HEADER HYDROLASE 11-MAY-11 3RZE TITLE STRUCTURE OF THE HUMAN HISTAMINE H1 RECEPTOR IN COMPLEX WITH DOXEPIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISTAMINE H1 RECEPTOR, LYSOZYME CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: H1R, HH1R, ENDOLYSIN, LYSIS PROTEIN, MURAMIDASE; COMPND 5 EC: 3.2.1.17; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: HRH1, E; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMD1163; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9K KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MEMBRANE PROTEIN, GPCR NETWORK, KEYWDS 2 GPCR, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR T.SHIMAMURA,G.W.HAN,M.SHIROISHI,S.WEYAND,H.TSUJIMOTO,G.WINTER, AUTHOR 2 V.KATRITCH,R.ABAGYAN,V.CHEREZOV,W.LIU,T.KOBAYASHI,R.STEVENS,S.IWATA, AUTHOR 3 GPCR NETWORK (GPCR) REVDAT 6 24-JAN-18 3RZE 1 AUTHOR REVDAT 5 16-AUG-17 3RZE 1 SOURCE REMARK REVDAT 4 20-JUL-11 3RZE 1 JRNL REVDAT 3 13-JUL-11 3RZE 1 JRNL REVDAT 2 22-JUN-11 3RZE 1 JRNL REVDAT 1 15-JUN-11 3RZE 0 JRNL AUTH T.SHIMAMURA,M.SHIROISHI,S.WEYAND,H.TSUJIMOTO,G.WINTER, JRNL AUTH 2 V.KATRITCH,R.ABAGYAN,V.CHEREZOV,W.LIU,G.W.HAN,T.KOBAYASHI, JRNL AUTH 3 R.C.STEVENS,S.IWATA JRNL TITL STRUCTURE OF THE HUMAN HISTAMINE H1 RECEPTOR COMPLEX WITH JRNL TITL 2 DOXEPIN. JRNL REF NATURE V. 475 65 2011 JRNL REFN ISSN 0028-0836 JRNL PMID 21697825 JRNL DOI 10.1038/NATURE10236 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 11996 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.640 REMARK 3 FREE R VALUE TEST SET COUNT : 797 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.40 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2834 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2369 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2636 REMARK 3 BIN R VALUE (WORKING SET) : 0.2343 REMARK 3 BIN FREE R VALUE : 0.2706 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.99 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 198 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3481 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 72 REMARK 3 SOLVENT ATOMS : 2 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.12 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.19 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -8.12760 REMARK 3 B22 (A**2) : -8.12760 REMARK 3 B33 (A**2) : 16.25530 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.625 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.882 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3640 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4934 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1232 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 62 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 522 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3580 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 471 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 4168 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.21 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.78 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.77 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|28 - A|485 } REMARK 3 ORIGIN FOR THE GROUP (A): 14.1334 33.5398 30.6388 REMARK 3 T TENSOR REMARK 3 T11: 0.2324 T22: 0.0944 REMARK 3 T33: -0.3040 T12: 0.0062 REMARK 3 T13: -0.0654 T23: 0.1063 REMARK 3 L TENSOR REMARK 3 L11: 1.4700 L22: 0.6106 REMARK 3 L33: 5.2307 L12: -0.2457 REMARK 3 L13: 0.6412 L23: -0.6945 REMARK 3 S TENSOR REMARK 3 S11: 0.1370 S12: 0.2784 S13: 0.0552 REMARK 3 S21: -0.3949 S22: 0.0854 S23: -0.1855 REMARK 3 S31: 0.1989 S32: -0.5442 S33: -0.2223 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1002 - A|1161 } REMARK 3 ORIGIN FOR THE GROUP (A): 35.9671 17.0318 70.5261 REMARK 3 T TENSOR REMARK 3 T11: -0.1015 T22: -0.2329 REMARK 3 T33: 0.0710 T12: 0.0006 REMARK 3 T13: 0.0152 T23: -0.0250 REMARK 3 L TENSOR REMARK 3 L11: 2.8613 L22: 1.6343 REMARK 3 L33: 1.3082 L12: 2.0242 REMARK 3 L13: -0.4496 L23: -0.2841 REMARK 3 S TENSOR REMARK 3 S11: -0.1723 S12: 0.1254 S13: -0.2560 REMARK 3 S21: -0.2881 S22: 0.0967 S23: -0.2262 REMARK 3 S31: 0.2478 S32: -0.0164 S33: 0.0756 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3RZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-11. REMARK 100 THE DEPOSITION ID IS D_1000065566. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-OCT-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97780 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12152 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 34.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.14000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 0.83000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2RH1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% PEG400, 300MM AMMONIUM REMARK 280 PHOSPHATE, 10MM MGCL2, 100MM NA-CITRATE PH 4.5, 1MM DOXEPIN, REMARK 280 LIPIDIC CUBIC PHASE, 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 44.07200 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 165.82700 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 44.07200 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 165.82700 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 44.07200 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 165.82700 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 44.07200 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 165.82700 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 44.07200 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 165.82700 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 44.07200 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 165.82700 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 44.07200 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 165.82700 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 44.07200 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 44.07200 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 165.82700 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 THR A 20 REMARK 465 THR A 21 REMARK 465 MET A 22 REMARK 465 ALA A 23 REMARK 465 SER A 24 REMARK 465 PRO A 25 REMARK 465 GLN A 26 REMARK 465 LEU A 27 REMARK 465 PHE A 168 REMARK 465 MET A 169 REMARK 465 GLN A 170 REMARK 465 GLN A 171 REMARK 465 THR A 172 REMARK 465 SER A 173 REMARK 465 VAL A 174 REMARK 465 ARG A 486 REMARK 465 SER A 487 REMARK 465 GLY A 488 REMARK 465 GLU A 489 REMARK 465 ASN A 490 REMARK 465 LEU A 491 REMARK 465 TYR A 492 REMARK 465 PHE A 493 REMARK 465 GLN A 494 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 442 CG CD CE NZ REMARK 470 ARG A 481 CG CD NE CZ NH1 NH2 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 TYR A 135 6.02 -65.24 REMARK 500 LYS A 137 27.01 81.62 REMARK 500 ARG A 139 77.73 -104.15 REMARK 500 LYS A 179 -148.77 -150.40 REMARK 500 GLU A 181 118.26 86.99 REMARK 500 ASP A 183 -26.17 73.98 REMARK 500 PHE A 199 -64.11 -135.84 REMARK 500 GLN A 219 -77.92 -125.61 REMARK 500 CYS A 221 176.98 38.12 REMARK 500 LYS A 442 21.77 92.28 REMARK 500 ASN A 443 56.01 107.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1205 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5EH A 1200 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D7V A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1205 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-53 RELATED DB: TARGETDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4 REMARK 999 LYSOZYME INSERTED BETWEEN CYS221 AND LEU450 OF H1. DBREF 3RZE A 20 221 UNP P35367 HRH1_HUMAN 20 221 DBREF 3RZE A 1002 1161 UNP P00720 LYS_BPT4 2 161 DBREF 3RZE A 405 487 UNP P35367 HRH1_HUMAN 405 487 SEQADV 3RZE THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 3RZE ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 3RZE GLY A 488 UNP P35367 EXPRESSION TAG SEQADV 3RZE GLU A 489 UNP P35367 EXPRESSION TAG SEQADV 3RZE ASN A 490 UNP P35367 EXPRESSION TAG SEQADV 3RZE LEU A 491 UNP P35367 EXPRESSION TAG SEQADV 3RZE TYR A 492 UNP P35367 EXPRESSION TAG SEQADV 3RZE PHE A 493 UNP P35367 EXPRESSION TAG SEQADV 3RZE GLN A 494 UNP P35367 EXPRESSION TAG SEQRES 1 A 452 THR THR MET ALA SER PRO GLN LEU MET PRO LEU VAL VAL SEQRES 2 A 452 VAL LEU SER THR ILE CYS LEU VAL THR VAL GLY LEU ASN SEQRES 3 A 452 LEU LEU VAL LEU TYR ALA VAL ARG SER GLU ARG LYS LEU SEQRES 4 A 452 HIS THR VAL GLY ASN LEU TYR ILE VAL SER LEU SER VAL SEQRES 5 A 452 ALA ASP LEU ILE VAL GLY ALA VAL VAL MET PRO MET ASN SEQRES 6 A 452 ILE LEU TYR LEU LEU MET SER LYS TRP SER LEU GLY ARG SEQRES 7 A 452 PRO LEU CYS LEU PHE TRP LEU SER MET ASP TYR VAL ALA SEQRES 8 A 452 SER THR ALA SER ILE PHE SER VAL PHE ILE LEU CYS ILE SEQRES 9 A 452 ASP ARG TYR ARG SER VAL GLN GLN PRO LEU ARG TYR LEU SEQRES 10 A 452 LYS TYR ARG THR LYS THR ARG ALA SER ALA THR ILE LEU SEQRES 11 A 452 GLY ALA TRP PHE LEU SER PHE LEU TRP VAL ILE PRO ILE SEQRES 12 A 452 LEU GLY TRP ASN HIS PHE MET GLN GLN THR SER VAL ARG SEQRES 13 A 452 ARG GLU ASP LYS CYS GLU THR ASP PHE TYR ASP VAL THR SEQRES 14 A 452 TRP PHE LYS VAL MET THR ALA ILE ILE ASN PHE TYR LEU SEQRES 15 A 452 PRO THR LEU LEU MET LEU TRP PHE TYR ALA LYS ILE TYR SEQRES 16 A 452 LYS ALA VAL ARG GLN HIS CYS ASN ILE PHE GLU MET LEU SEQRES 17 A 452 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 18 A 452 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 19 A 452 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 20 A 452 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 21 A 452 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 22 A 452 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 23 A 452 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 24 A 452 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 25 A 452 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 26 A 452 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 27 A 452 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 28 A 452 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LEU HIS SEQRES 29 A 452 MET ASN ARG GLU ARG LYS ALA ALA LYS GLN LEU GLY PHE SEQRES 30 A 452 ILE MET ALA ALA PHE ILE LEU CYS TRP ILE PRO TYR PHE SEQRES 31 A 452 ILE PHE PHE MET VAL ILE ALA PHE CYS LYS ASN CYS CYS SEQRES 32 A 452 ASN GLU HIS LEU HIS MET PHE THR ILE TRP LEU GLY TYR SEQRES 33 A 452 ILE ASN SER THR LEU ASN PRO LEU ILE TYR PRO LEU CYS SEQRES 34 A 452 ASN GLU ASN PHE LYS LYS THR PHE LYS ARG ILE LEU HIS SEQRES 35 A 452 ILE ARG SER GLY GLU ASN LEU TYR PHE GLN HET 5EH A1200 21 HET D7V A1201 21 HET PO4 A1202 5 HET PO4 A1203 5 HET PO4 A1204 5 HET OLC A1205 15 HETNAM 5EH (3E)-3-(DIBENZO[B,E]OXEPIN-11(6H)-YLIDENE)-N,N- HETNAM 2 5EH DIMETHYLPROPAN-1-AMINE HETNAM D7V (3Z)-3-(DIBENZO[B,E]OXEPIN-11(6H)-YLIDENE)-N,N- HETNAM 2 D7V DIMETHYLPROPAN-1-AMINE HETNAM PO4 PHOSPHATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 5EH C19 H21 N O FORMUL 3 D7V C19 H21 N O FORMUL 4 PO4 3(O4 P 3-) FORMUL 7 OLC C21 H40 O4 FORMUL 8 HOH *2(H2 O) HELIX 1 1 MET A 28 VAL A 31 5 4 HELIX 2 2 VAL A 32 GLU A 55 1 24 HELIX 3 3 THR A 60 GLY A 62 5 3 HELIX 4 4 ASN A 63 VAL A 79 1 17 HELIX 5 5 VAL A 79 MET A 90 1 12 HELIX 6 6 LEU A 95 GLN A 131 1 37 HELIX 7 7 THR A 140 PHE A 156 1 17 HELIX 8 8 TRP A 158 GLY A 164 1 7 HELIX 9 9 VAL A 187 PHE A 199 1 13 HELIX 10 10 PHE A 199 VAL A 217 1 19 HELIX 11 11 ASN A 1002 GLY A 1012 1 11 HELIX 12 12 SER A 1038 GLY A 1051 1 14 HELIX 13 13 THR A 1059 ARG A 1080 1 22 HELIX 14 14 LEU A 1084 LEU A 1091 1 8 HELIX 15 15 ASP A 1092 GLY A 1107 1 16 HELIX 16 16 GLY A 1107 ALA A 1112 1 6 HELIX 17 17 PHE A 1114 GLN A 1123 1 10 HELIX 18 18 ARG A 1125 ALA A 1134 1 10 HELIX 19 19 SER A 1136 THR A 1142 1 7 HELIX 20 20 THR A 1142 GLY A 1156 1 15 HELIX 21 21 TRP A 1158 LEU A 405 5 5 HELIX 22 22 MET A 407 LYS A 442 1 36 HELIX 23 23 LEU A 449 ASN A 472 1 24 HELIX 24 24 ASN A 472 HIS A 484 1 13 SHEET 1 A 3 LEU A1013 LYS A1019 0 SHEET 2 A 3 TYR A1025 ILE A1029 -1 O THR A1026 N TYR A1018 SHEET 3 A 3 HIS A1031 LEU A1032 -1 O HIS A1031 N ILE A1027 SSBOND 1 CYS A 100 CYS A 180 1555 1555 2.03 SSBOND 2 CYS A 441 CYS A 444 1555 1555 2.03 SITE 1 AC1 9 ASP A 107 TYR A 108 SER A 111 THR A 112 SITE 2 AC1 9 TRP A 158 TRP A 428 TYR A 431 PHE A 432 SITE 3 AC1 9 TYR A 458 SITE 1 AC2 12 ASP A 107 TYR A 108 SER A 111 THR A 112 SITE 2 AC2 12 ILE A 115 TRP A 158 ASN A 198 TRP A 428 SITE 3 AC2 12 TYR A 431 PHE A 432 PHE A 435 TYR A 458 SITE 1 AC3 6 ASP A 178 LYS A 179 LYS A 191 TYR A 431 SITE 2 AC3 6 PHE A 435 HIS A 450 SITE 1 AC4 2 ARG A1076 ARG A1080 SITE 1 AC5 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC6 4 GLU A1011 ARG A1014 ASN A1053 ASN A1055 CRYST1 88.144 88.144 331.654 90.00 90.00 90.00 I 4 2 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 0.011345 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011345 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003015 0.00000 ATOM 1 N MET A 28 11.579 13.109 10.857 1.00164.07 N ANISOU 1 N MET A 28 30028 19481 12831 -1646 -2793 -1333 N ATOM 2 CA MET A 28 10.243 12.524 10.957 1.00166.06 C ANISOU 2 CA MET A 28 30466 19735 12894 -2259 -3090 -1277 C ATOM 3 C MET A 28 9.813 12.069 12.377 1.00169.83 C ANISOU 3 C MET A 28 30971 20037 13519 -2593 -3244 -1166 C ATOM 4 O MET A 28 8.675 12.379 12.739 1.00169.06 O ANISOU 4 O MET A 28 30581 20236 13420 -3044 -3362 -980 O ATOM 5 CB MET A 28 10.010 11.433 9.898 1.00172.72 C ANISOU 5 CB MET A 28 31961 20323 13341 -2410 -3302 -1493 C ATOM 6 CG MET A 28 8.549 11.290 9.496 1.00178.23 C ANISOU 6 CG MET A 28 32659 21264 13797 -3031 -3551 -1400 C ATOM 7 SD MET A 28 8.299 10.450 7.910 1.00187.16 S ANISOU 7 SD MET A 28 34399 22262 14453 -3145 -3734 -1640 S ATOM 8 CE MET A 28 8.650 11.788 6.773 1.00181.52 C ANISOU 8 CE MET A 28 33148 22053 13769 -2717 -3431 -1595 C ATOM 9 N PRO A 29 10.637 11.357 13.207 1.00166.77 N ANISOU 9 N PRO A 29 30905 19216 13245 -2392 -3249 -1259 N ATOM 10 CA PRO A 29 10.152 10.982 14.554 1.00166.12 C ANISOU 10 CA PRO A 29 30815 19008 13294 -2738 -3397 -1128 C ATOM 11 C PRO A 29 10.140 12.135 15.573 1.00166.31 C ANISOU 11 C PRO A 29 30145 19374 13671 -2664 -3212 -905 C ATOM 12 O PRO A 29 9.493 12.012 16.618 1.00165.51 O ANISOU 12 O PRO A 29 29925 19304 13657 -3011 -3333 -758 O ATOM 13 CB PRO A 29 11.096 9.851 14.971 1.00169.76 C ANISOU 13 CB PRO A 29 31881 18889 13730 -2491 -3456 -1311 C ATOM 14 CG PRO A 29 12.363 10.136 14.256 1.00173.76 C ANISOU 14 CG PRO A 29 32402 19357 14261 -1847 -3211 -1472 C ATOM 15 CD PRO A 29 12.018 10.869 12.983 1.00169.25 C ANISOU 15 CD PRO A 29 31581 19170 13555 -1834 -3124 -1472 C ATOM 16 N LEU A 30 10.838 13.258 15.255 1.00160.14 N ANISOU 16 N LEU A 30 28921 18854 13072 -2226 -2927 -879 N ATOM 17 CA LEU A 30 10.970 14.469 16.081 1.00155.69 C ANISOU 17 CA LEU A 30 27726 18596 12833 -2086 -2728 -692 C ATOM 18 C LEU A 30 9.813 15.479 15.910 1.00158.03 C ANISOU 18 C LEU A 30 27517 19399 13127 -2367 -2727 -487 C ATOM 19 O LEU A 30 9.953 16.653 16.263 1.00153.82 O ANISOU 19 O LEU A 30 26475 19147 12822 -2181 -2535 -351 O ATOM 20 CB LEU A 30 12.333 15.141 15.822 1.00153.72 C ANISOU 20 CB LEU A 30 27296 18353 12757 -1502 -2437 -760 C ATOM 21 CG LEU A 30 13.548 14.439 16.417 1.00158.57 C ANISOU 21 CG LEU A 30 28209 18576 13465 -1159 -2386 -896 C ATOM 22 CD1 LEU A 30 14.698 14.421 15.438 1.00159.80 C ANISOU 22 CD1 LEU A 30 28514 18671 13533 -667 -2214 -1065 C ATOM 23 CD2 LEU A 30 13.961 15.077 17.730 1.00157.08 C ANISOU 23 CD2 LEU A 30 27619 18454 13609 -1047 -2260 -763 C ATOM 24 N VAL A 31 8.668 15.010 15.391 1.00158.07 N ANISOU 24 N VAL A 31 27677 19522 12860 -2815 -2950 -463 N ATOM 25 CA VAL A 31 7.459 15.813 15.195 1.00157.79 C ANISOU 25 CA VAL A 31 27198 19994 12760 -3105 -2986 -268 C ATOM 26 C VAL A 31 6.764 15.974 16.560 1.00160.95 C ANISOU 26 C VAL A 31 27302 20546 13307 -3387 -3062 -76 C ATOM 27 O VAL A 31 6.453 17.099 16.964 1.00157.64 O ANISOU 27 O VAL A 31 26351 20495 13051 -3299 -2930 95 O ATOM 28 CB VAL A 31 6.531 15.182 14.108 1.00165.62 C ANISOU 28 CB VAL A 31 28472 21082 13373 -3489 -3208 -319 C ATOM 29 CG1 VAL A 31 5.138 15.810 14.107 1.00165.39 C ANISOU 29 CG1 VAL A 31 27999 21600 13242 -3865 -3298 -97 C ATOM 30 CG2 VAL A 31 7.159 15.284 12.720 1.00166.59 C ANISOU 30 CG2 VAL A 31 28778 21161 13356 -3167 -3097 -483 C ATOM 31 N VAL A 32 6.555 14.840 17.269 1.00160.18 N ANISOU 31 N VAL A 32 27572 20148 13140 -3707 -3274 -107 N ATOM 32 CA VAL A 32 5.896 14.762 18.582 1.00159.49 C ANISOU 32 CA VAL A 32 27282 20171 13148 -4023 -3379 67 C ATOM 33 C VAL A 32 6.879 14.913 19.769 1.00160.96 C ANISOU 33 C VAL A 32 27391 20110 13657 -3698 -3232 62 C ATOM 34 O VAL A 32 6.440 15.210 20.886 1.00159.30 O ANISOU 34 O VAL A 32 26872 20074 13580 -3844 -3246 224 O ATOM 35 CB VAL A 32 4.969 13.517 18.738 1.00167.17 C ANISOU 35 CB VAL A 32 28650 21024 13843 -4634 -3708 85 C ATOM 36 CG1 VAL A 32 3.693 13.880 19.494 1.00166.70 C ANISOU 36 CG1 VAL A 32 28142 21449 13747 -5064 -3815 339 C ATOM 37 CG2 VAL A 32 4.630 12.879 17.389 1.00170.56 C ANISOU 37 CG2 VAL A 32 29485 21385 13935 -4840 -3864 -48 C ATOM 38 N VAL A 33 8.200 14.717 19.523 1.00156.78 N ANISOU 38 N VAL A 33 27125 19211 13235 -3250 -3091 -119 N ATOM 39 CA VAL A 33 9.273 14.844 20.524 1.00154.03 C ANISOU 39 CA VAL A 33 26717 18635 13172 -2898 -2942 -143 C ATOM 40 C VAL A 33 9.320 16.285 21.055 1.00153.23 C ANISOU 40 C VAL A 33 25975 18909 13335 -2687 -2724 12 C ATOM 41 O VAL A 33 9.333 16.486 22.270 1.00150.88 O ANISOU 41 O VAL A 33 25468 18632 13227 -2708 -2706 113 O ATOM 42 CB VAL A 33 10.643 14.350 19.975 1.00158.74 C ANISOU 42 CB VAL A 33 27706 18837 13772 -2447 -2836 -366 C ATOM 43 CG1 VAL A 33 11.797 14.707 20.910 1.00155.83 C ANISOU 43 CG1 VAL A 33 27164 18345 13699 -2041 -2646 -372 C ATOM 44 CG2 VAL A 33 10.615 12.848 19.717 1.00162.58 C ANISOU 44 CG2 VAL A 33 28889 18879 14006 -2638 -3071 -520 C ATOM 45 N LEU A 34 9.287 17.273 20.144 1.00148.41 N ANISOU 45 N LEU A 34 25081 18591 12718 -2505 -2574 36 N ATOM 46 CA LEU A 34 9.276 18.695 20.487 1.00144.95 C ANISOU 46 CA LEU A 34 24088 18493 12493 -2307 -2378 180 C ATOM 47 C LEU A 34 7.892 19.116 21.004 1.00148.36 C ANISOU 47 C LEU A 34 24181 19321 12870 -2659 -2489 381 C ATOM 48 O LEU A 34 7.800 20.068 21.781 1.00145.59 O ANISOU 48 O LEU A 34 23425 19182 12709 -2544 -2377 509 O ATOM 49 CB LEU A 34 9.686 19.559 19.278 1.00144.44 C ANISOU 49 CB LEU A 34 23886 18588 12407 -2009 -2195 147 C ATOM 50 CG LEU A 34 11.032 19.249 18.594 1.00149.61 C ANISOU 50 CG LEU A 34 24819 18952 13074 -1635 -2065 -40 C ATOM 51 CD1 LEU A 34 11.084 19.843 17.204 1.00150.18 C ANISOU 51 CD1 LEU A 34 24826 19222 13015 -1482 -1956 -62 C ATOM 52 CD2 LEU A 34 12.215 19.750 19.410 1.00149.84 C ANISOU 52 CD2 LEU A 34 24673 18864 13393 -1284 -1870 -45 C ATOM 53 N SER A 35 6.822 18.403 20.576 1.00147.44 N ANISOU 53 N SER A 35 24232 19316 12473 -3085 -2714 410 N ATOM 54 CA SER A 35 5.433 18.657 20.984 1.00147.53 C ANISOU 54 CA SER A 35 23928 19761 12367 -3458 -2844 607 C ATOM 55 C SER A 35 5.159 18.241 22.434 1.00150.49 C ANISOU 55 C SER A 35 24251 20092 12837 -3677 -2944 702 C ATOM 56 O SER A 35 4.441 18.957 23.130 1.00149.03 O ANISOU 56 O SER A 35 23637 20289 12699 -3742 -2925 878 O ATOM 57 CB SER A 35 4.446 17.981 20.035 1.00154.06 C ANISOU 57 CB SER A 35 24955 20737 12842 -3870 -3060 607 C ATOM 58 OG SER A 35 4.218 18.763 18.874 1.00161.28 O ANISOU 58 OG SER A 35 25684 21942 13654 -3718 -2966 620 O ATOM 59 N THR A 36 5.722 17.093 22.887 1.00147.61 N ANISOU 59 N THR A 36 24330 19272 12484 -3771 -3052 591 N ATOM 60 CA THR A 36 5.580 16.593 24.266 1.00147.01 C ANISOU 60 CA THR A 36 24263 19099 12495 -3971 -3149 674 C ATOM 61 C THR A 36 6.299 17.529 25.249 1.00146.70 C ANISOU 61 C THR A 36 23870 19088 12783 -3580 -2932 715 C ATOM 62 O THR A 36 5.812 17.745 26.362 1.00145.38 O ANISOU 62 O THR A 36 23434 19116 12689 -3713 -2961 858 O ATOM 63 CB THR A 36 6.029 15.124 24.392 1.00157.69 C ANISOU 63 CB THR A 36 26236 19924 13754 -4144 -3323 541 C ATOM 64 OG1 THR A 36 7.267 14.931 23.704 1.00157.78 O ANISOU 64 OG1 THR A 36 26569 19548 13831 -3730 -3201 331 O ATOM 65 CG2 THR A 36 4.984 14.142 23.874 1.00159.86 C ANISOU 65 CG2 THR A 36 26826 20224 13688 -4706 -3605 567 C ATOM 66 N ILE A 37 7.446 18.103 24.807 1.00140.81 N ANISOU 66 N ILE A 37 23118 18172 12212 -3110 -2718 593 N ATOM 67 CA ILE A 37 8.267 19.085 25.526 1.00136.96 C ANISOU 67 CA ILE A 37 22317 17699 12023 -2720 -2497 610 C ATOM 68 C ILE A 37 7.414 20.356 25.744 1.00138.39 C ANISOU 68 C ILE A 37 21974 18368 12239 -2717 -2421 786 C ATOM 69 O ILE A 37 7.401 20.910 26.842 1.00136.47 O ANISOU 69 O ILE A 37 21452 18236 12164 -2642 -2362 876 O ATOM 70 CB ILE A 37 9.598 19.340 24.742 1.00139.15 C ANISOU 70 CB ILE A 37 22730 17734 12407 -2285 -2308 448 C ATOM 71 CG1 ILE A 37 10.589 18.166 24.945 1.00140.59 C ANISOU 71 CG1 ILE A 37 23376 17441 12601 -2186 -2358 288 C ATOM 72 CG2 ILE A 37 10.250 20.686 25.103 1.00137.06 C ANISOU 72 CG2 ILE A 37 22067 17611 12401 -1923 -2070 495 C ATOM 73 CD1 ILE A 37 11.785 18.103 23.967 1.00146.78 C ANISOU 73 CD1 ILE A 37 24374 18009 13386 -1802 -2216 113 C ATOM 74 N CYS A 38 6.673 20.773 24.703 1.00134.88 N ANISOU 74 N CYS A 38 21418 18217 11614 -2793 -2435 832 N ATOM 75 CA CYS A 38 5.755 21.913 24.710 1.00133.30 C ANISOU 75 CA CYS A 38 20766 18501 11382 -2777 -2382 998 C ATOM 76 C CYS A 38 4.576 21.646 25.672 1.00136.28 C ANISOU 76 C CYS A 38 20946 19185 11648 -3133 -2547 1162 C ATOM 77 O CYS A 38 4.161 22.557 26.395 1.00134.06 O ANISOU 77 O CYS A 38 20280 19207 11448 -3020 -2473 1290 O ATOM 78 CB CYS A 38 5.275 22.198 23.286 1.00135.08 C ANISOU 78 CB CYS A 38 20986 18938 11399 -2792 -2385 999 C ATOM 79 SG CYS A 38 3.865 23.331 23.169 1.00139.12 S ANISOU 79 SG CYS A 38 20996 20098 11766 -2839 -2385 1220 S ATOM 80 N LEU A 39 4.066 20.391 25.683 1.00134.43 N ANISOU 80 N LEU A 39 20995 18868 11216 -3561 -2771 1157 N ATOM 81 CA LEU A 39 2.940 19.935 26.509 1.00135.28 C ANISOU 81 CA LEU A 39 20961 19269 11168 -3984 -2956 1320 C ATOM 82 C LEU A 39 3.207 19.994 28.008 1.00136.54 C ANISOU 82 C LEU A 39 20985 19367 11528 -3925 -2923 1378 C ATOM 83 O LEU A 39 2.277 20.255 28.775 1.00136.16 O ANISOU 83 O LEU A 39 20605 19726 11403 -4101 -2981 1550 O ATOM 84 CB LEU A 39 2.483 18.526 26.104 1.00138.65 C ANISOU 84 CB LEU A 39 21803 19541 11335 -4479 -3211 1288 C ATOM 85 CG LEU A 39 1.719 18.409 24.787 1.00145.67 C ANISOU 85 CG LEU A 39 22743 20672 11934 -4702 -3315 1293 C ATOM 86 CD1 LEU A 39 1.798 17.001 24.244 1.00149.13 C ANISOU 86 CD1 LEU A 39 23756 20729 12177 -5060 -3526 1172 C ATOM 87 CD2 LEU A 39 0.267 18.863 24.930 1.00148.97 C ANISOU 87 CD2 LEU A 39 22705 21761 12134 -4985 -3406 1520 C ATOM 88 N VAL A 40 4.458 19.730 28.431 1.00131.22 N ANISOU 88 N VAL A 40 20554 18217 11086 -3677 -2833 1240 N ATOM 89 CA VAL A 40 4.830 19.807 29.847 1.00129.31 C ANISOU 89 CA VAL A 40 20193 17896 11044 -3588 -2791 1282 C ATOM 90 C VAL A 40 4.985 21.264 30.295 1.00130.13 C ANISOU 90 C VAL A 40 19853 18248 11341 -3207 -2584 1337 C ATOM 91 O VAL A 40 4.491 21.623 31.361 1.00128.69 O ANISOU 91 O VAL A 40 19383 18321 11192 -3244 -2590 1460 O ATOM 92 CB VAL A 40 5.998 18.881 30.296 1.00133.10 C ANISOU 92 CB VAL A 40 21085 17819 11667 -3506 -2803 1140 C ATOM 93 CG1 VAL A 40 5.506 17.463 30.550 1.00136.04 C ANISOU 93 CG1 VAL A 40 21824 18022 11843 -3973 -3054 1168 C ATOM 94 CG2 VAL A 40 7.156 18.883 29.307 1.00132.25 C ANISOU 94 CG2 VAL A 40 21246 17359 11644 -3171 -2678 947 C ATOM 95 N THR A 41 5.593 22.110 29.437 1.00125.70 N ANISOU 95 N THR A 41 19249 17635 10877 -2859 -2411 1254 N ATOM 96 CA THR A 41 5.823 23.544 29.661 1.00123.34 C ANISOU 96 CA THR A 41 18606 17510 10749 -2489 -2215 1292 C ATOM 97 C THR A 41 4.526 24.337 29.883 1.00127.71 C ANISOU 97 C THR A 41 18762 18603 11160 -2549 -2240 1471 C ATOM 98 O THR A 41 4.534 25.298 30.654 1.00125.54 O ANISOU 98 O THR A 41 18214 18474 11013 -2315 -2132 1528 O ATOM 99 CB THR A 41 6.651 24.141 28.513 1.00131.76 C ANISOU 99 CB THR A 41 19760 18413 11890 -2184 -2056 1183 C ATOM 100 OG1 THR A 41 7.660 23.214 28.121 1.00132.93 O ANISOU 100 OG1 THR A 41 20291 18134 12081 -2165 -2065 1024 O ATOM 101 CG2 THR A 41 7.303 25.461 28.884 1.00127.99 C ANISOU 101 CG2 THR A 41 19050 17941 11642 -1802 -1851 1189 C ATOM 102 N VAL A 42 3.425 23.949 29.209 1.00126.90 N ANISOU 102 N VAL A 42 18630 18810 10777 -2849 -2382 1557 N ATOM 103 CA VAL A 42 2.129 24.629 29.360 1.00127.69 C ANISOU 103 CA VAL A 42 18333 19490 10693 -2903 -2417 1739 C ATOM 104 C VAL A 42 1.498 24.404 30.751 1.00132.23 C ANISOU 104 C VAL A 42 18695 20310 11236 -3084 -2505 1866 C ATOM 105 O VAL A 42 0.733 25.246 31.219 1.00131.90 O ANISOU 105 O VAL A 42 18280 20711 11126 -2960 -2467 1999 O ATOM 106 CB VAL A 42 1.122 24.399 28.190 1.00133.91 C ANISOU 106 CB VAL A 42 19095 20616 11170 -3151 -2535 1808 C ATOM 107 CG1 VAL A 42 1.663 24.938 26.871 1.00133.00 C ANISOU 107 CG1 VAL A 42 19097 20352 11083 -2889 -2414 1710 C ATOM 108 CG2 VAL A 42 0.709 22.934 28.056 1.00136.33 C ANISOU 108 CG2 VAL A 42 19674 20849 11276 -3672 -2766 1805 C ATOM 109 N GLY A 43 1.847 23.282 31.386 1.00129.03 N ANISOU 109 N GLY A 43 18542 19613 10871 -3349 -2617 1824 N ATOM 110 CA GLY A 43 1.356 22.892 32.704 1.00129.15 C ANISOU 110 CA GLY A 43 18411 19806 10854 -3564 -2713 1942 C ATOM 111 C GLY A 43 2.314 23.160 33.849 1.00130.11 C ANISOU 111 C GLY A 43 18536 19638 11261 -3295 -2598 1876 C ATOM 112 O GLY A 43 1.892 23.677 34.885 1.00129.43 O ANISOU 112 O GLY A 43 18145 19845 11189 -3221 -2571 1980 O ATOM 113 N LEU A 44 3.607 22.788 33.684 1.00124.42 N ANISOU 113 N LEU A 44 18157 18367 10751 -3145 -2533 1703 N ATOM 114 CA LEU A 44 4.651 22.971 34.702 1.00121.38 C ANISOU 114 CA LEU A 44 17802 17683 10636 -2895 -2428 1627 C ATOM 115 C LEU A 44 4.807 24.429 35.102 1.00122.77 C ANISOU 115 C LEU A 44 17648 18040 10961 -2498 -2246 1642 C ATOM 116 O LEU A 44 4.880 24.712 36.290 1.00121.11 O ANISOU 116 O LEU A 44 17275 17892 10849 -2414 -2218 1680 O ATOM 117 CB LEU A 44 6.003 22.373 34.268 1.00120.51 C ANISOU 117 CB LEU A 44 18088 17013 10686 -2768 -2382 1443 C ATOM 118 CG LEU A 44 6.113 20.844 34.160 1.00126.85 C ANISOU 118 CG LEU A 44 19312 17507 11380 -3095 -2561 1400 C ATOM 119 CD1 LEU A 44 7.417 20.446 33.500 1.00126.39 C ANISOU 119 CD1 LEU A 44 19616 16962 11446 -2869 -2487 1210 C ATOM 120 CD2 LEU A 44 5.986 20.160 35.518 1.00129.25 C ANISOU 120 CD2 LEU A 44 19637 17774 11700 -3299 -2670 1479 C ATOM 121 N ASN A 45 4.807 25.352 34.125 1.00119.21 N ANISOU 121 N ASN A 45 17112 17675 10506 -2266 -2133 1618 N ATOM 122 CA ASN A 45 4.885 26.792 34.385 1.00117.69 C ANISOU 122 CA ASN A 45 16657 17635 10424 -1894 -1973 1638 C ATOM 123 C ASN A 45 3.569 27.315 34.965 1.00122.89 C ANISOU 123 C ASN A 45 16960 18834 10898 -1925 -2022 1806 C ATOM 124 O ASN A 45 3.584 28.266 35.746 1.00121.82 O ANISOU 124 O ASN A 45 16623 18812 10850 -1657 -1928 1830 O ATOM 125 CB ASN A 45 5.258 27.568 33.122 1.00118.15 C ANISOU 125 CB ASN A 45 16768 17613 10511 -1658 -1850 1579 C ATOM 126 CG ASN A 45 6.741 27.761 32.947 1.00140.41 C ANISOU 126 CG ASN A 45 19787 19980 13580 -1431 -1714 1429 C ATOM 127 OD1 ASN A 45 7.398 28.478 33.710 1.00132.68 O ANISOU 127 OD1 ASN A 45 18729 18888 12794 -1203 -1607 1397 O ATOM 128 ND2 ASN A 45 7.300 27.143 31.922 1.00133.55 N ANISOU 128 ND2 ASN A 45 19177 18870 12696 -1488 -1717 1335 N ATOM 129 N LEU A 46 2.438 26.683 34.588 1.00121.24 N ANISOU 129 N LEU A 46 16678 18971 10415 -2253 -2173 1922 N ATOM 130 CA LEU A 46 1.093 27.017 35.060 1.00122.38 C ANISOU 130 CA LEU A 46 16460 19715 10325 -2326 -2239 2102 C ATOM 131 C LEU A 46 0.926 26.577 36.529 1.00126.79 C ANISOU 131 C LEU A 46 16907 20368 10899 -2466 -2305 2168 C ATOM 132 O LEU A 46 0.243 27.255 37.305 1.00126.84 O ANISOU 132 O LEU A 46 16590 20785 10821 -2321 -2279 2275 O ATOM 133 CB LEU A 46 0.060 26.317 34.161 1.00124.85 C ANISOU 133 CB LEU A 46 16755 20350 10333 -2700 -2396 2203 C ATOM 134 CG LEU A 46 -1.331 26.927 34.045 1.00131.08 C ANISOU 134 CG LEU A 46 17144 21827 10833 -2687 -2431 2386 C ATOM 135 CD1 LEU A 46 -1.311 28.228 33.252 1.00130.17 C ANISOU 135 CD1 LEU A 46 16922 21799 10737 -2246 -2279 2367 C ATOM 136 CD2 LEU A 46 -2.272 25.952 33.374 1.00136.64 C ANISOU 136 CD2 LEU A 46 17853 22829 11233 -3177 -2625 2488 C ATOM 137 N LEU A 47 1.582 25.449 36.899 1.00123.10 N ANISOU 137 N LEU A 47 16726 19515 10532 -2721 -2387 2101 N ATOM 138 CA LEU A 47 1.605 24.848 38.239 1.00122.93 C ANISOU 138 CA LEU A 47 16680 19486 10544 -2887 -2460 2153 C ATOM 139 C LEU A 47 2.282 25.786 39.247 1.00125.17 C ANISOU 139 C LEU A 47 16832 19671 11055 -2487 -2307 2092 C ATOM 140 O LEU A 47 1.787 25.929 40.365 1.00125.48 O ANISOU 140 O LEU A 47 16635 20004 11036 -2495 -2330 2190 O ATOM 141 CB LEU A 47 2.289 23.452 38.174 1.00123.33 C ANISOU 141 CB LEU A 47 17148 19058 10652 -3197 -2575 2074 C ATOM 142 CG LEU A 47 3.292 23.022 39.262 1.00126.33 C ANISOU 142 CG LEU A 47 17696 19050 11254 -3132 -2555 1999 C ATOM 143 CD1 LEU A 47 2.584 22.448 40.475 1.00127.90 C ANISOU 143 CD1 LEU A 47 17752 19520 11325 -3423 -2682 2156 C ATOM 144 CD2 LEU A 47 4.266 21.997 38.714 1.00128.20 C ANISOU 144 CD2 LEU A 47 18399 18726 11584 -3230 -2602 1860 C ATOM 145 N VAL A 48 3.405 26.421 38.834 1.00119.57 N ANISOU 145 N VAL A 48 16277 18568 10587 -2155 -2158 1934 N ATOM 146 CA VAL A 48 4.194 27.386 39.608 1.00117.07 C ANISOU 146 CA VAL A 48 15887 18097 10496 -1782 -2011 1854 C ATOM 147 C VAL A 48 3.303 28.613 39.873 1.00120.66 C ANISOU 147 C VAL A 48 16006 19006 10831 -1529 -1948 1948 C ATOM 148 O VAL A 48 3.236 29.085 41.008 1.00119.73 O ANISOU 148 O VAL A 48 15723 19020 10750 -1377 -1916 1970 O ATOM 149 CB VAL A 48 5.512 27.769 38.860 1.00119.19 C ANISOU 149 CB VAL A 48 16393 17894 10999 -1545 -1879 1687 C ATOM 150 CG1 VAL A 48 6.295 28.850 39.603 1.00117.15 C ANISOU 150 CG1 VAL A 48 16059 17499 10954 -1196 -1737 1613 C ATOM 151 CG2 VAL A 48 6.397 26.550 38.615 1.00118.92 C ANISOU 151 CG2 VAL A 48 16690 17438 11056 -1735 -1937 1591 C ATOM 152 N LEU A 49 2.594 29.087 38.824 1.00117.72 N ANISOU 152 N LEU A 49 15545 18886 10295 -1476 -1938 2004 N ATOM 153 CA LEU A 49 1.678 30.229 38.867 1.00118.03 C ANISOU 153 CA LEU A 49 15294 19375 10178 -1202 -1884 2100 C ATOM 154 C LEU A 49 0.471 29.991 39.781 1.00124.09 C ANISOU 154 C LEU A 49 15745 20704 10700 -1341 -1984 2265 C ATOM 155 O LEU A 49 0.000 30.935 40.414 1.00124.00 O ANISOU 155 O LEU A 49 15501 20996 10618 -1037 -1923 2314 O ATOM 156 CB LEU A 49 1.229 30.627 37.450 1.00118.76 C ANISOU 156 CB LEU A 49 15387 19601 10135 -1141 -1864 2130 C ATOM 157 CG LEU A 49 2.292 31.295 36.575 1.00121.30 C ANISOU 157 CG LEU A 49 15944 19477 10667 -891 -1728 1994 C ATOM 158 CD1 LEU A 49 1.995 31.096 35.104 1.00122.34 C ANISOU 158 CD1 LEU A 49 16158 19660 10667 -997 -1753 2013 C ATOM 159 CD2 LEU A 49 2.432 32.773 36.901 1.00122.76 C ANISOU 159 CD2 LEU A 49 16045 19671 10928 -442 -1591 1978 C ATOM 160 N TYR A 50 -0.011 28.738 39.867 1.00122.51 N ANISOU 160 N TYR A 50 15551 20641 10356 -1798 -2141 2353 N ATOM 161 CA TYR A 50 -1.126 28.370 40.742 1.00124.70 C ANISOU 161 CA TYR A 50 15525 21471 10384 -2007 -2250 2530 C ATOM 162 C TYR A 50 -0.635 28.245 42.191 1.00126.16 C ANISOU 162 C TYR A 50 15696 21527 10711 -1963 -2235 2504 C ATOM 163 O TYR A 50 -1.303 28.731 43.105 1.00126.16 O ANISOU 163 O TYR A 50 15396 21962 10579 -1820 -2222 2600 O ATOM 164 CB TYR A 50 -1.783 27.059 40.267 1.00128.88 C ANISOU 164 CB TYR A 50 16106 22164 10700 -2565 -2437 2642 C ATOM 165 CG TYR A 50 -3.111 26.743 40.929 1.00134.38 C ANISOU 165 CG TYR A 50 16437 23549 11071 -2825 -2557 2864 C ATOM 166 CD1 TYR A 50 -4.305 27.246 40.417 1.00138.81 C ANISOU 166 CD1 TYR A 50 16663 24748 11331 -2781 -2577 3010 C ATOM 167 CD2 TYR A 50 -3.180 25.899 42.034 1.00135.98 C ANISOU 167 CD2 TYR A 50 16625 23792 11247 -3131 -2657 2942 C ATOM 168 CE1 TYR A 50 -5.533 26.942 41.009 1.00142.59 C ANISOU 168 CE1 TYR A 50 16769 25926 11481 -3030 -2687 3230 C ATOM 169 CE2 TYR A 50 -4.400 25.587 42.634 1.00139.79 C ANISOU 169 CE2 TYR A 50 16756 24947 11412 -3402 -2768 3165 C ATOM 170 CZ TYR A 50 -5.576 26.109 42.117 1.00150.04 C ANISOU 170 CZ TYR A 50 17695 26910 12404 -3355 -2783 3309 C ATOM 171 OH TYR A 50 -6.784 25.800 42.699 1.00154.50 O ANISOU 171 OH TYR A 50 17874 28200 12627 -3628 -2891 3543 O ATOM 172 N ALA A 51 0.543 27.609 42.385 1.00120.66 N ANISOU 172 N ALA A 51 15321 20252 10271 -2059 -2233 2372 N ATOM 173 CA ALA A 51 1.189 27.371 43.678 1.00119.28 C ANISOU 173 CA ALA A 51 15187 19877 10255 -2036 -2224 2330 C ATOM 174 C ALA A 51 1.451 28.637 44.509 1.00122.30 C ANISOU 174 C ALA A 51 15405 20317 10744 -1577 -2085 2271 C ATOM 175 O ALA A 51 1.406 28.562 45.737 1.00122.20 O ANISOU 175 O ALA A 51 15272 20430 10730 -1568 -2100 2307 O ATOM 176 CB ALA A 51 2.483 26.592 43.485 1.00118.39 C ANISOU 176 CB ALA A 51 15465 19127 10393 -2142 -2228 2185 C ATOM 177 N VAL A 52 1.726 29.785 43.853 1.00118.00 N ANISOU 177 N VAL A 52 14881 19671 10282 -1207 -1956 2182 N ATOM 178 CA VAL A 52 1.990 31.066 44.524 1.00116.83 C ANISOU 178 CA VAL A 52 14643 19524 10224 -765 -1831 2112 C ATOM 179 C VAL A 52 0.691 31.670 45.068 1.00123.59 C ANISOU 179 C VAL A 52 15145 21017 10795 -600 -1843 2253 C ATOM 180 O VAL A 52 0.657 32.093 46.221 1.00123.09 O ANISOU 180 O VAL A 52 14958 21084 10728 -413 -1815 2247 O ATOM 181 CB VAL A 52 2.804 32.057 43.639 1.00118.81 C ANISOU 181 CB VAL A 52 15088 19396 10658 -457 -1700 1976 C ATOM 182 CG1 VAL A 52 2.882 33.450 44.263 1.00118.19 C ANISOU 182 CG1 VAL A 52 14940 19353 10615 -16 -1592 1922 C ATOM 183 CG2 VAL A 52 4.205 31.522 43.362 1.00116.56 C ANISOU 183 CG2 VAL A 52 15110 18525 10653 -570 -1672 1833 C ATOM 184 N ARG A 53 -0.371 31.689 44.252 1.00123.02 N ANISOU 184 N ARG A 53 14906 21367 10470 -661 -1887 2379 N ATOM 185 CA ARG A 53 -1.665 32.251 44.645 1.00125.78 C ANISOU 185 CA ARG A 53 14889 22396 10506 -480 -1898 2529 C ATOM 186 C ARG A 53 -2.392 31.393 45.679 1.00132.23 C ANISOU 186 C ARG A 53 15456 23656 11130 -785 -2012 2679 C ATOM 187 O ARG A 53 -3.091 31.950 46.531 1.00133.23 O ANISOU 187 O ARG A 53 15298 24251 11070 -548 -1990 2757 O ATOM 188 CB ARG A 53 -2.584 32.487 43.426 1.00128.68 C ANISOU 188 CB ARG A 53 15128 23127 10638 -466 -1917 2633 C ATOM 189 CG ARG A 53 -1.913 33.038 42.161 1.00142.23 C ANISOU 189 CG ARG A 53 17112 24408 12519 -296 -1833 2515 C ATOM 190 CD ARG A 53 -1.332 34.440 42.298 1.00157.39 C ANISOU 190 CD ARG A 53 19151 26060 14591 231 -1685 2392 C ATOM 191 NE ARG A 53 -0.862 34.946 41.007 1.00168.85 N ANISOU 191 NE ARG A 53 20822 27190 16145 355 -1616 2323 N ATOM 192 CZ ARG A 53 0.359 34.752 40.517 1.00181.86 C ANISOU 192 CZ ARG A 53 22782 28241 18075 260 -1570 2184 C ATOM 193 NH1 ARG A 53 1.259 34.066 41.212 1.00167.87 N ANISOU 193 NH1 ARG A 53 21147 26117 16518 60 -1587 2093 N ATOM 194 NH2 ARG A 53 0.690 35.242 39.330 1.00169.29 N ANISOU 194 NH2 ARG A 53 21356 26428 16537 376 -1506 2143 N ATOM 195 N SER A 54 -2.239 30.048 45.598 1.00129.52 N ANISOU 195 N SER A 54 15231 23169 10810 -1301 -2135 2725 N ATOM 196 CA SER A 54 -2.896 29.077 46.490 1.00131.31 C ANISOU 196 CA SER A 54 15269 23774 10849 -1686 -2265 2889 C ATOM 197 C SER A 54 -2.347 29.014 47.931 1.00133.76 C ANISOU 197 C SER A 54 15581 23950 11290 -1611 -2242 2846 C ATOM 198 O SER A 54 -3.133 28.964 48.885 1.00134.60 O ANISOU 198 O SER A 54 15383 24580 11178 -1643 -2281 2987 O ATOM 199 CB SER A 54 -2.939 27.686 45.855 1.00136.05 C ANISOU 199 CB SER A 54 16055 24227 11410 -2268 -2418 2954 C ATOM 200 OG SER A 54 -1.654 27.189 45.517 1.00142.60 O ANISOU 200 OG SER A 54 17310 24320 12552 -2343 -2405 2781 O ATOM 201 N GLU A 55 -1.008 29.015 48.080 1.00127.68 N ANISOU 201 N GLU A 55 15137 22518 10859 -1510 -2180 2659 N ATOM 202 CA GLU A 55 -0.325 28.928 49.371 1.00126.12 C ANISOU 202 CA GLU A 55 14981 22124 10813 -1443 -2160 2597 C ATOM 203 C GLU A 55 0.047 30.296 49.947 1.00128.31 C ANISOU 203 C GLU A 55 15204 22358 11191 -905 -2017 2469 C ATOM 204 O GLU A 55 0.583 31.145 49.232 1.00126.38 O ANISOU 204 O GLU A 55 15114 21810 11094 -616 -1917 2336 O ATOM 205 CB GLU A 55 0.918 28.017 49.257 1.00125.67 C ANISOU 205 CB GLU A 55 15304 21409 11036 -1673 -2193 2482 C ATOM 206 CG GLU A 55 1.458 27.505 50.583 1.00137.16 C ANISOU 206 CG GLU A 55 16794 22732 12589 -1753 -2224 2476 C ATOM 207 CD GLU A 55 0.459 26.753 51.441 1.00166.02 C ANISOU 207 CD GLU A 55 20211 26891 15979 -2074 -2347 2690 C ATOM 208 OE1 GLU A 55 0.084 25.620 51.062 1.00168.38 O ANISOU 208 OE1 GLU A 55 20600 27213 16164 -2532 -2483 2810 O ATOM 209 OE2 GLU A 55 0.031 27.309 52.478 1.00162.28 O ANISOU 209 OE2 GLU A 55 19466 26799 15393 -1874 -2310 2740 O ATOM 210 N ARG A 56 -0.232 30.495 51.248 1.00125.69 N ANISOU 210 N ARG A 56 14669 22320 10765 -787 -2015 2513 N ATOM 211 CA ARG A 56 0.117 31.725 51.963 1.00124.77 C ANISOU 211 CA ARG A 56 14531 22155 10722 -298 -1899 2385 C ATOM 212 C ARG A 56 1.619 31.721 52.299 1.00126.21 C ANISOU 212 C ARG A 56 15024 21673 11256 -256 -1852 2194 C ATOM 213 O ARG A 56 2.230 32.791 52.393 1.00124.60 O ANISOU 213 O ARG A 56 14934 21216 11191 109 -1751 2041 O ATOM 214 CB ARG A 56 -0.730 31.896 53.238 1.00126.51 C ANISOU 214 CB ARG A 56 14422 22955 10690 -183 -1917 2497 C ATOM 215 CG ARG A 56 -0.910 33.363 53.623 1.00135.08 C ANISOU 215 CG ARG A 56 15432 24189 11706 392 -1805 2402 C ATOM 216 CD ARG A 56 -1.473 33.566 55.017 1.00141.18 C ANISOU 216 CD ARG A 56 15936 25435 12270 560 -1809 2464 C ATOM 217 NE ARG A 56 -1.869 34.963 55.220 1.00147.33 N ANISOU 217 NE ARG A 56 16646 26423 12908 1135 -1713 2390 N ATOM 218 CZ ARG A 56 -1.121 35.888 55.815 1.00158.28 C ANISOU 218 CZ ARG A 56 18230 27465 14445 1501 -1638 2199 C ATOM 219 NH1 ARG A 56 0.073 35.576 56.304 1.00141.21 N ANISOU 219 NH1 ARG A 56 16302 24775 12578 1350 -1641 2069 N ATOM 220 NH2 ARG A 56 -1.568 37.131 55.938 1.00145.13 N ANISOU 220 NH2 ARG A 56 16539 25986 12616 2025 -1565 2139 N ATOM 221 N LYS A 57 2.205 30.504 52.459 1.00122.03 N ANISOU 221 N LYS A 57 14643 20870 10854 -637 -1933 2210 N ATOM 222 CA LYS A 57 3.620 30.246 52.772 1.00119.50 C ANISOU 222 CA LYS A 57 14594 19971 10839 -651 -1908 2057 C ATOM 223 C LYS A 57 4.558 30.550 51.593 1.00122.05 C ANISOU 223 C LYS A 57 15192 19793 11391 -569 -1837 1911 C ATOM 224 O LYS A 57 5.772 30.677 51.794 1.00119.82 O ANISOU 224 O LYS A 57 15101 19073 11354 -482 -1787 1768 O ATOM 225 CB LYS A 57 3.817 28.796 53.256 1.00121.80 C ANISOU 225 CB LYS A 57 14962 20174 11143 -1064 -2027 2145 C ATOM 226 CG LYS A 57 3.279 28.532 54.663 1.00131.35 C ANISOU 226 CG LYS A 57 15943 21771 12193 -1125 -2082 2261 C ATOM 227 CD LYS A 57 3.637 27.137 55.181 1.00134.76 C ANISOU 227 CD LYS A 57 16510 22029 12663 -1514 -2199 2341 C ATOM 228 CE LYS A 57 4.976 27.070 55.882 1.00133.83 C ANISOU 228 CE LYS A 57 16587 21456 12808 -1395 -2163 2195 C ATOM 229 NZ LYS A 57 4.960 27.791 57.180 1.00139.48 N ANISOU 229 NZ LYS A 57 17105 22403 13488 -1138 -2115 2168 N ATOM 230 N LEU A 58 3.989 30.665 50.369 1.00119.52 N ANISOU 230 N LEU A 58 14871 19570 10971 -602 -1835 1957 N ATOM 231 CA LEU A 58 4.712 30.964 49.127 1.00118.02 C ANISOU 231 CA LEU A 58 14912 18981 10950 -532 -1768 1845 C ATOM 232 C LEU A 58 4.422 32.392 48.594 1.00121.34 C ANISOU 232 C LEU A 58 15283 19493 11328 -154 -1663 1800 C ATOM 233 O LEU A 58 4.705 32.677 47.428 1.00120.27 O ANISOU 233 O LEU A 58 15290 19146 11260 -111 -1614 1754 O ATOM 234 CB LEU A 58 4.421 29.883 48.063 1.00118.79 C ANISOU 234 CB LEU A 58 15111 19047 10977 -885 -1855 1920 C ATOM 235 CG LEU A 58 5.325 28.641 48.066 1.00122.82 C ANISOU 235 CG LEU A 58 15876 19149 11641 -1169 -1921 1876 C ATOM 236 CD1 LEU A 58 4.919 27.648 49.151 1.00124.02 C ANISOU 236 CD1 LEU A 58 15949 19489 11684 -1445 -2041 1995 C ATOM 237 CD2 LEU A 58 5.249 27.930 46.738 1.00126.09 C ANISOU 237 CD2 LEU A 58 16472 19421 12016 -1399 -1972 1889 C ATOM 238 N HIS A 59 3.905 33.295 49.473 1.00118.02 N ANISOU 238 N HIS A 59 14686 19365 10792 138 -1627 1811 N ATOM 239 CA HIS A 59 3.601 34.703 49.168 1.00117.89 C ANISOU 239 CA HIS A 59 14655 19427 10710 547 -1536 1768 C ATOM 240 C HIS A 59 4.825 35.615 49.383 1.00119.14 C ANISOU 240 C HIS A 59 15053 19097 11119 783 -1444 1586 C ATOM 241 O HIS A 59 4.665 36.819 49.606 1.00119.14 O ANISOU 241 O HIS A 59 15073 19129 11067 1139 -1382 1534 O ATOM 242 CB HIS A 59 2.410 35.200 50.014 1.00120.68 C ANISOU 242 CB HIS A 59 14722 20352 10778 772 -1550 1866 C ATOM 243 CG HIS A 59 1.063 34.747 49.542 1.00126.19 C ANISOU 243 CG HIS A 59 15156 21615 11175 638 -1618 2055 C ATOM 244 ND1 HIS A 59 -0.044 34.806 50.371 1.00130.12 N ANISOU 244 ND1 HIS A 59 15334 22721 11383 730 -1654 2184 N ATOM 245 CD2 HIS A 59 0.677 34.268 48.337 1.00128.31 C ANISOU 245 CD2 HIS A 59 15428 21948 11377 424 -1655 2136 C ATOM 246 CE1 HIS A 59 -1.056 34.347 49.654 1.00131.16 C ANISOU 246 CE1 HIS A 59 15271 23282 11282 547 -1715 2347 C ATOM 247 NE2 HIS A 59 -0.670 34.008 48.425 1.00130.64 N ANISOU 247 NE2 HIS A 59 15399 22897 11341 352 -1723 2320 N ATOM 248 N THR A 60 6.043 35.034 49.289 1.00113.09 N ANISOU 248 N THR A 60 14477 17886 10606 581 -1440 1494 N ATOM 249 CA THR A 60 7.341 35.697 49.469 1.00111.02 C ANISOU 249 CA THR A 60 14426 17169 10589 710 -1367 1335 C ATOM 250 C THR A 60 7.591 36.770 48.406 1.00114.60 C ANISOU 250 C THR A 60 15045 17408 11092 912 -1280 1280 C ATOM 251 O THR A 60 7.245 36.584 47.234 1.00114.25 O ANISOU 251 O THR A 60 15020 17397 10993 843 -1274 1340 O ATOM 252 CB THR A 60 8.486 34.654 49.481 1.00115.25 C ANISOU 252 CB THR A 60 15085 17366 11338 434 -1390 1280 C ATOM 253 OG1 THR A 60 8.066 33.468 50.162 1.00114.62 O ANISOU 253 OG1 THR A 60 14881 17496 11175 194 -1488 1372 O ATOM 254 CG2 THR A 60 9.779 35.191 50.109 1.00112.15 C ANISOU 254 CG2 THR A 60 14824 16625 11161 532 -1337 1136 C ATOM 255 N VAL A 61 8.207 37.889 48.832 1.00110.46 N ANISOU 255 N VAL A 61 14654 16654 10660 1146 -1219 1168 N ATOM 256 CA VAL A 61 8.588 39.030 47.988 1.00109.88 C ANISOU 256 CA VAL A 61 14786 16317 10645 1334 -1140 1112 C ATOM 257 C VAL A 61 9.587 38.602 46.896 1.00111.01 C ANISOU 257 C VAL A 61 15075 16125 10978 1120 -1101 1083 C ATOM 258 O VAL A 61 9.417 38.969 45.732 1.00111.16 O ANISOU 258 O VAL A 61 15176 16096 10965 1167 -1059 1119 O ATOM 259 CB VAL A 61 9.017 40.283 48.817 1.00114.24 C ANISOU 259 CB VAL A 61 15484 16686 11236 1594 -1106 1000 C ATOM 260 CG1 VAL A 61 9.522 39.906 50.211 1.00113.63 C ANISOU 260 CG1 VAL A 61 15342 16598 11234 1519 -1148 929 C ATOM 261 CG2 VAL A 61 10.018 41.171 48.075 1.00113.62 C ANISOU 261 CG2 VAL A 61 15679 16175 11318 1626 -1037 920 C ATOM 262 N GLY A 62 10.556 37.770 47.272 1.00105.05 N ANISOU 262 N GLY A 62 14337 15185 10394 901 -1118 1028 N ATOM 263 CA GLY A 62 11.551 37.213 46.362 1.00103.09 C ANISOU 263 CA GLY A 62 14202 14661 10305 714 -1084 997 C ATOM 264 C GLY A 62 10.974 36.172 45.420 1.00104.95 C ANISOU 264 C GLY A 62 14391 15034 10450 540 -1123 1084 C ATOM 265 O GLY A 62 11.641 35.783 44.459 1.00103.90 O ANISOU 265 O GLY A 62 14368 14702 10407 429 -1089 1062 O ATOM 266 N ASN A 63 9.729 35.707 45.695 1.00101.10 N ANISOU 266 N ASN A 63 13739 14908 9767 505 -1199 1186 N ATOM 267 CA ASN A 63 9.003 34.733 44.873 1.00100.82 C ANISOU 267 CA ASN A 63 13654 15051 9601 305 -1260 1282 C ATOM 268 C ASN A 63 8.174 35.396 43.755 1.00104.17 C ANISOU 268 C ASN A 63 14064 15642 9874 431 -1229 1350 C ATOM 269 O ASN A 63 7.681 34.698 42.866 1.00104.04 O ANISOU 269 O ASN A 63 14036 15741 9756 263 -1272 1418 O ATOM 270 CB ASN A 63 8.156 33.782 45.730 1.00102.19 C ANISOU 270 CB ASN A 63 13654 15542 9630 133 -1371 1375 C ATOM 271 CG ASN A 63 8.869 32.523 46.176 1.00125.40 C ANISOU 271 CG ASN A 63 16669 18295 12682 -120 -1433 1348 C ATOM 272 OD1 ASN A 63 9.886 32.102 45.609 1.00117.14 O ANISOU 272 OD1 ASN A 63 15799 16916 11790 -194 -1404 1272 O ATOM 273 ND2 ASN A 63 8.318 31.863 47.185 1.00119.29 N ANISOU 273 ND2 ASN A 63 15765 17750 11810 -250 -1522 1422 N ATOM 274 N LEU A 64 8.055 36.744 43.781 1.00100.16 N ANISOU 274 N LEU A 64 13584 15127 9345 727 -1159 1330 N ATOM 275 CA LEU A 64 7.373 37.532 42.746 1.00100.64 C ANISOU 275 CA LEU A 64 13661 15309 9268 904 -1119 1393 C ATOM 276 C LEU A 64 8.242 37.598 41.473 1.00103.58 C ANISOU 276 C LEU A 64 14229 15352 9773 835 -1052 1350 C ATOM 277 O LEU A 64 7.715 37.777 40.373 1.00104.06 O ANISOU 277 O LEU A 64 14300 15518 9718 871 -1038 1416 O ATOM 278 CB LEU A 64 7.050 38.954 43.246 1.00101.53 C ANISOU 278 CB LEU A 64 13801 15464 9312 1269 -1071 1378 C ATOM 279 CG LEU A 64 5.904 39.093 44.256 1.00107.38 C ANISOU 279 CG LEU A 64 14324 16638 9836 1432 -1125 1443 C ATOM 280 CD1 LEU A 64 5.908 40.466 44.888 1.00108.35 C ANISOU 280 CD1 LEU A 64 14554 16683 9932 1806 -1076 1382 C ATOM 281 CD2 LEU A 64 4.549 38.836 43.606 1.00111.00 C ANISOU 281 CD2 LEU A 64 14581 17569 10024 1447 -1169 1591 C ATOM 282 N TYR A 65 9.573 37.446 41.644 1.00 98.23 N ANISOU 282 N TYR A 65 13688 14313 9323 740 -1010 1247 N ATOM 283 CA TYR A 65 10.586 37.414 40.591 1.00 97.05 C ANISOU 283 CA TYR A 65 13701 13865 9307 660 -941 1200 C ATOM 284 C TYR A 65 10.587 36.026 39.954 1.00100.71 C ANISOU 284 C TYR A 65 14156 14361 9747 411 -993 1215 C ATOM 285 O TYR A 65 11.027 35.873 38.815 1.00100.19 O ANISOU 285 O TYR A 65 14198 14163 9707 358 -948 1205 O ATOM 286 CB TYR A 65 11.973 37.717 41.176 1.00 97.28 C ANISOU 286 CB TYR A 65 13834 13573 9556 650 -887 1093 C ATOM 287 CG TYR A 65 12.097 39.078 41.823 1.00 99.66 C ANISOU 287 CG TYR A 65 14202 13781 9885 859 -849 1061 C ATOM 288 CD1 TYR A 65 12.463 40.193 41.079 1.00102.53 C ANISOU 288 CD1 TYR A 65 14730 13953 10272 973 -772 1062 C ATOM 289 CD2 TYR A 65 11.883 39.247 43.187 1.00100.28 C ANISOU 289 CD2 TYR A 65 14206 13942 9954 935 -895 1027 C ATOM 290 CE1 TYR A 65 12.582 41.451 41.667 1.00104.24 C ANISOU 290 CE1 TYR A 65 15068 14038 10500 1153 -751 1028 C ATOM 291 CE2 TYR A 65 11.991 40.502 43.787 1.00101.89 C ANISOU 291 CE2 TYR A 65 14514 14036 10164 1136 -870 982 C ATOM 292 CZ TYR A 65 12.346 41.604 43.023 1.00110.57 C ANISOU 292 CZ TYR A 65 15811 14915 11286 1240 -802 980 C ATOM 293 OH TYR A 65 12.461 42.850 43.597 1.00112.37 O ANISOU 293 OH TYR A 65 16200 14989 11506 1426 -791 932 O ATOM 294 N ILE A 66 10.104 35.016 40.698 1.00 97.83 N ANISOU 294 N ILE A 66 13683 14165 9321 257 -1092 1241 N ATOM 295 CA ILE A 66 9.977 33.628 40.239 1.00 97.98 C ANISOU 295 CA ILE A 66 13732 14207 9287 0 -1171 1260 C ATOM 296 C ILE A 66 8.665 33.507 39.436 1.00104.04 C ANISOU 296 C ILE A 66 14413 15297 9819 -54 -1228 1372 C ATOM 297 O ILE A 66 8.571 32.678 38.527 1.00103.87 O ANISOU 297 O ILE A 66 14476 15258 9733 -235 -1271 1382 O ATOM 298 CB ILE A 66 10.069 32.631 41.437 1.00100.54 C ANISOU 298 CB ILE A 66 14011 14548 9643 -161 -1261 1253 C ATOM 299 CG1 ILE A 66 11.328 32.874 42.334 1.00 99.71 C ANISOU 299 CG1 ILE A 66 13955 14175 9754 -78 -1205 1149 C ATOM 300 CG2 ILE A 66 9.948 31.168 41.001 1.00101.47 C ANISOU 300 CG2 ILE A 66 14223 14639 9694 -436 -1359 1272 C ATOM 301 CD1 ILE A 66 12.758 32.653 41.686 1.00105.75 C ANISOU 301 CD1 ILE A 66 14890 14597 10693 -85 -1130 1049 C ATOM 302 N VAL A 67 7.677 34.377 39.758 1.00102.19 N ANISOU 302 N VAL A 67 14020 15365 9445 123 -1227 1451 N ATOM 303 CA VAL A 67 6.373 34.483 39.092 1.00103.80 C ANISOU 303 CA VAL A 67 14091 15950 9398 130 -1273 1571 C ATOM 304 C VAL A 67 6.575 35.022 37.664 1.00107.82 C ANISOU 304 C VAL A 67 14726 16339 9901 225 -1199 1566 C ATOM 305 O VAL A 67 6.174 34.359 36.707 1.00108.18 O ANISOU 305 O VAL A 67 14787 16486 9829 52 -1249 1607 O ATOM 306 CB VAL A 67 5.362 35.331 39.925 1.00108.97 C ANISOU 306 CB VAL A 67 14535 16973 9895 363 -1280 1651 C ATOM 307 CG1 VAL A 67 4.167 35.790 39.086 1.00110.52 C ANISOU 307 CG1 VAL A 67 14602 17553 9837 479 -1293 1771 C ATOM 308 CG2 VAL A 67 4.885 34.564 41.155 1.00109.16 C ANISOU 308 CG2 VAL A 67 14390 17236 9850 204 -1376 1696 C ATOM 309 N SER A 68 7.223 36.205 37.532 1.00103.72 N ANISOU 309 N SER A 68 14313 15592 9503 478 -1086 1516 N ATOM 310 CA SER A 68 7.533 36.880 36.263 1.00103.69 C ANISOU 310 CA SER A 68 14445 15445 9507 589 -1001 1519 C ATOM 311 C SER A 68 8.331 35.980 35.304 1.00107.14 C ANISOU 311 C SER A 68 15022 15660 10027 371 -991 1462 C ATOM 312 O SER A 68 8.097 36.020 34.095 1.00107.09 O ANISOU 312 O SER A 68 15064 15703 9923 365 -974 1500 O ATOM 313 CB SER A 68 8.276 38.187 36.528 1.00106.46 C ANISOU 313 CB SER A 68 14922 15530 9999 833 -897 1470 C ATOM 314 OG SER A 68 8.718 38.810 35.333 1.00114.38 O ANISOU 314 OG SER A 68 16075 16359 11024 905 -813 1480 O ATOM 315 N LEU A 69 9.251 35.160 35.850 1.00103.05 N ANISOU 315 N LEU A 69 14570 14915 9669 216 -1005 1370 N ATOM 316 CA LEU A 69 10.042 34.207 35.081 1.00102.55 C ANISOU 316 CA LEU A 69 14651 14646 9667 45 -1001 1303 C ATOM 317 C LEU A 69 9.155 33.050 34.592 1.00108.16 C ANISOU 317 C LEU A 69 15348 15558 10190 -183 -1123 1350 C ATOM 318 O LEU A 69 9.346 32.579 33.472 1.00108.48 O ANISOU 318 O LEU A 69 15512 15527 10180 -265 -1120 1326 O ATOM 319 CB LEU A 69 11.226 33.683 35.903 1.00101.32 C ANISOU 319 CB LEU A 69 14563 14223 9710 -12 -987 1201 C ATOM 320 CG LEU A 69 12.204 32.781 35.153 1.00105.80 C ANISOU 320 CG LEU A 69 15294 14564 10340 -114 -966 1119 C ATOM 321 CD1 LEU A 69 13.089 33.583 34.227 1.00105.81 C ANISOU 321 CD1 LEU A 69 15376 14409 10420 16 -832 1091 C ATOM 322 CD2 LEU A 69 13.038 31.974 36.108 1.00108.04 C ANISOU 322 CD2 LEU A 69 15617 14678 10755 -183 -995 1042 C ATOM 323 N SER A 70 8.177 32.611 35.412 1.00105.34 N ANISOU 323 N SER A 70 14844 15467 9712 -296 -1234 1419 N ATOM 324 CA SER A 70 7.243 31.551 35.019 1.00106.41 C ANISOU 324 CA SER A 70 14959 15828 9642 -563 -1369 1483 C ATOM 325 C SER A 70 6.181 32.044 33.998 1.00110.62 C ANISOU 325 C SER A 70 15392 16683 9954 -521 -1380 1585 C ATOM 326 O SER A 70 5.622 31.225 33.261 1.00111.08 O ANISOU 326 O SER A 70 15489 16872 9846 -751 -1476 1618 O ATOM 327 CB SER A 70 6.601 30.892 36.238 1.00110.73 C ANISOU 327 CB SER A 70 15377 16574 10122 -736 -1486 1542 C ATOM 328 OG SER A 70 5.821 31.797 37.002 1.00120.69 O ANISOU 328 OG SER A 70 16399 18149 11307 -560 -1472 1628 O ATOM 329 N VAL A 71 5.931 33.383 33.948 1.00106.40 N ANISOU 329 N VAL A 71 14753 16265 9410 -224 -1288 1632 N ATOM 330 CA VAL A 71 5.015 34.055 33.007 1.00107.30 C ANISOU 330 CA VAL A 71 14774 16674 9322 -100 -1278 1733 C ATOM 331 C VAL A 71 5.702 34.044 31.633 1.00110.37 C ANISOU 331 C VAL A 71 15361 16821 9752 -105 -1212 1677 C ATOM 332 O VAL A 71 5.146 33.504 30.672 1.00111.15 O ANISOU 332 O VAL A 71 15471 17086 9678 -259 -1276 1716 O ATOM 333 CB VAL A 71 4.650 35.503 33.469 1.00111.49 C ANISOU 333 CB VAL A 71 15189 17337 9833 264 -1198 1790 C ATOM 334 CG1 VAL A 71 4.005 36.321 32.349 1.00112.57 C ANISOU 334 CG1 VAL A 71 15299 17673 9797 456 -1159 1880 C ATOM 335 CG2 VAL A 71 3.750 35.481 34.697 1.00112.01 C ANISOU 335 CG2 VAL A 71 15025 17750 9784 287 -1271 1861 C ATOM 336 N ALA A 72 6.931 34.614 31.563 1.00104.93 N ANISOU 336 N ALA A 72 14825 15758 9284 45 -1087 1589 N ATOM 337 CA ALA A 72 7.760 34.657 30.362 1.00104.24 C ANISOU 337 CA ALA A 72 14917 15437 9254 58 -1004 1535 C ATOM 338 C ALA A 72 7.939 33.246 29.817 1.00108.42 C ANISOU 338 C ALA A 72 15564 15898 9731 -213 -1086 1470 C ATOM 339 O ALA A 72 7.799 33.048 28.617 1.00109.17 O ANISOU 339 O ALA A 72 15737 16037 9706 -258 -1087 1476 O ATOM 340 CB ALA A 72 9.112 35.275 30.677 1.00103.56 C ANISOU 340 CB ALA A 72 14943 14994 9413 191 -879 1453 C ATOM 341 N ASP A 73 8.159 32.258 30.702 1.00104.51 N ANISOU 341 N ASP A 73 15097 15310 9301 -389 -1166 1413 N ATOM 342 CA ASP A 73 8.307 30.864 30.301 1.00105.17 C ANISOU 342 CA ASP A 73 15347 15291 9323 -642 -1263 1346 C ATOM 343 C ASP A 73 6.979 30.161 29.948 1.00110.77 C ANISOU 343 C ASP A 73 15999 16322 9768 -892 -1421 1432 C ATOM 344 O ASP A 73 7.011 29.089 29.338 1.00111.66 O ANISOU 344 O ASP A 73 16297 16345 9786 -1109 -1509 1379 O ATOM 345 CB ASP A 73 9.170 30.066 31.300 1.00106.29 C ANISOU 345 CB ASP A 73 15591 15164 9632 -719 -1287 1253 C ATOM 346 CG ASP A 73 10.661 30.394 31.278 1.00116.47 C ANISOU 346 CG ASP A 73 16987 16127 11141 -536 -1148 1148 C ATOM 347 OD1 ASP A 73 11.188 30.721 30.186 1.00116.74 O ANISOU 347 OD1 ASP A 73 17108 16076 11173 -437 -1055 1117 O ATOM 348 OD2 ASP A 73 11.317 30.234 32.329 1.00123.10 O ANISOU 348 OD2 ASP A 73 17819 16816 12135 -512 -1138 1101 O ATOM 349 N LEU A 74 5.816 30.759 30.298 1.00107.47 N ANISOU 349 N LEU A 74 15333 16291 9208 -861 -1460 1563 N ATOM 350 CA LEU A 74 4.525 30.173 29.906 1.00108.89 C ANISOU 350 CA LEU A 74 15415 16851 9109 -1110 -1609 1665 C ATOM 351 C LEU A 74 4.193 30.635 28.489 1.00112.73 C ANISOU 351 C LEU A 74 15912 17474 9446 -1030 -1573 1698 C ATOM 352 O LEU A 74 3.807 29.801 27.662 1.00114.24 O ANISOU 352 O LEU A 74 16205 17739 9463 -1277 -1678 1693 O ATOM 353 CB LEU A 74 3.369 30.488 30.878 1.00109.70 C ANISOU 353 CB LEU A 74 15214 17389 9077 -1123 -1677 1805 C ATOM 354 CG LEU A 74 2.005 29.851 30.535 1.00116.51 C ANISOU 354 CG LEU A 74 15931 18716 9624 -1424 -1841 1932 C ATOM 355 CD1 LEU A 74 1.980 28.350 30.840 1.00117.32 C ANISOU 355 CD1 LEU A 74 16193 18709 9675 -1857 -2004 1904 C ATOM 356 CD2 LEU A 74 0.880 30.562 31.245 1.00119.94 C ANISOU 356 CD2 LEU A 74 16009 19663 9899 -1302 -1858 2087 C ATOM 357 N ILE A 75 4.374 31.959 28.201 1.00107.14 N ANISOU 357 N ILE A 75 15128 16778 8801 -690 -1431 1731 N ATOM 358 CA ILE A 75 4.175 32.547 26.869 1.00107.07 C ANISOU 358 CA ILE A 75 15141 16870 8671 -563 -1376 1771 C ATOM 359 C ILE A 75 4.954 31.696 25.853 1.00110.41 C ANISOU 359 C ILE A 75 15829 17010 9111 -717 -1378 1652 C ATOM 360 O ILE A 75 4.378 31.286 24.852 1.00111.40 O ANISOU 360 O ILE A 75 15985 17314 9026 -858 -1451 1677 O ATOM 361 CB ILE A 75 4.517 34.079 26.853 1.00108.96 C ANISOU 361 CB ILE A 75 15338 17042 9021 -175 -1216 1810 C ATOM 362 CG1 ILE A 75 3.268 34.933 27.142 1.00110.55 C ANISOU 362 CG1 ILE A 75 15288 17681 9035 9 -1241 1962 C ATOM 363 CG2 ILE A 75 5.154 34.545 25.546 1.00108.99 C ANISOU 363 CG2 ILE A 75 15501 16870 9042 -52 -1109 1785 C ATOM 364 CD1 ILE A 75 2.918 35.127 28.595 1.00116.65 C ANISOU 364 CD1 ILE A 75 15897 18574 9851 73 -1268 1991 C ATOM 365 N VAL A 76 6.208 31.325 26.194 1.00105.39 N ANISOU 365 N VAL A 76 15378 15965 8701 -704 -1314 1521 N ATOM 366 CA VAL A 76 7.085 30.465 25.396 1.00105.39 C ANISOU 366 CA VAL A 76 15642 15676 8724 -799 -1308 1391 C ATOM 367 C VAL A 76 6.446 29.083 25.142 1.00112.45 C ANISOU 367 C VAL A 76 16661 16645 9421 -1144 -1493 1363 C ATOM 368 O VAL A 76 6.545 28.572 24.034 1.00113.22 O ANISOU 368 O VAL A 76 16937 16690 9393 -1224 -1520 1304 O ATOM 369 CB VAL A 76 8.514 30.375 26.004 1.00107.12 C ANISOU 369 CB VAL A 76 15988 15504 9209 -686 -1206 1272 C ATOM 370 CG1 VAL A 76 9.383 29.348 25.277 1.00107.31 C ANISOU 370 CG1 VAL A 76 16286 15260 9226 -759 -1211 1133 C ATOM 371 CG2 VAL A 76 9.194 31.738 25.998 1.00105.68 C ANISOU 371 CG2 VAL A 76 15725 15239 9189 -397 -1031 1300 C ATOM 372 N GLY A 77 5.764 28.528 26.139 1.00110.56 N ANISOU 372 N GLY A 77 16333 16539 9135 -1353 -1624 1414 N ATOM 373 CA GLY A 77 5.114 27.227 26.018 1.00112.88 C ANISOU 373 CA GLY A 77 16759 16898 9232 -1732 -1819 1407 C ATOM 374 C GLY A 77 3.837 27.203 25.197 1.00120.19 C ANISOU 374 C GLY A 77 17566 18243 9858 -1917 -1931 1516 C ATOM 375 O GLY A 77 3.621 26.271 24.419 1.00121.57 O ANISOU 375 O GLY A 77 17951 18385 9857 -2176 -2053 1466 O ATOM 376 N ALA A 78 2.968 28.214 25.388 1.00117.48 N ANISOU 376 N ALA A 78 16892 18310 9436 -1781 -1898 1666 N ATOM 377 CA ALA A 78 1.657 28.321 24.738 1.00119.66 C ANISOU 377 CA ALA A 78 16975 19084 9408 -1921 -2001 1800 C ATOM 378 C ALA A 78 1.630 29.068 23.394 1.00124.31 C ANISOU 378 C ALA A 78 17560 19770 9903 -1712 -1911 1814 C ATOM 379 O ALA A 78 0.760 28.790 22.562 1.00126.36 O ANISOU 379 O ALA A 78 17770 20350 9892 -1898 -2020 1878 O ATOM 380 CB ALA A 78 0.659 28.952 25.700 1.00120.69 C ANISOU 380 CB ALA A 78 16735 19662 9460 -1861 -2023 1965 C ATOM 381 N VAL A 79 2.581 29.970 23.167 1.00118.71 N ANISOU 381 N VAL A 79 16911 18794 9401 -1357 -1724 1761 N ATOM 382 CA VAL A 79 2.579 30.766 21.939 1.00118.78 C ANISOU 382 CA VAL A 79 16915 18893 9324 -1144 -1630 1795 C ATOM 383 C VAL A 79 3.780 30.543 21.013 1.00121.96 C ANISOU 383 C VAL A 79 17611 18896 9834 -1075 -1534 1650 C ATOM 384 O VAL A 79 3.618 30.414 19.800 1.00122.88 O ANISOU 384 O VAL A 79 17812 19098 9778 -1113 -1549 1642 O ATOM 385 CB VAL A 79 2.472 32.273 22.252 1.00121.66 C ANISOU 385 CB VAL A 79 17075 19380 9769 -757 -1489 1905 C ATOM 386 CG1 VAL A 79 2.763 33.095 21.006 1.00121.97 C ANISOU 386 CG1 VAL A 79 17181 19393 9769 -523 -1371 1927 C ATOM 387 CG2 VAL A 79 1.094 32.603 22.807 1.00122.67 C ANISOU 387 CG2 VAL A 79 16886 20026 9695 -760 -1580 2068 C ATOM 388 N VAL A 80 4.979 30.514 21.586 1.00116.89 N ANISOU 388 N VAL A 80 17105 17851 9457 -964 -1432 1542 N ATOM 389 CA VAL A 80 6.211 30.484 20.805 1.00116.45 C ANISOU 389 CA VAL A 80 17275 17462 9511 -835 -1310 1422 C ATOM 390 C VAL A 80 6.407 29.023 20.405 1.00123.87 C ANISOU 390 C VAL A 80 18481 18236 10346 -1098 -1433 1286 C ATOM 391 O VAL A 80 6.725 28.725 19.253 1.00124.49 O ANISOU 391 O VAL A 80 18736 18250 10314 -1093 -1416 1214 O ATOM 392 CB VAL A 80 7.456 30.961 21.578 1.00117.73 C ANISOU 392 CB VAL A 80 17466 17292 9973 -629 -1162 1362 C ATOM 393 CG1 VAL A 80 8.672 30.980 20.665 1.00117.27 C ANISOU 393 CG1 VAL A 80 17594 16980 9984 -495 -1030 1264 C ATOM 394 CG2 VAL A 80 7.211 32.336 22.181 1.00116.42 C ANISOU 394 CG2 VAL A 80 17081 17245 9906 -400 -1069 1486 C ATOM 395 N MET A 81 6.222 28.117 21.359 1.00122.43 N ANISOU 395 N MET A 81 18353 17977 10188 -1321 -1561 1250 N ATOM 396 CA MET A 81 6.457 26.687 21.116 1.00124.51 C ANISOU 396 CA MET A 81 18933 18016 10358 -1567 -1692 1115 C ATOM 397 C MET A 81 5.491 26.021 20.114 1.00133.15 C ANISOU 397 C MET A 81 20127 19329 11134 -1848 -1856 1126 C ATOM 398 O MET A 81 6.010 25.366 19.206 1.00134.35 O ANISOU 398 O MET A 81 20572 19274 11200 -1868 -1870 994 O ATOM 399 CB MET A 81 6.583 25.876 22.421 1.00126.49 C ANISOU 399 CB MET A 81 19256 18086 10719 -1734 -1788 1081 C ATOM 400 CG MET A 81 8.004 25.779 22.940 1.00128.49 C ANISOU 400 CG MET A 81 19651 17941 11229 -1516 -1664 959 C ATOM 401 SD MET A 81 8.074 25.656 24.742 1.00131.21 S ANISOU 401 SD MET A 81 19873 18207 11772 -1564 -1698 999 S ATOM 402 CE MET A 81 9.244 24.345 24.922 1.00128.26 C ANISOU 402 CE MET A 81 19897 17364 11474 -1578 -1734 816 C ATOM 403 N PRO A 82 4.126 26.148 20.218 1.00131.86 N ANISOU 403 N PRO A 82 19733 19594 10773 -2062 -1984 1275 N ATOM 404 CA PRO A 82 3.248 25.479 19.230 1.00134.57 C ANISOU 404 CA PRO A 82 20175 20160 10796 -2363 -2152 1284 C ATOM 405 C PRO A 82 3.381 26.014 17.803 1.00138.77 C ANISOU 405 C PRO A 82 20737 20779 11213 -2180 -2062 1266 C ATOM 406 O PRO A 82 3.331 25.226 16.860 1.00139.92 O ANISOU 406 O PRO A 82 21139 20864 11162 -2359 -2161 1170 O ATOM 407 CB PRO A 82 1.834 25.699 19.795 1.00137.49 C ANISOU 407 CB PRO A 82 20205 21035 10999 -2577 -2278 1475 C ATOM 408 CG PRO A 82 2.039 26.097 21.231 1.00139.81 C ANISOU 408 CG PRO A 82 20319 21277 11527 -2452 -2212 1528 C ATOM 409 CD PRO A 82 3.314 26.872 21.219 1.00132.78 C ANISOU 409 CD PRO A 82 19488 20043 10920 -2038 -1988 1442 C ATOM 410 N MET A 83 3.581 27.343 17.651 1.00134.08 N ANISOU 410 N MET A 83 19908 20303 10733 -1825 -1878 1354 N ATOM 411 CA MET A 83 3.754 28.024 16.364 1.00134.36 C ANISOU 411 CA MET A 83 19946 20428 10679 -1613 -1768 1367 C ATOM 412 C MET A 83 5.089 27.665 15.684 1.00138.49 C ANISOU 412 C MET A 83 20780 20542 11297 -1469 -1658 1190 C ATOM 413 O MET A 83 5.188 27.759 14.460 1.00139.21 O ANISOU 413 O MET A 83 20964 20691 11239 -1404 -1623 1162 O ATOM 414 CB MET A 83 3.613 29.548 16.517 1.00135.36 C ANISOU 414 CB MET A 83 19772 20753 10904 -1280 -1610 1523 C ATOM 415 CG MET A 83 2.191 30.035 16.765 1.00140.14 C ANISOU 415 CG MET A 83 20058 21868 11322 -1339 -1704 1710 C ATOM 416 SD MET A 83 2.055 31.849 16.716 1.00143.59 S ANISOU 416 SD MET A 83 20234 22496 11829 -883 -1521 1881 S ATOM 417 CE MET A 83 0.344 32.054 17.122 1.00142.29 C ANISOU 417 CE MET A 83 19712 22959 11395 -981 -1669 2075 C ATOM 418 N ASN A 84 6.106 27.258 16.466 1.00134.22 N ANISOU 418 N ASN A 84 20388 19624 10987 -1406 -1604 1077 N ATOM 419 CA ASN A 84 7.401 26.853 15.922 1.00134.33 C ANISOU 419 CA ASN A 84 20676 19287 11076 -1247 -1501 911 C ATOM 420 C ASN A 84 7.372 25.398 15.426 1.00141.11 C ANISOU 420 C ASN A 84 21903 19976 11736 -1489 -1668 750 C ATOM 421 O ASN A 84 8.189 25.038 14.577 1.00141.57 O ANISOU 421 O ASN A 84 22202 19845 11742 -1355 -1604 615 O ATOM 422 CB ASN A 84 8.532 27.080 16.924 1.00133.82 C ANISOU 422 CB ASN A 84 20598 18929 11318 -1048 -1368 865 C ATOM 423 CG ASN A 84 9.888 27.217 16.270 1.00159.85 C ANISOU 423 CG ASN A 84 24033 22005 14700 -782 -1194 761 C ATOM 424 OD1 ASN A 84 10.353 28.322 15.969 1.00153.41 O ANISOU 424 OD1 ASN A 84 23055 21252 13982 -554 -1022 839 O ATOM 425 ND2 ASN A 84 10.549 26.095 16.015 1.00152.89 N ANISOU 425 ND2 ASN A 84 23462 20869 13761 -802 -1238 588 N ATOM 426 N ILE A 85 6.429 24.570 15.944 1.00139.32 N ANISOU 426 N ILE A 85 21731 19824 11380 -1847 -1884 768 N ATOM 427 CA ILE A 85 6.243 23.164 15.532 1.00141.92 C ANISOU 427 CA ILE A 85 22451 19981 11491 -2141 -2082 629 C ATOM 428 C ILE A 85 5.661 23.125 14.090 1.00148.35 C ANISOU 428 C ILE A 85 23336 21026 12004 -2234 -2143 619 C ATOM 429 O ILE A 85 6.077 22.285 13.282 1.00149.60 O ANISOU 429 O ILE A 85 23867 20963 12010 -2264 -2198 451 O ATOM 430 CB ILE A 85 5.394 22.335 16.565 1.00145.97 C ANISOU 430 CB ILE A 85 22997 20515 11949 -2543 -2302 679 C ATOM 431 CG1 ILE A 85 6.013 22.382 17.988 1.00144.06 C ANISOU 431 CG1 ILE A 85 22686 20048 12001 -2432 -2235 687 C ATOM 432 CG2 ILE A 85 5.207 20.867 16.108 1.00149.91 C ANISOU 432 CG2 ILE A 85 23967 20790 12204 -2880 -2525 535 C ATOM 433 CD1 ILE A 85 5.042 22.071 19.163 1.00151.61 C ANISOU 433 CD1 ILE A 85 23489 21176 12940 -2766 -2398 816 C ATOM 434 N LEU A 86 4.726 24.065 13.777 1.00145.06 N ANISOU 434 N LEU A 86 22565 21058 11493 -2244 -2129 798 N ATOM 435 CA LEU A 86 4.065 24.228 12.471 1.00146.86 C ANISOU 435 CA LEU A 86 22775 21590 11435 -2312 -2178 830 C ATOM 436 C LEU A 86 5.074 24.445 11.345 1.00151.42 C ANISOU 436 C LEU A 86 23530 21994 12007 -2004 -2016 712 C ATOM 437 O LEU A 86 4.905 23.865 10.278 1.00153.40 O ANISOU 437 O LEU A 86 24013 22271 12003 -2119 -2106 617 O ATOM 438 CB LEU A 86 3.052 25.390 12.498 1.00146.35 C ANISOU 438 CB LEU A 86 22258 22029 11319 -2263 -2146 1061 C ATOM 439 CG LEU A 86 1.726 25.145 13.222 1.00151.83 C ANISOU 439 CG LEU A 86 22734 23082 11874 -2614 -2341 1202 C ATOM 440 CD1 LEU A 86 1.199 26.425 13.832 1.00150.26 C ANISOU 440 CD1 LEU A 86 22087 23231 11776 -2393 -2235 1410 C ATOM 441 CD2 LEU A 86 0.684 24.543 12.287 1.00157.61 C ANISOU 441 CD2 LEU A 86 23522 24138 12225 -2970 -2547 1220 C ATOM 442 N TYR A 87 6.132 25.253 11.599 1.00146.16 N ANISOU 442 N TYR A 87 22761 21164 11609 -1631 -1784 718 N ATOM 443 CA TYR A 87 7.226 25.562 10.664 1.00146.10 C ANISOU 443 CA TYR A 87 22871 21015 11625 -1316 -1600 631 C ATOM 444 C TYR A 87 8.090 24.342 10.346 1.00151.60 C ANISOU 444 C TYR A 87 23998 21346 12256 -1311 -1641 395 C ATOM 445 O TYR A 87 8.821 24.355 9.352 1.00152.21 O ANISOU 445 O TYR A 87 24217 21366 12250 -1099 -1531 302 O ATOM 446 CB TYR A 87 8.120 26.666 11.234 1.00144.59 C ANISOU 446 CB TYR A 87 22455 20741 11741 -988 -1367 712 C ATOM 447 CG TYR A 87 7.724 28.067 10.830 1.00145.63 C ANISOU 447 CG TYR A 87 22276 21179 11879 -824 -1247 907 C ATOM 448 CD1 TYR A 87 8.458 28.774 9.883 1.00147.50 C ANISOU 448 CD1 TYR A 87 22504 21428 12110 -566 -1066 926 C ATOM 449 CD2 TYR A 87 6.653 28.714 11.445 1.00145.99 C ANISOU 449 CD2 TYR A 87 22039 21498 11932 -906 -1309 1082 C ATOM 450 CE1 TYR A 87 8.123 30.081 9.537 1.00147.95 C ANISOU 450 CE1 TYR A 87 22316 21727 12173 -409 -959 1117 C ATOM 451 CE2 TYR A 87 6.308 30.020 11.106 1.00146.63 C ANISOU 451 CE2 TYR A 87 21873 21830 12011 -711 -1200 1262 C ATOM 452 CZ TYR A 87 7.050 30.703 10.158 1.00154.39 C ANISOU 452 CZ TYR A 87 22887 22780 12995 -469 -1028 1280 C ATOM 453 OH TYR A 87 6.699 31.986 9.822 1.00155.82 O ANISOU 453 OH TYR A 87 22864 23178 13162 -280 -931 1466 O ATOM 454 N LEU A 88 8.034 23.310 11.205 1.00148.22 N ANISOU 454 N LEU A 88 23784 20672 11859 -1521 -1792 303 N ATOM 455 CA LEU A 88 8.767 22.058 11.025 1.00149.45 C ANISOU 455 CA LEU A 88 24401 20448 11935 -1515 -1861 77 C ATOM 456 C LEU A 88 7.915 21.033 10.275 1.00156.36 C ANISOU 456 C LEU A 88 25601 21343 12466 -1858 -2103 -16 C ATOM 457 O LEU A 88 8.461 20.149 9.610 1.00158.08 O ANISOU 457 O LEU A 88 26235 21304 12523 -1799 -2147 -214 O ATOM 458 CB LEU A 88 9.217 21.498 12.376 1.00148.24 C ANISOU 458 CB LEU A 88 24342 19984 11996 -1542 -1896 33 C ATOM 459 CG LEU A 88 10.423 22.186 12.984 1.00150.22 C ANISOU 459 CG LEU A 88 24413 20110 12553 -1172 -1663 46 C ATOM 460 CD1 LEU A 88 10.246 22.359 14.473 1.00148.40 C ANISOU 460 CD1 LEU A 88 23987 19835 12562 -1267 -1688 145 C ATOM 461 CD2 LEU A 88 11.703 21.447 12.633 1.00153.60 C ANISOU 461 CD2 LEU A 88 25183 20215 12964 -902 -1589 -158 C ATOM 462 N LEU A 89 6.580 21.159 10.386 1.00153.35 N ANISOU 462 N LEU A 89 25029 21283 11953 -2211 -2264 129 N ATOM 463 CA LEU A 89 5.612 20.298 9.715 1.00156.38 C ANISOU 463 CA LEU A 89 25657 21767 11992 -2610 -2514 79 C ATOM 464 C LEU A 89 5.310 20.866 8.314 1.00161.66 C ANISOU 464 C LEU A 89 26227 22756 12439 -2520 -2462 105 C ATOM 465 O LEU A 89 5.369 20.130 7.328 1.00163.84 O ANISOU 465 O LEU A 89 26864 22932 12456 -2594 -2558 -54 O ATOM 466 CB LEU A 89 4.334 20.195 10.562 1.00156.69 C ANISOU 466 CB LEU A 89 25482 22067 11984 -3040 -2707 246 C ATOM 467 CG LEU A 89 3.474 18.970 10.310 1.00164.80 C ANISOU 467 CG LEU A 89 26852 23070 12694 -3554 -3012 179 C ATOM 468 CD1 LEU A 89 3.381 18.109 11.550 1.00164.91 C ANISOU 468 CD1 LEU A 89 27046 22815 12798 -3835 -3163 171 C ATOM 469 CD2 LEU A 89 2.097 19.369 9.827 1.00169.01 C ANISOU 469 CD2 LEU A 89 27073 24166 12976 -3862 -3138 353 C ATOM 470 N MET A 90 5.022 22.183 8.237 1.00156.42 N ANISOU 470 N MET A 90 25100 22460 11873 -2340 -2309 302 N ATOM 471 CA MET A 90 4.709 22.930 7.014 1.00157.07 C ANISOU 471 CA MET A 90 25019 22885 11774 -2217 -2237 376 C ATOM 472 C MET A 90 5.760 24.037 6.844 1.00158.44 C ANISOU 472 C MET A 90 25004 23014 12181 -1741 -1941 423 C ATOM 473 O MET A 90 5.752 24.998 7.615 1.00155.53 O ANISOU 473 O MET A 90 24302 22745 12049 -1601 -1822 584 O ATOM 474 CB MET A 90 3.297 23.555 7.108 1.00159.97 C ANISOU 474 CB MET A 90 24996 23768 12017 -2441 -2339 604 C ATOM 475 CG MET A 90 2.209 22.585 7.536 1.00165.94 C ANISOU 475 CG MET A 90 25843 24633 12573 -2955 -2627 610 C ATOM 476 SD MET A 90 0.752 23.439 8.180 1.00169.99 S ANISOU 476 SD MET A 90 25792 25755 13040 -3129 -2696 910 S ATOM 477 CE MET A 90 -0.175 23.675 6.671 1.00169.75 C ANISOU 477 CE MET A 90 25667 26222 12607 -3239 -2786 977 C ATOM 478 N SER A 91 6.666 23.895 5.847 1.00156.15 N ANISOU 478 N SER A 91 24939 22581 11811 -1502 -1828 284 N ATOM 479 CA SER A 91 7.766 24.829 5.541 1.00154.58 C ANISOU 479 CA SER A 91 24602 22344 11787 -1084 -1553 319 C ATOM 480 C SER A 91 7.369 26.320 5.521 1.00158.10 C ANISOU 480 C SER A 91 24618 23120 12334 -944 -1416 571 C ATOM 481 O SER A 91 8.127 27.161 6.012 1.00155.42 O ANISOU 481 O SER A 91 24104 22693 12256 -694 -1224 650 O ATOM 482 CB SER A 91 8.457 24.435 4.241 1.00160.03 C ANISOU 482 CB SER A 91 25567 22975 12264 -912 -1491 161 C ATOM 483 OG SER A 91 9.691 25.117 4.092 1.00168.29 O ANISOU 483 OG SER A 91 26519 23941 13484 -535 -1233 174 O ATOM 484 N LYS A 92 6.186 26.634 4.960 1.00156.86 N ANISOU 484 N LYS A 92 24307 23339 11953 -1105 -1525 696 N ATOM 485 CA LYS A 92 5.633 27.991 4.906 1.00155.94 C ANISOU 485 CA LYS A 92 23815 23555 11879 -968 -1428 940 C ATOM 486 C LYS A 92 4.652 28.183 6.061 1.00160.01 C ANISOU 486 C LYS A 92 24088 24227 12481 -1148 -1543 1074 C ATOM 487 O LYS A 92 4.077 27.210 6.558 1.00160.39 O ANISOU 487 O LYS A 92 24241 24253 12446 -1467 -1741 1002 O ATOM 488 CB LYS A 92 4.950 28.269 3.552 1.00160.46 C ANISOU 488 CB LYS A 92 24346 24490 12130 -983 -1466 1009 C ATOM 489 CG LYS A 92 5.926 28.626 2.432 1.00170.67 C ANISOU 489 CG LYS A 92 25750 25723 13374 -702 -1281 964 C ATOM 490 CD LYS A 92 5.238 28.742 1.075 1.00179.32 C ANISOU 490 CD LYS A 92 26841 27171 14123 -742 -1341 1012 C ATOM 491 CE LYS A 92 6.236 28.897 -0.049 1.00186.11 C ANISOU 491 CE LYS A 92 27847 27964 14900 -491 -1173 942 C ATOM 492 NZ LYS A 92 5.577 28.878 -1.381 1.00193.98 N ANISOU 492 NZ LYS A 92 28873 29296 15537 -546 -1247 964 N ATOM 493 N TRP A 93 4.462 29.438 6.481 1.00156.27 N ANISOU 493 N TRP A 93 23304 23913 12157 -942 -1421 1273 N ATOM 494 CA TRP A 93 3.592 29.802 7.600 1.00155.97 C ANISOU 494 CA TRP A 93 23003 24054 12204 -1028 -1495 1414 C ATOM 495 C TRP A 93 2.119 29.970 7.269 1.00161.49 C ANISOU 495 C TRP A 93 23480 25262 12619 -1190 -1649 1566 C ATOM 496 O TRP A 93 1.762 30.767 6.398 1.00162.07 O ANISOU 496 O TRP A 93 23422 25614 12541 -1023 -1591 1692 O ATOM 497 CB TRP A 93 4.117 31.038 8.330 1.00152.76 C ANISOU 497 CB TRP A 93 22408 23543 12089 -713 -1301 1539 C ATOM 498 CG TRP A 93 4.488 32.192 7.446 1.00154.48 C ANISOU 498 CG TRP A 93 22563 23835 12298 -409 -1123 1654 C ATOM 499 CD1 TRP A 93 3.736 33.300 7.191 1.00157.73 C ANISOU 499 CD1 TRP A 93 22751 24562 12619 -244 -1089 1862 C ATOM 500 CD2 TRP A 93 5.731 32.378 6.747 1.00154.01 C ANISOU 500 CD2 TRP A 93 22669 23530 12317 -224 -950 1582 C ATOM 501 NE1 TRP A 93 4.422 34.156 6.359 1.00157.50 N ANISOU 501 NE1 TRP A 93 22765 24468 12609 10 -914 1927 N ATOM 502 CE2 TRP A 93 5.649 33.615 6.070 1.00158.26 C ANISOU 502 CE2 TRP A 93 23083 24242 12808 13 -823 1763 C ATOM 503 CE3 TRP A 93 6.898 31.604 6.601 1.00155.05 C ANISOU 503 CE3 TRP A 93 23044 23338 12531 -225 -891 1389 C ATOM 504 CZ2 TRP A 93 6.696 34.108 5.281 1.00157.57 C ANISOU 504 CZ2 TRP A 93 23092 24018 12760 207 -641 1767 C ATOM 505 CZ3 TRP A 93 7.935 32.094 5.823 1.00156.51 C ANISOU 505 CZ3 TRP A 93 23297 23424 12747 -4 -704 1388 C ATOM 506 CH2 TRP A 93 7.829 33.329 5.171 1.00157.53 C ANISOU 506 CH2 TRP A 93 23286 23735 12832 187 -582 1579 C ATOM 507 N SER A 94 1.259 29.254 8.021 1.00158.31 N ANISOU 507 N SER A 94 23012 25001 12136 -1512 -1844 1571 N ATOM 508 CA SER A 94 -0.204 29.307 7.914 1.00159.91 C ANISOU 508 CA SER A 94 22956 25744 12057 -1715 -2013 1725 C ATOM 509 C SER A 94 -0.728 30.475 8.787 1.00161.83 C ANISOU 509 C SER A 94 22829 26239 12419 -1473 -1932 1936 C ATOM 510 O SER A 94 -1.940 30.665 8.938 1.00162.65 O ANISOU 510 O SER A 94 22650 26834 12315 -1574 -2049 2092 O ATOM 511 CB SER A 94 -0.813 27.980 8.368 1.00164.80 C ANISOU 511 CB SER A 94 23687 26397 12532 -2200 -2259 1642 C ATOM 512 OG SER A 94 -0.138 26.862 7.812 1.00173.15 O ANISOU 512 OG SER A 94 25166 27087 13536 -2382 -2326 1416 O ATOM 513 N LEU A 95 0.219 31.265 9.331 1.00155.65 N ANISOU 513 N LEU A 95 22059 25127 11955 -1143 -1730 1938 N ATOM 514 CA LEU A 95 0.022 32.405 10.221 1.00153.88 C ANISOU 514 CA LEU A 95 21580 24993 11895 -860 -1626 2096 C ATOM 515 C LEU A 95 -0.496 33.745 9.679 1.00157.23 C ANISOU 515 C LEU A 95 21795 25737 12208 -518 -1531 2298 C ATOM 516 O LEU A 95 -1.496 34.263 10.182 1.00157.29 O ANISOU 516 O LEU A 95 21526 26127 12111 -440 -1584 2457 O ATOM 517 CB LEU A 95 1.360 32.757 10.924 1.00151.25 C ANISOU 517 CB LEU A 95 21391 24141 11937 -650 -1447 2008 C ATOM 518 CG LEU A 95 1.787 31.876 12.103 1.00154.67 C ANISOU 518 CG LEU A 95 21921 24278 12569 -852 -1506 1877 C ATOM 519 CD1 LEU A 95 2.656 30.713 11.649 1.00155.16 C ANISOU 519 CD1 LEU A 95 22318 23988 12647 -1038 -1537 1664 C ATOM 520 CD2 LEU A 95 2.560 32.676 13.116 1.00154.51 C ANISOU 520 CD2 LEU A 95 21858 23975 12874 -593 -1349 1895 C ATOM 521 N GLY A 96 0.198 34.284 8.673 1.00152.99 N ANISOU 521 N GLY A 96 21399 25047 11682 -307 -1393 2294 N ATOM 522 CA GLY A 96 -0.083 35.586 8.081 1.00153.25 C ANISOU 522 CA GLY A 96 21311 25285 11632 41 -1283 2481 C ATOM 523 C GLY A 96 0.408 36.759 8.904 1.00154.81 C ANISOU 523 C GLY A 96 21476 25247 12096 377 -1123 2569 C ATOM 524 O GLY A 96 0.696 36.585 10.088 1.00152.38 O ANISOU 524 O GLY A 96 21159 24729 12010 331 -1122 2507 O ATOM 525 N ARG A 97 0.495 37.963 8.294 1.00152.29 N ANISOU 525 N ARG A 97 21160 24957 11747 707 -996 2716 N ATOM 526 CA ARG A 97 0.967 39.206 8.934 1.00151.17 C ANISOU 526 CA ARG A 97 21045 24566 11827 1035 -847 2813 C ATOM 527 C ARG A 97 0.564 39.447 10.410 1.00154.91 C ANISOU 527 C ARG A 97 21377 25045 12438 1103 -883 2837 C ATOM 528 O ARG A 97 1.474 39.704 11.199 1.00152.39 O ANISOU 528 O ARG A 97 21173 24320 12408 1154 -787 2769 O ATOM 529 CB ARG A 97 0.729 40.456 8.058 1.00153.21 C ANISOU 529 CB ARG A 97 21313 24956 11942 1370 -756 3009 C ATOM 530 CG ARG A 97 1.716 40.617 6.899 1.00161.45 C ANISOU 530 CG ARG A 97 22570 25770 13003 1387 -632 2989 C ATOM 531 CD ARG A 97 3.028 41.283 7.301 1.00165.63 C ANISOU 531 CD ARG A 97 23291 25798 13844 1498 -460 2969 C ATOM 532 NE ARG A 97 2.941 42.746 7.283 1.00168.70 N ANISOU 532 NE ARG A 97 23729 26128 14242 1835 -364 3168 N ATOM 533 CZ ARG A 97 3.984 43.563 7.401 1.00177.00 C ANISOU 533 CZ ARG A 97 24966 26784 15501 1942 -218 3205 C ATOM 534 NH1 ARG A 97 5.210 43.072 7.542 1.00159.46 N ANISOU 534 NH1 ARG A 97 22855 24237 13494 1754 -139 3062 N ATOM 535 NH2 ARG A 97 3.811 44.878 7.372 1.00162.70 N ANISOU 535 NH2 ARG A 97 23242 24909 13668 2237 -154 3391 N ATOM 536 N PRO A 98 -0.729 39.329 10.841 1.00153.74 N ANISOU 536 N PRO A 98 20971 25359 12084 1092 -1019 2926 N ATOM 537 CA PRO A 98 -1.045 39.565 12.267 1.00152.81 C ANISOU 537 CA PRO A 98 20719 25250 12091 1176 -1040 2944 C ATOM 538 C PRO A 98 -0.426 38.554 13.246 1.00155.31 C ANISOU 538 C PRO A 98 21097 25273 12641 873 -1080 2763 C ATOM 539 O PRO A 98 0.242 38.979 14.193 1.00152.98 O ANISOU 539 O PRO A 98 20874 24641 12610 993 -993 2722 O ATOM 540 CB PRO A 98 -2.583 39.560 12.304 1.00157.02 C ANISOU 540 CB PRO A 98 20937 26430 12293 1209 -1180 3090 C ATOM 541 CG PRO A 98 -3.021 39.716 10.874 1.00163.85 C ANISOU 541 CG PRO A 98 21787 27588 12878 1256 -1198 3184 C ATOM 542 CD PRO A 98 -1.961 39.035 10.077 1.00158.27 C ANISOU 542 CD PRO A 98 21344 26506 12287 1015 -1155 3026 C ATOM 543 N LEU A 99 -0.629 37.228 13.011 1.00153.09 N ANISOU 543 N LEU A 99 20810 25102 12254 481 -1216 2656 N ATOM 544 CA LEU A 99 -0.094 36.132 13.839 1.00151.40 C ANISOU 544 CA LEU A 99 20688 24616 12221 173 -1275 2488 C ATOM 545 C LEU A 99 1.429 36.045 13.759 1.00153.15 C ANISOU 545 C LEU A 99 21190 24270 12729 195 -1138 2338 C ATOM 546 O LEU A 99 2.073 35.770 14.775 1.00151.22 O ANISOU 546 O LEU A 99 21004 23726 12726 141 -1114 2243 O ATOM 547 CB LEU A 99 -0.686 34.764 13.427 1.00152.97 C ANISOU 547 CB LEU A 99 20881 25046 12196 -251 -1464 2417 C ATOM 548 CG LEU A 99 -2.126 34.429 13.823 1.00159.54 C ANISOU 548 CG LEU A 99 21418 26440 12761 -432 -1642 2535 C ATOM 549 CD1 LEU A 99 -2.641 33.249 13.012 1.00161.90 C ANISOU 549 CD1 LEU A 99 21766 26956 12792 -850 -1822 2480 C ATOM 550 CD2 LEU A 99 -2.238 34.106 15.304 1.00160.33 C ANISOU 550 CD2 LEU A 99 21413 26497 13007 -539 -1691 2518 C ATOM 551 N CYS A 100 1.998 36.237 12.546 1.00149.60 N ANISOU 551 N CYS A 100 20897 23711 12232 266 -1052 2322 N ATOM 552 CA CYS A 100 3.437 36.148 12.315 1.00147.73 C ANISOU 552 CA CYS A 100 20897 23016 12218 291 -917 2196 C ATOM 553 C CYS A 100 4.250 37.294 12.886 1.00149.82 C ANISOU 553 C CYS A 100 21198 22988 12741 561 -750 2249 C ATOM 554 O CYS A 100 5.343 37.039 13.384 1.00148.11 O ANISOU 554 O CYS A 100 21102 22412 12760 518 -677 2132 O ATOM 555 CB CYS A 100 3.772 35.873 10.854 1.00149.32 C ANISOU 555 CB CYS A 100 21244 23234 12258 256 -887 2157 C ATOM 556 SG CYS A 100 5.077 34.640 10.622 1.00152.37 S ANISOU 556 SG CYS A 100 21903 23228 12763 64 -863 1913 S ATOM 557 N LEU A 101 3.727 38.536 12.858 1.00146.45 N ANISOU 557 N LEU A 101 20678 22709 12259 835 -698 2423 N ATOM 558 CA LEU A 101 4.430 39.676 13.457 1.00144.87 C ANISOU 558 CA LEU A 101 20549 22209 12285 1073 -560 2478 C ATOM 559 C LEU A 101 4.387 39.608 14.997 1.00145.75 C ANISOU 559 C LEU A 101 20582 22213 12583 1058 -598 2429 C ATOM 560 O LEU A 101 5.336 40.054 15.650 1.00143.82 O ANISOU 560 O LEU A 101 20441 21619 12587 1122 -500 2387 O ATOM 561 CB LEU A 101 3.878 41.021 12.963 1.00146.60 C ANISOU 561 CB LEU A 101 20754 22577 12372 1390 -504 2677 C ATOM 562 CG LEU A 101 4.373 41.508 11.606 1.00152.68 C ANISOU 562 CG LEU A 101 21666 23291 13055 1472 -402 2748 C ATOM 563 CD1 LEU A 101 3.388 42.477 10.991 1.00155.30 C ANISOU 563 CD1 LEU A 101 21940 23920 13147 1744 -412 2949 C ATOM 564 CD2 LEU A 101 5.737 42.173 11.717 1.00154.10 C ANISOU 564 CD2 LEU A 101 22039 23028 13483 1528 -244 2736 C ATOM 565 N PHE A 102 3.294 39.039 15.569 1.00141.57 N ANISOU 565 N PHE A 102 19863 22009 11920 956 -743 2439 N ATOM 566 CA PHE A 102 3.118 38.875 17.018 1.00139.49 C ANISOU 566 CA PHE A 102 19497 21713 11790 925 -793 2400 C ATOM 567 C PHE A 102 3.986 37.748 17.560 1.00139.67 C ANISOU 567 C PHE A 102 19616 21446 12006 647 -816 2220 C ATOM 568 O PHE A 102 4.488 37.862 18.674 1.00137.28 O ANISOU 568 O PHE A 102 19324 20918 11919 671 -784 2167 O ATOM 569 CB PHE A 102 1.645 38.672 17.393 1.00142.76 C ANISOU 569 CB PHE A 102 19652 22629 11963 905 -936 2496 C ATOM 570 CG PHE A 102 1.285 39.243 18.744 1.00143.75 C ANISOU 570 CG PHE A 102 19650 22797 12170 1082 -938 2541 C ATOM 571 CD1 PHE A 102 1.202 40.619 18.937 1.00147.25 C ANISOU 571 CD1 PHE A 102 20120 23197 12630 1470 -846 2647 C ATOM 572 CD2 PHE A 102 1.009 38.407 19.819 1.00145.10 C ANISOU 572 CD2 PHE A 102 19698 23052 12384 868 -1038 2478 C ATOM 573 CE1 PHE A 102 0.864 41.147 20.187 1.00147.88 C ANISOU 573 CE1 PHE A 102 20106 23315 12765 1659 -851 2674 C ATOM 574 CE2 PHE A 102 0.666 38.937 21.067 1.00147.57 C ANISOU 574 CE2 PHE A 102 19886 23431 12753 1046 -1038 2518 C ATOM 575 CZ PHE A 102 0.595 40.303 21.242 1.00146.12 C ANISOU 575 CZ PHE A 102 19731 23206 12581 1450 -943 2608 C ATOM 576 N TRP A 103 4.186 36.679 16.763 1.00135.67 N ANISOU 576 N TRP A 103 19202 20935 11411 404 -870 2124 N ATOM 577 CA TRP A 103 5.062 35.559 17.106 1.00133.73 C ANISOU 577 CA TRP A 103 19099 20395 11316 176 -891 1948 C ATOM 578 C TRP A 103 6.520 36.040 17.112 1.00134.84 C ANISOU 578 C TRP A 103 19396 20130 11707 313 -722 1884 C ATOM 579 O TRP A 103 7.313 35.558 17.919 1.00132.56 O ANISOU 579 O TRP A 103 19170 19579 11618 238 -706 1772 O ATOM 580 CB TRP A 103 4.884 34.401 16.118 1.00133.70 C ANISOU 580 CB TRP A 103 19203 20482 11115 -71 -992 1863 C ATOM 581 CG TRP A 103 5.727 33.201 16.431 1.00133.97 C ANISOU 581 CG TRP A 103 19426 20208 11269 -272 -1026 1679 C ATOM 582 CD1 TRP A 103 5.441 32.212 17.323 1.00136.41 C ANISOU 582 CD1 TRP A 103 19742 20493 11596 -508 -1161 1611 C ATOM 583 CD2 TRP A 103 7.011 32.877 15.873 1.00133.02 C ANISOU 583 CD2 TRP A 103 19521 19768 11252 -231 -922 1550 C ATOM 584 NE1 TRP A 103 6.441 31.267 17.322 1.00135.37 N ANISOU 584 NE1 TRP A 103 19845 20024 11565 -605 -1155 1441 N ATOM 585 CE2 TRP A 103 7.424 31.656 16.451 1.00136.61 C ANISOU 585 CE2 TRP A 103 20120 20010 11774 -422 -1006 1398 C ATOM 586 CE3 TRP A 103 7.855 33.502 14.937 1.00134.58 C ANISOU 586 CE3 TRP A 103 19800 19859 11475 -45 -765 1557 C ATOM 587 CZ2 TRP A 103 8.643 31.046 16.127 1.00135.58 C ANISOU 587 CZ2 TRP A 103 20208 19577 11729 -394 -935 1246 C ATOM 588 CZ3 TRP A 103 9.063 32.897 14.618 1.00135.63 C ANISOU 588 CZ3 TRP A 103 20120 19722 11690 -43 -691 1413 C ATOM 589 CH2 TRP A 103 9.446 31.684 15.209 1.00135.93 C ANISOU 589 CH2 TRP A 103 20296 19565 11788 -196 -775 1255 C ATOM 590 N LEU A 104 6.862 36.999 16.221 1.00131.39 N ANISOU 590 N LEU A 104 19011 19665 11245 505 -599 1968 N ATOM 591 CA LEU A 104 8.190 37.620 16.139 1.00129.92 C ANISOU 591 CA LEU A 104 18948 19154 11261 619 -435 1948 C ATOM 592 C LEU A 104 8.428 38.481 17.382 1.00129.64 C ANISOU 592 C LEU A 104 18870 18950 11437 745 -387 1988 C ATOM 593 O LEU A 104 9.571 38.613 17.820 1.00128.14 O ANISOU 593 O LEU A 104 18755 18472 11459 742 -296 1925 O ATOM 594 CB LEU A 104 8.316 38.507 14.886 1.00131.67 C ANISOU 594 CB LEU A 104 19231 19430 11367 773 -332 2066 C ATOM 595 CG LEU A 104 8.528 37.815 13.539 1.00138.39 C ANISOU 595 CG LEU A 104 20170 20367 12044 682 -327 2012 C ATOM 596 CD1 LEU A 104 8.113 38.731 12.395 1.00140.72 C ANISOU 596 CD1 LEU A 104 20469 20843 12155 840 -272 2172 C ATOM 597 CD2 LEU A 104 9.972 37.359 13.361 1.00140.46 C ANISOU 597 CD2 LEU A 104 20560 20357 12450 631 -221 1886 C ATOM 598 N SER A 105 7.347 39.078 17.932 1.00124.05 N ANISOU 598 N SER A 105 18039 18445 10651 866 -451 2094 N ATOM 599 