 1557 CG1 VAL B 338 12230 23913 13715 1320 -2527 3115 C ATOM 1558 CG2 VAL B 338 202.488 276.376 812.492 1.00134.01 C ANISOU 1558 CG2 VAL B 338 12277 24239 14402 1664 -2164 3467 C ATOM 1559 O VAL B 338 198.088 277.943 812.378 1.00130.01 O ANISOU 1559 O VAL B 338 12189 24119 13091 958 -2978 3098 O ATOM 1560 C ILE B 339 197.526 280.842 813.404 1.00147.47 C ANISOU 1560 C ILE B 339 14049 26796 15187 609 -3220 3575 C ATOM 1561 CA ILE B 339 198.241 279.892 814.359 1.00147.85 C ANISOU 1561 CA ILE B 339 14043 26926 15208 687 -3194 3670 C ATOM 1562 N ILE B 339 199.369 279.232 813.717 1.00147.46 N ANISOU 1562 N ILE B 339 14018 26690 15320 968 -2964 3702 N ATOM 1563 CB ILE B 339 198.689 280.710 815.555 1.00150.36 C ANISOU 1563 CB ILE B 339 14070 27611 15451 614 -3286 3990 C ATOM 1564 CG1 ILE B 339 199.467 279.824 816.518 1.00151.38 C ANISOU 1564 CG1 ILE B 339 14106 27869 15541 770 -3204 4194 C ATOM 1565 CD1 ILE B 339 199.759 280.481 817.837 1.00154.31 C ANISOU 1565 CD1 ILE B 339 14168 28722 15740 729 -3327 4497 C ATOM 1566 CG2 ILE B 339 197.482 281.364 816.218 1.00151.35 C ANISOU 1566 CG2 ILE B 339 14127 27931 15447 293 -3527 3839 C ATOM 1567 O ILE B 339 196.326 281.077 813.538 1.00147.34 O ANISOU 1567 O ILE B 339 14095 26764 15123 383 -3344 3405 O ATOM 1568 C GLY B 340 196.966 281.522 810.346 1.00131.55 C ANISOU 1568 C GLY B 340 12274 24477 13234 946 -2976 3385 C ATOM 1569 CA GLY B 340 197.715 282.271 811.436 1.00133.25 C ANISOU 1569 CA GLY B 340 12241 24876 13510 840 -3023 3691 C ATOM 1570 N GLY B 340 198.276 281.400 812.456 1.00133.21 N ANISOU 1570 N GLY B 340 12200 24937 13476 818 -3068 3704 N ATOM 1571 O GLY B 340 196.118 282.094 809.653 1.00131.73 O ANISOU 1571 O GLY B 340 12347 24450 13255 941 -2941 3372 O ATOM 1572 C GLY B 341 197.332 279.180 807.912 1.00125.64 C ANISOU 1572 C GLY B 341 11853 23524 12363 1503 -2784 2681 C ATOM 1573 CA GLY B 341 196.623 279.364 809.244 1.00125.38 C ANISOU 1573 CA GLY B 341 11817 23470 12351 1163 -2930 2818 C ATOM 1574 N GLY B 341 197.300 280.241 810.189 1.00126.77 N ANISOU 1574 N GLY B 341 11790 23773 12603 1062 -2948 3155 N ATOM 1575 O GLY B 341 196.702 279.082 806.865 1.00125.43 O ANISOU 1575 O GLY B 341 11922 23529 12208 1651 -2760 2511 O ATOM 1576 C ASN B 342 199.321 277.570 806.235 1.00138.36 C ANISOU 1576 C ASN B 342 13389 25084 14098 2045 -2522 2066 C ATOM 1577 CA ASN B 342 199.414 278.988 806.736 1.00139.01 C ANISOU 1577 CA ASN B 342 13382 25277 14158 1971 -2531 2554 C ATOM 1578 N ASN B 342 198.653 279.124 807.953 1.00138.18 N ANISOU 1578 N ASN B 342 13313 25121 14067 1650 -2672 2746 N ATOM 1579 CB ASN B 342 200.869 279.363 806.958 1.00140.49 C ANISOU 1579 CB ASN B 342 13390 25469 14520 2094 -2378 2749 C ATOM 1580 CG ASN B 342 201.404 280.236 805.855 1.00141.96 C ANISOU 1580 CG ASN B 342 13495 25831 14613 2384 -2260 2811 C ATOM 1581 OD1 ASN B 342 202.168 279.789 804.995 1.00143.02 O ANISOU 1581 OD1 ASN B 342 13583 25989 14769 2637 -2135 2512 O ATOM 1582 ND2 ASN B 342 200.984 281.498 805.860 1.00142.42 N ANISOU 1582 ND2 ASN B 342 13514 26019 14580 2355 -2285 3179 N ATOM 1583 O ASN B 342 200.058 276.692 806.659 1.00138.57 O ANISOU 1583 O ASN B 342 13363 24939 14348 2030 -2439 1919 O ATOM 1584 C GLN B 343 199.476 275.269 804.581 1.00127.18 C ANISOU 1584 C GLN B 343 11998 23602 12723 2338 -2456 1020 C ATOM 1585 CA GLN B 343 198.176 276.068 804.691 1.00125.95 C ANISOU 1585 CA GLN B 343 11982 23572 12302 2230 -2598 1329 C ATOM 1586 N GLN B 343 198.386 277.359 805.326 1.00126.24 N ANISOU 1586 N GLN B 343 11963 23647 12354 2139 -2584 1834 N ATOM 1587 CB GLN B 343 197.474 276.259 803.330 1.00126.64 C ANISOU 1587 CB GLN B 343 12103 23942 12073 2499 -2620 1160 C ATOM 1588 CG GLN B 343 196.249 277.195 803.439 1.00126.06 C ANISOU 1588 CG GLN B 343 12133 23925 11839 2411 -2667 1543 C ATOM 1589 CD GLN B 343 195.365 277.267 802.195 1.00126.94 C ANISOU 1589 CD GLN B 343 12282 24301 11648 2700 -2645 1459 C ATOM 1590 OE1 GLN B 343 195.854 277.327 801.072 1.00128.76 O ANISOU 1590 OE1 GLN B 343 12408 24835 11680 3067 -2577 1296 O ATOM 1591 NE2 GLN B 343 194.052 277.286 802.401 1.00126.03 N ANISOU 1591 NE2 GLN B 343 12298 24099 11489 2558 -2684 1584 N ATOM 1592 O GLN B 343 199.589 274.215 805.190 1.00126.70 O ANISOU 1592 O GLN B 343 11945 23293 12901 2197 -2430 841 O ATOM 1593 C ARG B 344 202.325 274.582 805.008 1.00129.38 C ANISOU 1593 C ARG B 344 11927 23508 13722 2479 -2026 845 C ATOM 1594 CA ARG B 344 201.737 275.068 803.684 1.00129.69 C ANISOU 1594 CA ARG B 344 12008 23909 13360 2693 -2146 630 C ATOM 1595 N ARG B 344 200.463 275.780 803.849 1.00127.92 N ANISOU 1595 N ARG B 344 11948 23840 12816 2589 -2331 971 N ATOM 1596 CB ARG B 344 202.762 275.931 802.938 1.00131.92 C ANISOU 1596 CB ARG B 344 12140 24390 13595 2970 -2009 662 C ATOM 1597 O ARG B 344 203.058 273.599 805.032 1.00130.66 O ANISOU 1597 O ARG B 344 11976 23419 14251 2501 -1848 518 O ATOM 1598 C LYS B 345 201.627 274.106 808.262 1.00155.96 C ANISOU 1598 C LYS B 345 15412 26525 17320 1936 -2100 1687 C ATOM 1599 CA LYS B 345 202.553 274.993 807.429 1.00157.51 C ANISOU 1599 CA LYS B 345 15482 26851 17512 2152 -1991 1709 C ATOM 1600 N LYS B 345 201.998 275.276 806.099 1.00157.31 N ANISOU 1600 N LYS B 345 15525 27043 17201 2292 -2103 1389 N ATOM 1601 CB LYS B 345 202.876 276.296 808.180 1.00157.85 C ANISOU 1601 CB LYS B 345 15451 27059 17467 2111 -2012 2297 C ATOM 1602 O LYS B 345 202.106 273.256 809.008 1.00156.64 O ANISOU 1602 O LYS B 345 15429 26376 17710 1907 -1938 1727 O ATOM 1603 C ILE B 346 199.469 271.982 808.165 1.00124.35 C ANISOU 1603 C ILE B 346 11713 22319 13217 1700 -2331 1041 C ATOM 1604 CA ILE B 346 199.342 273.390 808.771 1.00124.08 C ANISOU 1604 CA ILE B 346 11683 22510 12950 1621 -2441 1550 C ATOM 1605 N ILE B 346 200.311 274.285 808.123 1.00125.49 N ANISOU 1605 N ILE B 346 11726 22805 13150 1810 -2336 1641 N ATOM 1606 CB ILE B 346 197.882 273.888 808.613 1.00122.48 C ANISOU 1606 CB ILE B 346 11658 22469 12410 1482 -2676 1563 C ATOM 1607 CG1 ILE B 346 197.777 275.382 808.881 1.00122.84 C ANISOU 1607 CG1 ILE B 346 11658 22720 12295 1423 -2753 1961 C ATOM 1608 CD1 ILE B 346 196.358 275.888 808.803 1.00121.88 C ANISOU 1608 CD1 ILE B 346 11673 22680 11955 1271 -2913 1981 C ATOM 1609 CG2 ILE B 346 196.925 273.120 809.536 1.00121.26 C ANISOU 1609 CG2 ILE B 346 11634 22212 12226 1266 -2780 1547 C ATOM 1610 O ILE B 346 198.754 271.052 808.537 1.00123.39 O ANISOU 1610 O ILE B 346 11690 22063 13129 1580 -2378 901 O ATOM 1611 C LEU B 347 202.099 270.139 806.955 1.00129.47 C ANISOU 1611 C LEU B 347 11917 22423 14855 2048 -1715 169 C ATOM 1612 CA LEU B 347 200.686 270.564 806.582 1.00127.11 C ANISOU 1612 CA LEU B 347 11834 22430 14030 1975 -2048 165 C ATOM 1613 N LEU B 347 200.391 271.842 807.217 1.00125.99 N ANISOU 1613 N LEU B 347 11779 22496 13595 1901 -2178 733 N ATOM 1614 CB LEU B 347 200.592 270.691 805.062 1.00127.99 C ANISOU 1614 CB LEU B 347 11903 22804 13922 2176 -2128 -321 C ATOM 1615 CG LEU B 347 199.198 270.886 804.474 1.00126.35 C ANISOU 1615 CG LEU B 347 11871 22882 13252 2177 -2386 -387 C ATOM 1616 CD1 LEU B 347 199.280 271.610 803.134 1.00127.72 C ANISOU 1616 CD1 LEU B 347 11978 23455 13093 2462 -2435 -567 C ATOM 1617 CD2 LEU B 347 198.517 269.544 804.316 1.00125.92 C ANISOU 1617 CD2 LEU B 347 11852 22695 13295 2103 -2434 -824 C ATOM 1618 O LEU B 347 202.468 268.976 806.817 1.00130.89 O ANISOU 1618 O LEU B 347 11979 22302 15453 2057 -1523 -224 O ATOM 1619 C GLN B 348 204.228 270.095 809.169 1.00162.38 C ANISOU 1619 C GLN B 348 15780 26103 19813 2102 -1102 1096 C ATOM 1620 CA GLN B 348 204.260 270.814 807.832 1.00162.32 C ANISOU 1620 CA GLN B 348 15783 26346 19547 2201 -1250 730 C ATOM 1621 N GLN B 348 202.894 271.096 807.417 1.00159.78 N ANISOU 1621 N GLN B 348 15677 26319 18713 2105 -1615 622 N ATOM 1622 CB GLN B 348 205.074 272.110 807.937 1.00163.19 C ANISOU 1622 CB GLN B 348 15809 26635 19561 2314 -1192 1159 C ATOM 1623 O GLN B 348 204.768 269.002 809.319 1.00164.22 O ANISOU 1623 O GLN B 348 15877 25953 20568 2137 -796 905 O ATOM 1624 C TYR B 349 202.326 269.333 811.768 1.00140.05 C ANISOU 1624 C TYR B 349 13218 23379 16614 1798 -1354 1855 C ATOM 1625 CA TYR B 349 203.542 270.205 811.500 1.00141.81 C ANISOU 1625 CA TYR B 349 13266 23639 16975 1950 -1185 2038 C ATOM 1626 N TYR B 349 203.564 270.716 810.135 1.00141.33 N ANISOU 1626 N TYR B 349 13235 23676 16787 1990 -1306 1607 N ATOM 1627 CB TYR B 349 203.604 271.363 812.505 1.00141.85 C ANISOU 1627 CB TYR B 349 13241 23997 16660 1937 -1304 2673 C ATOM 1628 CG TYR B 349 204.890 272.145 812.427 1.00143.93 C ANISOU 1628 CG TYR B 349 13305 24276 17105 2109 -1086 2950 C ATOM 1629 CD1 TYR B 349 206.096 271.543 812.746 1.00146.77 C ANISOU 1629 CD1 TYR B 349 13453 24317 17997 2294 -641 3112 C ATOM 1630 CE1 TYR B 349 207.277 272.231 812.668 1.00148.85 C ANISOU 1630 CE1 TYR B 349 13532 24570 18455 2461 -409 3371 C ATOM 1631 CZ TYR B 349 207.267 273.546 812.267 1.00147.99 C ANISOU 1631 CZ TYR B 349 13451 24791 17989 2446 -640 3472 C ATOM 1632 OH TYR B 349 208.456 274.237 812.194 1.00150.14 O ANISOU 1632 OH TYR B 349 13537 25053 18457 2623 -399 3745 O ATOM 1633 CE2 TYR B 349 206.080 274.172 811.940 1.00145.28 C ANISOU 1633 CE2 TYR B 349 13306 24757 17138 2266 -1070 3324 C ATOM 1634 CD2 TYR B 349 204.900 273.469 812.019 1.00143.33 C ANISOU 1634 CD2 TYR B 349 13240 24498 16719 2099 -1281 3063 C ATOM 1635 O TYR B 349 202.042 268.992 812.917 1.00140.22 O ANISOU 1635 O TYR B 349 13251 23426 16599 1765 -1325 2213 O ATOM 1636 C SER B 350 200.965 266.642 810.543 1.00171.01 C ANISOU 1636 C SER B 350 17282 26782 20912 1667 -1352 698 C ATOM 1637 CA SER B 350 200.479 268.066 810.807 1.00169.28 C ANISOU 1637 CA SER B 350 17200 26992 20128 1606 -1656 1078 C ATOM 1638 N SER B 350 201.609 268.984 810.704 1.00170.81 N ANISOU 1638 N SER B 350 17237 27258 20406 1736 -1523 1309 N ATOM 1639 CB SER B 350 199.376 268.454 809.816 1.00167.17 C ANISOU 1639 CB SER B 350 17114 26963 19440 1531 -1984 737 C ATOM 1640 OG SER B 350 198.086 268.169 810.333 1.00165.28 O ANISOU 1640 OG SER B 350 17072 26792 18936 1367 -2186 791 O ATOM 1641 O SER B 350 201.770 266.415 809.630 1.00172.77 O ANISOU 1641 O SER B 350 17339 26840 21464 1769 -1179 290 O ATOM 1642 C ARG B 351 199.988 263.333 810.669 1.00129.33 C ANISOU 1642 C ARG B 351 11978 20758 16402 1554 -1055 2 C ATOM 1643 CA ARG B 351 201.008 264.326 811.240 1.00130.55 C ANISOU 1643 CA ARG B 351 12029 21009 16565 1665 -913 518 C ATOM 1644 N ARG B 351 200.496 265.688 811.342 1.00128.39 N ANISOU 1644 N ARG B 351 11927 21203 15653 1609 -1269 808 N ATOM 1645 CB ARG B 351 201.525 263.844 812.597 1.00132.48 C ANISOU 1645 CB ARG B 351 12162 21046 17130 1762 -566 1097 C ATOM 1646 O ARG B 351 200.324 262.184 810.370 1.00131.24 O ANISOU 1646 O ARG B 351 12053 20615 17199 1574 -791 -375 O ATOM 1647 C THR B 352 196.557 263.737 809.325 1.00120.54 C ANISOU 1647 C THR B 352 11446 20343 14011 1281 -1998 -557 C ATOM 1648 CA THR B 352 197.646 262.934 810.062 1.00122.98 C ANISOU 1648 CA THR B 352 11545 20253 14929 1342 -1603 -418 C ATOM 1649 N THR B 352 198.750 263.793 810.502 1.00124.30 N ANISOU 1649 N THR B 352 11591 20459 15179 1438 -1449 -22 N ATOM 1650 CB THR B 352 197.068 262.143 811.274 1.00122.63 C ANISOU 1650 CB THR B 352 11594 20049 14952 1279 -1513 -86 C ATOM 1651 OG1 THR B 352 195.677 261.871 811.086 1.00120.37 O ANISOU 1651 OG1 THR B 352 11530 19896 14308 1156 -1787 -265 O ATOM 1652 CG2 THR B 352 197.230 262.941 812.544 1.00122.60 C ANISOU 1652 CG2 THR B 352 11638 20246 14696 1297 -1514 588 C ATOM 1653 O THR B 352 196.090 264.753 809.814 1.00119.08 O ANISOU 1653 O THR B 352 11413 20419 13412 1219 -2185 -168 O ATOM 1654 C TRP B 353 194.110 264.735 808.046 1.00121.56 C ANISOU 1654 C TRP B 353 11963 21076 13148 1196 -2600 -772 C ATOM 1655 CA TRP B 353 195.215 263.990 807.290 1.00123.91 C ANISOU 1655 CA TRP B 353 11996 21206 13878 1333 -2401 -1231 C ATOM 1656 N TRP B 353 196.177 263.281 808.137 1.00125.51 N ANISOU 1656 N TRP B 353 12046 21028 14616 1316 -2098 -1116 N ATOM 1657 CB TRP B 353 194.588 263.022 806.273 1.00124.27 C ANISOU 1657 CB TRP B 353 11997 21286 13932 1378 -2478 -1813 C ATOM 1658 CG TRP B 353 193.555 262.113 806.878 1.00122.91 C ANISOU 1658 CG TRP B 353 11976 20939 13786 1238 -2509 -1773 C ATOM 1659 CD1 TRP B 353 193.763 260.867 807.374 1.00123.88 C ANISOU 1659 CD1 TRP B 353 12002 20688 14379 1179 -2306 -1908 C ATOM 1660 NE1 TRP B 353 192.591 260.350 807.862 1.00122.20 N ANISOU 1660 NE1 TRP B 353 11988 20431 14012 1070 -2398 -1794 N ATOM 1661 CE2 TRP B 353 191.595 261.273 807.695 1.00120.20 C ANISOU 1661 CE2 TRP B 353 11961 20502 13209 1042 -2653 -1601 C ATOM 1662 CZ2 TRP B 353 190.249 261.203 808.023 1.00118.36 C ANISOU 1662 CZ2 TRP B 353 11967 20328 12677 939 -2797 -1459 C ATOM 1663 CH2 TRP B 353 189.473 262.283 807.734 1.00117.13 C ANISOU 1663 CH2 TRP B 353 11972 20458 12073 933 -2981 -1279 C ATOM 1664 CZ3 TRP B 353 190.007 263.417 807.125 1.00117.63 C ANISOU 1664 CZ3 TRP B 353 11965 20766 11963 1042 -3030 -1211 C ATOM 1665 CE3 TRP B 353 191.347 263.488 806.796 1.00119.28 C ANISOU 1665 CE3 TRP B 353 11951 20955 12414 1156 -2914 -1348 C ATOM 1666 CD2 TRP B 353 192.165 262.397 807.084 1.00120.64 C ANISOU 1666 CD2 TRP B 353 11953 20817 13069 1149 -2718 -1564 C ATOM 1667 O TRP B 353 193.635 265.772 807.576 1.00120.75 O ANISOU 1667 O TRP B 353 11952 21260 12667 1222 -2768 -663 O ATOM 1668 C TYR B 354 193.009 265.936 810.829 1.00117.78 C ANISOU 1668 C TYR B 354 11790 20737 12224 866 -2768 267 C ATOM 1669 CA TYR B 354 192.563 264.825 809.905 1.00117.49 C ANISOU 1669 CA TYR B 354 11772 20550 12318 914 -2749 -202 C ATOM 1670 N TYR B 354 193.673 264.204 809.189 1.00119.21 N ANISOU 1670 N TYR B 354 11767 20604 12922 1062 -2560 -524 N ATOM 1671 CB TYR B 354 191.694 263.818 810.665 1.00116.78 C ANISOU 1671 CB TYR B 354 11811 20298 12261 803 -2741 -193 C ATOM 1672 CG TYR B 354 192.460 262.877 811.546 1.00118.20 C ANISOU 1672 CG TYR B 354 11867 20212 12833 845 -2487 -59 C ATOM 1673 CD1 TYR B 354 192.510 261.526 811.260 1.00118.93 C ANISOU 1673 CD1 TYR B 354 11881 20007 13303 885 -2319 -368 C ATOM 1674 CE1 TYR B 354 193.214 260.650 812.068 1.00120.71 C ANISOU 1674 CE1 TYR B 354 11966 19938 13961 950 -2016 -196 C ATOM 1675 CZ TYR B 354 193.871 261.136 813.166 1.00121.79 C ANISOU 1675 CZ TYR B 354 12044 20141 14089 1007 -1891 317 C ATOM 1676 OH TYR B 354 194.576 260.280 813.966 1.00124.02 O ANISOU 1676 OH TYR B 354 12168 20148 14807 1128 -1536 567 O ATOM 1677 CE2 TYR B 354 193.827 262.469 813.471 1.00121.04 C ANISOU 1677 CE2 TYR B 354 12020 20398 13572 964 -2096 600 C ATOM 1678 CD2 TYR B 354 193.124 263.329 812.669 1.00119.24 C ANISOU 1678 CD2 TYR B 354 11928 20401 12976 866 -2388 398 C ATOM 1679 O TYR B 354 192.201 266.792 811.179 1.00116.89 O ANISOU 1679 O TYR B 354 11804 20817 11790 742 -2942 457 O ATOM 1680 C GLU B 355 194.922 268.287 811.267 1.00117.73 C ANISOU 1680 C GLU B 355 11521 21052 12159 974 -2711 900 C ATOM 1681 CA GLU B 355 194.850 266.996 812.071 1.00118.07 C ANISOU 1681 CA GLU B 355 11570 20870 12419 955 -2576 899 C ATOM 1682 N GLU B 355 194.286 265.930 811.219 1.00117.35 N ANISOU 1682 N GLU B 355 11549 20590 12448 964 -2569 439 N ATOM 1683 CB GLU B 355 196.235 266.630 812.623 1.00120.24 C ANISOU 1683 CB GLU B 355 11627 20979 13081 1102 -2276 1124 C ATOM 1684 O GLU B 355 194.585 269.358 811.779 1.00117.52 O ANISOU 1684 O GLU B 355 11526 21251 11876 872 -2853 1182 O ATOM 1685 C SER B 356 193.903 269.652 808.766 1.00115.67 C ANISOU 1685 C SER B 356 11377 21123 11450 1097 -2953 514 C ATOM 1686 CA SER B 356 195.342 269.256 809.032 1.00117.14 C ANISOU 1686 CA SER B 356 11373 21164 11971 1199 -2754 528 C ATOM 1687 N SER B 356 195.353 268.165 810.005 1.00117.21 N ANISOU 1687 N SER B 356 11387 20941 12205 1115 -2654 561 N ATOM 1688 CB SER B 356 195.977 268.816 807.718 1.00118.29 C ANISOU 1688 CB SER B 356 11393 21293 12258 1407 -2659 82 C ATOM 1689 OG SER B 356 196.942 267.799 807.921 1.00119.75 O ANISOU 1689 OG SER B 356 11419 21194 12888 1454 -2433 -106 O ATOM 1690 O SER B 356 193.506 270.777 809.022 1.00115.47 O ANISOU 1690 O SER B 356 11390 21253 11229 1015 -3046 793 O ATOM 1691 C PHE B 357 191.151 269.870 809.114 1.00117.98 C ANISOU 1691 C PHE B 357 12021 21473 11334 804 -3208 557 C ATOM 1692 CA PHE B 357 191.712 269.001 807.996 1.00118.41 C ANISOU 1692 CA PHE B 357 11992 21496 11502 1028 -3127 190 C ATOM 1693 N PHE B 357 193.115 268.718 808.254 1.00119.53 N ANISOU 1693 N PHE B 357 11959 21539 11916 1104 -2990 186 N ATOM 1694 CB PHE B 357 190.898 267.709 807.833 1.00117.65 C ANISOU 1694 CB PHE B 357 11995 21264 11441 1000 -3145 -118 C ATOM 1695 CG PHE B 357 189.451 267.952 807.512 1.00116.77 C ANISOU 1695 CG PHE B 357 12055 21231 11080 950 -3241 -104 C ATOM 1696 CD1 PHE B 357 188.997 267.900 806.214 1.00117.18 C ANISOU 1696 CD1 PHE B 357 12095 21457 10971 1159 -3252 -309 C ATOM 1697 CE1 PHE B 357 187.655 268.141 805.918 1.00116.75 C ANISOU 1697 CE1 PHE B 357 12183 21455 10722 1147 -3281 -229 C ATOM 1698 CZ PHE B 357 186.765 268.448 806.929 1.00115.92 C ANISOU 1698 CZ PHE B 357 12234 21190 10619 887 -3305 -11 C ATOM 1699 CE2 PHE B 357 187.209 268.509 808.214 1.00115.59 C ANISOU 1699 CE2 PHE B 357 12195 21023 10700 667 -3333 126 C ATOM 1700 CD2 PHE B 357 188.546 268.268 808.506 1.00116.01 C ANISOU 1700 CD2 PHE B 357 12105 21062 10911 718 -3299 116 C ATOM 1701 O PHE B 357 190.642 270.957 808.877 1.00118.13 O ANISOU 1701 O PHE B 357 12066 21619 11201 774 -3256 722 O ATOM 1702 C CYS B 358 191.537 271.527 811.452 1.00117.08 C ANISOU 1702 C CYS B 358 11788 21546 11152 484 -3305 1210 C ATOM 1703 CA CYS B 358 190.808 270.195 811.457 1.00116.02 C ANISOU 1703 CA CYS B 358 11804 21239 11041 459 -3302 951 C ATOM 1704 N CYS B 358 191.252 269.394 810.341 1.00115.76 N ANISOU 1704 N CYS B 358 11749 21094 11141 661 -3204 675 N ATOM 1705 CB CYS B 358 191.051 269.493 812.780 1.00116.51 C ANISOU 1705 CB CYS B 358 11839 21276 11153 389 -3279 1075 C ATOM 1706 SG CYS B 358 190.876 270.633 814.137 1.00117.88 S ANISOU 1706 SG CYS B 358 11926 21738 11124 199 -3415 1382 S ATOM 1707 O CYS B 358 190.908 272.571 811.315 1.00117.33 O ANISOU 1707 O CYS B 358 11833 21672 11076 387 -3374 1301 O ATOM 1708 C GLY B 359 193.133 273.803 810.772 1.00129.75 C ANISOU 1708 C GLY B 359 13098 23418 12784 663 -3233 1625 C ATOM 1709 CA GLY B 359 193.677 272.689 811.646 1.00129.80 C ANISOU 1709 CA GLY B 359 13079 23330 12907 662 -3182 1611 C ATOM 1710 N GLY B 359 192.860 271.485 811.607 1.00128.65 N ANISOU 1710 N GLY B 359 13094 23022 12765 617 -3198 1340 N ATOM 1711 O GLY B 359 192.690 274.827 811.269 1.00130.41 O ANISOU 1711 O GLY B 359 13139 23616 12794 503 -3314 1811 O ATOM 1712 C PHE B 360 191.268 275.060 809.054 1.00121.11 C ANISOU 1712 C PHE B 360 12151 22363 11501 701 -3239 1566 C ATOM 1713 CA PHE B 360 192.543 274.455 808.484 1.00121.16 C ANISOU 1713 CA PHE B 360 12077 22398 11562 950 -3162 1450 C ATOM 1714 N PHE B 360 193.195 273.598 809.460 1.00120.94 N ANISOU 1714 N PHE B 360 12016 22273 11664 867 -3164 1421 N ATOM 1715 CB PHE B 360 192.163 273.634 807.256 1.00120.74 C ANISOU 1715 CB PHE B 360 12103 22349 11424 1162 -3128 1124 C ATOM 1716 CG PHE B 360 193.329 273.190 806.411 1.00121.55 C ANISOU 1716 CG PHE B 360 12082 22522 11581 1430 -3043 904 C ATOM 1717 CD1 PHE B 360 193.668 271.852 806.315 1.00121.35 C ANISOU 1717 CD1 PHE B 360 12044 22371 11695 1468 -3018 542 C ATOM 1718 CE1 PHE B 360 194.725 271.442 805.531 1.00122.68 C ANISOU 1718 CE1 PHE B 360 12058 22584 11972 1690 -2921 252 C ATOM 1719 CZ PHE B 360 195.445 272.361 804.824 1.00124.06 C ANISOU 1719 CZ PHE B 360 12113 22967 12058 1900 -2861 338 C ATOM 1720 CE2 PHE B 360 195.113 273.692 804.900 1.00124.06 C ANISOU 1720 CE2 PHE B 360 12143 23105 11890 1890 -2884 754 C ATOM 1721 CD2 PHE B 360 194.056 274.102 805.682 1.00122.89 C ANISOU 1721 CD2 PHE B 360 12126 22876 11690 1647 -2967 1025 C ATOM 1722 O PHE B 360 191.212 276.247 809.324 1.00122.20 O ANISOU 1722 O PHE B 360 12193 22569 11667 607 -3237 1805 O ATOM 1723 C LEU B 361 189.050 275.649 810.911 1.00121.67 C ANISOU 1723 C LEU B 361 12325 22325 11580 95 -3405 1582 C ATOM 1724 CA LEU B 361 188.943 274.661 809.751 1.00120.33 C ANISOU 1724 CA LEU B 361 12292 22075 11354 345 -3331 1396 C ATOM 1725 N LEU B 361 190.244 274.229 809.229 1.00120.12 N ANISOU 1725 N LEU B 361 12184 22119 11337 590 -3288 1367 N ATOM 1726 CB LEU B 361 188.143 273.441 810.214 1.00119.16 C ANISOU 1726 CB LEU B 361 12310 21795 11169 228 -3391 1159 C ATOM 1727 CG LEU B 361 186.991 272.880 809.387 1.00118.47 C ANISOU 1727 CG LEU B 361 12386 21595 11032 298 -3337 985 C ATOM 1728 CD1 LEU B 361 185.969 273.951 809.072 1.00119.65 C ANISOU 1728 CD1 LEU B 361 12541 21695 11227 230 -3245 1125 C ATOM 1729 CD2 LEU B 361 187.526 272.259 808.126 1.00118.07 C ANISOU 1729 CD2 LEU B 361 12320 21620 10922 622 -3279 848 C ATOM 1730 O LEU B 361 188.345 276.650 810.980 1.00122.93 O ANISOU 1730 O LEU B 361 12433 22460 11817 -53 -3379 1664 O ATOM 1731 C LEU B 362 190.882 277.438 812.755 1.00122.31 C ANISOU 1731 C LEU B 362 11941 22812 11720 -87 -3531 2052 C ATOM 1732 CA LEU B 362 190.078 276.153 813.029 1.00120.95 C ANISOU 1732 CA LEU B 362 11973 22517 11464 -150 -3579 1791 C ATOM 1733 N LEU B 362 189.938 275.342 811.836 1.00119.28 N ANISOU 1733 N LEU B 362 11931 22129 11261 60 -3477 1643 N ATOM 1734 CB LEU B 362 190.720 275.336 814.170 1.00121.13 C ANISOU 1734 CB LEU B 362 11946 22678 11402 -148 -3646 1831 C ATOM 1735 CG LEU B 362 189.971 274.214 814.897 1.00120.58 C ANISOU 1735 CG LEU B 362 12017 22569 11229 -243 -3707 1643 C ATOM 1736 CD1 LEU B 362 190.844 273.659 816.009 1.00121.60 C ANISOU 1736 CD1 LEU B 362 12023 22897 11281 -158 -3714 1822 C ATOM 1737 CD2 LEU B 362 188.635 274.675 815.452 1.00121.53 C ANISOU 1737 CD2 LEU B 362 12170 22725 11279 -528 -3822 1464 C ATOM 1738 O LEU B 362 190.514 278.522 813.218 1.00124.07 O ANISOU 1738 O LEU B 362 12018 23117 12004 -284 -3577 2125 O ATOM 1739 C TYR B 363 192.883 279.201 810.554 1.00150.57 C ANISOU 1739 C TYR B 363 15286 26479 15446 454 -3234 2519 C ATOM 1740 CA TYR B 363 192.923 278.431 811.876 1.00150.31 C ANISOU 1740 CA TYR B 363 15253 26495 15363 268 -3373 2437 C ATOM 1741 N TYR B 363 191.977 277.321 812.003 1.00148.94 N ANISOU 1741 N TYR B 363 15282 26188 15122 182 -3426 2161 N ATOM 1742 CB TYR B 363 194.333 277.973 812.249 1.00150.48 C ANISOU 1742 CB TYR B 363 15169 26601 15404 432 -3327 2572 C ATOM 1743 CG TYR B 363 194.387 277.623 813.702 1.00151.28 C ANISOU 1743 CG TYR B 363 15188 26855 15435 280 -3438 2640 C ATOM 1744 CD1 TYR B 363 195.048 278.434 814.614 1.00153.29 C ANISOU 1744 CD1 TYR B 363 15197 27380 15666 235 -3489 2919 C ATOM 1745 CE1 TYR B 363 195.061 278.121 815.959 1.00154.59 C ANISOU 1745 CE1 TYR B 363 15253 27790 15695 149 -3595 2993 C ATOM 1746 CZ TYR B 363 194.392 276.993 816.397 1.00153.75 C ANISOU 1746 CZ TYR B 363 15305 27620 15491 101 -3636 2796 C ATOM 1747 OH TYR B 363 194.390 276.651 817.726 1.00155.42 O ANISOU 1747 OH TYR B 363 15400 28133 15518 69 -3726 2890 O ATOM 1748 CE2 TYR B 363 193.722 276.188 815.512 1.00151.52 C ANISOU 1748 CE2 TYR B 363 15281 27018 15274 115 -3582 2519 C ATOM 1749 CD2 TYR B 363 193.714 276.509 814.180 1.00150.37 C ANISOU 1749 CD2 TYR B 363 15221 26666 15245 203 -3492 2437 C ATOM 1750 O TYR B 363 192.913 280.432 810.570 1.00152.14 O ANISOU 1750 O TYR B 363 15331 26741 15735 398 -3198 2736 O ATOM 1751 C TYR B 364 191.300 279.863 808.062 1.00129.24 C ANISOU 1751 C TYR B 364 12751 23632 12723 784 -2957 2518 C ATOM 1752 CA TYR B 364 192.647 279.154 808.133 1.00128.42 C ANISOU 1752 CA TYR B 364 12616 23629 12548 932 -3008 2439 C ATOM 1753 N TYR B 364 192.808 278.493 809.424 1.00127.73 N ANISOU 1753 N TYR B 364 12535 23508 12489 691 -3149 2350 N ATOM 1754 CB TYR B 364 192.788 278.169 806.987 1.00127.60 C ANISOU 1754 CB TYR B 364 12618 23556 12306 1232 -2955 2182 C ATOM 1755 CG TYR B 364 192.852 278.841 805.635 1.00128.90 C ANISOU 1755 CG TYR B 364 12732 23881 12361 1575 -2805 2297 C ATOM 1756 CD1 TYR B 364 194.025 279.438 805.191 1.00130.06 C ANISOU 1756 CD1 TYR B 364 12735 24181 12499 1800 -2720 2437 C ATOM 1757 CE1 TYR B 364 194.085 280.054 803.951 1.00131.63 C ANISOU 1757 CE1 TYR B 364 12876 24585 12551 2161 -2572 2558 C ATOM 1758 CZ TYR B 364 192.962 280.067 803.143 1.00132.18 C ANISOU 1758 CZ TYR B 364 13020 24718 12482 2322 -2491 2577 C ATOM 1759 OH TYR B 364 193.004 280.671 801.916 1.00134.21 O ANISOU 1759 OH TYR B 364 13199 25244 12552 2744 -2319 2750 O ATOM 1760 CE2 TYR B 364 191.795 279.483 803.560 1.00131.01 C ANISOU 1760 CE2 TYR B 364 13014 24389 12375 2097 -2557 2455 C ATOM 1761 CD2 TYR B 364 191.742 278.871 804.795 1.00129.31 C ANISOU 1761 CD2 TYR B 364 12868 23958 12304 1715 -2722 2294 C ATOM 1762 O TYR B 364 191.133 280.918 808.659 1.00130.73 O ANISOU 1762 O TYR B 364 12797 23805 13070 583 -2949 2707 O ATOM 1763 C ILE B 365 187.877 278.904 807.422 1.00125.79 C ANISOU 1763 C ILE B 365 12683 22813 12300 635 -2832 2201 C ATOM 1764 CA ILE B 365 189.012 279.915 807.313 1.00126.97 C ANISOU 1764 CA ILE B 365 12638 23108 12496 743 -2791 2459 C ATOM 1765 N ILE B 365 190.334 279.300 807.344 1.00125.83 N ANISOU 1765 N ILE B 365 12474 23123 12214 881 -2900 2371 N ATOM 1766 CB ILE B 365 188.833 280.870 806.112 1.00128.86 C ANISOU 1766 CB ILE B 365 12797 23396 12769 1053 -2536 2759 C ATOM 1767 CG1 ILE B 365 188.561 280.108 804.817 1.00128.49 C ANISOU 1767 CG1 ILE B 365 12865 23487 12467 1451 -2448 2675 C ATOM 1768 CD1 ILE B 365 188.304 281.019 803.609 1.00130.91 C ANISOU 1768 CD1 ILE B 365 13078 23914 12749 1836 -2163 3027 C ATOM 1769 CG2 ILE B 365 190.053 281.752 805.955 1.00129.91 C ANISOU 1769 CG2 ILE B 365 12748 23690 12920 1197 -2496 3003 C ATOM 1770 O ILE B 365 187.836 277.923 806.694 1.00124.62 O ANISOU 1770 O ILE B 365 12657 22725 11970 860 -2837 2035 O ATOM 1771 C PRO B 366 184.758 278.254 807.771 1.00122.88 C ANISOU 1771 C PRO B 366 12586 21966 12137 274 -2691 1941 C ATOM 1772 CA PRO B 366 185.934 278.171 808.702 1.00122.05 C ANISOU 1772 CA PRO B 366 12397 22015 11961 131 -2919 1872 C ATOM 1773 N PRO B 366 186.955 279.149 808.356 1.00123.12 N ANISOU 1773 N PRO B 366 12351 22296 12134 281 -2862 2134 N ATOM 1774 CD PRO B 366 186.908 280.294 809.274 1.00125.10 C ANISOU 1774 CD PRO B 366 12409 22504 12621 -23 -2874 2235 C ATOM 1775 CG PRO B 366 186.452 279.653 810.538 1.00124.59 C ANISOU 1775 CG PRO B 366 12400 22414 12526 -357 -3073 1947 C ATOM 1776 CB PRO B 366 185.487 278.607 810.107 1.00123.21 C ANISOU 1776 CB PRO B 366 12460 22084 12269 -297 -3028 1760 C ATOM 1777 O PRO B 366 183.885 279.077 807.988 1.00124.86 O ANISOU 1777 O PRO B 366 12770 22014 12658 95 -2533 2029 O ATOM 1778 C SER B 367 183.445 275.811 805.531 1.00134.00 C ANISOU 1778 C SER B 367 14348 23482 13085 929 -2561 1691 C ATOM 1779 CA SER B 367 183.549 277.258 805.926 1.00135.91 C ANISOU 1779 CA SER B 367 14436 23622 13581 774 -2444 1959 C ATOM 1780 N SER B 367 184.734 277.406 806.757 1.00135.08 N ANISOU 1780 N SER B 367 14245 23614 13464 601 -2654 1890 N ATOM 1781 CB SER B 367 183.662 278.085 804.657 1.00137.94 C ANISOU 1781 CB SER B 367 14575 24035 13803 1187 -2191 2311 C ATOM 1782 OG SER B 367 184.415 277.382 803.683 1.00137.17 O ANISOU 1782 OG SER B 367 14481 24282 13355 1581 -2269 2221 O ATOM 1783 O SER B 367 184.446 275.126 805.404 1.00132.67 O ANISOU 1783 O SER B 367 14169 23501 12739 1044 -2725 1517 O ATOM 1784 C LEU B 368 181.973 273.911 803.342 1.00154.91 C ANISOU 1784 C LEU B 368 17165 26401 15293 1605 -2400 1532 C ATOM 1785 CA LEU B 368 182.047 273.977 804.881 1.00153.56 C ANISOU 1785 CA LEU B 368 17064 25922 15362 1093 -2547 1398 C ATOM 1786 N LEU B 368 182.229 275.344 805.316 1.00155.06 N ANISOU 1786 N LEU B 368 17134 26007 15776 935 -2450 1649 N ATOM 1787 CB LEU B 368 180.807 273.374 805.553 1.00153.02 C ANISOU 1787 CB LEU B 368 17159 25567 15415 829 -2529 1254 C ATOM 1788 CG LEU B 368 179.447 273.980 805.183 1.00155.16 C ANISOU 1788 CG LEU B 368 17448 25627 15876 866 -2219 1490 C ATOM 1789 CD1 LEU B 368 178.316 273.125 805.761 1.00154.44 C ANISOU 1789 CD1 LEU B 368 17534 25283 15861 645 -2218 1280 C ATOM 1790 CD2 LEU B 368 179.328 275.438 805.632 1.00157.33 C ANISOU 1790 CD2 LEU B 368 17592 25701 16483 663 -2050 1720 C ATOM 1791 O LEU B 368 181.954 272.828 802.749 1.00154.24 O ANISOU 1791 O LEU B 368 17112 26507 14985 1811 -2486 1301 O ATOM 1792 C GLU B 369 183.313 274.936 800.691 1.00146.59 C ANISOU 1792 C GLU B 369 15762 26216 13719 2632 -2190 1909 C ATOM 1793 CA GLU B 369 181.902 275.097 801.238 1.00146.80 C ANISOU 1793 CA GLU B 369 15912 25847 14019 2387 -2015 2082 C ATOM 1794 N GLU B 369 181.948 275.069 802.694 1.00144.88 N ANISOU 1794 N GLU B 369 15768 25217 14063 1834 -2172 1904 N ATOM 1795 CB GLU B 369 181.250 276.384 800.731 1.00149.90 C ANISOU 1795 CB GLU B 369 16203 26171 14582 2591 -1633 2610 C ATOM 1796 CG GLU B 369 179.758 276.267 800.395 1.00151.53 C ANISOU 1796 CG GLU B 369 16469 26206 14901 2702 -1339 2824 C ATOM 1797 CD GLU B 369 178.972 275.448 801.414 1.00149.47 C ANISOU 1797 CD GLU B 369 16399 25561 14832 2249 -1463 2507 C ATOM 1798 OE1 GLU B 369 178.389 276.043 802.346 1.00149.90 O ANISOU 1798 OE1 GLU B 369 16487 25171 15297 1846 -1352 2549 O ATOM 1799 OE2 GLU B 369 178.930 274.204 801.287 1.00147.72 O ANISOU 1799 OE2 GLU B 369 16275 25494 14359 2297 -1667 2189 O ATOM 1800 O GLU B 369 183.528 274.861 799.475 1.00148.38 O ANISOU 1800 O GLU B 369 15869 26887 13622 3120 -2127 1947 O ATOM 1801 C LEU B 370 186.020 273.231 801.612 1.00125.38 C ANISOU 1801 C LEU B 370 13030 23633 10978 2330 -2764 1013 C ATOM 1802 CA LEU B 370 185.652 274.644 801.225 1.00127.37 C ANISOU 1802 CA LEU B 370 13220 23933 11242 2487 -2539 1497 C ATOM 1803 N LEU B 370 184.272 274.872 801.608 1.00127.52 N ANISOU 1803 N LEU B 370 13356 23664 11433 2310 -2396 1709 N ATOM 1804 CB LEU B 370 186.581 275.620 801.928 1.00127.27 C ANISOU 1804 CB LEU B 370 13134 23802 11422 2290 -2553 1677 C ATOM 1805 CG LEU B 370 186.775 277.022 801.371 1.00129.60 C ANISOU 1805 CG LEU B 370 13292 24227 11725 2525 -2340 2111 C ATOM 1806 CD1 LEU B 370 187.962 277.689 802.011 1.00129.30 C ANISOU 1806 CD1 LEU B 370 13159 24139 11828 2358 -2413 2178 C ATOM 1807 CD2 LEU B 370 187.002 276.918 799.873 1.00131.66 C ANISOU 1807 CD2 LEU B 370 13440 24974 11611 3100 -2248 2116 C ATOM 1808 O LEU B 370 187.145 272.776 801.381 1.00125.32 O ANISOU 1808 O LEU B 370 12918 23788 10909 2428 -2872 732 O ATOM 1809 C SER B 371 186.093 270.357 801.698 1.00130.48 C ANISOU 1809 C SER B 371 13739 24242 11597 2230 -3048 126 C ATOM 1810 CA SER B 371 185.168 271.140 802.597 1.00129.76 C ANISOU 1810 CA SER B 371 13804 23836 11662 1942 -2964 504 C ATOM 1811 N SER B 371 185.045 272.551 802.206 1.00131.44 N ANISOU 1811 N SER B 371 13952 24143 11846 2088 -2797 920 N ATOM 1812 CB SER B 371 183.805 270.449 802.548 1.00129.38 C ANISOU 1812 CB SER B 371 13894 23679 11586 1909 -2925 459 C ATOM 1813 OG SER B 371 183.209 270.386 803.823 1.00127.94 O ANISOU 1813 OG SER B 371 13873 23114 11626 1497 -2949 505 O ATOM 1814 O SER B 371 187.194 269.972 802.090 1.00129.95 O ANISOU 1814 O SER B 371 13599 24106 11669 2127 -3132 -101 O ATOM 1815 C ALA B 372 187.656 269.517 799.254 1.00123.34 C ANISOU 1815 C ALA B 372 12391 24238 10236 3008 -3133 -602 C ATOM 1816 CA ALA B 372 186.218 269.199 799.568 1.00122.20 C ANISOU 1816 CA ALA B 372 12431 23906 10094 2880 -3103 -425 C ATOM 1817 N ALA B 372 185.623 270.154 800.474 1.00120.99 N ANISOU 1817 N ALA B 372 12454 23404 10112 2612 -3001 59 N ATOM 1818 CB ALA B 372 185.411 269.119 798.304 1.00124.50 C ANISOU 1818 CB ALA B 372 12629 24665 10008 3322 -3041 -399 C ATOM 1819 O ALA B 372 188.408 268.627 798.852 1.00124.22 O ANISOU 1819 O ALA B 372 12339 24491 10367 3090 -3223 -1118 O ATOM 1820 C GLU B 373 190.344 271.065 800.304 1.00120.91 C ANISOU 1820 C GLU B 373 11948 23673 10318 2785 -3076 -366 C ATOM 1821 CA GLU B 373 189.402 271.207 799.111 1.00122.66 C ANISOU 1821 CA GLU B 373 12137 24314 10154 3165 -3036 -312 C ATOM 1822 N GLU B 373 188.037 270.780 799.434 1.00121.38 N ANISOU 1822 N GLU B 373 12148 23970 10003 3017 -3038 -198 N ATOM 1823 CB GLU B 373 189.436 272.631 798.532 1.00124.44 C ANISOU 1823 CB GLU B 373 12305 24801 10175 3451 -2888 155 C ATOM 1824 O GLU B 373 191.504 270.696 800.147 1.00121.77 O ANISOU 1824 O GLU B 373 11905 23823 10538 2839 -3090 -696 O ATOM 1825 C TYR B 374 190.907 269.577 802.770 1.00139.83 C ANISOU 1825 C TYR B 374 14497 25219 13413 2047 -3155 -554 C ATOM 1826 CA TYR B 374 190.574 271.059 802.717 1.00140.09 C ANISOU 1826 CA TYR B 374 14577 25377 13275 2096 -3110 -69 C ATOM 1827 N TYR B 374 189.838 271.351 801.497 1.00141.50 N ANISOU 1827 N TYR B 374 14730 25899 13132 2424 -3075 -49 N ATOM 1828 CB TYR B 374 189.736 271.426 803.933 1.00138.47 C ANISOU 1828 CB TYR B 374 14547 24884 13183 1749 -3130 261 C ATOM 1829 CG TYR B 374 189.593 272.897 804.127 1.00139.07 C ANISOU 1829 CG TYR B 374 14615 24990 13234 1713 -3065 702 C ATOM 1830 CD1 TYR B 374 190.551 273.618 804.803 1.00139.26 C ANISOU 1830 CD1 TYR B 374 14551 24965 13395 1601 -3059 904 C ATOM 1831 CE1 TYR B 374 190.429 274.994 804.990 1.00140.11 C ANISOU 1831 CE1 TYR B 374 14615 25098 13522 1553 -2996 1290 C ATOM 1832 CZ TYR B 374 189.343 275.646 804.479 1.00140.93 C ANISOU 1832 CZ TYR B 374 14763 25231 13553 1623 -2899 1485 C ATOM 1833 OH TYR B 374 189.204 277.000 804.649 1.00142.20 O ANISOU 1833 OH TYR B 374 14847 25366 13817 1566 -2794 1853 O ATOM 1834 CE2 TYR B 374 188.385 274.939 803.794 1.00140.82 C ANISOU 1834 CE2 TYR B 374 14845 25259 13401 1762 -2874 1327 C ATOM 1835 CD2 TYR B 374 188.513 273.575 803.618 1.00139.82 C ANISOU 1835 CD2 TYR B 374 14762 25154 13208 1806 -2977 931 C ATOM 1836 O TYR B 374 192.036 269.186 803.070 1.00140.26 O ANISOU 1836 O TYR B 374 14432 25143 13717 2004 -3114 -734 O ATOM 1837 C LEU B 375 190.999 266.758 801.402 1.00124.03 C ANISOU 1837 C LEU B 375 12243 23356 11525 2271 -3230 -1747 C ATOM 1838 CA LEU B 375 190.073 267.309 802.497 1.00121.61 C ANISOU 1838 CA LEU B 375 12204 22791 11210 2005 -3235 -1214 C ATOM 1839 N LEU B 375 189.907 268.756 802.477 1.00121.63 N ANISOU 1839 N LEU B 375 12268 22930 11017 2058 -3206 -747 N ATOM 1840 CB LEU B 375 188.700 266.642 802.439 1.00120.69 C ANISOU 1840 CB LEU B 375 12230 22650 10979 1960 -3288 -1259 C ATOM 1841 CG LEU B 375 188.589 265.144 802.142 1.00121.11 C ANISOU 1841 CG LEU B 375 12195 22654 11168 1972 -3324 -1764 C ATOM 1842 CD1 LEU B 375 189.292 264.324 803.199 1.00120.39 C ANISOU 1842 CD1 LEU B 375 12088 22134 11520 1714 -3262 -1876 C ATOM 1843 CD2 LEU B 375 187.122 264.716 802.054 1.00120.24 C ANISOU 1843 CD2 LEU B 375 12243 22555 10888 1957 -3363 -1702 C ATOM 1844 O LEU B 375 191.547 265.675 801.535 1.00124.59 O ANISOU 1844 O LEU B 375 12192 23235 11911 2192 -3202 -2160 O ATOM 1845 C GLN B 376 193.484 267.293 799.535 1.00134.47 C ANISOU 1845 C GLN B 376 13029 25282 12780 2824 -3143 -2421 C ATOM 1846 CA GLN B 376 192.026 266.983 799.245 1.00133.57 C ANISOU 1846 CA GLN B 376 13049 25331 12371 2869 -3247 -2347 C ATOM 1847 N GLN B 376 191.178 267.493 800.316 1.00130.69 N ANISOU 1847 N GLN B 376 12969 24642 12045 2599 -3235 -1761 N ATOM 1848 CB GLN B 376 191.595 267.483 797.841 1.00135.99 C ANISOU 1848 CB GLN B 376 13238 26297 12136 3323 -3295 -2398 C ATOM 1849 CG GLN B 376 192.523 268.515 797.150 1.00138.24 C ANISOU 1849 CG GLN B 376 13370 26945 12211 3625 -3235 -2335 C ATOM 1850 CD GLN B 376 193.781 267.900 796.544 1.00141.14 C ANISOU 1850 CD GLN B 376 13431 27478 12716 3752 -3238 -3040 C ATOM 1851 OE1 GLN B 376 194.825 268.555 796.462 1.00142.32 O ANISOU 1851 OE1 GLN B 376 13484 27663 12926 3834 -3153 -3020 O ATOM 1852 NE2 GLN B 376 193.682 266.642 796.120 1.00142.59 N ANISOU 1852 NE2 GLN B 376 13439 27751 12987 3761 -3321 -3692 N ATOM 1853 O GLN B 376 194.329 266.401 799.450 1.00135.99 O ANISOU 1853 O GLN B 376 13023 25335 13312 2786 -3090 -2943 O ATOM 1854 C MET B 377 195.724 267.992 801.224 1.00139.27 C ANISOU 1854 C MET B 377 13584 25216 14115 2500 -2873 -2034 C ATOM 1855 CA MET B 377 195.143 268.955 800.189 1.00139.99 C ANISOU 1855 CA MET B 377 13697 25830 13664 2799 -2967 -1890 C ATOM 1856 N MET B 377 193.776 268.550 799.879 1.00139.12 N ANISOU 1856 N MET B 377 13705 25866 13287 2825 -3086 -1904 N ATOM 1857 CB MET B 377 195.204 270.385 800.746 1.00138.87 C ANISOU 1857 CB MET B 377 13680 25661 13425 2751 -2925 -1221 C ATOM 1858 CG MET B 377 194.396 271.437 800.017 1.00139.28 C ANISOU 1858 CG MET B 377 13795 26096 13031 2991 -2955 -882 C ATOM 1859 SD MET B 377 194.586 273.087 800.771 1.00138.44 S ANISOU 1859 SD MET B 377 13774 25874 12954 2880 -2872 -149 S ATOM 1860 CE MET B 377 195.975 273.724 799.834 1.00141.31 C ANISOU 1860 CE MET B 377 13908 26566 13219 3242 -2766 -274 C ATOM 1861 O MET B 377 196.800 267.419 801.031 1.00141.31 O ANISOU 1861 O MET B 377 13625 25353 14713 2535 -2749 -2457 O ATOM 1862 C SER B 378 195.848 265.583 803.034 1.00131.66 C ANISOU 1862 C SER B 378 12625 23313 14087 1998 -2689 -2300 C ATOM 1863 CA SER B 378 195.442 267.001 803.444 1.00129.86 C ANISOU 1863 CA SER B 378 12597 23256 13489 1979 -2781 -1663 C ATOM 1864 N SER B 378 194.991 267.815 802.321 1.00130.45 N ANISOU 1864 N SER B 378 12675 23796 13095 2224 -2901 -1681 N ATOM 1865 CB SER B 378 194.355 266.949 804.520 1.00127.30 C ANISOU 1865 CB SER B 378 12520 22755 13093 1735 -2860 -1263 C ATOM 1866 OG SER B 378 194.936 266.779 805.797 1.00126.94 O ANISOU 1866 OG SER B 378 12478 22385 13371 1557 -2733 -975 O ATOM 1867 O SER B 378 196.843 265.051 803.509 1.00132.94 O ANISOU 1867 O SER B 378 12637 23133 14742 1930 -2480 -2412 O ATOM 1868 C LEU B 379 196.534 263.422 800.813 1.00130.18 C ANISOU 1868 C LEU B 379 11842 23349 14271 2278 -2651 -3985 C ATOM 1869 CA LEU B 379 195.306 263.596 801.719 1.00126.49 C ANISOU 1869 CA LEU B 379 11718 22762 13579 2100 -2758 -3378 C ATOM 1870 N LEU B 379 195.072 264.977 802.144 1.00124.51 N ANISOU 1870 N LEU B 379 11688 22646 12973 2102 -2820 -2714 N ATOM 1871 CB LEU B 379 194.057 263.015 801.033 1.00126.17 C ANISOU 1871 CB LEU B 379 11721 23004 13213 2172 -2948 -3637 C ATOM 1872 CG LEU B 379 193.095 262.146 801.853 1.00124.05 C ANISOU 1872 CG LEU B 379 11632 22408 13095 1944 -2958 -3493 C ATOM 1873 CD1 LEU B 379 193.797 261.677 803.091 1.00123.65 C ANISOU 1873 CD1 LEU B 379 11584 21795 13603 1716 -2737 -3299 C ATOM 1874 CD2 LEU B 379 191.829 262.868 802.220 1.00121.27 C ANISOU 1874 CD2 LEU B 379 11599 22179 12298 1897 -3094 -2938 C ATOM 1875 O LEU B 379 197.125 262.345 800.758 1.00132.40 O ANISOU 1875 O LEU B 379 11883 23345 15079 2209 -2497 -4515 O ATOM 1876 C GLU B 380 199.327 264.404 800.205 1.00156.28 C ANISOU 1876 C GLU B 380 14713 26649 18018 2520 -2303 -4336 C ATOM 1877 CA GLU B 380 198.115 264.380 799.276 1.00155.85 C ANISOU 1877 CA GLU B 380 14720 27146 17350 2686 -2597 -4524 C ATOM 1878 N GLU B 380 196.913 264.466 800.090 1.00152.08 N ANISOU 1878 N GLU B 380 14569 26536 16677 2511 -2708 -3938 N ATOM 1879 CB GLU B 380 198.168 265.509 798.235 1.00157.12 C ANISOU 1879 CB GLU B 380 14848 27946 16904 3029 -2723 -4488 C ATOM 1880 CG GLU B 380 199.205 265.312 797.116 1.00161.75 C ANISOU 1880 CG GLU B 380 15060 28854 17545 3279 -2670 -5265 C ATOM 1881 CD GLU B 380 200.492 266.128 797.333 1.00162.87 C ANISOU 1881 CD GLU B 380 15136 28839 17910 3318 -2463 -5091 C ATOM 1882 OE1 GLU B 380 200.501 267.021 798.221 1.00160.03 O ANISOU 1882 OE1 GLU B 380 15022 28250 17533 3207 -2405 -4311 O ATOM 1883 OE2 GLU B 380 201.498 265.887 796.614 1.00166.88 O ANISOU 1883 OE2 GLU B 380 15326 29468 18615 3463 -2355 -5757 O ATOM 1884 O GLU B 380 200.347 263.789 799.916 1.00159.56 O ANISOU 1884 O GLU B 380 14831 26862 18933 2533 -2099 -4896 O ATOM 1885 C ALA B 381 200.622 264.087 803.148 1.00152.57 C ANISOU 1885 C ALA B 381 14352 24923 18697 2078 -1720 -3298 C ATOM 1886 CA ALA B 381 200.285 265.302 802.288 1.00151.85 C ANISOU 1886 CA ALA B 381 14358 25419 17917 2269 -1985 -3214 C ATOM 1887 N ALA B 381 199.186 265.089 801.339 1.00151.42 N ANISOU 1887 N ALA B 381 14353 25798 17384 2371 -2263 -3557 N ATOM 1888 CB ALA B 381 199.987 266.508 803.188 1.00148.98 C ANISOU 1888 CB ALA B 381 14256 25113 17237 2203 -2061 -2368 C ATOM 1889 O ALA B 381 201.792 263.764 803.347 1.00155.20 O ANISOU 1889 O ALA B 381 14459 24896 19615 2083 -1397 -3443 O ATOM 1890 C ASN B 382 198.661 261.256 804.380 1.00176.44 C ANISOU 1890 C ASN B 382 17524 27277 22236 1683 -1699 -3455 C ATOM 1891 CA ASN B 382 199.794 262.270 804.533 1.00177.42 C ANISOU 1891 CA ASN B 382 17583 27411 22418 1777 -1553 -3166 C ATOM 1892 N ASN B 382 199.597 263.428 803.672 1.00176.71 N ANISOU 1892 N ASN B 382 17572 27864 21707 1928 -1820 -3170 N ATOM 1893 CB ASN B 382 199.972 262.708 805.991 1.00175.86 C ANISOU 1893 CB ASN B 382 17543 26983 22293 1691 -1411 -2344 C ATOM 1894 CG ASN B 382 199.197 263.973 806.320 1.00172.72 C ANISOU 1894 CG ASN B 382 17437 26985 21204 1672 -1716 -1783 C ATOM 1895 OD1 ASN B 382 199.728 264.906 806.925 1.00172.49 O ANISOU 1895 OD1 ASN B 382 17437 27004 21097 1694 -1662 -1278 O ATOM 1896 ND2 ASN B 382 197.938 264.019 805.899 1.00170.66 N ANISOU 1896 ND2 ASN B 382 17364 27006 20473 1635 -2015 -1881 N ATOM 1897 O ASN B 382 197.485 261.574 804.597 1.00173.46 O ANISOU 1897 O ASN B 382 17424 27134 21347 1632 -1959 -3137 O ATOM 1898 C VAL B 383 197.130 258.633 804.756 1.00170.90 C ANISOU 1898 C VAL B 383 16804 26086 22045 1444 -1650 -3933 C ATOM 1899 CA VAL B 383 198.058 259.015 803.609 1.00173.80 C ANISOU 1899 CA VAL B 383 16896 26682 22457 1594 -1646 -4497 C ATOM 1900 N VAL B 383 199.028 260.037 803.994 1.00173.99 N ANISOU 1900 N VAL B 383 16935 26675 22499 1656 -1508 -4082 N ATOM 1901 CB VAL B 383 198.753 257.742 803.079 1.00178.06 C ANISOU 1901 CB VAL B 383 17020 26883 23753 1566 -1387 -5304 C ATOM 1902 CG1 VAL B 383 199.992 258.109 802.278 1.00181.68 C ANISOU 1902 CG1 VAL B 383 17168 27419 24443 1691 -1256 -5809 C ATOM 1903 CG2 VAL B 383 199.111 256.814 804.227 1.00178.89 C ANISOU 1903 CG2 VAL B 383 17061 26290 24621 1425 -978 -5024 C ATOM 1904 O VAL B 383 197.302 259.084 805.884 1.00169.49 O ANISOU 1904 O VAL B 383 16789 25732 21877 1396 -1533 -3261 O ATOM 1905 C VAL B 384 195.441 255.950 805.873 1.00133.99 C ANISOU 1905 C VAL B 384 12208 20738 17965 1181 -1480 -3982 C ATOM 1906 CA VAL B 384 195.170 257.388 805.453 1.00131.80 C ANISOU 1906 CA VAL B 384 12142 21004 16934 1266 -1807 -3755 C ATOM 1907 N VAL B 384 196.146 257.795 804.458 1.00134.36 N ANISOU 1907 N VAL B 384 12204 21505 17341 1392 -1788 -4225 N ATOM 1908 CB VAL B 384 193.734 257.567 804.919 1.00129.38 C ANISOU 1908 CB VAL B 384 12063 21126 15972 1277 -2173 -3794 C ATOM 1909 CG1 VAL B 384 193.630 257.019 803.531 1.00131.64 C ANISOU 1909 CG1 VAL B 384 12090 21688 16238 1387 -2299 -4570 C ATOM 1910 CG2 VAL B 384 192.717 256.928 805.846 1.00127.35 C ANISOU 1910 CG2 VAL