CA SER A 105 7.396 39.901 19.137 1.00121.74 C ANISOU 599 CA SER A 105 17717 18023 10516 1011 -424 2127 C ATOM 600 C SER A 105 7.485 39.018 20.385 1.00121.46 C ANISOU 600 C SER A 105 17608 17928 10613 849 -503 2008 C ATOM 601 O SER A 105 8.440 39.159 21.146 1.00119.70 O ANISOU 601 O SER A 105 17448 17418 10614 842 -441 1938 O ATOM 602 CB SER A 105 6.183 40.824 19.216 1.00126.26 C ANISOU 602 CB SER A 105 18191 18864 10917 1246 -463 2280 C ATOM 603 OG SER A 105 6.372 41.990 18.433 1.00135.69 O ANISOU 603 OG SER A 105 19512 19976 12069 1459 -363 2399 O ATOM 604 N MET A 106 6.529 38.068 20.556 1.00116.83 N ANISOU 604 N MET A 106 16895 17619 9877 692 -643 1991 N ATOM 605 CA MET A 106 6.441 37.145 21.698 1.00115.01 C ANISOU 605 CA MET A 106 16595 17376 9728 511 -739 1902 C ATOM 606 C MET A 106 7.651 36.243 21.923 1.00115.92 C ANISOU 606 C MET A 106 16849 17165 10031 342 -713 1745 C ATOM 607 O MET A 106 7.839 35.766 23.036 1.00114.29 O ANISOU 607 O MET A 106 16612 16862 9951 255 -758 1679 O ATOM 608 CB MET A 106 5.113 36.360 21.717 1.00118.65 C ANISOU 608 CB MET A 106 16896 18234 9950 342 -902 1946 C ATOM 609 CG MET A 106 3.872 37.243 21.891 1.00123.67 C ANISOU 609 CG MET A 106 17333 19251 10405 546 -934 2105 C ATOM 610 SD MET A 106 3.906 38.461 23.253 1.00126.93 S ANISOU 610 SD MET A 106 17685 19572 10972 853 -865 2152 S ATOM 611 CE MET A 106 4.127 39.975 22.347 1.00124.36 C ANISOU 611 CE MET A 106 17491 19139 10621 1198 -730 2256 C ATOM 612 N ASP A 107 8.478 36.028 20.891 1.00111.70 N ANISOU 612 N ASP A 107 16461 16479 9502 321 -638 1689 N ATOM 613 CA ASP A 107 9.705 35.243 21.005 1.00110.09 C ANISOU 613 CA ASP A 107 16390 15990 9451 224 -597 1545 C ATOM 614 C ASP A 107 10.806 36.150 21.569 1.00111.07 C ANISOU 614 C ASP A 107 16531 15861 9810 366 -459 1546 C ATOM 615 O ASP A 107 11.526 35.744 22.481 1.00109.62 O ANISOU 615 O ASP A 107 16359 15494 9798 315 -454 1457 O ATOM 616 CB ASP A 107 10.099 34.647 19.639 1.00113.11 C ANISOU 616 CB ASP A 107 16911 16362 9704 170 -572 1487 C ATOM 617 CG ASP A 107 11.470 33.999 19.590 1.00122.19 C ANISOU 617 CG ASP A 107 18199 17244 10984 151 -499 1349 C ATOM 618 OD1 ASP A 107 12.431 34.680 19.173 1.00122.29 O ANISOU 618 OD1 ASP A 107 18237 17143 11083 277 -353 1367 O ATOM 619 OD2 ASP A 107 11.577 32.801 19.941 1.00127.27 O ANISOU 619 OD2 ASP A 107 18930 17804 11623 12 -592 1230 O ATOM 620 N TYR A 108 10.907 37.385 21.046 1.00106.44 N ANISOU 620 N TYR A 108 15954 15271 9217 530 -357 1656 N ATOM 621 CA TYR A 108 11.896 38.369 21.476 1.00104.79 C ANISOU 621 CA TYR A 108 15786 14829 9200 630 -236 1679 C ATOM 622 C TYR A 108 11.567 39.040 22.815 1.00106.69 C ANISOU 622 C TYR A 108 15961 15020 9554 710 -267 1708 C ATOM 623 O TYR A 108 12.484 39.290 23.596 1.00105.11 O ANISOU 623 O TYR A 108 15786 14605 9546 699 -214 1659 O ATOM 624 CB TYR A 108 12.179 39.396 20.368 1.00106.73 C ANISOU 624 CB TYR A 108 16111 15059 9381 744 -124 1792 C ATOM 625 CG TYR A 108 13.174 38.903 19.337 1.00108.22 C ANISOU 625 CG TYR A 108 16374 15195 9550 676 -38 1740 C ATOM 626 CD1 TYR A 108 14.543 38.927 19.591 1.00109.70 C ANISOU 626 CD1 TYR A 108 16590 15187 9904 637 62 1684 C ATOM 627 CD2 TYR A 108 12.747 38.402 18.111 1.00109.72 C ANISOU 627 CD2 TYR A 108 16594 15561 9534 657 -57 1745 C ATOM 628 CE1 TYR A 108 15.465 38.484 18.642 1.00111.04 C ANISOU 628 CE1 TYR A 108 16805 15357 10029 606 149 1642 C ATOM 629 CE2 TYR A 108 13.658 37.944 17.158 1.00110.99 C ANISOU 629 CE2 TYR A 108 16826 15691 9653 625 25 1690 C ATOM 630 CZ TYR A 108 15.018 37.987 17.428 1.00116.95 C ANISOU 630 CZ TYR A 108 17597 16270 10570 612 133 1640 C ATOM 631 OH TYR A 108 15.927 37.538 16.498 1.00116.63 O ANISOU 631 OH TYR A 108 17605 16246 10464 610 222 1591 O ATOM 632 N VAL A 109 10.275 39.313 23.089 1.00103.11 N ANISOU 632 N VAL A 109 15418 14792 8968 795 -353 1785 N ATOM 633 CA VAL A 109 9.817 39.938 24.340 1.00102.22 C ANISOU 633 CA VAL A 109 15239 14681 8917 910 -388 1812 C ATOM 634 C VAL A 109 9.956 38.966 25.537 1.00102.88 C ANISOU 634 C VAL A 109 15240 14735 9114 760 -464 1701 C ATOM 635 O VAL A 109 10.558 39.348 26.541 1.00101.49 O ANISOU 635 O VAL A 109 15079 14370 9111 792 -434 1659 O ATOM 636 CB VAL A 109 8.399 40.591 24.230 1.00107.79 C ANISOU 636 CB VAL A 109 15858 15684 9411 1099 -445 1941 C ATOM 637 CG1 VAL A 109 7.945 41.194 25.561 1.00107.39 C ANISOU 637 CG1 VAL A 109 15745 15653 9406 1251 -479 1956 C ATOM 638 CG2 VAL A 109 8.364 41.657 23.137 1.00109.07 C ANISOU 638 CG2 VAL A 109 16137 15829 9477 1278 -364 2059 C ATOM 639 N ALA A 110 9.432 37.721 25.418 1.00 97.96 N ANISOU 639 N ALA A 110 14550 14284 8387 582 -568 1657 N ATOM 640 CA ALA A 110 9.485 36.698 26.475 1.00 96.02 C ANISOU 640 CA ALA A 110 14250 14015 8219 418 -656 1568 C ATOM 641 C ALA A 110 10.890 36.261 26.852 1.00 96.67 C ANISOU 641 C ALA A 110 14430 13785 8515 347 -595 1448 C ATOM 642 O ALA A 110 11.150 36.063 28.040 1.00 95.39 O ANISOU 642 O ALA A 110 14225 13538 8482 317 -623 1399 O ATOM 643 CB ALA A 110 8.654 35.489 26.099 1.00 97.51 C ANISOU 643 CB ALA A 110 14400 14425 8225 213 -786 1560 C ATOM 644 N SER A 111 11.787 36.092 25.858 1.00 91.55 N ANISOU 644 N SER A 111 13898 12999 7886 331 -512 1406 N ATOM 645 CA SER A 111 13.178 35.702 26.099 1.00 89.65 C ANISOU 645 CA SER A 111 13729 12515 7818 295 -442 1302 C ATOM 646 C SER A 111 13.970 36.818 26.793 1.00 91.64 C ANISOU 646 C SER A 111 13963 12605 8252 396 -346 1324 C ATOM 647 O SER A 111 14.814 36.523 27.636 1.00 91.05 O ANISOU 647 O SER A 111 13876 12387 8330 357 -334 1247 O ATOM 648 CB SER A 111 13.857 35.260 24.810 1.00 92.91 C ANISOU 648 CB SER A 111 14251 12886 8164 278 -376 1261 C ATOM 649 OG SER A 111 13.478 33.938 24.469 1.00 99.48 O ANISOU 649 OG SER A 111 15154 13774 8871 152 -479 1186 O ATOM 650 N THR A 112 13.665 38.089 26.475 1.00 86.74 N ANISOU 650 N THR A 112 13355 12003 7599 521 -291 1429 N ATOM 651 CA THR A 112 14.284 39.251 27.115 1.00 85.40 C ANISOU 651 CA THR A 112 13215 11661 7572 599 -220 1459 C ATOM 652 C THR A 112 13.738 39.348 28.544 1.00 87.53 C ANISOU 652 C THR A 112 13409 11948 7901 633 -302 1437 C ATOM 653 O THR A 112 14.503 39.604 29.475 1.00 86.57 O ANISOU 653 O THR A 112 13290 11666 7938 613 -281 1386 O ATOM 654 CB THR A 112 14.017 40.512 26.287 1.00 90.92 C ANISOU 654 CB THR A 112 14003 12355 8186 726 -155 1584 C ATOM 655 OG1 THR A 112 14.575 40.317 24.992 1.00 90.76 O ANISOU 655 OG1 THR A 112 14037 12342 8107 678 -78 1603 O ATOM 656 CG2 THR A 112 14.608 41.770 26.904 1.00 88.01 C ANISOU 656 CG2 THR A 112 13724 11772 7941 785 -98 1621 C ATOM 657 N ALA A 113 12.417 39.096 28.714 1.00 83.38 N ANISOU 657 N ALA A 113 12800 11652 7229 674 -399 1477 N ATOM 658 CA ALA A 113 11.732 39.103 30.012 1.00 82.14 C ANISOU 658 CA ALA A 113 12541 11587 7079 716 -482 1469 C ATOM 659 C ALA A 113 12.326 38.048 30.928 1.00 83.29 C ANISOU 659 C ALA A 113 12640 11654 7355 558 -527 1362 C ATOM 660 O ALA A 113 12.438 38.294 32.124 1.00 81.88 O ANISOU 660 O ALA A 113 12417 11422 7271 590 -548 1332 O ATOM 661 CB ALA A 113 10.242 38.860 29.833 1.00 83.74 C ANISOU 661 CB ALA A 113 12630 12124 7065 755 -576 1547 C ATOM 662 N SER A 114 12.742 36.896 30.359 1.00 79.25 N ANISOU 662 N SER A 114 12158 11119 6835 406 -542 1303 N ATOM 663 CA SER A 114 13.380 35.806 31.086 1.00 78.02 C ANISOU 663 CA SER A 114 11998 10862 6784 277 -584 1203 C ATOM 664 C SER A 114 14.733 36.243 31.642 1.00 80.08 C ANISOU 664 C SER A 114 12285 10898 7245 309 -496 1144 C ATOM 665 O SER A 114 14.927 36.131 32.850 1.00 79.00 O ANISOU 665 O SER A 114 12092 10717 7209 294 -533 1104 O ATOM 666 CB SER A 114 13.495 34.560 30.218 1.00 82.77 C ANISOU 666 CB SER A 114 12682 11469 7299 149 -621 1153 C ATOM 667 OG SER A 114 12.238 33.912 30.116 1.00 94.79 O ANISOU 667 OG SER A 114 14166 13204 8645 45 -744 1195 O ATOM 668 N ILE A 115 15.630 36.815 30.807 1.00 76.24 N ANISOU 668 N ILE A 115 11867 10299 6801 346 -383 1152 N ATOM 669 CA ILE A 115 16.920 37.317 31.304 1.00 75.54 C ANISOU 669 CA ILE A 115 11781 10042 6881 345 -302 1115 C ATOM 670 C ILE A 115 16.693 38.472 32.281 1.00 79.03 C ANISOU 670 C ILE A 115 12210 10427 7390 412 -309 1149 C ATOM 671 O ILE A 115 17.425 38.590 33.261 1.00 78.20 O ANISOU 671 O ILE A 115 12074 10221 7417 380 -306 1097 O ATOM 672 CB ILE A 115 17.979 37.641 30.198 1.00 79.26 C ANISOU 672 CB ILE A 115 12307 10446 7361 338 -179 1132 C ATOM 673 CG1 ILE A 115 19.405 37.759 30.798 1.00 79.28 C ANISOU 673 CG1 ILE A 115 12266 10338 7519 289 -115 1082 C ATOM 674 CG2 ILE A 115 17.610 38.877 29.351 1.00 80.96 C ANISOU 674 CG2 ILE A 115 12595 10663 7503 403 -119 1244 C ATOM 675 CD1 ILE A 115 20.538 37.371 29.876 1.00 87.76 C ANISOU 675 CD1 ILE A 115 13336 11428 8579 269 -16 1065 C ATOM 676 N PHE A 116 15.655 39.290 32.034 1.00 75.84 N ANISOU 676 N PHE A 116 11839 10100 6878 521 -326 1232 N ATOM 677 CA PHE A 116 15.347 40.417 32.904 1.00 75.83 C ANISOU 677 CA PHE A 116 11870 10037 6906 632 -339 1258 C ATOM 678 C PHE A 116 14.813 40.012 34.277 1.00 77.07 C ANISOU 678 C PHE A 116 11923 10278 7083 648 -432 1209 C ATOM 679 O PHE A 116 15.250 40.594 35.267 1.00 75.94 O ANISOU 679 O PHE A 116 11801 10012 7040 672 -432 1170 O ATOM 680 CB PHE A 116 14.524 41.502 32.187 1.00 79.27 C ANISOU 680 CB PHE A 116 12403 10510 7207 793 -318 1365 C ATOM 681 CG PHE A 116 15.338 42.379 31.251 1.00 82.16 C ANISOU 681 CG PHE A 116 12917 10701 7600 777 -217 1422 C ATOM 682 CD1 PHE A 116 16.732 42.367 31.288 1.00 85.34 C ANISOU 682 CD1 PHE A 116 13339 10942 8146 627 -150 1379 C ATOM 683 CD2 PHE A 116 14.711 43.247 30.365 1.00 85.82 C ANISOU 683 CD2 PHE A 116 13494 11183 7932 912 -190 1530 C ATOM 684 CE1 PHE A 116 17.478 43.185 30.436 1.00 87.51 C ANISOU 684 CE1 PHE A 116 13734 11088 8426 579 -59 1450 C ATOM 685 CE2 PHE A 116 15.461 44.076 29.522 1.00 89.70 C ANISOU 685 CE2 PHE A 116 14135 11508 8439 877 -100 1600 C ATOM 686 CZ PHE A 116 16.838 44.037 29.560 1.00 87.70 C ANISOU 686 CZ PHE A 116 13891 11106 8324 695 -35 1563 C ATOM 687 N SER A 117 13.953 38.959 34.342 1.00 72.33 N ANISOU 687 N SER A 117 11215 9883 6383 603 -515 1210 N ATOM 688 CA SER A 117 13.424 38.386 35.586 1.00 70.78 C ANISOU 688 CA SER A 117 10902 9805 6185 580 -609 1179 C ATOM 689 C SER A 117 14.588 37.837 36.415 1.00 73.21 C ANISOU 689 C SER A 117 11199 9948 6668 470 -603 1083 C ATOM 690 O SER A 117 14.646 38.097 37.617 1.00 72.88 O ANISOU 690 O SER A 117 11112 9888 6689 503 -634 1050 O ATOM 691 CB SER A 117 12.419 37.272 35.302 1.00 73.80 C ANISOU 691 CB SER A 117 11194 10429 6416 484 -700 1214 C ATOM 692 OG SER A 117 11.147 37.788 34.948 1.00 82.42 O ANISOU 692 OG SER A 117 12230 11764 7323 602 -731 1311 O ATOM 693 N VAL A 118 15.539 37.129 35.759 1.00 68.43 N ANISOU 693 N VAL A 118 10637 9237 6126 365 -560 1039 N ATOM 694 CA VAL A 118 16.739 36.575 36.396 1.00 67.10 C ANISOU 694 CA VAL A 118 10452 8938 6103 290 -546 956 C ATOM 695 C VAL A 118 17.644 37.705 36.939 1.00 70.09 C ANISOU 695 C VAL A 118 10847 9173 6611 324 -480 937 C ATOM 696 O VAL A 118 17.983 37.681 38.123 1.00 68.88 O ANISOU 696 O VAL A 118 10640 8987 6545 309 -515 888 O ATOM 697 CB VAL A 118 17.472 35.534 35.498 1.00 70.91 C ANISOU 697 CB VAL A 118 10982 9377 6582 219 -515 915 C ATOM 698 CG1 VAL A 118 18.793 35.079 36.111 1.00 70.35 C ANISOU 698 CG1 VAL A 118 10884 9200 6646 191 -487 838 C ATOM 699 CG2 VAL A 118 16.583 34.323 35.239 1.00 70.79 C ANISOU 699 CG2 VAL A 118 10989 9468 6441 148 -613 918 C ATOM 700 N PHE A 119 17.956 38.719 36.106 1.00 66.84 N ANISOU 700 N PHE A 119 10522 8680 6193 355 -397 984 N ATOM 701 CA PHE A 119 18.772 39.875 36.495 1.00 67.06 C ANISOU 701 CA PHE A 119 10607 8555 6317 344 -345 982 C ATOM 702 C PHE A 119 18.120 40.724 37.576 1.00 72.87 C ANISOU 702 C PHE A 119 11378 9261 7047 438 -403 977 C ATOM 703 O PHE A 119 18.832 41.271 38.416 1.00 72.69 O ANISOU 703 O PHE A 119 11378 9120 7121 396 -403 933 O ATOM 704 CB PHE A 119 19.085 40.753 35.289 1.00 69.54 C ANISOU 704 CB PHE A 119 11036 8792 6595 341 -256 1058 C ATOM 705 CG PHE A 119 20.201 41.739 35.521 1.00 71.41 C ANISOU 705 CG PHE A 119 11338 8866 6927 248 -201 1063 C ATOM 706 CD1 PHE A 119 21.529 41.331 35.490 1.00 74.29 C ANISOU 706 CD1 PHE A 119 11614 9234 7379 112 -148 1030 C ATOM 707 CD2 PHE A 119 19.929 43.084 35.735 1.00 74.18 C ANISOU 707 CD2 PHE A 119 11852 9072 7261 294 -207 1106 C ATOM 708 CE1 PHE A 119 22.565 42.248 35.686 1.00 76.05 C ANISOU 708 CE1 PHE A 119 11879 9347 7670 -19 -105 1050 C ATOM 709 CE2 PHE A 119 20.967 44.003 35.920 1.00 77.90 C ANISOU 709 CE2 PHE A 119 12416 9378 7805 158 -171 1118 C ATOM 710 CZ PHE A 119 22.278 43.578 35.899 1.00 75.83 C ANISOU 710 CZ PHE A 119 12033 9151 7629 -19 -122 1095 C ATOM 711 N ILE A 120 16.780 40.849 37.550 1.00 71.02 N ANISOU 711 N ILE A 120 11146 9153 6683 573 -454 1023 N ATOM 712 CA ILE A 120 16.051 41.608 38.564 1.00 71.92 C ANISOU 712 CA ILE A 120 11289 9284 6755 716 -508 1017 C ATOM 713 C ILE A 120 15.955 40.823 39.900 1.00 75.75 C ANISOU 713 C ILE A 120 11631 9869 7282 682 -585 949 C ATOM 714 O ILE A 120 15.973 41.440 40.974 1.00 75.44 O ANISOU 714 O ILE A 120 11618 9777 7268 750 -615 905 O ATOM 715 CB ILE A 120 14.724 42.252 38.034 1.00 76.27 C ANISOU 715 CB ILE A 120 11895 9959 7127 919 -521 1103 C ATOM 716 CG1 ILE A 120 14.334 43.531 38.803 1.00 78.23 C ANISOU 716 CG1 ILE A 120 12276 10118 7328 1118 -541 1097 C ATOM 717 CG2 ILE A 120 13.557 41.268 37.926 1.00 76.43 C ANISOU 717 CG2 ILE A 120 11747 10281 7010 940 -586 1143 C ATOM 718 CD1 ILE A 120 15.075 44.777 38.391 1.00 88.46 C ANISOU 718 CD1 ILE A 120 13819 11119 8673 1123 -483 1111 C ATOM 719 N LEU A 121 15.927 39.458 39.818 1.00 71.91 N ANISOU 719 N LEU A 121 11020 9504 6797 569 -618 938 N ATOM 720 CA LEU A 121 15.911 38.537 40.970 1.00 70.92 C ANISOU 720 CA LEU A 121 10773 9465 6708 505 -692 890 C ATOM 721 C LEU A 121 17.270 38.566 41.677 1.00 75.18 C ANISOU 721 C LEU A 121 11314 9840 7412 424 -668 810 C ATOM 722 O LEU A 121 17.299 38.650 42.901 1.00 74.61 O ANISOU 722 O LEU A 121 11191 9784 7375 442 -716 767 O ATOM 723 CB LEU A 121 15.553 37.095 40.536 1.00 70.28 C ANISOU 723 CB LEU A 121 10625 9509 6569 391 -741 911 C ATOM 724 CG LEU A 121 15.800 35.947 41.534 1.00 73.65 C ANISOU 724 CG LEU A 121 10972 9967 7045 288 -814 869 C ATOM 725 CD1 LEU A 121 14.706 35.861 42.571 1.00 73.68 C ANISOU 725 CD1 LEU A 121 10868 10174 6951 320 -902 905 C ATOM 726 CD2 LEU A 121 15.904 34.619 40.817 1.00 75.34 C ANISOU 726 CD2 LEU A 121 11220 10179 7226 164 -841 871 C ATOM 727 N CYS A 122 18.385 38.495 40.909 1.00 72.34 N ANISOU 727 N CYS A 122 10995 9356 7134 338 -594 796 N ATOM 728 CA CYS A 122 19.751 38.533 41.437 1.00 72.15 C ANISOU 728 CA CYS A 122 10942 9227 7244 251 -564 735 C ATOM 729 C CYS A 122 20.059 39.848 42.133 1.00 78.17 C ANISOU 729 C CYS A 122 11775 9874 8052 264 -559 713 C ATOM 730 O CYS A 122 20.733 39.821 43.164 1.00 78.11 O ANISOU 730 O CYS A 122 11711 9843 8125 210 -588 653 O ATOM 731 CB CYS A 122 20.782 38.217 40.361 1.00 72.37 C ANISOU 731 CB CYS A 122 10976 9212 7308 177 -480 742 C ATOM 732 SG CYS A 122 22.498 38.464 40.888 1.00 76.52 S ANISOU 732 SG CYS A 122 11432 9677 7965 67 -432 693 S ATOM 733 N ILE A 123 19.578 40.993 41.588 1.00 76.13 N ANISOU 733 N ILE A 123 11661 9533 7732 336 -532 760 N ATOM 734 CA ILE A 123 19.794 42.312 42.208 1.00 77.19 C ANISOU 734 CA ILE A 123 11934 9509 7884 356 -541 736 C ATOM 735 C ILE A 123 19.127 42.372 43.608 1.00 81.58 C ANISOU 735 C ILE A 123 12458 10128 8410 467 -627 677 C ATOM 736 O ILE A 123 19.724 42.909 44.551 1.00 81.20 O ANISOU 736 O ILE A 123 12453 9979 8420 421 -656 611 O ATOM 737 CB ILE A 123 19.459 43.501 41.252 1.00 81.42 C ANISOU 737 CB ILE A 123 12679 9909 8346 423 -496 807 C ATOM 738 CG1 ILE A 123 20.544 43.623 40.160 1.00 82.09 C ANISOU 738 CG1 ILE A 123 12794 9912 8486 253 -408 855 C ATOM 739 CG2 ILE A 123 19.268 44.836 42.009 1.00 83.78 C ANISOU 739 CG2 ILE A 123 13187 10032 8615 510 -536 777 C ATOM 740 CD1 ILE A 123 20.561 44.920 39.339 1.00 92.21 C ANISOU 740 CD1 ILE A 123 14311 11010 9715 254 -364 933 C ATOM 741 N ASP A 124 17.931 41.747 43.746 1.00 78.52 N ANISOU 741 N ASP A 124 11977 9936 7921 592 -672 705 N ATOM 742 CA ASP A 124 17.202 41.654 45.010 1.00 78.65 C ANISOU 742 CA ASP A 124 11921 10083 7880 702 -749 668 C ATOM 743 C ASP A 124 17.995 40.805 45.998 1.00 82.65 C ANISOU 743 C ASP A 124 12291 10618 8494 569 -785 604 C ATOM 744 O ASP A 124 18.386 41.318 47.041 1.00 83.36 O ANISOU 744 O ASP A 124 12408 10644 8621 576 -817 535 O ATOM 745 CB ASP A 124 15.788 41.082 44.801 1.00 80.35 C ANISOU 745 CB ASP A 124 12030 10555 7942 818 -786 739 C ATOM 746 CG ASP A 124 15.136 40.584 46.078 1.00 90.55 C ANISOU 746 CG ASP A 124 13178 12054 9173 872 -865 721 C ATOM 747 OD1 ASP A 124 14.569 41.416 46.816 1.00 92.15 O ANISOU 747 OD1 ASP A 124 13425 12301 9287 1054 -890 698 O ATOM 748 OD2 ASP A 124 15.226 39.364 46.354 1.00 95.02 O ANISOU 748 OD2 ASP A 124 13604 12731 9770 737 -902 729 O ATOM 749 N ARG A 125 18.256 39.542 45.681 1.00 78.20 N ANISOU 749 N ARG A 125 11607 10137 7969 460 -786 623 N ATOM 750 CA ARG A 125 19.008 38.674 46.590 1.00 77.73 C ANISOU 750 CA ARG A 125 11432 10106 7998 362 -822 572 C ATOM 751 C ARG A 125 20.291 39.327 47.122 1.00 84.03 C ANISOU 751 C ARG A 125 12257 10761 8909 284 -801 502 C ATOM 752 O ARG A 125 20.717 39.060 48.246 1.00 84.11 O ANISOU 752 O ARG A 125 12186 10808 8964 254 -848 449 O ATOM 753 CB ARG A 125 19.342 37.346 45.906 1.00 77.51 C ANISOU 753 CB ARG A 125 11343 10114 7994 270 -812 598 C ATOM 754 CG ARG A 125 18.571 36.155 46.452 1.00 89.07 C ANISOU 754 CG ARG A 125 12720 11732 9391 256 -895 627 C ATOM 755 CD ARG A 125 17.601 35.605 45.419 1.00103.32 C ANISOU 755 CD ARG A 125 14552 13624 11082 246 -905 700 C ATOM 756 NE ARG A 125 16.299 35.295 46.002 1.00113.60 N ANISOU 756 NE ARG A 125 15777 15133 12254 264 -988 756 N ATOM 757 CZ ARG A 125 15.656 34.146 45.826 1.00125.71 C ANISOU 757 CZ ARG A 125 17284 16781 13700 162 -1055 813 C ATOM 758 NH1 ARG A 125 16.194 33.189 45.082 1.00111.00 N ANISOU 758 NH1 ARG A 125 15499 14808 11868 65 -1051 805 N ATOM 759 NH2 ARG A 125 14.474 33.951 46.395 1.00109.92 N ANISOU 759 NH2 ARG A 125 15187 15013 11563 155 -1130 881 N ATOM 760 N TYR A 126 20.895 40.178 46.300 1.00 82.49 N ANISOU 760 N TYR A 126 12173 10421 8746 233 -734 512 N ATOM 761 CA TYR A 126 22.144 40.853 46.608 1.00 84.01 C ANISOU 761 CA TYR A 126 12396 10496 9028 105 -714 466 C ATOM 762 C TYR A 126 21.924 41.899 47.694 1.00 89.96 C ANISOU 762 C TYR A 126 13258 11166 9757 150 -773 405 C ATOM 763 O TYR A 126 22.657 41.920 48.678 1.00 89.73 O ANISOU 763 O TYR A 126 13172 11138 9783 67 -812 340 O ATOM 764 CB TYR A 126 22.707 41.497 45.335 1.00 86.74 C ANISOU 764 CB TYR A 126 12844 10727 9385 19 -629 519 C ATOM 765 CG TYR A 126 23.962 42.303 45.584 1.00 90.97 C ANISOU 765 CG TYR A 126 13417 11159 9987 -159 -614 494 C ATOM 766 CD1 TYR A 126 25.205 41.685 45.672 1.00 93.30 C ANISOU 766 CD1 TYR A 126 13541 11554 10354 -296 -588 483 C ATOM 767 CD2 TYR A 126 23.907 43.688 45.732 1.00 93.69 C ANISOU 767 CD2 TYR A 126 13979 11315 10304 -194 -632 486 C ATOM 768 CE1 TYR A 126 26.364 42.422 45.899 1.00 96.56 C ANISOU 768 CE1 TYR A 126 13957 11924 10807 -494 -580 473 C ATOM 769 CE2 TYR A 126 25.058 44.436 45.969 1.00 96.47 C ANISOU 769 CE2 TYR A 126 14381 11571 10701 -411 -634 470 C ATOM 770 CZ TYR A 126 26.288 43.799 46.047 1.00106.21 C ANISOU 770 CZ TYR A 126 15402 12950 12004 -577 -607 469 C ATOM 771 OH TYR A 126 27.437 44.523 46.276 1.00110.62 O ANISOU 771 OH TYR A 126 15977 13467 12589 -824 -614 467 O ATOM 772 N ARG A 127 20.906 42.761 47.518 1.00 88.66 N ANISOU 772 N ARG A 127 13257 10935 9493 301 -782 422 N ATOM 773 CA ARG A 127 20.557 43.783 48.507 1.00 90.29 C ANISOU 773 CA ARG A 127 13613 11050 9642 402 -842 355 C ATOM 774 C ARG A 127 19.906 43.157 49.751 1.00 93.47 C ANISOU 774 C ARG A 127 13871 11645 9998 518 -912 310 C ATOM 775 O ARG A 127 20.037 43.707 50.846 1.00 93.83 O ANISOU 775 O ARG A 127 13978 11647 10026 549 -968 228 O ATOM 776 CB ARG A 127 19.724 44.945 47.901 1.00 93.12 C ANISOU 776 CB ARG A 127 14222 11270 9888 571 -828 388 C ATOM 777 CG ARG A 127 18.434 44.557 47.162 1.00102.37 C ANISOU 777 CG ARG A 127 15340 12608 10947 763 -807 472 C ATOM 778 CD ARG A 127 17.252 45.403 47.596 1.00113.42 C ANISOU 778 CD ARG A 127 16880 14029 12184 1051 -846 462 C ATOM 779 NE ARG A 127 16.860 45.105 48.976 1.00123.13 N ANISOU 779 NE ARG A 127 17995 15422 13368 1147 -914 393 N ATOM 780 CZ ARG A 127 15.873 44.282 49.316 1.00134.04 C ANISOU 780 CZ ARG A 127 19165 17107 14655 1261 -940 432 C ATOM 781 NH1 ARG A 127 15.604 44.053 50.594 1.00113.71 N ANISOU 781 NH1 ARG A 127 16487 14683 12035 1331 -999 377 N ATOM 782 NH2 ARG A 127 15.146 43.684 48.380 1.00123.32 N ANISOU 782 NH2 ARG A 127 17698 15921 13237 1286 -913 534 N ATOM 783 N SER A 128 19.251 41.984 49.580 1.00 88.73 N ANISOU 783 N SER A 128 13087 11257 9368 558 -915 368 N ATOM 784 CA SER A 128 18.614 41.200 50.643 1.00 88.00 C ANISOU 784 CA SER A 128 12833 11382 9221 627 -981 359 C ATOM 785 C SER A 128 19.705 40.622 51.550 1.00 92.02 C ANISOU 785 C SER A 128 13230 11892 9840 481 -1011 299 C ATOM 786 O SER A 128 19.532 40.555 52.769 1.00 92.06 O ANISOU 786 O SER A 128 13173 11993 9811 530 -1073 252 O ATOM 787 CB SER A 128 17.786 40.066 50.043 1.00 90.29 C ANISOU 787 CB SER A 128 12989 11865 9452 633 -981 452 C ATOM 788 OG SER A 128 17.131 39.294 51.037 1.00 98.28 O ANISOU 788 OG SER A 128 13849 13099 10395 665 -1049 467 O ATOM 789 N VAL A 129 20.829 40.215 50.941 1.00 88.04 N ANISOU 789 N VAL A 129 12691 11307 9451 319 -967 306 N ATOM 790 CA VAL A 129 21.997 39.666 51.622 1.00 87.39 C ANISOU 790 CA VAL A 129 12491 11248 9467 192 -985 263 C ATOM 791 C VAL A 129 22.732 40.803 52.371 1.00 93.59 C ANISOU 791 C VAL A 129 13365 11916 10279 126 -1010 177 C ATOM 792 O VAL A 129 23.023 40.653 53.561 1.00 93.48 O ANISOU 792 O VAL A 129 13273 11973 10271 113 -1071 119 O ATOM 793 CB VAL A 129 22.883 38.870 50.609 1.00 90.01 C ANISOU 793 CB VAL A 129 12752 11571 9876 85 -922 306 C ATOM 794 CG1 VAL A 129 24.358 38.846 50.997 1.00 90.04 C ANISOU 794 CG1 VAL A 129 12668 11575 9969 -46 -913 264 C ATOM 795 CG2 VAL A 129 22.353 37.454 50.418 1.00 88.62 C ANISOU 795 CG2 VAL A 129 12486 11515 9672 128 -940 359 C ATOM 796 N GLN A 130 22.968 41.949 51.685 1.00 91.66 N ANISOU 796 N GLN A 130 13305 11488 10035 78 -972 174 N ATOM 797 CA GLN A 130 23.679 43.124 52.211 1.00 93.16 C ANISOU 797 CA GLN A 130 13643 11520 10235 -32 -1004 100 C ATOM 798 C GLN A 130 22.984 43.845 53.370 1.00 97.35 C ANISOU 798 C GLN A 130 14302 12013 10673 108 -1083 14 C ATOM 799 O GLN A 130 23.614 44.082 54.403 1.00 96.60 O ANISOU 799 O GLN A 130 14197 11914 10591 21 -1143 -67 O ATOM 800 CB GLN A 130 24.053 44.108 51.081 1.00 95.77 C ANISOU 800 CB GLN A 130 14169 11646 10572 -139 -948 141 C ATOM 801 CG GLN A 130 25.082 43.569 50.074 1.00111.87 C ANISOU 801 CG GLN A 130 16072 13739 12694 -317 -870 212 C ATOM 802 CD GLN A 130 26.502 43.509 50.594 1.00130.62 C ANISOU 802 CD GLN A 130 18314 16179 15135 -542 -885 181 C ATOM 803 OE1 GLN A 130 26.827 42.765 51.529 1.00124.54 O ANISOU 803 OE1 GLN A 130 17363 15565 14392 -533 -928 137 O ATOM 804 NE2 GLN A 130 27.394 44.248 49.948 1.00123.91 N ANISOU 804 NE2 GLN A 130 17537 15243 14301 -756 -849 218 N ATOM 805 N GLN A 131 21.702 44.200 53.197 1.00 94.83 N ANISOU 805 N GLN A 131 14099 11689 10243 338 -1084 32 N ATOM 806 CA GLN A 131 20.936 44.898 54.225 1.00 96.11 C ANISOU 806 CA GLN A 131 14390 11844 10282 533 -1150 -48 C ATOM 807 C GLN A 131 19.707 44.083 54.694 1.00 98.75 C ANISOU 807 C GLN A 131 14546 12459 10517 748 -1168 -11 C ATOM 808 O GLN A 131 18.646 44.145 54.064 1.00 97.96 O ANISOU 808 O GLN A 131 14472 12429 10320 924 -1139 56 O ATOM 809 CB GLN A 131 20.562 46.326 53.769 1.00 99.61 C ANISOU 809 CB GLN A 131 15180 12030 10636 645 -1149 -71 C ATOM 810 CG GLN A 131 20.051 47.225 54.903 1.00118.63 C ANISOU 810 CG GLN A 131 17791 14373 12910 844 -1226 -185 C ATOM 811 CD GLN A 131 19.784 48.661 54.500 1.00138.61 C ANISOU 811 CD GLN A 131 20727 16597 15342 963 -1237 -217 C ATOM 812 OE1 GLN A 131 20.019 49.093 53.361 1.00132.45 O ANISOU 812 OE1 GLN A 131 20095 15633 14599 874 -1188 -146 O ATOM 813 NE2 GLN A 131 19.289 49.441 55.445 1.00133.84 N ANISOU 813 NE2 GLN A 131 20334 15925 14596 1182 -1305 -325 N ATOM 814 N PRO A 132 19.824 43.325 55.813 1.00 94.66 N ANISOU 814 N PRO A 132 13836 12126 10005 727 -1218 -42 N ATOM 815 CA PRO A 132 18.660 42.556 56.297 1.00 93.79 C ANISOU 815 CA PRO A 132 13551 12303 9782 893 -1241 12 C ATOM 816 C PRO A 132 17.514 43.488 56.712 1.00 99.18 C ANISOU 816 C PRO A 132 14368 13041 10276 1182 -1263 -23 C ATOM 817 O PRO A 132 16.350 43.157 56.480 1.00 98.82 O ANISOU 817 O PRO A 132 14223 13218 10106 1344 -1253 59 O ATOM 818 CB PRO A 132 19.258 41.636 57.362 1.00 94.68 C ANISOU 818 CB PRO A 132 13467 12555 9953 774 -1290 -10 C ATOM 819 CG PRO A 132 20.472 42.339 57.831 1.00 99.91 C ANISOU 819 CG PRO A 132 14237 13026 10696 640 -1314 -118 C ATOM 820 CD PRO A 132 21.005 43.131 56.679 1.00 96.07 C ANISOU 820 CD PRO A 132 13940 12286 10277 543 -1260 -114 C ATOM 821 N LEU A 133 17.846 44.654 57.316 1.00 97.17 N ANISOU 821 N LEU A 133 14348 12592 9982 1251 -1299 -145 N ATOM 822 CA LEU A 133 16.877 45.661 57.759 1.00 98.70 C ANISOU 822 CA LEU A 133 14728 12795 9978 1569 -1324 -203 C ATOM 823 C LEU A 133 16.529 46.665 56.643 1.00106.87 C ANISOU 823 C LEU A 133 16040 13603 10963 1697 -1282 -179 C ATOM 824 O LEU A 133 17.016 47.804 56.623 1.00108.36 O ANISOU 824 O LEU A 133 16554 13471 11147 1698 -1303 -266 O ATOM 825 CB LEU A 133 17.377 46.320 59.063 1.00 99.30 C ANISOU 825 CB LEU A 133 14943 12773 10012 1591 -1399 -356 C ATOM 826 CG LEU A 133 17.359 45.451 60.308 1.00101.71 C ANISOU 826 CG LEU A 133 14984 13366 10295 1572 -1446 -374 C ATOM 827 CD1 LEU A 133 18.224 46.037 61.367 1.00102.70 C ANISOU 827 CD1 LEU A 133 15248 13343 10431 1490 -1517 -523 C ATOM 828 CD2 LEU A 133 15.952 45.261 60.836 1.00103.32 C ANISOU 828 CD2 LEU A 133 15059 13914 10286 1884 -1451 -333 C ATOM 829 N ARG A 134 15.671 46.216 55.711 1.00104.60 N ANISOU 829 N ARG A 134 15630 13486 10626 1792 -1229 -53 N ATOM 830 CA ARG A 134 15.177 47.023 54.595 1.00106.12 C ANISOU 830 CA ARG A 134 16041 13532 10749 1946 -1185 -3 C ATOM 831 C ARG A 134 13.689 47.309 54.865 1.00113.06 C ANISOU 831 C ARG A 134 16893 14688 11378 2347 -1192 26 C ATOM 832 O ARG A 134 12.887 47.429 53.933 1.00112.38 O ANISOU 832 O ARG A 134 16809 14694 11197 2503 -1151 124 O ATOM 833 CB ARG A 134 15.415 46.373 53.218 1.00104.81 C ANISOU 833 CB ARG A 134 15768 13352 10705 1746 -1119 117 C ATOM 834 CG ARG A 134 16.856 46.463 52.717 1.00114.62 C ANISOU 834 CG ARG A 134 17106 14295 12148 1419 -1096 94 C ATOM 835 CD ARG A 134 17.187 47.805 52.093 1.00127.89 C ANISOU 835 CD ARG A 134 19157 15621 13815 1439 -1084 71 C ATOM 836 NE ARG A 134 18.040 47.665 50.913 1.00137.46 N ANISOU 836 NE ARG A 134 20380 16683 15166 1177 -1023 143 N ATOM 837 CZ ARG A 134 18.541 48.686 50.225 1.00153.07 C ANISOU 837 CZ ARG A 134 22652 18349 17157 1097 -1006 153 C ATOM 838 NH1 ARG A 134 18.297 49.936 50.603 1.00142.25 N ANISOU 838 NH1 ARG A 134 21634 16740 15675 1258 -1054 86 N ATOM 839 NH2 ARG A 134 19.296 48.466 49.157 1.00138.13 N ANISOU 839 NH2 ARG A 134 20724 16382 15377 858 -944 231 N ATOM 840 N TYR A 135 13.346 47.464 56.172 1.00112.69 N ANISOU 840 N TYR A 135 16818 14794 11205 2527 -1245 -61 N ATOM 841 CA TYR A 135 12.026 47.796 56.728 1.00115.07 C ANISOU 841 CA TYR A 135 17079 15406 11236 2939 -1259 -55 C ATOM 842 C TYR A 135 11.625 49.215 56.284 1.00124.32 C ANISOU 842 C TYR A 135 18646 16332 12260 3273 -1252 -102 C ATOM 843 O TYR A 135 10.612 49.750 56.741 1.00125.79 O ANISOU 843 O TYR A 135 18880 16720 12195 3684 -1263 -122 O ATOM 844 CB TYR A 135 12.080 47.763 58.276 1.00116.79 C ANISOU 844 CB TYR A 135 17238 15762 11376 3017 -1320 -167 C ATOM 845 CG TYR A 135 12.949 48.856 58.866 1.00119.92 C ANISOU 845 CG TYR A 135 18017 15745 11803 3022 -1370 -344 C ATOM 846 CD1 TYR A 135 12.398 50.066 59.279 1.00124.50 C ANISOU 846 CD1 TYR A 135 18921 16219 12165 3414 -1399 -448 C ATOM 847 CD2 TYR A 135 14.329 48.697 58.972 1.00119.57 C ANISOU 847 CD2 TYR A 135 18026 15417 11988 2634 -1394 -405 C ATOM 848 CE1 TYR A 135 13.199 51.094 59.769 1.00126.58 C ANISOU 848 CE1 TYR A 135 19591 16060 12445 3387 -1459 -613 C ATOM 849 CE2 TYR A 135 15.138 49.719 59.460 1.00122.02 C ANISOU 849 CE2 TYR A 135 18695 15354 12314 2586 -1451 -558 C ATOM 850 CZ TYR A 135 14.568 50.914 59.861 1.00131.52 C ANISOU 850 CZ TYR A 135 20253 16416 13304 2948 -1489 -665 C ATOM 851 OH TYR A 135 15.359 51.920 60.350 1.00135.73 O ANISOU 851 OH TYR A 135 21181 16552 13837 2874 -1562 -821 O ATOM 852 N LEU A 136 12.452 49.817 55.403 1.00123.95 N ANISOU 852 N LEU A 136 18888 15851 12356 3097 -1234 -115 N ATOM 853 CA LEU A 136 12.289 51.132 54.788 1.00127.75 C ANISOU 853 CA LEU A 136 19801 16001 12737 3329 -1230 -140 C ATOM 854 C LEU A 136 11.417 51.026 53.507 1.00134.88 C ANISOU 854 C LEU A 136 20621 17067 13561 3483 -1165 18 C ATOM 855 O LEU A 136 11.444 51.928 52.657 1.00135.98 O ANISOU 855 O LEU A 136 21089 16908 13669 3584 -1147 40 O ATOM 856 CB LEU A 136 13.675 51.754 54.489 1.00128.17 C ANISOU 856 CB LEU A 136 20181 15534 12983 2991 -1250 -209 C ATOM 857 CG LEU A 136 14.596 51.076 53.461 1.00130.53 C ANISOU 857 CG LEU A 136 20330 15741 13526 2558 -1198 -113 C ATOM 858 CD1 LEU A 136 14.806 51.972 52.252 1.00131.72 C ANISOU 858 CD1 LEU A 136 20819 15544 13686 2541 -1166 -55 C ATOM 859 CD2 LEU A 136 15.939 50.748 54.080 1.00132.43 C ANISOU 859 CD2 LEU A 136 20517 15842 13959 2162 -1234 -193 C ATOM 860 N LYS A 137 10.681 49.931 53.349 1.00132.47 N ANISOU 860 N LYS A 137 19894 17223 13217 3475 -1137 133 N ATOM 861 CA LYS A 137 9.808 49.771 52.182 1.00133.57 C ANISOU 861 CA LYS A 137 19924 17569 13259 3605 -1086 283 C ATOM 862 C LYS A 137 10.466 49.290 50.883 1.00137.15 C ANISOU 862 C LYS A 137 20344 17853 13916 3255 -1037 374 C ATOM 863 O LYS A 137 9.985 49.575 49.786 1.00137.02 O ANISOU 863 O LYS A 137 20392 17841 13827 3370 -997 472 O ATOM 864 CB LYS A 137 8.991 51.046 51.951 1.00139.83 C ANISOU 864 CB LYS A 137 21032 18289 13807 4089 -1084 277 C ATOM 865 CG LYS A 137 7.653 51.065 52.672 1.00157.05 C ANISOU 865 CG LYS A 137 23025 20960 15687 4532 -1098 296 C ATOM 866 CD LYS A 137 7.736 50.345 54.008 1.00165.37 C ANISOU 866 CD LYS A 137 23812 22270 16749 4430 -1137 229 C ATOM 867 CE LYS A 137 6.391 49.756 54.402 1.00172.50 C ANISOU 867 CE LYS A 137 24316 23832 17396 4684 -1134 332 C ATOM 868 NZ LYS A 137 6.308 49.490 55.865 1.00177.48 N ANISOU 868 NZ LYS A 137 24797 24694 17945 4746 -1176 248 N ATOM 869 N TYR A 138 11.562 48.554 51.024 1.00133.22 N ANISOU 869 N TYR A 138 19737 17229 13653 2850 -1039 342 N ATOM 870 CA TYR A 138 12.276 47.925 49.909 1.00132.07 C ANISOU 870 CA TYR A 138 19516 16969 13697 2511 -992 417 C ATOM 871 C TYR A 138 12.108 46.431 49.601 1.00134.39 C ANISOU 871 C TYR A 138 19431 17577 14056 2289 -979 508 C ATOM 872 O TYR A 138 12.238 46.032 48.441 1.00133.32 O ANISOU 872 O TYR A 138 19255 17418 13984 2142 -936 592 O ATOM 873 CB TYR A 138 13.751 48.253 50.184 1.00133.64 C ANISOU 873 CB TYR A 138 19902 16777 14097 2223 -1002 318 C ATOM 874 CG TYR A 138 14.453 48.900 49.009 1.00137.07 C ANISOU 874 CG TYR A 138 20588 16870 14623 2079 -956 358 C ATOM 875 CD1 TYR A 138 14.736 50.262 49.006 1.00141.70 C ANISOU 875 CD1 TYR A 138 21587 17091 15163 2174 -976 304 C ATOM 876 CD2 TYR A 138 14.826 48.152 47.894 1.00136.56 C ANISOU 876 CD2 TYR A 138 20368 16844 14673 1847 -898 453 C ATOM 877 CE1 TYR A 138 15.382 50.865 47.927 1.00143.82 C ANISOU 877 CE1 TYR A 138 22091 17054 15502 2013 -937 360 C ATOM 878 CE2 TYR A 138 15.463 48.744 46.805 1.00138.30 C ANISOU 878 CE2 TYR A 138 20801 16787 14960 1715 -850 502 C ATOM 879 CZ TYR A 138 15.740 50.103 46.826 1.00148.86 C ANISOU 879 CZ TYR A 138 22532 17776 16253 1786 -869 464 C ATOM 880 OH TYR A 138 16.370 50.699 45.760 1.00151.08 O ANISOU 880 OH TYR A 138 23028 17787 16587 1628 -826 530 O ATOM 881 N ARG A 139 11.865 45.653 50.656 1.00130.59 N ANISOU 881 N ARG A 139 18710 17361 13549 2261 -1024 487 N ATOM 882 CA ARG A 139 11.535 44.237 50.570 1.00128.96 C ANISOU 882 CA ARG A 139 18174 17466 13358 2074 -1035 575 C ATOM 883 C ARG A 139 10.039 44.127 50.823 1.00133.15 C ANISOU 883 C ARG A 139 18519 18440 13632 2331 -1059 659 C ATOM 884 O ARG A 139 9.589 43.769 51.911 1.00133.04 O ANISOU 884 O ARG A 139 18332 18695 13522 2393 -1103 651 O ATOM 885 CB ARG A 139 12.312 43.435 51.613 1.00129.01 C ANISOU 885 CB ARG A 139 18049 17471 13498 1852 -1075 511 C ATOM 886 CG ARG A 139 12.319 41.936 51.364 1.00139.60 C ANISOU 886 CG ARG A 139 19142 18997 14903 1593 -1089 596 C ATOM 887 CD ARG A 139 13.149 41.583 50.140 1.00148.49 C ANISOU 887 CD ARG A 139 20339 19889 16191 1374 -1040 618 C ATOM 888 NE ARG A 139 13.982 40.405 50.366 1.00155.94 N ANISOU 888 NE ARG A 139 21167 20802 17284 1109 -1058 609 N ATOM 889 CZ ARG A 139 13.652 39.173 49.992 1.00169.82 C ANISOU 889 CZ ARG A 139 22778 22722 19026 962 -1081 691 C ATOM 890 NH1 ARG A 139 12.500 38.953 49.372 1.00154.86 N ANISOU 890 NH1 ARG A 139 20807 21060 16974 1017 -1091 791 N ATOM 891 NH2 ARG A 139 14.472 38.161 50.239 1.00158.80 N ANISOU 891 NH2 ARG A 139 21325 21257 17755 761 -1100 674 N ATOM 892 N THR A 140 9.285 44.460 49.786 1.00129.59 N ANISOU 892 N THR A 140 18095 18085 13057 2481 -1028 750 N ATOM 893 CA THR A 140 7.835 44.672 49.836 1.00130.67 C ANISOU 893 CA THR A 140 18089 18650 12911 2794 -1040 838 C ATOM 894 C THR A 140 7.281 44.686 48.393 1.00133.27 C ANISOU 894 C THR A 140 18410 19060 13165 2819 -1005 957 C ATOM 895 O THR A 140 8.048 44.871 47.443 1.00131.88 O ANISOU 895 O THR A 140 18419 18543 13147 2674 -964 947 O ATOM 896 CB THR A 140 7.309 45.818 50.741 1.00141.63 C ANISOU 896 CB THR A 140 19615 20091 14108 3220 -1051 765 C ATOM 897 OG1 THR A 140 5.880 45.793 50.786 1.00143.65 O ANISOU 897 OG1 THR A 140 19647 20866 14069 3507 -1061 874 O ATOM 898 CG2 THR A 140 7.789 47.185 50.302 1.00140.97 C ANISOU 898 CG2 THR A 140 19948 19560 14053 3417 -1021 686 C ATOM 899 N LYS A 141 5.954 44.479 48.244 1.00130.14 N ANISOU 899 N LYS A 141 17782 19150 12514 2997 -1022 1077 N ATOM 900 CA LYS A 141 5.231 44.464 46.965 1.00130.10 C ANISOU 900 CA LYS A 141 17721 19327 12385 3048 -1001 1203 C ATOM 901 C LYS A 141 5.411 45.772 46.191 1.00133.49 C ANISOU 901 C LYS A 141 18487 19433 12800 3320 -948 1179 C ATOM 902 O LYS A 141 5.626 45.728 44.983 1.00132.29 O ANISOU 902 O LYS A 141 18413 19141 12712 3201 -915 1234 O ATOM 903 CB LYS A 141 3.732 44.190 47.186 1.00134.43 C ANISOU 903 CB LYS A 141 17946 20515 12616 3241 -1037 1332 C ATOM 904 CG LYS A 141 3.424 42.802 47.740 1.00145.87 C ANISOU 904 CG LYS A 141 19057 22322 14047 2912 -1100 1401 C ATOM 905 CD LYS A 141 1.951 42.649 48.102 1.00155.68 C ANISOU 905 CD LYS A 141 19964 24240 14946 3104 -1138 1536 C ATOM 906 CE LYS A 141 1.689 42.836 49.577 1.00163.46 C ANISOU 906 CE LYS A 141 20840 25446 15819 3296 -1159 1491 C ATOM 907 NZ LYS A 141 0.285 42.497 49.933 1.00172.74 N ANISOU 907 NZ LYS A 141 21629 27351 16651 3416 -1198 1646 N ATOM 908 N THR A 142 5.357 46.929 46.895 1.00130.64 N ANISOU 908 N THR A 142 18354 18932 12352 3679 -944 1094 N ATOM 909 CA THR A 142 5.516 48.270 46.311 1.00131.48 C ANISOU 909 CA THR A 142 18848 18686 12423 3964 -908 1068 C ATOM 910 C THR A 142 6.871 48.519 45.622 1.00131.62 C ANISOU 910 C THR A 142 19158 18136 12716 3667 -874 1013 C ATOM 911 O THR A 142 6.959 49.393 44.756 1.00132.28 O ANISOU 911 O THR A 142 19520 17965 12773 3804 -840 1044 O ATOM 912 CB THR A 142 4.998 49.394 47.250 1.00143.47 C ANISOU 912 CB THR A 142 20560 20218 13733 4451 -926 993 C ATOM 913 OG1 THR A 142 5.040 50.646 46.563 1.00147.15 O ANISOU 913 OG1 THR A 142 21431 20346 14135 4734 -900 989 O ATOM 914 CG2 THR A 142 5.773 49.505 48.558 1.00140.88 C ANISOU 914 CG2 THR A 142 20343 19657 13527 4369 -960 834 C ATOM 915 N ARG A 143 7.909 47.738 45.988 1.00123.94 N ANISOU 915 N ARG A 143 18109 16995 11988 3268 -881 945 N ATOM 916 CA ARG A 143 9.246 47.827 45.399 1.00121.51 C ANISOU 916 CA ARG A 143 18004 16233 11930 2956 -847 902 C ATOM 917 C ARG A 143 9.538 46.634 44.472 1.00121.43 C ANISOU 917 C ARG A 143 17772 16325 12042 2612 -822 977 C ATOM 918 O ARG A 143 10.321 46.775 43.527 1.00120.26 O ANISOU 918 O ARG A 143 17769 15902 12023 2436 -775 992 O ATOM 919 CB ARG A 143 10.317 47.963 46.492 1.00119.91 C ANISOU 919 CB ARG A 143 17915 15751 11896 2796 -874 761 C ATOM 920 CG ARG A 143 11.566 48.727 46.058 1.00128.15 C ANISOU 920 CG ARG A 143 19288 16294 13110 2617 -847 710 C ATOM 921 CD ARG A 143 11.360 50.229 46.103 1.00137.70 C ANISOU 921 CD ARG A 143 20904 17225 14190 2923 -858 677 C ATOM 922 NE ARG A 143 12.608 50.959 45.891 1.00143.13 N ANISOU 922 NE ARG A 143 21916 17434 15033 2692 -852 626 N ATOM 923 CZ ARG A 143 12.703 52.284 45.836 1.00158.52 C ANISOU 923 CZ ARG A 143 24298 19028 16903 2858 -871 598 C ATOM 924 NH1 ARG A 143 11.619 53.040 45.971 1.00147.41 N ANISOU 924 NH1 ARG A 143 23064 17683 15261 3311 -891 606 N ATOM 925 NH2 ARG A 143 13.879 52.865 45.643 1.00146.57 N ANISOU 925 NH2 ARG A 143 23056 17105 15527 2575 -874 567 N ATOM 926 N ALA A 144 8.903 45.469 44.737 1.00115.78 N ANISOU 926 N ALA A 144 16721 16002 11267 2514 -857 1026 N ATOM 927 CA ALA A 144 9.056 44.261 43.926 1.00113.36 C ANISOU 927 CA ALA A 144 16230 15802 11039 2205 -852 1090 C ATOM 928 C ALA A 144 8.246 44.395 42.634 1.00117.69 C ANISOU 928 C ALA A 144 16763 16520 11435 2310 -828 1210 C ATOM 929 O ALA A 144 8.818 44.246 41.554 1.00117.22 O ANISOU 929 O ALA A 144 16789 16275 11474 2143 -785 1233 O ATOM 930 CB ALA A 144 8.619 43.031 44.709 1.00113.06 C ANISOU 930 CB ALA A 144 15893 16098 10967 2052 -915 1108 C ATOM 931 N SER A 145 6.930 44.728 42.743 1.00114.73 N ANISOU 931 N SER A 145 16275 16516 10802 2608 -853 1289 N ATOM 932 CA SER A 145 6.022 44.913 41.598 1.00114.94 C ANISOU 932 CA SER A 145 16257 16776 10640 2753 -840 1414 C ATOM 933 C SER A 145 6.357 46.148 40.742 1.00118.53 C ANISOU 933 C SER A 145 17042 16892 11102 2952 -778 1421 C ATOM 934 O SER A 145 5.937 46.213 39.589 1.00118.65 O ANISOU 934 O SER A 145 17056 17005 11020 2992 -756 1520 O ATOM 935 CB SER A 145 4.562 44.917 42.042 1.00119.65 C ANISOU 935 CB SER A 145 16607 17915 10939 3024 -885 1502 C ATOM 936 OG SER A 145 4.234 43.720 42.730 1.00126.18 O ANISOU 936 OG SER A 145 17129 19069 11746 2785 -948 1522 O ATOM 937 N ALA A 146 7.131 47.105 41.294 1.00114.62 N ANISOU 937 N ALA A 146 16841 15994 10715 3050 -758 1323 N ATOM 938 CA ALA A 146 7.590 48.296 40.580 1.00115.31 C ANISOU 938 CA ALA A 146 17295 15693 10824 3183 -711 1330 C ATOM 939 C ALA A 146 8.745 47.920 39.656 1.00116.64 C ANISOU 939 C ALA A 146 17537 15569 11213 2811 -662 1331 C ATOM 940 O ALA A 146 8.859 48.488 38.571 1.00116.98 O ANISOU 940 O ALA A 146 17762 15454 11231 2850 -617 1402 O ATOM 941 CB ALA A 146 8.043 49.359 41.564 1.00117.31 C ANISOU 941 CB ALA A 146 17850 15615 11106 3357 -726 1220 C ATOM 942 N THR A 147 9.600 46.964 40.090 1.00110.63 N ANISOU 942 N THR A 147 16633 14752 10650 2469 -669 1257 N ATOM 943 CA THR A 147 10.745 46.471 39.316 1.00108.71 C ANISOU 943 CA THR A 147 16416 14287 10602 2130 -620 1249 C ATOM 944 C THR A 147 10.401 45.292 38.395 1.00110.87 C ANISOU 944 C THR A 147 16457 14824 10844 1962 -616 1318 C ATOM 945 O THR A 147 11.167 45.011 37.477 1.00109.79 O ANISOU 945 O THR A 147 16367 14539 10811 1760 -566 1330 O ATOM 946 CB THR A 147 12.017 46.303 40.171 1.00115.21 C ANISOU 946 CB THR A 147 17279 14853 11642 1893 -622 1133 C ATOM 947 OG1 THR A 147 11.693 45.645 41.395 1.00116.42 O ANISOU 947 OG1 THR A 147 17234 15210 11791 1897 -683 1071 O ATOM 948 CG2 THR A 147 12.707 47.632 40.464 1.00114.31 C ANISOU 948 CG2 THR A 147 17497 14356 11579 1955 -609 1086 C ATOM 949 N ILE A 148 9.246 44.660 38.592 1.00107.42 N ANISOU 949 N ILE A 148 15786 14784 10244 2045 -671 1367 N ATOM 950 CA ILE A 148 8.811 43.565 37.717 1.00106.72 C ANISOU 950 CA ILE A 148 15507 14951 10092 1871 -687 1434 C ATOM 951 C ILE A 148 7.886 44.044 36.590 1.00111.70 C ANISOU 951 C ILE A 148 16154 15770 10518 2062 -672 1554 C ATOM 952 O ILE A 148 7.540 43.283 35.686 1.00111.27 O ANISOU 952 O ILE A 148 15980 15904 10392 1922 -685 1614 O ATOM 953 CB ILE A 148 8.100 42.455 38.514 1.00109.69 C ANISOU 953 CB ILE A 148 15606 15677 10393 1769 -771 1438 C ATOM 954 CG1 ILE A 148 6.822 42.996 39.158 1.00112.30 C ANISOU 954 CG1 ILE A 148 15822 16354 10494 2074 -813 1498 C ATOM 955 CG2 ILE A 148 9.030 41.878 39.570 1.00108.97 C ANISOU 955 CG2 ILE A 148 15497 15408 10498 1576 -788 1329 C ATOM 956 CD1 ILE A 148 5.697 41.987 39.223 1.00121.97 C ANISOU 956 CD1 ILE A 148 16743 18068 11531 1979 -891 1585 C ATOM 957 N LEU A 149 7.497 45.311 36.665 1.00109.67 N ANISOU 957 N LEU A 149 16063 15452 10155 2390 -652 1587 N ATOM 958 CA LEU A 149 6.611 45.966 35.701 1.00111.21 C ANISOU 958 CA LEU A 149 16304 15813 10136 2647 -637 1707 C ATOM 959 C LEU A 149 7.536 46.755 34.767 1.00115.09 C ANISOU 959 C LEU A 149 17100 15891 10738 2617 -560 1718 C ATOM 960 O LEU A 149 7.392 46.663 33.548 1.00115.29 O ANISOU 960 O LEU A 149 17129 15978 10697 2580 -531 1802 O ATOM 961 CB LEU A 149 5.598 46.895 36.396 1.00113.38 C ANISOU 961 CB LEU A 149 16602 16278 10199 3077 -664 1739 C ATOM 962 CG LEU A 149 4.437 47.384 35.536 1.00120.32 C ANISOU 962 CG LEU A 149 17443 17472 10801 3386 -665 1878 C ATOM 963 CD1 LEU A 149 3.114 46.908 36.089 1.00121.49 C ANISOU 963 CD1 LEU A 149 17250 18205 10704 3539 -731 1940 C ATOM 964 CD2 LEU A 149 4.451 48.896 35.412 1.00124.79 C ANISOU 964 CD2 LEU A 149 18366 17753 11294 3768 -627 1898 C ATOM 965 N GLY A 150 8.516 47.455 35.358 1.00110.97 N ANISOU 965 N GLY A 150 16818 14965 10380 2592 -534 1636 N ATOM 966 CA GLY A 150 9.538 48.227 34.658 1.00110.88 C ANISOU 966 CA GLY A 150 17102 14543 10485 2503 -468 1648 C ATOM 967 C GLY A 150 10.463 47.366 33.817 1.00112.18 C ANISOU 967 C GLY A 150 17181 14643 10799 2146 -420 1643 C ATOM 968 O GLY A 150 10.995 47.839 32.806 1.00112.82 O ANISOU 968 O GLY A 150 17431 14535 10900 2085 -358 1706 O ATOM 969 N ALA A 151 10.652 46.087 34.224 1.00105.48 N ANISOU 969 N ALA A 151 16082 13958 10040 1920 -448 1574 N ATOM 970 CA ALA A 151 11.458 45.103 33.497 1.00103.24 C ANISOU 970 CA ALA A 151 15707 13650 9870 1621 -412 1554 C ATOM 971 C ALA A 151 10.739 44.688 32.210 1.00105.90 C ANISOU 971 C ALA A 151 15964 14224 10049 1639 -405 1648 C ATOM 972 O ALA A 151 11.401 44.499 31.190 1.00105.40 O ANISOU 972 O ALA A 151 15954 14064 10029 1495 -345 1669 O ATOM 973 CB ALA A 151 11.732 43.886 34.365 1.00102.17 C ANISOU 973 CB ALA A 151 15369 13610 9840 1428 -460 1457 C ATOM 974 N TRP A 152 9.391 44.587 32.244 1.00101.81 N ANISOU 974 N TRP A 152 15312 14042 9329 1819 -466 1711 N ATOM 975 CA TRP A 152 8.589 44.250 31.066 1.00102.00 C ANISOU 975 CA TRP A 152 15249 14336 9170 1843 -475 1808 C ATOM 976 C TRP A 152 8.470 45.419 30.075 1.00108.41 C ANISOU 976 C TRP A 152 16265 15043 9881 2051 -415 1914 C ATOM 977 O TRP A 152 8.071 45.205 28.927 1.00108.29 O ANISOU 977 O TRP A 152 16212 15194 9738 2043 -405 1994 O ATOM 978 CB TRP A 152 7.217 43.701 31.459 1.00100.84 C ANISOU 978 CB TRP A 152 14856 14635 8824 1928 -568 1852 C ATOM 979 CG TRP A 152 7.281 42.322 32.032 1.00 99.86 C ANISOU 979 CG TRP A 152 14540 14639 8763 1650 -635 1779 C ATOM 980 CD1 TRP A 152 7.639 41.982 33.300 1.00101.74 C ANISOU 980 CD1 TRP A 152 14726 14802 9129 1573 -666 1691 C ATOM 981 CD2 TRP A 152 6.985 41.092 31.355 1.00 99.44 C ANISOU 981 CD2 TRP A 152 14355 14791 8635 1406 -688 1790 C ATOM 982 NE1 TRP A 152 7.567 40.619 33.466 1.00100.08 N ANISOU 982 NE1 TRP A 152 14363 14735 8929 1306 -734 1658 N ATOM 983 CE2 TRP A 152 7.167 40.046 32.288 1.00102.05 C ANISOU 983 CE2 TRP A 152 14576 15144 9053 1192 -753 1713 C ATOM 984 CE3 TRP A 152 6.580 40.769 30.050 1.00101.31 C ANISOU 984 CE3 TRP A 152 14577 15189 8728 1344 -693 1856 C ATOM 985 CZ2 TRP A 152 6.960 38.699 31.958 1.00101.08 C ANISOU 985 CZ2 TRP A 152 14362 15166 8877 915 -828 1700 C ATOM 986 CZ3 TRP A 152 6.380 39.434 29.722 1.00102.50 C ANISOU 986 CZ3 TRP A 152 14627 15495 8825 1064 -769 1832 C ATOM 987 CH2 TRP A 152 6.574 38.416 30.668 1.00102.03 C ANISOU 987 CH2 TRP A 152 14491 15420 8853 850 -838 1755 C ATOM 988 N PHE A 153 8.835 46.645 30.513 1.00106.92 N ANISOU 988 N PHE A 153 16317 14564 9743 2225 -381 1917 N ATOM 989 CA PHE A 153 8.849 47.853 29.685 1.00109.18 C ANISOU 989 CA PHE A 153 16868 14668 9948 2415 -329 2021 C ATOM 990 C PHE A 153 10.073 47.809 28.766 1.00112.72 C ANISOU 990 C PHE A 153 17438 14855 10537 2150 -247 2029 C ATOM 991 O PHE A 153 9.957 48.146 27.590 1.00113.05 O ANISOU 991 O PHE A 153 17566 14912 10476 2197 -205 2135 O ATOM 992 CB PHE A 153 8.850 49.122 30.560 1.00112.77 C ANISOU 992 CB PHE A 153 17582 14865 10400 2668 -338 2009 C ATOM 993 CG PHE A 153 9.017 50.437 29.829 1.00116.93 C ANISOU 993 CG PHE A 153 18462 15107 10860 2839 -293 2112 C ATOM 994 CD1 PHE A 153 7.937 51.041 29.194 1.00122.30 C ANISOU 994 CD1 PHE A 153 19204 15967 11296 3183 -303 2237 C ATOM 995 CD2 PHE A 153 10.246 51.089 29.809 1.00119.68 C ANISOU 995 CD2 PHE A 153 19087 15015 11372 2653 -246 2095 C ATOM 996 CE1 PHE A 153 8.090 52.262 28.526 1.00125.61 C ANISOU 996 CE1 PHE A 153 19987 16096 11644 3351 -267 2342 C ATOM 997 CE2 PHE A 153 10.398 52.312 29.143 1.00124.92 C ANISOU 997 CE2 PHE A 153 20110 15393 11962 2781 -215 2205 C ATOM 998 CZ PHE A 153 9.319 52.891 28.508 1.00125.01 C ANISOU 998 CZ PHE A 153 20210 15551 11737 3137 -225 2327 C ATOM 999 N LEU A 154 11.232 47.375 29.295 1.00108.36 N ANISOU 999 N LEU A 154 16870 14101 10199 1884 -225 1924 N ATOM 1000 CA LEU A 154 12.462 47.240 28.516 1.00108.00 C ANISOU 1000 CA LEU A 154 16890 13868 10276 1628 -144 1928 C ATOM 1001 C LEU A 154 12.425 46.019 27.573 1.00110.53 C ANISOU 1001 C LEU A 154 17011 14430 10555 1476 -130 1923 C ATOM 1002 O LEU A 154 13.187 45.965 26.603 1.00109.76 O ANISOU 1002 O LEU A 154 16964 14257 10482 1339 -55 1958 O ATOM 1003 CB LEU A 154 13.686 47.182 29.438 1.00107.13 C ANISOU 1003 CB LEU A 154 16805 13518 10383 1418 -129 1823 C ATOM 1004 CG LEU A 154 14.696 48.318 29.282 1.00113.53 C ANISOU 1004 CG LEU A 154 17881 13984 11270 1329 -72 1872 C ATOM 1005 CD1 LEU A 154 15.701 48.306 30.412 1.00112.86 C ANISOU 1005 CD1 LEU A 154 17797 13716 11369 1146 -84 1765 C ATOM 1006 CD2 LEU A 154 15.425 48.248 27.938 1.00116.96 C ANISOU 1006 CD2 LEU A 154 18337 14404 11698 1160 19 1956 C ATOM 1007 N SER A 155 11.531 45.054 27.861 1.00106.58 N ANISOU 1007 N SER A 155 16298 14223 9975 1495 -206 1883 N ATOM 1008 CA SER A 155 11.331 43.835 27.081 1.00105.99 C ANISOU 1008 CA SER A 155 16066 14375 9833 1351 -223 1865 C ATOM 1009 C SER A 155 10.333 44.046 25.948 1.00112.25 C ANISOU 1009 C SER A 155 16852 15401 10398 1489 -232 1983 C ATOM 1010 O SER A 155 10.560 43.545 24.845 1.00111.92 O ANISOU 1010 O SER A 155 16801 15420 10301 1378 -200 1999 O ATOM 1011 CB SER A 155 10.865 42.695 27.978 1.00108.25 C ANISOU 1011 CB SER A 155 16155 14847 10130 1258 -317 1776 C ATOM 1012 OG SER A 155 11.882 42.341 28.898 1.00115.94 O ANISOU 1012 OG SER A 155 17125 15618 11308 1115 -306 1667 O ATOM 1013 N PHE A 156 9.231 44.784 26.212 1.00110.79 N ANISOU 1013 N PHE A 156 16667 15365 10061 1749 -276 2066 N ATOM 1014 CA PHE A 156 8.206 45.078 25.208 1.00112.53 C ANISOU 1014 CA PHE A 156 16866 15849 10042 1922 -291 2192 C ATOM 1015 C PHE A 156 8.652 46.087 24.149 1.00118.29 C ANISOU 1015 C PHE A 156 17825 16381 10741 2015 -202 2297 C ATOM 1016 O PHE A 156 7.935 46.289 23.166 1.00119.28 O ANISOU 1016 O PHE A 156 17942 16712 10668 2142 -204 2407 O ATOM 1017 CB PHE A 156 6.869 45.483 25.846 1.00115.59 C ANISOU 1017 CB PHE A 156 17150 16520 10249 2201 -367 2253 C ATOM 1018 CG PHE A 156 5.835 44.383 25.812 1.00117.16 C ANISOU 1018 CG PHE A 156 17063 17167 10284 2111 -464 2257 C ATOM 1019 CD1 PHE A 156 5.280 43.965 24.609 1.00121.31 C ANISOU 1019 CD1 PHE A 156 17508 17959 10626 2061 -484 2331 C ATOM 1020 CD2 PHE A 156 5.404 43.776 26.983 1.00118.47 C ANISOU 1020 CD2 PHE A 156 17047 17501 10463 2057 -542 2195 C ATOM 1021 CE1 PHE A 156 4.329 42.941 24.577 1.00122.44 C ANISOU 1021 CE1 PHE A 156 17401 18519 10602 1928 -589 2339 C ATOM 1022 CE2 PHE A 156 4.442 42.760 26.950 1.00121.49 C ANISOU 1022 CE2 PHE A 156 17174 18308 10678 1926 -642 2217 C ATOM 1023 CZ PHE A 156 3.915 42.347 25.747 1.00120.65 C ANISOU 1023 CZ PHE A 156 16999 18451 10390 1850 -669 2288 C ATOM 1024 N LEU A 157 9.851 46.688 24.324 1.00115.14 N ANISOU 1024 N LEU A 157 17623 15601 10525 1926 -126 2274 N ATOM 1025 CA LEU A 157 10.451 47.622 23.371 1.00116.76 C ANISOU 1025 CA LEU A 157 18060 15586 10716 1946 -40 2381 C ATOM 1026 C LEU A 157 10.821 46.903 22.068 1.00121.81 C ANISOU 1026 C LEU A 157 18625 16350 11307 1770 11 2402 C ATOM 1027 O LEU A 157 11.051 47.562 21.056 1.00122.92 O ANISOU 1027 O LEU A 157 18915 16417 11373 1805 77 2518 O ATOM 1028 CB LEU A 157 11.696 48.302 23.969 1.00116.73 C ANISOU 1028 CB LEU A 157 18253 15182 10916 1819 14 2347 C ATOM 1029 CG LEU A 157 11.457 49.472 24.927 1.00122.67 C ANISOU 1029 CG LEU A 157 19223 15707 11679 2027 -20 2364 C ATOM 1030 CD1 LEU A 157 12.720 49.811 25.689 1.00122.37 C ANISOU 1030 CD1 LEU A 157 19316 15325 11854 1815 8 2292 C ATOM 1031 CD2 LEU A 157 10.950 50.709 24.196 1.00127.86 C ANISOU 1031 CD2 LEU A 157 20149 16266 12165 2283 -3 2525 C ATOM 1032 N TRP A 158 10.855 45.550 22.097 1.00117.56 N ANISOU 1032 N TRP A 158 17876 15995 10795 1588 -24 2290 N ATOM 1033 CA TRP A 158 11.157 44.678 20.960 1.00117.28 C ANISOU 1033 CA TRP A 158 17772 16091 10697 1430 8 2273 C ATOM 1034 C TRP A 158 10.111 44.745 19.856 1.00122.78 C ANISOU 1034 C TRP A 158 18440 17068 11143 1561 -19 2383 C ATOM 1035 O TRP A 158 10.450 44.514 18.697 1.00122.85 O ANISOU 1035 O TRP A 158 18475 17126 11075 1486 34 2413 O ATOM 1036 CB TRP A 158 11.365 43.233 21.423 1.00114.19 C ANISOU 1036 CB TRP A 158 17217 15788 10382 1232 -45 2117 C ATOM 1037 CG TRP A 158 12.765 42.992 21.874 1.00113.94 C ANISOU 1037 CG TRP A 158 17217 15509 10564 1067 21 2021 C ATOM 1038 CD1 TRP A 158 13.253 43.134 23.138 1.00115.90 C ANISOU 1038 CD1 TRP A 158 17462 15583 10993 1032 10 1952 C ATOM 1039 CD2 TRP A 158 13.892 42.713 21.037 1.00113.90 C ANISOU 1039 CD2 TRP A 158 17251 15430 10596 938 118 2003 C ATOM 1040 NE1 TRP A 158 14.610 42.912 23.149 1.00114.91 N ANISOU 1040 NE1 TRP A 158 17354 15292 11014 877 88 1892 N ATOM 1041 CE2 TRP A 158 15.029 42.650 21.870 1.00117.00 C ANISOU 1041 CE2 TRP A 158 17639 15626 11191 825 158 1924 C ATOM 1042 CE3 TRP A 158 14.050 42.492 19.660 1.00116.03 C ANISOU 1042 CE3 TRP A 158 17547 15810 10731 916 174 2047 C ATOM 1043 CZ2 TRP A 158 16.306 42.361 21.374 1.00116.36 C ANISOU 1043 CZ2 TRP A 158 17556 15484 11171 700 255 1893 C ATOM 1044 CZ3 TRP A 158 15.317 42.223 19.169 1.00117.50 C ANISOU 1044 CZ3 TRP A 158 17747 15919 10980 800 275 2011 C ATOM 1045 CH2 TRP A 158 16.422 42.139 20.023 1.00117.28 C ANISOU 1045 CH2 TRP A 158 17692 15725 11145 697 315 1937 C ATOM 1046 N VAL A 159 8.851 45.074 20.214 1.00120.31 N ANISOU 1046 N VAL A 159 18061 16965 10685 1769 -100 2445 N ATOM 1047 CA VAL A 159 7.717 45.209 19.287 1.00121.87 C ANISOU 1047 CA VAL A 159 18200 17488 10617 1926 -140 2564 C ATOM 1048 C VAL A 159 7.949 46.401 18.312 1.00127.57 C ANISOU 1048 C VAL A 159 19139 18071 11262 2090 -52 2718 C ATOM 1049 O VAL A 159 7.488 46.350 17.165 1.00128.38 O ANISOU 1049 O VAL A 159 19218 18388 11171 2135 -50 2806 O ATOM 1050 CB VAL A 159 6.352 45.264 20.041 1.00126.37 C ANISOU 1050 CB VAL A 159 18610 18365 11041 2121 -247 2598 C ATOM 1051 CG1 VAL A 159 5.173 45.142 19.080 1.00128.07 C ANISOU 1051 CG1 VAL A 159 18697 19003 10960 2232 -305 2710 C ATOM 1052 CG2 VAL A 159 6.265 44.171 21.100 1.00124.37 C ANISOU 1052 CG2 VAL A 159 18173 18199 10883 1928 -328 2460 C ATOM 1053 N ILE A 160 8.718 47.430 18.755 1.00124.24 N ANISOU 1053 N ILE A 160 18940 17280 10987 2146 15 2750 N ATOM 1054 CA ILE A 160 9.091 48.598 17.947 1.00125.91 C ANISOU 1054 CA ILE A 160 19407 17287 11148 2253 96 2902 C ATOM 1055 C ILE A 160 9.971 48.183 16.730 1.00131.14 C ANISOU 1055 C ILE A 160 20076 17940 11811 2029 183 2919 C ATOM 1056 O ILE A 160 9.441 48.261 15.619 1.00132.22 O ANISOU 1056 O ILE A 160 20209 18281 11748 2121 190 3024 O ATOM 1057 CB ILE A 160 9.641 49.787 18.799 1.00129.26 C ANISOU 1057 CB ILE A 160 20096 17306 11709 2335 123 2930 C ATOM 1058 CG1 ILE A 160 8.611 50.293 19.845 1.00130.19 C ANISOU 1058 CG1 ILE A 160 20231 17476 11760 2641 38 2927 C ATOM 1059 CG2 ILE A 160 10.215 50.925 17.945 1.00131.56 C ANISOU 1059 CG2 ILE A 160 20689 17335 11962 2361 204 3091 C ATOM 1060 CD1 ILE A 160 7.199 50.735 19.325 1.00140.38 C ANISOU 1060 CD1 ILE A 160 21499 19078 12761 3006 -12 3062 C ATOM 1061 N PRO A 161 11.223 47.640 16.867 1.00127.05 N ANISOU 1061 N PRO A 161 19535 17257 11481 1756 245 2815 N ATOM 1062 CA PRO A 161 11.978 47.225 15.665 1.00127.46 C ANISOU 1062 CA PRO A 161 19574 17364 11490 1591 331 2834 C ATOM 1063 C PRO A 161 11.392 46.045 14.867 1.00132.24 C ANISOU 1063 C PRO A 161 19998 18311 11935 1552 287 2770 C ATOM 1064 O PRO A 161 11.943 45.692 13.823 1.00132.49 O ANISOU 1064 O PRO A 161 20029 18410 11900 1450 354 2779 O ATOM 1065 CB PRO A 161 13.386 46.932 16.207 1.00127.91 C ANISOU 1065 CB PRO A 161 19624 17202 11773 1353 397 2732 C ATOM 1066 CG PRO A 161 13.435 47.591 17.556 1.00131.76 C ANISOU 1066 CG PRO A 161 20198 17447 12416 1396 359 2708 C ATOM 1067 CD PRO A 161 12.046 47.441 18.077 1.00126.98 C ANISOU 1067 CD PRO A 161 19511 17023 11711 1607 247 2687 C ATOM 1068 N ILE A 162 10.265 45.459 15.329 1.00129.04 N ANISOU 1068 N ILE A 162 19447 18137 11447 1626 169 2712 N ATOM 1069 CA ILE A 162 9.563 44.381 14.623 1.00129.47 C ANISOU 1069 CA ILE A 162 19351 18521 11321 1565 99 2660 C ATOM 1070 C ILE A 162 8.765 44.980 13.442 1.00137.60 C ANISOU 1070 C ILE A 162 20415 19771 12093 1737 100 2826 C ATOM 1071 O ILE A 162 8.681 44.357 12.377 1.00138.15 O ANISOU 1071 O ILE A 162 20442 20037 12010 1657 99 2815 O ATOM 1072 CB ILE A 162 8.726 43.497 15.607 1.00131.26 C ANISOU 1072 CB ILE A 162 19401 18923 11550 1518 -34 2549 C ATOM 1073 CG1 ILE A 162 9.617 42.494 16.402 1.00129.55 C ANISOU 1073 CG1 ILE A 162 19146 18534 11544 1295 -38 2365 C ATOM 1074 CG2 ILE A 162 7.517 42.800 14.961 1.00132.89 C ANISOU 1074 CG2 ILE A 162 19464 19531 11497 1510 -143 2565 C ATOM 1075 CD1 ILE A 162 10.557 41.517 15.606 1.00135.30 C ANISOU 1075 CD1 ILE A 162 19902 19223 12281 1106 13 2256 C ATOM 1076 N LEU A 163 8.238 46.214 13.619 1.00136.59 N ANISOU 1076 N LEU A 163 20393 19595 11912 1988 105 2978 N ATOM 1077 CA LEU A 163 7.487 46.961 12.596 1.00139.08 C ANISOU 1077 CA LEU A 163 20769 20093 11983 2207 109 3160 C ATOM 1078 C LEU A 163 8.312 48.088 11.907 1.00145.09 C ANISOU 1078 C LEU A 163 21786 20575 12766 2259 231 3308 C ATOM 1079 O LEU A 163 7.794 48.782 11.029 1.00146.46 O ANISOU 1079 O LEU A 163 22049 20859 12742 2447 243 3475 O ATOM 1080 CB LEU A 163 6.149 47.495 13.169 1.00140.16 C ANISOU 1080 CB LEU A 163 20842 20437 11976 2500 15 3243 C ATOM 1081 CG LEU A 163 6.205 48.407 14.408 1.00144.45 C ANISOU 1081 CG LEU A 163 21517 20704 12661 2677 17 3255 C ATOM 1082 CD1 LEU A 163 6.023 49.866 14.026 1.00146.97 C ANISOU 1082 CD1 LEU A 163 22101 20865 12875 2982 61 3446 C ATOM 1083 CD2 LEU A 163 5.142 48.014 15.414 1.00145.76 C ANISOU 1083 CD2 LEU A 163 21472 21141 12768 2789 -96 3197 C ATOM 1084 N GLY A 164 9.580 48.229 12.302 1.00141.62 N ANISOU 1084 N GLY A 164 21454 19801 12552 2079 314 3255 N ATOM 1085 CA GLY A 164 10.493 49.252 11.802 1.00143.26 C ANISOU 1085 CA GLY A 164 21901 19730 12803 2051 423 3394 C ATOM 1086 C GLY A 164 11.399 48.851 10.653 1.00148.73 C ANISOU 1086 C GLY A 164 22576 20477 13456 1854 523 3410 C ATOM 1087 O GLY A 164 12.503 48.338 10.867 1.00146.89 O ANISOU 1087 O GLY A 164 22293 20135 13382 1626 585 3305 O ATOM 1088 N TRP A 165 10.945 49.129 9.424 1.00148.50 N ANISOU 1088 N TRP A 165 22587 20637 13199 1963 543 3551 N ATOM 1089 CA TRP A 165 11.684 48.892 8.180 1.00149.77 C ANISOU 1089 CA TRP A 165 22748 20892 13268 1824 642 3599 C ATOM 1090 C TRP A 165 12.194 50.229 7.610 1.00156.18 C ANISOU 1090 C TRP A 165 23814 21488 14039 1855 734 3833 C ATOM 1091 O TRP A 165 12.963 50.228 6.645 1.00157.12 O ANISOU 1091 O TRP A 165 23952 21654 14092 1723 834 3905 O ATOM 1092 CB TRP A 165 10.833 48.136 7.131 1.00149.30 C ANISOU 1092 CB TRP A 165 22547 21226 12955 1892 594 3584 C ATOM 1093 CG TRP A 165 9.375 47.998 7.465 1.00150.75 C ANISOU 1093 CG TRP A 165 22630 21639 13009 2089 458 3576 C ATOM 1094 CD1 TRP A 165 8.724 46.855 7.819 1.00152.25 C ANISOU 1094 CD1 TRP A 165 22613 22066 13168 2027 351 3410 C ATOM 1095 CD2 TRP A 165 8.393 49.048 7.497 1.00152.21 C ANISOU 1095 CD2 TRP A 165 22915 21857 13061 2381 413 3752 C ATOM 1096 NE1 TRP A 165 7.394 47.120 8.059 1.00152.71 N ANISOU 1096 NE1 TRP A 165 22599 22348 13076 2240 244 3479 N ATOM 1097 CE2 TRP A 165 7.164 48.459 7.873 1.00155.99 C ANISOU 1097 CE2 TRP A 165 23195 22651 13423 2488 283 3684 C ATOM 1098 CE3 TRP A 165 8.434 50.435 7.255 1.00155.64 C ANISOU 1098 CE3 TRP A 165 23605 22082 13448 2569 464 3966 C ATOM 1099 CZ2 TRP A 165 5.983 49.205 8.000 1.00156.91 C ANISOU 1099 CZ2 TRP A 165 23322 22928 13368 2806 213 3821 C ATOM 1100 CZ3 TRP A 165 7.264 51.171 7.378 1.00158.73 C ANISOU 1100 CZ3 TRP A 165 24052 22582 13675 2903 390 4093 C ATOM 1101 CH2 TRP A 165 6.057 50.558 7.747 1.00158.97 C ANISOU 1101 CH2 TRP A 165 23844 22973 13583 3034 271 4020 C ATOM 1102 N ASN A 166 11.776 51.363 8.232 1.00153.34 N ANISOU 1102 N ASN A 166 23667 20887 13707 2028 696 3950 N ATOM 1103 CA ASN A 166 12.126 52.745 7.872 1.00155.46 C ANISOU 1103 CA ASN A 166 24254 20879 13936 2073 753 4181 C ATOM 1104 C ASN A 166 13.636 53.013 7.860 1.00160.34 C ANISOU 1104 C ASN A 166 24961 21255 14706 1752 862 4215 C ATOM 1105 O ASN A 166 14.103 53.805 7.040 1.00162.19 O ANISOU 1105 O ASN A 166 25385 21394 14846 1689 935 4417 O ATOM 1106 CB ASN A 166 11.442 53.736 8.819 1.00154.76 C ANISOU 1106 CB ASN A 166 24391 20536 13875 2321 673 4238 C ATOM 1107 CG ASN A 166 9.936 53.742 8.751 1.00169.49 C ANISOU 1107 CG ASN A 166 26191 22666 15541 2684 575 4264 C ATOM 1108 OD1 ASN A 166 9.277 52.727 8.992 1.00159.10 O ANISOU 1108 OD1 ASN A 166 24586 21665 14199 2712 509 4114 O ATOM 1109 ND2 ASN A 166 9.359 54.863 8.353 1.00162.81 N ANISOU 1109 ND2 ASN A 166 25610 21725 14525 2963 561 4468 N ATOM 1110 N HIS A 167 14.390 52.351 8.765 1.00155.26 N ANISOU 1110 N HIS A 167 24171 20538 14283 1544 869 4031 N ATOM 1111 CA HIS A 167 15.844 52.479 8.933 1.00155.28 C ANISOU 1111 CA HIS A 167 24193 20371 14436 1228 962 4039 C ATOM 1112 C HIS A 167 16.671 51.866 7.772 1.00159.43 C ANISOU 1112 C HIS A 167 24555 21157 14864 1051 1078 4062 C ATOM 1113 O HIS A 167 16.103 51.266 6.854 1.00158.92 O ANISOU 1113 O HIS A 167 24373 21386 14622 1171 1079 4047 O ATOM 1114 CB HIS A 167 16.263 51.884 10.293 1.00153.67 C ANISOU 1114 CB HIS A 167 23855 20060 14473 1111 922 3826 C ATOM 1115 CG HIS A 167 17.381 52.622 10.964 1.00157.82 C ANISOU 1115 CG HIS A 167 24527 20274 15164 868 961 3878 C ATOM 1116 ND1 HIS A 167 18.676 52.132 10.957 1.00159.21 N ANISOU 1116 ND1 HIS A 167 24537 20518 15436 581 1049 3827 N ATOM 1117 CD2 HIS A 167 17.362 53.794 11.639 1.00160.96 C ANISOU 1117 CD2 HIS A 167 25225 20309 15623 875 917 3976 C ATOM 1118 CE1 HIS A 167 19.398 53.014 11.629 1.00159.68 C ANISOU 1118 CE1 HIS A 167 24777 20279 15616 391 1052 3902 C ATOM 1119 NE2 HIS A 167 18.653 54.035 12.053 1.00161.13 N ANISOU 1119 NE2 HIS A 167 25265 20171 15784 549 970 3988 N ATOM 1120 N ARG A 175 13.576 37.288 2.100 1.00149.40 N ANISOU 1120 N ARG A 175 22288 22418 12061 1056 494 2014 N ATOM 1121 CA ARG A 175 12.989 36.127 2.768 1.00148.48 C ANISOU 1121 CA ARG A 175 22224 22237 11956 939 320 1815 C ATOM 1122 C ARG A 175 13.968 34.939 2.842 1.00153.08 C ANISOU 1122 C ARG A 175 22928 22685 12551 936 340 1578 C ATOM 1123 O ARG A 175 14.761 34.740 1.917 1.00153.63 O ANISOU 1123 O ARG A 175 23059 22835 12480 1032 450 1535 O ATOM 1124 CB ARG A 175 11.679 35.716 2.075 1.00149.30 C ANISOU 1124 CB ARG A 175 22359 22581 11787 867 157 1804 C ATOM 1125 CG ARG A 175 10.493 36.622 2.396 1.00156.30 C ANISOU 1125 CG ARG A 175 23109 23602 12674 871 82 2000 C ATOM 1126 CD ARG A 175 9.457 36.579 1.291 1.00164.23 C ANISOU 1126 CD ARG A 175 24110 24934 13357 859 -12 2060 C ATOM 1127 NE ARG A 175 8.128 36.178 1.766 1.00170.13 N ANISOU 1127 NE ARG A 175 24782 25843 14019 725 -213 2049 N ATOM 1128 CZ ARG A 175 7.566 34.994 1.534 1.00182.88 C ANISOU 1128 CZ ARG A 175 26474 27564 15448 533 -381 1886 C ATOM 1129 NH1 ARG A 175 8.214 34.067 0.839 1.00171.18 N ANISOU 1129 NH1 ARG A 175 25183 26009 13847 485 -374 1700 N ATOM 1130 NH2 ARG A 175 6.351 34.729 1.994 1.00168.52 N ANISOU 1130 NH2 ARG A 175 24553 25934 13543 386 -560 1911 N ATOM 1131 N ARG A 176 13.909 34.157 3.950 1.00149.07 N ANISOU 1131 N ARG A 176 22458 21984 12196 843 234 1432 N ATOM 1132 CA ARG A 176 14.748 32.969 4.191 1.00149.25 C ANISOU 1132 CA ARG A 176 22625 21845 12237 860 228 1202 C ATOM 1133 C ARG A 176 13.970 31.739 4.728 1.00154.17 C ANISOU 1133 C ARG A 176 23401 22366 12813 698 11 1023 C ATOM 1134 O ARG A 176 12.736 31.773 4.778 1.00153.67 O ANISOU 1134 O ARG A 176 23306 22416 12665 552 -136 1079 O ATOM 1135 CB ARG A 176 15.988 33.309 5.039 1.00147.36 C ANISOU 1135 CB ARG A 176 22293 21434 12261 944 373 1215 C ATOM 1136 CG ARG A 176 17.136 33.831 4.195 1.00157.51 C ANISOU 1136 CG ARG A 176 23524 22835 13485 1094 579 1286 C ATOM 1137 CD ARG A 176 18.446 33.870 4.947 1.00165.73 C ANISOU 1137 CD ARG A 176 24484 23755 14731 1163 705 1258 C ATOM 1138 NE ARG A 176 19.553 34.171 4.039 1.00176.24 N ANISOU 1138 NE ARG A 176 25759 25260 15946 1297 893 1311 N ATOM 1139 CZ ARG A 176 20.451 35.132 4.230 1.00191.29 C ANISOU 1139 CZ ARG A 176 27495 27203 17983 1303 1052 1473 C ATOM 1140 NH1 ARG A 176 20.403 35.891 5.319 1.00177.13 N ANISOU 1140 NH1 ARG A 176 25600 25252 16452 1195 1044 1582 N ATOM 1141 NH2 ARG A 176 21.415 35.332 3.342 1.00180.58 N ANISOU 1141 NH2 ARG A 176 26075 26055 16482 1405 1217 1528 N ATOM 1142 N GLU A 177 14.688 30.647 5.088 1.00151.83 N ANISOU 1142 N GLU A 177 23273 21872 12543 725 -11 816 N ATOM 1143 CA GLU A 177 14.080 29.395 5.557 1.00152.33 C ANISOU 1143 CA GLU A 177 23542 21793 12544 560 -219 640 C ATOM 1144 C GLU A 177 14.283 29.038 7.052 1.00155.92 C ANISOU 1144 C GLU A 177 23982 22001 13261 494 -273 590 C ATOM 1145 O GLU A 177 14.007 27.899 7.448 1.00156.09 O ANISOU 1145 O GLU A 177 24215 21861 13229 371 -432 433 O ATOM 1146 CB GLU A 177 14.501 28.234 4.647 1.00155.99 C ANISOU 1146 CB GLU A 177 24309 22210 12750 631 -256 422 C ATOM 1147 CG GLU A 177 13.335 27.372 4.206 1.00167.07 C ANISOU 1147 CG GLU A 177 25924 23654 13902 405 -486 326 C ATOM 1148 CD GLU A 177 13.739 26.165 3.386 1.00188.25 C ANISOU 1148 CD GLU A 177 28970 26234 16321 472 -544 87 C ATOM 1149 OE1 GLU A 177 14.362 26.352 2.316 1.00181.05 O ANISOU 1149 OE1 GLU A 177 28086 25454 15248 680 -409 65 O ATOM 1150 OE2 GLU A 177 13.415 25.030 3.804 1.00184.79 O ANISOU 1150 OE2 GLU A 177 28809 25582 15820 317 -729 -77 O ATOM 1151 N ASP A 178 14.727 30.005 7.884 1.00151.82 N ANISOU 1151 N ASP A 178 23232 21444 13008 558 -153 726 N ATOM 1152 CA ASP A 178 14.932 29.766 9.320 1.00150.45 C ANISOU 1152 CA ASP A 178 23021 21060 13084 504 -195 690 C ATOM 1153 C ASP A 178 13.659 29.922 10.166 1.00153.43 C ANISOU 1153 C ASP A 178 23301 21470 13525 296 -353 775 C ATOM 1154 O ASP A 178 13.320 29.001 10.915 1.00152.87 O ANISOU 1154 O ASP A 178 23345 21263 13476 153 -501 672 O ATOM 1155 CB ASP A 178 16.132 30.551 9.894 1.00151.31 C ANISOU 1155 CB ASP A 178 22960 21098 13435 660 -6 761 C ATOM 1156 CG ASP A 178 16.341 31.943 9.327 1.00163.27 C ANISOU 1156 CG ASP A 178 24287 22776 14973 741 153 959 C ATOM 1157 OD1 ASP A 178 16.043 32.925 10.041 1.00163.12 O ANISOU 1157 OD1 ASP A 178 24104 22744 15128 699 172 1108 O ATOM 1158 OD2 ASP A 178 16.845 32.051 8.184 1.00170.22 O ANISOU 1158 OD2 ASP A 178 25201 23788 15688 853 259 965 O ATOM 1159 N LYS A 179 12.950 31.070 10.033 1.00149.39 N ANISOU 1159 N LYS A 179 22588 21151 13021 291 -324 968 N ATOM 1160 CA LYS A 179 11.704 31.363 10.761 1.00148.13 C ANISOU 1160 CA LYS A 179 22295 21099 12888 143 -457 1072 C ATOM 1161 C LYS A 179 10.736 32.298 9.980 1.00151.79 C ANISOU 1161 C LYS A 179 22624 21857 13190 166 -458 1250 C ATOM 1162 O LYS A 179 10.696 32.234 8.748 1.00152.95 O ANISOU 1162 O LYS A 179 22847 22141 13125 199 -438 1245 O ATOM 1163 CB LYS A 179 11.988 31.845 12.210 1.00148.40 C ANISOU 1163 CB LYS A 179 22190 20982 13215 166 -421 1121 C ATOM 1164 CG LYS A 179 12.784 33.145 12.345 1.00159.15 C ANISOU 1164 CG LYS A 179 23415 22297 14757 346 -232 1247 C ATOM 1165 CD LYS A 179 12.681 33.694 13.765 1.00166.39 C ANISOU 1165 CD LYS A 179 24197 23112 15912 338 -241 1309 C ATOM 1166 CE LYS A 179 13.029 35.158 13.856 1.00174.81 C ANISOU 1166 CE LYS A 179 25149 24167 17105 475 -100 1470 C ATOM 1167 NZ LYS A 179 14.477 35.401 13.643 1.00183.66 N ANISOU 1167 NZ LYS A 179 26296 25150 18336 560 63 1447 N ATOM 1168 N CYS A 180 9.942 33.130 10.698 1.00146.35 N ANISOU 1168 N CYS A 180 21745 21279 12584 166 -488 1402 N ATOM 1169 CA CYS A 180 8.991 34.103 10.151 1.00146.22 C ANISOU 1169 CA CYS A 180 21587 21544 12426 236 -491 1587 C ATOM 1170 C CYS A 180 9.719 35.255 9.448 1.00148.76 C ANISOU 1170 C CYS A 180 21895 21839 12786 450 -301 1707 C ATOM 1171 O CYS A 180 9.126 35.925 8.597 1.00149.73 O ANISOU 1171 O CYS A 180 21970 22183 12738 531 -287 1843 O ATOM 1172 CB CYS A 180 8.067 34.617 11.254 1.00145.48 C ANISOU 1172 CB CYS A 180 21311 21551 12413 224 -568 1699 C ATOM 1173 SG CYS A 180 6.775 35.753 10.683 1.00150.54 S ANISOU 1173 SG CYS A 180 21775 22576 12847 357 -591 1929 S ATOM 1174 N GLU A 181 11.015 35.450 9.795 1.00142.79 N ANISOU 1174 N GLU A 181 21183 20830 12242 527 -160 1663 N ATOM 1175 CA GLU A 181 11.956 36.476 9.331 1.00142.07 C ANISOU 1175 CA GLU A 181 21086 20668 12226 678 28 1771 C ATOM 1176 C GLU A 181 11.850 37.741 10.161 1.00142.17 C ANISOU 1176 C GLU A 181 21003 20598 12419 766 79 1930 C ATOM 1177 O GLU A 181 10.808 38.402 10.192 1.00141.35 O ANISOU 1177 O GLU A 181 20832 20639 12235 825 20 2061 O ATOM 1178 CB GLU A 181 11.934 36.717 7.808 1.00145.68 C ANISOU 1178 CB GLU A 181 21593 21316 12443 746 89 1840 C ATOM 1179 CG GLU A 181 13.145 36.158 7.070 1.00158.80 C ANISOU 1179 CG GLU A 181 23357 22920 14060 776 200 1727 C ATOM 1180 CD GLU A 181 13.486 34.701 7.311 1.00178.60 C ANISOU 1180 CD GLU A 181 25983 25324 16552 694 121 1489 C ATOM 1181 OE1 GLU A 181 14.558 34.437 7.900 1.00168.74 O ANISOU 1181 OE1 GLU A 181 24747 23893 15473 728 199 1403 O ATOM 1182 OE2 GLU A 181 12.682 33.824 6.922 1.00175.10 O ANISOU 1182 OE2 GLU A 181 25632 24983 15916 594 -26 1392 O ATOM 1183 N THR A 182 12.946 38.096 10.827 1.00136.72 N ANISOU 1183 N THR A 182 20313 19679 11954 786 186 1918 N ATOM 1184 CA THR A 182 12.952 39.183 11.810 1.00135.03 C ANISOU 1184 CA THR A 182 20048 19325 11931 843 219 2032 C ATOM 1185 C THR A 182 13.044 40.613 11.260 1.00138.00 C ANISOU 1185 C THR A 182 20460 19693 12281 962 324 2238 C ATOM 1186 O THR A 182 13.295 41.550 12.019 1.00137.48 O ANISOU 1186 O THR A 182 20407 19453 12376 1003 365 2322 O ATOM 1187 CB THR A 182 14.079 38.986 12.847 1.00141.95 C ANISOU 1187 CB THR A 182 20914 19963 13059 788 274 1935 C ATOM 1188 OG1 THR A 182 14.049 40.056 13.799 1.00141.02 O ANISOU 1188 OG1 THR A 182 20771 19700 13108 833 292 2036 O ATOM 1189 CG2 THR A 182 15.436 38.961 12.161 1.00141.08 C ANISOU 1189 CG2 THR A 182 20838 19807 12959 787 422 1919 C ATOM 1190 N ASP A 183 12.838 40.788 9.959 1.00134.27 N ANISOU 1190 N ASP A 183 20026 19394 11597 1012 361 2321 N ATOM 1191 CA ASP A 183 12.827 42.143 9.359 1.00134.75 C ANISOU 1191 CA ASP A 183 20149 19449 11602 1127 449 2537 C ATOM 1192 C ASP A 183 14.256 42.758 9.247 1.00137.58 C ANISOU 1192 C ASP A 183 20565 19621 12090 1079 610 2598 C ATOM 1193 O ASP A 183 14.500 43.594 8.378 1.00138.45 O ANISOU 1193 O ASP A 183 20745 19757 12102 1122 700 2762 O ATOM 1194 CB ASP A 183 11.711 43.028 9.978 1.00136.47 C ANISOU 1194 CB ASP A 183 20362 19672 11816 1262 370 2661 C ATOM 1195 CG ASP A 183 11.280 44.243 9.176 1.00145.03 C ANISOU 1195 CG ASP A 183 21538 20814 12753 1426 415 2884 C ATOM 1196 OD1 ASP A 183 11.831 45.340 9.420 1.00145.62 O ANISOU 1196 OD1 ASP A 183 21732 20660 12937 1471 497 3008 O ATOM 1197 OD2 ASP A 183 10.318 44.123 8.390 1.00150.23 O ANISOU 1197 OD2 ASP A 183 22159 21742 13179 1509 352 2940 O ATOM 1198 N PHE A 184 15.191 42.331 10.119 1.00132.22 N ANISOU 1198 N PHE A 184 19847 18779 11614 979 640 2476 N ATOM 1199 CA PHE A 184 16.584 42.786 10.154 1.00132.10 C ANISOU 1199 CA PHE A 184 19840 18634 11719 899 779 2521 C ATOM 1200 C PHE A 184 17.642 41.671 10.142 1.00134.48 C ANISOU 1200 C PHE A 184 20064 18978 12055 827 831 2349 C ATOM 1201 O PHE A 184 18.821 41.930 10.395 1.00134.10 O ANISOU 1201 O PHE A 184 19975 18856 12119 753 934 2369 O ATOM 1202 CB PHE A 184 16.740 43.793 11.327 1.00133.31 C ANISOU 1202 CB PHE A 184 20037 18534 12083 873 774 2599 C ATOM 1203 CG PHE A 184 16.122 43.414 12.659 1.00132.95 C ANISOU 1203 CG PHE A 184 19947 18391 12179 889 652 2478 C ATOM 1204 CD1 PHE A 184 16.729 42.477 13.486 1.00134.36 C ANISOU 1204 CD1 PHE A 184 20036 18514 12502 801 634 2303 C ATOM 1205 CD2 PHE A 184 14.970 44.048 13.116 1.00134.88 C ANISOU 1205 CD2 PHE A 184 20238 18609 12403 1008 561 2552 C ATOM 1206 CE1 PHE A 184 16.167 42.142 14.723 1.00133.42 C ANISOU 1206 CE1 PHE A 184 19874 18314 12505 805 522 2206 C ATOM 1207 CE2 PHE A 184 14.405 43.704 14.350 1.00135.84 C ANISOU 1207 CE2 PHE A 184 20299 18679 12637 1024 454 2450 C ATOM 1208 CZ PHE A 184 15.008 42.756 15.145 1.00132.20 C ANISOU 1208 CZ PHE A 184 19750 18159 12323 908 435 2280 C ATOM 1209 N TYR A 185 17.212 40.433 9.799 1.00130.33 N ANISOU 1209 N TYR A 185 19527 18584 11407 853 755 2187 N ATOM 1210 CA TYR A 185 18.046 39.227 9.698 1.00130.07 C ANISOU 1210 CA TYR A 185 19471 18592 11358 841 782 2002 C ATOM 1211 C TYR A 185 19.322 39.405 8.868 1.00134.93 C ANISOU 1211 C TYR A 185 20052 19312 11904 854 951 2052 C ATOM 1212 O TYR A 185 20.320 38.726 9.117 1.00133.84 O ANISOU 1212 O TYR A 185 19862 19178 11814 862 1006 1934 O ATOM 1213 CB TYR A 185 17.219 38.016 9.216 1.00131.80 C ANISOU 1213 CB TYR A 185 19755 18927 11396 863 660 1848 C ATOM 1214 CG TYR A 185 16.723 38.099 7.787 1.00135.96 C ANISOU 1214 CG TYR A 185 20336 19667 11657 915 673 1914 C ATOM 1215 CD1 TYR A 185 17.349 37.386 6.769 1.00139.62 C ANISOU 1215 CD1 TYR A 185 20847 20262 11939 966 738 1822 C ATOM 1216 CD2 TYR A 185 15.598 38.853 7.458 1.00137.19 C ANISOU 1216 CD2 TYR A 185 20497 19911 11719 935 615 2063 C ATOM 1217 CE1 TYR A 185 16.893 37.449 5.453 1.00142.20 C ANISOU 1217 CE1 TYR A 185 21226 20797 12009 1013 747 1878 C ATOM 1218 CE2 TYR A 185 15.143 38.937 6.142 1.00139.83 C ANISOU 1218 CE2 TYR A 185 20873 20459 11796 986 624 2131 C ATOM 1219 CZ TYR A 185 15.786 38.223 5.145 1.00148.37 C ANISOU 1219 CZ TYR A 185 22003 21663 12709 1013 688 2035 C ATOM 1220 OH TYR A 185 15.340 38.288 3.849 1.00151.43 O ANISOU 1220 OH TYR A 185 22433 22272 12832 1062 694 2095 O ATOM 1221 N ASP A 186 19.274 40.327 7.886 1.00133.16 N ANISOU 1221 N ASP A 186 19851 19193 11550 867 1032 2239 N ATOM 1222 CA ASP A 186 20.376 40.702 6.996 1.00134.48 C ANISOU 1222 CA ASP A 186 19973 19504 11619 859 1198 2342 C ATOM 1223 C ASP A 186 21.309 41.715 7.682 1.00136.90 C ANISOU 1223 C ASP A 186 20219 19683 12112 736 1289 2484 C ATOM 1224 O ASP A 186 22.496 41.766 7.349 1.00138.18 O ANISOU 1224 O ASP A 186 20287 19971 12244 691 1421 2524 O ATOM 1225 CB ASP A 186 19.825 41.296 5.682 1.00138.07 C ANISOU 1225 CB ASP A 186 20495 20120 11846 906 1231 2503 C ATOM 1226 CG ASP A 186 20.007 40.415 4.460 1.00151.03 C ANISOU 1226 CG ASP A 186 22142 22012 13230 998 1273 2407 C ATOM 1227 OD1 ASP A 186 19.482 39.279 4.461 1.00150.89 O ANISOU 1227 OD1 ASP A 186 22173 22019 13140 1055 1166 2205 O ATOM 1228 OD2 ASP A 186 20.636 40.878 3.485 1.00160.01 O ANISOU 1228 OD2 ASP A 186 23252 23321 14222 1005 1405 2539 O ATOM 1229 N VAL A 187 20.767 42.525 8.628 1.00130.02 N ANISOU 1229 N VAL A 187 19403 18583 11414 679 1216 2560 N ATOM 1230 CA VAL A 187 21.525 43.545 9.362 1.00128.79 C ANISOU 1230 CA VAL A 187 19240 18262 11434 538 1272 2689 C ATOM 1231 C VAL A 187 22.366 42.844 10.434 1.00130.24 C ANISOU 1231 C VAL A 187 19298 18393 11793 483 1270 2527 C ATOM 1232 O VAL A 187 21.818 42.408 11.449 1.00128.04 O ANISOU 1232 O VAL A 187 19028 17972 11649 513 1157 2397 O ATOM 1233 CB VAL A 187 20.626 44.669 9.967 1.00131.63 C ANISOU 1233 CB VAL A 187 19746 18380 11887 534 1188 2816 C ATOM 1234 CG1 VAL A 187 21.452 45.898 10.321 1.00132.41 C ANISOU 1234 CG1 VAL A 187 19906 18312 12092 365 1259 2992 C ATOM 1235 CG2 VAL A 187 19.483 45.051 9.034 1.00132.31 C ANISOU 1235 CG2 VAL A 187 19946 18542 11784 662 1149 2925 C ATOM 1236 N THR A 188 23.684 42.703 10.191 1.00127.08 N ANISOU 1236 N THR A 188 18768 18145 11371 414 1396 2542 N ATOM 1237 CA THR A 188 24.581 42.047 11.149 1.00125.45 C ANISOU 1237 CA THR A 188 18423 17935 11306 383 1404 2403 C ATOM 1238 C THR A 188 25.181 43.008 12.170 1.00127.69 C ANISOU 1238 C THR A 188 18677 18052 11786 190 1414 2506 C ATOM 1239 O THR A 188 25.744 42.542 13.158 1.00126.40 O ANISOU 1239 O THR A 188 18409 17854 11762 163 1393 2392 O ATOM 1240 CB THR A 188 25.601 41.096 10.496 1.00135.61 C ANISOU 1240 CB THR A 188 19567 19509 12449 473 1512 2311 C ATOM 1241 OG1 THR A 188 26.586 41.844 9.788 1.00139.22 O ANISOU 1241 OG1 THR A 188 19924 20165 12807 359 1660 2499 O ATOM 1242 CG2 THR A 188 24.951 40.034 9.609 1.00134.36 C ANISOU 1242 CG2 THR A 188 19488 19466 12097 670 1474 2167 C ATOM 1243 N TRP A 189 25.049 44.336 11.958 1.00124.15 N ANISOU 1243 N TRP A 189 18346 17488 11339 55 1434 2720 N ATOM 1244 CA TRP A 189 25.541 45.312 12.936 1.00123.49 C ANISOU 1244 CA TRP A 189 18293 17201 11427 -150 1421 2815 C ATOM 1245 C TRP A 189 24.541 45.483 14.088 1.00122.10 C ANISOU 1245 C TRP A 189 18248 16727 11417 -91 1275 2730 C ATOM 1246 O TRP A 189 24.955 45.693 15.228 1.00120.66 O ANISOU 1246 O TRP A 189 18040 16401 11405 -200 1237 2689 O ATOM 1247 CB TRP A 189 25.960 46.655 12.297 1.00125.17 C ANISOU 1247 CB TRP A 189 18612 17384 11563 -347 1497 3081 C ATOM 1248 CG TRP A 189 24.850 47.527 11.772 1.00126.91 C ANISOU 1248 CG TRP A 189 19086 17426 11708 -277 1447 3218 C ATOM 1249 CD1 TRP A 189 24.513 47.719 10.464 1.00131.43 C ANISOU 1249 CD1 TRP A 189 19721 18141 12077 -205 1504 3342 C ATOM 1250 CD2 TRP A 189 24.029 48.431 12.534 1.00126.32 C ANISOU 1250 CD2 TRP A 189 19245 17009 11741 -267 1339 3266 C ATOM 1251 NE1 TRP A 189 23.496 48.644 10.366 1.00131.34 N ANISOU 1251 NE1 TRP A 189 19960 17901 12041 -138 1433 3465 N ATOM 1252 CE2 TRP A 189 23.173 49.090 11.622 1.00131.61 C ANISOU 1252 CE2 TRP A 189 20108 17637 12259 -159 1332 3417 C ATOM 1253 CE3 TRP A 189 23.908 48.722 13.907 1.00126.19 C ANISOU 1253 CE3 TRP A 189 19297 16731 11920 -311 1244 3189 C ATOM 1254 CZ2 TRP A 189 22.211 50.021 12.036 1.00131.03 C ANISOU 1254 CZ2 TRP A 189 20297 17273 12217 -68 1236 3493 C ATOM 1255 CZ3 TRP A 189 22.949 49.636 14.316 1.00127.74 C ANISOU 1255 CZ3 TRP A 189 19754 16636 12145 -227 1150 3255 C ATOM 1256 CH2 TRP A 189 22.117 50.279 13.388 1.00129.79 C ANISOU 1256 CH2 TRP A 189 20208 16863 12245 -95 1147 3406 C ATOM 1257 N PHE A 190 23.229 45.392 13.781 1.00116.02 N ANISOU 1257 N PHE A 190 17603 15901 10579 84 1195 2708 N ATOM 1258 CA PHE A 190 22.142 45.486 14.756 1.00113.30 C ANISOU 1258 CA PHE A 190 17357 15348 10344 180 1059 2634 C ATOM 1259 C PHE A 190 21.985 44.158 15.496 1.00113.46 C ANISOU 1259 C PHE A 190 17242 15424 10444 260 989 2406 C ATOM 1260 O PHE A 190 21.705 44.167 16.694 1.00111.08 O ANISOU 1260 O PHE A 190 16948 14963 10294 257 903 2329 O ATOM 1261 CB PHE A 190 20.826 45.885 14.071 1.00115.39 C ANISOU 1261 CB PHE A 190 17770 15606 10468 340 1005 2718 C ATOM 1262 CG PHE A 190 19.638 46.049 14.993 1.00115.46 C ANISOU 1262 CG PHE A 190 17861 15463 10546 468 872 2666 C ATOM 1263 CD1 PHE A 190 19.445 47.230 15.702 1.00118.92 C ANISOU 1263 CD1 PHE A 190 18468 15646 11069 458 835 2764 C ATOM 1264 CD2 PHE A 190 18.688 45.042 15.116 1.00115.89 C ANISOU 1264 CD2 PHE A 190 17835 15643 10555 599 780 2526 C ATOM 1265 CE1 PHE A 190 18.338 47.388 16.542 1.00118.57 C ANISOU 1265 CE1 PHE A 190 18488 15502 11061 615 720 2716 C ATOM 1266 CE2 PHE A 190 17.580 45.202 15.956 1.00117.48 C ANISOU 1266 CE2 PHE A 190 18077 15764 10795 715 662 2495 C ATOM 1267 CZ PHE A 190 17.411 46.375 16.660 1.00115.94 C ANISOU 1267 CZ PHE A 190 18027 15344 10679 743 639 2588 C ATOM 1268 N LYS A 191 22.160 43.024 14.780 1.00109.47 N ANISOU 1268 N LYS A 191 16639 15134 9822 335 1020 2300 N ATOM 1269 CA LYS A 191 22.083 41.670 15.331 1.00107.59 C ANISOU 1269 CA LYS A 191 16315 14937 9626 408 953 2087 C ATOM 1270 C LYS A 191 23.112 41.452 16.448 1.00111.00 C ANISOU 1270 C LYS A 191 16633 15307 10236 322 969 2010 C ATOM 1271 O LYS A 191 22.816 40.736 17.404 1.00109.24 O ANISOU 1271 O LYS A 191 16385 15004 10116 359 876 1868 O ATOM 1272 CB LYS A 191 22.290 40.622 14.232 1.00110.77 C ANISOU 1272 CB LYS A 191 16684 15560 9842 503 1000 2002 C ATOM 1273 CG LYS A 191 21.009 39.990 13.713 1.00123.48 C ANISOU 1273 CG LYS A 191 18387 17218 11314 606 896 1933 C ATOM 1274 CD LYS A 191 21.308 38.618 13.104 1.00135.11 C ANISOU 1274 CD LYS A 191 19854 18834 12648 693 900 1767 C ATOM 1275 CE LYS A 191 20.135 37.971 12.402 1.00145.97 C ANISOU 1275 CE LYS A 191 21335 20283 13844 754 798 1704 C ATOM 1276 NZ LYS A 191 19.083 37.493 13.341 1.00153.27 N ANISOU 1276 NZ LYS A 191 22295 21095 14847 725 634 1617 N ATOM 1277 N VAL A 192 24.311 42.063 16.328 1.00108.98 N ANISOU 1277 N VAL A 192 16297 15108 10001 195 1083 2113 N ATOM 1278 CA VAL A 192 25.383 41.948 17.329 1.00108.63 C ANISOU 1278 CA VAL A 192 16116 15054 10103 94 1104 2062 C ATOM 1279 C VAL A 192 25.214 42.922 18.491 1.00111.88 C ANISOU 1279 C VAL A 192 16598 15219 10693 -37 1036 2115 C ATOM 1280 O VAL A 192 25.671 42.631 19.595 1.00110.32 O ANISOU 1280 O VAL A 192 16312 14969 10636 -81 998 2023 O ATOM 1281 CB VAL A 192 26.827 41.957 16.753 1.00114.73 C ANISOU 1281 CB VAL A 192 16720 16076 10795 13 1250 2129 C ATOM 1282 CG1 VAL A 192 27.042 40.810 15.769 1.00115.22 C ANISOU 1282 CG1 VAL A 192 16718 16386 10677 199 1310 2030 C ATOM 1283 CG2 VAL A 192 27.191 43.303 16.124 1.00116.66 C ANISOU 1283 CG2 VAL A 192 17013 16330 10984 -176 1331 2363 C ATOM 1284 N MET A 193 24.570 44.074 18.241 1.00109.57 N ANISOU 1284 N MET A 193 16479 14773 10380 -82 1017 2261 N ATOM 1285 CA MET A 193 24.321 45.086 19.263 1.00109.44 C ANISOU 1285 CA MET A 193 16590 14491 10499 -174 946 2311 C ATOM 1286 C MET A 193 23.200 44.645 20.220 1.00112.36 C ANISOU 1286 C MET A 193 17002 14735 10953 -24 813 2176 C ATOM 1287 O MET A 193 23.266 44.958 21.407 1.00111.37 O ANISOU 1287 O MET A 193 16896 14449 10970 -79 751 2132 O ATOM 1288 CB MET A 193 24.015 46.441 18.626 1.00113.55 C ANISOU 1288 CB MET A 193 17325 14877 10943 -236 967 2514 C ATOM 1289 CG MET A 193 24.447 47.603 19.482 1.00118.39 C ANISOU 1289 CG MET A 193 18073 15240 11669 -425 939 2597 C ATOM 1290 SD MET A 193 23.738 49.176 18.943 1.00125.04 S ANISOU 1290 SD MET A 193 19270 15821 12418 -424 918 2812 S ATOM 1291 CE MET A 193 22.070 49.030 19.606 1.00119.89 C ANISOU 1291 CE MET A 193 18732 15036 11784 -108 784 2700 C ATOM 1292 N THR A 194 22.191 43.905 19.712 1.00108.61 N ANISOU 1292 N THR A 194 16533 14357 10377 148 768 2113 N ATOM 1293 CA THR A 194 21.102 43.368 20.540 1.00106.61 C ANISOU 1293 CA THR A 194 16286 14051 10170 268 642 1998 C ATOM 1294 C THR A 194 21.563 42.094 21.250 1.00109.10 C ANISOU 1294 C THR A 194 16453 14431 10570 261 611 1823 C ATOM 1295 O THR A 194 20.990 41.726 22.276 1.00107.41 O ANISOU 1295 O THR A 194 16223 14148 10440 298 511 1732 O ATOM 1296 CB THR A 194 19.824 43.127 19.734 1.00112.91 C ANISOU 1296 CB THR A 194 17143 14953 10806 415 592 2018 C ATOM 1297 OG1 THR A 194 20.102 42.266 18.631 1.00112.10 O ANISOU 1297 OG1 THR A 194 16981 15041 10570 431 647 1983 O ATOM 1298 CG2 THR A 194 19.162 44.417 19.278 1.00112.38 C ANISOU 1298 CG2 THR A 194 17240 14800 10657 476 595 2188 C ATOM 1299 N ALA A 195 22.598 41.424 20.699 1.00105.70 N ANISOU 1299 N ALA A 195 15918 14144 10101 230 699 1784 N ATOM 1300 CA ALA A 195 23.197 40.224 21.276 1.00104.28 C ANISOU 1300 CA ALA A 195 