B 384 12031 20649 15706 1143 -2165 -3455 C ATOM 1911 O VAL B 384 196.042 255.187 805.125 1.00137.32 O ANISOU 1911 O VAL B 384 12279 20999 18897 1196 -1331 -4658 O ATOM 1912 C ASP B 385 194.158 253.270 807.243 1.00197.88 C ANISOU 1912 C ASP B 385 20314 28015 26856 986 -1115 -3860 C ATOM 1913 CA ASP B 385 195.232 254.261 807.620 1.00198.35 C ANISOU 1913 CA ASP B 385 20358 28072 26933 1055 -983 -3500 C ATOM 1914 N ASP B 385 195.015 255.599 807.084 1.00196.18 N ANISOU 1914 N ASP B 385 20269 28341 25930 1104 -1349 -3426 N ATOM 1915 CB ASP B 385 195.332 254.276 809.138 1.00197.69 C ANISOU 1915 CB ASP B 385 20430 27734 26950 1069 -735 -2696 C ATOM 1916 CG ASP B 385 196.675 254.717 809.610 1.00199.88 C ANISOU 1916 CG ASP B 385 20536 27799 27609 1164 -403 -2392 C ATOM 1917 OD1 ASP B 385 197.306 255.501 808.870 1.00200.37 O ANISOU 1917 OD1 ASP B 385 20509 28061 27560 1201 -504 -2643 O ATOM 1918 OD2 ASP B 385 197.098 254.286 810.703 1.00201.35 O ANISOU 1918 OD2 ASP B 385 20668 27640 28197 1233 -23 -1880 O ATOM 1919 O ASP B 385 193.014 253.351 807.697 1.00194.97 O ANISOU 1919 O ASP B 385 20257 27816 26006 945 -1319 -3511 O ATOM 1920 C ILE B 386 193.670 250.384 807.495 1.00150.51 C ANISOU 1920 C ILE B 386 13940 21166 22080 863 -629 -4386 C ATOM 1921 CA ILE B 386 193.748 251.148 806.187 1.00150.43 C ANISOU 1921 CA ILE B 386 13858 21683 21616 901 -993 -4941 C ATOM 1922 N ILE B 386 194.554 252.312 806.424 1.00149.92 N ANISOU 1922 N ILE B 386 13872 21737 21351 969 -976 -4589 N ATOM 1923 CB ILE B 386 194.396 250.280 805.125 1.00154.88 C ANISOU 1923 CB ILE B 386 13926 22102 22820 882 -863 -5880 C ATOM 1924 CG1 ILE B 386 195.751 249.781 805.633 1.00158.76 C ANISOU 1924 CG1 ILE B 386 14090 21931 24300 859 -308 -5903 C ATOM 1925 CD1 ILE B 386 196.617 249.128 804.573 1.00163.91 C ANISOU 1925 CD1 ILE B 386 14201 22423 25653 824 -145 -6906 C ATOM 1926 CG2 ILE B 386 194.573 251.085 803.838 1.00155.42 C ANISOU 1926 CG2 ILE B 386 13893 22780 22381 981 -1209 -6419 C ATOM 1927 O ILE B 386 192.736 249.617 807.702 1.00149.64 O ANISOU 1927 O ILE B 386 13922 20983 21952 815 -664 -4362 O ATOM 1928 C THR B 387 193.382 250.074 810.483 1.00133.58 C ANISOU 1928 C THR B 387 12201 18508 20045 953 -111 -2735 C ATOM 1929 CA THR B 387 194.681 249.925 809.679 1.00137.28 C ANISOU 1929 CA THR B 387 12249 18708 21202 959 137 -3290 C ATOM 1930 N THR B 387 194.639 250.616 808.386 1.00136.48 N ANISOU 1930 N THR B 387 12118 19061 20679 918 -268 -3900 N ATOM 1931 CB THR B 387 195.868 250.381 810.556 1.00139.08 C ANISOU 1931 CB THR B 387 12393 18690 21763 1086 530 -2717 C ATOM 1932 OG1 THR B 387 195.636 251.707 811.033 1.00135.84 O ANISOU 1932 OG1 THR B 387 12317 18771 20524 1130 217 -2172 O ATOM 1933 CG2 THR B 387 197.142 250.371 809.766 1.00142.72 C ANISOU 1933 CG2 THR B 387 12462 18895 22870 1088 775 -3261 C ATOM 1934 O THR B 387 192.628 249.109 810.652 1.00133.61 O ANISOU 1934 O THR B 387 12224 18337 20202 918 -53 -2787 O ATOM 1935 C ASN B 388 190.663 251.699 810.886 1.00126.34 C ANISOU 1935 C ASN B 388 12178 18640 17184 853 -1058 -2155 C ATOM 1936 CA ASN B 388 191.903 251.524 811.752 1.00129.05 C ANISOU 1936 CA ASN B 388 12320 18627 18086 960 -614 -1774 C ATOM 1937 N ASN B 388 193.117 251.277 810.978 1.00132.12 N ANISOU 1937 N ASN B 388 12331 18740 19129 981 -376 -2236 N ATOM 1938 CB ASN B 388 192.096 252.728 812.661 1.00127.71 C ANISOU 1938 CB ASN B 388 12353 18764 17406 1018 -706 -1142 C ATOM 1939 CG ASN B 388 192.985 253.767 812.046 1.00127.91 C ANISOU 1939 CG ASN B 388 12278 18966 17356 1030 -801 -1275 C ATOM 1940 OD1 ASN B 388 193.921 254.253 812.682 1.00129.25 O ANISOU 1940 OD1 ASN B 388 12360 19093 17656 1131 -592 -868 O ATOM 1941 ND2 ASN B 388 192.722 254.098 810.784 1.00126.91 N ANISOU 1941 ND2 ASN B 388 12143 19063 17015 961 -1096 -1830 N ATOM 1942 O ASN B 388 190.586 252.600 810.051 1.00125.05 O ANISOU 1942 O ASN B 388 12069 18841 16605 832 -1364 -2390 O ATOM 1943 C ASP B 389 187.574 251.978 810.518 1.00141.96 C ANISOU 1943 C ASP B 389 14783 21235 17921 705 -1749 -2184 C ATOM 1944 CA ASP B 389 188.511 250.809 810.249 1.00145.20 C ANISOU 1944 CA ASP B 389 14813 21211 19144 744 -1408 -2528 C ATOM 1945 N ASP B 389 189.688 250.831 811.102 1.00147.17 N ANISOU 1945 N ASP B 389 14919 21176 19824 816 -1059 -2168 N ATOM 1946 CB ASP B 389 187.773 249.467 810.370 1.00145.83 C ANISOU 1946 CB ASP B 389 14860 21017 19530 720 -1275 -2659 C ATOM 1947 CG ASP B 389 188.411 248.368 809.526 1.00149.12 C ANISOU 1947 CG ASP B 389 14848 21111 20699 715 -1063 -3291 C ATOM 1948 OD1 ASP B 389 189.662 248.353 809.420 1.00151.73 O ANISOU 1948 OD1 ASP B 389 14887 21205 21558 744 -814 -3437 O ATOM 1949 OD2 ASP B 389 187.665 247.522 808.978 1.00149.40 O ANISOU 1949 OD2 ASP B 389 14815 21129 20823 678 -1133 -3662 O ATOM 1950 O ASP B 389 186.369 251.872 810.320 1.00140.27 O ANISOU 1950 O ASP B 389 14769 21178 17349 659 -1946 -2236 O ATOM 1951 C TRP B 390 187.697 255.470 810.426 1.00132.82 C ANISOU 1951 C TRP B 390 13981 20932 15554 678 -2287 -1669 C ATOM 1952 CA TRP B 390 187.295 254.260 811.260 1.00133.34 C ANISOU 1952 CA TRP B 390 14076 20692 15894 661 -2087 -1548 C ATOM 1953 N TRP B 390 188.125 253.097 810.960 1.00135.84 N ANISOU 1953 N TRP B 390 14082 20635 16896 721 -1797 -1845 N ATOM 1954 CB TRP B 390 187.408 254.622 812.745 1.00133.35 C ANISOU 1954 CB TRP B 390 14206 20709 15751 664 -1988 -966 C ATOM 1955 CG TRP B 390 188.566 255.532 813.063 1.00134.26 C ANISOU 1955 CG TRP B 390 14204 20921 15889 721 -1927 -712 C ATOM 1956 CD1 TRP B 390 189.753 255.185 813.638 1.00136.62 C ANISOU 1956 CD1 TRP B 390 14281 20988 16639 841 -1599 -483 C ATOM 1957 NE1 TRP B 390 190.560 256.289 813.753 1.00136.87 N ANISOU 1957 NE1 TRP B 390 14258 21217 16529 874 -1642 -273 N ATOM 1958 CE2 TRP B 390 189.900 257.379 813.243 1.00134.68 C ANISOU 1958 CE2 TRP B 390 14161 21290 15722 767 -1999 -374 C ATOM 1959 CZ2 TRP B 390 190.306 258.712 813.133 1.00134.21 C ANISOU 1959 CZ2 TRP B 390 14110 21512 15373 754 -2156 -233 C ATOM 1960 CH2 TRP B 390 189.422 259.597 812.572 1.00132.30 C ANISOU 1960 CH2 TRP B 390 14045 21545 14676 651 -2460 -350 C ATOM 1961 CZ3 TRP B 390 188.161 259.184 812.121 1.00130.89 C ANISOU 1961 CZ3 TRP B 390 14038 21376 14317 575 -2602 -588 C ATOM 1962 CE3 TRP B 390 187.760 257.868 812.230 1.00131.19 C ANISOU 1962 CE3 TRP B 390 14077 21164 14605 586 -2473 -736 C ATOM 1963 CD2 TRP B 390 188.641 256.939 812.802 1.00133.11 C ANISOU 1963 CD2 TRP B 390 14136 21112 15326 677 -2169 -635 C ATOM 1964 O TRP B 390 186.870 256.325 810.090 1.00131.11 O ANISOU 1964 O TRP B 390 13957 21014 14843 639 -2536 -1628 O ATOM 1965 C GLU B 391 188.939 256.851 808.074 1.00123.22 C ANISOU 1965 C GLU B 391 12448 20180 14191 848 -2509 -2294 C ATOM 1966 CA GLU B 391 189.558 256.694 809.453 1.00123.67 C ANISOU 1966 CA GLU B 391 12514 19944 14530 798 -2274 -1855 C ATOM 1967 N GLU B 391 188.987 255.544 810.122 1.00123.76 N ANISOU 1967 N GLU B 391 12577 19681 14764 751 -2135 -1795 N ATOM 1968 CB GLU B 391 191.070 256.530 809.357 1.00126.20 C ANISOU 1968 CB GLU B 391 12533 20043 15376 878 -2013 -1970 C ATOM 1969 CG GLU B 391 191.826 257.830 809.366 1.00126.11 C ANISOU 1969 CG GLU B 391 12516 20248 15153 924 -2070 -1733 C ATOM 1970 CD GLU B 391 193.303 257.622 809.591 1.00128.78 C ANISOU 1970 CD GLU B 391 12577 20297 16056 1003 -1739 -1714 C ATOM 1971 OE1 GLU B 391 193.699 256.462 809.803 1.00130.82 O ANISOU 1971 OE1 GLU B 391 12648 20155 16902 1017 -1440 -1859 O ATOM 1972 OE2 GLU B 391 194.065 258.612 809.553 1.00129.09 O ANISOU 1972 OE2 GLU B 391 12572 20482 15993 1058 -1746 -1543 O ATOM 1973 O GLU B 391 188.393 257.902 807.759 1.00121.81 O ANISOU 1973 O GLU B 391 12431 20325 13526 860 -2718 -2149 O ATOM 1974 C GLN B 392 186.978 256.286 805.892 1.00119.28 C ANISOU 1974 C GLN B 392 11967 20197 13156 989 -2877 -3000 C ATOM 1975 CA GLN B 392 188.439 255.844 805.917 1.00121.61 C ANISOU 1975 CA GLN B 392 11959 20246 14002 1001 -2671 -3258 C ATOM 1976 N GLN B 392 188.997 255.795 807.265 1.00121.34 N ANISOU 1976 N GLN B 392 11992 19844 14267 895 -2454 -2821 N ATOM 1977 CB GLN B 392 188.598 254.502 805.212 1.00124.04 C ANISOU 1977 CB GLN B 392 11960 20424 14746 1032 -2587 -3883 C ATOM 1978 CG GLN B 392 187.927 254.449 803.845 1.00124.79 C ANISOU 1978 CG GLN B 392 11951 20995 14470 1185 -2826 -4333 C ATOM 1979 CD GLN B 392 188.479 255.459 802.850 1.00125.91 C ANISOU 1979 CD GLN B 392 11969 21599 14272 1371 -2966 -4511 C ATOM 1980 OE1 GLN B 392 189.673 255.505 802.590 1.00128.09 O ANISOU 1980 OE1 GLN B 392 11990 21819 14857 1405 -2861 -4808 O ATOM 1981 NE2 GLN B 392 187.599 256.243 802.266 1.00124.79 N ANISOU 1981 NE2 GLN B 392 11989 21910 13516 1515 -3169 -4327 N ATOM 1982 O GLN B 392 186.616 257.205 805.170 1.00118.84 O ANISOU 1982 O GLN B 392 11972 20518 12664 1098 -3043 -2964 O ATOM 1983 C PRO B 393 184.499 257.512 806.838 1.00120.20 C ANISOU 1983 C PRO B 393 12730 20494 12446 838 -3089 -2209 C ATOM 1984 CA PRO B 393 184.721 256.016 806.697 1.00121.43 C ANISOU 1984 CA PRO B 393 12700 20420 13019 850 -2978 -2582 C ATOM 1985 N PRO B 393 186.131 255.635 806.685 1.00123.31 N ANISOU 1985 N PRO B 393 12658 20480 13713 873 -2828 -2805 N ATOM 1986 CD PRO B 393 186.379 254.409 807.468 1.00124.14 C ANISOU 1986 CD PRO B 393 12683 20155 14328 791 -2602 -2828 C ATOM 1987 CG PRO B 393 185.013 254.039 807.986 1.00122.43 C ANISOU 1987 CG PRO B 393 12735 19898 13883 716 -2655 -2614 C ATOM 1988 CB PRO B 393 184.191 255.290 807.928 1.00120.54 C ANISOU 1988 CB PRO B 393 12760 19974 13066 703 -2858 -2331 C ATOM 1989 O PRO B 393 183.632 258.052 806.169 1.00119.76 O ANISOU 1989 O PRO B 393 12770 20694 12039 919 -3200 -2174 O ATOM 1990 SG CYS B 394 184.378 261.106 810.158 1.00116.16 S ANISOU 1990 SG CYS B 394 12722 20068 11344 394 -3186 -846 S ATOM 1991 CB CYS B 394 185.563 260.086 809.250 1.00117.32 C ANISOU 1991 CB CYS B 394 12598 20120 11858 579 -3078 -1205 C ATOM 1992 CA CYS B 394 184.964 259.587 807.936 1.00117.49 C ANISOU 1992 CA CYS B 394 12573 20254 11814 709 -3135 -1566 C ATOM 1993 C CYS B 394 185.348 260.461 806.753 1.00118.24 C ANISOU 1993 C CYS B 394 12545 20662 11720 885 -3212 -1674 C ATOM 1994 O CYS B 394 184.730 261.494 806.517 1.00117.77 O ANISOU 1994 O CYS B 394 12602 20790 11355 904 -3281 -1455 O ATOM 1995 N CYS B 394 185.259 258.182 807.691 1.00118.44 N ANISOU 1995 N CYS B 394 12534 20184 12285 756 -3036 -1913 N ATOM 1996 N VAL B 395 186.341 260.021 805.990 1.00111.17 N ANISOU 1996 N VAL B 395 11392 19821 11027 1027 -3174 -2030 N ATOM 1997 CA VAL B 395 186.660 260.673 804.729 1.00112.41 C ANISOU 1997 CA VAL B 395 11400 20352 10961 1252 -3250 -2211 C ATOM 1998 C VAL B 395 185.438 260.696 803.834 1.00112.43 C ANISOU 1998 C VAL B 395 11468 20642 10608 1403 -3344 -2263 C ATOM 1999 O VAL B 395 185.041 261.729 803.328 1.00112.53 O ANISOU 1999 O VAL B 395 11539 20924 10292 1534 -3382 -2034 O ATOM 2000 CB VAL B 395 187.770 259.937 803.981 1.00114.72 C ANISOU 2000 CB VAL B 395 11367 20676 11544 1381 -3198 -2737 C ATOM 2001 CG1 VAL B 395 188.090 260.647 802.691 1.00116.39 C ANISOU 2001 CG1 VAL B 395 11415 21361 11448 1653 -3287 -2936 C ATOM 2002 CG2 VAL B 395 188.999 259.835 804.847 1.00115.16 C ANISOU 2002 CG2 VAL B 395 11332 20394 12030 1261 -3033 -2659 C ATOM 2003 N ASP B 396 184.836 259.533 803.654 1.00115.01 N ANISOU 2003 N ASP B 396 11769 20899 11030 1402 -3348 -2532 N ATOM 2004 CA ASP B 396 183.654 259.401 802.826 1.00115.32 C ANISOU 2004 CA ASP B 396 11848 21215 10755 1571 -3412 -2570 C ATOM 2005 C ASP B 396 182.556 260.288 803.356 1.00113.72 C ANISOU 2005 C ASP B 396 11942 20943 10323 1479 -3385 -2062 C ATOM 2006 O ASP B 396 181.733 260.784 802.598 1.00114.35 O ANISOU 2006 O ASP B 396 12053 21296 10099 1674 -3383 -1920 O ATOM 2007 CB ASP B 396 183.194 257.949 802.801 1.00115.62 C ANISOU 2007 CB ASP B 396 11821 21111 11000 1530 -3405 -2902 C ATOM 2008 CG ASP B 396 184.302 257.013 802.394 1.00117.69 C ANISOU 2008 CG ASP B 396 11749 21348 11621 1566 -3389 -3460 C ATOM 2009 OD1 ASP B 396 185.410 257.513 802.089 1.00118.91 O ANISOU 2009 OD1 ASP B 396 11732 21614 11833 1637 -3384 -3597 O ATOM 2010 OD2 ASP B 396 184.075 255.785 802.375 1.00118.37 O ANISOU 2010 OD2 ASP B 396 11724 21283 11969 1519 -3360 -3779 O ATOM 2011 N ILE B 397 182.545 260.510 804.657 1.00110.51 N ANISOU 2011 N ILE B 397 11726 20189 10074 1199 -3342 -1790 N ATOM 2012 CA ILE B 397 181.533 261.382 805.203 1.00109.53 C ANISOU 2012 CA ILE B 397 11843 19988 9787 1077 -3311 -1397 C ATOM 2013 C ILE B 397 181.766 262.795 804.700 1.00110.27 C ANISOU 2013 C ILE B 397 11896 20312 9689 1199 -3301 -1156 C ATOM 2014 O ILE B 397 180.834 263.482 804.274 1.00110.74 O ANISOU 2014 O ILE B 397 12035 20473 9570 1291 -3236 -928 O ATOM 2015 CB ILE B 397 181.552 261.382 806.698 1.00108.31 C ANISOU 2015 CB ILE B 397 11846 19515 9790 777 -3292 -1214 C ATOM 2016 CG1 ILE B 397 181.364 259.952 807.192 1.00107.87 C ANISOU 2016 CG1 ILE B 397 11817 19231 9939 698 -3261 -1408 C ATOM 2017 CD1 ILE B 397 181.539 259.788 808.678 1.00107.22 C ANISOU 2017 CD1 ILE B 397 11845 18905 9989 475 -3224 -1229 C ATOM 2018 CG2 ILE B 397 180.445 262.295 807.211 1.00107.91 C ANISOU 2018 CG2 ILE B 397 12002 19402 9599 632 -3260 -914 C ATOM 2019 N ILE B 398 183.026 263.217 804.730 1.00121.37 N ANISOU 2019 N ILE B 398 13161 21783 11170 1218 -3329 -1188 N ATOM 2020 CA ILE B 398 183.411 264.551 804.265 1.00122.22 C ANISOU 2020 CA ILE B 398 13206 22108 11123 1347 -3310 -956 C ATOM 2021 C ILE B 398 183.322 264.688 802.746 1.00124.07 C ANISOU 2021 C ILE B 398 13281 22767 11092 1736 -3302 -1070 C ATOM 2022 O ILE B 398 183.353 265.798 802.214 1.00125.12 O ANISOU 2022 O ILE B 398 13373 23115 11051 1910 -3243 -813 O ATOM 2023 CB ILE B 398 184.850 264.888 804.681 1.00122.34 C ANISOU 2023 CB ILE B 398 13097 22090 11296 1288 -3328 -970 C ATOM 2024 CG1 ILE B 398 185.102 264.465 806.124 1.00121.13 C ANISOU 2024 CG1 ILE B 398 13035 21603 11384 989 -3327 -896 C ATOM 2025 CD1 ILE B 398 186.571 264.410 806.499 1.00121.63 C ANISOU 2025 CD1 ILE B 398 12939 21604 11670 979 -3295 -942 C ATOM 2026 CG2 ILE B 398 185.104 266.341 804.514 1.00122.94 C ANISOU 2026 CG2 ILE B 398 13151 22315 11246 1349 -3298 -651 C ATOM 2027 N SER B 399 183.229 263.561 802.045 1.00113.71 N ANISOU 2027 N SER B 399 11848 21611 9745 1895 -3352 -1454 N ATOM 2028 CA SER B 399 183.242 263.578 800.590 1.00116.10 C ANISOU 2028 CA SER B 399 11939 22434 9739 2309 -3373 -1633 C ATOM 2029 C SER B 399 181.842 263.656 800.028 1.00116.76 C ANISOU 2029 C SER B 399 12105 22692 9568 2504 -3296 -1400 C ATOM 2030 O SER B 399 181.647 264.047 798.883 1.00119.06 O ANISOU 2030 O SER B 399 12248 23464 9526 2903 -3260 -1336 O ATOM 2031 CB SER B 399 183.953 262.348 800.050 1.00117.42 C ANISOU 2031 CB SER B 399 11855 22751 10007 2400 -3473 -2247 C ATOM 2032 OG SER B 399 185.332 262.389 800.361 1.00117.61 O ANISOU 2032 OG SER B 399 11753 22648 10286 2295 -3483 -2453 O ATOM 2033 N GLY B 400 180.865 263.299 800.843 1.00153.68 N ANISOU 2033 N GLY B 400 17004 26993 14393 2249 -3246 -1249 N ATOM 2034 CA GLY B 400 179.492 263.289 800.392 1.00154.42 C ANISOU 2034 CA GLY B 400 17181 27176 14314 2415 -3129 -1019 C ATOM 2035 C GLY B 400 179.040 261.868 800.143 1.00154.52 C ANISOU 2035 C GLY B 400 17139 27237 14333 2454 -3203 -1373 C ATOM 2036 O GLY B 400 177.856 261.560 800.278 1.00154.22 O ANISOU 2036 O GLY B 400 17244 27061 14290 2431 -3108 -1209 O ATOM 2037 N LYS B 401 179.991 261.005 799.784 1.00150.02 N ANISOU 2037 N LYS B 401 16343 26840 13820 2506 -3352 -1877 N ATOM 2038 CA LYS B 401 179.717 259.584 799.581 1.00150.42 C ANISOU 2038 CA LYS B 401 16285 26910 13959 2511 -3427 -2289 C ATOM 2039 C LYS B 401 179.390 258.925 800.914 1.00147.86 C ANISOU 2039 C LYS B 401 16198 25984 13998 2100 -3391 -2245 C ATOM 2040 O LYS B 401 180.256 258.320 801.552 1.00147.15 O ANISOU 2040 O LYS B 401 16057 25621 14234 1884 -3429 -2501 O ATOM 2041 CB LYS B 401 180.917 258.882 798.946 1.00152.32 C ANISOU 2041 CB LYS B 401 16180 27417 14278 2621 -3563 -2900 C ATOM 2042 N ILE B 402 178.137 259.050 801.339 1.00144.42 N ANISOU 2042 N ILE B 402 16009 25347 13519 2018 -3284 -1904 N ATOM 2043 CA ILE B 402 177.702 258.479 802.600 1.00142.35 C ANISOU 2043 CA ILE B 402 15979 24578 13529 1669 -3242 -1844 C ATOM 2044 C ILE B 402 177.693 256.953 802.524 1.00142.60 C ANISOU 2044 C ILE B 402 15890 24546 13747 1655 -3290 -2240 C ATOM 2045 O ILE B 402 178.571 256.312 803.087 1.00142.19 O ANISOU 2045 O ILE B 402 15760 24263 14002 1486 -3319 -2479 O ATOM 2046 CB ILE B 402 176.335 259.053 803.018 1.00141.73 C ANISOU 2046 CB ILE B 402 16172 24309 13370 1590 -3095 -1432 C ATOM 2047 CG1 ILE B 402 176.503 260.516 803.446 1.00141.48 C ANISOU 2047 CG1 ILE B 402 16245 24197 13313 1484 -3032 -1092 C ATOM 2048 CD1 ILE B 402 175.214 261.170 803.929 1.00141.43 C ANISOU 2048 CD1 ILE B 402 16468 23940 13330 1359 -2851 -748 C ATOM 2049 CG2 ILE B 402 175.731 258.250 804.148 1.00140.17 C ANISOU 2049 CG2 ILE B 402 16185 23687 13386 1299 -3058 -1447 C ATOM 2050 N HIS B 403 176.728 256.388 801.802 1.00132.29 N ANISOU 2050 N HIS B 403 14537 23443 12283 1855 -3271 -2289 N ATOM 2051 CA HIS B 403 176.529 254.931 801.696 1.00132.78 C ANISOU 2051 CA HIS B 403 14473 23448 12529 1846 -3304 -2649 C ATOM 2052 C HIS B 403 177.734 254.045 802.041 1.00132.99 C ANISOU 2052 C HIS B 403 14299 23276 12956 1689 -3358 -3082 C ATOM 2053 O HIS B 403 177.577 253.027 802.711 1.00132.36 O ANISOU 2053 O HIS B 403 14259 22842 13188 1512 -3299 -3185 O ATOM 2054 CB HIS B 403 175.951 254.548 800.317 1.00135.32 C ANISOU 2054 CB HIS B 403 14550 24314 12549 2229 -3352 -2821 C ATOM 2055 CG HIS B 403 176.680 255.157 799.165 1.00137.70 C ANISOU 2055 CG HIS B 403 14564 25199 12558 2553 -3453 -2991 C ATOM 2056 ND1 HIS B 403 176.540 256.481 798.796 1.00138.11 N ANISOU 2056 ND1 HIS B 403 14694 25488 12294 2744 -3388 -2585 N ATOM 2057 CE1 HIS B 403 177.305 256.734 797.752 1.00140.63 C ANISOU 2057 CE1 HIS B 403 14703 26364 12367 3053 -3496 -2847 C ATOM 2058 NE2 HIS B 403 177.941 255.619 797.425 1.00142.02 N ANISOU 2058 NE2 HIS B 403 14586 26670 12707 3045 -3639 -3467 N ATOM 2059 CD2 HIS B 403 177.572 254.624 798.290 1.00140.24 C ANISOU 2059 CD2 HIS B 403 14492 25930 12861 2732 -3602 -3551 C ATOM 2060 N SER B 404 178.924 254.429 801.587 1.00127.76 N ANISOU 2060 N SER B 404 13411 22817 12317 1767 -3430 -3319 N ATOM 2061 CA SER B 404 180.146 253.663 801.858 1.00128.57 C ANISOU 2061 CA SER B 404 13283 22693 12873 1632 -3421 -3735 C ATOM 2062 C SER B 404 180.473 253.575 803.362 1.00126.47 C ANISOU 2062 C SER B 404 13245 21848 12961 1318 -3288 -3453 C ATOM 2063 O SER B 404 181.503 253.022 803.763 1.00127.20 O ANISOU 2063 O SER B 404 13172 21672 13488 1209 -3205 -3671 O ATOM 2064 CB SER B 404 181.334 254.274 801.113 1.00130.39 C ANISOU 2064 CB SER B 404 13252 23248 13041 1783 -3496 -4003 C ATOM 2065 OG SER B 404 180.902 255.043 800.010 1.00131.67 O ANISOU 2065 OG SER B 404 13352 23994 12683 2104 -3594 -3936 O ATOM 2066 N ILE B 405 179.591 254.137 804.183 1.00122.62 N ANISOU 2066 N ILE B 405 13108 21192 12290 1196 -3245 -2972 N ATOM 2067 CA ILE B 405 179.704 254.071 805.637 1.00121.04 C ANISOU 2067 CA ILE B 405 13122 20560 12306 944 -3137 -2684 C ATOM 2068 C ILE B 405 179.014 252.811 806.150 1.00120.81 C ANISOU 2068 C ILE B 405 13158 20245 12501 861 -3042 -2734 C ATOM 2069 O ILE B 405 179.603 252.023 806.892 1.00121.11 O ANISOU 2069 O ILE B 405 13130 19962 12927 759 -2917 -2779 O ATOM 2070 CB ILE B 405 179.066 255.331 806.294 1.00119.46 C ANISOU 2070 CB ILE B 405 13232 20364 11795 843 -3148 -2219 C ATOM 2071 CG1 ILE B 405 180.091 256.445 806.340 1.00119.56 C ANISOU 2071 CG1 ILE B 405 13182 20492 11755 840 -3189 -2107 C ATOM 2072 CD1 ILE B 405 181.493 255.917 806.165 1.00120.79 C ANISOU 2072 CD1 ILE B 405 13058 20596 12239 878 -3162 -2402 C ATOM 2073 CG2 ILE B 405 178.544 255.053 807.675 1.00118.27 C ANISOU 2073 CG2 ILE B 405 13326 19885 11726 630 -3062 -1969 C ATOM 2074 N LEU B 406 177.774 252.617 805.703 1.00125.69 N ANISOU 2074 N LEU B 406 13882 20983 12890 939 -3068 -2702 N ATOM 2075 CA LEU B 406 176.870 251.624 806.270 1.00125.19 C ANISOU 2075 CA LEU B 406 13955 20658 12955 859 -2971 -2650 C ATOM 2076 C LEU B 406 177.347 250.169 806.192 1.00126.56 C ANISOU 2076 C LEU B 406 13869 20635 13582 861 -2893 -3006 C ATOM 2077 O LEU B 406 177.028 249.369 807.076 1.00126.15 O ANISOU 2077 O LEU B 406 13927 20247 13759 754 -2756 -2890 O ATOM 2078 CB LEU B 406 175.483 251.773 805.648 1.00125.10 C ANISOU 2078 CB LEU B 406 14072 20841 12617 980 -2992 -2543 C ATOM 2079 CG LEU B 406 174.959 253.207 805.659 1.00124.36 C ANISOU 2079 CG LEU B 406 14194 20883 12174 984 -3003 -2195 C ATOM 2080 CD1 LEU B 406 173.918 253.417 804.582 1.00125.34 C ANISOU 2080 CD1 LEU B 406 14303 21306 12015 1222 -2991 -2131 C ATOM 2081 CD2 LEU B 406 174.406 253.564 807.012 1.00122.95 C ANISOU 2081 CD2 LEU B 406 14335 20384 11997 742 -2916 -1889 C ATOM 2082 N PRO B 407 178.080 249.807 805.127 1.00114.33 N ANISOU 2082 N PRO B 407 11953 19305 12181 992 -2963 -3463 N ATOM 2083 CA PRO B 407 178.621 248.445 805.112 1.00116.16 C ANISOU 2083 CA PRO B 407 11890 19286 12961 955 -2851 -3850 C ATOM 2084 C PRO B 407 179.813 248.281 806.050 1.00116.48 C ANISOU 2084 C PRO B 407 11866 18920 13472 819 -2667 -3783 C ATOM 2085 O PRO B 407 180.130 247.164 806.439 1.00117.81 O ANISOU 2085 O PRO B 407 11868 18725 14168 759 -2473 -3923 O ATOM 2086 CB PRO B 407 179.052 248.251 803.654 1.00118.81 C ANISOU 2086 CB PRO B 407 11815 20049 13278 1138 -2998 -4426 C ATOM 2087 CG PRO B 407 178.267 249.265 802.891 1.00118.17 C ANISOU 2087 CG PRO B 407 11873 20472 12553 1328 -3171 -4238 C ATOM 2088 CD PRO B 407 178.167 250.444 803.806 1.00115.59 C ANISOU 2088 CD PRO B 407 11928 19987 12002 1210 -3133 -3681 C ATOM 2089 N VAL B 408 180.479 249.374 806.397 1.00123.04 N ANISOU 2089 N VAL B 408 12799 19809 14143 790 -2696 -3547 N ATOM 2090 CA VAL B 408 181.545 249.303 807.385 1.00123.44 C ANISOU 2090 CA VAL B 408 12809 19504 14590 697 -2494 -3370 C ATOM 2091 C VAL B 408 180.902 249.296 808.752 1.00121.77 C ANISOU 2091 C VAL B 408 12932 19068 14268 604 -2386 -2846 C ATOM 2092 O VAL B 408 181.292 248.520 809.623 1.00122.68 O ANISOU 2092 O VAL B 408 12996 18827 14788 576 -2144 -2703 O ATOM 2093 CB VAL B 408 182.519 250.505 807.316 1.00123.31 C ANISOU 2093 CB VAL B 408 12768 19657 14427 714 -2559 -3277 C ATOM 2094 CG1 VAL B 408 183.492 250.469 808.482 1.00123.76 C ANISOU 2094 CG1 VAL B 408 12812 19367 14843 646 -2324 -2973 C ATOM 2095 CG2 VAL B 408 183.286 250.516 806.011 1.00125.45 C ANISOU 2095 CG2 VAL B 408 12683 20174 14809 826 -2647 -3827 C ATOM 2096 N MET B 409 179.911 250.167 808.929 1.00119.99 N ANISOU 2096 N MET B 409 13024 19062 13505 576 -2541 -2569 N ATOM 2097 CA MET B 409 179.212 250.300 810.199 1.00118.75 C ANISOU 2097 CA MET B 409 13180 18780 13161 485 -2477 -2144 C ATOM 2098 C MET B 409 178.744 248.943 810.686 1.00119.39 C ANISOU 2098 C MET B 409 13260 18563 13541 489 -2291 -2142 C ATOM 2099 O MET B 409 179.057 248.536 811.805 1.00119.96 O ANISOU 2099 O MET B 409 13369 18412 13797 479 -2100 -1872 O ATOM 2100 CB MET B 409 178.027 251.248 810.057 1.00117.18 C ANISOU 2100 CB MET B 409 13263 18820 12441 446 -2643 -1994 C ATOM 2101 CG MET B 409 178.432 252.674 809.742 1.00116.71 C ANISOU 2101 CG MET B 409 13221 19022 12102 440 -2785 -1909 C ATOM 2102 SD MET B 409 179.058 253.615 811.151 1.00116.41 S ANISOU 2102 SD MET B 409 13304 18969 11959 317 -2765 -1529 S ATOM 2103 CE MET B 409 177.610 254.470 811.722 1.00115.43 C ANISOU 2103 CE MET B 409 13510 18939 11407 183 -2845 -1318 C ATOM 2104 N GLU B 410 178.002 248.238 809.840 1.00111.90 N ANISOU 2104 N GLU B 410 12247 17639 12633 534 -2332 -2420 N ATOM 2105 CA GLU B 410 177.504 246.909 810.198 1.00112.65 C ANISOU 2105 CA GLU B 410 12318 17447 13037 543 -2152 -2438 C ATOM 2106 C GLU B 410 178.625 246.000 810.707 1.00114.68 C ANISOU 2106 C GLU B 410 12311 17342 13921 560 -1879 -2463 C ATOM 2107 O GLU B 410 178.484 245.344 811.727 1.00115.16 O ANISOU 2107 O GLU B 410 12454 17138 14162 572 -1655 -2174 O ATOM 2108 CB GLU B 410 176.766 246.248 809.031 1.00113.19 C ANISOU 2108 CB GLU B 410 12250 17635 13121 611 -2241 -2804 C ATOM 2109 CG GLU B 410 177.657 245.914 807.867 1.00115.22 C ANISOU 2109 CG GLU B 410 12084 18008 13686 679 -2297 -3319 C ATOM 2110 CD GLU B 410 177.052 244.872 806.933 1.00116.71 C ANISOU 2110 CD GLU B 410 12042 18276 14026 756 -2329 -3715 C ATOM 2111 OE1 GLU B 410 175.876 244.493 807.187 1.00115.76 O ANISOU 2111 OE1 GLU B 410 12138 18111 13736 764 -2303 -3518 O ATOM 2112 OE2 GLU B 410 177.757 244.439 805.969 1.00119.10 O ANISOU 2112 OE2 GLU B 410 11931 18703 14619 811 -2377 -4244 O ATOM 2113 N SER B 411 179.750 245.972 810.004 1.00118.40 N ANISOU 2113 N SER B 411 12446 17798 14742 580 -1863 -2798 N ATOM 2114 CA SER B 411 180.861 245.101 810.387 1.00120.95 C ANISOU 2114 CA SER B 411 12464 17713 15779 598 -1540 -2855 C ATOM 2115 C SER B 411 181.286 245.298 811.836 1.00120.97 C ANISOU 2115 C SER B 411 12624 17528 15812 628 -1309 -2276 C ATOM 2116 O SER B 411 181.905 244.421 812.423 1.00123.22 O ANISOU 2116 O SER B 411 12718 17427 16675 688 -954 -2147 O ATOM 2117 CB SER B 411 182.074 245.337 809.487 1.00122.76 C ANISOU 2117 CB SER B 411 12334 17986 16324 603 -1561 -3296 C ATOM 2118 OG SER B 411 182.969 246.282 810.055 1.00122.44 O ANISOU 2118 OG SER B 411 12354 17972 16195 610 -1520 -2991 O ATOM 2119 N LEU B 412 180.952 246.456 812.405 1.00115.59 N ANISOU 2119 N LEU B 412 12257 17143 14520 605 -1493 -1926 N ATOM 2120 CA LEU B 412 181.357 246.811 813.762 1.00115.93 C ANISOU 2120 CA LEU B 412 12423 17161 14462 661 -1334 -1395 C ATOM 2121 C LEU B 412 180.224 246.522 814.704 1.00115.20 C ANISOU 2121 C LEU B 412 12624 17106 14041 678 -1310 -1078 C ATOM 2122 O LEU B 412 180.348 245.729 815.631 1.00116.85 O ANISOU 2122 O LEU B 412 12801 17103 14495 795 -1014 -771 O ATOM 2123 CB LEU B 412 181.724 248.288 813.844 1.00114.66 C ANISOU 2123 CB LEU B 412 12378 17343 13844 617 -1560 -1259 C ATOM 2124 CG LEU B 412 182.856 248.629 812.889 1.00115.49 C ANISOU 2124 CG LEU B 412 12201 17439 14239 617 -1584 -1577 C ATOM 2125 CD1 LEU B 412 183.550 249.935 813.273 1.00115.00 C ANISOU 2125 CD1 LEU B 412 12194 17621 13878 615 -1684 -1317 C ATOM 2126 CD2 LEU B 412 183.834 247.473 812.920 1.00118.41 C ANISOU 2126 CD2 LEU B 412 12223 17371 15397 695 -1208 -1684 C ATOM 2127 N ASP B 413 179.107 247.182 814.471 1.00114.98 N ANISOU 2127 N ASP B 413 12872 17350 13466 581 -1592 -1143 N ATOM 2128 CA ASP B 413 177.911 246.846 815.204 1.00114.48 C ANISOU 2128 CA ASP B 413 13077 17305 13117 581 -1572 -952 C ATOM 2129 C ASP B 413 176.664 246.998 814.344 1.00112.77 C ANISOU 2129 C ASP B 413 13029 17198 12620 489 -1786 -1215 C ATOM 2130 O ASP B 413 176.172 248.108 814.133 1.00111.39 O ANISOU 2130 O ASP B 413 13030 17281 12013 399 -2008 -1231 O ATOM 2131 CB ASP B 413 177.765 247.714 816.430 1.00114.42 C ANISOU 2131 CB ASP B 413 13284 17562 12630 580 -1627 -588 C ATOM 2132 CG ASP B 413 176.395 247.575 817.043 1.00113.95 C ANISOU 2132 CG ASP B 413 13515 17587 12194 548 -1663 -506 C ATOM 2133 OD1 ASP B 413 175.917 246.414 817.136 1.00114.59 O ANISOU 2133 OD1 ASP B 413 13598 17434 12507 626 -1477 -495 O ATOM 2134 OD2 ASP B 413 175.783 248.612 817.398 1.00113.18 O ANISOU 2134 OD2 ASP B 413 13626 17767 11611 439 -1861 -485 O ATOM 2135 N SER B 414 176.158 245.869 813.857 1.00109.89 N ANISOU 2135 N SER B 414 12586 16627 12541 526 -1684 -1397 N ATOM 2136 CA SER B 414 174.986 245.837 812.999 1.00108.76 C ANISOU 2136 CA SER B 414 12557 16583 12184 490 -1835 -1612 C ATOM 2137 C SER B 414 173.900 246.771 813.509 1.00107.39 C ANISOU 2137 C SER B 414 12743 16603 11457 410 -1960 -1422 C ATOM 2138 O SER B 414 173.253 247.456 812.735 1.00106.42 O ANISOU 2138 O SER B 414 12706 16654 11074 371 -2122 -1540 O ATOM 2139 CB SER B 414 174.463 244.411 812.922 1.00109.72 C ANISOU 2139 CB SER B 414 12600 16442 12649 553 -1652 -1693 C ATOM 2140 OG SER B 414 174.527 243.806 814.193 1.00110.71 O ANISOU 2140 OG SER B 414 12805 16361 12900 610 -1405 -1360 O ATOM 2141 N CYS B 415 173.708 246.796 814.819 1.00129.77 N ANISOU 2141 N CYS B 415 15757 19420 14130 402 -1861 -1133 N ATOM 2142 CA CYS B 415 172.663 247.612 815.416 1.00129.16 C ANISOU 2142 CA CYS B 415 15985 19509 13579 305 -1956 -1032 C ATOM 2143 C CYS B 415 172.752 249.098 815.085 1.00128.32 C ANISOU 2143 C CYS B 415 15929 19645 13181 188 -2167 -1082 C ATOM 2144 O CYS B 415 171.845 249.642 814.455 1.00127.59 O ANISOU 2144 O CYS B 415 15959 19605 12915 122 -2249 -1186 O ATOM 2145 CB CYS B 415 172.623 247.425 816.933 1.00130.44 C ANISOU 2145 CB CYS B 415 16268 19715 13579 347 -1832 -759 C ATOM 2146 SG CYS B 415 171.249 248.330 817.684 1.00130.47 S ANISOU 2146 SG CYS B 415 16604 19924 13044 204 -1938 -770 S ATOM 2147 N THR B 416 173.820 249.761 815.529 1.00108.08 N ANISOU 2147 N THR B 416 13260 17218 10587 179 -2219 -973 N ATOM 2148 CA THR B 416 173.917 251.220 815.359 1.00107.55 C ANISOU 2148 CA THR B 416 13233 17379 10253 62 -2402 -990 C ATOM 2149 C THR B 416 173.944 251.614 813.886 1.00106.60 C ANISOU 2149 C THR B 416 13014 17287 10203 77 -2503 -1183 C ATOM 2150 O THR B 416 173.490 252.696 813.521 1.00106.21 O ANISOU 2150 O THR B 416 13048 17368 9940 -2 -2604 -1198 O ATOM 2151 CB THR B 416 175.145 251.876 816.080 1.00108.31 C ANISOU 2151 CB THR B 416 13201 17647 10306 69 -2440 -818 C ATOM 2152 OG1 THR B 416 176.310 251.777 815.248 1.00108.14 O ANISOU 2152 OG1 THR B 416 12935 17568 10585 149 -2434 -889 O ATOM 2153 CG2 THR B 416 175.409 251.230 817.440 1.00109.91 C ANISOU 2153 CG2 THR B 416 13406 17870 10485 167 -2290 -573 C ATOM 2154 N ALA B 417 174.501 250.742 813.053 1.00109.92 N ANISOU 2154 N ALA B 417 13223 17606 10934 195 -2457 -1338 N ATOM 2155 CA ALA B 417 174.516 250.968 811.614 1.00109.62 C ANISOU 2155 CA ALA B 417 13047 17687 10915 269 -2556 -1557 C ATOM 2156 C ALA B 417 173.088 251.017 811.057 1.00109.25 C ANISOU 2156 C ALA B 417 13165 17671 10673 283 -2559 -1580 C ATOM 2157 O ALA B 417 172.710 251.969 810.386 1.00109.07 O ANISOU 2157 O ALA B 417 13178 17819 10446 301 -2631 -1562 O ATOM 2158 CB ALA B 417 175.333 249.900 810.916 1.00110.49 C ANISOU 2158 CB ALA B 417 12858 17707 11417 383 -2502 -1807 C ATOM 2159 N ALA B 418 172.295 249.989 811.337 1.00126.57 N ANISOU 2159 N ALA B 418 15448 19685 12956 298 -2444 -1585 N ATOM 2160 CA ALA B 418 170.880 250.029 811.009 1.00126.43 C ANISOU 2160 CA ALA B 418 15613 19656 12769 310 -2398 -1551 C ATOM 2161 C ALA B 418 170.242 251.336 811.475 1.00126.29 C ANISOU 2161 C ALA B 418 15817 19686 12481 175 -2410 -1398 C ATOM 2162 O ALA B 418 169.362 251.868 810.813 1.00126.50 O ANISOU 2162 O ALA B 418 15915 19756 12394 211 -2373 -1362 O ATOM 2163 CB ALA B 418 170.172 248.862 811.634 1.00126.66 C ANISOU 2163 CB ALA B 418 15755 19458 12914 309 -2252 -1522 C ATOM 2164 N PHE B 419 170.684 251.854 812.617 1.00116.56 N ANISOU 2164 N PHE B 419 14663 18454 11171 34 -2440 -1309 N ATOM 2165 CA PHE B 419 170.051 253.047 813.187 1.00117.00 C ANISOU 2165 CA PHE B 419 14890 18547 11017 -131 -2448 -1242 C ATOM 2166 C PHE B 419 170.639 254.387 812.738 1.00117.00 C ANISOU 2166 C PHE B 419 14790 18717 10946 -170 -2554 -1210 C ATOM 2167 O PHE B 419 169.948 255.405 812.810 1.00117.67 O ANISOU 2167 O PHE B 419 14972 18793 10943 -285 -2519 -1180 O ATOM 2168 CB PHE B 419 169.961 252.962 814.716 1.00117.78 C ANISOU 2168 CB PHE B 419 15117 18635 11000 -258 -2429 -1202 C ATOM 2169 CG PHE B 419 168.827 252.109 815.204 1.00118.28 C ANISOU 2169 CG PHE B 419 15363 18531 11046 -260 -2287 -1225 C ATOM 2170 CD1 PHE B 419 167.517 252.547 815.094 1.00118.90 C ANISOU 2170 CD1 PHE B 419 15614 18500 11062 -353 -2192 -1286 C ATOM 2171 CE1 PHE B 419 166.475 251.771 815.524 1.00119.49 C ANISOU 2171 CE1 PHE B 419 15858 18413 11129 -349 -2046 -1315 C ATOM 2172 CZ PHE B 419 166.723 250.540 816.069 1.00119.42 C ANISOU 2172 CZ PHE B 419 15850 18365 11160 -240 -1997 -1262 C ATOM 2173 CE2 PHE B 419 168.024 250.085 816.187 1.00118.97 C ANISOU 2173 CE2 PHE B 419 15608 18396 11199 -139 -2067 -1177 C ATOM 2174 CD2 PHE B 419 169.069 250.868 815.753 1.00118.42 C ANISOU 2174 CD2 PHE B 419 15369 18473 11152 -155 -2208 -1171 C ATOM 2175 N THR B 420 171.896 254.393 812.287 1.00105.67 N ANISOU 2175 N THR B 420 13150 17411 9590 -77 -2653 -1225 N ATOM 2176 CA THR B 420 172.433 255.586 811.638 1.00105.72 C ANISOU 2176 CA THR B 420 13046 17589 9532 -63 -2738 -1187 C ATOM 2177 C THR B 420 171.873 255.648 810.236 1.00105.87 C ANISOU 2177 C THR B 420 13010 17680 9537 116 -2693 -1207 C ATOM 2178 O THR B 420 171.553 256.716 809.745 1.00106.42 O ANISOU 2178 O THR B 420 13084 17828 9523 132 -2663 -1102 O ATOM 2179 CB THR B 420 173.981 255.647 811.597 1.00105.50 C ANISOU 2179 CB THR B 420 12809 17687 9590 -8 -2840 -1202 C ATOM 2180 OG1 THR B 420 174.521 254.381 811.200 1.00105.40 O ANISOU 2180 OG1 THR B 420 12649 17608 9790 127 -2811 -1342 O ATOM 2181 CG2 THR B 420 174.527 256.011 812.955 1.00105.87 C ANISOU 2181 CG2 THR B 420 12888 17757 9580 -152 -2873 -1088 C ATOM 2182 N ALA B 421 171.743 254.495 809.593 1.00117.35 N ANISOU 2182 N ALA B 421 14383 19127 11078 274 -2670 -1329 N ATOM 2183 CA ALA B 421 171.169 254.448 808.265 1.00117.99 C ANISOU 2183 CA ALA B 421 14375 19368 11089 499 -2631 -1343 C ATOM 2184 C ALA B 421 169.885 255.241 808.261 1.00118.65 C ANISOU 2184 C ALA B 421 14646 19359 11077 464 -2474 -1138 C ATOM 2185 O ALA B 421 169.657 256.053 807.365 1.00119.58 O ANISOU 2185 O ALA B 421 14693 19642 11100 621 -2417 -1004 O ATOM 2186 CB ALA B 421 170.904 253.026 807.851 1.00118.15 C ANISOU 2186 CB ALA B 421 14309 19363 11220 626 -2609 -1511 C ATOM 2187 N MET B 422 169.059 255.024 809.276 1.00180.76 N ANISOU 2187 N MET B 422 22732 26959 18988 274 -2374 -1112 N ATOM 2188 CA MET B 422 167.747 255.646 809.317 1.00181.84 C ANISOU 2188 CA MET B 422 23036 26933 19124 221 -2172 -972 C ATOM 2189 C MET B 422 167.797 257.159 809.367 1.00182.76 C ANISOU 2189 C MET B 422 23145 27057 19239 119 -2128 -852 C ATOM 2190 O MET B 422 167.125 257.825 808.591 1.00184.09 O ANISOU 2190 O MET B 422 23292 27218 19437 248 -1945 -674 O ATOM 2191 CB MET B 422 166.941 255.119 810.489 1.00181.91 C ANISOU 2191 CB MET B 422 23265 26673 19182 20 -2083 -1041 C ATOM 2192 CG MET B 422 166.723 253.625 810.416 1.00181.30 C ANISOU 2192 CG MET B 422 23197 26541 19146 135 -2071 -1114 C ATOM 2193 SD MET B 422 165.002 253.180 810.663 1.00182.32 S ANISOU 2193 SD MET B 422 23558 26387 19328 110 -1806 -1062 S ATOM 2194 CE MET B 422 164.251 253.839 809.176 1.00183.66 C ANISOU 2194 CE MET B 422 23637 26641 19505 360 -1621 -846 C ATOM 2195 N ILE B 423 168.589 257.701 810.282 1.00143.03 N ANISOU 2195 N ILE B 423 18108 22045 14193 -92 -2268 -924 N ATOM 2196 CA ILE B 423 168.667 259.150 810.435 1.00144.13 C ANISOU 2196 CA ILE B 423 18215 22183 14367 -224 -2233 -842 C ATOM 2197 C ILE B 423 168.991 259.759 809.104 1.00144.56 C ANISOU 2197 C ILE B 423 18104 22424 14399 34 -2190 -661 C ATOM 2198 O ILE B 423 168.340 260.701 808.653 1.00146.20 O ANISOU 2198 O ILE B 423 18300 22551 14700 72 -1984 -483 O ATOM 2199 CB ILE B 423 169.808 259.579 811.348 1.00143.64 C ANISOU 2199 CB ILE B 423 18085 22247 14244 -399 -2441 -922 C ATOM 2200 CG1 ILE B 423 170.011 258.565 812.467 1.00142.95 C ANISOU 2200 CG1 ILE B 423 18083 22138 14094 -500 -2540 -1058 C ATOM 2201 CD1 ILE B 423 171.394 258.628 813.097 1.00142.39 C ANISOU 2201 CD1 ILE B 423 17889 22259 13954 -532 -2728 -1060 C ATOM 2202 CG2 ILE B 423 169.553 260.984 811.880 1.00145.31 C ANISOU 2202 CG2 ILE B 423 18288 22395 14529 -625 -2386 -911 C ATOM 2203 N CYS B 424 170.031 259.221 808.487 1.00108.41 N ANISOU 2203 N CYS B 424 13373 18102 9715 224 -2363 -715 N ATOM 2204 CA CYS B 424 170.439 259.672 807.183 1.00109.08 C ANISOU 2204 CA CYS B 424 13273 18466 9708 521 -2354 -592 C ATOM 2205 C CYS B 424 169.201 259.855 806.339 1.00110.77 C ANISOU 2205 C CYS B 424 13510 18652 9925 734 -2092 -373 C ATOM 2206 O CYS B 424 168.880 260.972 805.966 1.00112.35 O ANISOU 2206 O CYS B 424 13675 18837 10176 798 -1911 -133 O ATOM 2207 CB CYS B 424 171.389 258.667 806.553 1.00108.26 C ANISOU 2207 CB CYS B 424 12995 18623 9517 719 -2539 -790 C ATOM 2208 SG CYS B 424 172.994 258.563 807.373 1.00106.93 S ANISOU 2208 SG CYS B 424 12742 18474 9413 539 -2764 -971 S ATOM 2209 N GLU B 425 168.477 258.770 806.083 1.00127.15 N ANISOU 2209 N GLU B 425 15633 20697 11980 848 -2034 -426 N ATOM 2210 CA GLU B 425 167.280 258.824 805.234 1.00129.04 C ANISOU 2210 CA GLU B 425 15874 20941 12214 1107 -1756 -175 C ATOM 2211 C GLU B 425 166.323 259.955 805.627 1.00130.76 C ANISOU 2211 C GLU B 425 16215 20814 12653 958 -1445 60 C ATOM 2212 O GLU B 425 165.682 260.561 804.774 1.00132.99 O ANISOU 2212 O GLU B 425 16423 21138 12970 1221 -1163 382 O ATOM 2213 CB GLU B 425 166.546 257.477 805.235 1.00128.67 C ANISOU 2213 CB GLU B 425 15899 20824 12164 1163 -1730 -282 C ATOM 2214 CG GLU B 425 165.659 257.227 804.023 1.00130.69 C ANISOU 2214 CG GLU B 425 16050 21290 12316 1568 -1519 -43 C ATOM 2215 CD GLU B 425 165.002 255.858 804.064 1.00130.31 C ANISOU 2215 CD GLU B 425 16054 21183 12275 1610 -1514 -166 C ATOM 2216 OE1 GLU B 425 164.521 255.460 805.152 1.00129.27 O ANISOU 2216 OE1 GLU B 425 16148 20655 12315 1307 -1470 -273 O ATOM 2217 OE2 GLU B 425 164.951 255.177 803.017 1.00131.34 O ANISOU 2217 OE2 GLU B 425 15981 21693 12227 1960 -1552 -167 O ATOM 2218 N ALA B 426 166.230 260.229 806.919 1.00115.77 N ANISOU 2218 N ALA B 426 14474 18592 10920 555 -1473 -109 N ATOM 2219 CA ALA B 426 165.436 261.345 807.398 1.00117.83 C ANISOU 2219 CA ALA B 426 14804 18512 11455 348 -1197 -5 C ATOM 2220 C ALA B 426 165.965 262.612 806.788 1.00119.13 C ANISOU 2220 C ALA B 426 14795 18805 11663 465 -1123 225 C ATOM 2221 O ALA B 426 165.351 263.177 805.896 1.00121.41 O ANISOU 2221 O ALA B 426 15001 19073 12057 728 -804 559 O ATOM 2222 CB ALA B 426 165.526 261.444 808.883 1.00117.28 C ANISOU 2222 CB ALA B 426 14860 18229 11472 -86 -1331 -313 C ATOM 2223 N LYS B 427 167.112 263.055 807.286 1.00116.91 N ANISOU 2223 N LYS B 427 14450 18662 11307 294 -1392 81 N ATOM 2224 CA LYS B 427 167.766 264.245 806.764 1.00117.96 C ANISOU 2224 CA LYS B 427 14412 18939 11468 396 -1355 286 C ATOM 2225 C LYS B 427 167.931 264.195 805.232 1.00118.78 C ANISOU 2225 C LYS B 427 14356 19402 11372 905 -1264 585 C ATOM 2226 O LYS B 427 167.839 265.223 804.557 1.00120.96 O ANISOU 2226 O LYS B 427 14505 19719 11736 1103 -1026 908 O ATOM 2227 CB LYS B 427 169.132 264.413 807.421 1.00116.13 C ANISOU 2227 CB LYS B 427 14125 18888 11111 206 -1705 82 C ATOM 2228 CG LYS B 427 169.865 265.689 807.039 1.00117.18 C ANISOU 2228 CG LYS B 427 14086 19149 11288 267 -1680 274 C ATOM 2229 CD LYS B 427 169.911 266.697 808.200 1.00118.15 C ANISOU 2229 CD LYS B 427 14203 19042 11647 -144 -1686 155 C ATOM 2230 CE LYS B 427 168.716 267.665 808.203 1.00121.38 C ANISOU 2230 CE LYS B 427 14595 19072 12452 -251 -1285 296 C ATOM 2231 NZ LYS B 427 168.943 268.832 809.128 1.00122.98 N ANISOU 2231 NZ LYS B 427 14694 19127 12906 -618 -1299 158 N ATOM 2232 N GLY B 428 168.154 263.000 804.686 1.00118.26 N ANISOU 2232 N GLY B 428 14268 19623 11042 1135 -1437 470 N ATOM 2233 CA GLY B 428 168.436 262.839 803.267 1.00119.33 C ANISOU 2233 CA GLY B 428 14204 20232 10906 1631 -1426 647 C ATOM 2234 C GLY B 428 169.934 262.828 803.002 1.00118.07 C ANISOU 2234 C GLY B 428 13886 20447 10528 1699 -1752 453 C ATOM 2235 O GLY B 428 170.488 261.845 802.503 1.00117.31 O ANISOU 2235 O GLY B 428 13681 20673 10218 1872 -1970 212 O ATOM 2236 N LEU B 454 155.849 243.220 793.892 1.00144.12 N ANISOU 2236 N LEU B 454 14924 27670 12165 6184 -868 507 N ATOM 2237 CA LEU B 454 156.573 242.240 794.686 1.00141.10 C ANISOU 2237 CA LEU B 454 14578 26871 12164 5661 -1174 -149 C ATOM 2238 C LEU B 454 158.075 242.512 794.673 1.00139.90 C ANISOU 2238 C LEU B 454 14265 26894 11997 5440 -1567 -727 C ATOM 2239 O LEU B 454 158.780 242.094 793.745 1.00142.72 O ANISOU 2239 O LEU B 454 14104 28022 12100 5681 -1892 -1194 O ATOM 2240 CB LEU B 454 156.291 240.831 794.164 1.00143.59 C ANISOU 2240 CB LEU B 454 14484 27606 12467 5840 -1322 -449 C ATOM 2241 N PHE B 455 158.554 243.211 795.706 1.00194.26 N ANISOU 2241 N PHE B 455 21571 33082 19156 4989 -1528 -717 N ATOM 2242 CA PHE B 455 159.975 243.563 795.836 1.00192.82 C ANISOU 2242 CA PHE B 455 21298 32952 19014 4748 -1845 -1196 C ATOM 2243 C PHE B 455 160.418 243.660 797.308 1.00188.32 C ANISOU 2243 C PHE B 455 21175 31473 18906 4143 -1824 -1305 C ATOM 2244 O PHE B 455 160.399 244.735 797.908 1.00186.38 O ANISOU 2244 O PHE B 455 21287 30840 18688 3975 -1672 -998 O ATOM 2245 CB PHE B 455 160.284 244.861 795.073 1.00194.50 C ANISOU 2245 CB PHE B 455 21418 33674 18809 5082 -1831 -939 C ATOM 2246 CG PHE B 455 159.060 245.667 794.723 1.00196.31 C ANISOU 2246 CG PHE B 455 21810 33957 18823 5457 -1412 -168 C ATOM 2247 CD1 PHE B 455 158.197 246.107 795.713 1.00194.01 C ANISOU 2247 CD1 PHE B 455 22021 32841 18854 5184 -1043 275 C ATOM 2248 CE1 PHE B 455 157.069 246.841 795.400 1.00196.16 C ANISOU 2248 CE1 PHE B 455 22415 33082 19033 5514 -596 967 C ATOM 2249 CZ PHE B 455 156.794 247.151 794.088 1.00200.61 C ANISOU 2249 CZ PHE B 455 22607 34477 19140 6170 -499 1308 C ATOM 2250 CE2 PHE B 455 157.640 246.722 793.085 1.00202.98 C ANISOU 2250 CE2 PHE B 455 22403 35696 19024 6486 -896 886 C ATOM 2251 CD2 PHE B 455 158.769 245.983 793.404 1.00200.84 C ANISOU 2251 CD2 PHE B 455 22004 35419 18886 6106 -1358 110 C ATOM 2252 N SER B 456 160.840 242.526 797.869 1.00131.07 N ANISOU 2252 N SER B 456 13860 23920 12021 3843 -1965 -1743 N ATOM 2253 CA SER B 456 161.084 242.392 799.318 1.00127.40 C ANISOU 2253 CA SER B 456 13799 22629 11980 3340 -1895 -1777 C ATOM 2254 C SER B 456 162.420 243.000 799.877 1.00125.31 C ANISOU 2254 C SER B 456 13600 22167 11845 3036 -2073 -2039 C ATOM 2255 O SER B 456 162.525 243.315 801.072 1.00122.53 O ANISOU 2255 O SER B 456 13631 21216 11709 2691 -1974 -1912 O ATOM 2256 CB SER B 456 160.879 240.925 799.715 1.00127.42 C ANISOU 2256 CB SER B 456 13710 22362 12343 3200 -1890 -2025 C ATOM 2257 OG SER B 456 160.941 240.096 798.565 1.00130.83 O ANISOU 2257 OG SER B 456 13607 23432 12669 3504 -2061 -2356 O ATOM 2258 N TYR B 457 163.432 243.100 799.003 1.00191.96 N ANISOU 2258 N TYR B 457 21637 31153 20146 3186 -2334 -2428 N ATOM 2259 CA TYR B 457 164.637 243.925 799.206 1.00190.74 C ANISOU 2259 CA TYR B 457 21497 30976 20000 3023 -2483 -2601 C ATOM 2260 C TYR B 457 164.950 244.734 797.968 1.00193.27 C ANISOU 2260 C TYR B 457 21526 32043 19864 3406 -2612 -2618 C ATOM 2261 O TYR B 457 164.318 244.571 796.920 1.00196.30 O ANISOU 2261 O TYR B 457 21646 33026 19914 3822 -2606 -2537 O ATOM 2262 CB TYR B 457 165.878 243.094 799.521 1.00190.55 C ANISOU 2262 CB TYR B 457 21228 30783 20388 2764 -2668 -3186 C ATOM 2263 CG TYR B 457 165.630 241.621 799.449 1.00191.99 C