15619 14024 9978 253 683 1628 C ATOM 1301 C ALA A 195 23.882 40.590 22.592 1.00106.88 C ANISOU 1301 C ALA A 195 15876 14245 10490 151 667 1608 C ATOM 1302 O ALA A 195 23.747 39.858 23.567 1.00105.22 O ANISOU 1302 O ALA A 195 15622 13990 10368 185 588 1487 O ATOM 1303 CB ALA A 195 24.206 39.623 20.311 1.00106.32 C ANISOU 1303 CB ALA A 195 15794 14482 10123 283 795 1611 C ATOM 1304 N ILE A 196 24.565 41.747 22.636 1.00103.79 N ANISOU 1304 N ILE A 196 15488 13804 10143 8 731 1733 N ATOM 1305 CA ILE A 196 25.245 42.213 23.841 1.00103.06 C ANISOU 1305 CA ILE A 196 15341 13611 10205 -124 710 1724 C ATOM 1306 C ILE A 196 24.270 42.892 24.805 1.00105.21 C ANISOU 1306 C ILE A 196 15752 13653 10569 -112 600 1721 C ATOM 1307 O ILE A 196 24.150 42.437 25.940 1.00103.52 O ANISOU 1307 O ILE A 196 15485 13386 10461 -89 523 1612 O ATOM 1308 CB ILE A 196 26.520 43.040 23.525 1.00108.25 C ANISOU 1308 CB ILE A 196 15934 14341 10854 -325 815 1851 C ATOM 1309 CG1 ILE A 196 27.523 42.196 22.709 1.00109.78 C ANISOU 1309 CG1 ILE A 196 15941 14830 10942 -289 926 1834 C ATOM 1310 CG2 ILE A 196 27.176 43.565 24.808 1.00109.17 C ANISOU 1310 CG2 ILE A 196 16008 14353 11120 -492 775 1840 C ATOM 1311 CD1 ILE A 196 28.350 42.981 21.707 1.00119.58 C ANISOU 1311 CD1 ILE A 196 17144 16218 12072 -443 1049 2007 C ATOM 1312 N ILE A 197 23.552 43.940 24.345 1.00101.97 N ANISOU 1312 N ILE A 197 15522 13122 10100 -100 592 1840 N ATOM 1313 CA ILE A 197 22.568 44.701 25.133 1.00101.10 C ANISOU 1313 CA ILE A 197 15571 12810 10034 -35 496 1850 C ATOM 1314 C ILE A 197 21.536 43.811 25.856 1.00102.00 C ANISOU 1314 C ILE A 197 15628 12959 10168 122 391 1722 C ATOM 1315 O ILE A 197 21.268 44.039 27.038 1.00100.94 O ANISOU 1315 O ILE A 197 15514 12711 10128 136 315 1668 O ATOM 1316 CB ILE A 197 21.941 45.872 24.292 1.00105.93 C ANISOU 1316 CB ILE A 197 16401 13315 10534 9 513 2009 C ATOM 1317 CG1 ILE A 197 22.904 47.096 24.167 1.00108.57 C ANISOU 1317 CG1 ILE A 197 16864 13497 10888 -202 571 2144 C ATOM 1318 CG2 ILE A 197 20.511 46.281 24.713 1.00106.02 C ANISOU 1318 CG2 ILE A 197 16552 13225 10507 211 415 2008 C ATOM 1319 CD1 ILE A 197 23.289 47.896 25.500 1.00114.68 C ANISOU 1319 CD1 ILE A 197 17746 14032 11795 -330 506 2119 C ATOM 1320 N ASN A 198 21.009 42.777 25.172 1.00 96.83 N ANISOU 1320 N ASN A 198 14904 12471 9416 218 383 1674 N ATOM 1321 CA ASN A 198 20.013 41.868 25.751 1.00 94.61 C ANISOU 1321 CA ASN A 198 14572 12248 9125 320 277 1572 C ATOM 1322 C ASN A 198 20.549 40.548 26.354 1.00 96.45 C ANISOU 1322 C ASN A 198 14674 12544 9431 286 249 1431 C ATOM 1323 O ASN A 198 19.799 39.862 27.052 1.00 95.00 O ANISOU 1323 O ASN A 198 14458 12380 9256 329 150 1356 O ATOM 1324 CB ASN A 198 18.845 41.637 24.787 1.00 94.18 C ANISOU 1324 CB ASN A 198 14563 12320 8901 431 246 1615 C ATOM 1325 CG ASN A 198 18.078 42.896 24.479 1.00113.01 C ANISOU 1325 CG ASN A 198 17083 14645 11211 522 244 1747 C ATOM 1326 OD1 ASN A 198 17.055 43.194 25.099 1.00106.63 O ANISOU 1326 OD1 ASN A 198 16301 13833 10379 633 161 1754 O ATOM 1327 ND2 ASN A 198 18.566 43.679 23.528 1.00105.12 N ANISOU 1327 ND2 ASN A 198 16178 13607 10158 490 335 1862 N ATOM 1328 N PHE A 199 21.830 40.199 26.116 1.00 92.61 N ANISOU 1328 N PHE A 199 14109 12100 8980 216 333 1404 N ATOM 1329 CA PHE A 199 22.400 38.970 26.671 1.00 91.24 C ANISOU 1329 CA PHE A 199 13832 11977 8857 224 310 1275 C ATOM 1330 C PHE A 199 23.798 39.126 27.266 1.00 95.82 C ANISOU 1330 C PHE A 199 14298 12562 9547 139 372 1260 C ATOM 1331 O PHE A 199 23.934 38.922 28.466 1.00 94.92 O ANISOU 1331 O PHE A 199 14131 12389 9546 118 310 1194 O ATOM 1332 CB PHE A 199 22.299 37.789 25.689 1.00 93.08 C ANISOU 1332 CB PHE A 199 14081 12330 8953 303 318 1212 C ATOM 1333 CG PHE A 199 22.787 36.452 26.203 1.00 93.89 C ANISOU 1333 CG PHE A 199 14140 12453 9082 348 280 1077 C ATOM 1334 CD1 PHE A 199 21.926 35.591 26.875 1.00 95.73 C ANISOU 1334 CD1 PHE A 199 14420 12634 9319 364 152 997 C ATOM 1335 CD2 PHE A 199 24.095 36.033 25.972 1.00 96.70 C ANISOU 1335 CD2 PHE A 199 14413 12895 9432 383 371 1040 C ATOM 1336 CE1 PHE A 199 22.372 34.347 27.330 1.00 96.32 C ANISOU 1336 CE1 PHE A 199 14499 12693 9404 409 109 881 C ATOM 1337 CE2 PHE A 199 24.541 34.791 26.430 1.00 99.27 C ANISOU 1337 CE2 PHE A 199 14728 13228 9762 468 333 917 C ATOM 1338 CZ PHE A 199 23.676 33.955 27.104 1.00 96.24 C ANISOU 1338 CZ PHE A 199 14431 12743 9392 479 200 837 C ATOM 1339 N TYR A 200 24.827 39.466 26.455 1.00 93.77 N ANISOU 1339 N TYR A 200 13985 12403 9240 83 490 1328 N ATOM 1340 CA TYR A 200 26.221 39.603 26.915 1.00 94.38 C ANISOU 1340 CA TYR A 200 13914 12558 9388 -15 554 1332 C ATOM 1341 C TYR A 200 26.446 40.625 28.035 1.00 96.30 C ANISOU 1341 C TYR A 200 14160 12664 9766 -168 515 1369 C ATOM 1342 O TYR A 200 27.252 40.371 28.933 1.00 95.07 O ANISOU 1342 O TYR A 200 13875 12551 9695 -220 504 1315 O ATOM 1343 CB TYR A 200 27.205 39.793 25.743 1.00 98.15 C ANISOU 1343 CB TYR A 200 14313 13227 9753 -55 691 1419 C ATOM 1344 CG TYR A 200 27.283 38.589 24.827 1.00101.01 C ANISOU 1344 CG TYR A 200 14653 13750 9978 122 731 1343 C ATOM 1345 CD1 TYR A 200 28.084 37.495 25.148 1.00103.56 C ANISOU 1345 CD1 TYR A 200 14856 14200 10291 234 745 1233 C ATOM 1346 CD2 TYR A 200 26.553 38.539 23.642 1.00101.99 C ANISOU 1346 CD2 TYR A 200 14894 13893 9965 194 750 1376 C ATOM 1347 CE1 TYR A 200 28.149 36.377 24.316 1.00105.23 C ANISOU 1347 CE1 TYR A 200 15100 14526 10358 423 773 1149 C ATOM 1348 CE2 TYR A 200 26.597 37.420 22.810 1.00103.29 C ANISOU 1348 CE2 TYR A 200 15074 14184 9986 356 775 1290 C ATOM 1349 CZ TYR A 200 27.402 36.343 23.149 1.00111.33 C ANISOU 1349 CZ TYR A 200 16005 15299 10995 475 786 1173 C ATOM 1350 OH TYR A 200 27.474 35.242 22.332 1.00113.24 O ANISOU 1350 OH TYR A 200 16309 15638 11078 658 805 1077 O ATOM 1351 N LEU A 201 25.719 41.761 27.991 1.00 92.48 N ANISOU 1351 N LEU A 201 13838 12013 9286 -221 486 1457 N ATOM 1352 CA LEU A 201 25.779 42.802 29.016 1.00 92.17 C ANISOU 1352 CA LEU A 201 13873 11797 9351 -346 433 1483 C ATOM 1353 C LEU A 201 25.087 42.308 30.306 1.00 92.38 C ANISOU 1353 C LEU A 201 13892 11740 9468 -250 318 1362 C ATOM 1354 O LEU A 201 25.799 42.227 31.311 1.00 91.74 O ANISOU 1354 O LEU A 201 13713 11660 9483 -334 293 1307 O ATOM 1355 CB LEU A 201 25.225 44.155 28.519 1.00 93.73 C ANISOU 1355 CB LEU A 201 14294 11822 9499 -393 437 1613 C ATOM 1356 CG LEU A 201 25.289 45.333 29.499 1.00 99.78 C ANISOU 1356 CG LEU A 201 15207 12358 10345 -515 376 1638 C ATOM 1357 CD1 LEU A 201 26.620 46.072 29.391 1.00102.25 C ANISOU 1357 CD1 LEU A 201 15498 12679 10672 -793 436 1731 C ATOM 1358 CD2 LEU A 201 24.121 46.289 29.272 1.00103.41 C ANISOU 1358 CD2 LEU A 201 15932 12616 10742 -401 330 1708 C ATOM 1359 N PRO A 202 23.776 41.893 30.330 1.00 86.29 N ANISOU 1359 N PRO A 202 13191 10940 8655 -89 246 1322 N ATOM 1360 CA PRO A 202 23.212 41.376 31.593 1.00 83.86 C ANISOU 1360 CA PRO A 202 12847 10597 8421 -24 141 1221 C ATOM 1361 C PRO A 202 23.954 40.155 32.154 1.00 85.32 C ANISOU 1361 C PRO A 202 12867 10888 8664 -28 131 1118 C ATOM 1362 O PRO A 202 24.330 40.215 33.318 1.00 84.84 O ANISOU 1362 O PRO A 202 12747 10786 8701 -76 86 1067 O ATOM 1363 CB PRO A 202 21.739 41.097 31.266 1.00 84.91 C ANISOU 1363 CB PRO A 202 13053 10753 8457 122 79 1226 C ATOM 1364 CG PRO A 202 21.667 41.025 29.806 1.00 90.46 C ANISOU 1364 CG PRO A 202 13795 11534 9041 145 150 1293 C ATOM 1365 CD PRO A 202 22.749 41.906 29.264 1.00 87.70 C ANISOU 1365 CD PRO A 202 13470 11146 8706 23 251 1379 C ATOM 1366 N THR A 203 24.259 39.112 31.332 1.00 80.37 N ANISOU 1366 N THR A 203 12182 10390 7966 30 175 1088 N ATOM 1367 CA THR A 203 24.993 37.921 31.796 1.00 79.19 C ANISOU 1367 CA THR A 203 11913 10328 7848 71 167 992 C ATOM 1368 C THR A 203 26.330 38.193 32.481 1.00 83.39 C ANISOU 1368 C THR A 203 12303 10915 8468 -22 209 987 C ATOM 1369 O THR A 203 26.733 37.401 33.326 1.00 82.64 O ANISOU 1369 O THR A 203 12119 10858 8424 21 167 908 O ATOM 1370 CB THR A 203 25.074 36.798 30.754 1.00 85.88 C ANISOU 1370 CB THR A 203 12774 11278 8576 180 202 953 C ATOM 1371 OG1 THR A 203 25.426 35.605 31.445 1.00 85.26 O ANISOU 1371 OG1 THR A 203 12648 11223 8526 256 152 851 O ATOM 1372 CG2 THR A 203 26.125 37.052 29.677 1.00 86.89 C ANISOU 1372 CG2 THR A 203 12839 11543 8633 168 335 1010 C ATOM 1373 N LEU A 204 27.017 39.285 32.118 1.00 81.05 N ANISOU 1373 N LEU A 204 11988 10634 8174 -160 284 1080 N ATOM 1374 CA LEU A 204 28.290 39.634 32.743 1.00 81.80 C ANISOU 1374 CA LEU A 204 11933 10815 8331 -296 316 1092 C ATOM 1375 C LEU A 204 28.073 40.364 34.076 1.00 84.75 C ANISOU 1375 C LEU A 204 12350 11035 8817 -400 225 1069 C ATOM 1376 O LEU A 204 28.758 40.056 35.053 1.00 84.36 O ANISOU 1376 O LEU A 204 12167 11050 8834 -436 194 1014 O ATOM 1377 CB LEU A 204 29.177 40.440 31.785 1.00 83.94 C ANISOU 1377 CB LEU A 204 12159 11198 8535 -445 428 1213 C ATOM 1378 CG LEU A 204 30.447 39.732 31.308 1.00 89.93 C ANISOU 1378 CG LEU A 204 12699 12249 9223 -414 525 1215 C ATOM 1379 CD1 LEU A 204 30.150 38.749 30.177 1.00 89.97 C ANISOU 1379 CD1 LEU A 204 12731 12347 9104 -202 578 1183 C ATOM 1380 CD2 LEU A 204 31.479 40.738 30.857 1.00 94.76 C ANISOU 1380 CD2 LEU A 204 13217 12998 9791 -649 613 1350 C ATOM 1381 N LEU A 205 27.097 41.302 34.119 1.00 80.58 N ANISOU 1381 N LEU A 205 12013 10310 8293 -419 179 1108 N ATOM 1382 CA LEU A 205 26.726 42.069 35.316 1.00 79.50 C ANISOU 1382 CA LEU A 205 11968 10005 8234 -475 89 1079 C ATOM 1383 C LEU A 205 26.049 41.163 36.337 1.00 80.60 C ANISOU 1383 C LEU A 205 12058 10148 8418 -334 -3 972 C ATOM 1384 O LEU A 205 26.254 41.333 37.537 1.00 80.22 O ANISOU 1384 O LEU A 205 11977 10060 8444 -381 -67 917 O ATOM 1385 CB LEU A 205 25.796 43.241 34.955 1.00 80.02 C ANISOU 1385 CB LEU A 205 12276 9873 8256 -464 71 1151 C ATOM 1386 CG LEU A 205 26.416 44.637 34.919 1.00 86.64 C ANISOU 1386 CG LEU A 205 13254 10569 9099 -673 88 1235 C ATOM 1387 CD1 LEU A 205 26.993 44.948 33.540 1.00 88.45 C ANISOU 1387 CD1 LEU A 205 13487 10872 9249 -780 196 1360 C ATOM 1388 CD2 LEU A 205 25.392 45.689 35.299 1.00 88.44 C ANISOU 1388 CD2 LEU A 205 13750 10545 9306 -599 16 1247 C ATOM 1389 N MET A 206 25.262 40.192 35.852 1.00 75.58 N ANISOU 1389 N MET A 206 11422 9569 7725 -181 -15 947 N ATOM 1390 CA MET A 206 24.552 39.197 36.647 1.00 73.93 C ANISOU 1390 CA MET A 206 11177 9382 7531 -72 -104 867 C ATOM 1391 C MET A 206 25.564 38.330 37.367 1.00 77.96 C ANISOU 1391 C MET A 206 11532 9985 8103 -85 -111 799 C ATOM 1392 O MET A 206 25.421 38.109 38.568 1.00 76.56 O ANISOU 1392 O MET A 206 11314 9789 7985 -77 -189 744 O ATOM 1393 CB MET A 206 23.729 38.324 35.718 1.00 75.80 C ANISOU 1393 CB MET A 206 11460 9673 7669 36 -107 871 C ATOM 1394 CG MET A 206 22.434 37.885 36.286 1.00 78.40 C ANISOU 1394 CG MET A 206 11826 9995 7967 110 -211 846 C ATOM 1395 SD MET A 206 21.403 37.301 34.934 1.00 82.63 S ANISOU 1395 SD MET A 206 12446 10596 8354 176 -211 884 S ATOM 1396 CE MET A 206 22.395 35.911 34.319 1.00 79.49 C ANISOU 1396 CE MET A 206 12014 10257 7933 191 -170 820 C ATOM 1397 N LEU A 207 26.598 37.858 36.625 1.00 76.09 N ANISOU 1397 N LEU A 207 11204 9871 7836 -88 -26 809 N ATOM 1398 CA LEU A 207 27.708 37.044 37.128 1.00 76.52 C ANISOU 1398 CA LEU A 207 11098 10058 7918 -61 -14 757 C ATOM 1399 C LEU A 207 28.508 37.831 38.176 1.00 82.22 C ANISOU 1399 C LEU A 207 11715 10797 8726 -206 -30 759 C ATOM 1400 O LEU A 207 28.750 37.301 39.260 1.00 81.41 O ANISOU 1400 O LEU A 207 11529 10728 8676 -175 -92 698 O ATOM 1401 CB LEU A 207 28.617 36.589 35.966 1.00 77.81 C ANISOU 1401 CB LEU A 207 11187 10383 7995 -8 96 782 C ATOM 1402 CG LEU A 207 28.587 35.095 35.579 1.00 82.46 C ANISOU 1402 CG LEU A 207 11799 11025 8507 191 89 713 C ATOM 1403 CD1 LEU A 207 27.235 34.666 35.009 1.00 81.40 C ANISOU 1403 CD1 LEU A 207 11854 10762 8312 252 35 700 C ATOM 1404 CD2 LEU A 207 29.661 34.783 34.554 1.00 87.14 C ANISOU 1404 CD2 LEU A 207 12297 11813 9000 268 207 733 C ATOM 1405 N TRP A 208 28.847 39.115 37.875 1.00 80.60 N ANISOU 1405 N TRP A 208 11543 10554 8526 -377 13 832 N ATOM 1406 CA TRP A 208 29.576 40.045 38.755 1.00 81.58 C ANISOU 1406 CA TRP A 208 11616 10669 8711 -571 -12 843 C ATOM 1407 C TRP A 208 28.890 40.193 40.119 1.00 82.10 C ANISOU 1407 C TRP A 208 11748 10599 8848 -549 -128 768 C ATOM 1408 O TRP A 208 29.570 40.154 41.148 1.00 81.98 O ANISOU 1408 O TRP A 208 11615 10651 8882 -620 -170 726 O ATOM 1409 CB TRP A 208 29.750 41.417 38.068 1.00 82.54 C ANISOU 1409 CB TRP A 208 11857 10700 8804 -765 35 943 C ATOM 1410 CG TRP A 208 30.225 42.535 38.957 1.00 85.33 C ANISOU 1410 CG TRP A 208 12255 10960 9205 -992 -19 952 C ATOM 1411 CD1 TRP A 208 29.460 43.516 39.517 1.00 88.40 C ANISOU 1411 CD1 TRP A 208 12875 11095 9617 -1031 -96 937 C ATOM 1412 CD2 TRP A 208 31.580 42.816 39.339 1.00 87.05 C ANISOU 1412 CD2 TRP A 208 12300 11347 9429 -1215 -4 979 C ATOM 1413 NE1 TRP A 208 30.250 44.382 40.240 1.00 89.71 N ANISOU 1413 NE1 TRP A 208 13057 11221 9808 -1275 -139 941 N ATOM 1414 CE2 TRP A 208 31.558 43.980 40.142 1.00 92.23 C ANISOU 1414 CE2 TRP A 208 13116 11809 10118 -1415 -86 973 C ATOM 1415 CE3 TRP A 208 32.813 42.189 39.092 1.00 89.53 C ANISOU 1415 CE3 TRP A 208 12334 11979 9704 -1256 66 1007 C ATOM 1416 CZ2 TRP A 208 32.722 44.537 40.691 1.00 93.50 C ANISOU 1416 CZ2 TRP A 208 13170 12078 10279 -1700 -107 998 C ATOM 1417 CZ3 TRP A 208 33.965 42.743 39.632 1.00 93.01 C ANISOU 1417 CZ3 TRP A 208 12630 12570 10141 -1520 54 1044 C ATOM 1418 CH2 TRP A 208 33.914 43.900 40.424 1.00 94.64 C ANISOU 1418 CH2 TRP A 208 13002 12572 10385 -1761 -36 1040 C ATOM 1419 N PHE A 209 27.552 40.340 40.115 1.00 75.86 N ANISOU 1419 N PHE A 209 11127 9653 8044 -442 -177 758 N ATOM 1420 CA PHE A 209 26.730 40.473 41.318 1.00 74.14 C ANISOU 1420 CA PHE A 209 10972 9337 7861 -385 -281 695 C ATOM 1421 C PHE A 209 26.647 39.154 42.087 1.00 75.64 C ANISOU 1421 C PHE A 209 11031 9634 8074 -273 -334 628 C ATOM 1422 O PHE A 209 26.708 39.170 43.317 1.00 74.58 O ANISOU 1422 O PHE A 209 10851 9500 7985 -287 -406 574 O ATOM 1423 CB PHE A 209 25.324 40.983 40.961 1.00 75.40 C ANISOU 1423 CB PHE A 209 11319 9366 7963 -278 -306 722 C ATOM 1424 CG PHE A 209 25.169 42.482 40.843 1.00 78.24 C ANISOU 1424 CG PHE A 209 11875 9548 8304 -352 -305 765 C ATOM 1425 CD1 PHE A 209 26.219 43.277 40.395 1.00 83.00 C ANISOU 1425 CD1 PHE A 209 12508 10108 8918 -549 -250 819 C ATOM 1426 CD2 PHE A 209 23.956 43.095 41.133 1.00 80.51 C ANISOU 1426 CD2 PHE A 209 12330 9718 8541 -219 -361 761 C ATOM 1427 CE1 PHE A 209 26.070 44.660 40.272 1.00 85.53 C ANISOU 1427 CE1 PHE A 209 13065 10222 9210 -634 -262 865 C ATOM 1428 CE2 PHE A 209 23.807 44.483 41.010 1.00 84.94 C ANISOU 1428 CE2 PHE A 209 13125 10081 9068 -253 -366 797 C ATOM 1429 CZ PHE A 209 24.862 45.254 40.573 1.00 84.61 C ANISOU 1429 CZ PHE A 209 13153 9950 9047 -469 -320 849 C ATOM 1430 N TYR A 210 26.520 38.017 41.364 1.00 70.84 N ANISOU 1430 N TYR A 210 10387 9105 7422 -164 -306 631 N ATOM 1431 CA TYR A 210 26.449 36.683 41.963 1.00 69.22 C ANISOU 1431 CA TYR A 210 10110 8969 7222 -61 -361 579 C ATOM 1432 C TYR A 210 27.775 36.279 42.606 1.00 73.42 C ANISOU 1432 C TYR A 210 10475 9624 7798 -82 -351 546 C ATOM 1433 O TYR A 210 27.767 35.663 43.674 1.00 72.30 O ANISOU 1433 O TYR A 210 10277 9508 7686 -37 -424 502 O ATOM 1434 CB TYR A 210 25.981 35.634 40.948 1.00 69.82 C ANISOU 1434 CB TYR A 210 10250 9060 7219 47 -344 587 C ATOM 1435 CG TYR A 210 25.766 34.284 41.589 1.00 70.83 C ANISOU 1435 CG TYR A 210 10370 9207 7336 136 -422 541 C ATOM 1436 CD1 TYR A 210 24.604 34.010 42.306 1.00 71.85 C ANISOU 1436 CD1 TYR A 210 10555 9292 7452 140 -522 537 C ATOM 1437 CD2 TYR A 210 26.750 33.301 41.539 1.00 72.10 C ANISOU 1437 CD2 TYR A 210 10470 9440 7486 220 -399 509 C ATOM 1438 CE1 TYR A 210 24.417 32.782 42.936 1.00 72.14 C ANISOU 1438 CE1 TYR A 210 10604 9335 7471 188 -603 512 C ATOM 1439 CE2 TYR A 210 26.575 32.070 42.165 1.00 72.62 C ANISOU 1439 CE2 TYR A 210 10571 9486 7533 304 -481 473 C ATOM 1440 CZ TYR A 210 25.406 31.816 42.865 1.00 79.20 C ANISOU 1440 CZ TYR A 210 11478 10254 8361 268 -586 479 C ATOM 1441 OH TYR A 210 25.223 30.602 43.475 1.00 81.98 O ANISOU 1441 OH TYR A 210 11887 10576 8685 320 -674 460 O ATOM 1442 N ALA A 211 28.908 36.644 41.965 1.00 71.30 N ANISOU 1442 N ALA A 211 10112 9460 7519 -153 -261 581 N ATOM 1443 CA ALA A 211 30.267 36.411 42.470 1.00 72.15 C ANISOU 1443 CA ALA A 211 10021 9750 7643 -183 -239 569 C ATOM 1444 C ALA A 211 30.471 37.194 43.773 1.00 75.95 C ANISOU 1444 C ALA A 211 10455 10210 8193 -325 -311 543 C ATOM 1445 O ALA A 211 31.363 36.866 44.554 1.00 76.48 O ANISOU 1445 O ALA A 211 10355 10427 8276 -335 -331 519 O ATOM 1446 CB ALA A 211 31.296 36.840 41.436 1.00 74.57 C ANISOU 1446 CB ALA A 211 10229 10207 7898 -264 -126 634 C ATOM 1447 N LYS A 212 29.624 38.218 44.007 1.00 71.40 N ANISOU 1447 N LYS A 212 10036 9451 7640 -413 -353 544 N ATOM 1448 CA LYS A 212 29.604 39.021 45.225 1.00 71.05 C ANISOU 1448 CA LYS A 212 10013 9340 7642 -525 -433 504 C ATOM 1449 C LYS A 212 28.685 38.359 46.276 1.00 73.03 C ANISOU 1449 C LYS A 212 10289 9551 7910 -385 -528 443 C ATOM 1450 O LYS A 212 29.037 38.347 47.459 1.00 73.21 O ANISOU 1450 O LYS A 212 10228 9625 7962 -418 -593 395 O ATOM 1451 CB LYS A 212 29.183 40.469 44.931 1.00 74.03 C ANISOU 1451 CB LYS A 212 10587 9530 8011 -657 -433 533 C ATOM 1452 CG LYS A 212 30.279 41.309 44.293 1.00 91.23 C ANISOU 1452 CG LYS A 212 12735 11753 10174 -881 -368 599 C ATOM 1453 CD LYS A 212 29.960 42.798 44.376 1.00102.48 C ANISOU 1453 CD LYS A 212 14399 12947 11590 -1038 -404 615 C ATOM 1454 CE LYS A 212 31.112 43.670 43.925 1.00116.60 C ANISOU 1454 CE LYS A 212 16170 14778 13356 -1329 -363 690 C ATOM 1455 NZ LYS A 212 32.257 43.644 44.879 1.00126.10 N ANISOU 1455 NZ LYS A 212 17178 16157 14577 -1509 -406 659 N ATOM 1456 N ILE A 213 27.523 37.790 45.841 1.00 67.24 N ANISOU 1456 N ILE A 213 9656 8751 7140 -245 -539 453 N ATOM 1457 CA ILE A 213 26.569 37.067 46.705 1.00 65.02 C ANISOU 1457 CA ILE A 213 9389 8467 6850 -134 -627 422 C ATOM 1458 C ILE A 213 27.274 35.828 47.280 1.00 70.19 C ANISOU 1458 C ILE A 213 9905 9242 7520 -75 -652 399 C ATOM 1459 O ILE A 213 27.239 35.620 48.492 1.00 69.62 O ANISOU 1459 O ILE A 213 9776 9208 7468 -65 -727 364 O ATOM 1460 CB ILE A 213 25.243 36.714 45.960 1.00 66.23 C ANISOU 1460 CB ILE A 213 9663 8566 6937 -40 -632 458 C ATOM 1461 CG1 ILE A 213 24.399 37.968 45.721 1.00 66.24 C ANISOU 1461 CG1 ILE A 213 9799 8465 6906 -48 -629 479 C ATOM 1462 CG2 ILE A 213 24.425 35.668 46.715 1.00 65.33 C ANISOU 1462 CG2 ILE A 213 9531 8499 6792 38 -720 449 C ATOM 1463 CD1 ILE A 213 23.406 37.839 44.621 1.00 72.27 C ANISOU 1463 CD1 ILE A 213 10657 9210 7593 20 -604 533 C ATOM 1464 N TYR A 214 27.952 35.048 46.404 1.00 68.31 N ANISOU 1464 N TYR A 214 9624 9070 7260 -18 -589 418 N ATOM 1465 CA TYR A 214 28.714 33.847 46.753 1.00 69.12 C ANISOU 1465 CA TYR A 214 9628 9282 7354 87 -601 401 C ATOM 1466 C TYR A 214 29.913 34.130 47.669 1.00 75.97 C ANISOU 1466 C TYR A 214 10310 10295 8259 32 -608 380 C ATOM 1467 O TYR A 214 30.385 33.215 48.336 1.00 75.49 O ANISOU 1467 O TYR A 214 10167 10325 8191 134 -646 363 O ATOM 1468 CB TYR A 214 29.257 33.173 45.484 1.00 71.27 C ANISOU 1468 CB TYR A 214 9910 9601 7569 186 -517 420 C ATOM 1469 CG TYR A 214 29.885 31.818 45.730 1.00 74.04 C ANISOU 1469 CG TYR A 214 10223 10029 7880 358 -536 399 C ATOM 1470 CD1 TYR A 214 29.122 30.656 45.687 1.00 75.60 C ANISOU 1470 CD1 TYR A 214 10584 10111 8030 469 -600 390 C ATOM 1471 CD2 TYR A 214 31.251 31.695 45.979 1.00 76.26 C ANISOU 1471 CD2 TYR A 214 10317 10506 8154 411 -493 395 C ATOM 1472 CE1 TYR A 214 29.694 29.406 45.920 1.00 77.66 C ANISOU 1472 CE1 TYR A 214 10866 10400 8241 645 -627 371 C ATOM 1473 CE2 TYR A 214 31.834 30.451 46.217 1.00 78.08 C ANISOU 1473 CE2 TYR A 214 10530 10808 8330 618 -512 378 C ATOM 1474 CZ TYR A 214 31.052 29.308 46.184 1.00 86.12 C ANISOU 1474 CZ TYR A 214 11756 11660 9305 744 -580 363 C ATOM 1475 OH TYR A 214 31.626 28.080 46.414 1.00 89.30 O ANISOU 1475 OH TYR A 214 12195 12093 9641 964 -606 347 O ATOM 1476 N LYS A 215 30.397 35.392 47.699 1.00 75.28 N ANISOU 1476 N LYS A 215 10172 10230 8201 -139 -579 385 N ATOM 1477 CA LYS A 215 31.511 35.831 48.549 1.00 76.78 C ANISOU 1477 CA LYS A 215 10188 10573 8413 -251 -596 369 C ATOM 1478 C LYS A 215 31.030 36.248 49.939 1.00 81.83 C ANISOU 1478 C LYS A 215 10855 11150 9088 -306 -701 317 C ATOM 1479 O LYS A 215 31.850 36.338 50.849 1.00 82.90 O ANISOU 1479 O LYS A 215 10844 11422 9231 -371 -740 293 O ATOM 1480 CB LYS A 215 32.147 37.133 48.019 1.00 80.41 C ANISOU 1480 CB LYS A 215 10629 11051 8873 -474 -541 402 C ATOM 1481 CG LYS A 215 33.484 37.493 48.666 1.00 92.87 C ANISOU 1481 CG LYS A 215 11993 12848 10444 -628 -550 404 C ATOM 1482 CD LYS A 215 33.979 38.869 48.220 1.00101.90 C ANISOU 1482 CD LYS A 215 13165 13973 11578 -910 -519 446 C ATOM 1483 CE LYS A 215 35.132 39.364 49.064 1.00111.43 C ANISOU 1483 CE LYS A 215 14188 15381 12770 -1126 -563 443 C ATOM 1484 NZ LYS A 215 35.600 40.709 48.632 1.00120.11 N ANISOU 1484 NZ LYS A 215 15351 16439 13845 -1449 -548 495 N ATOM 1485 N ALA A 216 29.709 36.475 50.103 1.00 78.42 N ANISOU 1485 N ALA A 216 10594 10545 8657 -269 -746 302 N ATOM 1486 CA ALA A 216 29.082 36.898 51.358 1.00 78.73 C ANISOU 1486 CA ALA A 216 10676 10533 8704 -285 -840 252 C ATOM 1487 C ALA A 216 28.685 35.719 52.255 1.00 85.03 C ANISOU 1487 C ALA A 216 11419 11399 9490 -150 -911 243 C ATOM 1488 O ALA A 216 28.780 35.832 53.480 1.00 85.20 O ANISOU 1488 O ALA A 216 11380 11478 9514 -168 -983 203 O ATOM 1489 CB ALA A 216 27.807 37.686 51.120 1.00 78.75 C ANISOU 1489 CB ALA A 216 10873 10366 8682 -270 -852 250 C ATOM 1490 N VAL A 217 28.245 34.599 51.655 1.00 83.24 N ANISOU 1490 N VAL A 217 11232 11158 9237 -29 -897 284 N ATOM 1491 CA VAL A 217 27.795 33.395 52.375 1.00 83.48 C ANISOU 1491 CA VAL A 217 11258 11220 9241 77 -971 296 C ATOM 1492 C VAL A 217 28.707 32.181 52.056 1.00 90.24 C ANISOU 1492 C VAL A 217 12058 12146 10084 187 -948 316 C ATOM 1493 O VAL A 217 28.212 31.067 51.849 1.00 89.77 O ANISOU 1493 O VAL A 217 12097 12028 9982 282 -979 346 O ATOM 1494 CB VAL A 217 26.272 33.077 52.239 1.00 86.13 C ANISOU 1494 CB VAL A 217 11728 11473 9525 109 -1014 330 C ATOM 1495 CG1 VAL A 217 25.439 33.950 53.175 1.00 85.74 C ANISOU 1495 CG1 VAL A 217 11687 11433 9457 75 -1069 307 C ATOM 1496 CG2 VAL A 217 25.786 33.199 50.794 1.00 85.47 C ANISOU 1496 CG2 VAL A 217 11759 11298 9417 109 -948 362 C ATOM 1497 N ARG A 218 30.025 32.387 52.123 1.00 89.04 N ANISOU 1497 N ARG A 218 11752 12129 9950 177 -906 301 N ATOM 1498 CA ARG A 218 30.994 31.325 51.815 1.00 90.11 C ANISOU 1498 CA ARG A 218 11818 12371 10050 330 -876 318 C ATOM 1499 C ARG A 218 32.071 30.993 52.876 1.00 95.81 C ANISOU 1499 C ARG A 218 12350 13289 10763 386 -913 309 C ATOM 1500 O ARG A 218 33.194 31.492 52.814 1.00 97.72 O ANISOU 1500 O ARG A 218 12409 13718 11002 336 -864 306 O ATOM 1501 CB ARG A 218 31.673 31.610 50.471 1.00 90.67 C ANISOU 1501 CB ARG A 218 11857 12493 10102 332 -762 333 C ATOM 1502 CG ARG A 218 32.858 30.707 50.170 1.00102.78 C ANISOU 1502 CG ARG A 218 13278 14201 11573 516 -715 344 C ATOM 1503 CD ARG A 218 33.967 31.468 49.461 1.00116.84 C ANISOU 1503 CD ARG A 218 14875 16183 13334 438 -613 364 C ATOM 1504 NE ARG A 218 34.170 30.992 48.096 1.00126.65 N ANISOU 1504 NE ARG A 218 16176 17436 14508 573 -520 383 N ATOM 1505 CZ ARG A 218 34.755 31.702 47.137 1.00138.70 C ANISOU 1505 CZ ARG A 218 17607 19087 16007 483 -418 415 C ATOM 1506 NH1 ARG A 218 35.199 32.926 47.392 1.00125.33 N ANISOU 1506 NH1 ARG A 218 15773 17494 14352 233 -405 436 N ATOM 1507 NH2 ARG A 218 34.898 31.189 45.923 1.00124.05 N ANISOU 1507 NH2 ARG A 218 15810 17250 14073 633 -336 427 N ATOM 1508 N GLN A 219 31.656 30.068 53.750 1.00 90.42 N ANISOU 1508 N GLN A 219 11724 12570 10061 488 -1000 318 N ATOM 1509 CA GLN A 219 32.450 29.424 54.784 1.00 89.99 C ANISOU 1509 CA GLN A 219 11541 12672 9980 597 -1053 324 C ATOM 1510 C GLN A 219 32.336 27.909 54.604 1.00 91.31 C ANISOU 1510 C GLN A 219 11860 12750 10082 819 -1084 360 C ATOM 1511 O GLN A 219 33.226 27.275 54.061 1.00 92.51 O ANISOU 1511 O GLN A 219 11984 12987 10179 1002 -1034 368 O ATOM 1512 CB GLN A 219 31.892 29.823 56.146 1.00 90.43 C ANISOU 1512 CB GLN A 219 11567 12732 10060 491 -1147 307 C ATOM 1513 CG GLN A 219 32.761 29.447 57.299 1.00101.93 C ANISOU 1513 CG GLN A 219 12856 14382 11490 562 -1203 310 C ATOM 1514 CD GLN A 219 34.094 29.000 56.834 1.00117.76 C ANISOU 1514 CD GLN A 219 14718 16573 13451 706 -1143 326 C ATOM 1515 OE1 GLN A 219 34.192 28.197 55.928 1.00110.23 O ANISOU 1515 OE1 GLN A 219 13869 15556 12459 872 -1096 350 O ATOM 1516 NE2 GLN A 219 35.139 29.534 57.429 1.00111.98 N ANISOU 1516 NE2 GLN A 219 13744 16095 12709 647 -1144 311 N ATOM 1517 N HIS A 220 31.205 27.361 55.049 1.00 83.56 N ANISOU 1517 N HIS A 220 11055 11602 9091 798 -1168 385 N ATOM 1518 CA HIS A 220 30.851 25.923 55.068 1.00 81.21 C ANISOU 1518 CA HIS A 220 10970 11162 8723 947 -1234 430 C ATOM 1519 C HIS A 220 31.714 25.079 55.959 1.00 77.13 C ANISOU 1519 C HIS A 220 10397 10750 8158 1130 -1285 454 C ATOM 1520 O HIS A 220 32.017 23.925 55.743 1.00 77.12 O ANISOU 1520 O HIS A 220 10552 10668 8082 1333 -1308 480 O ATOM 1521 CB HIS A 220 30.618 25.348 53.692 1.00 82.79 C ANISOU 1521 CB HIS A 220 11377 11201 8877 1025 -1188 430 C ATOM 1522 CG HIS A 220 29.454 25.972 53.009 1.00 85.42 C ANISOU 1522 CG HIS A 220 11805 11414 9238 839 -1174 429 C ATOM 1523 ND1 HIS A 220 28.401 25.433 52.359 1.00 87.25 N ANISOU 1523 ND1 HIS A 220 12267 11463 9422 788 -1210 455 N ATOM 1524 CD2 HIS A 220 29.265 27.331 52.987 1.00 86.57 C ANISOU 1524 CD2 HIS A 220 11805 11635 9453 680 -1125 403 C ATOM 1525 CE1 HIS A 220 27.610 26.472 51.946 1.00 85.94 C ANISOU 1525 CE1 HIS A 220 12060 11297 9295 622 -1175 449 C ATOM 1526 NE2 HIS A 220 28.153 27.607 52.338 1.00 85.22 N ANISOU 1526 NE2 HIS A 220 11759 11347 9275 572 -1124 415 N ATOM 1527 N CYS A 221 32.083 25.728 57.017 1.00 67.01 N ANISOU 1527 N CYS A 221 8902 9648 6912 1056 -1309 442 N ATOM 1528 CA CYS A 221 32.646 25.048 58.177 1.00 64.64 C ANISOU 1528 CA CYS A 221 8534 9462 6567 1187 -1383 475 C ATOM 1529 C CYS A 221 33.580 23.874 57.905 1.00 60.38 C ANISOU 1529 C CYS A 221 8056 8947 5937 1488 -1376 503 C ATOM 1530 O CYS A 221 33.809 23.472 56.764 1.00 59.93 O ANISOU 1530 O CYS A 221 8119 8810 5844 1619 -1313 491 O ATOM 1531 CB CYS A 221 31.522 24.599 59.117 1.00 64.27 C ANISOU 1531 CB CYS A 221 8626 9290 6504 1099 -1496 526 C ATOM 1532 SG CYS A 221 31.431 25.524 60.667 1.00 67.56 S ANISOU 1532 SG CYS A 221 8813 9905 6952 945 -1554 507 S ATOM 1533 N ASN A1002 34.107 23.340 59.001 1.00 45.79 N ANISOU 1533 N ASN A1002 6020 5143 6235 -1289 -250 165 N ATOM 1534 CA ASN A1002 34.985 22.236 59.008 1.00 42.34 C ANISOU 1534 CA ASN A1002 5653 4666 5766 -1288 -52 -47 C ATOM 1535 C ASN A1002 34.972 21.892 60.433 1.00 39.53 C ANISOU 1535 C ASN A1002 5236 4176 5607 -1048 -26 -94 C ATOM 1536 O ASN A1002 34.211 22.408 61.162 1.00 39.40 O ANISOU 1536 O ASN A1002 5146 4131 5694 -943 -144 11 O ATOM 1537 CB ASN A1002 36.412 22.472 58.499 1.00 41.64 C ANISOU 1537 CB ASN A1002 5596 4588 5635 -1331 76 -136 C ATOM 1538 CG ASN A1002 37.044 23.771 58.970 1.00 54.35 C ANISOU 1538 CG ASN A1002 7131 6160 7360 -1206 9 -30 C ATOM 1539 OD1 ASN A1002 37.700 23.809 59.970 1.00 43.76 O ANISOU 1539 OD1 ASN A1002 5737 4718 6174 -1016 66 -83 O ATOM 1540 ND2 ASN A1002 36.904 24.803 58.198 1.00 48.98 N ANISOU 1540 ND2 ASN A1002 6449 5566 6595 -1335 -107 120 N ATOM 1541 N ILE A1003 35.819 20.987 60.817 1.00 30.16 N ANISOU 1541 N ILE A1003 4073 2910 4477 -973 135 -253 N ATOM 1542 CA ILE A1003 35.869 20.397 62.148 1.00 25.78 C ANISOU 1542 CA ILE A1003 3468 2237 4089 -776 170 -299 C ATOM 1543 C ILE A1003 36.513 21.387 63.122 1.00 27.93 C ANISOU 1543 C ILE A1003 3648 2461 4503 -606 129 -235 C ATOM 1544 O ILE A1003 36.071 21.459 64.271 1.00 28.45 O ANISOU 1544 O ILE A1003 3651 2477 4682 -475 72 -196 O ATOM 1545 CB ILE A1003 36.482 18.971 62.172 1.00 27.50 C ANISOU 1545 CB ILE A1003 3734 2373 4341 -767 350 -469 C ATOM 1546 CG1 ILE A1003 36.299 18.285 63.523 1.00 25.37 C ANISOU 1546 CG1 ILE A1003 3414 1994 4231 -595 350 -475 C ATOM 1547 CG2 ILE A1003 37.930 18.955 61.695 1.00 28.77 C ANISOU 1547 CG2 ILE A1003 3901 2513 4518 -776 500 -571 C ATOM 1548 CD1 ILE A1003 36.471 16.871 63.478 1.00 29.89 C ANISOU 1548 CD1 ILE A1003 4035 2477 4844 -608 487 -602 C ATOM 1549 N PHE A1004 37.547 22.142 62.692 1.00 22.19 N ANISOU 1549 N PHE A1004 2914 1757 3761 -624 163 -231 N ATOM 1550 CA PHE A1004 38.199 23.119 63.578 1.00 19.84 C ANISOU 1550 CA PHE A1004 2533 1421 3583 -487 131 -177 C ATOM 1551 C PHE A1004 37.221 24.217 63.928 1.00 22.79 C ANISOU 1551 C PHE A1004 2856 1803 4001 -461 -23 -41 C ATOM 1552 O PHE A1004 37.143 24.621 65.084 1.00 20.83 O ANISOU 1552 O PHE A1004 2536 1502 3878 -333 -54 -22 O ATOM 1553 CB PHE A1004 39.464 23.701 62.933 1.00 21.27 C ANISOU 1553 CB PHE A1004 2722 1634 3724 -536 200 -200 C ATOM 1554 CG PHE A1004 40.030 24.927 63.611 1.00 20.77 C ANISOU 1554 CG PHE A1004 2587 1552 3752 -444 149 -128 C ATOM 1555 CD1 PHE A1004 40.813 24.811 64.755 1.00 22.32 C ANISOU 1555 CD1 PHE A1004 2715 1695 4070 -303 200 -168 C ATOM 1556 CD2 PHE A1004 39.809 26.193 63.089 1.00 22.00 C ANISOU 1556 CD2 PHE A1004 2740 1744 3873 -514 49 -14 C ATOM 1557 CE1 PHE A1004 41.350 25.942 65.367 1.00 22.07 C ANISOU 1557 CE1 PHE A1004 2624 1658 4105 -246 163 -117 C ATOM 1558 CE2 PHE A1004 40.333 27.323 63.711 1.00 24.04 C ANISOU 1558 CE2 PHE A1004 2939 1970 4226 -440 17 37 C ATOM 1559 CZ PHE A1004 41.099 27.191 64.846 1.00 20.89 C ANISOU 1559 CZ PHE A1004 2482 1529 3928 -312 80 -26 C ATOM 1560 N GLU A1005 36.455 24.669 62.926 1.00 20.06 N ANISOU 1560 N GLU A1005 2538 1524 3559 -596 -116 54 N ATOM 1561 CA GLU A1005 35.450 25.693 63.093 1.00 19.76 C ANISOU 1561 CA GLU A1005 2434 1480 3593 -579 -265 200 C ATOM 1562 C GLU A1005 34.333 25.208 63.977 1.00 21.92 C ANISOU 1562 C GLU A1005 2662 1718 3949 -496 -306 195 C ATOM 1563 O GLU A1005 33.923 25.955 64.850 1.00 21.99 O ANISOU 1563 O GLU A1005 2584 1670 4100 -390 -358 241 O ATOM 1564 CB GLU A1005 34.964 26.188 61.742 1.00 22.98 C ANISOU 1564 CB GLU A1005 2873 1978 3879 -760 -365 330 C ATOM 1565 CG GLU A1005 36.051 26.893 60.931 1.00 36.97 C ANISOU 1565 CG GLU A1005 4681 3792 5574 -854 -338 355 C ATOM 1566 CD GLU A1005 36.705 28.113 61.565 1.00 62.69 C ANISOU 1566 CD GLU A1005 7872 6969 8977 -737 -355 403 C ATOM 1567 OE1 GLU A1005 35.990 28.933 62.189 1.00 62.75 O ANISOU 1567 OE1 GLU A1005 7796 6903 9142 -644 -450 501 O ATOM 1568 OE2 GLU A1005 37.942 28.255 61.421 1.00 54.58 O ANISOU 1568 OE2 GLU A1005 6874 5952 7912 -748 -262 334 O ATOM 1569 N MET A1006 33.932 23.921 63.838 1.00 17.80 N ANISOU 1569 N MET A1006 2198 1222 3344 -545 -259 118 N ATOM 1570 CA MET A1006 32.911 23.203 64.633 1.00 16.01 C ANISOU 1570 CA MET A1006 1944 974 3167 -490 -281 95 C ATOM 1571 C MET A1006 33.310 23.177 66.135 1.00 16.66 C ANISOU 1571 C MET A1006 1966 977 3387 -325 -233 34 C ATOM 1572 O MET A1006 32.558 23.668 66.977 1.00 17.84 O ANISOU 1572 O MET A1006 2036 1105 3638 -255 -292 70 O ATOM 1573 CB MET A1006 32.747 21.768 64.079 1.00 18.49 C ANISOU 1573 CB MET A1006 2354 1318 3354 -594 -208 1 C ATOM 1574 CG MET A1006 31.539 21.027 64.594 1.00 22.19 C ANISOU 1574 CG MET A1006 2810 1788 3834 -590 -249 -2 C ATOM 1575 SD MET A1006 31.786 19.222 64.715 1.00 26.91 S ANISOU 1575 SD MET A1006 3504 2338 4384 -617 -108 -158 S ATOM 1576 CE MET A1006 30.166 18.659 64.510 1.00 24.25 C ANISOU 1576 CE MET A1006 3178 2067 3968 -725 -195 -119 C ATOM 1577 N LEU A1007 34.505 22.647 66.464 1.00 10.38 N ANISOU 1577 N LEU A1007 1072 423 2449 -168 -120 -40 N ATOM 1578 CA LEU A1007 34.985 22.604 67.850 1.00 8.58 C ANISOU 1578 CA LEU A1007 658 388 2214 -37 -86 -59 C ATOM 1579 C LEU A1007 35.387 23.970 68.423 1.00 11.32 C ANISOU 1579 C LEU A1007 1093 387 2821 -65 -120 -44 C ATOM 1580 O LEU A1007 35.476 24.116 69.640 1.00 10.67 O ANISOU 1580 O LEU A1007 903 382 2768 -10 -113 -60 O ATOM 1581 CB LEU A1007 36.054 21.544 68.062 1.00 7.92 C ANISOU 1581 CB LEU A1007 537 388 2082 -18 25 -107 C ATOM 1582 CG LEU A1007 35.471 20.161 68.179 1.00 10.30 C ANISOU 1582 CG LEU A1007 1012 401 2500 -73 53 -168 C ATOM 1583 CD1 LEU A1007 36.043 19.257 67.150 1.00 11.76 C ANISOU 1583 CD1 LEU A1007 1342 426 2700 -151 160 -252 C ATOM 1584 CD2 LEU A1007 35.678 19.606 69.525 1.00 8.98 C ANISOU 1584 CD2 LEU A1007 691 392 2329 -16 60 -147 C ATOM 1585 N ARG A1008 35.574 24.979 67.552 1.00 9.44 N ANISOU 1585 N ARG A1008 753 387 2447 -52 -156 13 N ATOM 1586 CA ARG A1008 35.831 26.342 67.986 1.00 8.79 C ANISOU 1586 CA ARG A1008 549 382 2408 -19 -186 42 C ATOM 1587 C ARG A1008 34.496 26.843 68.542 1.00 10.65 C ANISOU 1587 C ARG A1008 813 384 2850 -35 -259 79 C ATOM 1588 O ARG A1008 34.480 27.332 69.670 1.00 10.02 O ANISOU 1588 O ARG A1008 610 381 2816 -3 -237 40 O ATOM 1589 CB ARG A1008 36.335 27.217 66.829 1.00 8.35 C ANISOU 1589 CB ARG A1008 507 388 2279 -28 -215 95 C ATOM 1590 CG ARG A1008 37.094 28.448 67.268 1.00 12.06 C ANISOU 1590 CG ARG A1008 1130 398 3056 -102 -201 127 C ATOM 1591 CD ARG A1008 37.208 29.417 66.118 1.00 30.92 C ANISOU 1591 CD ARG A1008 3606 2652 5492 -214 -260 242 C ATOM 1592 NE ARG A1008 37.660 30.731 66.576 1.00 57.38 N ANISOU 1592 NE ARG A1008 6905 5938 8959 -176 -263 268 N ATOM 1593 CZ ARG A1008 38.142 31.687 65.783 1.00 84.24 C ANISOU 1593 CZ ARG A1008 10321 9331 12354 -242 -296 353 C ATOM 1594 NH1 ARG A1008 38.244 31.487 64.472 1.00 76.91 N ANISOU 1594 NH1 ARG A1008 9458 8475 11290 -364 -333 424 N ATOM 1595 NH2 ARG A1008 38.527 32.850 66.295 1.00 72.76 N ANISOU 1595 NH2 ARG A1008 8822 7803 11022 -208 -288 364 N ATOM 1596 N ILE A1009 33.365 26.616 67.807 1.00 8.51 N ANISOU 1596 N ILE A1009 436 387 2409 -20 -336 124 N ATOM 1597 CA ILE A1009 32.005 26.983 68.239 1.00 8.88 C ANISOU 1597 CA ILE A1009 449 391 2535 -27 -386 153 C ATOM 1598 C ILE A1009 31.708 26.298 69.611 1.00 14.47 C ANISOU 1598 C ILE A1009 1339 556 3602 -35 -347 95 C ATOM 1599 O ILE A1009 31.242 26.961 70.549 1.00 15.49 O ANISOU 1599 O ILE A1009 1379 646 3860 18 -338 67 O ATOM 1600 CB ILE A1009 30.920 26.572 67.188 1.00 10.12 C ANISOU 1600 CB ILE A1009 666 415 2763 -89 -504 260 C ATOM 1601 CG1 ILE A1009 31.111 27.087 65.733 1.00 10.77 C ANISOU 1601 CG1 ILE A1009 830 466 2797 -180 -581 385 C ATOM 1602 CG2 ILE A1009 29.502 26.751 67.688 1.00 10.06 C ANISOU 1602 CG2 ILE A1009 539 414 2868 -70 -566 289 C ATOM 1603 CD1 ILE A1009 31.758 28.444 65.506 1.00 24.30 C ANISOU 1603 CD1 ILE A1009 2631 1846 4756 -283 -594 502 C ATOM 1604 N ASP A1010 32.007 24.985 69.722 1.00 10.95 N ANISOU 1604 N ASP A1010 848 382 2929 -31 -301 33 N ATOM 1605 CA ASP A1010 31.687 24.199 70.897 1.00 10.77 C ANISOU 1605 CA ASP A1010 801 381 2911 -10 -267 -30 C ATOM 1606 C ASP A1010 32.586 24.317 72.124 1.00 16.80 C ANISOU 1606 C ASP A1010 1658 892 3834 27 -204 -98 C ATOM 1607 O ASP A1010 32.079 24.301 73.247 1.00 17.71 O ANISOU 1607 O ASP A1010 1717 1022 3990 35 -194 -141 O ATOM 1608 CB ASP A1010 31.508 22.741 70.497 1.00 12.30 C ANISOU 1608 CB ASP A1010 1182 387 3103 -66 -253 -54 C ATOM 1609 CG ASP A1010 30.281 22.462 69.649 1.00 25.58 C ANISOU 1609 CG ASP A1010 2895 2069 4753 -145 -321 -7 C ATOM 1610 OD1 ASP A1010 29.224 23.103 69.894 1.00 26.36 O ANISOU 1610 OD1 ASP A1010 2909 2177 4931 -136 -384 35 O ATOM 1611 OD2 ASP A1010 30.340 21.529 68.821 1.00 29.52 O ANISOU 1611 OD2 ASP A1010 3484 2589 5144 -220 -304 -19 O ATOM 1612 N GLU A1011 33.908 24.372 71.935 1.00 14.62 N ANISOU 1612 N GLU A1011 1414 610 3531 40 -160 -103 N ATOM 1613 CA GLU A1011 34.866 24.439 73.043 1.00 13.58 C ANISOU 1613 CA GLU A1011 1248 493 3420 68 -112 -139 C ATOM 1614 C GLU A1011 35.494 25.816 73.246 1.00 17.70 C ANISOU 1614 C GLU A1011 1725 1003 3999 78 -96 -145 C ATOM 1615 O GLU A1011 35.939 26.124 74.341 1.00 18.82 O ANISOU 1615 O GLU A1011 1819 1172 4160 74 -65 -183 O ATOM 1616 CB GLU A1011 35.949 23.336 72.909 1.00 14.52 C ANISOU 1616 CB GLU A1011 1412 615 3492 80 -68 -137 C ATOM 1617 CG GLU A1011 35.417 21.933 73.183 1.00 27.50 C ANISOU 1617 CG GLU A1011 3085 2254 5110 71 -70 -141 C ATOM 1618 CD GLU A1011 36.394 20.774 73.324 1.00 53.29 C ANISOU 1618 CD GLU A1011 6368 5493 8387 96 -22 -131 C ATOM 1619 OE1 GLU A1011 35.996 19.636 72.984 1.00 37.80 O ANISOU 1619 OE1 GLU A1011 4457 3491 6413 84 -8 -139 O ATOM 1620 OE2 GLU A1011 37.527 20.982 73.817 1.00 51.24 O ANISOU 1620 OE2 GLU A1011 6061 5245 8162 126 0 -110 O ATOM 1621 N GLY A1012 35.567 26.617 72.198 1.00 14.37 N ANISOU 1621 N GLY A1012 1319 546 3594 71 -117 -103 N ATOM 1622 CA GLY A1012 36.190 27.933 72.285 1.00 15.11 C ANISOU 1622 CA GLY A1012 1379 612 3751 74 -101 -102 C ATOM 1623 C GLY A1012 37.695 27.899 72.081 1.00 20.18 C ANISOU 1623 C GLY A1012 2049 1281 4336 69 -56 -103 C ATOM 1624 O GLY A1012 38.354 26.935 72.477 1.00 20.83 O ANISOU 1624 O GLY A1012 2140 1405 4370 81 -24 -122 O ATOM 1625 N LEU A1013 38.252 28.978 71.505 1.00 16.05 N ANISOU 1625 N LEU A1013 1529 732 3838 52 -56 -74 N ATOM 1626 CA LEU A1013 39.678 29.106 71.232 1.00 16.04 C ANISOU 1626 CA LEU A1013 1545 762 3788 38 -11 -76 C ATOM 1627 C LEU A1013 40.372 30.068 72.188 1.00 20.93 C ANISOU 1627 C LEU A1013 2111 1386 4454 30 24 -112 C ATOM 1628 O LEU A1013 40.219 31.277 72.049 1.00 22.66 O ANISOU 1628 O LEU A1013 2317 1549 4744 11 17 -103 O ATOM 1629 CB LEU A1013 39.836 29.562 69.784 1.00 16.83 C ANISOU 1629 CB LEU A1013 1697 846 3850 -7 -36 -14 C ATOM 1630 CG LEU A1013 41.223 29.793 69.227 1.00 22.17 C ANISOU 1630 CG LEU A1013 2396 1558 4469 -40 12 -14 C ATOM 1631 CD1 LEU A1013 41.454 28.910 68.031 1.00 22.96 C ANISOU 1631 CD1 LEU A1013 2560 1695 4467 -86 35 -11 C ATOM 1632 CD2 LEU A1013 41.341 31.211 68.714 1.00 25.65 C ANISOU 1632 CD2 LEU A1013 2838 1960 4947 -87 -20 44 C ATOM 1633 N ARG A1014 41.141 29.530 73.146 1.00 15.85 N ANISOU 1633 N ARG A1014 1433 809 3778 32 61 -146 N ATOM 1634 CA ARG A1014 41.949 30.306 74.101 1.00 15.10 C ANISOU 1634 CA ARG A1014 1288 755 3693 -8 96 -182 C ATOM 1635 C ARG A1014 43.374 30.586 73.531 1.00 20.25 C ANISOU 1635 C ARG A1014 1945 1442 4307 -25 125 -154 C ATOM 1636 O ARG A1014 44.083 29.650 73.150 1.00 20.72 O ANISOU 1636 O ARG A1014 2007 1541 4326 2 138 -127 O ATOM 1637 CB ARG A1014 42.062 29.554 75.436 1.00 12.34 C ANISOU 1637 CB ARG A1014 888 489 3310 -27 102 -203 C ATOM 1638 CG ARG A1014 40.773 29.505 76.225 1.00 14.44 C ANISOU 1638 CG ARG A1014 1138 743 3606 -43 92 -253 C ATOM 1639 CD ARG A1014 40.997 28.988 77.615 1.00 16.06 C ANISOU 1639 CD ARG A1014 1291 1055 3756 -106 97 -270 C ATOM 1640 NE ARG A1014 39.727 28.767 78.299 1.00 32.17 N ANISOU 1640 NE ARG A1014 3319 3095 5808 -132 94 -323 N ATOM 1641 CZ ARG A1014 39.166 29.626 79.145 1.00 57.48 C ANISOU 1641 CZ ARG A1014 6489 6309 9043 -206 142 -424 C ATOM 1642 NH1 ARG A1014 39.761 30.778 79.422 1.00 47.14 N ANISOU 1642 NH1 ARG A1014 5159 4998 7755 -266 197 -483 N ATOM 1643 NH2 ARG A1014 38.006 29.340 79.718 1.00 53.72 N ANISOU 1643 NH2 ARG A1014 5994 5838 8580 -231 149 -479 N ATOM 1644 N LEU A1015 43.793 31.858 73.454 1.00 16.73 N ANISOU 1644 N LEU A1015 1497 974 3888 -70 143 -167 N ATOM 1645 CA LEU A1015 45.143 32.171 72.929 1.00 15.88 C ANISOU 1645 CA LEU A1015 1389 909 3735 -99 172 -144 C ATOM 1646 C LEU A1015 46.221 32.403 74.007 1.00 21.14 C ANISOU 1646 C LEU A1015 1989 1670 4373 -150 205 -167 C ATOM 1647 O LEU A1015 47.396 32.547 73.670 1.00 21.50 O ANISOU 1647 O LEU A1015 2016 1769 4384 -173 230 -146 O ATOM 1648 CB LEU A1015 45.133 33.244 71.821 1.00 15.41 C ANISOU 1648 CB LEU A1015 1380 779 3697 -132 162 -112 C ATOM 1649 CG LEU A1015 44.291 32.853 70.601 1.00 19.31 C ANISOU 1649 CG LEU A1015 1933 1222 4180 -112 116 -58 C ATOM 1650 CD1 LEU A1015 44.074 34.012 69.663 1.00 19.03 C ANISOU 1650 CD1 LEU A1015 1935 1116 4180 -162 79 6 C ATOM 1651 CD2 LEU A1015 44.870 31.646 69.874 1.00 23.46 C ANISOU 1651 CD2 LEU A1015 2483 1811 4618 -101 143 -55 C ATOM 1652 N LYS A1016 45.813 32.363 75.297 1.00 18.03 N ANISOU 1652 N LYS A1016 1552 1315 3983 -183 204 -209 N ATOM 1653 CA LYS A1016 46.652 32.507 76.489 1.00 17.89 C ANISOU 1653 CA LYS A1016 1467 1416 3916 -267 221 -224 C ATOM 1654 C LYS A1016 46.299 31.369 77.486 1.00 22.10 C ANISOU 1654 C LYS A1016 1954 2027 4416 -267 187 -200 C ATOM 1655 O LYS A1016 45.104 31.092 77.657 1.00 23.07 O ANISOU 1655 O LYS A1016 2103 2097 4566 -243 175 -233 O ATOM 1656 CB LYS A1016 46.449 33.898 77.138 1.00 19.74 C ANISOU 1656 CB LYS A1016 1702 1626 4173 -369 268 -316 C ATOM 1657 CG LYS A1016 47.295 34.107 78.393 1.00 27.66 C ANISOU 1657 CG LYS A1016 2640 2777 5094 -499 289 -342 C ATOM 1658 CD LYS A1016 47.122 35.459 79.016 1.00 41.19 C ANISOU 1658 CD LYS A1016 4361 4460 6829 -620 361 -462 C ATOM 1659 CE LYS A1016 48.306 35.780 79.899 1.00 60.28 C ANISOU 1659 CE LYS A1016 6724 7040 9138 -771 380 -470 C ATOM 1660 NZ LYS A1016 48.218 37.148 80.481 1.00 70.15 N ANISOU 1660 NZ LYS A1016 7990 8254 10408 -912 473 -611 N ATOM 1661 N ILE A1017 47.321 30.708 78.127 1.00 17.18 N ANISOU 1661 N ILE A1017 1254 1530 3745 -299 164 -128 N ATOM 1662 CA ILE A1017 47.116 29.600 79.088 1.00 16.38 C ANISOU 1662 CA ILE A1017 1099 1509 3616 -314 114 -67 C ATOM 1663 C ILE A1017 46.146 30.043 80.173 1.00 21.50 C ANISOU 1663 C ILE A1017 1756 2194 4220 -422 122 -152 C ATOM 1664 O ILE A1017 46.348 31.091 80.801 1.00 21.85 O ANISOU 1664 O ILE A1017 1788 2292 4221 -545 164 -230 O ATOM 1665 CB ILE A1017 48.422 28.975 79.711 1.00 19.13 C ANISOU 1665 CB ILE A1017 1336 1994 3937 -352 73 55 C ATOM 1666 CG1 ILE A1017 49.274 28.262 78.694 1.00 19.75 C ANISOU 1666 CG1 ILE A1017 1387 2023 4096 -230 81 131 C ATOM 1667 CG2 ILE A1017 48.118 27.994 80.826 1.00 18.34 C ANISOU 1667 CG2 ILE A1017 1180 1983 3806 -402 5 138 C ATOM 1668 CD1 ILE A1017 50.651 27.907 79.257 1.00 33.49 C ANISOU 1668 CD1 ILE A1017 2992 3889 5843 -265 46 255 C ATOM 1669 N TYR A1018 45.083 29.244 80.361 1.00 17.35 N ANISOU 1669 N TYR A1018 1250 1635 3706 -385 96 -152 N ATOM 1670 CA TYR A1018 44.092 29.470 81.390 1.00 17.51 C ANISOU 1670 CA TYR A1018 1270 1698 3686 -489 112 -237 C ATOM 1671 C TYR A1018 44.268 28.391 82.458 1.00 20.00 C ANISOU 1671 C TYR A1018 1525 2153 3920 -567 45 -139 C ATOM 1672 O TYR A1018 44.387 27.225 82.105 1.00 18.88 O ANISOU 1672 O TYR A1018 1375 1984 3814 -472 -12 -25 O ATOM 1673 CB TYR A1018 42.670 29.437 80.777 1.00 19.15 C ANISOU 1673 CB TYR A1018 1538 1767 3970 -400 129 -305 C ATOM 1674 CG TYR A1018 41.579 29.467 81.822 1.00 22.61 C ANISOU 1674 CG TYR A1018 1961 2249 4379 -498 152 -396 C ATOM 1675 CD1 TYR A1018 41.390 30.589 82.627 1.00 25.76 C ANISOU 1675 CD1 TYR A1018 2339 2682 4767 -630 233 -533 C ATOM 1676 CD2 TYR A1018 40.798 28.343 82.075 1.00 24.02 C ANISOU 1676 CD2 TYR A1018 2145 2445 4537 -478 105 -354 C ATOM 1677 CE1 TYR A1018 40.448 30.597 83.657 1.00 27.92 C ANISOU 1677 CE1 TYR A1018 2590 3013 5005 -745 277 -639 C ATOM 1678 CE2 TYR A1018 39.850 28.336 83.102 1.00 26.21 C ANISOU 1678 CE2 TYR A1018 2402 2787 4770 -590 132 -440 C ATOM 1679 CZ TYR A1018 39.675 29.470 83.889 1.00 38.87 C ANISOU 1679 CZ TYR A1018 3978 4431 6359 -726 223 -589 C ATOM 1680 OH TYR A1018 38.724 29.501 84.884 1.00 46.48 O ANISOU 1680 OH TYR A1018 4917 5461 7281 -853 274 -703 O ATOM 1681 N LYS A1019 44.308 28.772 83.747 1.00 17.50 N ANISOU 1681 N LYS A1019 1167 1985 3498 -755 54 -180 N ATOM 1682 CA LYS A1019 44.383 27.830 84.880 1.00 18.00 C ANISOU 1682 CA LYS A1019 1171 2208 3462 -875 -23 -73 C ATOM 1683 C LYS A1019 42.990 27.767 85.504 1.00 23.73 C ANISOU 1683 C LYS A1019 1928 2939 4149 -951 10 -185 C ATOM 1684 O LYS A1019 42.502 28.787 86.017 1.00 24.77 O ANISOU 1684 O LYS A1019 2072 3095 4246 -1073 102 -356 O ATOM 1685 CB LYS A1019 45.402 28.271 85.935 1.00 20.74 C ANISOU 1685 CB LYS A1019 1441 2757 3680 -1080 -43 -32 C ATOM 1686 CG LYS A1019 45.397 27.443 87.219 1.00 31.86 C ANISOU 1686 CG LYS A1019 2785 4359 4960 -1256 -132 87 C ATOM 1687 CD LYS A1019 45.867 28.276 88.409 1.00 49.08 C ANISOU 1687 CD LYS A1019 4922 6758 6968 -1538 -107 30 C ATOM 1688 CE LYS A1019 46.193 27.465 89.640 1.00 63.38 C ANISOU 1688 CE LYS A1019 6649 8803 8630 -1745 -226 206 C ATOM 1689 NZ LYS A1019 46.134 28.306 90.866 1.00 73.91 N ANISOU 1689 NZ LYS A1019 7972 10351 9758 -2068 -168 77 N ATOM 1690 N ASP A1020 42.343 26.588 85.457 1.00 19.74 N ANISOU 1690 N ASP A1020 1434 2403 3663 -885 -52 -102 N ATOM 1691 CA ASP A1020 41.003 26.467 86.009 1.00 19.91 C ANISOU 1691 CA ASP A1020 1481 2436 3649 -957 -21 -206 C ATOM 1692 C ASP A1020 40.930 26.386 87.556 1.00 28.07 C ANISOU 1692 C ASP A1020 2465 3687 4512 -1218 -34 -212 C ATOM 1693 O ASP A1020 41.948 26.603 88.224 1.00 29.20 O ANISOU 1693 O ASP A1020 2555 3984 4557 -1360 -67 -143 O ATOM 1694 CB ASP A1020 40.166 25.419 85.262 1.00 20.30 C ANISOU 1694 CB ASP A1020 1576 2357 3781 -799 -62 -152 C ATOM 1695 CG ASP A1020 40.368 23.971 85.649 1.00 32.00 C ANISOU 1695 CG ASP A1020 3033 3893 5234 -807 -169 32 C ATOM 1696 OD1 ASP A1020 40.942 23.714 86.735 1.00 34.23 O ANISOU 1696 OD1 ASP A1020 3253 4344 5410 -969 -228 131 O ATOM 1697 OD2 ASP A1020 39.889 23.090 84.900 1.00 37.63 O ANISOU 1697 OD2 ASP A1020 3787 4481 6028 -669 -194 80 O ATOM 1698 N THR A1021 39.726 26.107 88.120 1.00 25.14 N ANISOU 1698 N THR A1021 2109 3348 4096 -1300 -8 -298 N ATOM 1699 CA THR A1021 39.532 26.027 89.570 1.00 25.74 C ANISOU 1699 CA THR A1021 2146 3644 3990 -1577 -8 -323 C ATOM 1700 C THR A1021 40.208 24.860 90.243 1.00 29.56 C ANISOU 1700 C THR A1021 2581 4281 4368 -1676 -161 -73 C ATOM 1701 O THR A1021 40.580 25.000 91.394 1.00 30.51 O ANISOU 1701 O THR A1021 2654 4623 4316 -1935 -183 -48 O ATOM 1702 CB THR A1021 38.094 26.265 89.993 1.00 31.82 C ANISOU 1702 CB THR A1021 2935 4409 4744 -1659 93 -520 C ATOM 1703 OG1 THR A1021 37.220 25.463 89.194 1.00 34.53 O ANISOU 1703 OG1 THR A1021 3317 4602 5201 -1466 55 -477 O ATOM 1704 CG2 THR A1021 37.715 27.717 89.899 1.00 26.88 C ANISOU 1704 CG2 THR A1021 2314 3708 4193 -1680 261 -775 C ATOM 1705 N GLU A1022 40.415 23.740 89.541 1.00 25.54 N ANISOU 1705 N GLU A1022 2077 3659 3969 -1486 -264 116 N ATOM 1706 CA GLU A1022 41.113 22.588 90.121 1.00 26.90 C ANISOU 1706 CA GLU A1022 2184 3939 4096 -1553 -416 385 C ATOM 1707 C GLU A1022 42.609 22.536 89.718 1.00 34.25 C ANISOU 1707 C GLU A1022 3048 4859 5107 -1462 -483 557 C ATOM 1708 O GLU A1022 43.282 21.497 89.883 1.00 35.16 O ANISOU 1708 O GLU A1022 3093 4995 5272 -1438 -611 807 O ATOM 1709 CB GLU A1022 40.392 21.270 89.815 1.00 27.67 C ANISOU 1709 CB GLU A1022 2314 3926 4273 -1440 -483 493 C ATOM 1710 CG GLU A1022 38.943 21.217 90.252 1.00 39.54 C ANISOU 1710 CG GLU A1022 3870 5458 5695 -1540 -428 345 C ATOM 1711 CD GLU A1022 38.622 21.678 91.655 1.00 57.64 C ANISOU 1711 CD GLU A1022 6131 7998 7770 -1859 -405 265 C ATOM 1712 OE1 GLU A1022 39.342 21.268 92.595 1.00 50.72 O ANISOU 1712 OE1 GLU A1022 5190 7312 6767 -2052 -515 451 O ATOM 1713 OE2 GLU A1022 37.626 22.422 91.815 1.00 47.51 O ANISOU 1713 OE2 GLU A1022 4882 6721 6450 -1925 -275 21 O ATOM 1714 N GLY A1023 43.101 23.680 89.222 1.00 31.10 N ANISOU 1714 N GLY A1023 2660 4425 4731 -1419 -393 423 N ATOM 1715 CA GLY A1023 44.486 23.890 88.819 1.00 31.37 C ANISOU 1715 CA GLY A1023 2630 4461 4827 -1350 -427 536 C ATOM 1716 C GLY A1023 44.875 23.208 87.528 1.00 34.30 C ANISOU 1716 C GLY A1023 3007 4619 5404 -1069 -440 624 C ATOM 1717 O GLY A1023 45.941 22.602 87.455 1.00 36.79 O ANISOU 1717 O GLY A1023 3233 4948 5799 -1016 -521 821 O ATOM 1718 N TYR A1024 44.053 23.340 86.496 1.00 27.22 N ANISOU 1718 N TYR A1024 2208 3534 4600 -902 -356 477 N ATOM 1719 CA TYR A1024 44.322 22.726 85.205 1.00 25.98 C ANISOU 1719 CA TYR A1024 2073 3182 4614 -666 -346 522 C ATOM 1720 C TYR A1024 44.583 23.802 84.140 1.00 28.35 C ANISOU 1720 C TYR A1024 2424 3386 4963 -566 -248 379 C ATOM 1721 O TYR A1024 43.804 24.751 84.013 1.00 28.72 O ANISOU 1721 O TYR A1024 2536 3407 4969 -597 -175 207 O ATOM 1722 CB TYR A1024 43.154 21.795 84.813 1.00 27.03 C ANISOU 1722 CB TYR A1024 2279 3189 4803 -576 -347 504 C ATOM 1723 CG TYR A1024 43.102 20.514 85.623 1.00 31.38 C ANISOU 1723 CG TYR A1024 2778 3792 5353 -636 -453 690 C ATOM 1724 CD1 TYR A1024 43.659 19.334 85.138 1.00 34.10 C ANISOU 1724 CD1 TYR A1024 3083 4016 5858 -499 -498 852 C ATOM 1725 CD2 TYR A1024 42.510 20.483 86.882 1.00 33.46 C ANISOU 1725 CD2 TYR A1024 3027 4220 5464 -843 -502 706 C ATOM 1726 CE1 TYR A1024 43.609 18.151 85.874 1.00 34.14 C ANISOU 1726 CE1 TYR A1024 3034 4044 5892 -551 -602 1044 C ATOM 1727 CE2 TYR A1024 42.485 19.310 87.640 1.00 35.74 C ANISOU 1727 CE2 TYR A1024 3266 4565 5748 -917 -615 905 C ATOM 1728 CZ TYR A1024 43.037 18.149 87.131 1.00 43.06 C ANISOU 1728 CZ TYR A1024 4153 5352 6855 -764 -672 1085 C ATOM 1729 OH TYR A1024 43.023 16.996 87.871 1.00 50.42 O ANISOU 1729 OH TYR A1024 5030 6316 7811 -834 -789 1302 O ATOM 1730 N TYR A1025 45.667 23.624 83.363 1.00 21.77 N ANISOU 1730 N TYR A1025 1549 2491 4231 -448 -246 456 N ATOM 1731 CA TYR A1025 46.137 24.534 82.320 1.00 19.10 C ANISOU 1731 CA TYR A1025 1247 2076 3934 -366 -167 357 C ATOM 1732 C TYR A1025 45.639 24.174 80.892 1.00 20.43 C ANISOU 1732 C TYR A1025 1502 2056 4205 -195 -112 293 C ATOM 1733 O TYR A1025 46.019 23.167 80.304 1.00 19.53 O ANISOU 1733 O TYR A1025 1369 1858 4194 -85 -115 370 O ATOM 1734 CB TYR A1025 47.669 24.721 82.423 1.00 21.34 C ANISOU 1734 CB TYR A1025 1425 2447 4237 -384 -188 463 C ATOM 1735 CG TYR A1025 48.127 25.215 83.787 1.00 24.77 C ANISOU 1735 CG TYR A1025 1781 3092 4539 -591 -242 517 C ATOM 1736 CD1 TYR A1025 48.164 26.573 84.085 1.00 27.67 C ANISOU 1736 CD1 TYR A1025 2178 3535 4799 -720 -184 381 C ATOM 1737 CD2 TYR A1025 48.484 24.318 84.794 1.00 26.43 C ANISOU 1737 CD2 TYR A1025 1888 3425 4728 -678 -351 706 C ATOM 1738 CE1 TYR A1025 48.563 27.029 85.342 1.00 30.73 C ANISOU 1738 CE1 TYR A1025 2502 4131 5044 -945 -220 409 C ATOM 1739 CE2 TYR A1025 48.857 24.762 86.063 1.00 28.31 C ANISOU 1739 CE2 TYR A1025 2058 3887 4812 -908 -408 761 C ATOM 1740 CZ TYR A1025 48.907 26.118 86.328 1.00 38.43 C ANISOU 1740 CZ TYR A1025 3378 5255 5970 -1048 -336 600 C ATOM 1741 OH TYR A1025 49.292 26.563 87.570 1.00 45.73 O ANISOU 1741 OH TYR A1025 4240 6414 6724 -1307 -378 635 O ATOM 1742 N THR A1026 44.750 25.007 80.362 1.00 16.96 N ANISOU 1742 N THR A1026 1151 1551 3740 -188 -60 151 N ATOM 1743 CA THR A1026 44.112 24.841 79.059 1.00 15.31 C ANISOU 1743 CA THR A1026 1029 1197 3589 -73 -20 90 C ATOM 1744 C THR A1026 44.580 25.965 78.165 1.00 17.30 C ANISOU 1744 C THR A1026 1311 1412 3848 -54 33 25 C ATOM 1745 O THR A1026 44.689 27.117 78.619 1.00 18.50 O ANISOU 1745 O THR A1026 1453 1615 3959 -135 50 -31 O ATOM 1746 CB THR A1026 42.560 24.914 79.255 1.00 23.63 C ANISOU 1746 CB THR A1026 2144 2218 4615 -98 -24 10 C ATOM 1747 OG1 THR A1026 42.114 23.769 79.963 1.00 29.60 O ANISOU 1747 OG1 THR A1026 2882 3003 5361 -117 -73 76 O ATOM 1748 CG2 THR A1026 41.782 24.995 77.964 1.00 20.14 C ANISOU 1748 CG2 THR A1026 1786 1654 4214 -15 3 -49 C ATOM 1749 N ILE A1027 44.800 25.637 76.887 1.00 10.15 N ANISOU 1749 N ILE A1027 450 416 2992 35 66 23 N ATOM 1750 CA ILE A1027 45.148 26.559 75.815 1.00 9.48 C ANISOU 1750 CA ILE A1027 385 380 2837 -1 108 -22 C ATOM 1751 C ILE A1027 44.523 26.003 74.528 1.00 13.58 C ANISOU 1751 C ILE A1027 1008 710 3442 106 131 -50 C ATOM 1752 O ILE A1027 44.342 24.791 74.408 1.00 13.31 O ANISOU 1752 O ILE A1027 979 641 3439 151 134 -28 O ATOM 1753 CB ILE A1027 46.693 26.768 75.718 1.00 11.99 C ANISOU 1753 CB ILE A1027 656 664 3234 42 139 15 C ATOM 1754 CG1 ILE A1027 47.063 27.882 74.753 1.00 11.08 C ANISOU 1754 CG1 ILE A1027 587 525 3099 22 180 -34 C ATOM 1755 CG2 ILE A1027 47.433 25.479 75.349 1.00 14.05 C ANISOU 1755 CG2 ILE A1027 868 900 3571 119 163 75 C ATOM 1756 CD1 ILE A1027 47.538 29.016 75.369 1.00 17.63 C ANISOU 1756 CD1 ILE A1027 1386 1419 3896 -57 180 -49 C ATOM 1757 N GLY A1028 44.199 26.885 73.594 1.00 10.67 N ANISOU 1757 N GLY A1028 657 396 3002 56 141 -82 N ATOM 1758 CA GLY A1028 43.623 26.511 72.311 1.00 11.39 C ANISOU 1758 CA GLY A1028 836 401 3091 82 152 -98 C ATOM 1759 C GLY A1028 42.178 26.076 72.393 1.00 17.17 C ANISOU 1759 C GLY A1028 1642 1023 3858 109 109 -111 C ATOM 1760 O GLY A1028 41.391 26.678 73.123 1.00 16.69 O ANISOU 1760 O GLY A1028 1563 966 3814 93 71 -121 O ATOM 1761 N ILE A1029 41.821 25.048 71.592 1.00 15.70 N ANISOU 1761 N ILE A1029 1509 801 3655 121 127 -119 N ATOM 1762 CA ILE A1029 40.499 24.421 71.534 1.00 15.65 C ANISOU 1762 CA ILE A1029 1544 767 3636 116 89 -125 C ATOM 1763 C ILE A1029 40.558 23.295 72.582 1.00 22.82 C ANISOU 1763 C ILE A1029 2413 1677 4581 152 92 -113 C ATOM 1764 O ILE A1029 40.685 22.106 72.239 1.00 23.82 O ANISOU 1764 O ILE A1029 2563 1762 4726 172 130 -119 O ATOM 1765 CB ILE A1029 40.147 23.885 70.124 1.00 18.77 C ANISOU 1765 CB ILE A1029 2021 1135 3975 77 113 -144 C ATOM 1766 CG1 ILE A1029 40.504 24.875 68.985 1.00 19.33 C ANISOU 1766 CG1 ILE A1029 2126 1224 3995 18 115 -133 C ATOM 1767 CG2 ILE A1029 38.713 23.372 70.049 1.00 19.22 C ANISOU 1767 CG2 ILE A1029 2116 1179 4008 55 63 -142 C ATOM 1768 CD1 ILE A1029 39.442 25.796 68.529 1.00 23.40 C ANISOU 1768 CD1 ILE A1029 2661 1739 4492 -29 32 -82 C ATOM 1769 N GLY A1030 40.550 23.716 73.852 1.00 19.36 N ANISOU 1769 N GLY A1030 1912 1288 4158 145 58 -96 N ATOM 1770 CA GLY A1030 40.576 22.846 75.011 1.00 18.76 C ANISOU 1770 CA GLY A1030 1788 1241 4101 148 36 -58 C ATOM 1771 C GLY A1030 41.701 21.847 75.017 1.00 22.83 C ANISOU 1771 C GLY A1030 2265 1736 4675 192 68 -4 C ATOM 1772 O GLY A1030 41.470 20.665 75.275 1.00 23.69 O ANISOU 1772 O GLY A1030 2373 1804 4823 212 61 31 O ATOM 1773 N HIS A1031 42.917 22.294 74.696 1.00 19.37 N ANISOU 1773 N HIS A1031 1787 1313 4261 209 107 5 N ATOM 1774 CA HIS A1031 44.058 21.389 74.745 1.00 19.61 C ANISOU 1774 CA HIS A1031 1748 1317 4384 261 143 62 C ATOM 1775 C HIS A1031 44.538 21.491 76.146 1.00 22.13 C ANISOU 1775 C HIS A1031 1969 1730 4710 230 77 157 C ATOM 1776 O HIS A1031 44.923 22.578 76.567 1.00 23.22 O ANISOU 1776 O HIS A1031 2075 1955 4791 177 60 151 O ATOM 1777 CB HIS A1031 45.165 21.783 73.746 1.00 20.88 C ANISOU 1777 CB HIS A1031 1898 1465 4570 284 222 26 C ATOM 1778 CG HIS A1031 46.419 20.975 73.895 1.00 25.48 C ANISOU 1778 CG HIS A1031 2376 2023 5283 344 266 88 C ATOM 1779 ND1 HIS A1031 46.657 19.859 73.116 1.00 28.00 N ANISOU 1779 ND1 HIS A1031 2701 2228 5710 402 357 52 N ATOM 1780 CD2 HIS A1031 47.462 21.148 74.744 1.00 27.81 C ANISOU 1780 CD2 HIS A1031 2548 2391 5628 349 233 183 C ATOM 1781 CE1 HIS A1031 47.829 19.392 73.516 1.00 28.52 C ANISOU 1781 CE1 HIS A1031 2636 2284 5916 459 379 132 C ATOM 1782 NE2 HIS A1031 48.347 20.133 74.499 1.00 28.69 N ANISOU 1782 NE2 HIS A1031 2573 2426 5901 427 295 225 N ATOM 1783 N LEU A1032 44.445 20.397 76.895 1.00 17.56 N ANISOU 1783 N LEU A1032 1344 1137 4190 241 35 246 N ATOM 1784 CA LEU A1032 44.890 20.338 78.294 1.00 17.62 C ANISOU 1784 CA LEU A1032 1249 1255 4190 181 -46 368 C ATOM 1785 C LEU A1032 46.390 20.143 78.287 1.00 24.85 C ANISOU 1785 C LEU A1032 2047 2182 5211 226 -33 464 C ATOM 1786 O LEU A1032 46.938 19.482 77.397 1.00 25.96 O ANISOU 1786 O LEU A1032 2174 2208 5481 323 40 455 O ATOM 1787 CB LEU A1032 44.226 19.159 79.017 1.00 17.69 C ANISOU 1787 CB LEU A1032 1251 1239 4230 168 -107 455 C ATOM 1788 CG LEU A1032 44.126 19.241 80.524 1.00 22.34 C ANISOU 1788 CG LEU A1032 1774 1977 4739 45 -207 558 C ATOM 1789 CD1 LEU A1032 42.801 19.876 80.969 1.00 21.38 C ANISOU 1789 CD1 LEU A1032 1729 1920 4472 -52 -218 448 C ATOM 1790 CD2 LEU A1032 44.224 17.871 81.115 1.00 26.48 C ANISOU 1790 CD2 LEU A1032 2238 2462 5361 56 -273 722 C ATOM 1791 N LEU A1033 47.067 20.732 79.241 1.00 23.60 N ANISOU 1791 N LEU A1033 1799 2165 5004 146 -93 545 N ATOM 1792 CA LEU A1033 48.505 20.569 79.275 1.00 25.09 C ANISOU 1792 CA LEU A1033 1854 2380 5299 183 -92 654 C ATOM 1793 C LEU A1033 48.803 19.616 80.417 1.00 37.39 C ANISOU 1793 C LEU A1033 3291 3987 6928 153 -199 858 C ATOM 1794 O LEU A1033 48.943 20.017 81.572 1.00 38.11 O ANISOU 1794 O LEU A1033 3323 4246 6913 18 -292 950 O ATOM 1795 CB LEU A1033 49.222 21.932 79.337 1.00 23.85 C ANISOU 1795 CB LEU A1033 1673 2346 5042 109 -80 609 C ATOM 1796 CG LEU A1033 48.858 22.894 78.189 1.00 25.28 C ANISOU 1796 CG LEU A1033 1976 2468 5161 130 11 431 C ATOM 1797 CD1 LEU A1033 49.012 24.318 78.612 1.00 25.02 C ANISOU 1797 CD1 LEU A1033 1955 2553 5001 17 2 376 C ATOM 1798 CD2 LEU A1033 49.663 22.618 76.952 1.00 26.00 C ANISOU 1798 CD2 LEU A1033 2054 2465 5360 231 105 396 C ATOM 1799 N THR A1034 48.745 18.316 80.078 1.00 39.51 N ANISOU 1799 N THR A1034 3538 4102 7371 260 -182 922 N ATOM 1800 CA THR A1034 48.907 17.152 80.959 1.00 42.36 C ANISOU 1800 CA THR A1034 3791 4446 7856 260 -280 1135 C ATOM 1801 C THR A1034 50.186 17.180 81.773 1.00 50.34 C ANISOU 1801 C THR A1034 4610 5579 8936 220 -371 1347 C ATOM 1802 O THR A1034 51.274 17.401 81.230 1.00 49.84 O ANISOU 1802 O THR A1034 4455 5496 8984 295 -313 1351 O ATOM 1803 CB THR A1034 48.811 15.835 80.151 1.00 56.27 C ANISOU 1803 CB THR A1034 5560 5972 9847 409 -202 1133 C ATOM 1804 OG1 THR A1034 49.943 15.700 79.267 1.00 59.55 O ANISOU 1804 OG1 THR A1034 5889 6288 10451 530 -94 1109 O ATOM 1805 CG2 THR A1034 47.487 15.699 79.389 1.00 54.21 C ANISOU 1805 CG2 THR A1034 5485 5608 9503 421 -126 943 C ATOM 1806 N LYS A1035 50.047 16.894 83.077 1.00 50.51 N ANISOU 1806 N LYS A1035 4564 5735 8893 90 -518 1535 N ATOM 1807 CA LYS A1035 51.143 16.844 84.055 1.00 52.90 C ANISOU 1807 CA LYS A1035 4673 6192 9233 5 -646 1786 C ATOM 1808 C LYS A1035 51.913 18.142 84.271 1.00 57.33 C ANISOU 1808 C LYS A1035 5191 6950 9640 -102 -647 1744 C ATOM 1809 O LYS A1035 53.143 18.191 84.134 1.00 58.62 O ANISOU 1809 O LYS A1035 5204 7139 9930 -54 -653 1852 O ATOM 1810 CB LYS A1035 52.089 15.636 83.832 1.00 57.16 C ANISOU 1810 CB LYS A1035 5037 6574 10108 162 -663 1995 C ATOM 1811 CG LYS A1035 51.377 14.286 83.952 1.00 70.80 C ANISOU 1811 CG LYS A1035 6784 8127 11990 223 -695 2093 C ATOM 1812 CD LYS A1035 52.304 13.176 84.395 1.00 85.36 C ANISOU 1812 CD LYS A1035 8407 9889 14138 295 -790 2405 C ATOM 1813 CE LYS A1035 53.043 12.504 83.266 1.00 98.65 C ANISOU 1813 CE LYS A1035 10007 11309 16168 528 -640 2359 C ATOM 1814 NZ LYS A1035 53.948 11.475 83.817 1.00112.01 N ANISOU 1814 NZ LYS A1035 11453 12918 18187 595 -745 2690 N ATOM 1815 N SER A1036 51.146 19.215 84.510 1.00 51.11 N ANISOU 1815 N SER A1036 4541 6281 8599 -238 -622 1563 N ATOM 1816 CA SER A1036 51.676 20.543 84.737 1.00 49.66 C ANISOU 1816 CA SER A1036 4350 6270 8249 -364 -606 1483 C ATOM 1817 C SER A1036 51.308 21.062 86.103 1.00 51.95 C ANISOU 1817 C SER A1036 4640 6797 8300 -623 -700 1523 C ATOM 1818 O SER A1036 50.310 21.772 86.228 1.00 51.12 O ANISOU 1818 O SER A1036 4674 6719 8032 -711 -642 1327 O ATOM 1819 CB SER A1036 51.107 21.425 83.638 1.00 50.87 C ANISOU 1819 CB SER A1036 4666 6313 8349 -287 -459 1205 C ATOM 1820 OG SER A1036 51.655 21.043 82.388 1.00 59.80 O ANISOU 1820 OG SER A1036 5783 7269 9671 -92 -366 1169 O ATOM 1821 N PRO A1037 52.064 20.674 87.157 1.00 47.94 N ANISOU 1821 N PRO A1037 3972 6466 7777 -760 -845 1780 N ATOM 1822 CA PRO A1037 51.746 21.170 88.507 1.00 47.52 C ANISOU 1822 CA PRO A1037 3919 6674 7463 -1057 -930 1813 C ATOM 1823 C PRO A1037 51.629 22.693 88.577 1.00 47.82 C ANISOU 1823 C PRO A1037 4051 6827 7292 -1200 -828 1566 C ATOM 1824 O PRO A1037 50.556 23.190 88.936 1.00 48.11 O ANISOU 1824 O PRO A1037 4213 6896 7171 -1317 -771 1382 O ATOM 1825 CB PRO A1037 52.895 20.639 89.367 1.00 51.92 C ANISOU 1825 CB PRO A1037 4262 7406 8059 -1168 -1100 2147 C ATOM 1826 CG PRO A1037 53.967 20.230 88.391 1.00 57.33 C ANISOU 1826 CG PRO A1037 4829 7928 9026 -922 -1071 2238 C ATOM 1827 CD PRO A1037 53.250 19.794 87.173 1.00 51.28 C ANISOU 1827 CD PRO A1037 4193 6868 8424 -668 -935 2057 C ATOM 1828 N SER A1038 52.681 23.425 88.141 1.00 40.67 N ANISOU 1828 N SER A1038 3088 5953 6413 -1174 -787 1544 N ATOM 1829 CA SER A1038 52.751 24.895 88.141 1.00 38.92 C ANISOU 1829 CA SER A1038 2944 5820 6026 -1303 -687 1326 C ATOM 1830 C SER A1038 52.493 25.487 86.765 1.00 38.63 C ANISOU 1830 C SER A1038 3028 5559 6090 -1096 -536 1102 C ATOM 1831 O SER A1038 52.542 24.747 85.782 1.00 38.52 O ANISOU 1831 O SER A1038 3014 5354 6269 -864 -513 1135 O ATOM 1832 CB SER A1038 54.141 25.339 88.586 1.00 45.04 C ANISOU 1832 CB SER A1038 3570 6796 6748 -1439 -752 1467 C ATOM 1833 OG SER A1038 55.127 24.976 87.632 1.00 54.66 O ANISOU 1833 OG SER A1038 4692 7894 8184 -1220 -743 1563 O ATOM 1834 N LEU A1039 52.316 26.833 86.673 1.00 31.32 N ANISOU 1834 N LEU A1039 2197 4659 5045 -1192 -433 886 N ATOM 1835 CA LEU A1039 52.161 27.492 85.377 1.00 28.36 C ANISOU 1835 CA LEU A1039 1925 4089 4760 -1022 -309 706 C ATOM 1836 C LEU A1039 53.454 27.373 84.584 1.00 33.85 C ANISOU 1836 C LEU A1039 2525 4757 5578 -899 -308 805 C ATOM 1837 O LEU A1039 53.393 27.161 83.376 1.00 33.87 O ANISOU 1837 O LEU A1039 2577 4575 5715 -702 -242 749 O ATOM 1838 CB LEU A1039 51.702 28.956 85.499 1.00 27.54 C ANISOU 1838 CB LEU A1039 1929 4001 4535 -1155 -203 476 C ATOM 1839 CG LEU A1039 51.856 29.889 84.267 1.00 30.97 C ANISOU 1839 CG LEU A1039 2446 4278 5044 -1034 -96 332 C ATOM 1840 CD1 LEU A1039 51.036 29.416 83.050 1.00 30.30 C ANISOU 1840 CD1 LEU A1039 2452 3962 5096 -805 -55 278 C ATOM 1841 CD2 LEU A1039 51.478 31.311 84.606 1.00 32.05 C ANISOU 1841 CD2 LEU A1039 2663 4432 5083 -1191 -2 133 C ATOM 1842 N ASN A1040 54.616 27.445 85.249 1.00 31.80 N ANISOU 1842 N ASN A1040 2120 4687 5274 -1024 -383 958 N ATOM 1843 CA ASN A1040 55.887 27.313 84.540 1.00 32.51 C ANISOU 1843 CA ASN A1040 2095 4761 5495 -911 -378 1056 C ATOM 1844 C ASN A1040 56.108 25.937 83.926 1.00 36.21 C ANISOU 1844 C ASN A1040 2478 5084 6198 -687 -404 1199 C ATOM 1845 O ASN A1040 56.789 25.849 82.904 1.00 36.65 O ANISOU 1845 O ASN A1040 2496 5035 6395 -536 -334 1181 O ATOM 1846 CB ASN A1040 57.073 27.800 85.367 1.00 37.24 C ANISOU 1846 CB ASN A1040 2550 5606 5993 -1107 -450 1183 C ATOM 1847 CG ASN A1040 57.340 29.274 85.177 1.00 66.38 C ANISOU 1847 CG ASN A1040 6322 9349 9550 -1230 -355 998 C ATOM 1848 OD1 ASN A1040 56.582 30.141 85.635 1.00 59.02 O ANISOU 1848 OD1 ASN A1040 5514 8446 8465 -1381 -303 828 O ATOM 1849 ND2 ASN A1040 58.408 29.589 84.455 1.00 61.73 N ANISOU 1849 ND2 ASN A1040 5664 8755 9035 -1163 -318 1017 N ATOM 1850 N ALA A1041 55.485 24.882 84.500 1.00 31.73 N ANISOU 1850 N ALA A1041 1888 4494 5673 -672 -487 1319 N ATOM 1851 CA ALA A1041 55.566 23.520 83.962 1.00 31.77 C ANISOU 1851 CA ALA A1041 1823 4328 5921 -464 -499 1442 C ATOM 1852 C ALA A1041 54.711 23.453 82.699 1.00 34.58 C ANISOU 1852 C ALA A1041 2346 4450 6344 -291 -365 1230 C ATOM 1853 O ALA A1041 55.160 22.918 81.681 1.00 34.63 O ANISOU 1853 O ALA A1041 2318 4304 6535 -116 -289 1218 O ATOM 1854 CB ALA A1041 55.067 22.513 84.985 1.00 33.37 C ANISOU 1854 CB ALA A1041 1971 4577 6131 -527 -631 1630 C ATOM 1855 N ALA A1042 53.490 24.046 82.766 1.00 29.66 N ANISOU 1855 N ALA A1042 1895 3808 5565 -358 -331 1057 N ATOM 1856 CA ALA A1042 52.522 24.166 81.679 1.00 27.39 C ANISOU 1856 CA ALA A1042 1772 3336 5297 -240 -226 864 C ATOM 1857 C ALA A1042 53.109 25.008 80.529 1.00 31.54 C ANISOU 1857 C ALA A1042 2337 3806 5840 -180 -119 737 C ATOM 1858 O ALA A1042 52.926 24.655 79.351 1.00 31.57 O ANISOU 1858 O ALA A1042 2404 3651 5941 -42 -36 657 O ATOM 1859 CB ALA A1042 51.251 24.809 82.203 1.00 26.70 C ANISOU 1859 CB ALA A1042 1816 3281 5047 -356 -225 734 C ATOM 1860 N LYS A1043 53.845 26.100 80.876 1.00 26.45 N ANISOU 1860 N LYS A1043 1655 3301 5092 -304 -120 722 N ATOM 1861 CA LYS A1043 54.496 26.969 79.903 1.00 24.80 C ANISOU 1861 CA LYS A1043 1475 3064 4884 -278 -31 622 C ATOM 1862 C LYS A1043 55.582 26.182 79.202 1.00 29.75 C ANISOU 1862 C LYS A1043 1978 3644 5684 -148 2 710 C ATOM 1863 O LYS A1043 55.623 26.194 77.980 1.00 29.37 O ANISOU 1863 O LYS A1043 1989 3474 5695 -48 101 607 O ATOM 1864 CB LYS A1043 55.053 28.229 80.568 1.00 26.50 C ANISOU 1864 CB LYS A1043 1670 3444 4954 -458 -43 597 C ATOM 1865 CG LYS A1043 54.041 29.358 80.687 1.00 28.93 C ANISOU 1865 CG LYS A1043 2130 3724 5136 -555 0 425 C ATOM 1866 CD LYS A1043 54.597 30.479 81.535 1.00 35.95 C ANISOU 1866 CD LYS A1043 2991 4779 5890 -759 -5 399 C ATOM 1867 CE LYS A1043 53.921 31.802 81.286 1.00 46.29 C ANISOU 1867 CE LYS A1043 4439 6012 7136 -826 79 209 C ATOM 1868 NZ LYS A1043 54.365 32.832 82.261 1.00 52.83 N ANISOU 1868 NZ LYS A1043 5244 6997 7832 -1050 89 162 N ATOM 1869 N SER A1044 56.393 25.413 79.961 1.00 28.46 N ANISOU 1869 N SER A1044 1633 3568 5614 -150 -80 905 N ATOM 1870 CA SER A1044 57.466 24.589 79.393 1.00 29.52 C ANISOU 1870 CA SER A1044 1610 3644 5962 -15 -42 1001 C ATOM 1871 C SER A1044 56.997 23.406 78.517 1.00 32.87 C ANISOU 1871 C SER A1044 2067 3849 6573 166 35 960 C ATOM 1872 O SER A1044 57.752 22.946 77.652 1.00 34.60 O ANISOU 1872 O SER A1044 2206 3977 6964 281 134 941 O ATOM 1873 CB SER A1044 58.418 24.099 80.475 1.00 35.05 C ANISOU 1873 CB SER A1044 2088 4491 6740 -68 -165 1249 C ATOM 1874 OG SER A1044 59.545 23.490 79.862 1.00 51.00 O ANISOU 1874 OG SER A1044 3937 6450 8993 65 -109 1326 O ATOM 1875 N GLU A1045 55.787 22.900 78.756 1.00 26.51 N ANISOU 1875 N GLU A1045 1372 2963 5736 178 2 938 N ATOM 1876 CA GLU A1045 55.270 21.790 77.979 1.00 26.11 C ANISOU 1876 CA GLU A1045 1366 2711 5843 323 77 890 C ATOM 1877 C GLU A1045 54.766 22.356 76.664 1.00 27.18 C ANISOU 1877 C GLU A1045 1672 2755 5899 347 204 667 C ATOM 1878 O GLU A1045 55.043 21.791 75.602 1.00 26.40 O ANISOU 1878 O GLU A1045 1573 2528 5930 445 324 587 O ATOM 1879 CB GLU A1045 54.160 21.089 78.766 1.00 27.69 C ANISOU 1879 CB GLU A1045 1621 2881 6019 303 -15 958 C ATOM 1880 CG GLU A1045 53.627 19.800 78.165 1.00 43.25 C ANISOU 1880 CG GLU A1045 3625 4646 8164 436 46 937 C ATOM 1881 CD GLU A1045 52.315 19.325 78.768 1.00 76.27 C ANISOU 1881 CD GLU A1045 7909 8802 12269 396 -30 954 C ATOM 1882 OE1 GLU A1045 51.976 19.767 79.891 1.00 73.68 O ANISOU 1882 OE1 GLU A1045 7578 8625 11791 266 -147 1032 O ATOM 1883 OE2 GLU A1045 51.618 18.515 78.112 1.00 75.38 O ANISOU 1883 OE2 GLU A1045 7880 8523 12237 478 37 878 O ATOM 1884 N LEU A1046 54.064 23.510 76.742 1.00 22.63 N ANISOU 1884 N LEU A1046 1234 2249 5115 241 181 568 N ATOM 1885 CA LEU A1046 53.484 24.246 75.608 1.00 20.45 C ANISOU 1885 CA LEU A1046 1119 1909 4741 233 265 392 C ATOM 1886 C LEU A1046 54.585 24.705 74.661 1.00 24.88 C ANISOU 1886 C LEU A1046 1639 2483 5331 242 362 336 C ATOM 1887 O LEU A1046 54.442 24.555 73.451 1.00 24.01 O ANISOU 1887 O LEU A1046 1607 2280 5235 280 464 223 O ATOM 1888 CB LEU A1046 52.669 25.448 76.130 1.00 18.60 C ANISOU 1888 CB LEU A1046 991 1749 4327 116 207 338 C ATOM 1889 CG LEU A1046 52.151 26.440 75.108 1.00 21.23 C ANISOU 1889 CG LEU A1046 1467 2032 4569 88 264 200 C ATOM 1890 CD1 LEU A1046 51.017 25.875 74.365 1.00 20.93 C ANISOU 1890 CD1 LEU A1046 1542 1870 4540 145 288 133 C ATOM 1891 CD2 LEU A1046 51.687 27.706 75.768 1.00 22.20 C ANISOU 1891 CD2 LEU A1046 1643 2222 4572 -24 219 164 C ATOM 1892 N ASP A1047 55.696 25.233 75.225 1.00 22.89 N ANISOU 1892 N ASP A1047 1260 2362 5076 189 332 417 N ATOM 1893 CA ASP A1047 56.884 25.699 74.501 1.00 23.60 C ANISOU 1893 CA ASP A1047 1281 2493 5192 183 417 383 C ATOM 1894 C ASP A1047 57.533 24.556 73.712 1.00 26.76 C ANISOU 1894 C ASP A1047 1581 2787 5798 308 528 372 C ATOM 1895 O ASP A1047 58.002 24.777 72.588 1.00 26.57 O ANISOU 1895 O ASP A1047 1581 2736 5779 310 650 257 O ATOM 1896 CB ASP A1047 57.884 26.382 75.461 1.00 26.77 C ANISOU 1896 CB ASP A1047 1549 3072 5551 89 343 494 C ATOM 1897 CG ASP A1047 57.498 27.812 75.853 1.00 39.93 C ANISOU 1897 CG ASP A1047 3329 4831 7013 -60 300 434 C ATOM 1898 OD1 ASP A1047 56.450 28.300 75.371 1.00 39.63 O ANISOU 1898 OD1 ASP A1047 3460 4708 6888 -74 320 320 O ATOM 1899 OD2 ASP A1047 58.253 28.446 76.639 1.00 44.83 O ANISOU 1899 OD2 ASP A1047 3859 5604 7571 -168 248 504 O ATOM 1900 N LYS A1048 57.496 23.320 74.284 1.00 22.74 N ANISOU 1900 N LYS A1048 967 2209 5465 403 494 484 N ATOM 1901 CA LYS A1048 57.983 22.103 73.637 1.00 22.95 C ANISOU 1901 CA LYS A1048 891 2091 5735 533 612 470 C ATOM 1902 C LYS A1048 57.048 21.740 72.466 1.00 26.33 C ANISOU 1902 C LYS A1048 1500 2375 6130 556 729 283 C ATOM 1903 O LYS A1048 57.535 21.511 71.365 1.00 28.39 O ANISOU 1903 O LYS A1048 1754 2571 6463 581 887 155 O ATOM 1904 CB LYS A1048 58.124 20.952 74.642 1.00 25.19 C ANISOU 1904 CB LYS A1048 1016 2328 6227 617 526 665 C ATOM 1905 CG LYS A1048 59.009 19.832 74.131 1.00 36.10 C ANISOU 1905 CG LYS A1048 2224 3568 7925 757 651 682 C ATOM 1906 CD LYS A1048 59.412 18.863 75.228 1.00 53.30 C ANISOU 1906 CD LYS A1048 4195 5718 10337 831 538 935 C ATOM 1907 CE LYS A1048 60.145 17.656 74.672 1.00 70.06 C ANISOU 1907 CE LYS A1048 6146 7644 12831 992 682 940 C ATOM 1908 NZ LYS A1048 60.846 16.878 75.731 1.00 80.84 N ANISOU 1908 NZ LYS A1048 7253 9002 14461 1063 558 1233 N ATOM 1909 N ALA A1049 55.720 21.762 72.687 1.00 19.62 N ANISOU 1909 N ALA A1049 808 1495 5152 523 656 261 N ATOM 1910 CA ALA A1049 54.701 21.473 71.669 1.00 18.15 C ANISOU 1910 CA ALA A1049 800 1197 4898 512 735 107 C ATOM 1911 C ALA A1049 54.738 22.418 70.475 1.00 21.90 C ANISOU 1911 C ALA A1049 1387 1714 5218 429 820 -41 C ATOM 1912 O ALA A1049 54.781 21.965 69.338 1.00 21.62 O ANISOU 1912 O ALA A1049 1399 1603 5211 427 960 -172 O ATOM 1913 CB ALA A1049 53.310 21.515 72.297 1.00 17.35 C ANISOU 1913 CB ALA A1049 818 1093 4682 485 617 137 C ATOM 1914 N ILE A1050 54.672 23.734 70.734 1.00 18.14 N ANISOU 1914 N ILE A1050 964 1357 4573 339 737 -20 N ATOM 1915 CA ILE A1050 54.633 24.749 69.692 1.00 16.73 C ANISOU 1915 CA ILE A1050 898 1219 4238 240 785 -123 C ATOM 1916 C ILE A1050 55.966 24.921 68.982 1.00 22.54 C ANISOU 1916 C ILE A1050 1545 2001 5020 221 905 -175 C ATOM 1917 O ILE A1050 55.975 25.131 67.773 1.00 24.42 O ANISOU 1917 O ILE A1050 1868 2232 5178 151 1003 -291 O ATOM 1918 CB ILE A1050 53.972 26.046 70.207 1.00 17.94 C ANISOU 1918 CB ILE A1050 1141 1443 4231 157 662 -86 C ATOM 1919 CG1 ILE A1050 52.470 25.885 70.170 1.00 17.65 C ANISOU 1919 CG1 ILE A1050 1237 1336 4133 155 604 -106 C ATOM 1920 CG2 ILE A1050 54.343 27.258 69.365 1.00 19.03 C ANISOU 1920 CG2 ILE A1050 1345 1639 4247 53 693 -139 C ATOM 1921 CD1 ILE A1050 51.931 25.475 71.370 1.00 29.29 C ANISOU 1921 CD1 ILE A1050 2675 2806 5649 197 514 -30 C ATOM 1922 N GLY A1051 57.059 24.799 69.731 1.00 18.46 N ANISOU 1922 N GLY A1051 850 1540 4625 269 894 -83 N ATOM 1923 CA GLY A1051 58.412 24.925 69.215 1.00 19.11 C ANISOU 1923 CA GLY A1051 808 1676 4778 261 1006 -117 C ATOM 1924 C GLY A1051 58.961 26.336 69.251 1.00 22.28 C ANISOU 1924 C GLY A1051 1223 2217 5024 146 962 -101 C ATOM 1925 O GLY A1051 59.688 26.728 68.335 1.00 24.52 O ANISOU 1925 O GLY A1051 1500 2543 5272 85 1069 -187 O ATOM 1926 N ARG A1052 58.632 27.106 70.310 1.00 15.93 N ANISOU 1926 N ARG A1052 552 1427 4074 87 780 1 N ATOM 1927 CA ARG A1052 59.115 28.470 70.553 1.00 14.94 C ANISOU 1927 CA ARG A1052 527 1376 3774 -11 705 17 C ATOM 1928 C ARG A1052 58.913 28.901 71.996 1.00 19.09 C ANISOU 1928 C ARG A1052 814 2085 4353 -50 631 129 C ATOM 1929 O ARG A1052 58.321 28.150 72.771 1.00 18.19 O ANISOU 1929 O ARG A1052 677 1935 4300 11 565 195 O ATOM 1930 CB ARG A1052 58.480 29.474 69.597 1.00 12.13 C ANISOU 1930 CB ARG A1052 535 903 3171 -65 650 -87 C ATOM 1931 CG ARG A1052 56.992 29.684 69.730 1.00 15.19 C ANISOU 1931 CG ARG A1052 699 1411 3660 -122 704 -84 C ATOM 1932 CD ARG A1052 56.589 30.820 68.805 1.00 14.07 C ANISOU 1932 CD ARG A1052 704 1258 3381 -232 705 -135 C ATOM 1933 NE ARG A1052 55.221 31.273 69.036 1.00 14.82 N ANISOU 1933 NE ARG A1052 923 1281 3426 -243 616 -123 N ATOM 1934 CZ ARG A1052 54.885 32.173 69.949 1.00 31.80 C ANISOU 1934 CZ ARG A1052 3089 3441 5553 -282 538 -88 C ATOM 1935 NH1 ARG A1052 55.812 32.711 70.732 1.00 21.87 N ANISOU 1935 NH1 ARG A1052 1742 2277 4290 -329 531 -59 N ATOM 1936 NH2 ARG A1052 53.619 32.538 70.093 1.00 23.72 N ANISOU 1936 NH2 ARG A1052 2161 2337 4516 -283 475 -89 N ATOM 1937 N ASN A1053 59.380 30.121 72.357 1.00 16.22 N ANISOU 1937 N ASN A1053 501 1808 3854 -161 582 140 N ATOM 1938 CA ASN A1053 59.192 30.675 73.698 1.00 16.00 C ANISOU 1938 CA ASN A1053 490 1851 3737 -227 466 211 C ATOM 1939 C ASN A1053 57.908 31.525 73.729 1.00 20.62 C ANISOU 1939 C ASN A1053 1177 2404 4253 -308 451 139 C ATOM 1940 O ASN A1053 57.950 32.744 73.617 1.00 20.29 O ANISOU 1940 O ASN A1053 1209 2383 4118 -414 456 91 O ATOM 1941 CB ASN A1053 60.423 31.442 74.141 1.00 16.40 C ANISOU 1941 CB ASN A1053 509 2023 3700 -306 439 255 C ATOM 1942 CG ASN A1053 60.413 31.852 75.584 1.00 47.11 C ANISOU 1942 CG ASN A1053 4188 6113 7598 -468 374 340 C ATOM 1943 OD1 ASN A1053 61.431 32.238 76.180 1.00 47.12 O ANISOU 1943 OD1 ASN A1053 4067 6270 7566 -566 347 410 O ATOM 1944 ND2 ASN A1053 59.251 31.758 76.184 1.00 45.22 N ANISOU 1944 ND2 ASN A1053 4039 5819 7322 -471 321 325 N ATOM 1945 N THR A1054 56.766 30.843 73.862 1.00 19.33 N ANISOU 1945 N THR A1054 1079 2145 4120 -235 420 131 N ATOM 1946 CA THR A1054 55.405 31.389 73.809 1.00 18.79 C ANISOU 1946 CA THR A1054 1164 1984 3992 -257 393 66 C ATOM 1947 C THR A1054 55.044 32.308 74.930 1.00 25.04 C ANISOU 1947 C THR A1054 1974 2828 4713 -364 341 58 C ATOM 1948 O THR A1054 54.333 33.279 74.691 1.00 26.04 O ANISOU 1948 O THR A1054 2210 2882 4802 -413 348 -11 O ATOM 1949 CB THR A1054 54.350 30.278 73.671 1.00 18.46 C ANISOU 1949 CB THR A1054 1166 1841 4008 -152 378 65 C ATOM 1950 OG1 THR A1054 54.373 29.461 74.846 1.00 17.52 O ANISOU 1950 OG1 THR A1054 947 1776 3934 -129 318 149 O ATOM 1951 CG2 THR A1054 54.544 29.431 72.416 1.00 12.51 C ANISOU 1951 CG2 THR A1054 456 997 3300 -63 448 32 C ATOM 1952 N ASN A1055 55.491 32.004 76.144 1.00 22.77 N ANISOU 1952 N ASN A1055 1576 2662 4415 -413 291 129 N ATOM 1953 CA ASN A1055 55.122 32.797 77.311 1.00 23.67 C ANISOU 1953 CA ASN A1055 1706 2845 4444 -548 257 100 C ATOM 1954 C ASN A1055 53.638 32.650 77.641 1.00 28.20 C ANISOU 1954 C ASN A1055 2370 3323 5021 -524 239 43 C ATOM 1955 O ASN A1055 53.005 33.582 78.137 1.00 30.24 O ANISOU 1955 O ASN A1055 2691 3562 5237 -618 255 -44 O ATOM 1956 CB ASN A1055 55.470 34.270 77.092 1.00 27.46 C ANISOU 1956 CB ASN A1055 2243 3328 4862 -664 304 20 C ATOM 1957 CG ASN A1055 55.295 35.103 78.347 1.00 63.56 C ANISOU 1957 CG ASN A1055 6816 7983 9350 -833 297 -32 C ATOM 1958 OD1 ASN A1055 55.214 34.570 79.453 1.00 65.52 O ANISOU 1958 OD1 ASN A1055 6996 8343 9557 -892 248 15 O ATOM 1959 ND2 ASN A1055 55.236 36.419 78.180 1.00 58.46 N ANISOU 1959 ND2 ASN A1055 6248 7283 8680 -927 352 -129 N ATOM 1960 N GLY A1056 53.092 31.471 77.359 1.00 22.92 N ANISOU 1960 N GLY A1056 1702 2588 4419 -401 216 85 N ATOM 1961 CA GLY A1056 51.683 31.189 77.596 1.00 21.10 C ANISOU 1961 CA GLY A1056 1548 2273 4196 -370 197 39 C ATOM 1962 C GLY A1056 50.789 31.801 76.539 1.00 21.73 C ANISOU 1962 C GLY A1056 1752 2204 4302 -323 234 -47 C ATOM 1963 O GLY A1056 49.574 31.687 76.635 1.00 21.31 O ANISOU 1963 O GLY A1056 1757 2074 4267 -296 221 -87 O ATOM 1964 N VAL A1057 51.363 32.448 75.519 1.00 15.30 N ANISOU 1964 N VAL A1057 971 1353 3490 -321 274 -63 N ATOM 1965 CA VAL A1057 50.564 33.076 74.472 1.00 12.81 C ANISOU 1965 CA VAL A1057 764 907 3196 -297 290 -110 C ATOM 1966 C VAL A1057 50.866 32.511 73.105 1.00 16.88 C ANISOU 1966 C VAL A1057 1310 1386 3719 -232 313 -86 C ATOM 1967 O VAL A1057 51.969 32.703 72.581 1.00 17.66 O ANISOU 1967 O VAL A1057 1378 1536 3796 -259 352 -74 O ATOM 1968 CB VAL A1057 50.622 34.628 74.469 1.00 15.28 C ANISOU 1968 CB VAL A1057 1118 1184 3503 -393 313 -159 C ATOM 1969 CG1 VAL A1057 49.734 35.202 73.365 1.00 14.29 C ANISOU 1969 CG1 VAL A1057 1088 915 3425 -364 305 -164 C ATOM 1970 CG2 VAL A1057 50.245 35.213 75.832 1.00 15.15 C ANISOU 1970 CG2 VAL A1057 1078 1197 3482 -481 320 -221 C ATOM 1971 N ILE A1058 49.862 31.856 72.521 1.00 12.78 N ANISOU 1971 N ILE A1058 850 785 3220 -167 298 -90 N ATOM 1972 CA ILE A1058 49.915 31.280 71.177 1.00 12.81 C ANISOU 1972 CA ILE A1058 902 754 3213 -135 329 -89 C ATOM 1973 C ILE A1058 49.009 32.100 70.239 1.00 21.10 C ANISOU 1973 C ILE A1058 2054 1722 4241 -175 300 -89 C ATOM 1974 O ILE A1058 48.336 33.018 70.713 1.00 21.85 O ANISOU 1974 O ILE A1058 2167 1768 4369 -199 261 -88 O ATOM 1975 CB ILE A1058 49.661 29.735 71.113 1.00 14.32 C ANISOU 1975 CB ILE A1058 1074 928 3440 -50 344 -88 C ATOM 1976 CG1 ILE A1058 48.337 29.333 71.751 1.00 13.22 C ANISOU 1976 CG1 ILE A1058 964 739 3321 -16 287 -86 C ATOM 1977 CG2 ILE A1058 50.812 28.955 71.708 1.00 14.19 C ANISOU 1977 CG2 ILE A1058 938 978 3476 -11 377 -58 C ATOM 1978 CD1 ILE A1058 47.609 28.456 70.986 1.00 14.84 C ANISOU 1978 CD1 ILE A1058 1226 885 3526 21 295 -100 C ATOM 1979 N THR A1059 49.027 31.788 68.918 1.00 19.76 N ANISOU 1979 N THR A1059 1942 1543 4025 -196 324 -86 N ATOM 1980 CA THR A1059 48.274 32.446 67.836 1.00 20.20 C ANISOU 1980 CA THR A1059 2087 1547 4043 -259 281 -50 C ATOM 1981 C THR A1059 47.227 31.473 67.281 1.00 26.17 C ANISOU 1981 C THR A1059 2892 2272 4779 -235 260 -51 C ATOM 1982 O THR A1059 47.345 30.282 67.561 1.00 27.01 O ANISOU 1982 O THR A1059 2970 2393 4897 -175 304 -95 O ATOM 1983 CB THR A1059 49.255 32.887 66.735 1.00 26.31 C ANISOU 1983 CB THR A1059 2887 2374 4737 -354 326 -44 C ATOM 1984 OG1 THR A1059 49.663 31.751 65.990 1.00 23.52 O ANISOU 1984 OG1 THR A1059 2538 2066 4331 -358 403 -96 O ATOM 1985 CG2 THR A1059 50.494 33.583 67.287 1.00 26.52 C ANISOU 1985 CG2 THR A1059 2851 2453 4772 -379 365 -56 C ATOM 1986 N LYS A1060 46.227 31.942 66.489 1.00 23.14 N ANISOU 1986 N LYS A1060 2574 1846 4372 -289 190 9 N ATOM 1987 CA LYS A1060 45.182 31.053 65.931 1.00 22.90 C ANISOU 1987 CA LYS A1060 2591 1804 4307 -291 161 14 C ATOM 1988 C LYS A1060 45.769 29.874 65.168 1.00 28.11 C ANISOU 1988 C LYS A1060 3277 2520 4882 -324 255 -58 C ATOM 1989 O LYS A1060 45.307 28.741 65.333 1.00 28.25 O ANISOU 1989 O LYS A1060 3299 2523 4911 -277 280 -104 O ATOM 1990 CB LYS A1060 44.215 31.816 65.003 1.00 25.60 C ANISOU 1990 CB LYS A1060 2986 2120 4623 -377 62 119 C ATOM 1991 CG LYS A1060 43.048 30.973 64.454 1.00 32.59 C ANISOU 1991 CG LYS A1060 3913 3010 5461 -401 18 138 C ATOM 1992 CD LYS A1060 43.044 30.883 62.918 1.00 47.01 C ANISOU 1992 CD LYS A1060 5814 4911 7135 -562 5 182 C ATOM 1993 CE LYS A1060 43.803 29.712 62.319 1.00 62.56 C ANISOU 1993 CE LYS A1060 7824 6955 8991 -617 134 59 C ATOM 1994 NZ LYS A1060 43.734 29.706 60.827 1.00 71.99 N ANISOU 1994 NZ LYS A1060 9097 8241 10014 -816 129 89 N ATOM 1995 N ASP A1061 46.768 30.157 64.317 1.00 24.82 N ANISOU 1995 N ASP A1061 2877 2163 4389 -414 317 -77 N ATOM 1996 CA ASP A1061 47.431 29.188 63.456 1.00 25.58 C ANISOU 1996 CA ASP A1061 2995 2312 4413 -471 437 -170 C ATOM 1997 C ASP A1061 48.185 28.123 64.246 1.00 27.13 C ANISOU 1997 C ASP A1061 3108 2488 4712 -350 538 -256 C ATOM 1998 O ASP A1061 48.250 26.969 63.799 1.00 27.67 O ANISOU 1998 O ASP A1061 3188 2546 4780 -353 634 -342 O ATOM 1999 CB ASP A1061 48.317 29.912 62.441 1.00 29.95 C ANISOU 1999 CB ASP A1061 3575 2942 4863 -611 480 -169 C ATOM 2000 CG ASP A1061 47.546 30.902 61.558 1.00 55.96 C ANISOU 2000 CG ASP A1061 6948 6257 8057 -750 363 -50 C ATOM 2001 OD1 ASP A1061 47.113 31.970 62.083 1.00 58.96 O ANISOU 2001 OD1 ASP A1061 7313 6580 8510 -715 252 57 O ATOM 2002 OD2 ASP A1061 47.379 30.616 60.345 1.00 65.21 O ANISOU 2002 OD2 ASP A1061 8191 7500 9087 -907 385 -61 O ATOM 2003 N GLU A1062 48.706 28.498 65.447 1.00 20.52 N ANISOU 2003 N GLU A1062 2183 1641 3971 -254 514 -224 N ATOM 2004 CA GLU A1062 49.408 27.587 66.358 1.00 18.15 C ANISOU 2004 CA GLU A1062 1782 1330 3785 -142 573 -255 C ATOM 2005 C GLU A1062 48.326 26.734 67.019 1.00 19.13 C ANISOU 2005 C GLU A1062 1917 1391 3962 -66 523 -243 C ATOM 2006 O GLU A1062 48.421 25.517 66.986 1.00 18.44 O ANISOU 2006 O GLU A1062 1808 1264 3935 -17 592 -289 O ATOM 2007 CB GLU A1062 50.273 28.349 67.391 1.00 18.46 C ANISOU 2007 CB GLU A1062 1727 1412 3875 -109 545 -207 C ATOM 2008 CG GLU A1062 51.321 29.240 66.748 1.00 26.15 C ANISOU 2008 CG GLU A1062 2693 2451 4791 -194 592 -217 C ATOM 2009 CD GLU A1062 52.393 29.895 67.602 1.00 54.28 C ANISOU 2009 CD GLU A1062 6158 6077 8391 -186 588 -184 C ATOM 2010 OE1 GLU A1062 52.118 30.260 68.769 1.00 41.12 O ANISOU 2010 OE1 GLU A1062 4456 4409 6758 -154 514 -138 O ATOM 2011 OE2 GLU A1062 53.509 30.093 67.071 1.00 59.56 O ANISOU 2011 OE2 GLU A1062 6784 6806 9041 -233 664 -211 