ANISOU 2263 CG TYR B 457 21158 30904 20886 2747 -2670 -3496 C ATOM 2264 CD1 TYR B 457 165.538 240.869 800.601 1.00190.07 C ANISOU 2264 CD1 TYR B 457 21140 29983 21097 2435 -2520 -3453 C ATOM 2265 CE1 TYR B 457 165.277 239.493 800.537 1.00191.62 C ANISOU 2265 CE1 TYR B 457 21089 30087 21629 2426 -2487 -3708 C ATOM 2266 CZ TYR B 457 165.098 238.898 799.300 1.00195.17 C ANISOU 2266 CZ TYR B 457 21048 31166 21940 2719 -2636 -4049 C ATOM 2267 OH TYR B 457 164.823 237.557 799.149 1.00197.14 O ANISOU 2267 OH TYR B 457 20999 31379 22528 2721 -2615 -4334 O ATOM 2268 CE2 TYR B 457 165.178 239.648 798.162 1.00197.23 C ANISOU 2268 CE2 TYR B 457 21078 32165 21695 3047 -2805 -4106 C ATOM 2269 CD2 TYR B 457 165.435 240.987 798.234 1.00195.63 C ANISOU 2269 CD2 TYR B 457 21138 32020 21175 3071 -2808 -3811 C ATOM 2270 N ARG B 458 165.981 245.565 798.107 1.00133.80 N ANISOU 2270 N ARG B 458 14019 24506 12313 3286 -2725 -2728 N ATOM 2271 CA ARG B 458 166.279 246.662 797.175 1.00135.60 C ANISOU 2271 CA ARG B 458 14096 25326 12100 3618 -2785 -2605 C ATOM 2272 C ARG B 458 165.039 247.540 797.020 1.00135.96 C ANISOU 2272 C ARG B 458 14402 25387 11870 3862 -2492 -1907 C ATOM 2273 O ARG B 458 164.781 248.090 795.942 1.00138.91 O ANISOU 2273 O ARG B 458 14560 26404 11818 4327 -2457 -1691 O ATOM 2274 CB ARG B 458 166.801 246.170 795.820 1.00139.67 C ANISOU 2274 CB ARG B 458 14026 26708 12332 3997 -3036 -3097 C ATOM 2275 N ASN B 459 164.268 247.623 798.115 1.00149.32 N ANISOU 2275 N ASN B 459 16535 26369 13829 3563 -2255 -1568 N ATOM 2276 CA ASN B 459 163.209 248.620 798.291 1.00149.29 C ANISOU 2276 CA ASN B 459 16846 26139 13738 3652 -1918 -942 C ATOM 2277 C ASN B 459 163.879 249.960 798.517 1.00148.29 C ANISOU 2277 C ASN B 459 16849 25926 13567 3545 -1917 -805 C ATOM 2278 O ASN B 459 163.613 250.938 797.820 1.00150.26 O ANISOU 2278 O ASN B 459 17040 26487 13563 3867 -1763 -434 O ATOM 2279 CB ASN B 459 162.335 248.297 799.516 1.00147.01 C ANISOU 2279 CB ASN B 459 16971 25096 13790 3297 -1695 -762 C ATOM 2280 CG ASN B 459 161.150 247.383 799.188 1.00148.62 C ANISOU 2280 CG ASN B 459 17131 25351 13987 3512 -1519 -602 C ATOM 2281 OD1 ASN B 459 160.985 246.328 799.800 1.00147.43 O ANISOU 2281 OD1 ASN B 459 17050 24885 14082 3297 -1551 -810 O ATOM 2282 ND2 ASN B 459 160.314 247.798 798.237 1.00151.57 N ANISOU 2282 ND2 ASN B 459 17383 26118 14089 3963 -1300 -187 N ATOM 2283 N GLY B 460 164.741 249.990 799.525 1.00129.46 N ANISOU 2283 N GLY B 460 14629 23113 11448 3108 -2064 -1072 N ATOM 2284 CA GLY B 460 165.598 251.127 799.780 1.00128.45 C ANISOU 2284 CA GLY B 460 14572 22932 11300 2975 -2126 -1038 C ATOM 2285 C GLY B 460 166.806 250.603 800.533 1.00126.31 C ANISOU 2285 C GLY B 460 14283 22430 11281 2621 -2374 -1494 C ATOM 2286 O GLY B 460 166.733 249.516 801.106 1.00125.35 O ANISOU 2286 O GLY B 460 14195 22027 11405 2429 -2406 -1712 O ATOM 2287 N MET B 461 167.908 251.352 800.536 1.00149.25 N ANISOU 2287 N MET B 461 17121 25436 14150 2554 -2512 -1605 N ATOM 2288 CA MET B 461 169.122 250.922 801.231 1.00147.64 C ANISOU 2288 CA MET B 461 16874 25005 14216 2252 -2696 -1988 C ATOM 2289 C MET B 461 169.011 250.980 802.748 1.00145.01 C ANISOU 2289 C MET B 461 16902 24038 14159 1842 -2603 -1851 C ATOM 2290 O MET B 461 169.516 250.094 803.435 1.00144.06 O ANISOU 2290 O MET B 461 16770 23651 14317 1636 -2659 -2092 O ATOM 2291 CB MET B 461 170.324 251.741 800.779 1.00148.14 C ANISOU 2291 CB MET B 461 16756 25373 14158 2325 -2845 -2123 C ATOM 2292 CG MET B 461 171.564 251.605 801.678 1.00146.42 C ANISOU 2292 CG MET B 461 16555 24825 14254 1994 -2956 -2380 C ATOM 2293 SD MET B 461 172.192 249.916 801.880 1.00146.82 S ANISOU 2293 SD MET B 461 16360 24706 14716 1864 -3044 -2915 S ATOM 2294 CE MET B 461 173.932 250.234 802.125 1.00146.68 C ANISOU 2294 CE MET B 461 16172 24633 14928 1718 -3155 -3207 C ATOM 2295 N ALA B 462 168.354 252.018 803.266 1.00115.79 N ANISOU 2295 N ALA B 462 13487 20116 10392 1742 -2442 -1474 N ATOM 2296 CA ALA B 462 168.125 252.135 804.707 1.00113.95 C ANISOU 2296 CA ALA B 462 13573 19372 10350 1380 -2360 -1373 C ATOM 2297 C ALA B 462 167.051 251.141 805.177 1.00113.77 C ANISOU 2297 C ALA B 462 13711 19073 10445 1322 -2220 -1343 C ATOM 2298 O ALA B 462 167.183 250.513 806.230 1.00112.59 O ANISOU 2298 O ALA B 462 13694 18609 10478 1091 -2224 -1435 O ATOM 2299 CB ALA B 462 167.756 253.560 805.081 1.00113.92 C ANISOU 2299 CB ALA B 462 13767 19238 10279 1275 -2234 -1073 C ATOM 2300 N SER B 463 165.993 250.987 804.389 1.00153.48 N ANISOU 2300 N SER B 463 18714 24240 15360 1566 -2075 -1181 N ATOM 2301 CA SER B 463 164.947 250.024 804.717 1.00153.54 C ANISOU 2301 CA SER B 463 18853 24010 15476 1547 -1927 -1140 C ATOM 2302 C SER B 463 165.440 248.572 804.687 1.00153.35 C ANISOU 2302 C SER B 463 18638 24016 15613 1552 -2064 -1466 C ATOM 2303 O SER B 463 164.661 247.647 804.857 1.00153.57 O ANISOU 2303 O SER B 463 18724 23884 15740 1567 -1955 -1452 O ATOM 2304 CB SER B 463 163.760 250.191 803.762 1.00155.58 C ANISOU 2304 CB SER B 463 19076 24455 15581 1863 -1715 -857 C ATOM 2305 OG SER B 463 162.659 249.379 804.145 1.00155.71 O ANISOU 2305 OG SER B 463 19253 24195 15713 1834 -1531 -774 O ATOM 2306 N TYR B 464 166.733 248.371 804.479 1.00111.36 N ANISOU 2306 N TYR B 464 13075 18869 10369 1535 -2273 -1765 N ATOM 2307 CA TYR B 464 167.273 247.025 804.313 1.00111.91 C ANISOU 2307 CA TYR B 464 12883 18958 10680 1549 -2368 -2121 C ATOM 2308 C TYR B 464 168.035 246.591 805.541 1.00110.50 C ANISOU 2308 C TYR B 464 12802 18367 10815 1264 -2363 -2213 C ATOM 2309 O TYR B 464 168.027 245.416 805.883 1.00110.74 O ANISOU 2309 O TYR B 464 12763 18184 11127 1215 -2306 -2349 O ATOM 2310 CB TYR B 464 168.198 246.965 803.100 1.00113.71 C ANISOU 2310 CB TYR B 464 12684 19685 10835 1764 -2568 -2468 C ATOM 2311 CG TYR B 464 169.030 245.701 802.959 1.00114.78 C ANISOU 2311 CG TYR B 464 12479 19803 11327 1723 -2666 -2946 C ATOM 2312 CD1 TYR B 464 168.642 244.689 802.096 1.00116.97 C ANISOU 2312 CD1 TYR B 464 12448 20356 11638 1920 -2706 -3209 C ATOM 2313 CE1 TYR B 464 169.404 243.542 801.941 1.00118.50 C ANISOU 2313 CE1 TYR B 464 12280 20508 12238 1861 -2772 -3704 C ATOM 2314 CZ TYR B 464 170.580 243.397 802.642 1.00117.88 C ANISOU 2314 CZ TYR B 464 12154 20077 12558 1626 -2760 -3894 C ATOM 2315 OH TYR B 464 171.335 242.251 802.473 1.00119.95 O ANISOU 2315 OH TYR B 464 12020 20230 13324 1564 -2764 -4394 O ATOM 2316 CE2 TYR B 464 171.000 244.395 803.498 1.00115.63 C ANISOU 2316 CE2 TYR B 464 12183 19549 12200 1463 -2720 -3585 C ATOM 2317 CD2 TYR B 464 170.227 245.540 803.650 1.00114.08 C ANISOU 2317 CD2 TYR B 464 12336 19433 11574 1503 -2695 -3140 C ATOM 2318 N MET B 465 168.724 247.530 806.186 1.00109.16 N ANISOU 2318 N MET B 465 12762 18107 10606 1105 -2403 -2115 N ATOM 2319 CA MET B 465 169.473 247.225 807.405 1.00108.21 C ANISOU 2319 CA MET B 465 12725 17655 10734 886 -2372 -2123 C ATOM 2320 C MET B 465 168.502 247.206 808.578 1.00107.34 C ANISOU 2320 C MET B 465 12976 17235 10572 741 -2215 -1854 C ATOM 2321 O MET B 465 168.783 246.652 809.627 1.00107.04 O ANISOU 2321 O MET B 465 13018 16946 10708 626 -2139 -1813 O ATOM 2322 CB MET B 465 170.584 248.254 807.627 1.00107.68 C ANISOU 2322 CB MET B 465 12628 17672 10615 802 -2478 -2111 C ATOM 2323 CG MET B 465 171.176 248.735 806.328 1.00108.68 C ANISOU 2323 CG MET B 465 12476 18197 10622 982 -2626 -2307 C ATOM 2324 SD MET B 465 172.927 249.113 806.493 1.00108.75 S ANISOU 2324 SD MET B 465 12277 18228 10816 906 -2728 -2486 S ATOM 2325 CE MET B 465 173.644 247.444 806.633 1.00110.04 C ANISOU 2325 CE MET B 465 12147 18137 11525 879 -2649 -2839 C ATOM 2326 N LEU B 466 167.352 247.834 808.381 1.00109.58 N ANISOU 2326 N LEU B 466 13460 17555 10621 772 -2141 -1669 N ATOM 2327 CA LEU B 466 166.291 247.754 809.354 1.00109.32 C ANISOU 2327 CA LEU B 466 13741 17245 10549 650 -1975 -1493 C ATOM 2328 C LEU B 466 165.804 246.317 809.424 1.00109.71 C ANISOU 2328 C LEU B 466 13760 17134 10789 719 -1869 -1548 C ATOM 2329 O LEU B 466 165.966 245.647 810.443 1.00109.50 O ANISOU 2329 O LEU B 466 13821 16880 10904 623 -1797 -1529 O ATOM 2330 CB LEU B 466 165.135 248.685 808.987 1.00109.85 C ANISOU 2330 CB LEU B 466 13978 17336 10423 683 -1858 -1309 C ATOM 2331 CG LEU B 466 165.156 250.065 809.642 1.00109.70 C ANISOU 2331 CG LEU B 466 14130 17266 10286 496 -1853 -1208 C ATOM 2332 CD1 LEU B 466 163.723 250.426 810.010 1.00110.61 C ANISOU 2332 CD1 LEU B 466 14499 17153 10377 423 -1621 -1076 C ATOM 2333 CD2 LEU B 466 166.070 250.099 810.862 1.00108.97 C ANISOU 2333 CD2 LEU B 466 14083 17102 10217 298 -1960 -1278 C ATOM 2334 N ASN B 467 165.216 245.843 808.332 1.00110.02 N ANISOU 2334 N ASN B 467 13653 17325 10823 916 -1847 -1593 N ATOM 2335 CA ASN B 467 164.645 244.504 808.297 1.00110.63 C ANISOU 2335 CA ASN B 467 13679 17269 11086 993 -1739 -1640 C ATOM 2336 C ASN B 467 165.681 243.413 808.552 1.00110.87 C ANISOU 2336 C ASN B 467 13470 17189 11468 960 -1781 -1862 C ATOM 2337 O ASN B 467 165.365 242.370 809.096 1.00111.17 O ANISOU 2337 O ASN B 467 13541 16976 11721 945 -1643 -1838 O ATOM 2338 CB ASN B 467 163.918 244.261 806.968 1.00111.98 C ANISOU 2338 CB ASN B 467 13667 17724 11156 1249 -1731 -1654 C ATOM 2339 CG ASN B 467 162.758 245.245 806.725 1.00112.32 C ANISOU 2339 CG ASN B 467 13938 17801 10937 1323 -1583 -1357 C ATOM 2340 OD1 ASN B 467 161.605 244.984 807.084 1.00112.60 O ANISOU 2340 OD1 ASN B 467 14192 17610 10983 1320 -1373 -1178 O ATOM 2341 ND2 ASN B 467 163.063 246.360 806.069 1.00112.65 N ANISOU 2341 ND2 ASN B 467 13905 18114 10785 1409 -1657 -1297 N ATOM 2342 N SER B 468 166.929 243.647 808.178 1.00115.67 N ANISOU 2342 N SER B 468 13822 17952 12174 954 -1934 -2068 N ATOM 2343 CA SER B 468 167.951 242.625 808.394 1.00116.46 C ANISOU 2343 CA SER B 468 13654 17885 12709 920 -1912 -2290 C ATOM 2344 C SER B 468 168.568 242.723 809.787 1.00115.73 C ANISOU 2344 C SER B 468 13736 17500 12736 768 -1807 -2098 C ATOM 2345 O SER B 468 169.357 241.866 810.187 1.00116.65 O ANISOU 2345 O SER B 468 13664 17394 13262 754 -1698 -2175 O ATOM 2346 CB SER B 468 169.035 242.671 807.311 1.00117.67 C ANISOU 2346 CB SER B 468 13395 18323 12992 997 -2087 -2666 C ATOM 2347 OG SER B 468 169.474 243.999 807.081 1.00116.88 O ANISOU 2347 OG SER B 468 13361 18464 12585 989 -2228 -2607 O ATOM 2348 N PHE B 469 168.208 243.781 810.518 1.00107.71 N ANISOU 2348 N PHE B 469 13046 16503 11377 675 -1819 -1849 N ATOM 2349 CA PHE B 469 168.563 243.909 811.926 1.00107.45 C ANISOU 2349 CA PHE B 469 13195 16294 11337 571 -1725 -1636 C ATOM 2350 C PHE B 469 167.495 243.268 812.783 1.00107.67 C ANISOU 2350 C PHE B 469 13474 16122 11315 573 -1541 -1454 C ATOM 2351 O PHE B 469 167.819 242.562 813.723 1.00108.38 O ANISOU 2351 O PHE B 469 13570 16033 11578 594 -1388 -1324 O ATOM 2352 CB PHE B 469 168.718 245.363 812.320 1.00106.62 C ANISOU 2352 CB PHE B 469 13266 16358 10885 463 -1846 -1525 C ATOM 2353 CG PHE B 469 168.973 245.572 813.783 1.00106.83 C ANISOU 2353 CG PHE B 469 13462 16319 10808 384 -1775 -1319 C ATOM 2354 CD1 PHE B 469 170.191 245.206 814.363 1.00107.52 C ANISOU 2354 CD1 PHE B 469 13377 16348 11126 421 -1716 -1247 C ATOM 2355 CE1 PHE B 469 170.421 245.404 815.713 1.00108.21 C ANISOU 2355 CE1 PHE B 469 13590 16468 11057 411 -1643 -1013 C ATOM 2356 CZ PHE B 469 169.443 245.994 816.499 1.00108.28 C ANISOU 2356 CZ PHE B 469 13887 16589 10666 332 -1665 -934 C ATOM 2357 CE2 PHE B 469 168.241 246.390 815.927 1.00107.59 C ANISOU 2357 CE2 PHE B 469 13972 16496 10410 250 -1714 -1058 C ATOM 2358 CD2 PHE B 469 168.014 246.184 814.574 1.00106.82 C ANISOU 2358 CD2 PHE B 469 13760 16348 10479 291 -1753 -1206 C ATOM 2359 N ALA B 470 166.229 243.510 812.450 1.00107.76 N ANISOU 2359 N ALA B 470 13679 16166 11101 578 -1525 -1424 N ATOM 2360 CA ALA B 470 165.092 242.790 813.046 1.00108.20 C ANISOU 2360 CA ALA B 470 13949 16026 11137 602 -1334 -1298 C ATOM 2361 C ALA B 470 165.257 241.263 813.072 1.00109.11 C ANISOU 2361 C ALA B 470 13883 15934 11640 710 -1184 -1316 C ATOM 2362 O ALA B 470 164.917 240.582 814.054 1.00109.75 O ANISOU 2362 O ALA B 470 14103 15825 11770 736 -997 -1151 O ATOM 2363 CB ALA B 470 163.824 243.141 812.312 1.00108.14 C ANISOU 2363 CB ALA B 470 14072 16066 10949 634 -1308 -1291 C ATOM 2364 N PHE B 471 165.754 240.738 811.968 1.00109.17 N ANISOU 2364 N PHE B 471 13553 16000 11926 784 -1256 -1536 N ATOM 2365 CA PHE B 471 165.914 239.312 811.807 1.00110.47 C ANISOU 2365 CA PHE B 471 13470 15964 12541 869 -1114 -1627 C ATOM 2366 C PHE B 471 167.079 238.766 812.628 1.00111.40 C ANISOU 2366 C PHE B 471 13434 15856 13035 857 -975 -1568 C ATOM 2367 O PHE B 471 167.306 237.549 812.686 1.00112.91 O ANISOU 2367 O PHE B 471 13405 15797 13700 921 -786 -1604 O ATOM 2368 CB PHE B 471 166.105 238.994 810.327 1.00111.29 C ANISOU 2368 CB PHE B 471 13202 16272 12814 948 -1258 -1966 C ATOM 2369 CG PHE B 471 164.859 239.162 809.519 1.00111.20 C ANISOU 2369 CG PHE B 471 13280 16462 12508 1047 -1303 -1946 C ATOM 2370 CD1 PHE B 471 164.680 238.463 808.339 1.00112.66 C ANISOU 2370 CD1 PHE B 471 13126 16843 12838 1184 -1367 -2198 C ATOM 2371 CE1 PHE B 471 163.522 238.621 807.603 1.00112.94 C ANISOU 2371 CE1 PHE B 471 13228 17101 12585 1327 -1374 -2109 C ATOM 2372 CZ PHE B 471 162.517 239.466 808.046 1.00111.80 C ANISOU 2372 CZ PHE B 471 13496 16901 12081 1308 -1279 -1781 C ATOM 2373 CE2 PHE B 471 162.677 240.161 809.226 1.00110.43 C ANISOU 2373 CE2 PHE B 471 13652 16507 11798 1132 -1224 -1604 C ATOM 2374 CD2 PHE B 471 163.842 240.006 809.962 1.00110.11 C ANISOU 2374 CD2 PHE B 471 13540 16325 11971 1015 -1253 -1678 C ATOM 2375 N GLU B 472 167.840 239.666 813.235 1.00120.11 N ANISOU 2375 N GLU B 472 14622 17045 13970 792 -1041 -1462 N ATOM 2376 CA GLU B 472 168.849 239.250 814.191 1.00121.28 C ANISOU 2376 CA GLU B 472 14668 17001 14413 827 -854 -1287 C ATOM 2377 C GLU B 472 168.178 238.954 815.509 1.00121.74 C ANISOU 2377 C GLU B 472 15019 16963 14273 892 -654 -934 C ATOM 2378 O GLU B 472 168.439 237.931 816.149 1.00123.41 O ANISOU 2378 O GLU B 472 15131 16929 14830 1013 -377 -746 O ATOM 2379 CB GLU B 472 169.880 240.340 814.405 1.00120.77 C ANISOU 2379 CB GLU B 472 14581 17111 14196 764 -991 -1263 C ATOM 2380 CG GLU B 472 171.017 240.270 813.445 1.00121.41 C ANISOU 2380 CG GLU B 472 14276 17185 14668 749 -1063 -1569 C ATOM 2381 CD GLU B 472 172.212 241.064 813.925 1.00121.49 C ANISOU 2381 CD GLU B 472 14232 17266 14663 723 -1088 -1460 C ATOM 2382 OE1 GLU B 472 172.368 241.200 815.164 1.00121.91 O ANISOU 2382 OE1 GLU B 472 14446 17291 14584 770 -949 -1101 O ATOM 2383 OE2 GLU B 472 172.991 241.536 813.058 1.00121.43 O ANISOU 2383 OE2 GLU B 472 14004 17377 14756 682 -1241 -1733 O ATOM 2384 N LEU B 473 167.301 239.859 815.910 1.00111.28 N ANISOU 2384 N LEU B 473 14037 15838 12405 825 -772 -858 N ATOM 2385 CA LEU B 473 166.663 239.760 817.204 1.00112.07 C ANISOU 2385 CA LEU B 473 14416 15946 12219 883 -622 -594 C ATOM 2386 C LEU B 473 165.751 238.539 817.286 1.00112.92 C ANISOU 2386 C LEU B 473 14575 15818 12509 992 -395 -516 C ATOM 2387 O LEU B 473 165.629 237.907 818.339 1.00114.43 O ANISOU 2387 O LEU B 473 14852 15933 12695 1130 -166 -257 O ATOM 2388 CB LEU B 473 165.893 241.041 817.503 1.00111.18 C ANISOU 2388 CB LEU B 473 14610 16084 11550 749 -800 -644 C ATOM 2389 CG LEU B 473 166.701 242.327 817.345 1.00110.36 C ANISOU 2389 CG LEU B 473 14451 16215 11266 629 -1030 -728 C ATOM 2390 CD1 LEU B 473 165.904 243.509 817.884 1.00110.27 C ANISOU 2390 CD1 LEU B 473 14718 16409 10769 492 -1144 -775 C ATOM 2391 CD2 LEU B 473 168.029 242.225 818.041 1.00111.40 C ANISOU 2391 CD2 LEU B 473 14400 16393 11533 718 -970 -550 C ATOM 2392 N CYS B 474 165.123 238.189 816.172 1.00128.90 N ANISOU 2392 N CYS B 474 16529 17762 14685 963 -447 -718 N ATOM 2393 CA CYS B 474 164.178 237.070 816.167 1.00129.69 C ANISOU 2393 CA CYS B 474 16673 17651 14952 1062 -242 -650 C ATOM 2394 C CYS B 474 164.857 235.704 816.200 1.00131.41 C ANISOU 2394 C CYS B 474 16573 17581 15776 1186 -3 -586 C ATOM 2395 O CYS B 474 164.198 234.665 816.084 1.00132.29 O ANISOU 2395 O CYS B 474 16648 17491 16125 1272 178 -545 O ATOM 2396 CB CYS B 474 163.252 237.175 814.963 1.00128.79 C ANISOU 2396 CB CYS B 474 16563 17595 14776 1023 -362 -852 C ATOM 2397 SG CYS B 474 162.332 238.707 814.951 1.00127.49 S ANISOU 2397 SG CYS B 474 16753 17660 14027 897 -524 -874 S ATOM 2398 N SER B 475 166.176 235.721 816.367 1.00116.55 N ANISOU 2398 N SER B 475 14445 15654 14183 1197 28 -572 N ATOM 2399 CA SER B 475 166.962 234.505 816.461 1.00118.76 C ANISOU 2399 CA SER B 475 14380 15602 15141 1307 316 -506 C ATOM 2400 C SER B 475 167.841 234.651 817.704 1.00120.12 C ANISOU 2400 C SER B 475 14575 15759 15307 1429 516 -138 C ATOM 2401 O SER B 475 168.751 233.865 817.955 1.00122.36 O ANISOU 2401 O SER B 475 14559 15760 16170 1543 808 1 O ATOM 2402 CB SER B 475 167.807 234.335 815.197 1.00119.09 C ANISOU 2402 CB SER B 475 13992 15588 15667 1213 192 -923 C ATOM 2403 OG SER B 475 167.909 232.976 814.809 1.00121.26 O ANISOU 2403 OG SER B 475 13920 15531 16624 1269 427 -1042 O ATOM 2404 N LEU B 476 167.534 235.679 818.484 1.00118.48 N ANISOU 2404 N LEU B 476 14700 15872 14447 1418 374 19 N ATOM 2405 CA LEU B 476 168.303 236.040 819.670 1.00119.88 C ANISOU 2405 CA LEU B 476 14908 16193 14449 1554 497 364 C ATOM 2406 C LEU B 476 167.627 235.575 820.946 1.00121.68 C ANISOU 2406 C LEU B 476 15361 16493 14377 1775 740 742 C ATOM 2407 O LEU B 476 168.276 235.075 821.846 1.00124.21 O ANISOU 2407 O LEU B 476 15563 16775 14855 2020 1043 1131 O ATOM 2408 CB LEU B 476 168.479 237.552 819.723 1.00118.21 C ANISOU 2408 CB LEU B 476 14860 16368 13686 1402 157 243 C ATOM 2409 CG LEU B 476 169.427 238.062 820.790 1.00119.73 C ANISOU 2409 CG LEU B 476 15018 16785 13689 1535 227 555 C ATOM 2410 CD1 LEU B 476 170.506 237.036 821.049 1.00122.28 C ANISOU 2410 CD1 LEU B 476 15004 16795 14660 1751 612 843 C ATOM 2411 CD2 LEU B 476 170.024 239.385 820.351 1.00118.05 C ANISOU 2411 CD2 LEU B 476 14789 16819 13247 1348 -98 345 C ATOM 2412 N GLY B 477 166.317 235.763 821.027 1.00152.70 N ANISOU 2412 N GLY B 477 19606 20547 17867 1713 630 638 N ATOM 2413 CA GLY B 477 165.545 235.196 822.113 1.00154.62 C ANISOU 2413 CA GLY B 477 20054 20850 17845 1927 868 927 C ATOM 2414 C GLY B 477 165.048 236.161 823.165 1.00155.21 C ANISOU 2414 C GLY B 477 20430 21391 17153 1946 728 960 C ATOM 2415 O GLY B 477 164.169 235.815 823.949 1.00156.73 O ANISOU 2415 O GLY B 477 20832 21691 17028 2088 867 1078 O ATOM 2416 N ASP B 478 165.597 237.367 823.201 1.00123.90 N ANISOU 2416 N ASP B 478 16467 17722 12888 1805 457 826 N ATOM 2417 CA ASP B 478 165.173 238.324 824.219 1.00125.02 C ANISOU 2417 CA ASP B 478 16834 18345 12322 1804 307 787 C ATOM 2418 C ASP B 478 163.694 238.701 824.104 1.00124.27 C ANISOU 2418 C ASP B 478 17048 18281 11886 1625 189 467 C ATOM 2419 O ASP B 478 163.307 239.469 823.226 1.00122.05 O ANISOU 2419 O ASP B 478 16838 17926 11609 1350 -36 144 O ATOM 2420 CB ASP B 478 166.030 239.580 824.185 1.00124.27 C ANISOU 2420 CB ASP B 478 16653 18539 12026 1659 31 674 C ATOM 2421 CG ASP B 478 165.889 240.405 825.442 1.00126.56 C ANISOU 2421 CG ASP B 478 17062 19390 11636 1732 -75 690 C ATOM 2422 OD1 ASP B 478 164.756 240.482 825.979 1.00127.69 O ANISOU 2422 OD1 ASP B 478 17437 19697 11383 1718 -83 529 O ATOM 2423 OD2 ASP B 478 166.914 240.971 825.890 1.00127.55 O ANISOU 2423 OD2 ASP B 478 17024 19809 11629 1809 -146 842 O ATOM 2424 N LYS B 479 162.880 238.168 825.012 1.00127.35 N ANISOU 2424 N LYS B 479 17610 18784 11994 1808 376 577 N ATOM 2425 CA LYS B 479 161.429 238.322 824.962 1.00127.22 C ANISOU 2425 CA LYS B 479 17876 18725 11738 1672 354 294 C ATOM 2426 C LYS B 479 160.990 239.783 824.942 1.00126.73 C ANISOU 2426 C LYS B 479 17954 18906 11292 1378 63 -115 C ATOM 2427 O LYS B 479 159.861 240.092 824.572 1.00126.22 O ANISOU 2427 O LYS B 479 18084 18696 11179 1196 45 -395 O ATOM 2428 CB LYS B 479 160.772 237.580 826.135 1.00130.41 C ANISOU 2428 CB LYS B 479 18420 19303 11828 1957 607 477 C ATOM 2429 N GLU B 480 161.883 240.680 825.341 1.00139.27 N ANISOU 2429 N GLU B 480 19422 20843 12651 1339 -133 -135 N ATOM 2430 CA GLU B 480 161.544 242.094 825.421 1.00139.36 C ANISOU 2430 CA GLU B 480 19519 21100 12331 1062 -393 -526 C ATOM 2431 C GLU B 480 161.945 242.871 824.174 1.00136.28 C ANISOU 2431 C GLU B 480 19040 20490 12249 800 -588 -670 C ATOM 2432 O GLU B 480 161.666 244.065 824.059 1.00136.20 O ANISOU 2432 O GLU B 480 19079 20596 12073 555 -772 -973 O ATOM 2433 CB GLU B 480 162.206 242.718 826.643 1.00142.18 C ANISOU 2433 CB GLU B 480 19779 22048 12195 1176 -511 -498 C ATOM 2434 CG GLU B 480 161.739 242.130 827.957 1.00146.00 C ANISOU 2434 CG GLU B 480 20339 22899 12237 1467 -344 -402 C ATOM 2435 CD GLU B 480 162.425 242.761 829.150 1.00149.33 C ANISOU 2435 CD GLU B 480 20614 24017 12109 1631 -475 -364 C ATOM 2436 OE1 GLU B 480 162.995 243.858 828.976 1.00148.64 O ANISOU 2436 OE1 GLU B 480 20413 24108 11956 1425 -732 -540 O ATOM 2437 OE2 GLU B 480 162.406 242.158 830.251 1.00152.87 O ANISOU 2437 OE2 GLU B 480 21040 24867 12178 1992 -315 -138 O ATOM 2438 N LEU B 481 162.580 242.190 823.228 1.00120.06 N ANISOU 2438 N LEU B 481 16831 18125 10659 861 -533 -474 N ATOM 2439 CA LEU B 481 163.056 242.853 822.019 1.00117.50 C ANISOU 2439 CA LEU B 481 16389 17661 10595 673 -715 -598 C ATOM 2440 C LEU B 481 162.188 242.566 820.785 1.00115.74 C ANISOU 2440 C LEU B 481 16228 17088 10659 583 -666 -718 C ATOM 2441 O LEU B 481 162.293 243.255 819.770 1.00114.10 O ANISOU 2441 O LEU B 481 15956 16826 10570 442 -808 -848 O ATOM 2442 CB LEU B 481 164.529 242.519 821.760 1.00116.84 C ANISOU 2442 CB LEU B 481 16025 17565 10803 790 -729 -378 C ATOM 2443 CG LEU B 481 165.479 242.951 822.879 1.00118.70 C ANISOU 2443 CG LEU B 481 16163 18181 10758 903 -772 -206 C ATOM 2444 CD1 LEU B 481 166.926 242.730 822.485 1.00118.10 C ANISOU 2444 CD1 LEU B 481 15799 18022 11049 993 -753 -7 C ATOM 2445 CD2 LEU B 481 165.244 244.394 823.233 1.00119.11 C ANISOU 2445 CD2 LEU B 481 16306 18567 10383 693 -1017 -465 C ATOM 2446 N TRP B 482 161.332 241.553 820.869 1.00120.30 N ANISOU 2446 N TRP B 482 16917 17463 11329 697 -452 -646 N ATOM 2447 CA TRP B 482 160.386 241.296 819.793 1.00119.15 C ANISOU 2447 CA TRP B 482 16831 17039 11400 644 -385 -734 C ATOM 2448 C TRP B 482 159.506 242.509 819.501 1.00119.11 C ANISOU 2448 C TRP B 482 16992 17052 11213 433 -457 -969 C ATOM 2449 O TRP B 482 159.286 242.842 818.344 1.00117.82 O ANISOU 2449 O TRP B 482 16771 16775 11223 376 -497 -1016 O ATOM 2450 CB TRP B 482 159.565 240.033 820.062 1.00120.14 C ANISOU 2450 CB TRP B 482 17057 16957 11633 808 -124 -603 C ATOM 2451 CG TRP B 482 160.390 238.817 819.850 1.00119.98 C ANISOU 2451 CG TRP B 482 16798 16797 11993 992 -21 -387 C ATOM 2452 CD1 TRP B 482 161.398 238.375 820.645 1.00121.12 C ANISOU 2452 CD1 TRP B 482 16804 17029 12186 1142 49 -179 C ATOM 2453 NE1 TRP B 482 161.954 237.235 820.119 1.00121.06 N ANISOU 2453 NE1 TRP B 482 16545 16768 12686 1269 190 -44 N ATOM 2454 CE2 TRP B 482 161.307 236.921 818.952 1.00119.85 C ANISOU 2454 CE2 TRP B 482 16350 16422 12766 1203 167 -199 C ATOM 2455 CZ2 TRP B 482 161.511 235.867 818.065 1.00119.78 C ANISOU 2455 CZ2 TRP B 482 16072 16173 13266 1272 255 -212 C ATOM 2456 CH2 TRP B 482 160.708 235.805 816.964 1.00118.88 C ANISOU 2456 CH2 TRP B 482 15945 16005 13219 1221 191 -376 C ATOM 2457 CZ3 TRP B 482 159.718 236.759 816.731 1.00118.08 C ANISOU 2457 CZ3 TRP B 482 16102 16019 12742 1114 94 -474 C ATOM 2458 CE3 TRP B 482 159.511 237.809 817.608 1.00118.20 C ANISOU 2458 CE3 TRP B 482 16383 16194 12334 1013 37 -485 C ATOM 2459 CD2 TRP B 482 160.318 237.904 818.748 1.00119.11 C ANISOU 2459 CD2 TRP B 482 16506 16433 12316 1052 47 -373 C ATOM 2460 N PRO B 483 159.022 243.191 820.550 1.00121.73 N ANISOU 2460 N PRO B 483 17496 17547 11208 333 -454 -1128 N ATOM 2461 CA PRO B 483 158.288 244.428 820.269 1.00122.16 C ANISOU 2461 CA PRO B 483 17653 17567 11195 104 -489 -1380 C ATOM 2462 C PRO B 483 159.137 245.438 819.501 1.00120.62 C ANISOU 2462 C PRO B 483 17287 17464 11080 -11 -702 -1405 C ATOM 2463 O PRO B 483 158.595 246.440 819.038 1.00120.90 O ANISOU 2463 O PRO B 483 17363 17418 11156 -173 -693 -1550 O ATOM 2464 CB PRO B 483 157.959 244.967 821.662 1.00124.98 C ANISOU 2464 CB PRO B 483 18131 18173 11180 15 -499 -1613 C ATOM 2465 CG PRO B 483 157.954 243.771 822.535 1.00126.17 C ANISOU 2465 CG PRO B 483 18334 18412 11192 249 -371 -1447 C ATOM 2466 CD PRO B 483 158.984 242.837 821.980 1.00124.11 C ANISOU 2466 CD PRO B 483 17886 18073 11196 441 -384 -1108 C ATOM 2467 N VAL B 484 160.443 245.194 819.390 1.00115.30 N ANISOU 2467 N VAL B 484 16414 16938 10456 80 -853 -1257 N ATOM 2468 CA VAL B 484 161.304 246.030 818.554 1.00113.79 C ANISOU 2468 CA VAL B 484 16046 16830 10358 5 -1044 -1267 C ATOM 2469 C VAL B 484 161.300 245.493 817.139 1.00112.14 C ANISOU 2469 C VAL B 484 15712 16449 10446 112 -1015 -1179 C ATOM 2470 O VAL B 484 161.099 246.243 816.185 1.00111.56 O ANISOU 2470 O VAL B 484 15595 16363 10429 61 -1056 -1219 O ATOM 2471 CB VAL B 484 162.758 246.076 819.064 1.00113.56 C ANISOU 2471 CB VAL B 484 15836 17043 10267 58 -1202 -1168 C ATOM 2472 CG1 VAL B 484 163.713 246.372 817.931 1.00111.72 C ANISOU 2472 CG1 VAL B 484 15385 16815 10250 65 -1343 -1136 C ATOM 2473 CG2 VAL B 484 162.908 247.101 820.170 1.00115.26 C ANISOU 2473 CG2 VAL B 484 16098 17553 10141 -71 -1315 -1293 C ATOM 2474 N ALA B 485 161.514 244.184 817.013 1.00114.21 N ANISOU 2474 N ALA B 485 15887 16608 10899 281 -931 -1060 N ATOM 2475 CA ALA B 485 161.489 243.523 815.710 1.00113.24 C ANISOU 2475 CA ALA B 485 15593 16382 11051 400 -914 -1036 C ATOM 2476 C ALA B 485 160.240 243.914 814.939 1.00113.45 C ANISOU 2476 C ALA B 485 15738 16316 11053 390 -812 -1056 C ATOM 2477 O ALA B 485 160.299 244.678 813.977 1.00113.01 O ANISOU 2477 O ALA B 485 15585 16356 10998 387 -892 -1076 O ATOM 2478 CB ALA B 485 161.568 242.015 815.873 1.00113.60 C ANISOU 2478 CB ALA B 485 15554 16274 11336 556 -773 -940 C ATOM 2479 N ILE B 486 159.107 243.407 815.390 1.00113.48 N ANISOU 2479 N ILE B 486 15944 16137 11037 411 -600 -1019 N ATOM 2480 CA ILE B 486 157.837 243.742 814.777 1.00114.18 C ANISOU 2480 CA ILE B 486 16155 16087 11142 419 -427 -997 C ATOM 2481 C ILE B 486 157.533 245.252 814.687 1.00114.80 C ANISOU 2481 C ILE B 486 16312 16186 11119 258 -430 -1075 C ATOM 2482 O ILE B 486 156.859 245.708 813.761 1.00115.27 O ANISOU 2482 O ILE B 486 16355 16181 11263 316 -306 -992 O ATOM 2483 CB ILE B 486 156.694 242.987 815.474 1.00115.47 C ANISOU 2483 CB ILE B 486 16543 16026 11303 449 -173 -967 C ATOM 2484 CG1 ILE B 486 156.530 241.592 814.861 1.00115.13 C ANISOU 2484 CG1 ILE B 486 16376 15897 11471 658 -85 -831 C ATOM 2485 CD1 ILE B 486 156.970 240.452 815.767 1.00115.32 C ANISOU 2485 CD1 ILE B 486 16394 15872 11549 726 -48 -782 C ATOM 2486 CG2 ILE B 486 155.367 243.784 815.449 1.00117.03 C ANISOU 2486 CG2 ILE B 486 16947 16039 11479 356 51 -1013 C ATOM 2487 N GLY B 487 158.034 246.029 815.637 1.00135.08 N ANISOU 2487 N GLY B 487 18938 18859 13526 77 -549 -1215 N ATOM 2488 CA GLY B 487 157.861 247.471 815.589 1.00135.92 C ANISOU 2488 CA GLY B 487 19071 18978 13596 -98 -557 -1320 C ATOM 2489 C GLY B 487 158.549 248.043 814.364 1.00134.71 C ANISOU 2489 C GLY B 487 18704 18962 13518 -18 -685 -1208 C ATOM 2490 O GLY B 487 157.957 248.793 813.591 1.00135.50 O ANISOU 2490 O GLY B 487 18791 18981 13714 1 -547 -1132 O ATOM 2491 N LEU B 488 159.816 247.678 814.186 1.00110.28 N ANISOU 2491 N LEU B 488 15425 16080 10396 54 -920 -1187 N ATOM 2492 CA LEU B 488 160.587 248.094 813.022 1.00109.31 C ANISOU 2492 CA LEU B 488 15072 16144 10316 159 -1063 -1125 C ATOM 2493 C LEU B 488 159.891 247.644 811.742 1.00109.60 C ANISOU 2493 C LEU B 488 15020 16172 10452 387 -932 -992 C ATOM 2494 O LEU B 488 159.629 248.445 810.858 1.00110.22 O ANISOU 2494 O LEU B 488 15027 16326 10525 471 -873 -887 O ATOM 2495 CB LEU B 488 162.004 247.516 813.073 1.00108.01 C ANISOU 2495 CB LEU B 488 14708 16156 10175 211 -1286 -1168 C ATOM 2496 CG LEU B 488 163.001 248.104 814.072 1.00107.81 C ANISOU 2496 CG LEU B 488 14679 16248 10038 58 -1443 -1229 C ATOM 2497 CD1 LEU B 488 164.314 247.322 814.060 1.00106.98 C ANISOU 2497 CD1 LEU B 488 14359 16235 10053 152 -1568 -1227 C ATOM 2498 CD2 LEU B 488 163.245 249.568 813.772 1.00107.94 C ANISOU 2498 CD2 LEU B 488 14660 16383 9968 -52 -1532 -1250 C ATOM 2499 N ILE B 489 159.591 246.355 811.648 1.00110.37 N ANISOU 2499 N ILE B 489 15097 16203 10636 516 -869 -972 N ATOM 2500 CA ILE B 489 158.954 245.792 810.465 1.00110.97 C ANISOU 2500 CA ILE B 489 15045 16339 10779 761 -762 -854 C ATOM 2501 C ILE B 489 157.641 246.490 810.057 1.00112.57 C ANISOU 2501 C ILE B 489 15383 16407 10981 820 -479 -669 C ATOM 2502 O ILE B 489 157.224 246.393 808.909 1.00113.47 O ANISOU 2502 O ILE B 489 15345 16673 11095 1073 -392 -505 O ATOM 2503 CB ILE B 489 158.718 244.291 810.639 1.00110.92 C ANISOU 2503 CB ILE B 489 15015 16229 10902 852 -706 -872 C ATOM 2504 CG1 ILE B 489 159.990 243.515 810.360 1.00110.12 C ANISOU 2504 CG1 ILE B 489 14623 16299 10918 908 -929 -1024 C ATOM 2505 CD1 ILE B 489 159.709 242.063 810.094 1.00110.64 C ANISOU 2505 CD1 ILE B 489 14556 16300 11182 1050 -854 -1043 C ATOM 2506 CG2 ILE B 489 157.675 243.804 809.680 1.00112.09 C ANISOU 2506 CG2 ILE B 489 15102 16395 11092 1082 -527 -724 C ATOM 2507 N ALA B 490 156.992 247.196 810.978 1.00117.40 N ANISOU 2507 N ALA B 490 16246 16752 11608 606 -313 -702 N ATOM 2508 CA ALA B 490 155.803 247.944 810.611 1.00119.41 C ANISOU 2508 CA ALA B 490 16600 16807 11965 641 13 -541 C ATOM 2509 C ALA B 490 155.837 249.346 811.184 1.00120.34 C ANISOU 2509 C ALA B 490 16805 16801 12117 390 56 -645 C ATOM 2510 O ALA B 490 156.567 250.196 810.691 1.00120.02 O ANISOU 2510 O ALA B 490 16614 16951 12036 403 -75 -604 O ATOM 2511 CB ALA B 490 154.573 247.211 811.057 1.00120.59 C ANISOU 2511 CB ALA B 490 16948 16652 12219 649 299 -509 C ATOM 2512 N THR B 496 155.686 247.206 801.442 1.00123.68 N ANISOU 2512 N THR B 496 15217 20186 11591 3272 31 815 N ATOM 2513 CA THR B 496 154.363 246.674 801.077 1.00125.95 C ANISOU 2513 CA THR B 496 15511 20423 11921 3545 379 1156 C ATOM 2514 C THR B 496 153.620 245.914 802.202 1.00124.58 C ANISOU 2514 C THR B 496 15660 19635 12038 3230 533 1066 C ATOM 2515 O THR B 496 154.136 244.939 802.765 1.00122.54 O ANISOU 2515 O THR B 496 15414 19303 11844 3009 268 701 O ATOM 2516 CB THR B 496 154.388 245.824 799.747 1.00128.36 C ANISOU 2516 CB THR B 496 15369 21481 11922 4044 237 1186 C ATOM 2517 OG1 THR B 496 153.475 244.717 799.851 1.00129.03 O ANISOU 2517 OG1 THR B 496 15480 21424 12120 4113 389 1253 O ATOM 2518 CG2 THR B 496 155.803 245.318 799.392 1.00127.29 C ANISOU 2518 CG2 THR B 496 14914 21837 11614 4007 -283 661 C ATOM 2519 N ARG B 497 152.396 246.362 802.488 1.00162.04 N ANISOU 2519 N ARG B 497 20642 23944 16980 3241 999 1412 N ATOM 2520 CA ARG B 497 151.606 245.884 803.622 1.00161.21 C ANISOU 2520 CA ARG B 497 20878 23226 17149 2937 1204 1330 C ATOM 2521 C ARG B 497 151.233 244.413 803.565 1.00161.09 C ANISOU 2521 C ARG B 497 20796 23280 17131 3046 1156 1267 C ATOM 2522 O ARG B 497 151.119 243.765 804.604 1.00159.47 O ANISOU 2522 O ARG B 497 20822 22689 17081 2750 1131 1041 O ATOM 2523 CB ARG B 497 150.339 246.720 803.781 1.00163.76 C ANISOU 2523 CB ARG B 497 21409 23084 17727 2964 1765 1697 C ATOM 2524 N SER B 498 151.018 243.882 802.370 1.00128.39 N ANISOU 2524 N SER B 498 16320 19655 12806 3491 1156 1473 N ATOM 2525 CA SER B 498 150.713 242.464 802.260 1.00128.54 C ANISOU 2525 CA SER B 498 16219 19778 12842 3597 1090 1387 C ATOM 2526 C SER B 498 151.964 241.587 802.481 1.00126.25 C ANISOU 2526 C SER B 498 15750 19689 12529 3400 599 871 C ATOM 2527 O SER B 498 151.860 240.413 802.856 1.00125.64 O ANISOU 2527 O SER B 498 15663 19479 12596 3318 544 703 O ATOM 2528 CB SER B 498 150.072 242.169 800.908 1.00132.03 C ANISOU 2528 CB SER B 498 16312 20775 13080 4157 1243 1756 C ATOM 2529 OG SER B 498 149.719 240.802 800.802 1.00132.48 O ANISOU 2529 OG SER B 498 16229 20929 13177 4256 1193 1671 O ATOM 2530 N ALA B 499 153.142 242.166 802.247 1.00128.09 N ANISOU 2530 N ALA B 499 15830 20214 12626 3332 283 636 N ATOM 2531 CA ALA B 499 154.398 241.435 802.398 1.00126.43 C ANISOU 2531 CA ALA B 499 15413 20167 12457 3156 -133 148 C ATOM 2532 C ALA B 499 154.780 241.315 803.873 1.00123.58 C ANISOU 2532 C ALA B 499 15396 19216 12341 2695 -165 -60 C ATOM 2533 O ALA B 499 155.038 240.215 804.371 1.00122.76 O ANISOU 2533 O ALA B 499 15259 18952 12431 2564 -255 -283 O ATOM 2534 CB ALA B 499 155.504 242.119 801.620 1.00126.74 C ANISOU 2534 CB ALA B 499 15163 20722 12270 3266 -425 -26 C ATOM 2535 N LYS B 500 154.836 242.456 804.560 1.00126.26 N ANISOU 2535 N LYS B 500 16033 19267 12673 2473 -82 18 N ATOM 2536 CA LYS B 500 155.018 242.460 806.002 1.00124.24 C ANISOU 2536 CA LYS B 500 16110 18519 12577 2086 -72 -130 C ATOM 2537 C LYS B 500 154.143 241.357 806.613 1.00124.45 C ANISOU 2537 C LYS B 500 16299 18216 12772 2058 130 -82 C ATOM 2538 O LYS B 500 154.643 240.456 807.280 1.00123.34 O ANISOU 2538 O LYS B 500 16157 17940 12766 1917 13 -283 O ATOM 2539 CB LYS B 500 154.671 243.833 806.578 1.00124.21 C ANISOU 2539 CB LYS B 500 16399 18243 12551 1906 104 1 C ATOM 2540 N LYS B 501 152.840 241.402 806.357 1.00118.64 N ANISOU 2540 N LYS B 501 15681 17346 12051 2222 468 215 N ATOM 2541 CA LYS B 501 151.938 240.374 806.873 1.00119.08 C ANISOU 2541 CA LYS B 501 15889 17097 12259 2225 689 286 C ATOM 2542 C LYS B 501 152.487 238.951 806.752 1.00118.62 C ANISOU 2542 C LYS B 501 15579 17183 12307 2279 486 93 C ATOM 2543 O LYS B 501 152.375 238.174 807.678 1.00117.93 O ANISOU 2543 O LYS B 501 15654 16779 12374 2133 550 20 O ATOM 2544 CB LYS B 501 150.576 240.449 806.192 1.00121.56 C ANISOU 2544 CB LYS B 501 16222 17385 12580 2508 1065 661 C ATOM 2545 N MET B 502 153.074 238.598 805.616 1.00137.36 N ANISOU 2545 N MET B 502 17530 20044 14618 2500 258 -8 N ATOM 2546 CA MET B 502 153.541 237.221 805.442 1.00137.61 C ANISOU 2546 CA MET B 502 17261 20187 14836 2541 99 -243 C ATOM 2547 C MET B 502 154.841 236.987 806.208 1.00135.79 C ANISOU 2547 C MET B 502 17002 19809 14781 2263 -132 -572 C ATOM 2548 O MET B 502 155.183 235.854 806.541 1.00135.83 O ANISOU 2548 O MET B 502 16872 19674 15064 2207 -159 -734 O ATOM 2549 CB MET B 502 153.667 236.846 803.944 1.00139.89 C ANISOU 2549 CB MET B 502 17044 21102 15006 2883 -64 -314 C ATOM 2550 CG MET B 502 154.078 235.364 803.638 1.00140.97 C ANISOU 2550 CG MET B 502 16780 21381 15402 2930 -217 -626 C ATOM 2551 SD MET B 502 152.936 233.987 804.078 1.00141.89 S ANISOU 2551 SD MET B 502 16981 21142 15788 2985 77 -442 S ATOM 2552 CE MET B 502 153.702 232.599 803.249 1.00144.08 C ANISOU 2552 CE MET B 502 16597 21805 16342 3085 -189 -903 C ATOM 2553 N VAL B 503 155.549 238.071 806.506 1.00116.37 N ANISOU 2553 N VAL B 503 14661 17362 12191 2104 -260 -635 N ATOM 2554 CA VAL B 503 156.797 237.989 807.268 1.00114.85 C ANISOU 2554 CA VAL B 503 14452 17037 12149 1865 -443 -885 C ATOM 2555 C VAL B 503 156.515 237.898 808.774 1.00113.75 C ANISOU 2555 C VAL B 503 14713 16427 12081 1648 -263 -778 C ATOM 2556 O VAL B 503 157.058 237.036 809.472 1.00113.48 O ANISOU 2556 O VAL B 503 14637 16198 12282 1564 -261 -871 O ATOM 2557 CB VAL B 503 157.763 239.165 806.919 1.00114.12 C ANISOU 2557 CB VAL B 503 14276 17209 11876 1808 -671 -1003 C ATOM 2558 CG1 VAL B 503 158.467 239.680 808.151 1.00112.39 C ANISOU 2558 CG1 VAL B 503 14304 16715 11686 1529 -708 -1045 C ATOM 2559 CG2 VAL B 503 158.763 238.731 805.858 1.00115.12 C ANISOU 2559 CG2 VAL B 503 13910 17753 12079 1936 -935 -1321 C ATOM 2560 N ILE B 504 155.646 238.782 809.260 1.00116.64 N ANISOU 2560 N ILE B 504 15436 16627 12257 1581 -86 -588 N ATOM 2561 CA ILE B 504 155.188 238.746 810.646 1.00116.32 C ANISOU 2561 CA ILE B 504 15764 16220 12212 1409 94 -527 C ATOM 2562 C ILE B 504 154.627 237.367 810.938 1.00117.05 C ANISOU 2562 C ILE B 504 15860 16112 12501 1505 273 -454 C ATOM 2563 O ILE B 504 154.883 236.790 811.986 1.00116.84 O ANISOU 2563 O ILE B 504 15949 15884 12561 1422 330 -469 O ATOM 2564 CB ILE B 504 154.089 239.813 810.907 1.00117.01 C ANISOU 2564 CB ILE B 504 16171 16154 12134 1346 312 -393 C ATOM 2565 CG1 ILE B 504 154.720 241.192 811.115 1.00116.34 C ANISOU 2565 CG1 ILE B 504 16144 16165 11896 1172 163 -488 C ATOM 2566 CD1 ILE B 504 153.737 242.353 811.126 1.00117.57 C ANISOU 2566 CD1 ILE B 504 16513 16172 11987 1112 389 -390 C ATOM 2567 CG2 ILE B 504 153.234 239.444 812.112 1.00117.66 C ANISOU 2567 CG2 ILE B 504 16585 15894 12225 1250 559 -359 C ATOM 2568 N ALA B 505 153.892 236.832 809.970 1.00117.80 N ANISOU 2568 N ALA B 505 15798 16302 12661 1714 369 -351 N ATOM 2569 CA ALA B 505 153.172 235.579 810.138 1.00118.76 C ANISOU 2569 CA ALA B 505 15921 16232 12971 1826 573 -247 C ATOM 2570 C ALA B 505 154.074 234.363 810.351 1.00118.73 C ANISOU 2570 C ALA B 505 15652 16185 13275 1820 478 -395 C ATOM 2571 O ALA B 505 153.604 233.345 810.836 1.00119.44 O ANISOU 2571 O ALA B 505 15794 16037 13549 1871 674 -296 O ATOM 2572 CB ALA B 505 152.238 235.347 808.980 1.00120.30 C ANISOU 2572 CB ALA B 505 15956 16604 13148 2077 686 -89 C ATOM 2573 N GLU B 506 155.352 234.444 809.990 1.00116.74 N ANISOU 2573 N GLU B 506 15101 16130 13124 1765 218 -626 N ATOM 2574 CA GLU B 506 156.247 233.304 810.212 1.00117.24 C ANISOU 2574 CA GLU B 506 14878 16078 13590 1748 191 -778 C ATOM 2575 C GLU B 506 157.253 233.598 811.308 1.00116.27 C ANISOU 2575 C GLU B 506 14876 15792 13508 1583 161 -799 C ATOM 2576 O GLU B 506 158.013 232.723 811.723 1.00116.93 O ANISOU 2576 O GLU B 506 14768 15699 13960 1573 222 -849 O ATOM 2577 CB GLU B 506 156.995 232.920 808.945 1.00118.32 C ANISOU 2577 CB GLU B 506 14486 16540 13930 1830 -37 -1084 C ATOM 2578 CG GLU B 506 156.249 233.212 807.659 1.00119.34 C ANISOU 2578 CG GLU B 506 14460 17067 13816 2029 -115 -1077 C ATOM 2579 CD GLU B 506 156.848 232.474 806.471 1.00121.36 C ANISOU 2579 CD GLU B 506 14126 17689 14294 2152 -316 -1432 C ATOM 2580 OE1 GLU B 506 157.302 231.319 806.666 1.00122.46 O ANISOU 2580 OE1 GLU B 506 14001 17633 14896 2106 -271 -1619 O ATOM 2581 OE2 GLU B 506 156.858 233.049 805.355 1.00122.24 O ANISOU 2581 OE2 GLU B 506 14017 18296 14132 2309 -503 -1534 O ATOM 2582 N LEU B 507 157.258 234.845 811.760 1.00113.87 N ANISOU 2582 N LEU B 507 14863 15553 12849 1470 92 -747 N ATOM 2583 CA LEU B 507 158.071 235.256 812.889 1.00113.21 C ANISOU 2583 CA LEU B 507 14926 15381 12706 1339 70 -725 C ATOM 2584 C LEU B 507 157.346 234.996 814.219 1.00113.71 C ANISOU 2584 C LEU B 507 15351 15213 12640 1340 316 -514 C ATOM 2585 O LEU B 507 157.857 234.272 815.073 1.00114.40 O ANISOU 2585 O LEU B 507 15410 15155 12902 1380 439 -416 O ATOM 2586 CB LEU B 507 158.432 236.732 812.760 1.00112.06 C ANISOU 2586 CB LEU B 507 14883 15454 12241 1217 -133 -801 C ATOM 2587 CG LEU B 507 159.673 237.052 811.939 1.00111.62 C ANISOU 2587 CG LEU B 507 14483 15628 12301 1196 -386 -1014 C ATOM 2588 CD1 LEU B 507 160.137 238.454 812.251 1.00110.55 C ANISOU 2588 CD1 LEU B 507 14502 15635 11867 1059 -537 -1027 C ATOM 2589 CD2 LEU B 507 160.781 236.055 812.208 1.00112.31 C ANISOU 2589 CD2 LEU B 507 14283 15580 12810 1206 -363 -1103 C ATOM 2590 N LEU B 508 156.157 235.575 814.384 1.00126.00 N ANISOU 2590 N LEU B 508 17224 16743 13907 1318 419 -444 N ATOM 2591 CA LEU B 508 155.363 235.397 815.601 1.00126.93 C ANISOU 2591 CA LEU B 508 17681 16690 13856 1322 649 -317 C ATOM 2592 C LEU B 508 155.362 233.974 816.193 1.00128.06 C ANISOU 2592 C LEU B 508 17771 16635 14253 1472 866 -156 C ATOM 2593 O LEU B 508 155.349 233.810 817.416 1.00129.00 O ANISOU 2593 O LEU B 508 18081 16710 14224 1504 1000 -48 O ATOM 2594 CB LEU B 508 153.933 235.902 815.395 1.00127.47 C ANISOU 2594 CB LEU B 508 18012 16678 13744 1308 802 -295 C ATOM 2595 CG LEU B 508 153.715 237.329 815.908 1.00127.52 C ANISOU 2595 CG LEU B 508 18262 16757 13433 1125 748 -421 C ATOM 2596 CD1 LEU B 508 152.235 237.741 815.786 1.00128.76 C ANISOU 2596 CD1 LEU B 508 18663 16737 13521 1111 994 -405 C ATOM 2597 CD2 LEU B 508 154.199 237.462 817.358 1.00128.16 C ANISOU 2597 CD2 LEU B 508 18494 16903 13297 1056 728 -473 C ATOM 2598 N PRO B 509 155.351 232.940 815.333 1.00121.08 N ANISOU 2598 N PRO B 509 16601 15660 13742 1584 914 -137 N ATOM 2599 CA PRO B 509 155.477 231.553 815.800 1.00122.41 C ANISOU 2599 CA PRO B 509 16646 15604 14259 1724 1139 18 C ATOM 2600 C PRO B 509 156.601 231.308 816.810 1.00123.01 C ANISOU 2600 C PRO B 509 16656 15637 14446 1748 1190 116 C ATOM 2601 O PRO B 509 156.463 230.457 817.680 1.00124.50 O ANISOU 2601 O PRO B 509 16907 15655 14744 1891 1456 344 O ATOM 2602 CB PRO B 509 155.769 230.785 814.506 1.00122.70 C ANISOU 2602 CB PRO B 509 16244 15649 14728 1776 1061 -119 C ATOM 2603 CG PRO B 509 155.023 231.540 813.463 1.00121.99 C ANISOU 2603 CG PRO B 509 16192 15771 14389 1759 919 -217 C ATOM 2604 CD PRO B 509 154.955 232.997 813.912 1.00120.81 C ANISOU 2604 CD PRO B 509 16365 15745 13791 1621 811 -237 C ATOM 2605 N HIS B 510 157.701 232.036 816.692 1.00124.72 N ANISOU 2605 N HIS B 510 16735 16014 14640 1641 970 -14 N ATOM 2606 CA HIS B 510 158.885 231.717 817.478 1.00125.65 C ANISOU 2606 CA HIS B 510 16705 16078 14959 1699 1053 114 C ATOM 2607 C HIS B 510 159.017 232.602 818.717 1.00125.80 C ANISOU 2607 C HIS B 510 17023 16297 14480 1691 1033 233 C ATOM 2608 O HIS B 510 160.021 232.547 819.427 1.00126.73 O ANISOU 2608 O HIS B 510 17032 16453 14666 1766 1092 383 O ATOM 2609 CB HIS B 510 160.148 231.810 816.607 1.00125.19 C ANISOU 2609 CB HIS B 510 16243 16053 15271 1613 866 -105 C ATOM 2610 CG HIS B 510 160.222 230.776 815.521 1.00126.02 C ANISOU 2610 CG HIS B 510 15954 16002 15928 1643 900 -279 C ATOM 2611 ND1 HIS B 510 159.396 230.784 814.414 1.00125.49 N ANISOU 2611 ND1 HIS B 510 15834 16051 15794 1625 768 -463 N ATOM 2612 CE1 HIS B 510 159.694 229.762 813.632 1.00126.93 C ANISOU 2612 CE1 HIS B 510 15590 16126 16511 1666 808 -639 C ATOM 2613 NE2 HIS B 510 160.687 229.091 814.189 1.00128.40 N ANISOU 2613 NE2 HIS B 510 15551 16058 17176 1689 992 -581 N ATOM 2614 CD2 HIS B 510 161.041 229.704 815.364 1.00127.85 C ANISOU 2614 CD2 HIS B 510 15778 15986 16813 1698 1064 -317 C ATOM 2615 N TYR B 511 158.001 233.414 818.974 1.00122.23 N ANISOU 2615 N TYR B 511 16914 15982 13546 1610 971 158 N ATOM 2616 CA TYR B 511 158.013 234.298 820.129 1.00122.90 C ANISOU 2616 CA TYR B 511 17252 16313 13131 1584 926 175 C ATOM 2617 C TYR B 511 158.050 233.480 821.388 1.00125.27 C ANISOU 2617 C TYR B 511 17617 16616 13365 1824 1200 465 C ATOM 2618 O TYR B 511 157.238 232.570 821.568 1.00126.37 O ANISOU 2618 O TYR B 511 17845 16572 13598 1963 1445 600 O ATOM 2619 CB TYR B 511 156.778 235.186 820.156 1.00122.70 C