O ATOM 2012 N ALA A1063 47.251 27.368 67.522 1.00 14.13 N ANISOU 2012 N ALA A1063 1319 739 3312 -66 414 -188 N ATOM 2013 CA ALA A1063 46.103 26.699 68.120 1.00 13.50 C ANISOU 2013 CA ALA A1063 1252 611 3264 -14 360 -177 C ATOM 2014 C ALA A1063 45.516 25.675 67.151 1.00 21.50 C ANISOU 2014 C ALA A1063 2338 1594 4235 -46 403 -226 C ATOM 2015 O ALA A1063 45.079 24.611 67.596 1.00 22.00 O ANISOU 2015 O ALA A1063 2393 1615 4350 9 413 -243 O ATOM 2016 CB ALA A1063 45.045 27.720 68.495 1.00 13.40 C ANISOU 2016 CB ALA A1063 1265 583 3243 -33 257 -127 C ATOM 2017 N GLU A1064 45.526 25.981 65.831 1.00 20.19 N ANISOU 2017 N GLU A1064 2245 1460 3968 -156 431 -248 N ATOM 2018 CA GLU A1064 45.031 25.065 64.802 1.00 21.40 C ANISOU 2018 CA GLU A1064 2474 1607 4049 -232 486 -311 C ATOM 2019 C GLU A1064 46.017 23.911 64.582 1.00 25.94 C ANISOU 2019 C GLU A1064 3016 2154 4685 -205 645 -422 C ATOM 2020 O GLU A1064 45.570 22.785 64.418 1.00 26.02 O ANISOU 2020 O GLU A1064 3057 2113 4718 -200 700 -484 O ATOM 2021 CB GLU A1064 44.690 25.790 63.489 1.00 23.71 C ANISOU 2021 CB GLU A1064 2852 1966 4192 -395 454 -285 C ATOM 2022 CG GLU A1064 43.731 24.995 62.621 1.00 36.83 C ANISOU 2022 CG GLU A1064 4599 3641 5754 -499 461 -320 C ATOM 2023 CD GLU A1064 43.483 25.510 61.215 1.00 73.60 C ANISOU 2023 CD GLU A1064 9338 8392 10236 -702 436 -290 C ATOM 2024 OE1 GLU A1064 43.482 24.684 60.272 1.00 76.35 O ANISOU 2024 OE1 GLU A1064 9751 8782 10477 -832 534 -390 O ATOM 2025 OE2 GLU A1064 43.245 26.731 61.060 1.00 74.87 O ANISOU 2025 OE2 GLU A1064 9496 8582 10367 -745 317 -163 O ATOM 2026 N LYS A1065 47.347 24.178 64.619 1.00 23.01 N ANISOU 2026 N LYS A1065 2572 1806 4363 -182 722 -446 N ATOM 2027 CA LYS A1065 48.395 23.156 64.482 1.00 24.12 C ANISOU 2027 CA LYS A1065 2644 1906 4615 -136 882 -543 C ATOM 2028 C LYS A1065 48.208 22.121 65.591 1.00 28.26 C ANISOU 2028 C LYS A1065 3099 2337 5302 6 870 -514 C ATOM 2029 O LYS A1065 48.102 20.923 65.320 1.00 29.09 O ANISOU 2029 O LYS A1065 3212 2358 5482 24 969 -593 O ATOM 2030 CB LYS A1065 49.794 23.803 64.585 1.00 28.29 C ANISOU 2030 CB LYS A1065 3077 2487 5184 -120 932 -537 C ATOM 2031 CG LYS A1065 50.977 22.836 64.398 1.00 54.67 C ANISOU 2031 CG LYS A1065 6316 5783 8674 -67 1107 -634 C ATOM 2032 CD LYS A1065 51.986 22.875 65.562 1.00 63.67 C ANISOU 2032 CD LYS A1065 7293 6921 9979 66 1084 -547 C ATOM 2033 CE LYS A1065 53.243 22.092 65.237 1.00 72.86 C ANISOU 2033 CE LYS A1065 8331 8042 11309 114 1260 -631 C ATOM 2034 NZ LYS A1065 54.179 22.022 66.389 1.00 78.24 N ANISOU 2034 NZ LYS A1065 8835 8728 12166 239 1219 -515 N ATOM 2035 N LEU A1066 48.121 22.607 66.835 1.00 23.74 N ANISOU 2035 N LEU A1066 2464 1781 4776 87 748 -400 N ATOM 2036 CA LEU A1066 47.888 21.833 68.058 1.00 22.67 C ANISOU 2036 CA LEU A1066 2260 1589 4765 195 697 -333 C ATOM 2037 C LEU A1066 46.565 21.090 67.944 1.00 25.48 C ANISOU 2037 C LEU A1066 2707 1886 5089 180 668 -355 C ATOM 2038 O LEU A1066 46.489 19.955 68.404 1.00 26.11 O ANISOU 2038 O LEU A1066 2752 1882 5286 247 696 -350 O ATOM 2039 CB LEU A1066 47.775 22.784 69.269 1.00 21.34 C ANISOU 2039 CB LEU A1066 2043 1488 4575 216 562 -225 C ATOM 2040 CG LEU A1066 48.936 22.935 70.223 1.00 25.09 C ANISOU 2040 CG LEU A1066 2381 2009 5143 270 551 -150 C ATOM 2041 CD1 LEU A1066 48.609 23.996 71.264 1.00 23.01 C ANISOU 2041 CD1 LEU A1066 2106 1826 4811 238 433 -81 C ATOM 2042 CD2 LEU A1066 49.247 21.625 70.914 1.00 27.30 C ANISOU 2042 CD2 LEU A1066 2565 2224 5586 361 567 -96 C ATOM 2043 N PHE A1067 45.510 21.750 67.389 1.00 19.48 N ANISOU 2043 N PHE A1067 2052 1167 4181 91 601 -361 N ATOM 2044 CA PHE A1067 44.200 21.131 67.256 1.00 18.40 C ANISOU 2044 CA PHE A1067 1996 996 4001 61 563 -374 C ATOM 2045 C PHE A1067 44.355 19.931 66.373 1.00 24.92 C ANISOU 2045 C PHE A1067 2865 1754 4851 25 702 -486 C ATOM 2046 O PHE A1067 44.121 18.820 66.839 1.00 26.10 O ANISOU 2046 O PHE A1067 2999 1815 5102 84 731 -496 O ATOM 2047 CB PHE A1067 43.137 22.099 66.700 1.00 19.05 C ANISOU 2047 CB PHE A1067 2158 1139 3940 -34 465 -342 C ATOM 2048 CG PHE A1067 41.798 21.444 66.445 1.00 19.67 C ANISOU 2048 CG PHE A1067 2311 1198 3965 -81 427 -353 C ATOM 2049 CD1 PHE A1067 40.992 21.033 67.502 1.00 21.01 C ANISOU 2049 CD1 PHE A1067 2455 1336 4190 -14 357 -310 C ATOM 2050 CD2 PHE A1067 41.342 21.242 65.152 1.00 22.03 C ANISOU 2050 CD2 PHE A1067 2701 1527 4142 -214 461 -405 C ATOM 2051 CE1 PHE A1067 39.751 20.443 67.267 1.00 21.45 C ANISOU 2051 CE1 PHE A1067 2574 1384 4194 -65 321 -320 C ATOM 2052 CE2 PHE A1067 40.097 20.647 64.918 1.00 24.60 C ANISOU 2052 CE2 PHE A1067 3090 1851 4407 -274 420 -409 C ATOM 2053 CZ PHE A1067 39.309 20.256 65.977 1.00 21.59 C ANISOU 2053 CZ PHE A1067 2679 1429 4095 -191 350 -366 C ATOM 2054 N ASN A1068 44.856 20.141 65.133 1.00 21.76 N ANISOU 2054 N ASN A1068 2510 1390 4368 -79 802 -575 N ATOM 2055 CA ASN A1068 45.119 19.090 64.148 1.00 22.50 C ANISOU 2055 CA ASN A1068 2648 1428 4473 -149 974 -723 C ATOM 2056 C ASN A1068 45.838 17.877 64.772 1.00 29.06 C ANISOU 2056 C ASN A1068 3384 2120 5536 -17 1086 -760 C ATOM 2057 O ASN A1068 45.527 16.758 64.398 1.00 31.18 O ANISOU 2057 O ASN A1068 3696 2295 5857 -42 1191 -858 O ATOM 2058 CB ASN A1068 45.871 19.646 62.937 1.00 19.89 C ANISOU 2058 CB ASN A1068 2347 1178 4032 -281 1075 -810 C ATOM 2059 CG ASN A1068 45.090 20.669 62.136 1.00 42.75 C ANISOU 2059 CG ASN A1068 5342 4198 6703 -441 967 -759 C ATOM 2060 OD1 ASN A1068 43.915 20.962 62.395 1.00 36.46 O ANISOU 2060 OD1 ASN A1068 4590 3423 5841 -453 822 -665 O ATOM 2061 ND2 ASN A1068 45.730 21.247 61.137 1.00 36.95 N ANISOU 2061 ND2 ASN A1068 4635 3551 5855 -575 1032 -808 N ATOM 2062 N GLN A1069 46.731 18.084 65.762 1.00 24.73 N ANISOU 2062 N GLN A1069 2704 1559 5135 117 1052 -668 N ATOM 2063 CA GLN A1069 47.403 16.976 66.430 1.00 24.71 C ANISOU 2063 CA GLN A1069 2587 1424 5378 247 1126 -653 C ATOM 2064 C GLN A1069 46.385 16.196 67.224 1.00 27.37 C ANISOU 2064 C GLN A1069 2951 1688 5760 292 1039 -585 C ATOM 2065 O GLN A1069 46.193 15.019 66.948 1.00 28.86 O ANISOU 2065 O GLN A1069 3162 1747 6057 299 1145 -662 O ATOM 2066 CB GLN A1069 48.570 17.457 67.304 1.00 25.95 C ANISOU 2066 CB GLN A1069 2586 1615 5657 352 1084 -540 C ATOM 2067 CG GLN A1069 49.759 17.965 66.495 1.00 39.52 C ANISOU 2067 CG GLN A1069 4255 3382 7379 318 1208 -624 C ATOM 2068 CD GLN A1069 50.750 18.762 67.304 1.00 62.43 C ANISOU 2068 CD GLN A1069 7023 6367 10331 382 1133 -502 C ATOM 2069 OE1 GLN A1069 50.916 18.594 68.526 1.00 56.70 O ANISOU 2069 OE1 GLN A1069 6194 5634 9715 475 1028 -356 O ATOM 2070 NE2 GLN A1069 51.458 19.638 66.617 1.00 55.72 N ANISOU 2070 NE2 GLN A1069 6172 5610 9390 311 1186 -557 N ATOM 2071 N ASP A1070 45.650 16.876 68.120 1.00 23.02 N ANISOU 2071 N ASP A1070 2410 1220 5114 301 860 -461 N ATOM 2072 CA ASP A1070 44.583 16.313 68.967 1.00 21.94 C ANISOU 2072 CA ASP A1070 2301 1050 4986 323 758 -387 C ATOM 2073 C ASP A1070 43.519 15.540 68.183 1.00 24.47 C ANISOU 2073 C ASP A1070 2748 1312 5238 240 811 -490 C ATOM 2074 O ASP A1070 43.022 14.557 68.702 1.00 23.88 O ANISOU 2074 O ASP A1070 2677 1147 5250 272 801 -464 O ATOM 2075 CB ASP A1070 43.937 17.405 69.842 1.00 22.18 C ANISOU 2075 CB ASP A1070 2331 1203 4893 310 587 -282 C ATOM 2076 CG ASP A1070 44.767 17.858 71.035 1.00 38.15 C ANISOU 2076 CG ASP A1070 4226 3280 6991 378 514 -161 C ATOM 2077 OD1 ASP A1070 44.522 18.983 71.537 1.00 39.82 O ANISOU 2077 OD1 ASP A1070 4434 3597 7099 346 418 -117 O ATOM 2078 OD2 ASP A1070 45.644 17.079 71.486 1.00 46.07 O ANISOU 2078 OD2 ASP A1070 5125 4215 8166 454 552 -105 O ATOM 2079 N VAL A1071 43.221 15.943 66.937 1.00 20.97 N ANISOU 2079 N VAL A1071 2404 925 4638 117 868 -599 N ATOM 2080 CA VAL A1071 42.249 15.283 66.051 1.00 21.85 C ANISOU 2080 CA VAL A1071 2641 1014 4649 -4 922 -704 C ATOM 2081 C VAL A1071 42.767 13.909 65.548 1.00 28.93 C ANISOU 2081 C VAL A1071 3540 1752 5698 -3 1122 -841 C ATOM 2082 O VAL A1071 42.012 12.922 65.525 1.00 27.99 O ANISOU 2082 O VAL A1071 3485 1549 5603 -37 1153 -886 O ATOM 2083 CB VAL A1071 41.830 16.203 64.876 1.00 25.39 C ANISOU 2083 CB VAL A1071 3182 1596 4871 -164 905 -751 C ATOM 2084 CG1 VAL A1071 40.780 15.532 63.996 1.00 25.68 C ANISOU 2084 CG1 VAL A1071 3342 1638 4779 -317 943 -842 C ATOM 2085 CG2 VAL A1071 41.310 17.527 65.400 1.00 23.90 C ANISOU 2085 CG2 VAL A1071 2974 1521 4588 -148 720 -614 C ATOM 2086 N ASP A1072 44.046 13.870 65.114 1.00 27.63 N ANISOU 2086 N ASP A1072 3307 1545 5646 28 1268 -918 N ATOM 2087 CA ASP A1072 44.711 12.650 64.672 1.00 29.98 C ANISOU 2087 CA ASP A1072 3576 1671 6144 47 1485 -1060 C ATOM 2088 C ASP A1072 44.742 11.739 65.908 1.00 34.34 C ANISOU 2088 C ASP A1072 4034 2070 6942 209 1436 -937 C ATOM 2089 O ASP A1072 44.213 10.622 65.859 1.00 34.69 O ANISOU 2089 O ASP A1072 4128 1977 7077 194 1506 -996 O ATOM 2090 CB ASP A1072 46.124 12.952 64.146 1.00 33.47 C ANISOU 2090 CB ASP A1072 3926 2112 6678 68 1633 -1142 C ATOM 2091 CG ASP A1072 46.202 13.951 62.992 1.00 56.03 C ANISOU 2091 CG ASP A1072 6866 5139 9283 -103 1665 -1236 C ATOM 2092 OD1 ASP A1072 45.292 13.938 62.119 1.00 58.94 O ANISOU 2092 OD1 ASP A1072 7378 5577 9440 -283 1675 -1323 O ATOM 2093 OD2 ASP A1072 47.186 14.732 62.946 1.00 65.73 O ANISOU 2093 OD2 ASP A1072 8014 6438 10522 -73 1675 -1213 O ATOM 2094 N ALA A1073 45.200 12.286 67.055 1.00 29.00 N ANISOU 2094 N ALA A1073 3238 1441 6339 334 1289 -751 N ATOM 2095 CA ALA A1073 45.208 11.578 68.327 1.00 28.17 C ANISOU 2095 CA ALA A1073 3037 1236 6429 459 1199 -589 C ATOM 2096 C ALA A1073 43.819 10.995 68.680 1.00 30.85 C ANISOU 2096 C ALA A1073 3484 1551 6687 407 1113 -562 C ATOM 2097 O ALA A1073 43.751 9.907 69.240 1.00 30.13 O ANISOU 2097 O ALA A1073 3355 1308 6787 469 1126 -505 O ATOM 2098 CB ALA A1073 45.681 12.506 69.423 1.00 27.63 C ANISOU 2098 CB ALA A1073 2858 1294 6346 531 1030 -402 C ATOM 2099 N ALA A1074 42.718 11.698 68.320 1.00 26.59 N ANISOU 2099 N ALA A1074 3069 1154 5881 289 1026 -596 N ATOM 2100 CA ALA A1074 41.347 11.252 68.608 1.00 25.20 C ANISOU 2100 CA ALA A1074 2987 981 5608 227 941 -575 C ATOM 2101 C ALA A1074 40.921 10.175 67.642 1.00 31.83 C ANISOU 2101 C ALA A1074 3931 1699 6464 134 1099 -740 C ATOM 2102 O ALA A1074 40.386 9.174 68.113 1.00 32.92 O ANISOU 2102 O ALA A1074 4088 1723 6697 147 1094 -713 O ATOM 2103 CB ALA A1074 40.361 12.417 68.593 1.00 23.66 C ANISOU 2103 CB ALA A1074 2856 974 5159 145 793 -539 C ATOM 2104 N VAL A1075 41.177 10.341 66.313 1.00 28.71 N ANISOU 2104 N VAL A1075 3604 1329 5975 24 1244 -914 N ATOM 2105 CA VAL A1075 40.845 9.302 65.329 1.00 30.09 C ANISOU 2105 CA VAL A1075 3883 1394 6154 -99 1425 -1104 C ATOM 2106 C VAL A1075 41.632 8.001 65.597 1.00 36.47 C ANISOU 2106 C VAL A1075 4615 1946 7295 11 1592 -1151 C ATOM 2107 O VAL A1075 41.004 6.944 65.657 1.00 37.87 O ANISOU 2107 O VAL A1075 4853 1991 7545 -24 1642 -1195 O ATOM 2108 CB VAL A1075 40.828 9.739 63.845 1.00 34.59 C ANISOU 2108 CB VAL A1075 4554 2077 6511 -291 1541 -1282 C ATOM 2109 CG1 VAL A1075 39.874 10.898 63.632 1.00 32.71 C ANISOU 2109 CG1 VAL A1075 4383 2065 5980 -399 1353 -1195 C ATOM 2110 CG2 VAL A1075 42.213 10.103 63.341 1.00 35.72 C ANISOU 2110 CG2 VAL A1075 4618 2208 6745 -256 1683 -1363 C ATOM 2111 N ARG A1076 42.965 8.092 65.882 1.00 32.73 N ANISOU 2111 N ARG A1076 3994 1398 7044 152 1655 -1113 N ATOM 2112 CA ARG A1076 43.804 6.939 66.250 1.00 34.47 C ANISOU 2112 CA ARG A1076 4098 1363 7638 287 1792 -1112 C ATOM 2113 C ARG A1076 43.145 6.181 67.411 1.00 39.06 C ANISOU 2113 C ARG A1076 4661 1842 8337 363 1654 -934 C ATOM 2114 O ARG A1076 42.897 4.985 67.303 1.00 40.59 O ANISOU 2114 O ARG A1076 4887 1831 8705 354 1771 -1004 O ATOM 2115 CB ARG A1076 45.235 7.371 66.652 1.00 35.35 C ANISOU 2115 CB ARG A1076 4021 1460 7949 441 1804 -1020 C ATOM 2116 CG ARG A1076 46.189 7.604 65.465 1.00 48.79 C ANISOU 2116 CG ARG A1076 5704 3161 9673 389 2031 -1233 C ATOM 2117 CD ARG A1076 47.381 8.505 65.790 1.00 53.14 C ANISOU 2117 CD ARG A1076 6099 3807 10284 494 1984 -1130 C ATOM 2118 NE ARG A1076 47.966 8.180 67.093 1.00 65.94 N ANISOU 2118 NE ARG A1076 7540 5335 12178 683 1866 -890 N ATOM 2119 CZ ARG A1076 48.407 9.080 67.967 1.00 85.50 C ANISOU 2119 CZ ARG A1076 9915 7962 14609 754 1679 -689 C ATOM 2120 NH1 ARG A1076 48.363 10.375 67.676 1.00 74.61 N ANISOU 2120 NH1 ARG A1076 8594 6807 12949 672 1601 -706 N ATOM 2121 NH2 ARG A1076 48.904 8.692 69.136 1.00 75.54 N ANISOU 2121 NH2 ARG A1076 8490 6628 13584 894 1568 -462 N ATOM 2122 N GLY A1077 42.789 6.903 68.462 1.00 34.36 N ANISOU 2122 N GLY A1077 4030 1400 7626 408 1414 -723 N ATOM 2123 CA GLY A1077 42.119 6.340 69.626 1.00 33.84 C ANISOU 2123 CA GLY A1077 3949 1289 7619 448 1260 -542 C ATOM 2124 C GLY A1077 40.756 5.743 69.332 1.00 35.77 C ANISOU 2124 C GLY A1077 4353 1516 7721 318 1261 -627 C ATOM 2125 O GLY A1077 40.379 4.762 69.978 1.00 36.90 O ANISOU 2125 O GLY A1077 4492 1520 8008 342 1233 -542 O ATOM 2126 N ILE A1078 40.002 6.330 68.366 1.00 28.91 N ANISOU 2126 N ILE A1078 3621 796 6569 167 1283 -778 N ATOM 2127 CA ILE A1078 38.675 5.844 67.990 1.00 27.74 C ANISOU 2127 CA ILE A1078 3619 663 6256 20 1279 -860 C ATOM 2128 C ILE A1078 38.865 4.483 67.369 1.00 35.67 C ANISOU 2128 C ILE A1078 4670 1423 7459 -16 1502 -1021 C ATOM 2129 O ILE A1078 38.180 3.539 67.770 1.00 36.34 O ANISOU 2129 O ILE A1078 4802 1392 7614 -40 1491 -993 O ATOM 2130 CB ILE A1078 37.906 6.826 67.051 1.00 28.76 C ANISOU 2130 CB ILE A1078 3859 1018 6050 -141 1240 -956 C ATOM 2131 CG1 ILE A1078 37.250 7.958 67.845 1.00 26.16 C ANISOU 2131 CG1 ILE A1078 3500 894 5546 -119 1005 -789 C ATOM 2132 CG2 ILE A1078 36.851 6.122 66.188 1.00 29.69 C ANISOU 2132 CG2 ILE A1078 4128 1124 6027 -330 1322 -1108 C ATOM 2133 CD1 ILE A1078 37.104 9.224 67.036 1.00 29.90 C ANISOU 2133 CD1 ILE A1078 4008 1563 5790 -205 964 -830 C ATOM 2134 N LEU A1079 39.813 4.376 66.405 1.00 33.12 N ANISOU 2134 N LEU A1079 4331 1016 7238 -26 1718 -1198 N ATOM 2135 CA LEU A1079 40.103 3.131 65.682 1.00 35.10 C ANISOU 2135 CA LEU A1079 4620 1018 7698 -73 1982 -1403 C ATOM 2136 C LEU A1079 40.679 2.014 66.582 1.00 40.51 C ANISOU 2136 C LEU A1079 5183 1412 8796 102 2022 -1287 C ATOM 2137 O LEU A1079 40.374 0.845 66.352 1.00 41.96 O ANISOU 2137 O LEU A1079 5426 1380 9138 54 2167 -1395 O ATOM 2138 CB LEU A1079 40.949 3.380 64.418 1.00 36.18 C ANISOU 2138 CB LEU A1079 4764 1160 7821 -152 2214 -1640 C ATOM 2139 CG LEU A1079 40.422 4.409 63.387 1.00 38.72 C ANISOU 2139 CG LEU A1079 5209 1763 7740 -359 2185 -1749 C ATOM 2140 CD1 LEU A1079 41.420 4.605 62.269 1.00 39.97 C ANISOU 2140 CD1 LEU A1079 5354 1921 7912 -434 2417 -1965 C ATOM 2141 CD2 LEU A1079 39.065 4.011 62.800 1.00 39.55 C ANISOU 2141 CD2 LEU A1079 5491 1939 7597 -585 2183 -1853 C ATOM 2142 N ARG A1080 41.429 2.375 67.650 1.00 36.38 N ANISOU 2142 N ARG A1080 4492 892 8439 289 1876 -1048 N ATOM 2143 CA ARG A1080 41.949 1.416 68.639 1.00 37.13 C ANISOU 2143 CA ARG A1080 4449 744 8916 451 1856 -866 C ATOM 2144 C ARG A1080 40.779 0.893 69.510 1.00 38.55 C ANISOU 2144 C ARG A1080 4702 922 9022 405 1682 -713 C ATOM 2145 O ARG A1080 40.998 0.085 70.422 1.00 37.13 O ANISOU 2145 O ARG A1080 4426 562 9119 508 1623 -524 O ATOM 2146 CB ARG A1080 42.999 2.073 69.573 1.00 35.20 C ANISOU 2146 CB ARG A1080 3992 593 8790 613 1708 -620 C ATOM 2147 CG ARG A1080 44.332 2.409 68.944 1.00 39.38 C ANISOU 2147 CG ARG A1080 4412 1054 9495 703 1875 -727 C ATOM 2148 CD ARG A1080 45.345 2.761 70.024 1.00 50.98 C ANISOU 2148 CD ARG A1080 5664 2547 11158 873 1723 -452 C ATOM 2149 NE ARG A1080 46.293 3.800 69.594 1.00 65.01 N ANISOU 2149 NE ARG A1080 7362 4473 12864 901 1762 -507 N ATOM 2150 CZ ARG A1080 47.417 3.580 68.911 1.00 82.53 C ANISOU 2150 CZ ARG A1080 9470 6557 15332 971 1981 -638 C ATOM 2151 NH1 ARG A1080 47.758 2.347 68.554 1.00 72.74 N ANISOU 2151 NH1 ARG A1080 8176 5007 14454 1028 2198 -741 N ATOM 2152 NH2 ARG A1080 48.201 4.591 68.571 1.00 68.63 N ANISOU 2152 NH2 ARG A1080 7647 4961 13470 978 1995 -676 N ATOM 2153 N ASN A1081 39.554 1.406 69.260 1.00 35.06 N ANISOU 2153 N ASN A1081 4417 695 8210 247 1586 -774 N ATOM 2154 CA ASN A1081 38.359 1.053 70.026 1.00 35.12 C ANISOU 2154 CA ASN A1081 4497 747 8099 181 1421 -651 C ATOM 2155 C ASN A1081 37.454 0.090 69.293 1.00 42.81 C ANISOU 2155 C ASN A1081 5631 1602 9034 28 1561 -838 C ATOM 2156 O ASN A1081 37.094 0.317 68.129 1.00 43.22 O ANISOU 2156 O ASN A1081 5802 1734 8884 -119 1686 -1066 O ATOM 2157 CB ASN A1081 37.593 2.289 70.482 1.00 30.11 C ANISOU 2157 CB ASN A1081 3887 440 7113 126 1196 -551 C ATOM 2158 CG ASN A1081 36.848 2.070 71.757 1.00 55.84 C ANISOU 2158 CG ASN A1081 7133 3740 10343 126 994 -340 C ATOM 2159 OD1 ASN A1081 35.695 1.627 71.760 1.00 48.12 O ANISOU 2159 OD1 ASN A1081 6266 2783 9234 8 962 -373 O ATOM 2160 ND2 ASN A1081 37.498 2.383 72.868 1.00 51.41 N ANISOU 2160 ND2 ASN A1081 6430 3216 9889 239 854 -118 N ATOM 2161 N ALA A1082 37.087 -0.992 70.000 1.00 41.31 N ANISOU 2161 N ALA A1082 5442 1225 9028 44 1533 -730 N ATOM 2162 CA ALA A1082 36.249 -2.072 69.489 1.00 43.16 C ANISOU 2162 CA ALA A1082 5821 1308 9272 -97 1662 -883 C ATOM 2163 C ALA A1082 34.813 -1.661 69.188 1.00 46.28 C ANISOU 2163 C ALA A1082 6371 1950 9265 -293 1562 -952 C ATOM 2164 O ALA A1082 34.297 -2.018 68.139 1.00 46.97 O ANISOU 2164 O ALA A1082 6593 2023 9232 -461 1716 -1180 O ATOM 2165 CB ALA A1082 36.275 -3.242 70.451 1.00 45.73 C ANISOU 2165 CB ALA A1082 6091 1376 9909 -20 1625 -703 C ATOM 2166 N LYS A1083 34.171 -0.920 70.089 1.00 42.05 N ANISOU 2166 N LYS A1083 5807 1643 8526 -285 1313 -761 N ATOM 2167 CA LYS A1083 32.797 -0.459 69.893 1.00 40.76 C ANISOU 2167 CA LYS A1083 5757 1719 8010 -452 1204 -801 C ATOM 2168 C LYS A1083 32.746 0.729 68.915 1.00 44.47 C ANISOU 2168 C LYS A1083 6259 2421 8217 -522 1214 -927 C ATOM 2169 O LYS A1083 31.709 0.966 68.277 1.00 44.41 O ANISOU 2169 O LYS A1083 6356 2574 7944 -692 1191 -1020 O ATOM 2170 CB LYS A1083 32.173 -0.053 71.242 1.00 41.40 C ANISOU 2170 CB LYS A1083 5778 1957 7995 -416 954 -564 C ATOM 2171 CG LYS A1083 31.746 -1.230 72.116 1.00 56.66 C ANISOU 2171 CG LYS A1083 7722 3725 10079 -432 911 -442 C ATOM 2172 CD LYS A1083 30.892 -0.798 73.309 1.00 62.82 C ANISOU 2172 CD LYS A1083 8469 4711 10688 -462 680 -253 C ATOM 2173 CE LYS A1083 29.406 -0.975 73.103 1.00 70.57 C ANISOU 2173 CE LYS A1083 9569 5819 11425 -642 639 -329 C ATOM 2174 NZ LYS A1083 28.667 -0.794 74.379 1.00 78.32 N ANISOU 2174 NZ LYS A1083 10506 6953 12301 -672 443 -148 N ATOM 2175 N LEU A1084 33.852 1.457 68.803 1.00 39.95 N ANISOU 2175 N LEU A1084 5591 1868 7722 -401 1238 -913 N ATOM 2176 CA LEU A1084 33.900 2.655 67.973 1.00 38.23 C ANISOU 2176 CA LEU A1084 5388 1865 7271 -458 1228 -996 C ATOM 2177 C LEU A1084 34.220 2.367 66.507 1.00 43.40 C ANISOU 2177 C LEU A1084 6134 2464 7892 -589 1458 -1247 C ATOM 2178 O LEU A1084 33.443 2.715 65.617 1.00 43.45 O ANISOU 2178 O LEU A1084 6244 2637 7630 -774 1459 -1354 O ATOM 2179 CB LEU A1084 34.912 3.654 68.540 1.00 37.09 C ANISOU 2179 CB LEU A1084 5105 1792 7197 -290 1142 -865 C ATOM 2180 CG LEU A1084 34.401 4.585 69.642 1.00 39.16 C ANISOU 2180 CG LEU A1084 5301 2248 7330 -238 903 -668 C ATOM 2181 CD1 LEU A1084 35.542 5.400 70.230 1.00 40.01 C ANISOU 2181 CD1 LEU A1084 5272 2392 7540 -85 847 -552 C ATOM 2182 CD2 LEU A1084 33.304 5.495 69.111 1.00 36.71 C ANISOU 2182 CD2 LEU A1084 5062 2172 6715 -369 811 -711 C ATOM 2183 N LYS A1085 35.366 1.742 66.259 1.00 40.30 N ANISOU 2183 N LYS A1085 5692 1847 7774 -505 1653 -1338 N ATOM 2184 CA LYS A1085 35.837 1.517 64.873 1.00 40.35 C ANISOU 2184 CA LYS A1085 5769 1802 7762 -636 1905 -1604 C ATOM 2185 C LYS A1085 34.696 1.234 63.839 1.00 40.99 C ANISOU 2185 C LYS A1085 6026 1991 7559 -916 1969 -1784 C ATOM 2186 O LYS A1085 34.628 1.983 62.864 1.00 38.50 O ANISOU 2186 O LYS A1085 5763 1871 6994 -1064 1991 -1885 O ATOM 2187 CB LYS A1085 37.011 0.511 64.795 1.00 45.12 C ANISOU 2187 CB LYS A1085 6300 2084 8760 -524 2148 -1709 C ATOM 2188 CG LYS A1085 37.757 0.499 63.457 1.00 60.90 C ANISOU 2188 CG LYS A1085 8332 4048 10757 -635 2420 -1988 C ATOM 2189 CD LYS A1085 39.113 -0.230 63.545 1.00 69.68 C ANISOU 2189 CD LYS A1085 9312 4855 12310 -466 2640 -2054 C ATOM 2190 CE LYS A1085 39.586 -0.818 62.229 1.00 80.23 C ANISOU 2190 CE LYS A1085 10712 6062 13709 -622 2989 -2401 C ATOM 2191 NZ LYS A1085 40.066 0.210 61.260 1.00 91.07 N ANISOU 2191 NZ LYS A1085 12098 7665 14838 -735 3049 -2531 N ATOM 2192 N PRO A1086 33.729 0.295 64.071 1.00 37.86 N ANISOU 2192 N PRO A1086 5716 1511 7156 -1009 1964 -1796 N ATOM 2193 CA PRO A1086 32.663 0.076 63.073 1.00 38.61 C ANISOU 2193 CA PRO A1086 5971 1739 6962 -1296 2016 -1959 C ATOM 2194 C PRO A1086 31.712 1.245 62.781 1.00 43.16 C ANISOU 2194 C PRO A1086 6576 2662 7162 -1421 1800 -1865 C ATOM 2195 O PRO A1086 31.207 1.336 61.649 1.00 44.29 O ANISOU 2195 O PRO A1086 6826 2953 7050 -1673 1864 -2009 O ATOM 2196 CB PRO A1086 31.912 -1.136 63.624 1.00 40.69 C ANISOU 2196 CB PRO A1086 6295 1827 7338 -1329 2029 -1948 C ATOM 2197 CG PRO A1086 32.171 -1.111 65.075 1.00 43.38 C ANISOU 2197 CG PRO A1086 6508 2077 7896 -1077 1859 -1693 C ATOM 2198 CD PRO A1086 33.601 -0.679 65.175 1.00 39.11 C ANISOU 2198 CD PRO A1086 5836 1449 7575 -883 1925 -1669 C ATOM 2199 N VAL A1087 31.446 2.131 63.781 1.00 37.38 N ANISOU 2199 N VAL A1087 5745 2060 6398 -1262 1549 -1623 N ATOM 2200 CA VAL A1087 30.534 3.263 63.566 1.00 35.30 C ANISOU 2200 CA VAL A1087 5485 2095 5834 -1356 1347 -1521 C ATOM 2201 C VAL A1087 31.208 4.336 62.742 1.00 40.04 C ANISOU 2201 C VAL A1087 6060 2836 6319 -1384 1363 -1554 C ATOM 2202 O VAL A1087 30.689 4.716 61.693 1.00 41.63 O ANISOU 2202 O VAL A1087 6334 3219 6266 -1602 1358 -1620 O ATOM 2203 CB VAL A1087 29.913 3.839 64.847 1.00 36.60 C ANISOU 2203 CB VAL A1087 5556 2349 6000 -1210 1103 -1289 C ATOM 2204 CG1 VAL A1087 28.741 4.749 64.491 1.00 35.35 C ANISOU 2204 CG1 VAL A1087 5408 2463 5559 -1343 928 -1215 C ATOM 2205 CG2 VAL A1087 29.464 2.724 65.785 1.00 36.78 C ANISOU 2205 CG2 VAL A1087 5593 2212 6171 -1168 1096 -1243 C ATOM 2206 N TYR A1088 32.376 4.802 63.213 1.00 34.81 N ANISOU 2206 N TYR A1088 5290 2095 5840 -1178 1377 -1498 N ATOM 2207 CA TYR A1088 33.207 5.796 62.552 1.00 33.49 C ANISOU 2207 CA TYR A1088 5087 2033 5605 -1178 1403 -1523 C ATOM 2208 C TYR A1088 33.342 5.448 61.057 1.00 38.86 C ANISOU 2208 C TYR A1088 5881 2747 6137 -1431 1605 -1755 C ATOM 2209 O TYR A1088 32.901 6.238 60.215 1.00 38.48 O ANISOU 2209 O TYR A1088 5877 2924 5821 -1609 1532 -1748 O ATOM 2210 CB TYR A1088 34.579 5.864 63.260 1.00 34.00 C ANISOU 2210 CB TYR A1088 5029 1938 5950 -935 1460 -1479 C ATOM 2211 CG TYR A1088 35.564 6.837 62.647 1.00 35.62 C ANISOU 2211 CG TYR A1088 5188 2234 6112 -923 1502 -1510 C ATOM 2212 CD1 TYR A1088 35.437 8.211 62.848 1.00 35.76 C ANISOU 2212 CD1 TYR A1088 5153 2447 5989 -881 1310 -1356 C ATOM 2213 CD2 TYR A1088 36.644 6.384 61.894 1.00 38.18 C ANISOU 2213 CD2 TYR A1088 5515 2438 6553 -952 1745 -1698 C ATOM 2214 CE1 TYR A1088 36.340 9.111 62.286 1.00 35.91 C ANISOU 2214 CE1 TYR A1088 5134 2546 5965 -881 1345 -1377 C ATOM 2215 CE2 TYR A1088 37.561 7.274 61.339 1.00 39.41 C ANISOU 2215 CE2 TYR A1088 5627 2688 6661 -953 1787 -1728 C ATOM 2216 CZ TYR A1088 37.400 8.639 61.532 1.00 46.17 C ANISOU 2216 CZ TYR A1088 6441 3745 7357 -922 1579 -1560 C ATOM 2217 OH TYR A1088 38.278 9.529 60.962 1.00 48.60 O ANISOU 2217 OH TYR A1088 6713 4147 7607 -939 1615 -1584 O ATOM 2218 N ASP A1089 33.848 4.213 60.747 1.00 35.92 N ANISOU 2218 N ASP A1089 5558 2151 5940 -1469 1857 -1958 N ATOM 2219 CA ASP A1089 34.055 3.683 59.391 1.00 36.59 C ANISOU 2219 CA ASP A1089 5754 2232 5918 -1726 2105 -2229 C ATOM 2220 C ASP A1089 32.827 3.827 58.512 1.00 39.91 C ANISOU 2220 C ASP A1089 6299 2890 5974 -2037 2033 -2263 C ATOM 2221 O ASP A1089 32.952 4.279 57.386 1.00 40.49 O ANISOU 2221 O ASP A1089 6430 3134 5822 -2260 2096 -2366 O ATOM 2222 CB ASP A1089 34.536 2.226 59.423 1.00 40.33 C ANISOU 2222 CB ASP A1089 6254 2390 6679 -1703 2375 -2427 C ATOM 2223 CG ASP A1089 35.967 2.005 59.890 1.00 49.65 C ANISOU 2223 CG ASP A1089 7303 3330 8229 -1453 2517 -2447 C ATOM 2224 OD1 ASP A1089 36.738 2.985 59.931 1.00 47.14 O ANISOU 2224 OD1 ASP A1089 6893 3112 7906 -1344 2455 -2366 O ATOM 2225 OD2 ASP A1089 36.325 0.833 60.190 1.00 61.51 O ANISOU 2225 OD2 ASP A1089 8790 4539 10042 -1372 2694 -2542 O ATOM 2226 N SER A1090 31.642 3.492 59.030 1.00 36.14 N ANISOU 2226 N SER A1090 5855 2445 5431 -2064 1887 -2158 N ATOM 2227 CA SER A1090 30.393 3.608 58.279 1.00 36.53 C ANISOU 2227 CA SER A1090 6003 2732 5147 -2356 1792 -2158 C ATOM 2228 C SER A1090 30.034 5.071 57.968 1.00 40.14 C ANISOU 2228 C SER A1090 6406 3480 5365 -2400 1557 -1968 C ATOM 2229 O SER A1090 29.375 5.340 56.959 1.00 40.92 O ANISOU 2229 O SER A1090 6575 3802 5169 -2687 1515 -1987 O ATOM 2230 CB SER A1090 29.251 2.970 59.067 1.00 38.30 C ANISOU 2230 CB SER A1090 6246 2917 5391 -2336 1675 -2065 C ATOM 2231 OG SER A1090 28.141 3.851 59.212 1.00 43.89 O ANISOU 2231 OG SER A1090 6916 3877 5881 -2383 1403 -1857 O ATOM 2232 N LEU A1091 30.417 5.998 58.882 1.00 34.46 N ANISOU 2232 N LEU A1091 5556 2756 4780 -2125 1394 -1770 N ATOM 2233 CA LEU A1091 30.067 7.419 58.838 1.00 32.49 C ANISOU 2233 CA LEU A1091 5233 2732 4380 -2108 1160 -1563 C ATOM 2234 C LEU A1091 30.807 8.227 57.819 1.00 39.36 C ANISOU 2234 C LEU A1091 6111 3728 5116 -2226 1205 -1602 C ATOM 2235 O LEU A1091 32.020 8.068 57.651 1.00 39.57 O ANISOU 2235 O LEU A1091 6132 3633 5271 -2160 1388 -1735 O ATOM 2236 CB LEU A1091 30.173 8.097 60.229 1.00 29.36 C ANISOU 2236 CB LEU A1091 4701 2277 4177 -1792 989 -1360 C ATOM 2237 CG LEU A1091 29.204 7.632 61.293 1.00 31.67 C ANISOU 2237 CG LEU A1091 4967 2523 4543 -1699 873 -1262 C ATOM 2238 CD1 LEU A1091 29.589 8.159 62.623 1.00 28.90 C ANISOU 2238 CD1 LEU A1091 4494 2098 4390 -1417 767 -1117 C ATOM 2239 CD2 LEU A1091 27.784 8.016 60.963 1.00 34.44 C ANISOU 2239 CD2 LEU A1091 5327 3085 4673 -1867 698 -1157 C ATOM 2240 N ASP A1092 30.070 9.160 57.193 1.00 37.29 N ANISOU 2240 N ASP A1092 5844 3714 4612 -2391 1023 -1460 N ATOM 2241 CA ASP A1092 30.582 10.124 56.225 1.00 38.21 C ANISOU 2241 CA ASP A1092 5960 3996 4563 -2530 1004 -1432 C ATOM 2242 C ASP A1092 31.464 11.209 56.881 1.00 40.39 C ANISOU 2242 C ASP A1092 6119 4223 5006 -2261 924 -1303 C ATOM 2243 O ASP A1092 31.576 11.280 58.109 1.00 38.75 O ANISOU 2243 O ASP A1092 5825 3879 5020 -1980 863 -1219 O ATOM 2244 CB ASP A1092 29.404 10.788 55.504 1.00 41.17 C ANISOU 2244 CB ASP A1092 6342 4638 4663 -2770 791 -1262 C ATOM 2245 CG ASP A1092 28.419 11.478 56.421 1.00 52.02 C ANISOU 2245 CG ASP A1092 7601 6052 6114 -2592 529 -1008 C ATOM 2246 OD1 ASP A1092 27.344 10.899 56.674 1.00 52.56 O ANISOU 2246 OD1 ASP A1092 7683 6143 6144 -2649 466 -983 O ATOM 2247 OD2 ASP A1092 28.705 12.620 56.846 1.00 56.13 O ANISOU 2247 OD2 ASP A1092 8016 6584 6728 -2414 394 -843 O ATOM 2248 N ALA A1093 32.029 12.088 56.041 1.00 36.74 N ANISOU 2248 N ALA A1093 5656 3894 4411 -2378 914 -1277 N ATOM 2249 CA ALA A1093 32.871 13.240 56.378 1.00 34.28 C ANISOU 2249 CA ALA A1093 5249 3576 4199 -2196 841 -1159 C ATOM 2250 C ALA A1093 32.350 14.087 57.542 1.00 34.61 C ANISOU 2250 C ALA A1093 5172 3595 4382 -1944 615 -928 C ATOM 2251 O ALA A1093 33.062 14.230 58.539 1.00 33.27 O ANISOU 2251 O ALA A1093 4927 3282 4430 -1685 638 -918 O ATOM 2252 CB ALA A1093 33.018 14.120 55.153 1.00 36.36 C ANISOU 2252 CB ALA A1093 5543 4051 4221 -2444 791 -1105 C ATOM 2253 N VAL A1094 31.141 14.625 57.420 1.00 30.06 N ANISOU 2253 N VAL A1094 4570 3160 3693 -2029 408 -751 N ATOM 2254 CA VAL A1094 30.576 15.479 58.461 1.00 27.82 C ANISOU 2254 CA VAL A1094 4164 2856 3549 -1811 212 -552 C ATOM 2255 C VAL A1094 30.154 14.693 59.701 1.00 30.17 C ANISOU 2255 C VAL A1094 4433 3014 4016 -1627 227 -586 C ATOM 2256 O VAL A1094 30.341 15.150 60.829 1.00 28.05 O ANISOU 2256 O VAL A1094 4073 2658 3927 -1393 170 -514 O ATOM 2257 CB VAL A1094 29.365 16.277 57.938 1.00 32.65 C ANISOU 2257 CB VAL A1094 4732 3650 4025 -1955 -9 -344 C ATOM 2258 CG1 VAL A1094 29.466 16.466 56.432 1.00 34.79 C ANISOU 2258 CG1 VAL A1094 5080 4099 4039 -2269 -4 -341 C ATOM 2259 CG2 VAL A1094 28.068 15.575 58.309 1.00 33.03 C ANISOU 2259 CG2 VAL A1094 4775 3717 4056 -1988 -78 -321 C ATOM 2260 N ARG A1095 29.580 13.514 59.486 1.00 27.18 N ANISOU 2260 N ARG A1095 4138 2623 3568 -1754 305 -696 N ATOM 2261 CA ARG A1095 29.083 12.686 60.580 1.00 25.56 C ANISOU 2261 CA ARG A1095 3917 2296 3499 -1619 312 -719 C ATOM 2262 C ARG A1095 30.211 12.157 61.443 1.00 28.68 C ANISOU 2262 C ARG A1095 4297 2489 4111 -1410 453 -815 C ATOM 2263 O ARG A1095 30.002 11.982 62.641 1.00 27.78 O ANISOU 2263 O ARG A1095 4122 2289 4145 -1236 402 -758 O ATOM 2264 CB ARG A1095 28.129 11.597 60.089 1.00 25.67 C ANISOU 2264 CB ARG A1095 4025 2352 3376 -1829 351 -802 C ATOM 2265 CG ARG A1095 26.743 12.145 59.723 1.00 27.78 C ANISOU 2265 CG ARG A1095 4253 2816 3485 -1972 149 -640 C ATOM 2266 CD ARG A1095 25.746 11.035 59.486 1.00 27.30 C ANISOU 2266 CD ARG A1095 4272 2792 3309 -2156 176 -712 C ATOM 2267 NE ARG A1095 24.387 11.536 59.293 1.00 32.10 N ANISOU 2267 NE ARG A1095 4812 3585 3799 -2267 -30 -537 N ATOM 2268 CZ ARG A1095 23.803 11.676 58.107 1.00 44.73 C ANISOU 2268 CZ ARG A1095 6448 5385 5164 -2551 -97 -487 C ATOM 2269 NH1 ARG A1095 24.457 11.361 56.997 1.00 31.60 N ANISOU 2269 NH1 ARG A1095 4901 3770 3334 -2772 38 -619 N ATOM 2270 NH2 ARG A1095 22.562 12.144 58.022 1.00 31.23 N ANISOU 2270 NH2 ARG A1095 4647 3834 3384 -2629 -299 -300 N ATOM 2271 N ARG A1096 31.426 11.986 60.865 1.00 24.99 N ANISOU 2271 N ARG A1096 3868 1959 3668 -1430 621 -943 N ATOM 2272 CA ARG A1096 32.630 11.576 61.611 1.00 23.52 C ANISOU 2272 CA ARG A1096 3640 1586 3712 -1228 749 -1011 C ATOM 2273 C ARG A1096 33.031 12.708 62.556 1.00 25.80 C ANISOU 2273 C ARG A1096 3808 1885 4110 -1018 617 -856 C ATOM 2274 O ARG A1096 33.391 12.437 63.706 1.00 25.18 O ANISOU 2274 O ARG A1096 3665 1690 4214 -831 615 -821 O ATOM 2275 CB ARG A1096 33.797 11.252 60.672 1.00 22.42 C ANISOU 2275 CB ARG A1096 3550 1396 3573 -1313 962 -1187 C ATOM 2276 CG ARG A1096 33.688 9.891 60.010 1.00 34.11 C ANISOU 2276 CG ARG A1096 5139 2789 5032 -1477 1161 -1392 C ATOM 2277 CD ARG A1096 34.655 9.772 58.853 1.00 47.65 C ANISOU 2277 CD ARG A1096 6906 4509 6689 -1627 1371 -1581 C ATOM 2278 NE ARG A1096 35.433 8.534 58.921 1.00 57.22 N ANISOU 2278 NE ARG A1096 8133 5489 8118 -1576 1623 -1780 N ATOM 2279 CZ ARG A1096 35.409 7.583 57.993 1.00 74.82 C ANISOU 2279 CZ ARG A1096 10468 7674 10287 -1792 1841 -2011 C ATOM 2280 NH1 ARG A1096 34.655 7.722 56.908 1.00 63.69 N ANISOU 2280 NH1 ARG A1096 9166 6463 8569 -2098 1827 -2068 N ATOM 2281 NH2 ARG A1096 36.148 6.490 58.137 1.00 63.19 N ANISOU 2281 NH2 ARG A1096 8987 5954 9069 -1714 2077 -2185 N ATOM 2282 N ALA A1097 32.921 13.985 62.074 1.00 21.14 N ANISOU 2282 N ALA A1097 3187 1439 3405 -1067 500 -754 N ATOM 2283 CA ALA A1097 33.242 15.193 62.840 1.00 18.57 C ANISOU 2283 CA ALA A1097 2756 1131 3170 -900 381 -618 C ATOM 2284 C ALA A1097 32.389 15.243 64.100 1.00 22.25 C ANISOU 2284 C ALA A1097 3152 1574 3727 -772 258 -519 C ATOM 2285 O ALA A1097 32.970 15.347 65.197 1.00 21.91 O ANISOU 2285 O ALA A1097 3039 1452 3835 -600 260 -493 O ATOM 2286 CB ALA A1097 33.033 16.435 62.001 1.00 18.95 C ANISOU 2286 CB ALA A1097 2794 1324 3083 -1007 273 -518 C ATOM 2287 N ALA A1098 31.033 15.048 63.957 1.00 16.78 N ANISOU 2287 N ALA A1098 2479 957 2941 -873 165 -475 N ATOM 2288 CA ALA A1098 30.091 14.966 65.076 1.00 15.22 C ANISOU 2288 CA ALA A1098 2215 764 2804 -775 68 -401 C ATOM 2289 C ALA A1098 30.513 13.894 66.079 1.00 21.29 C ANISOU 2289 C ALA A1098 2995 1383 3712 -678 153 -467 C ATOM 2290 O ALA A1098 30.393 14.128 67.281 1.00 20.81 O ANISOU 2290 O ALA A1098 2856 1300 3749 -554 91 -404 O ATOM 2291 CB ALA A1098 28.706 14.668 64.577 1.00 16.42 C ANISOU 2291 CB ALA A1098 2402 1000 2838 -938 -12 -375 C ATOM 2292 N LEU A1099 31.046 12.736 65.604 1.00 19.58 N ANISOU 2292 N LEU A1099 2864 1069 3507 -734 302 -589 N ATOM 2293 CA LEU A1099 31.539 11.687 66.505 1.00 18.81 C ANISOU 2293 CA LEU A1099 2761 817 3570 -629 382 -623 C ATOM 2294 C LEU A1099 32.861 12.104 67.176 1.00 21.97 C ANISOU 2294 C LEU A1099 3077 1147 4123 -462 411 -589 C ATOM 2295 O LEU A1099 32.958 11.990 68.393 1.00 21.26 O ANISOU 2295 O LEU A1099 2919 1015 4143 -348 359 -512 O ATOM 2296 CB LEU A1099 31.666 10.331 65.803 1.00 19.95 C ANISOU 2296 CB LEU A1099 3009 850 3721 -735 543 -766 C ATOM 2297 CG LEU A1099 31.923 9.154 66.736 1.00 24.39 C ANISOU 2297 CG LEU A1099 3562 1236 4468 -639 604 -772 C ATOM 2298 CD1 LEU A1099 30.655 8.397 66.996 1.00 25.27 C ANISOU 2298 CD1 LEU A1099 3728 1357 4516 -732 555 -766 C ATOM 2299 CD2 LEU A1099 33.028 8.265 66.213 1.00 26.85 C ANISOU 2299 CD2 LEU A1099 3907 1373 4922 -629 807 -903 C ATOM 2300 N ILE A1100 33.844 12.623 66.409 1.00 19.15 N ANISOU 2300 N ILE A1100 2720 799 3759 -466 485 -636 N ATOM 2301 CA ILE A1100 35.115 13.150 66.961 1.00 19.32 C ANISOU 2301 CA ILE A1100 2652 779 3909 -323 506 -597 C ATOM 2302 C ILE A1100 34.807 14.202 68.081 1.00 24.11 C ANISOU 2302 C ILE A1100 3167 1467 4525 -229 349 -463 C ATOM 2303 O ILE A1100 35.378 14.155 69.182 1.00 22.44 O ANISOU 2303 O ILE A1100 2879 1213 4434 -115 330 -402 O ATOM 2304 CB ILE A1100 35.988 13.759 65.822 1.00 22.24 C ANISOU 2304 CB ILE A1100 3042 1189 4219 -381 591 -667 C ATOM 2305 CG1 ILE A1100 36.597 12.638 64.940 1.00 23.51 C ANISOU 2305 CG1 ILE A1100 3268 1241 4423 -454 792 -830 C ATOM 2306 CG2 ILE A1100 37.085 14.712 66.369 1.00 20.13 C ANISOU 2306 CG2 ILE A1100 2675 936 4037 -253 565 -599 C ATOM 2307 CD1 ILE A1100 36.614 12.929 63.477 1.00 26.15 C ANISOU 2307 CD1 ILE A1100 3685 1669 4580 -640 867 -933 C ATOM 2308 N ASN A1101 33.858 15.122 67.777 1.00 20.66 N ANISOU 2308 N ASN A1101 2735 1149 3965 -295 242 -419 N ATOM 2309 CA ASN A1101 33.372 16.150 68.683 1.00 19.19 C ANISOU 2309 CA ASN A1101 2466 1032 3792 -232 118 -324 C ATOM 2310 C ASN A1101 32.942 15.523 70.045 1.00 23.44 C ANISOU 2310 C ASN A1101 2964 1540 4404 -174 81 -289 C ATOM 2311 O ASN A1101 33.306 16.045 71.102 1.00 24.36 O ANISOU 2311 O ASN A1101 3002 1672 4584 -96 41 -238 O ATOM 2312 CB ASN A1101 32.209 16.878 68.010 1.00 15.69 C ANISOU 2312 CB ASN A1101 2033 688 3239 -325 24 -286 C ATOM 2313 CG ASN A1101 31.838 18.194 68.625 1.00 20.91 C ANISOU 2313 CG ASN A1101 2600 1403 3940 -266 -78 -205 C ATOM 2314 OD1 ASN A1101 31.636 18.321 69.844 1.00 7.01 O ANISOU 2314 OD1 ASN A1101 411 387 1865 2 -93 -98 O ATOM 2315 ND2 ASN A1101 31.660 19.192 67.769 1.00 20.08 N ANISOU 2315 ND2 ASN A1101 2487 1354 3790 -316 -131 -156 N ATOM 2316 N MET A1102 32.189 14.401 70.013 1.00 17.51 N ANISOU 2316 N MET A1102 2270 753 3629 -234 96 -318 N ATOM 2317 CA MET A1102 31.729 13.730 71.224 1.00 15.63 C ANISOU 2317 CA MET A1102 2004 493 3443 -207 58 -277 C ATOM 2318 C MET A1102 32.944 13.198 71.932 1.00 19.04 C ANISOU 2318 C MET A1102 2397 831 4007 -117 108 -247 C ATOM 2319 O MET A1102 33.123 13.501 73.105 1.00 18.52 O ANISOU 2319 O MET A1102 2255 800 3982 -68 49 -174 O ATOM 2320 CB MET A1102 30.722 12.606 70.917 1.00 18.09 C ANISOU 2320 CB MET A1102 2393 777 3701 -305 71 -316 C ATOM 2321 CG MET A1102 29.374 13.120 70.439 1.00 21.20 C ANISOU 2321 CG MET A1102 2795 1288 3971 -398 -9 -312 C ATOM 2322 SD MET A1102 28.127 11.853 70.075 1.00 26.04 S ANISOU 2322 SD MET A1102 3497 1898 4499 -539 -2 -356 S ATOM 2323 CE MET A1102 27.733 11.262 71.689 1.00 21.91 C ANISOU 2323 CE MET A1102 2926 1353 4048 -493 -48 -301 C ATOM 2324 N VAL A1103 33.828 12.485 71.211 1.00 16.74 N ANISOU 2324 N VAL A1103 2145 427 3787 -104 222 -302 N ATOM 2325 CA VAL A1103 35.086 11.940 71.758 1.00 17.85 C ANISOU 2325 CA VAL A1103 2227 460 4094 -7 278 -261 C ATOM 2326 C VAL A1103 35.918 13.033 72.495 1.00 20.38 C ANISOU 2326 C VAL A1103 2444 859 4441 71 218 -182 C ATOM 2327 O VAL A1103 36.395 12.805 73.611 1.00 19.00 O ANISOU 2327 O VAL A1103 2191 674 4354 122 174 -82 O ATOM 2328 CB VAL A1103 35.877 11.220 70.639 1.00 23.85 C ANISOU 2328 CB VAL A1103 3036 1091 4935 -11 436 -367 C ATOM 2329 CG1 VAL A1103 37.269 10.810 71.104 1.00 24.35 C ANISOU 2329 CG1 VAL A1103 3006 1040 5205 106 498 -317 C ATOM 2330 CG2 VAL A1103 35.095 10.013 70.116 1.00 24.90 C ANISOU 2330 CG2 VAL A1103 3269 1132 5059 -101 506 -449 C ATOM 2331 N PHE A1104 36.014 14.245 71.873 1.00 15.83 N ANISOU 2331 N PHE A1104 1856 397 3763 56 209 -215 N ATOM 2332 CA PHE A1104 36.662 15.441 72.413 1.00 13.69 C ANISOU 2332 CA PHE A1104 1410 395 3398 78 159 -150 C ATOM 2333 C PHE A1104 36.032 15.902 73.748 1.00 16.28 C ANISOU 2333 C PHE A1104 1785 596 3803 98 55 -98 C ATOM 2334 O PHE A1104 36.763 16.393 74.597 1.00 17.79 O ANISOU 2334 O PHE A1104 1898 831 4030 130 28 -41 O ATOM 2335 CB PHE A1104 36.591 16.556 71.382 1.00 14.06 C ANISOU 2335 CB PHE A1104 1539 398 3405 58 165 -205 C ATOM 2336 CG PHE A1104 37.854 16.826 70.596 1.00 15.50 C ANISOU 2336 CG PHE A1104 1770 445 3674 92 253 -254 C ATOM 2337 CD1 PHE A1104 38.613 17.963 70.839 1.00 18.34 C ANISOU 2337 CD1 PHE A1104 2068 862 4037 126 229 -220 C ATOM 2338 CD2 PHE A1104 38.259 15.972 69.586 1.00 18.59 C ANISOU 2338 CD2 PHE A1104 2218 757 4088 62 371 -338 C ATOM 2339 CE1 PHE A1104 39.766 18.216 70.111 1.00 19.82 C ANISOU 2339 CE1 PHE A1104 2246 1038 4249 137 311 -256 C ATOM 2340 CE2 PHE A1104 39.422 16.221 68.863 1.00 22.02 C ANISOU 2340 CE2 PHE A1104 2638 1176 4551 72 467 -388 C ATOM 2341 CZ PHE A1104 40.164 17.340 69.126 1.00 19.98 C ANISOU 2341 CZ PHE A1104 2314 984 4292 111 431 -340 C ATOM 2342 N GLN A1105 34.705 15.719 73.953 1.00 11.90 N ANISOU 2342 N GLN A1105 1110 384 3029 24 4 -93 N ATOM 2343 CA GLN A1105 34.008 16.098 75.189 1.00 10.64 C ANISOU 2343 CA GLN A1105 860 381 2801 5 -72 -59 C ATOM 2344 C GLN A1105 33.925 15.001 76.264 1.00 16.90 C ANISOU 2344 C GLN A1105 1824 782 3815 -12 -101 -3 C ATOM 2345 O GLN A1105 34.079 15.306 77.431 1.00 17.35 O ANISOU 2345 O GLN A1105 1812 917 3862 -36 -148 50 O ATOM 2346 CB GLN A1105 32.607 16.610 74.861 1.00 10.58 C ANISOU 2346 CB GLN A1105 895 385 2741 -20 -109 -98 C ATOM 2347 CG GLN A1105 31.766 17.075 76.062 1.00 9.71 C ANISOU 2347 CG GLN A1105 710 387 2591 -27 -160 -90 C ATOM 2348 CD GLN A1105 30.306 17.241 75.729 1.00 21.94 C ANISOU 2348 CD GLN A1105 2440 1617 4278 -132 -193 -154 C ATOM 2349 OE1 GLN A1105 29.820 16.809 74.681 1.00 23.37 O ANISOU 2349 OE1 GLN A1105 2684 1768 4429 -154 -191 -165 O ATOM 2350 NE2 GLN A1105 29.556 17.830 76.642 1.00 14.41 N ANISOU 2350 NE2 GLN A1105 1415 738 3322 -165 -216 -177 N ATOM 2351 N MET A1106 33.659 13.752 75.893 1.00 15.95 N ANISOU 2351 N MET A1106 1766 568 3728 -24 -73 -2 N ATOM 2352 CA MET A1106 33.494 12.674 76.867 1.00 17.35 C ANISOU 2352 CA MET A1106 1931 717 3946 -55 -110 82 C ATOM 2353 C MET A1106 34.584 11.593 76.878 1.00 23.61 C ANISOU 2353 C MET A1106 2708 1368 4893 5 -68 158 C ATOM 2354 O MET A1106 34.720 10.887 77.875 1.00 24.97 O ANISOU 2354 O MET A1106 2838 1527 5122 -14 -123 276 O ATOM 2355 CB MET A1106 32.141 12.010 76.652 1.00 20.74 C ANISOU 2355 CB MET A1106 2432 1140 4307 -132 -120 38 C ATOM 2356 CG MET A1106 30.986 12.925 76.884 1.00 25.00 C ANISOU 2356 CG MET A1106 2953 1814 4731 -191 -170 -12 C ATOM 2357 SD MET A1106 29.511 12.164 76.198 1.00 31.29 S ANISOU 2357 SD MET A1106 3836 2599 5455 -275 -169 -71 S ATOM 2358 CE MET A1106 29.552 12.806 74.537 1.00 28.26 C ANISOU 2358 CE MET A1106 3502 2198 5039 -257 -122 -152 C ATOM 2359 N GLY A1107 35.294 11.423 75.766 1.00 21.09 N ANISOU 2359 N GLY A1107 2419 941 4652 66 30 93 N ATOM 2360 CA GLY A1107 36.348 10.418 75.637 1.00 22.19 C ANISOU 2360 CA GLY A1107 2529 918 4984 137 99 142 C ATOM 2361 C GLY A1107 35.894 9.150 74.943 1.00 26.79 C ANISOU 2361 C GLY A1107 3201 1340 5637 113 186 76 C ATOM 2362 O GLY A1107 34.698 8.857 74.949 1.00 25.54 O ANISOU 2362 O GLY A1107 3117 1214 5371 28 155 41 O ATOM 2363 N GLU A1108 36.850 8.389 74.338 1.00 25.36 N ANISOU 2363 N GLU A1108 3008 983 5646 181 309 47 N ATOM 2364 CA GLU A1108 36.628 7.088 73.685 1.00 27.66 C ANISOU 2364 CA GLU A1108 3376 1081 6054 160 428 -33 C ATOM 2365 C GLU A1108 35.678 6.203 74.513 1.00 33.48 C ANISOU 2365 C GLU A1108 4144 1785 6790 99 346 57 C ATOM 2366 O GLU A1108 34.652 5.765 73.998 1.00 34.01 O ANISOU 2366 O GLU A1108 4323 1839 6759 4 379 -43 O ATOM 2367 CB GLU A1108 37.961 6.325 