ANISOU 2619 CB TYR B 511 17547 16363 12709 1445 874 -17 C ATOM 2620 CG TYR B 511 156.734 236.113 821.342 1.00123.97 C ANISOU 2620 CG TYR B 511 17925 16814 12365 1393 812 -103 C ATOM 2621 CD1 TYR B 511 157.843 236.861 821.701 1.00123.78 C ANISOU 2621 CD1 TYR B 511 17786 17052 12193 1338 614 -129 C ATOM 2622 CE1 TYR B 511 157.812 237.723 822.778 1.00125.36 C ANISOU 2622 CE1 TYR B 511 18136 17587 11909 1297 532 -242 C ATOM 2623 CZ TYR B 511 156.660 237.855 823.523 1.00127.35 C ANISOU 2623 CZ TYR B 511 18651 17912 11826 1296 649 -387 C ATOM 2624 OH TYR B 511 156.642 238.720 824.605 1.00129.53 O ANISOU 2624 OH TYR B 511 19023 18585 11607 1252 546 -583 O ATOM 2625 CE2 TYR B 511 155.534 237.119 823.184 1.00127.51 C ANISOU 2625 CE2 TYR B 511 18811 17629 12008 1345 872 -365 C ATOM 2626 CD2 TYR B 511 155.578 236.253 822.094 1.00125.73 C ANISOU 2626 CD2 TYR B 511 18438 17073 12260 1399 952 -195 C ATOM 2627 N PRO B 512 159.008 233.794 822.265 1.00137.37 N ANISOU 2627 N PRO B 512 19089 18379 14726 1908 1179 599 N ATOM 2628 CA PRO B 512 159.165 233.109 823.555 1.00140.24 C ANISOU 2628 CA PRO B 512 19483 18848 14953 2209 1455 942 C ATOM 2629 C PRO B 512 158.212 233.643 824.622 1.00141.99 C ANISOU 2629 C PRO B 512 20041 19398 14511 2253 1461 857 C ATOM 2630 O PRO B 512 158.679 234.175 825.629 1.00143.79 O ANISOU 2630 O PRO B 512 20291 20027 14314 2358 1410 919 O ATOM 2631 CB PRO B 512 160.619 233.423 823.942 1.00140.84 C ANISOU 2631 CB PRO B 512 19326 19103 15083 2283 1405 1107 C ATOM 2632 CG PRO B 512 161.268 233.897 822.664 1.00138.13 C ANISOU 2632 CG PRO B 512 18776 18610 15097 2026 1153 851 C ATOM 2633 CD PRO B 512 160.185 234.608 821.932 1.00136.15 C ANISOU 2633 CD PRO B 512 18744 18369 14618 1779 935 502 C ATOM 2634 N PHE B 513 156.906 233.501 824.406 1.00145.82 N ANISOU 2634 N PHE B 513 20756 19737 14914 2186 1531 698 N ATOM 2635 CA PHE B 513 155.900 234.034 825.322 1.00147.81 C ANISOU 2635 CA PHE B 513 21312 20258 14590 2186 1546 506 C ATOM 2636 C PHE B 513 155.844 233.286 826.654 1.00151.36 C ANISOU 2636 C PHE B 513 21817 20952 14743 2554 1813 799 C ATOM 2637 O PHE B 513 156.043 232.059 826.702 1.00152.17 O ANISOU 2637 O PHE B 513 21799 20829 15191 2814 2099 1183 O ATOM 2638 CB PHE B 513 154.528 233.990 824.661 1.00147.00 C ANISOU 2638 CB PHE B 513 21415 19861 14577 2037 1618 292 C ATOM 2639 CG PHE B 513 153.999 232.605 824.491 1.00147.54 C ANISOU 2639 CG PHE B 513 21477 19606 14978 2247 1930 567 C ATOM 2640 CD2 PHE B 513 154.454 231.800 823.464 1.00145.81 C ANISOU 2640 CD2 PHE B 513 21001 19057 15344 2263 1972 739 C ATOM 2641 CE2 PHE B 513 153.973 230.522 823.313 1.00146.60 C ANISOU 2641 CE2 PHE B 513 21057 18861 15782 2448 2261 976 C ATOM 2642 CZ PHE B 513 153.029 230.029 824.192 1.00148.95 C ANISOU 2642 CZ PHE B 513 21597 19179 15818 2640 2526 1086 C ATOM 2643 CE1 PHE B 513 152.570 230.823 825.220 1.00150.76 C ANISOU 2643 CE1 PHE B 513 22093 19755 15433 2638 2486 902 C ATOM 2644 CD1 PHE B 513 153.060 232.101 825.369 1.00150.15 C ANISOU 2644 CD1 PHE B 513 22029 19985 15037 2436 2183 625 C ATOM 2645 N VAL B 514 155.555 234.038 827.724 1.00137.56 N ANISOU 2645 N VAL B 514 20223 19686 12357 2587 1728 598 N ATOM 2646 CA VAL B 514 155.420 233.488 829.082 1.00141.66 C ANISOU 2646 CA VAL B 514 20799 20594 12432 2977 1953 826 C ATOM 2647 C VAL B 514 154.241 234.075 829.861 1.00144.37 C ANISOU 2647 C VAL B 514 21410 21268 12176 2924 1919 392 C ATOM 2648 O VAL B 514 153.292 233.374 830.188 1.00146.14 O ANISOU 2648 O VAL B 514 21802 21401 12323 3084 2171 423 O ATOM 2649 CB VAL B 514 156.683 233.734 829.909 1.00143.60 C ANISOU 2649 CB VAL B 514 20831 21326 12406 3215 1896 1094 C ATOM 2650 CG1 VAL B 514 156.381 233.541 831.379 1.00148.51 C ANISOU 2650 CG1 VAL B 514 21528 22548 12354 3605 2050 1203 C ATOM 2651 CG2 VAL B 514 157.808 232.816 829.463 1.00142.56 C ANISOU 2651 CG2 VAL B 514 20412 20857 12895 3398 2093 1615 C ATOM 2652 N THR B 515 154.329 235.367 830.157 1.00142.30 N ANISOU 2652 N THR B 515 21162 21384 11520 2696 1619 -36 N ATOM 2653 CA THR B 515 153.311 236.076 830.912 1.00145.46 C ANISOU 2653 CA THR B 515 21752 22128 11387 2596 1561 -568 C ATOM 2654 C THR B 515 151.996 236.113 830.165 1.00144.18 C ANISOU 2654 C THR B 515 21817 21443 11523 2319 1671 -889 C ATOM 2655 O THR B 515 151.967 236.032 828.941 1.00140.43 O ANISOU 2655 O THR B 515 21328 20434 11597 2116 1667 -799 O ATOM 2656 CB THR B 515 153.735 237.535 831.135 1.00145.98 C ANISOU 2656 CB THR B 515 21729 22599 11139 2323 1202 -1010 C ATOM 2657 OG1 THR B 515 155.116 237.588 831.501 1.00146.13 O ANISOU 2657 OG1 THR B 515 21501 22995 11025 2530 1082 -650 O ATOM 2658 CG2 THR B 515 152.898 238.174 832.227 1.00150.75 C ANISOU 2658 CG2 THR B 515 22434 23727 11116 2304 1150 -1571 C ATOM 2659 N ASN B 516 150.899 236.258 830.899 1.00185.21 N ANISOU 2659 N ASN B 516 27201 26823 16349 2329 1780 -1277 N ATOM 2660 CA ASN B 516 149.629 236.499 830.249 1.00184.61 C ANISOU 2660 CA ASN B 516 27327 26257 16558 2041 1904 -1633 C ATOM 2661 C ASN B 516 149.711 237.823 829.529 1.00182.73 C ANISOU 2661 C ASN B 516 27037 25869 16523 1604 1659 -2018 C ATOM 2662 O ASN B 516 149.010 238.054 828.545 1.00180.81 O ANISOU 2662 O ASN B 516 26883 25099 16716 1361 1753 -2124 O ATOM 2663 CB ASN B 516 148.482 236.560 831.242 1.00189.40 C ANISOU 2663 CB ASN B 516 28117 27111 16734 2100 2067 -2082 C ATOM 2664 CG ASN B 516 147.190 237.019 830.590 1.00189.29 C ANISOU 2664 CG ASN B 516 28287 26568 17065 1763 2219 -2504 C ATOM 2665 OD1 ASN B 516 146.627 238.036 830.970 1.00192.10 O ANISOU 2665 OD1 ASN B 516 28678 27061 17252 1502 2155 -3134 O ATOM 2666 ND2 ASN B 516 146.737 236.286 829.582 1.00186.34 N ANISOU 2666 ND2 ASN B 516 28000 25584 17217 1770 2441 -2158 N ATOM 2667 N ASP B 517 150.564 238.701 830.042 1.00150.97 N ANISOU 2667 N ASP B 517 22853 22334 12174 1535 1367 -2197 N ATOM 2668 CA ASP B 517 150.796 239.989 829.407 1.00149.34 C ANISOU 2668 CA ASP B 517 22561 22022 12158 1143 1128 -2519 C ATOM 2669 C ASP B 517 151.504 239.801 828.059 1.00144.25 C ANISOU 2669 C ASP B 517 21815 20940 12053 1074 1067 -2095 C ATOM 2670 O ASP B 517 151.136 240.417 827.057 1.00142.25 O ANISOU 2670 O ASP B 517 21583 20289 12176 798 1057 -2233 O ATOM 2671 CB ASP B 517 151.604 240.898 830.335 1.00151.81 C ANISOU 2671 CB ASP B 517 22695 23014 11970 1122 827 -2781 C ATOM 2672 CG ASP B 517 151.035 240.942 831.745 1.00157.49 C ANISOU 2672 CG ASP B 517 23454 24324 12061 1276 862 -3190 C ATOM 2673 OD1 ASP B 517 151.750 241.398 832.667 1.00160.22 O ANISOU 2673 OD1 ASP B 517 23621 25368 11887 1397 639 -3303 O ATOM 2674 OD2 ASP B 517 149.874 240.512 831.930 1.00159.52 O ANISOU 2674 OD2 ASP B 517 23902 24382 12326 1298 1117 -3400 O ATOM 2675 N ASP B 518 152.518 238.945 828.037 1.00140.80 N ANISOU 2675 N ASP B 518 21243 20587 11666 1348 1052 -1585 N ATOM 2676 CA ASP B 518 153.202 238.623 826.796 1.00136.59 C ANISOU 2676 CA ASP B 518 20577 19674 11647 1311 1007 -1238 C ATOM 2677 C ASP B 518 152.201 238.191 825.747 1.00134.88 C ANISOU 2677 C ASP B 518 20482 18905 11863 1223 1207 -1211 C ATOM 2678 O ASP B 518 152.256 238.640 824.604 1.00132.28 O ANISOU 2678 O ASP B 518 20087 18300 11872 1033 1122 -1226 O ATOM 2679 CB ASP B 518 154.201 237.496 827.017 1.00136.13 C ANISOU 2679 CB ASP B 518 20357 19691 11674 1649 1087 -718 C ATOM 2680 CG ASP B 518 155.348 237.907 827.900 1.00137.65 C ANISOU 2680 CG ASP B 518 20381 20416 11504 1780 916 -629 C ATOM 2681 OD1 ASP B 518 155.856 237.031 828.632 1.00139.45 O ANISOU 2681 OD1 ASP B 518 20525 20847 11613 2141 1078 -244 O ATOM 2682 OD2 ASP B 518 155.734 239.102 827.862 1.00137.32 O ANISOU 2682 OD2 ASP B 518 20274 20590 11310 1544 646 -912 O ATOM 2683 N ILE B 519 151.289 237.311 826.139 1.00134.32 N ANISOU 2683 N ILE B 519 20573 18708 11756 1398 1486 -1145 N ATOM 2684 CA ILE B 519 150.291 236.811 825.219 1.00133.15 C ANISOU 2684 CA ILE B 519 20531 18064 11996 1363 1711 -1075 C ATOM 2685 C ILE B 519 149.269 237.896 824.913 1.00134.05 C ANISOU 2685 C ILE B 519 20789 17996 12149 1067 1752 -1500 C ATOM 2686 O ILE B 519 148.753 237.977 823.803 1.00132.39 O ANISOU 2686 O ILE B 519 20582 17403 12315 969 1848 -1434 O ATOM 2687 CB ILE B 519 149.608 235.557 825.776 1.00135.02 C ANISOU 2687 CB ILE B 519 20899 18214 12190 1647 2023 -867 C ATOM 2688 CG1 ILE B 519 150.570 234.367 825.734 1.00133.87 C ANISOU 2688 CG1 ILE B 519 20560 18069 12234 1933 2066 -367 C ATOM 2689 CD1 ILE B 519 149.886 233.018 825.792 1.00134.78 C ANISOU 2689 CD1 ILE B 519 20751 17927 12533 2190 2403 -73 C ATOM 2690 CG2 ILE B 519 148.340 235.246 825.002 1.00134.70 C ANISOU 2690 CG2 ILE B 519 21006 17706 12470 1589 2278 -883 C ATOM 2691 N GLU B 520 148.990 238.743 825.895 1.00175.29 N ANISOU 2691 N GLU B 520 26092 23510 17001 940 1696 -1940 N ATOM 2692 CA GLU B 520 148.095 239.876 825.688 1.00176.83 C ANISOU 2692 CA GLU B 520 26375 23508 17307 627 1763 -2401 C ATOM 2693 C GLU B 520 148.641 240.758 824.566 1.00173.93 C ANISOU 2693 C GLU B 520 25855 22977 17254 415 1586 -2345 C ATOM 2694 O GLU B 520 147.881 241.345 823.788 1.00173.95 O ANISOU 2694 O GLU B 520 25899 22605 17589 241 1747 -2452 O ATOM 2695 CB GLU B 520 147.931 240.675 826.989 1.00181.07 C ANISOU 2695 CB GLU B 520 26937 24478 17385 513 1672 -2956 C ATOM 2696 CG GLU B 520 146.938 241.841 826.929 1.00183.76 C ANISOU 2696 CG GLU B 520 27335 24578 17905 165 1797 -3531 C ATOM 2697 CD GLU B 520 146.917 242.679 828.211 1.00188.36 C ANISOU 2697 CD GLU B 520 27862 25669 18036 28 1648 -4171 C ATOM 2698 OE1 GLU B 520 147.802 242.480 829.072 1.00189.10 O ANISOU 2698 OE1 GLU B 520 27854 26366 17629 216 1401 -4114 O ATOM 2699 OE2 GLU B 520 146.018 243.538 828.356 1.00191.65 O ANISOU 2699 OE2 GLU B 520 28308 25896 18616 -256 1796 -4738 O ATOM 2700 N TRP B 521 149.968 240.833 824.486 1.00139.18 N ANISOU 2700 N TRP B 521 21267 18860 12756 462 1289 -2147 N ATOM 2701 CA TRP B 521 150.649 241.578 823.430 1.00136.37 C ANISOU 2701 CA TRP B 521 20746 18414 12654 311 1098 -2059 C ATOM 2702 C TRP B 521 150.592 240.851 822.086 1.00133.42 C ANISOU 2702 C TRP B 521 20310 17699 12683 433 1197 -1667 C ATOM 2703 O TRP B 521 150.122 241.401 821.083 1.00132.69 O ANISOU 2703 O TRP B 521 20201 17346 12871 326 1278 -1663 O ATOM 2704 CB TRP B 521 152.115 241.838 823.814 1.00135.28 C ANISOU 2704 CB TRP B 521 20418 18696 12285 342 769 -1978 C ATOM 2705 CG TRP B 521 152.945 242.445 822.700 1.00132.24 C ANISOU 2705 CG TRP B 521 19850 18243 12154 234 571 -1846 C ATOM 2706 CD1 TRP B 521 152.895 243.735 822.235 1.00132.21 C ANISOU 2706 CD1 TRP B 521 19798 18189 12247 -16 482 -2069 C ATOM 2707 NE1 TRP B 521 153.799 243.909 821.216 1.00129.27 N ANISOU 2707 NE1 TRP B 521 19244 17805 12067 -2 312 -1840 N ATOM 2708 CE2 TRP B 521 154.453 242.726 821.003 1.00127.49 C ANISOU 2708 CE2 TRP B 521 18930 17605 11907 231 285 -1518 C ATOM 2709 CZ2 TRP B 521 155.442 242.412 820.083 1.00124.87 C ANISOU 2709 CZ2 TRP B 521 18385 17281 11780 319 139 -1283 C ATOM 2710 CH2 TRP B 521 155.929 241.138 820.094 1.00124.14 C ANISOU 2710 CH2 TRP B 521 18199 17165 11804 535 183 -1036 C ATOM 2711 CZ3 TRP B 521 155.447 240.181 820.990 1.00125.80 C ANISOU 2711 CZ3 TRP B 521 18537 17350 11912 690 379 -952 C ATOM 2712 CE3 TRP B 521 154.448 240.488 821.905 1.00128.30 C ANISOU 2712 CE3 TRP B 521 19087 17705 11958 632 511 -1162 C ATOM 2713 CD2 TRP B 521 153.940 241.784 821.920 1.00129.27 C ANISOU 2713 CD2 TRP B 521 19292 17846 11977 384 459 -1485 C ATOM 2714 N MET B 522 151.086 239.617 822.069 1.00129.67 N ANISOU 2714 N MET B 522 19768 17255 12246 677 1204 -1335 N ATOM 2715 CA MET B 522 151.109 238.833 820.849 1.00127.37 C ANISOU 2715 CA MET B 522 19357 16716 12321 804 1266 -1022 C ATOM 2716 C MET B 522 149.758 238.873 820.153 1.00128.09 C ANISOU 2716 C MET B 522 19576 16462 12629 781 1542 -1028 C ATOM 2717 O MET B 522 149.695 238.965 818.931 1.00126.62 O ANISOU 2717 O MET B 522 19263 16147 12698 801 1543 -878 O ATOM 2718 CB MET B 522 151.502 237.398 821.146 1.00127.12 C ANISOU 2718 CB MET B 522 19256 16691 12352 1061 1343 -730 C ATOM 2719 CG MET B 522 151.999 236.650 819.933 1.00124.85 C ANISOU 2719 CG MET B 522 18722 16266 12448 1166 1298 -481 C ATOM 2720 SD MET B 522 152.650 235.061 820.419 1.00125.17 S ANISOU 2720 SD MET B 522 18620 16286 12653 1434 1409 -178 S ATOM 2721 CE MET B 522 151.206 234.338 821.161 1.00127.59 C ANISOU 2721 CE MET B 522 19219 16415 12845 1571 1770 -124 C ATOM 2722 N LEU B 523 148.680 238.816 820.926 1.00127.23 N ANISOU 2722 N LEU B 523 19700 16231 12411 765 1794 -1199 N ATOM 2723 CA LEU B 523 147.354 238.924 820.349 1.00128.45 C ANISOU 2723 CA LEU B 523 19980 16018 12806 743 2116 -1205 C ATOM 2724 C LEU B 523 147.139 240.322 819.801 1.00128.89 C ANISOU 2724 C LEU B 523 20005 15973 12994 518 2116 -1393 C ATOM 2725 O LEU B 523 146.690 240.488 818.666 1.00128.34 O ANISOU 2725 O LEU B 523 19868 15685 13210 565 2263 -1190 O ATOM 2726 CB LEU B 523 146.292 238.595 821.384 1.00131.62 C ANISOU 2726 CB LEU B 523 20630 16309 13069 763 2400 -1407 C ATOM 2727 CG LEU B 523 146.358 237.163 821.917 1.00131.64 C ANISOU 2727 CG LEU B 523 20673 16376 12966 1030 2478 -1163 C ATOM 2728 CD1 LEU B 523 145.182 236.856 822.834 1.00135.05 C ANISOU 2728 CD1 LEU B 523 21359 16692 13262 1075 2795 -1361 C ATOM 2729 CD2 LEU B 523 146.397 236.180 820.764 1.00129.34 C ANISOU 2729 CD2 LEU B 523 20238 15892 13014 1219 2541 -738 C ATOM 2730 N SER B 524 147.479 241.325 820.610 1.00157.68 N ANISOU 2730 N SER B 524 23671 19809 16433 298 1963 -1762 N ATOM 2731 CA SER B 524 147.407 242.726 820.192 1.00158.38 C ANISOU 2731 CA SER B 524 23694 19806 16677 63 1955 -1962 C ATOM 2732 C SER B 524 147.938 242.896 818.780 1.00155.60 C ANISOU 2732 C SER B 524 23147 19429 16546 151 1857 -1608 C ATOM 2733 O SER B 524 147.553 243.820 818.065 1.00156.34 O ANISOU 2733 O SER B 524 23189 19332 16881 64 1999 -1599 O ATOM 2734 CB SER B 524 148.200 243.627 821.144 1.00159.28 C ANISOU 2734 CB SER B 524 23753 20270 16498 -145 1663 -2334 C ATOM 2735 OG SER B 524 148.165 244.979 820.712 1.00160.06 O ANISOU 2735 OG SER B 524 23760 20255 16799 -377 1668 -2516 O ATOM 2736 N ILE B 525 148.833 242.001 818.387 1.00142.49 N ANISOU 2736 N ILE B 525 21351 17972 14816 340 1635 -1328 N ATOM 2737 CA ILE B 525 149.324 241.997 817.024 1.00140.27 C ANISOU 2737 CA ILE B 525 20853 17738 14707 465 1530 -1038 C ATOM 2738 C ILE B 525 148.270 241.412 816.077 1.00140.87 C ANISOU 2738 C ILE B 525 20934 17561 15030 666 1847 -760 C ATOM 2739 O ILE B 525 147.754 242.112 815.197 1.00141.68 O ANISOU 2739 O ILE B 525 20981 17535 15316 692 2021 -638 O ATOM 2740 CB ILE B 525 150.673 241.261 816.928 1.00137.73 C ANISOU 2740 CB ILE B 525 20336 17710 14284 576 1199 -915 C ATOM 2741 CG1 ILE B 525 151.702 241.997 817.790 1.00137.46 C ANISOU 2741 CG1 ILE B 525 20277 17937 14014 401 921 -1137 C ATOM 2742 CD1 ILE B 525 153.111 241.520 817.616 1.00135.27 C ANISOU 2742 CD1 ILE B 525 19779 17909 13709 489 631 -1016 C ATOM 2743 CG2 ILE B 525 151.140 241.167 815.478 1.00135.97 C ANISOU 2743 CG2 ILE B 525 19853 17585 14225 722 1085 -691 C ATOM 2744 N CYS B 526 147.929 240.146 816.284 1.00177.15 N ANISOU 2744 N CYS B 526 25583 22090 19635 831 1951 -629 N ATOM 2745 CA CYS B 526 146.977 239.442 815.426 1.00177.79 C ANISOU 2745 CA CYS B 526 25643 21979 19930 1052 2236 -342 C ATOM 2746 C CYS B 526 145.751 240.266 815.068 1.00180.26 C ANISOU 2746 C CYS B 526 26070 21982 20438 1022 2623 -310 C ATOM 2747 O CYS B 526 145.199 240.134 813.981 1.00180.75 O ANISOU 2747 O CYS B 526 26019 21981 20678 1230 2819 0 O ATOM 2748 CB CYS B 526 146.550 238.138 816.092 1.00178.28 C ANISOU 2748 CB CYS B 526 25827 21933 19977 1171 2375 -285 C ATOM 2749 SG CYS B 526 147.940 237.157 816.668 1.00176.25 S ANISOU 2749 SG CYS B 526 25427 21953 19586 1224 2036 -286 S ATOM 2750 N VAL B 527 145.321 241.118 815.987 1.00130.75 N ANISOU 2750 N VAL B 527 19994 15532 14154 777 2755 -636 N ATOM 2751 CA VAL B 527 144.196 241.984 815.703 1.00133.66 C ANISOU 2751 CA VAL B 527 20442 15534 14809 714 3174 -648 C ATOM 2752 C VAL B 527 144.498 242.893 814.499 1.00133.25 C ANISOU 2752 C VAL B 527 20172 15550 14908 781 3163 -408 C ATOM 2753 O VAL B 527 143.868 242.768 813.449 1.00134.12 O ANISOU 2753 O VAL B 527 20185 15557 15216 1028 3437 -26 O ATOM 2754 CB VAL B 527 143.768 242.797 816.955 1.00136.47 C ANISOU 2754 CB VAL B 527 20989 15705 15158 396 3295 -1162 C ATOM 2755 CG1 VAL B 527 144.814 243.844 817.310 1.00135.69 C ANISOU 2755 CG1 VAL B 527 20786 15867 14901 158 2940 -1444 C ATOM 2756 CG2 VAL B 527 142.398 243.446 816.751 1.00140.28 C ANISOU 2756 CG2 VAL B 527 21560 15685 16056 339 3847 -1200 C ATOM 2757 N GLU B 528 145.486 243.772 814.639 1.00171.80 N ANISOU 2757 N GLU B 528 24958 20652 19667 600 2848 -597 N ATOM 2758 CA GLU B 528 145.802 244.749 813.604 1.00171.75 C ANISOU 2758 CA GLU B 528 24751 20720 19786 658 2848 -393 C ATOM 2759 CB GLU B 528 146.714 245.852 814.154 1.00171.26 C ANISOU 2759 CB GLU B 528 24649 20804 19619 369 2562 -719 C ATOM 2760 CG GLU B 528 145.993 246.851 815.065 1.00174.65 C ANISOU 2760 CG GLU B 528 25220 20883 20258 52 2831 -1118 C ATOM 2761 CD GLU B 528 146.851 248.051 815.446 1.00174.61 C ANISOU 2761 CD GLU B 528 25115 21034 20194 -216 2572 -1410 C ATOM 2762 OE2 GLU B 528 146.300 249.019 816.020 1.00177.84 O ANISOU 2762 OE2 GLU B 528 25562 21165 20844 -484 2799 -1755 O ATOM 2763 OE1 GLU B 528 148.073 248.025 815.177 1.00171.63 O ANISOU 2763 OE1 GLU B 528 24601 21049 19561 -165 2156 -1317 O ATOM 2764 C GLU B 528 146.408 244.118 812.356 1.00169.53 C ANISOU 2764 C GLU B 528 24224 20795 19395 985 2646 -4 C ATOM 2765 O GLU B 528 146.256 244.651 811.252 1.00170.38 O ANISOU 2765 O GLU B 528 24159 20963 19616 1183 2790 305 O ATOM 2766 N TRP B 529 147.073 242.982 812.528 1.00146.75 N ANISOU 2766 N TRP B 529 21292 18161 16305 1060 2339 -28 N ATOM 2767 CA TRP B 529 147.713 242.313 811.399 1.00145.08 C ANISOU 2767 CA TRP B 529 20797 18315 16010 1340 2115 223 C ATOM 2768 C TRP B 529 146.925 241.127 810.862 1.00145.82 C ANISOU 2768 C TRP B 529 20843 18374 16187 1622 2320 488 C ATOM 2769 O TRP B 529 147.354 240.478 809.900 1.00145.04 O ANISOU 2769 O TRP B 529 20467 18613 16030 1868 2146 651 O ATOM 2770 CB TRP B 529 149.138 241.889 811.750 1.00142.35 C ANISOU 2770 CB TRP B 529 20334 18280 15473 1247 1642 16 C ATOM 2771 CG TRP B 529 150.099 243.011 811.707 1.00141.44 C ANISOU 2771 CG TRP B 529 20131 18351 15260 1094 1393 -120 C ATOM 2772 CD1 TRP B 529 150.687 243.630 812.771 1.00140.93 C ANISOU 2772 CD1 TRP B 529 20189 18267 15092 810 1228 -406 C ATOM 2773 NE1 TRP B 529 151.510 244.638 812.331 1.00140.23 N ANISOU 2773 NE1 TRP B 529 19951 18382 14950 752 1029 -433 N ATOM 2774 CE2 TRP B 529 151.455 244.691 810.963 1.00140.41 C ANISOU 2774 CE2 TRP B 529 19755 18576 15018 1016 1070 -162 C ATOM 2775 CZ2 TRP B 529 152.096 245.537 810.074 1.00140.17 C ANISOU 2775 CZ2 TRP B 529 19515 18807 14935 1102 938 -67 C ATOM 2776 CH2 TRP B 529 151.842 245.360 808.742 1.00141.03 C ANISOU 2776 CH2 TRP B 529 19402 19145 15040 1445 1024 226 C ATOM 2777 CZ3 TRP B 529 150.971 244.366 808.289 1.00142.08 C ANISOU 2777 CZ3 TRP B 529 19507 19245 15232 1687 1229 423 C ATOM 2778 CE3 TRP B 529 150.337 243.527 809.167 1.00142.09 C ANISOU 2778 CE3 TRP B 529 19726 18938 15325 1578 1366 336 C ATOM 2779 CD2 TRP B 529 150.573 243.683 810.536 1.00141.27 C ANISOU 2779 CD2 TRP B 529 19863 18601 15213 1243 1291 37 C ATOM 2780 N ARG B 530 145.784 240.847 811.486 1.00143.37 N ANISOU 2780 N ARG B 530 20780 17679 16016 1585 2687 496 N ATOM 2781 CA ARG B 530 144.869 239.794 811.031 1.00144.50 C ANISOU 2781 CA ARG B 530 20902 17733 16269 1854 2952 777 C ATOM 2782 C ARG B 530 145.544 238.455 810.657 1.00142.68 C ANISOU 2782 C ARG B 530 20444 17822 15946 2027 2654 827 C ATOM 2783 O ARG B 530 145.500 238.024 809.500 1.00143.10 O ANISOU 2783 O ARG B 530 20215 18152 16005 2319 2634 1075 O ATOM 2784 CB ARG B 530 143.989 240.306 809.878 1.00146.96 C ANISOU 2784 CB ARG B 530 21090 18009 16738 2129 3320 1174 C ATOM 2785 N LEU B 531 146.155 237.800 811.643 1.00139.61 N ANISOU 2785 N LEU B 531 20148 17408 15489 1863 2447 587 N ATOM 2786 CA LEU B 531 146.793 236.495 811.443 1.00138.35 C ANISOU 2786 CA LEU B 531 19767 17449 15352 1990 2227 602 C ATOM 2787 C LEU B 531 146.021 235.371 812.129 1.00139.22 C ANISOU 2787 C LEU B 531 20046 17286 15565 2049 2476 673 C ATOM 2788 O LEU B 531 146.625 234.553 812.811 1.00138.29 O ANISOU 2788 O LEU B 531 19918 17168 15458 2001 2340 569 O ATOM 2789 CB LEU B 531 148.210 236.488 812.025 1.00136.28 C ANISOU 2789 CB LEU B 531 19427 17356 14997 1808 1845 342 C ATOM 2790 CG LEU B 531 149.274 237.490 811.576 1.00135.03 C ANISOU 2790 CG LEU B 531 19101 17479 14725 1714 1535 212 C ATOM 2791 CD1 LEU B 531 148.894 238.879 811.983 1.00135.71 C ANISOU 2791 CD1 LEU B 531 19423 17421 14721 1533 1653 145 C ATOM 2792 CD2 LEU B 531 150.620 237.134 812.189 1.00133.33 C ANISOU 2792 CD2 LEU B 531 18786 17385 14488 1585 1223 7 C ATOM 2793 N PRO B 532 144.691 235.307 811.934 1.00128.66 N ANISOU 2793 N PRO B 532 18849 15706 14329 2178 2873 884 N ATOM 2794 CA PRO B 532 143.870 234.459 812.799 1.00129.75 C ANISOU 2794 CA PRO B 532 19228 15531 14540 2194 3154 913 C ATOM 2795 C PRO B 532 144.404 233.039 812.910 1.00128.80 C ANISOU 2795 C PRO B 532 18935 15511 14493 2303 3006 952 C ATOM 2796 O PRO B 532 144.170 232.390 813.919 1.00129.22 O ANISOU 2796 O PRO B 532 19187 15362 14548 2272 3138 914 O ATOM 2797 CB PRO B 532 142.502 234.464 812.105 1.00132.11 C ANISOU 2797 CB PRO B 532 19563 15639 14994 2404 3581 1217 C ATOM 2798 CG PRO B 532 142.506 235.658 811.252 1.00132.65 C ANISOU 2798 CG PRO B 532 19521 15827 15055 2427 3594 1303 C ATOM 2799 CD PRO B 532 143.922 235.795 810.780 1.00130.34 C ANISOU 2799 CD PRO B 532 18941 15967 14615 2392 3101 1171 C ATOM 2800 N GLU B 533 145.111 232.561 811.894 1.00205.05 N ANISOU 2800 N GLU B 533 28200 25483 24227 2439 2755 1009 N ATOM 2801 CA GLU B 533 145.700 231.232 811.964 1.00204.58 C ANISOU 2801 CA GLU B 533 27911 25482 24338 2514 2630 996 C ATOM 2802 CB GLU B 533 146.403 230.876 810.645 1.00204.40 C ANISOU 2802 CB GLU B 533 27391 25856 24416 2656 2353 971 C ATOM 2803 CG GLU B 533 145.483 230.861 809.414 1.00206.20 C ANISOU 2803 CG GLU B 533 27433 26277 24634 2930 2500 1217 C ATOM 2804 CD GLU B 533 146.251 230.852 808.088 1.00206.44 C ANISOU 2804 CD GLU B 533 26961 26844 24635 3076 2171 1117 C ATOM 2805 OE1 GLU B 533 147.501 230.784 808.120 1.00205.17 O ANISOU 2805 OE1 GLU B 533 26591 26843 24520 2938 1840 824 O ATOM 2806 OE2 GLU B 533 145.611 230.913 807.013 1.00208.28 O ANISOU 2806 OE2 GLU B 533 26986 27363 24789 3352 2258 1330 O ATOM 2807 C GLU B 533 146.676 231.146 813.142 1.00203.34 C ANISOU 2807 C GLU B 533 27866 25256 24138 2323 2473 796 C ATOM 2808 O GLU B 533 146.914 230.063 813.683 1.00203.56 O ANISOU 2808 O GLU B 533 27844 25171 24329 2375 2527 836 O ATOM 2809 N ILE B 534 147.209 232.299 813.548 1.00128.06 N ANISOU 2809 N ILE B 534 18469 15795 14394 2127 2311 615 N ATOM 2810 CA ILE B 534 148.275 232.365 814.559 1.00127.07 C ANISOU 2810 CA ILE B 534 18392 15704 14184 1977 2128 449 C ATOM 2811 CB ILE B 534 149.143 233.655 814.424 1.00125.77 C ANISOU 2811 CB ILE B 534 18190 15757 13839 1796 1839 255 C ATOM 2812 CG1 ILE B 534 150.624 233.378 814.705 1.00124.55 C ANISOU 2812 CG1 ILE B 534 17817 15757 13751 1739 1567 146 C ATOM 2813 CD1 ILE B 534 151.522 233.409 813.468 1.00123.60 C ANISOU 2813 CD1 ILE B 534 17291 15889 13782 1771 1294 62 C ATOM 2814 CG2 ILE B 534 148.666 234.723 815.350 1.00126.42 C ANISOU 2814 CG2 ILE B 534 18626 15741 13666 1622 1936 127 C ATOM 2815 C ILE B 534 147.721 232.324 815.969 1.00128.20 C ANISOU 2815 C ILE B 534 18907 15644 14158 1926 2350 430 C ATOM 2816 O ILE B 534 148.378 231.841 816.885 1.00128.21 O ANISOU 2816 O ILE B 534 18924 15664 14126 1929 2313 419 O ATOM 2817 N ALA B 535 146.515 232.848 816.152 1.00124.79 N ANISOU 2817 N ALA B 535 18755 15037 13623 1899 2606 423 N ATOM 2818 CA ALA B 535 145.923 232.871 817.479 1.00126.45 C ANISOU 2818 CA ALA B 535 19303 15103 13639 1851 2815 321 C ATOM 2819 CB ALA B 535 144.916 233.987 817.590 1.00128.01 C ANISOU 2819 CB ALA B 535 19749 15147 13741 1711 3007 152 C ATOM 2820 C ALA B 535 145.280 231.527 817.791 1.00127.65 C ANISOU 2820 C ALA B 535 19509 15069 13923 2060 3091 536 C ATOM 2821 O ALA B 535 145.561 230.922 818.824 1.00128.36 O ANISOU 2821 O ALA B 535 19683 15179 13908 2124 3137 551 O ATOM 2822 N LYS B 536 144.432 231.063 816.875 1.00153.26 N ANISOU 2822 N LYS B 536 22681 18160 17393 2197 3288 737 N ATOM 2823 CA LYS B 536 143.727 229.791 817.024 1.00154.51 C ANISOU 2823 CA LYS B 536 22867 18124 17716 2405 3572 967 C ATOM 2824 CB LYS B 536 143.249 229.260 815.668 1.00154.53 C ANISOU 2824 CB LYS B 536 22611 18108 17996 2574 3646 1205 C ATOM 2825 C LYS B 536 144.603 228.761 817.718 1.00154.24 C ANISOU 2825 C LYS B 536 22716 18145 17743 2493 3498 1042 C ATOM 2826 O LYS B 536 144.217 228.225 818.752 1.00155.77 O ANISOU 2826 O LYS B 536 23121 18229 17834 2585 3721 1098 O ATOM 2827 N GLU B 537 145.791 228.504 817.177 1.00200.84 N ANISOU 2827 N GLU B 537 28269 24216 23823 2480 3216 1040 N ATOM 2828 CA GLU B 537 146.669 227.502 817.779 1.00201.03 C ANISOU 2828 CA GLU B 537 28132 24231 24020 2578 3212 1147 C ATOM 2829 CB GLU B 537 147.830 227.111 816.867 1.00199.84 C ANISOU 2829 CB GLU B 537 27516 24196 24217 2562 2954 1111 C ATOM 2830 CG GLU B 537 148.645 225.965 817.463 1.00200.72 C ANISOU 2830 CG GLU B 537 27424 24195 24646 2679 3055 1257 C ATOM 2831 CD GLU B 537 149.989 225.772 816.801 1.00199.94 C ANISOU 2831 CD GLU B 537 26876 24190 24903 2612 2808 1127 C ATOM 2832 OE1 GLU B 537 150.133 226.142 815.620 1.00198.99 O ANISOU 2832 OE1 GLU B 537 26520 24235 24853 2530 2570 941 O ATOM 2833 OE2 GLU B 537 150.902 225.240 817.466 1.00200.67 O ANISOU 2833 OE2 GLU B 537 26833 24199 25213 2662 2878 1217 O ATOM 2834 C GLU B 537 147.199 227.912 819.149 1.00201.54 C ANISOU 2834 C GLU B 537 28414 24400 23762 2535 3190 1072 C ATOM 2835 O GLU B 537 147.292 227.080 820.046 1.00202.98 O ANISOU 2835 O GLU B 537 28643 24520 23962 2702 3385 1249 O ATOM 2836 N ILE B 538 147.561 229.181 819.315 1.00131.06 N ANISOU 2836 N ILE B 538 19594 15667 14537 2342 2965 831 N ATOM 2837 CA ILE B 538 147.956 229.661 820.639 1.00132.07 C ANISOU 2837 CA ILE B 538 19918 15976 14285 2317 2935 730 C ATOM 2838 CB ILE B 538 148.045 231.205 820.705 1.00131.48 C ANISOU 2838 CB ILE B 538 19975 16091 13891 2067 2708 407 C ATOM 2839 CG1 ILE B 538 149.267 231.704 819.922 1.00129.17 C ANISOU 2839 CG1 ILE B 538 19391 15951 13737 1944 2371 353 C ATOM 2840 CD1 ILE B 538 150.554 230.891 820.150 1.00128.81 C ANISOU 2840 CD1 ILE B 538 19071 15975 13896 2066 2295 530 C ATOM 2841 CG2 ILE B 538 148.088 231.681 822.158 1.00133.49 C ANISOU 2841 CG2 ILE B 538 20457 16576 13687 2063 2722 246 C ATOM 2842 C ILE B 538 146.925 229.175 821.652 1.00134.63 C ANISOU 2842 C ILE B 538 20542 16212 14401 2471 3265 795 C ATOM 2843 O ILE B 538 147.252 228.488 822.624 1.00136.18 O ANISOU 2843 O ILE B 538 20757 16489 14498 2666 3394 964 O ATOM 2844 N TYR B 539 145.677 229.542 821.382 1.00133.60 N ANISOU 2844 N TYR B 539 20627 15914 14223 2406 3431 677 N ATOM 2845 CA TYR B 539 144.509 229.131 822.151 1.00136.22 C ANISOU 2845 CA TYR B 539 21245 16111 14400 2533 3775 686 C ATOM 2846 CB TYR B 539 143.252 229.336 821.289 1.00136.45 C ANISOU 2846 CB TYR B 539 21378 15844 14623 2476 3980 665 C ATOM 2847 CG TYR B 539 141.915 229.014 821.939 1.00139.31 C ANISOU 2847 CG TYR B 539 22042 16005 14884 2580 4374 635 C ATOM 2848 CD1 TYR B 539 141.425 227.707 821.963 1.00140.19 C ANISOU 2848 CD1 TYR B 539 22148 15932 15185 2835 4652 959 C ATOM 2849 CE1 TYR B 539 140.193 227.413 822.535 1.00142.92 C ANISOU 2849 CE1 TYR B 539 22773 16089 15441 2941 5027 931 C ATOM 2850 CZ TYR B 539 139.436 228.432 823.078 1.00145.04 C ANISOU 2850 CZ TYR B 539 23311 16338 15461 2774 5133 525 C ATOM 2851 OH TYR B 539 138.222 228.145 823.644 1.00148.12 O ANISOU 2851 OH TYR B 539 23963 16529 15785 2873 5523 444 O ATOM 2852 CE2 TYR B 539 139.893 229.732 823.056 1.00144.41 C ANISOU 2852 CE2 TYR B 539 23216 16421 15233 2502 4867 173 C ATOM 2853 CD2 TYR B 539 141.122 230.018 822.481 1.00141.43 C ANISOU 2853 CD2 TYR B 539 22576 16241 14917 2415 4488 255 C ATOM 2854 C TYR B 539 144.627 227.680 822.625 1.00137.30 C ANISOU 2854 C TYR B 539 21312 16178 14676 2830 3994 1038 C ATOM 2855 O TYR B 539 144.082 227.319 823.670 1.00139.85 O ANISOU 2855 O TYR B 539 21855 16539 14741 2992 4232 1059 O ATOM 2856 N THR B 540 145.351 226.860 821.867 1.00161.79 N ANISOU 2856 N THR B 540 24082 19190 18200 2907 3927 1292 N ATOM 2857 CA THR B 540 145.469 225.439 822.184 1.00163.03 C ANISOU 2857 CA THR B 540 24113 19207 18625 3179 4176 1645 C ATOM 2858 CB THR B 540 145.664 224.579 820.921 1.00161.77 C ANISOU 2858 CB THR B 540 23583 18835 19046 3204 4162 1815 C ATOM 2859 OG1 THR B 540 147.010 224.713 820.448 1.00160.18 O ANISOU 2859 OG1 THR B 540 23039 18751 19070 3101 3873 1754 O ATOM 2860 CG2 THR B 540 144.692 225.006 819.827 1.00160.92 C ANISOU 2860 CG2 THR B 540 23515 18633 18997 3095 4145 1708 C ATOM 2861 C THR B 540 146.549 225.102 823.220 1.00164.14 C ANISOU 2861 C THR B 540 24165 19540 18659 3338 4179 1804 C ATOM 2862 O THR B 540 146.367 224.171 824.014 1.00166.42 O ANISOU 2862 O THR B 540 24503 19780 18949 3615 4481 2084 O ATOM 2863 N THR B 541 147.665 225.834 823.221 1.00139.09 N ANISOU 2863 N THR B 541 20855 16592 15403 3200 3879 1671 N ATOM 2864 CA THR B 541 148.661 225.633 824.276 1.00140.60 C ANISOU 2864 CA THR B 541 20972 17007 15444 3384 3914 1856 C ATOM 2865 CB THR B 541 150.000 226.298 823.959 1.00138.81 C ANISOU 2865 CB THR B 541 20501 16942 15298 3222 3592 1753 C ATOM 2866 OG1 THR B 541 149.872 227.715 824.124 1.00138.03 O ANISOU 2866 OG1 THR B 541 20608 17123 14712 2991 3316 1386 O ATOM 2867 CG2 THR B 541 150.427 225.968 822.536 1.00136.51 C ANISOU 2867 CG2 THR B 541 19869 16394 15604 3072 3456 1717 C ATOM 2868 C THR B 541 148.100 226.232 825.555 1.00143.03 C ANISOU 2868 C THR B 541 21629 17643 15074 3471 3978 1717 C ATOM 2869 O THR B 541 148.190 225.628 826.630 1.00145.85 O ANISOU 2869 O THR B 541 22033 18162 15220 3785 4215 1973 O ATOM 2870 N LEU B 542 147.527 227.428 825.418 1.00136.95 N ANISOU 2870 N LEU B 542 21069 16987 13978 3205 3782 1296 N ATOM 2871 CA LEU B 542 146.836 228.114 826.509 1.00139.65 C ANISOU 2871 CA LEU B 542 21717 17630 13711 3217 3822 1005 C ATOM 2872 CB LEU B 542 146.262 229.445 826.023 1.00138.61 C ANISOU 2872 CB LEU B 542 21730 17480 13457 2852 3622 521 C ATOM 2873 CG LEU B 542 145.887 230.452 827.105 1.00141.47 C ANISOU 2873 CG LEU B 542 22306 18219 13227 2770 3555 74 C ATOM 2874 CD1 LEU B 542 147.116 231.240 827.529 1.00141.11 C ANISOU 2874 CD1 LEU B 542 22105 18605 12907 2701 3223 -26 C ATOM 2875 CD2 LEU B 542 144.821 231.388 826.606 1.00141.54 C ANISOU 2875 CD2 LEU B 542 22490 17998 13292 2462 3576 -354 C ATOM 2876 C LEU B 542 145.705 227.269 827.065 1.00142.37 C ANISOU 2876 C LEU B 542 22276 17855 13964 3460 4203 1124 C ATOM 2877 O LEU B 542 145.605 227.069 828.270 1.00145.64 O ANISOU 2877 O LEU B 542 22810 18593 13933 3712 4345 1156 O ATOM 2878 N GLY B 543 144.841 226.794 826.176 1.00143.78 N ANISOU 2878 N GLY B 543 22490 17608 14534 3406 4371 1192 N ATOM 2879 CA GLY B 543 143.770 225.902 826.563 1.00146.14 C ANISOU 2879 CA GLY B 543 22969 17728 14830 3639 4756 1351 C ATOM 2880 C GLY B 543 144.294 224.636 827.211 1.00147.82 C ANISOU 2880 C GLY B 543 23049 17989 15126 4028 4991 1836 C ATOM 2881 O GLY B 543 143.707 224.118 828.157 1.00151.03 O ANISOU 2881 O GLY B 543 23635 18511 15238 4308 5277 1939 O ATOM 2882 N ASN B 544 145.413 224.134 826.712 1.00157.05 N ANISOU 2882 N ASN B 544 23883 19066 16722 4061 4900 2132 N ATOM 2883 CA ASN B 544 145.963 222.908 827.260 1.00158.96 C ANISOU 2883 CA ASN B 544 23947 19272 17179 4432 5185 2633 C ATOM 2884 CB ASN B 544 147.041 222.347 826.341 1.00156.82 C ANISOU 2884 CB ASN B 544 23253 18734 17598 4370 5106 2859 C ATOM 2885 CG ASN B 544 146.452 221.601 825.174 1.00155.42 C ANISOU 2885 CG ASN B 544 22933 18116 18005 4285 5201 2919 C ATOM 2886 OD1 ASN B 544 145.315 221.139 825.242 1.00156.61 O ANISOU 2886 OD1 ASN B 544 23278 18110 18116 4392 5450 2984 O ATOM 2887 ND2 ASN B 544 147.212 221.482 824.097 1.00153.22 N ANISOU 2887 ND2 ASN B 544 22294 17668 18256 4105 5006 2878 N ATOM 2888 C ASN B 544 146.463 223.043 828.695 1.00162.19 C ANISOU 2888 C ASN B 544 24431 20172 17024 4729 5258 2752 C ATOM 2889 O ASN B 544 146.107 222.237 829.555 1.00165.47 O ANISOU 2889 O ASN B 544 24928 20670 17272 5108 5607 3058 O ATOM 2890 N GLN B 545 147.271 224.069 828.955 1.00163.54 N ANISOU 2890 N GLN B 545 24559 20708 16870 4587 4937 2524 N ATOM 2891 CA GLN B 545 147.817 224.285 830.292 1.00166.89 C ANISOU 2891 CA GLN B 545 25007 21701 16703 4890 4970 2635 C ATOM 2892 CB GLN B 545 148.782 225.463 830.300 1.00165.50 C ANISOU 2892 CB GLN B 545 24728 21863 16293 4664 4569 2373 C ATOM 2893 CG GLN B 545 150.083 225.169 829.598 1.00163.14 C ANISOU 2893 CG GLN B 545 24067 21321 16597 4612 4495 2668 C ATOM 2894 CD GLN B 545 150.835 226.432 829.239 1.00160.76 C ANISOU 2894 CD GLN B 545 23693 21226 16163 4278 4060 2320 C ATOM 2895 OE1 GLN B 545 150.413 227.535 829.583 1.00161.09 O ANISOU 2895 OE1 GLN B 545 23940 21607 15660 4095 3821 1875 O ATOM 2896 NE2 GLN B 545 151.952 226.279 828.543 1.00158.65 N ANISOU 2896 NE2 GLN B 545 23113 20741 16427 4191 3972 2492 N ATOM 2897 C GLN B 545 146.715 224.502 831.318 1.00170.53 C ANISOU 2897 C GLN B 545 25798 22522 16473 5056 5101 2388 C ATOM 2898 O GLN B 545 146.882 224.187 832.494 1.00174.51 O ANISOU 2898 O GLN B 545 26318 23485 16503 5471 5285 2615 O ATOM 2899 N MET B 546 145.585 225.033 830.869 1.00165.89 N ANISOU 2899 N MET B 546 25452 21741 15836 4754 5034 1923 N ATOM 2900 CA MET B 546 144.418 225.164 831.730 1.00169.58 C ANISOU 2900 CA MET B 546 26222 22451 15760 4876 5205 1620 C ATOM 2901 CB MET B 546 143.331 225.987 831.042 1.00168.17 C ANISOU 2901 CB MET B 546 26256 21971 15670 4448 5108 1059 C ATOM 2902 CG MET B 546 143.235 227.419 831.540 1.00169.59 C ANISOU 2902 CG MET B 546 26538 22569 15329 4183 4816 396 C ATOM 2903 SD MET B 546 142.026 227.597 832.863 1.00175.66 S ANISOU 2903 SD MET B 546 27591 23756 15395 4361 5030 -98 S ATOM 2904 CE MET B 546 140.484 227.470 831.947 1.00174.69 C ANISOU 2904 CE MET B 546 27705 22890 15780 4106 5319 -301 C ATOM 2905 C MET B 546 143.882 223.796 832.113 1.00172.00 C ANISOU 2905 C MET B 546 26579 22596 16178 5299 5663 2090 C ATOM 2906 O MET B 546 143.538 223.558 833.266 1.00176.38 O ANISOU 2906 O MET B 546 27260 23586 16171 5659 5860 2113 O ATOM 2907 N LEU B 547 143.811 222.895 831.141 1.00173.92 N ANISOU 2907 N LEU B 547 26700 22248 17136 5272 5831 2454 N ATOM 2908 CA LEU B 547 143.296 221.551 831.391 1.00176.05 C ANISOU 2908 CA LEU B 547 26987 22290 17616 5652 6283 2926 C ATOM 2909 CB LEU B 547 143.151 220.767 830.089 1.00172.86 C ANISOU 2909 CB LEU B 547 26410 21222 18048 5502 6381 3178 C ATOM 2910 CG LEU B 547 141.992 221.201 829.187 1.00170.92 C ANISOU 2910 CG LEU B 547 26355 20632 17956 5162 6326 2800 C ATOM 2911 CD1 LEU B 547 142.381 221.093 827.701 1.00166.82 C ANISOU 2911 CD1 LEU B 547 25555 19697 18131 4875 6141 2864 C ATOM 2912 CD2 LEU B 547 140.700 220.425 829.502 1.00173.54 C ANISOU 2912 CD2 LEU B 547 26917 20769 18251 5395 6745 2920 C ATOM 2913 C LEU B 547 144.220 220.815 832.327 1.00179.01 C ANISOU 2913 C LEU B 547 27172 22981 17863 6139 6499 3475 C ATOM 2914 O LEU B 547 143.778 220.106 833.219 1.00182.92 O ANISOU 2914 O LEU B 547 27770 23667 18065 6572 6853 3749 O ATOM 2915 N SER B 548 145.515 220.993 832.117 1.00161.22 N ANISOU 2915 N SER B 548 24630 20784 15841 6090 6313 3655 N ATOM 2916 CA SER B 548 146.522 220.396 832.983 1.00164.26 C ANISOU 2916 CA SER B 548 24793 21463 16156 6561 6543 4219 C ATOM 2917 CB SER B 548 147.921 220.794 832.525 1.00161.85 C ANISOU 2917 CB SER B 548 24170 21126 16198 6385 6293 4303 C ATOM 2918 OG SER B 548 147.975 220.850 831.110 1.00157.25 O ANISOU 2918 OG SER B 548 23461 19975 16312 5928 6087 4097 O ATOM 2919 C SER B 548 146.294 220.858 834.410 1.00168.93 C ANISOU 2919 C SER B 548 25577 22839 15769 6909 6571 4107 C ATOM 2920 O SER B 548 146.510 220.106 835.355 1.00173.15 O ANISOU 2920 O SER B 548 26043 23671 16077 7464 6932 4623 O ATOM 2921 N ALA B 549 145.851 222.103 834.559 1.00174.70 N ANISOU 2921 N ALA B 549 26520 23927 15930 6597 6202 3420 N ATOM 2922 CA ALA B 549 145.548 222.648 835.876 1.00179.55 C ANISOU 2922 CA ALA B 549 27291 25354 15576 6874 6170 3146 C ATOM 2923 CB ALA B 549 145.372 224.155 835.810 1.00178.48 C ANISOU 2923 CB ALA B 549 27273 25519 15024 6408 5694 2341 C ATOM 2924 C ALA B 549 144.304 221.991 836.455 1.00183.19 C ANISOU 2924 C ALA B 549 28001 25862 15739 7169 6527 3131 C ATOM 2925 O ALA B 549 144.357 221.402 837.526 1.00188.02 O ANISOU 2925 O ALA B 549 28593 26968 15879 7740 6817 3498 O ATOM 2926 N HIS B 550 143.181 222.088 835.755 1.00180.84 N ANISOU 2926 N HIS B 550 27930 25071 15711 6813 6533 2735 N ATOM 2927 CA HIS B 550 141.971 221.444 836.245 1.00184.24 C ANISOU 2927 CA HIS B 550 28601 25484 15917 7078 6899 2717 C ATOM 2928 C HIS B 550 142.306 220.021 836.665 1.00186.57 C ANISOU 2928 C HIS B 550 28752 25728 16406 7668 7363 3566 C ATOM 2929 O HIS B 550 142.010 219.607 837.780 1.00191.76 O ANISOU 2929 O HIS B 550 29488 26908 16464 8182 7632 3730 O ATOM 2930 CB HIS B 550 140.841 221.454 835.203 1.00181.23 C ANISOU 2930 CB HIS B 550 28416 24389 16054 6660 6947 2408 C ATOM 2931 CG HIS B 550 139.634 220.657 835.613 1.00184.50 C ANISOU 2931 CG HIS B 550 29059 24689 16354 6946 7375 2477 C ATOM 2932 ND1 HIS B 550 138.582 221.205 836.317 1.00188.32 N ANISOU 2932 ND1 HIS B 550 29818 25501 16236 6938 7417 1855 N ATOM 2933 CE1 HIS B 550 137.675 220.273 836.548 1.00190.73 C ANISOU 2933 CE1 HIS B 550 30279 25610 16580 7237 7845 2083 C ATOM 2934 NE2 HIS B 550 138.099 219.139 836.020 1.00188.59 N ANISOU 2934 NE2 HIS B 550 29835 24895 16925 7436 8078 2844 N ATOM 2935 CD2 HIS B 550 139.326 219.351 835.434 1.00184.84 C ANISOU 2935 CD2 HIS B 550 29079 24327 16824 7252 7794 3077 C ATOM 2936 N ASN B 551 142.950 219.281 835.774 1.00223.04 N ANISOU 2936 N ASN B 551 33130 29738 21876 7606 7467 4093 N ATOM 2937 CA ASN B 551 143.266 217.889 836.044 1.00225.22 C ANISOU 2937 CA ASN B 551 33223 29826 22524 8119 7956 4908 C ATOM 2938 C ASN B 551 144.140 217.705 837.282 1.00229.99 C ANISOU 2938 C ASN B 551 33667 31127 22591 8714 8130 5374 C ATOM 2939 O ASN B 551 144.395 216.580 837.721 1.00233.02 O ANISOU 2939 O ASN B 551 33896 31451 23189 9241 8607 6101 O ATOM 2940 CB ASN B 551 143.948 217.249 834.839 1.00221.02 C ANISOU 2940 CB ASN B 551 32382 28543 23052 7888 7990 5279 C ATOM 2941 CG ASN B 551 144.256 215.786 835.067 1.00223.59 C ANISOU 2941 CG ASN B 551 32473 28580 23900 8382 8538 6095 C ATOM 2942 OD1 ASN B 551 143.349 214.959 835.166 1.00225.33 O ANISOU 2942 OD1 ASN B 551 32819 28573 24221 8596 8895 6294 O ATOM 2943 ND2 ASN B 551 145.540 215.458 835.166 1.00224.17 N ANISOU 2943 ND2 ASN B 551 32190 28638 24346 8575 8646 6585 N ATOM 2944 N ILE B 552 144.597 218.811 837.849 1.00185.57 N ANISOU 2944 N ILE B 552 28053 26179 16275 8656 7767 4983 N ATOM 2945 CA ILE B 552 145.446 218.740 839.029 1.00190.45 C ANISOU 2945 CA ILE B 552 28493 27566 16303 9249 7907 5424 C ATOM 2946 C ILE B 552 144.720 219.261 840.275 1.00195.99 C ANISOU 2946 C ILE B 552 29419 29206 15844 9566 7859 4995 C ATOM 2947 O ILE B 552 144.998 218.832 841.390 1.00201.64 O ANISOU 2947 O ILE B 552 30037 30601 15977 10243 8144 5457 O ATOM 2948 CB ILE B 552 146.794 219.462 838.790 1.00188.18 C ANISOU 2948 CB ILE B 552 27936 27412 16151 9055 7578 5459 C ATOM 2949 CG1 ILE B 552 147.610 218.714 837.733 1.00184.26 C ANISOU 2949 CG1 ILE B 552 27149 26057 16806 8890 7739 5974 C ATOM 2950 CD1 ILE B 552 147.787 217.238 838.034 1.00187.45 C ANISOU 2950 CD1 ILE B 552 27362 26169 17692 9459 8381 6854 C ATOM 2951 CG2 ILE B 552 147.594 219.571 840.068 1.00193.70 C ANISOU 2951 CG2 ILE B 552 28461 29028 16108 9676 7688 5854 C ATOM 2952 N ILE B 553 143.768 220.163 840.074 1.00197.20 N ANISOU 2952 N ILE B 553 29844 29398 15684 9095 7530 4107 N ATOM 2953 CA ILE B 553 142.952 220.667 841.176 1.00202.75 C ANISOU 2953 CA ILE B 553 30745 30931 15358 9319 7480 3539 C ATOM 2954 C ILE B 553 141.920 219.633 841.663 1.00206.62 C ANISOU 2954 C ILE B 553 31421 31388 15696 9766 7972 3778 C ATOM 2955 O ILE B 553 141.690 219.488 842.865 1.00213.04 O ANISOU 2955 O ILE B 553 32257 33047 15643 10336 8139 3797 O ATOM 2956 CB ILE B 553 142.268 222.002 840.797 1.00200.79 C ANISOU 2956 CB ILE B 553 30693 30666 14932 8640 7016 2463 C ATOM 2957 CG1 ILE B 553 143.280 223.146 840.873 1.00199.75 C ANISOU 2957 CG1 ILE B 553 30365 31000 14532 8404 6538 2171 C ATOM 2958 CD1 ILE B 553 142.675 224.517 840.677 1.00199.00 C ANISOU 2958 CD1 ILE B 553 30413 30994 14205 7797 6110 1115 C ATOM 2959 CG2 ILE B 553 141.072 222.282 841.694 1.00206.37 C ANISOU 2959 CG2 ILE B 553 31636 31930 14844 8782 7076 1787 C ATOM 2960 N GLU B 554 141.307 218.907 840.731 1.00254.98 N ANISOU 2960 N GLU B 554 37659 36584 22637 9537 8206 3968 N ATOM 2961 CA GLU B 554 140.344 217.869 841.098 1.00258.27 C ANISOU 2961 CA GLU B 554 38244 36878 23009 9946 8698 4251 C ATOM 2962 C GLU B 554 141.009 216.779 841.931 1.00262.72 C ANISOU 2962 C GLU B 554 38592 37808 23420 10753 9159 5213 C ATOM 2963 O GLU B 554 140.549 216.461 843.029 1.00268.90 O ANISOU 2963 O GLU B 554 39461 39275 23433 11334 9423 5290 O ATOM 2964 CB GLU B 554 139.700 217.249 839.853 1.00253.37 C ANISOU 2964 CB GLU B 554 37718 35174 23376 9559 8863 4370 C ATOM 2965 CG GLU B 554 138.834 218.208 839.042 1.00249.83 C ANISOU 2965 CG GLU B 554 37502 34329 23094 8852 8534 3507 C ATOM 2966 CD GLU B 554 137.508 218.523 839.712 1.00254.17 C ANISOU 2966 CD GLU B 554 38371 35194 23008 8901 8639 2851 C ATOM 2967 OE1 GLU B 554 137.183 217.872 840.733 1.00259.68 O ANISOU 2967 OE1 GLU B 554 39127 36387 23153 9498 8978 3092 O ATOM 2968 OE2 GLU B 554 136.791 219.424 839.206 1.00252.39 O ANISOU 2968 OE2 GLU B 554 38320 34713 22864 8356 8411 2097 O ATOM 2969 N SER B 555 142.090 216.222 841.387 1.00208.47 N ANISOU 2969 N SER B 555 31422 30473 17314 10791 9278 5931 N ATOM 2970 CA SER B 555 142.856 215.129 842.006 1.00212.34 C ANISOU 2970 CA SER B 555 31641 31115 17924 11524 9794 6958 C ATOM 2971 C SER B 555 142.405 214.707 843.406 1.00220.13 C ANISOU 2971 C SER B 555 32709 32984 17946 12327 10160 7215 C ATOM 2972 O SER B 555 142.310 215.527 844.317 1.00224.12 O ANISOU 2972 O SER B 555 33287 34468 17400 12510 9908 6737 O ATOM 2973 CB SER B 555 144.355 215.450 842.001 1.00211.45 C ANISOU 2973 CB SER B 555 31179 31172 17992 11570 9650 7333 C ATOM 2974 OG SER B 555 144.589 216.742 842.519 1.00212.47 O ANISOU 2974 OG SER B 555 31355 32122 17254 11432 9155 6699 O CONECT 727 726 1990 CONECT 1990 727 1991 END