73.523 1.00 31.23 C ANISOU 2367 CB GLU A1108 3745 1327 6795 271 545 -9 C ATOM 2368 CG GLU A1108 38.746 6.657 72.268 1.00 47.02 C ANISOU 2368 CG GLU A1108 5756 3284 8824 295 709 -176 C ATOM 2369 CD GLU A1108 39.444 8.006 72.232 1.00 73.80 C ANISOU 2369 CD GLU A1108 9080 6839 12122 333 664 -160 C ATOM 2370 OE1 GLU A1108 39.731 8.576 73.314 1.00 55.51 O ANISOU 2370 OE1 GLU A1108 6667 4628 9797 377 525 2 O ATOM 2371 OE2 GLU A1108 39.726 8.482 71.107 1.00 78.22 O ANISOU 2371 OE2 GLU A1108 9686 7424 12609 302 774 -312 O ATOM 2372 N THR A1109 36.015 5.975 75.797 1.00 30.14 N ANISOU 2372 N THR A1109 3623 1369 6461 134 232 254 N ATOM 2373 CA THR A1109 35.246 5.146 76.729 1.00 30.50 C ANISOU 2373 CA THR A1109 3683 1395 6510 65 139 373 C ATOM 2374 C THR A1109 33.808 5.647 76.948 1.00 33.80 C ANISOU 2374 C THR A1109 4177 1999 6664 -59 57 318 C ATOM 2375 O THR A1109 32.872 4.839 76.916 1.00 36.56 O ANISOU 2375 O THR A1109 4609 2299 6984 -141 61 294 O ATOM 2376 CB THR A1109 36.024 4.948 78.034 1.00 36.98 C ANISOU 2376 CB THR A1109 4368 2221 7463 105 20 615 C ATOM 2377 OG1 THR A1109 37.319 4.433 77.728 1.00 44.28 O ANISOU 2377 OG1 THR A1109 5206 2954 8666 230 105 667 O ATOM 2378 CG2 THR A1109 35.335 4.013 78.981 1.00 30.99 C ANISOU 2378 CG2 THR A1109 3621 1433 6720 20 -78 761 C ATOM 2379 N GLY A1110 33.654 6.950 77.196 1.00 25.90 N ANISOU 2379 N GLY A1110 3140 1202 5497 -72 -10 300 N ATOM 2380 CA GLY A1110 32.357 7.579 77.424 1.00 22.67 C ANISOU 2380 CA GLY A1110 2770 969 4873 -172 -78 244 C ATOM 2381 C GLY A1110 31.456 7.486 76.216 1.00 23.00 C ANISOU 2381 C GLY A1110 2923 994 4825 -224 -6 86 C ATOM 2382 O GLY A1110 30.291 7.120 76.353 1.00 22.03 O ANISOU 2382 O GLY A1110 2851 915 4604 -320 -40 65 O ATOM 2383 N VAL A1111 32.008 7.787 75.020 1.00 18.36 N ANISOU 2383 N VAL A1111 2343 395 4236 -173 93 -21 N ATOM 2384 CA VAL A1111 31.302 7.734 73.741 1.00 17.78 C ANISOU 2384 CA VAL A1111 2329 413 4015 -231 165 -157 C ATOM 2385 C VAL A1111 30.886 6.311 73.435 1.00 25.06 C ANISOU 2385 C VAL A1111 3407 1049 5066 -322 237 -208 C ATOM 2386 O VAL A1111 29.709 6.113 73.133 1.00 25.99 O ANISOU 2386 O VAL A1111 3594 1230 5050 -435 217 -262 O ATOM 2387 CB VAL A1111 32.084 8.394 72.578 1.00 20.47 C ANISOU 2387 CB VAL A1111 2747 611 4420 -219 253 -261 C ATOM 2388 CG1 VAL A1111 31.272 8.394 71.285 1.00 20.02 C ANISOU 2388 CG1 VAL A1111 2793 595 4218 -340 304 -389 C ATOM 2389 CG2 VAL A1111 32.474 9.814 72.937 1.00 19.40 C ANISOU 2389 CG2 VAL A1111 2525 613 4235 -158 178 -212 C ATOM 2390 N ALA A1112 31.823 5.311 73.589 1.00 23.27 N ANISOU 2390 N ALA A1112 3166 618 5057 -254 318 -171 N ATOM 2391 CA ALA A1112 31.582 3.858 73.362 1.00 24.53 C ANISOU 2391 CA ALA A1112 3404 581 5334 -306 409 -209 C ATOM 2392 C ALA A1112 30.568 3.190 74.302 1.00 31.12 C ANISOU 2392 C ALA A1112 4262 1435 6129 -387 307 -112 C ATOM 2393 O ALA A1112 30.258 2.009 74.110 1.00 34.54 O ANISOU 2393 O ALA A1112 4769 1706 6647 -445 378 -144 O ATOM 2394 CB ALA A1112 32.839 3.034 73.622 1.00 26.58 C ANISOU 2394 CB ALA A1112 3599 609 5890 -190 489 -140 C ATOM 2395 N GLY A1113 30.011 3.971 75.236 1.00 26.59 N ANISOU 2395 N GLY A1113 3629 1060 5415 -406 158 -16 N ATOM 2396 CA GLY A1113 28.982 3.529 76.169 1.00 26.78 C ANISOU 2396 CA GLY A1113 3665 1153 5359 -504 57 67 C ATOM 2397 C GLY A1113 27.709 4.221 75.696 1.00 31.06 C ANISOU 2397 C GLY A1113 4249 1883 5671 -604 24 -41 C ATOM 2398 O GLY A1113 26.929 4.684 76.528 1.00 33.09 O ANISOU 2398 O GLY A1113 4460 2302 5811 -657 -80 11 O ATOM 2399 N PHE A1114 27.561 4.325 74.377 1.00 25.69 N ANISOU 2399 N PHE A1114 3642 1185 4936 -635 115 -183 N ATOM 2400 CA PHE A1114 26.379 4.873 73.723 1.00 24.39 C ANISOU 2400 CA PHE A1114 3514 1182 4573 -742 84 -268 C ATOM 2401 C PHE A1114 25.921 3.810 72.737 1.00 31.08 C ANISOU 2401 C PHE A1114 4488 1926 5397 -863 186 -380 C ATOM 2402 O PHE A1114 25.825 4.038 71.531 1.00 31.51 O ANISOU 2402 O PHE A1114 4599 2011 5364 -928 252 -493 O ATOM 2403 CB PHE A1114 26.716 6.171 72.991 1.00 24.97 C ANISOU 2403 CB PHE A1114 3546 1362 4580 -691 82 -314 C ATOM 2404 CG PHE A1114 26.402 7.411 73.780 1.00 24.58 C ANISOU 2404 CG PHE A1114 3387 1484 4471 -645 -32 -246 C ATOM 2405 CD1 PHE A1114 25.091 7.751 74.068 1.00 26.92 C ANISOU 2405 CD1 PHE A1114 3654 1927 4649 -726 -114 -242 C ATOM 2406 CD2 PHE A1114 27.418 8.235 74.233 1.00 25.50 C ANISOU 2406 CD2 PHE A1114 3421 1609 4659 -527 -46 -196 C ATOM 2407 CE1 PHE A1114 24.799 8.891 74.793 1.00 26.93 C ANISOU 2407 CE1 PHE A1114 3546 2064 4624 -686 -191 -204 C ATOM 2408 CE2 PHE A1114 27.133 9.376 74.958 1.00 27.47 C ANISOU 2408 CE2 PHE A1114 3575 2002 4862 -500 -129 -158 C ATOM 2409 CZ PHE A1114 25.822 9.704 75.238 1.00 25.30 C ANISOU 2409 CZ PHE A1114 3270 1855 4487 -577 -193 -169 C ATOM 2410 N THR A1115 25.656 2.637 73.294 1.00 29.03 N ANISOU 2410 N THR A1115 4272 1546 5212 -911 199 -343 N ATOM 2411 CA THR A1115 25.427 1.381 72.563 1.00 29.83 C ANISOU 2411 CA THR A1115 4498 1483 5352 -1020 322 -447 C ATOM 2412 C THR A1115 24.268 1.475 71.547 1.00 32.29 C ANISOU 2412 C THR A1115 4890 1934 5442 -1197 332 -568 C ATOM 2413 O THR A1115 24.509 1.298 70.344 1.00 32.34 O ANISOU 2413 O THR A1115 4976 1893 5419 -1268 454 -706 O ATOM 2414 CB THR A1115 25.267 0.223 73.529 1.00 38.49 C ANISOU 2414 CB THR A1115 5613 2439 6574 -1040 303 -350 C ATOM 2415 OG1 THR A1115 26.210 0.356 74.604 1.00 34.87 O ANISOU 2415 OG1 THR A1115 5049 1921 6279 -896 241 -190 O ATOM 2416 CG2 THR A1115 25.398 -1.118 72.832 1.00 41.14 C ANISOU 2416 CG2 THR A1115 6067 2531 7035 -1114 463 -457 C ATOM 2417 N ASN A1116 23.035 1.750 72.011 1.00 27.15 N ANISOU 2417 N ASN A1116 4213 1465 4638 -1281 209 -517 N ATOM 2418 CA ASN A1116 21.892 1.832 71.105 1.00 26.35 C ANISOU 2418 CA ASN A1116 4165 1512 4334 -1455 196 -600 C ATOM 2419 C ASN A1116 22.055 2.874 70.011 1.00 30.07 C ANISOU 2419 C ASN A1116 4617 2109 4701 -1463 199 -653 C ATOM 2420 O ASN A1116 22.026 2.500 68.835 1.00 31.60 O ANISOU 2420 O ASN A1116 4907 2285 4814 -1597 294 -770 O ATOM 2421 CB ASN A1116 20.561 1.946 71.839 1.00 22.47 C ANISOU 2421 CB ASN A1116 3623 1190 3724 -1534 67 -530 C ATOM 2422 CG ASN A1116 20.208 0.732 72.672 1.00 56.07 C ANISOU 2422 CG ASN A1116 7931 5335 8037 -1597 74 -493 C ATOM 2423 OD1 ASN A1116 20.724 -0.382 72.481 1.00 59.47 O ANISOU 2423 OD1 ASN A1116 8461 5547 8586 -1621 186 -537 O ATOM 2424 ND2 ASN A1116 19.305 0.917 73.622 1.00 47.13 N ANISOU 2424 ND2 ASN A1116 6730 4345 6834 -1632 -39 -414 N ATOM 2425 N SER A1117 22.298 4.155 70.377 1.00 23.57 N ANISOU 2425 N SER A1117 3673 1400 3881 -1335 104 -572 N ATOM 2426 CA SER A1117 22.478 5.244 69.409 1.00 22.16 C ANISOU 2426 CA SER A1117 3465 1338 3619 -1336 87 -590 C ATOM 2427 C SER A1117 23.550 4.923 68.352 1.00 27.01 C ANISOU 2427 C SER A1117 4168 1830 4266 -1356 236 -702 C ATOM 2428 O SER A1117 23.262 5.036 67.162 1.00 28.26 O ANISOU 2428 O SER A1117 4384 2072 4280 -1505 266 -773 O ATOM 2429 CB SER A1117 22.787 6.551 70.125 1.00 24.05 C ANISOU 2429 CB SER A1117 3566 1659 3912 -1175 -11 -492 C ATOM 2430 OG SER A1117 21.718 6.958 70.963 1.00 34.24 O ANISOU 2430 OG SER A1117 4765 3081 5164 -1181 -127 -419 O ATOM 2431 N LEU A1118 24.742 4.435 68.784 1.00 21.56 N ANISOU 2431 N LEU A1118 3478 959 3755 -1217 336 -713 N ATOM 2432 CA LEU A1118 25.862 4.060 67.918 1.00 21.61 C ANISOU 2432 CA LEU A1118 3504 922 3785 -1159 514 -801 C ATOM 2433 C LEU A1118 25.447 3.035 66.882 1.00 30.20 C ANISOU 2433 C LEU A1118 4781 1835 4856 -1432 637 -994 C ATOM 2434 O LEU A1118 25.955 3.048 65.750 1.00 30.24 O ANISOU 2434 O LEU A1118 4849 1831 4811 -1523 762 -1125 O ATOM 2435 CB LEU A1118 27.014 3.507 68.748 1.00 21.38 C ANISOU 2435 CB LEU A1118 3390 773 3962 -955 588 -745 C ATOM 2436 CG LEU A1118 27.872 4.526 69.475 1.00 22.11 C ANISOU 2436 CG LEU A1118 3450 699 4254 -860 493 -682 C ATOM 2437 CD1 LEU A1118 28.658 3.868 70.607 1.00 22.11 C ANISOU 2437 CD1 LEU A1118 3358 596 4448 -698 504 -573 C ATOM 2438 CD2 LEU A1118 28.813 5.246 68.509 1.00 23.53 C ANISOU 2438 CD2 LEU A1118 3628 884 4429 -838 574 -761 C ATOM 2439 N ARG A1119 24.510 2.135 67.271 1.00 31.11 N ANISOU 2439 N ARG A1119 4950 1924 4947 -1529 618 -992 N ATOM 2440 CA ARG A1119 23.963 1.113 66.374 1.00 33.27 C ANISOU 2440 CA ARG A1119 5362 2154 5126 -1755 742 -1145 C ATOM 2441 C ARG A1119 23.039 1.774 65.353 1.00 37.28 C ANISOU 2441 C ARG A1119 5892 2922 5350 -1957 668 -1168 C ATOM 2442 O ARG A1119 23.180 1.499 64.173 1.00 37.90 O ANISOU 2442 O ARG A1119 6067 3013 5321 -2136 794 -1316 O ATOM 2443 CB ARG A1119 23.230 0.036 67.161 1.00 33.08 C ANISOU 2443 CB ARG A1119 5379 2032 5157 -1800 727 -1116 C ATOM 2444 CG ARG A1119 23.244 -1.326 66.501 1.00 49.32 C ANISOU 2444 CG ARG A1119 7582 3898 7260 -1962 925 -1293 C ATOM 2445 CD ARG A1119 22.058 -2.186 66.937 1.00 67.82 C ANISOU 2445 CD ARG A1119 9985 6248 9536 -2102 877 -1272 C ATOM 2446 NE ARG A1119 21.681 -2.018 68.346 1.00 79.05 N ANISOU 2446 NE ARG A1119 11310 7703 11023 -1967 706 -1078 N ATOM 2447 CZ ARG A1119 22.342 -2.548 69.371 1.00 99.90 C ANISOU 2447 CZ ARG A1119 13913 10138 13904 -1810 715 -985 C ATOM 2448 NH1 ARG A1119 23.440 -3.266 69.163 1.00 91.76 N ANISOU 2448 NH1 ARG A1119 12919 8832 13113 -1736 884 -1057 N ATOM 2449 NH2 ARG A1119 21.926 -2.340 70.614 1.00 90.30 N ANISOU 2449 NH2 ARG A1119 12614 8998 12699 -1734 555 -813 N ATOM 2450 N MET A1120 22.161 2.667 65.796 1.00 33.09 N ANISOU 2450 N MET A1120 5262 2597 4712 -1933 471 -1021 N ATOM 2451 CA MET A1120 21.298 3.403 64.877 1.00 33.73 C ANISOU 2451 CA MET A1120 5329 2929 4558 -2104 371 -994 C ATOM 2452 C MET A1120 22.106 4.194 63.844 1.00 37.86 C ANISOU 2452 C MET A1120 5855 3510 5020 -2126 414 -1032 C ATOM 2453 O MET A1120 21.690 4.333 62.694 1.00 37.50 O ANISOU 2453 O MET A1120 5861 3618 4771 -2350 413 -1074 O ATOM 2454 CB MET A1120 20.372 4.343 65.651 1.00 34.93 C ANISOU 2454 CB MET A1120 5336 3254 4682 -2020 161 -819 C ATOM 2455 CG MET A1120 19.505 3.646 66.687 1.00 38.60 C ANISOU 2455 CG MET A1120 5788 3696 5181 -2019 112 -779 C ATOM 2456 SD MET A1120 18.608 4.805 67.738 1.00 40.96 S ANISOU 2456 SD MET A1120 5896 4172 5496 -1893 -92 -607 S ATOM 2457 CE MET A1120 18.462 3.851 69.246 1.00 36.73 C ANISOU 2457 CE MET A1120 5366 3506 5082 -1821 -77 -591 C ATOM 2458 N LEU A1121 23.259 4.711 64.262 1.00 35.03 N ANISOU 2458 N LEU A1121 5438 3044 4827 -1914 445 -1009 N ATOM 2459 CA LEU A1121 24.119 5.505 63.388 1.00 35.03 C ANISOU 2459 CA LEU A1121 5433 3092 4784 -1919 487 -1039 C ATOM 2460 C LEU A1121 24.695 4.584 62.341 1.00 41.02 C ANISOU 2460 C LEU A1121 6330 3754 5502 -2093 707 -1248 C ATOM 2461 O LEU A1121 24.466 4.831 61.163 1.00 42.43 O ANISOU 2461 O LEU A1121 6564 4086 5471 -2316 722 -1302 O ATOM 2462 CB LEU A1121 25.226 6.254 64.173 1.00 33.43 C ANISOU 2462 CB LEU A1121 5130 2799 4775 -1651 470 -965 C ATOM 2463 CG LEU A1121 24.775 7.367 65.136 1.00 36.23 C ANISOU 2463 CG LEU A1121 5342 3260 5165 -1493 275 -783 C ATOM 2464 CD1 LEU A1121 25.913 7.793 66.023 1.00 35.74 C ANISOU 2464 CD1 LEU A1121 5202 3081 5295 -1258 292 -740 C ATOM 2465 CD2 LEU A1121 24.237 8.575 64.392 1.00 38.26 C ANISOU 2465 CD2 LEU A1121 5541 3725 5270 -1574 144 -691 C ATOM 2466 N GLN A1122 25.365 3.476 62.773 1.00 37.92 N ANISOU 2466 N GLN A1122 5989 3106 5311 -2014 878 -1363 N ATOM 2467 CA GLN A1122 25.943 2.392 61.941 1.00 39.81 C ANISOU 2467 CA GLN A1122 6356 3184 5587 -2159 1133 -1596 C ATOM 2468 C GLN A1122 24.907 1.911 60.912 1.00 44.74 C ANISOU 2468 C GLN A1122 7100 3956 5944 -2495 1165 -1704 C ATOM 2469 O GLN A1122 25.219 1.848 59.726 1.00 45.82 O ANISOU 2469 O GLN A1122 7319 4150 5940 -2704 1303 -1862 O ATOM 2470 CB GLN A1122 26.339 1.222 62.846 1.00 41.61 C ANISOU 2470 CB GLN A1122 6596 3119 6096 -2017 1246 -1634 C ATOM 2471 CG GLN A1122 27.262 0.190 62.236 1.00 59.21 C ANISOU 2471 CG GLN A1122 8910 5101 8488 -2070 1533 -1864 C ATOM 2472 CD GLN A1122 27.920 -0.572 63.369 1.00 87.16 C ANISOU 2472 CD GLN A1122 12390 8346 12378 -1832 1583 -1806 C ATOM 2473 OE1 GLN A1122 28.995 -0.205 63.845 1.00 86.91 O ANISOU 2473 OE1 GLN A1122 12256 8215 12551 -1611 1592 -1739 O ATOM 2474 NE2 GLN A1122 27.241 -1.573 63.922 1.00 76.08 N ANISOU 2474 NE2 GLN A1122 11038 6821 11048 -1869 1583 -1792 N ATOM 2475 N GLN A1123 23.650 1.672 61.378 1.00 40.82 N ANISOU 2475 N GLN A1123 6602 3552 5356 -2560 1023 -1607 N ATOM 2476 CA GLN A1123 22.464 1.231 60.630 1.00 41.36 C ANISOU 2476 CA GLN A1123 6761 3787 5168 -2872 1003 -1661 C ATOM 2477 C GLN A1123 21.792 2.331 59.773 1.00 44.24 C ANISOU 2477 C GLN A1123 7081 4480 5250 -3046 831 -1549 C ATOM 2478 O GLN A1123 20.794 2.052 59.105 1.00 45.24 O ANISOU 2478 O GLN A1123 7264 4780 5143 -3324 791 -1567 O ATOM 2479 CB GLN A1123 21.440 0.613 61.596 1.00 42.09 C ANISOU 2479 CB GLN A1123 6842 3848 5301 -2844 905 -1577 C ATOM 2480 CG GLN A1123 21.820 -0.760 62.136 1.00 60.54 C ANISOU 2480 CG GLN A1123 9263 5880 7859 -2795 1087 -1703 C ATOM 2481 CD GLN A1123 20.614 -1.443 62.726 1.00 86.00 C ANISOU 2481 CD GLN A1123 12514 9131 11032 -2884 1001 -1648 C ATOM 2482 OE1 GLN A1123 19.582 -1.620 62.067 1.00 87.97 O ANISOU 2482 OE1 GLN A1123 12821 9564 11039 -3149 964 -1682 O ATOM 2483 NE2 GLN A1123 20.714 -1.859 63.975 1.00 74.64 N ANISOU 2483 NE2 GLN A1123 11029 7520 9810 -2685 966 -1556 N ATOM 2484 N LYS A1124 22.336 3.568 59.797 1.00 39.01 N ANISOU 2484 N LYS A1124 6310 3897 4613 -2892 725 -1422 N ATOM 2485 CA LYS A1124 21.887 4.745 59.026 1.00 38.06 C ANISOU 2485 CA LYS A1124 6124 4055 4280 -3017 552 -1279 C ATOM 2486 C LYS A1124 20.431 5.182 59.280 1.00 41.23 C ANISOU 2486 C LYS A1124 6433 4665 4568 -3075 312 -1082 C ATOM 2487 O LYS A1124 19.715 5.617 58.378 1.00 41.33 O ANISOU 2487 O LYS A1124 6432 4918 4352 -3310 198 -999 O ATOM 2488 CB LYS A1124 22.293 4.637 57.543 1.00 41.58 C ANISOU 2488 CB LYS A1124 6683 4608 4508 -3320 685 -1429 C ATOM 2489 CG LYS A1124 23.772 4.275 57.407 1.00 48.36 C ANISOU 2489 CG LYS A1124 7603 5245 5527 -3223 932 -1627 C ATOM 2490 CD LYS A1124 24.297 4.293 55.983 1.00 59.73 C ANISOU 2490 CD LYS A1124 9142 6796 6757 -3516 1081 -1790 C ATOM 2491 CE LYS A1124 25.790 4.058 55.954 1.00 72.53 C ANISOU 2491 CE LYS A1124 10786 8194 8578 -3379 1321 -1972 C ATOM 2492 NZ LYS A1124 26.545 5.092 56.728 1.00 79.32 N ANISOU 2492 NZ LYS A1124 11508 8998 9631 -3044 1206 -1805 N ATOM 2493 N ARG A1125 20.037 5.009 60.542 1.00 37.13 N ANISOU 2493 N ARG A1125 5842 4046 4220 -2866 246 -1009 N ATOM 2494 CA ARG A1125 18.773 5.484 61.084 1.00 36.58 C ANISOU 2494 CA ARG A1125 5648 4132 4120 -2845 35 -827 C ATOM 2495 C ARG A1125 19.076 6.765 61.849 1.00 39.81 C ANISOU 2495 C ARG A1125 5894 4540 4692 -2566 -97 -663 C ATOM 2496 O ARG A1125 19.383 6.750 63.041 1.00 39.07 O ANISOU 2496 O ARG A1125 5748 4304 4793 -2330 -88 -649 O ATOM 2497 CB ARG A1125 18.157 4.440 62.015 1.00 36.80 C ANISOU 2497 CB ARG A1125 5707 4054 4223 -2819 66 -872 C ATOM 2498 CG ARG A1125 18.457 3.003 61.621 1.00 50.05 C ANISOU 2498 CG ARG A1125 7568 5579 5871 -2984 281 -1089 C ATOM 2499 CD ARG A1125 18.011 2.031 62.701 1.00 63.05 C ANISOU 2499 CD ARG A1125 9236 7081 7639 -2915 306 -1108 C ATOM 2500 NE ARG A1125 17.988 0.653 62.219 1.00 80.21 N ANISOU 2500 NE ARG A1125 11581 9130 9764 -3123 492 -1302 N ATOM 2501 CZ ARG A1125 16.914 0.057 61.712 1.00 96.95 C ANISOU 2501 CZ ARG A1125 13768 11383 11686 -3399 477 -1342 C ATOM 2502 NH1 ARG A1125 15.768 0.718 61.618 1.00 83.40 N ANISOU 2502 NH1 ARG A1125 11947 9934 9807 -3490 273 -1186 N ATOM 2503 NH2 ARG A1125 16.984 -1.201 61.298 1.00 83.65 N ANISOU 2503 NH2 ARG A1125 12246 9556 9979 -3587 672 -1540 N ATOM 2504 N TRP A1126 18.990 7.868 61.123 1.00 36.32 N ANISOU 2504 N TRP A1126 5374 4262 4163 -2618 -217 -538 N ATOM 2505 CA TRP A1126 19.443 9.191 61.549 1.00 34.46 C ANISOU 2505 CA TRP A1126 5001 4022 4070 -2391 -318 -402 C ATOM 2506 C TRP A1126 18.411 9.815 62.465 1.00 36.95 C ANISOU 2506 C TRP A1126 5148 4402 4490 -2261 -485 -245 C ATOM 2507 O TRP A1126 18.804 10.405 63.465 1.00 35.38 O ANISOU 2507 O TRP A1126 4860 4105 4480 -2017 -499 -209 O ATOM 2508 CB TRP A1126 19.846 10.142 60.411 1.00 33.89 C ANISOU 2508 CB TRP A1126 4914 4076 3887 -2496 -374 -322 C ATOM 2509 CG TRP A1126 20.795 9.551 59.408 1.00 35.85 C ANISOU 2509 CG TRP A1126 5325 4292 4006 -2668 -197 -496 C ATOM 2510 CD1 TRP A1126 20.588 9.440 58.071 1.00 40.48 C ANISOU 2510 CD1 TRP A1126 5989 5051 4342 -2983 -194 -514 C ATOM 2511 CD2 TRP A1126 22.062 8.924 59.671 1.00 35.39 C ANISOU 2511 CD2 TRP A1126 5363 4019 4065 -2556 16 -685 C ATOM 2512 NE1 TRP A1126 21.653 8.805 57.478 1.00 40.33 N ANISOU 2512 NE1 TRP A1126 6114 4936 4273 -3077 26 -728 N ATOM 2513 CE2 TRP A1126 22.573 8.482 58.433 1.00 40.28 C ANISOU 2513 CE2 TRP A1126 6113 4683 4508 -2806 158 -832 C ATOM 2514 CE3 TRP A1126 22.817 8.691 60.836 1.00 35.36 C ANISOU 2514 CE3 TRP A1126 5337 3797 4302 -2279 99 -736 C ATOM 2515 CZ2 TRP A1126 23.823 7.874 58.311 1.00 39.91 C ANISOU 2515 CZ2 TRP A1126 6161 4453 4547 -2764 390 -1036 C ATOM 2516 CZ3 TRP A1126 24.049 8.058 60.717 1.00 37.07 C ANISOU 2516 CZ3 TRP A1126 5645 3837 4605 -2237 307 -911 C ATOM 2517 CH2 TRP A1126 24.539 7.657 59.464 1.00 39.45 C ANISOU 2517 CH2 TRP A1126 6064 4169 4756 -2468 457 -1065 C ATOM 2518 N ASP A1127 17.117 9.686 62.156 1.00 34.89 N ANISOU 2518 N ASP A1127 4836 4307 4113 -2428 -600 -160 N ATOM 2519 CA ASP A1127 16.089 10.260 63.022 1.00 34.89 C ANISOU 2519 CA ASP A1127 4657 4367 4233 -2308 -741 -26 C ATOM 2520 C ASP A1127 15.911 9.457 64.329 1.00 37.37 C ANISOU 2520 C ASP A1127 4987 4557 4654 -2188 -666 -121 C ATOM 2521 O ASP A1127 15.774 10.050 65.410 1.00 35.15 O ANISOU 2521 O ASP A1127 4578 4234 4543 -1989 -709 -71 O ATOM 2522 CB ASP A1127 14.775 10.493 62.266 1.00 39.36 C ANISOU 2522 CB ASP A1127 5130 5161 4664 -2516 -904 124 C ATOM 2523 CG ASP A1127 14.802 11.739 61.395 1.00 56.52 C ANISOU 2523 CG ASP A1127 7195 7455 6827 -2548 -1046 309 C ATOM 2524 OD1 ASP A1127 15.004 11.600 60.163 1.00 57.72 O ANISOU 2524 OD1 ASP A1127 7440 7719 6773 -2784 -1051 319 O ATOM 2525 OD2 ASP A1127 14.632 12.855 61.947 1.00 67.21 O ANISOU 2525 OD2 ASP A1127 8370 8787 8380 -2348 -1145 442 O ATOM 2526 N GLU A1128 15.991 8.112 64.229 1.00 34.49 N ANISOU 2526 N GLU A1128 4785 4124 4195 -2320 -543 -265 N ATOM 2527 CA GLU A1128 15.938 7.222 65.375 1.00 33.61 C ANISOU 2527 CA GLU A1128 4713 3881 4175 -2236 -468 -347 C ATOM 2528 C GLU A1128 17.067 7.623 66.314 1.00 35.29 C ANISOU 2528 C GLU A1128 4900 3926 4582 -1978 -410 -363 C ATOM 2529 O GLU A1128 16.790 7.852 67.492 1.00 36.25 O ANISOU 2529 O GLU A1128 4924 4028 4820 -1839 -450 -323 O ATOM 2530 CB GLU A1128 16.134 5.763 64.952 1.00 36.47 C ANISOU 2530 CB GLU A1128 5269 4148 4438 -2410 -320 -504 C ATOM 2531 CG GLU A1128 14.868 5.029 64.538 1.00 54.72 C ANISOU 2531 CG GLU A1128 7616 6599 6578 -2660 -361 -511 C ATOM 2532 CD GLU A1128 15.111 3.626 64.000 1.00 71.42 C ANISOU 2532 CD GLU A1128 9934 8606 8598 -2856 -193 -688 C ATOM 2533 OE1 GLU A1128 15.400 2.711 64.809 1.00 47.94 O ANISOU 2533 OE1 GLU A1128 7033 5444 5739 -2782 -92 -769 O ATOM 2534 OE2 GLU A1128 15.041 3.454 62.759 1.00 57.56 O ANISOU 2534 OE2 GLU A1128 8262 6950 6657 -3092 -159 -744 O ATOM 2535 N ALA A1129 18.318 7.774 65.794 1.00 27.83 N ANISOU 2535 N ALA A1129 4029 2882 3664 -1928 -318 -420 N ATOM 2536 CA ALA A1129 19.476 8.164 66.607 1.00 25.04 C ANISOU 2536 CA ALA A1129 3647 2381 3486 -1698 -265 -428 C ATOM 2537 C ALA A1129 19.314 9.565 67.196 1.00 28.57 C ANISOU 2537 C ALA A1129 3923 2901 4031 -1538 -385 -306 C ATOM 2538 O ALA A1129 19.500 9.726 68.410 1.00 26.87 O ANISOU 2538 O ALA A1129 3643 2623 3944 -1385 -386 -294 O ATOM 2539 CB ALA A1129 20.772 8.040 65.823 1.00 25.60 C ANISOU 2539 CB ALA A1129 3819 2349 3560 -1699 -140 -516 C ATOM 2540 N ALA A1130 18.873 10.553 66.377 1.00 25.50 N ANISOU 2540 N ALA A1130 3454 2650 3585 -1593 -489 -210 N ATOM 2541 CA ALA A1130 18.644 11.924 66.848 1.00 24.57 C ANISOU 2541 CA ALA A1130 3163 2581 3590 -1448 -595 -95 C ATOM 2542 C ALA A1130 17.594 11.998 67.964 1.00 29.60 C ANISOU 2542 C ALA A1130 3675 3260 4310 -1391 -653 -64 C ATOM 2543 O ALA A1130 17.665 12.901 68.806 1.00 28.47 O ANISOU 2543 O ALA A1130 3408 3095 4315 -1235 -677 -31 O ATOM 2544 CB ALA A1130 18.240 12.822 65.703 1.00 26.06 C ANISOU 2544 CB ALA A1130 3285 2901 3714 -1542 -708 28 C ATOM 2545 N VAL A1131 16.628 11.053 67.987 1.00 26.87 N ANISOU 2545 N VAL A1131 3362 2977 3868 -1531 -664 -87 N ATOM 2546 CA VAL A1131 15.637 11.038 69.066 1.00 26.42 C ANISOU 2546 CA VAL A1131 3191 2969 3880 -1496 -703 -74 C ATOM 2547 C VAL A1131 16.247 10.398 70.298 1.00 29.77 C ANISOU 2547 C VAL A1131 3675 3271 4366 -1405 -610 -161 C ATOM 2548 O VAL A1131 16.082 10.898 71.415 1.00 29.31 O ANISOU 2548 O VAL A1131 3506 3215 4415 -1298 -617 -157 O ATOM 2549 CB VAL A1131 14.283 10.413 68.649 1.00 31.37 C ANISOU 2549 CB VAL A1131 3802 3735 4384 -1685 -768 -46 C ATOM 2550 CG1 VAL A1131 13.364 10.187 69.849 1.00 30.93 C ANISOU 2550 CG1 VAL A1131 3648 3717 4386 -1662 -779 -62 C ATOM 2551 CG2 VAL A1131 13.584 11.301 67.627 1.00 32.53 C ANISOU 2551 CG2 VAL A1131 3827 4026 4506 -1757 -898 91 C ATOM 2552 N ASN A1132 16.983 9.308 70.086 1.00 26.37 N ANISOU 2552 N ASN A1132 3413 2730 3877 -1456 -517 -236 N ATOM 2553 CA ASN A1132 17.604 8.563 71.169 1.00 25.25 C ANISOU 2553 CA ASN A1132 3331 2462 3802 -1387 -442 -285 C ATOM 2554 C ASN A1132 18.646 9.392 71.921 1.00 26.97 C ANISOU 2554 C ASN A1132 3486 2611 4151 -1204 -424 -269 C ATOM 2555 O ASN A1132 18.540 9.577 73.142 1.00 25.18 O ANISOU 2555 O ASN A1132 3184 2396 3989 -1140 -435 -258 O ATOM 2556 CB ASN A1132 18.175 7.262 70.658 1.00 24.89 C ANISOU 2556 CB ASN A1132 3462 2288 3709 -1475 -341 -360 C ATOM 2557 CG ASN A1132 18.291 6.246 71.744 1.00 46.01 C ANISOU 2557 CG ASN A1132 6185 4858 6437 -1465 -298 -375 C ATOM 2558 OD1 ASN A1132 17.319 5.953 72.468 1.00 37.58 O ANISOU 2558 OD1 ASN A1132 5075 3868 5337 -1527 -346 -355 O ATOM 2559 ND2 ASN A1132 19.489 5.698 71.883 1.00 37.28 N ANISOU 2559 ND2 ASN A1132 5161 3579 5426 -1391 -209 -401 N ATOM 2560 N LEU A1133 19.603 9.963 71.173 1.00 22.97 N ANISOU 2560 N LEU A1133 3003 2056 3670 -1140 -398 -267 N ATOM 2561 CA LEU A1133 20.637 10.822 71.732 1.00 21.26 C ANISOU 2561 CA LEU A1133 2729 1784 3566 -981 -382 -251 C ATOM 2562 C LEU A1133 20.035 12.016 72.526 1.00 24.11 C ANISOU 2562 C LEU A1133 2924 2236 4001 -906 -449 -210 C ATOM 2563 O LEU A1133 20.544 12.368 73.593 1.00 22.88 O ANISOU 2563 O LEU A1133 2717 2053 3923 -815 -428 -218 O ATOM 2564 CB LEU A1133 21.582 11.277 70.616 1.00 20.98 C ANISOU 2564 CB LEU A1133 2742 1707 3523 -957 -349 -257 C ATOM 2565 CG LEU A1133 22.682 10.299 70.245 1.00 24.60 C ANISOU 2565 CG LEU A1133 3334 2027 3987 -964 -236 -324 C ATOM 2566 CD1 LEU A1133 23.423 10.751 69.016 1.00 23.77 C ANISOU 2566 CD1 LEU A1133 3273 1914 3843 -983 -197 -346 C ATOM 2567 CD2 LEU A1133 23.654 10.161 71.365 1.00 27.37 C ANISOU 2567 CD2 LEU A1133 3665 2274 4462 -832 -196 -316 C ATOM 2568 N ALA A1134 18.901 12.568 72.053 1.00 20.64 N ANISOU 2568 N ALA A1134 2393 1907 3541 -960 -524 -170 N ATOM 2569 CA ALA A1134 18.213 13.671 72.724 1.00 19.77 C ANISOU 2569 CA ALA A1134 2109 1865 3538 -892 -570 -145 C ATOM 2570 C ALA A1134 17.674 13.261 74.095 1.00 25.32 C ANISOU 2570 C ALA A1134 2765 2600 4257 -907 -544 -196 C ATOM 2571 O ALA A1134 17.390 14.145 74.904 1.00 25.95 O ANISOU 2571 O ALA A1134 2709 2712 4437 -845 -538 -215 O ATOM 2572 CB ALA A1134 17.089 14.182 71.858 1.00 21.17 C ANISOU 2572 CB ALA A1134 2189 2143 3711 -955 -660 -70 C ATOM 2573 N LYS A1135 17.545 11.925 74.369 1.00 20.68 N ANISOU 2573 N LYS A1135 2287 1998 3571 -1003 -520 -223 N ATOM 2574 CA LYS A1135 17.048 11.380 75.657 1.00 19.03 C ANISOU 2574 CA LYS A1135 2052 1830 3349 -1053 -502 -257 C ATOM 2575 C LYS A1135 18.196 11.124 76.658 1.00 24.15 C ANISOU 2575 C LYS A1135 2751 2399 4024 -998 -452 -266 C ATOM 2576 O LYS A1135 17.934 10.852 77.835 1.00 22.70 O ANISOU 2576 O LYS A1135 2535 2265 3826 -1046 -443 -282 O ATOM 2577 CB LYS A1135 16.256 10.070 75.437 1.00 19.23 C ANISOU 2577 CB LYS A1135 2166 1880 3258 -1201 -513 -261 C ATOM 2578 CG LYS A1135 14.951 10.249 74.698 1.00 15.24 C ANISOU 2578 CG LYS A1135 1643 1548 2602 -1105 -517 -184 C ATOM 2579 CD LYS A1135 14.446 8.984 74.042 1.00 18.16 C ANISOU 2579 CD LYS A1135 2083 1870 2948 -1445 -580 -246 C ATOM 2580 CE LYS A1135 13.035 9.192 73.537 1.00 31.95 C ANISOU 2580 CE LYS A1135 3723 3769 4649 -1547 -654 -213 C ATOM 2581 NZ LYS A1135 12.535 8.064 72.714 1.00 38.35 N ANISOU 2581 NZ LYS A1135 4657 4604 5309 -1726 -662 -220 N ATOM 2582 N SER A1136 19.464 11.175 76.173 1.00 22.62 N ANISOU 2582 N SER A1136 2633 2097 3864 -916 -424 -248 N ATOM 2583 CA SER A1136 20.663 10.906 76.966 1.00 22.60 C ANISOU 2583 CA SER A1136 2671 2017 3901 -861 -389 -229 C ATOM 2584 C SER A1136 20.880 11.902 78.081 1.00 27.79 C ANISOU 2584 C SER A1136 3213 2740 4606 -815 -386 -243 C ATOM 2585 O SER A1136 20.335 13.010 78.045 1.00 28.76 O ANISOU 2585 O SER A1136 3225 2930 4772 -785 -391 -280 O ATOM 2586 CB SER A1136 21.900 10.835 76.077 1.00 25.75 C ANISOU 2586 CB SER A1136 3151 2293 4339 -782 -353 -215 C ATOM 2587 OG SER A1136 22.212 12.086 75.484 1.00 35.24 O ANISOU 2587 OG SER A1136 4292 3514 5582 -701 -359 -222 O ATOM 2588 N ARG A1137 21.698 11.502 79.072 1.00 23.24 N ANISOU 2588 N ARG A1137 2657 2141 4034 -821 -375 -208 N ATOM 2589 CA ARG A1137 22.080 12.320 80.218 1.00 21.74 C ANISOU 2589 CA ARG A1137 2376 2025 3861 -814 -363 -223 C ATOM 2590 C ARG A1137 22.985 13.425 79.708 1.00 22.35 C ANISOU 2590 C ARG A1137 2422 2056 4015 -693 -341 -235 C ATOM 2591 O ARG A1137 22.938 14.532 80.226 1.00 22.59 O ANISOU 2591 O ARG A1137 2355 2149 4080 -677 -318 -289 O ATOM 2592 CB ARG A1137 22.820 11.471 81.253 1.00 23.28 C ANISOU 2592 CB ARG A1137 2608 2210 4025 -872 -379 -144 C ATOM 2593 CG ARG A1137 22.516 11.874 82.674 1.00 43.38 C ANISOU 2593 CG ARG A1137 5068 4902 6512 -980 -377 -170 C ATOM 2594 CD ARG A1137 23.424 11.163 83.657 1.00 56.88 C ANISOU 2594 CD ARG A1137 6805 6617 8190 -1045 -415 -54 C ATOM 2595 NE ARG A1137 22.741 10.099 84.399 1.00 63.76 N ANISOU 2595 NE ARG A1137 7706 7544 8977 -1196 -454 0 N ATOM 2596 CZ ARG A1137 22.715 8.825 84.023 1.00 76.09 C ANISOU 2596 CZ ARG A1137 9361 8993 10556 -1207 -487 88 C ATOM 2597 NH1 ARG A1137 23.297 8.445 82.890 1.00 54.24 N ANISOU 2597 NH1 ARG A1137 6667 6056 7888 -1081 -470 111 N ATOM 2598 NH2 ARG A1137 22.099 7.921 84.771 1.00 68.55 N ANISOU 2598 NH2 ARG A1137 8429 8092 9523 -1357 -526 145 N ATOM 2599 N TRP A1138 23.769 13.133 78.657 1.00 16.30 N ANISOU 2599 N TRP A1138 1736 1178 3278 -619 -336 -199 N ATOM 2600 CA TRP A1138 24.685 14.054 78.011 1.00 15.40 C ANISOU 2600 CA TRP A1138 1610 1016 3226 -515 -316 -201 C ATOM 2601 C TRP A1138 23.883 15.228 77.509 1.00 17.83 C ANISOU 2601 C TRP A1138 1836 1373 3567 -491 -325 -247 C ATOM 2602 O TRP A1138 24.229 16.378 77.789 1.00 15.28 O ANISOU 2602 O TRP A1138 1436 1063 3305 -438 -308 -272 O ATOM 2603 CB TRP A1138 25.416 13.314 76.878 1.00 14.83 C ANISOU 2603 CB TRP A1138 1645 827 3162 -478 -296 -173 C ATOM 2604 CG TRP A1138 26.007 14.160 75.795 1.00 15.87 C ANISOU 2604 CG TRP A1138 1781 923 3325 -405 -278 -186 C ATOM 2605 CD1 TRP A1138 27.034 15.042 75.917 1.00 18.26 C ANISOU 2605 CD1 TRP A1138 2044 1212 3682 -327 -260 -178 C ATOM 2606 CD2 TRP A1138 25.663 14.133 74.399 1.00 16.47 C ANISOU 2606 CD2 TRP A1138 1912 981 3365 -428 -279 -200 C ATOM 2607 NE1 TRP A1138 27.327 15.597 74.696 1.00 17.70 N ANISOU 2607 NE1 TRP A1138 1999 1112 3617 -294 -251 -186 N ATOM 2608 CE2 TRP A1138 26.504 15.053 73.744 1.00 19.48 C ANISOU 2608 CE2 TRP A1138 2281 1340 3780 -362 -264 -195 C ATOM 2609 CE3 TRP A1138 24.706 13.432 73.639 1.00 18.51 C ANISOU 2609 CE3 TRP A1138 2227 1256 3550 -521 -293 -212 C ATOM 2610 CZ2 TRP A1138 26.428 15.291 72.364 1.00 18.91 C ANISOU 2610 CZ2 TRP A1138 2253 1267 3665 -393 -268 -195 C ATOM 2611 CZ3 TRP A1138 24.634 13.667 72.271 1.00 20.10 C ANISOU 2611 CZ3 TRP A1138 2471 1463 3703 -558 -296 -216 C ATOM 2612 CH2 TRP A1138 25.487 14.588 71.649 1.00 20.33 C ANISOU 2612 CH2 TRP A1138 2487 1475 3761 -498 -286 -203 C ATOM 2613 N TYR A1139 22.754 14.936 76.854 1.00 15.92 N ANISOU 2613 N TYR A1139 1598 1159 3293 -541 -355 -251 N ATOM 2614 CA TYR A1139 21.857 15.969 76.356 1.00 16.20 C ANISOU 2614 CA TYR A1139 1532 1239 3385 -524 -382 -262 C ATOM 2615 C TYR A1139 21.275 16.811 77.504 1.00 19.06 C ANISOU 2615 C TYR A1139 1757 1667 3818 -525 -355 -325 C ATOM 2616 O TYR A1139 21.133 18.019 77.360 1.00 18.70 O ANISOU 2616 O TYR A1139 1610 1612 3884 -463 -346 -342 O ATOM 2617 CB TYR A1139 20.759 15.372 75.460 1.00 18.52 C ANISOU 2617 CB TYR A1139 1849 1569 3620 -600 -431 -235 C ATOM 2618 CG TYR A1139 19.806 16.412 74.909 1.00 20.93 C ANISOU 2618 CG TYR A1139 2027 1922 4005 -583 -479 -209 C ATOM 2619 CD1 TYR A1139 19.966 16.921 73.626 1.00 22.84 C ANISOU 2619 CD1 TYR A1139 2278 2142 4256 -564 -527 -139 C ATOM 2620 CD2 TYR A1139 18.726 16.869 75.666 1.00 22.45 C ANISOU 2620 CD2 TYR A1139 2077 2181 4273 -595 -477 -246 C ATOM 2621 CE1 TYR A1139 19.072 17.857 73.106 1.00 24.82 C ANISOU 2621 CE1 TYR A1139 2395 2432 4602 -552 -592 -76 C ATOM 2622 CE2 TYR A1139 17.842 17.821 75.167 1.00 23.91 C ANISOU 2622 CE2 TYR A1139 2118 2389 4577 -566 -522 -205 C ATOM 2623 CZ TYR A1139 18.019 18.315 73.889 1.00 31.75 C ANISOU 2623 CZ TYR A1139 3118 3355 5592 -541 -590 -105 C ATOM 2624 OH TYR A1139 17.129 19.241 73.414 1.00 33.43 O ANISOU 2624 OH TYR A1139 3172 3586 5943 -514 -652 -30 O ATOM 2625 N ASN A1140 20.932 16.186 78.628 1.00 16.71 N ANISOU 2625 N ASN A1140 1452 1432 3464 -607 -333 -364 N ATOM 2626 CA ASN A1140 20.377 16.919 79.763 1.00 17.34 C ANISOU 2626 CA ASN A1140 1406 1590 3594 -642 -283 -453 C ATOM 2627 C ASN A1140 21.424 17.876 80.373 1.00 17.03 C ANISOU 2627 C ASN A1140 1333 1530 3608 -595 -229 -493 C ATOM 2628 O ASN A1140 21.071 18.989 80.752 1.00 16.79 O ANISOU 2628 O ASN A1140 1184 1513 3682 -577 -173 -577 O ATOM 2629 CB ASN A1140 19.741 15.940 80.787 1.00 26.84 C ANISOU 2629 CB ASN A1140 2620 2888 4691 -778 -276 -481 C ATOM 2630 CG ASN A1140 19.811 16.308 82.269 1.00 75.49 C ANISOU 2630 CG ASN A1140 8712 9143 10830 -865 -210 -567 C ATOM 2631 OD1 ASN A1140 20.548 15.701 83.069 1.00 79.67 O ANISOU 2631 OD1 ASN A1140 9305 9703 11261 -938 -217 -531 O ATOM 2632 ND2 ASN A1140 19.088 17.374 82.651 1.00 67.72 N ANISOU 2632 ND2 ASN A1140 7585 8202 9946 -866 -141 -682 N ATOM 2633 N GLN A1141 22.712 17.470 80.388 1.00 11.61 N ANISOU 2633 N GLN A1141 805 859 2747 -381 -193 -388 N ATOM 2634 CA GLN A1141 23.809 18.260 80.956 1.00 10.25 C ANISOU 2634 CA GLN A1141 649 716 2531 -241 -126 -386 C ATOM 2635 C GLN A1141 24.345 19.390 80.068 1.00 12.98 C ANISOU 2635 C GLN A1141 873 885 3173 -424 -188 -454 C ATOM 2636 O GLN A1141 24.381 20.524 80.527 1.00 14.10 O ANISOU 2636 O GLN A1141 927 1032 3399 -419 -133 -531 O ATOM 2637 CB GLN A1141 24.879 17.353 81.538 1.00 10.16 C ANISOU 2637 CB GLN A1141 707 727 2428 -284 -153 -312 C ATOM 2638 CG GLN A1141 24.240 16.528 82.631 1.00 14.85 C ANISOU 2638 CG GLN A1141 1207 1319 3118 -730 -230 -388 C ATOM 2639 CD GLN A1141 25.107 15.543 83.334 1.00 37.83 C ANISOU 2639 CD GLN A1141 4176 4248 5950 -796 -272 -282 C ATOM 2640 OE1 GLN A1141 26.334 15.495 83.157 1.00 41.31 O ANISOU 2640 OE1 GLN A1141 4648 4630 6417 -733 -288 -205 O ATOM 2641 NE2 GLN A1141 24.468 14.779 84.212 1.00 17.95 N ANISOU 2641 NE2 GLN A1141 1658 1820 3341 -935 -291 -268 N ATOM 2642 N THR A1142 24.700 19.113 78.805 1.00 9.82 N ANISOU 2642 N THR A1142 572 538 2622 -116 -185 -314 N ATOM 2643 CA THR A1142 25.143 20.139 77.871 1.00 9.83 C ANISOU 2643 CA THR A1142 526 482 2729 -65 -200 -301 C ATOM 2644 C THR A1142 24.035 20.033 76.783 1.00 16.96 C ANISOU 2644 C THR A1142 1421 1231 3790 -268 -294 -313 C ATOM 2645 O THR A1142 24.082 19.111 75.973 1.00 19.55 O ANISOU 2645 O THR A1142 1845 1547 4034 -291 -331 -259 O ATOM 2646 CB THR A1142 26.602 19.880 77.446 1.00 17.29 C ANISOU 2646 CB THR A1142 1568 1231 3772 -226 -237 -303 C ATOM 2647 OG1 THR A1142 26.737 18.591 76.837 1.00 18.77 O ANISOU 2647 OG1 THR A1142 1858 1392 3882 -244 -262 -251 O ATOM 2648 CG2 THR A1142 27.546 19.952 78.598 1.00 19.79 C ANISOU 2648 CG2 THR A1142 1872 1582 4066 -248 -200 -324 C ATOM 2649 N PRO A1143 23.069 20.945 76.786 1.00 14.47 N ANISOU 2649 N PRO A1143 983 921 3593 -251 -295 -335 N ATOM 2650 CA PRO A1143 21.940 20.860 75.851 1.00 14.30 C ANISOU 2650 CA PRO A1143 922 913 3598 -264 -365 -271 C ATOM 2651 C PRO A1143 22.222 21.511 74.497 1.00 22.07 C ANISOU 2651 C PRO A1143 1915 1843 4626 -218 -428 -168 C ATOM 2652 O PRO A1143 21.842 20.970 73.459 1.00 24.28 O ANISOU 2652 O PRO A1143 2246 2151 4828 -268 -498 -88 O ATOM 2653 CB PRO A1143 20.832 21.625 76.578 1.00 16.26 C ANISOU 2653 CB PRO A1143 1002 1182 3994 -259 -330 -337 C ATOM 2654 CG PRO A1143 21.556 22.595 77.442 1.00 21.95 C ANISOU 2654 CG PRO A1143 1675 1860 4805 -219 -241 -426 C ATOM 2655 CD PRO A1143 22.812 21.898 77.880 1.00 17.27 C ANISOU 2655 CD PRO A1143 1216 1286 4059 -248 -220 -437 C ATOM 2656 N ASN A1144 22.879 22.664 74.521 1.00 18.53 N ANISOU 2656 N ASN A1144 1421 1329 4291 -147 -401 -169 N ATOM 2657 CA ASN A1144 23.159 23.442 73.305 1.00 18.41 C ANISOU 2657 CA ASN A1144 1402 1263 4330 -113 -465 -59 C ATOM 2658 C ASN A1144 24.217 22.793 72.449 1.00 20.98 C ANISOU 2658 C ASN A1144 1882 1593 4497 -144 -479 -18 C ATOM 2659 O ASN A1144 24.049 22.778 71.233 1.00 22.29 O ANISOU 2659 O ASN A1144 2079 1776 4616 -189 -552 81 O ATOM 2660 CB ASN A1144 23.459 24.914 73.609 1.00 21.57 C ANISOU 2660 CB ASN A1144 1698 1576 4922 -34 -427 -73 C ATOM 2661 CG ASN A1144 22.520 25.585 74.617 1.00 46.03 C ANISOU 2661 CG ASN A1144 4634 4649 8205 -4 -366 -161 C ATOM 2662 OD1 ASN A1144 21.319 25.299 74.640 1.00 35.70 O ANISOU 2662 OD1 ASN A1144 3242 3382 6941 -27 -397 -148 O ATOM 2663 ND2 ASN A1144 23.019 26.479 75.481 1.00 44.11 N ANISOU 2663 ND2 ASN A1144 4339 4345 8075 33 -267 -265 N ATOM 2664 N ARG A1145 25.246 22.160 73.062 1.00 15.73 N ANISOU 2664 N ARG A1145 1308 923 3747 -139 -410 -91 N ATOM 2665 CA ARG A1145 26.261 21.430 72.281 1.00 15.02 C ANISOU 2665 CA ARG A1145 1352 822 3532 -164 -400 -72 C ATOM 2666 C ARG A1145 25.627 20.149 71.759 1.00 19.35 C ANISOU 2666 C ARG A1145 1977 1412 3961 -250 -423 -64 C ATOM 2667 O ARG A1145 25.713 19.895 70.553 1.00 20.39 O ANISOU 2667 O ARG A1145 2179 1557 4012 -311 -450 -20 O ATOM 2668 CB ARG A1145 27.538 21.107 73.083 1.00 11.81 C ANISOU 2668 CB ARG A1145 981 417 3089 -116 -324 -128 C ATOM 2669 CG ARG A1145 28.727 20.603 72.230 1.00 11.87 C ANISOU 2669 CG ARG A1145 1087 410 3013 -117 -294 -113 C ATOM 2670 CD ARG A1145 29.921 20.362 73.146 1.00 16.85 C ANISOU 2670 CD ARG A1145 1747 973 3682 -84 -234 -152 C ATOM 2671 NE ARG A1145 31.140 19.880 72.491 1.00 14.80 N ANISOU 2671 NE ARG A1145 1561 671 3389 -71 -187 -150 N ATOM 2672 CZ ARG A1145 32.314 19.762 73.115 1.00 25.56 C ANISOU 2672 CZ ARG A1145 2915 2015 4783 -26 -143 -156 C ATOM 2673 NH1 ARG A1145 32.432 20.098 74.393 1.00 17.41 N ANISOU 2673 NH1 ARG A1145 1814 1015 3785 -10 -148 -159 N ATOM 2674 NH2 ARG A1145 33.371 19.285 72.472 1.00 9.99 N ANISOU 2674 NH2 ARG A1145 797 387 2610 -1 -88 -126 N ATOM 2675 N ALA A1146 24.939 19.380 72.650 1.00 13.67 N ANISOU 2675 N ALA A1146 1246 724 3226 -276 -411 -110 N ATOM 2676 CA ALA A1146 24.278 18.136 72.278 1.00 12.40 C ANISOU 2676 CA ALA A1146 1157 596 2958 -367 -426 -112 C ATOM 2677 C ALA A1146 23.304 18.348 71.131 1.00 17.10 C ANISOU 2677 C ALA A1146 1730 1247 3521 -440 -506 -40 C ATOM 2678 O ALA A1146 23.384 17.602 70.154 1.00 18.25 O ANISOU 2678 O ALA A1146 1978 1407 3548 -530 -509 -30 O ATOM 2679 CB ALA A1146 23.598 17.507 73.465 1.00 12.45 C ANISOU 2679 CB ALA A1146 1132 638 2962 -387 -411 -158 C ATOM 2680 N LYS A1147 22.493 19.433 71.164 1.00 12.07 N ANISOU 2680 N LYS A1147 958 662 2968 -364 -559 25 N ATOM 2681 CA LYS A1147 21.584 19.756 70.058 1.00 12.30 C ANISOU 2681 CA LYS A1147 949 749 2975 -417 -656 139 C ATOM 2682 C LYS A1147 22.374 19.964 68.761 1.00 17.67 C ANISOU 2682 C LYS A1147 1699 1404 3610 -531 -694 193 C ATOM 2683 O LYS A1147 22.059 19.274 67.786 1.00 19.93 O ANISOU 2683 O LYS A1147 2063 1760 3751 -665 -730 227 O ATOM 2684 CB LYS A1147 20.686 20.964 70.351 1.00 14.12 C ANISOU 2684 CB LYS A1147 973 953 3440 -414 -724 191 C ATOM 2685 CG LYS A1147 19.602 20.721 71.406 1.00 28.72 C ANISOU 2685 CG LYS A1147 2717 2836 5360 -406 -703 128 C ATOM 2686 CD LYS A1147 18.665 21.921 71.593 1.00 37.17 C ANISOU 2686 CD LYS A1147 3576 3887 6660 -340 -742 184 C ATOM 2687 CE LYS A1147 18.451 22.267 73.043 1.00 47.90 C ANISOU 2687 CE LYS A1147 4837 5212 8150 -272 -637 46 C ATOM 2688 NZ LYS A1147 17.848 23.615 73.196 1.00 67.27 N ANISOU 2688 NZ LYS A1147 7088 7597 10875 -185 -638 76 N ATOM 2689 N ARG A1148 23.441 20.836 68.766 1.00 11.67 N ANISOU 2689 N ARG A1148 946 630 2860 -358 -652 210 N ATOM 2690 CA ARG A1148 24.260 21.098 67.578 1.00 11.04 C ANISOU 2690 CA ARG A1148 942 608 2646 -348 -663 272 C ATOM 2691 C ARG A1148 24.862 19.812 67.020 1.00 16.47 C ANISOU 2691 C ARG A1148 1788 1208 3262 -604 -605 169 C ATOM 2692 O ARG A1148 24.798 19.598 65.807 1.00 18.38 O ANISOU 2692 O ARG A1148 2095 1517 3371 -744 -638 214 O ATOM 2693 CB ARG A1148 25.352 22.141 67.836 1.00 8.61 C ANISOU 2693 CB ARG A1148 574 418 2278 -85 -606 267 C ATOM 2694 CG ARG A1148 24.862 23.568 68.047 1.00 13.81 C ANISOU 2694 CG ARG A1148 1112 733 3401 -323 -707 340 C ATOM 2695 CD ARG A1148 25.991 24.602 68.167 1.00 18.49 C ANISOU 2695 CD ARG A1148 1699 1247 4078 -244 -667 337 C ATOM 2696 NE ARG A1148 26.831 24.393 69.347 1.00 16.86 N ANISOU 2696 NE ARG A1148 1520 994 3893 -162 -554 198 N ATOM 2697 CZ ARG A1148 26.778 25.108 70.466 1.00 36.01 C ANISOU 2697 CZ ARG A1148 3852 3364 6467 -75 -509 140 C ATOM 2698 NH1 ARG A1148 25.956 26.151 70.563 1.00 13.32 N ANISOU 2698 NH1 ARG A1148 844 444 3773 -36 -551 195 N ATOM 2699 NH2 ARG A1148 27.565 24.804 71.489 1.00 40.06 N ANISOU 2699 NH2 ARG A1148 4397 3866 6957 -39 -419 29 N ATOM 2700 N VAL A1149 25.396 18.927 67.904 1.00 12.40 N ANISOU 2700 N VAL A1149 1324 673 2716 -507 -500 59 N ATOM 2701 CA VAL A1149 25.983 17.631 67.522 1.00 12.31 C ANISOU 2701 CA VAL A1149 1438 680 2557 -539 -403 -23 C ATOM 2702 C VAL A1149 24.913 16.671 66.976 1.00 19.98 C ANISOU 2702 C VAL A1149 2483 1637 3473 -769 -439 -45 C ATOM 2703 O VAL A1149 25.072 16.171 65.863 1.00 20.79 O ANISOU 2703 O VAL A1149 2683 1774 3444 -908 -410 -69 O ATOM 2704 CB VAL A1149 26.854 17.032 68.646 1.00 13.17 C ANISOU 2704 CB VAL A1149 1588 621 2797 -507 -317 -121 C ATOM 2705 CG1 VAL A1149 27.136 15.542 68.433 1.00 12.79 C ANISOU 2705 CG1 VAL A1149 1620 617 2621 -502 -217 -185 C ATOM 2706 CG2 VAL A1149 28.154 17.814 68.757 1.00 12.74 C ANISOU 2706 CG2 VAL A1149 1505 541 2794 -398 -274 -120 C ATOM 2707 N ILE A1150 23.802 16.474 67.727 1.00 17.75 N ANISOU 2707 N ILE A1150 2131 1386 3227 -760 -490 -27 N ATOM 2708 CA ILE A1150 22.650 15.646 67.331 1.00 18.49 C ANISOU 2708 CA ILE A1150 2253 1559 3214 -904 -529 -22 C ATOM 2709 C ILE A1150 22.070 16.084 65.946 1.00 25.67 C ANISOU 2709 C ILE A1150 3153 2586 4013 -1056 -625 80 C ATOM 2710 O ILE A1150 21.807 15.224 65.094 1.00 26.66 O ANISOU 2710 O ILE A1150 3380 2771 3979 -1231 -607 47 O ATOM 2711 CB ILE A1150 21.598 15.647 68.468 1.00 20.41 C ANISOU 2711 CB ILE A1150 2389 1827 3541 -851 -574 -10 C ATOM 2712 CG1 ILE A1150 22.057 14.732 69.624 1.00 18.92 C ANISOU 2712 CG1 ILE A1150 2254 1552 3382 -791 -483 -106 C ATOM 2713 CG2 ILE A1150 20.219 15.261 67.953 1.00 22.59 C ANISOU 2713 CG2 ILE A1150 2637 2216 3729 -995 -655 41 C ATOM 2714 CD1 ILE A1150 21.431 14.986 70.889 1.00 16.39 C ANISOU 2714 CD1 ILE A1150 1826 1250 3150 -726 -503 -109 C ATOM 2715 N THR A1151 21.915 17.419 65.722 1.00 22.79 N ANISOU 2715 N THR A1151 2668 2255 3737 -1003 -724 206 N ATOM 2716 CA THR A1151 21.444 17.979 64.449 1.00 23.90 C ANISOU 2716 CA THR A1151 2779 2511 3793 -1146 -841 348 C ATOM 2717 C THR A1151 22.397 17.573 63.324 1.00 27.79 C ANISOU 2717 C THR A1151 3424 3026 4109 -1288 -773 296 C ATOM 2718 O THR A1151 21.952 17.202 62.238 1.00 29.20 O ANISOU 2718 O THR A1151 3658 3327 4109 -1502 -818 337 O ATOM 2719 CB THR A1151 21.197 19.496 64.569 1.00 31.08 C ANISOU 2719 CB THR A1151 3518 3407 4883 -1036 -951 501 C ATOM 2720 OG1 THR A1151 19.859 19.681 65.029 1.00 37.92 O ANISOU 2720 OG1 THR A1151 4237 4318 5855 -1014 -1040 578 O ATOM 2721 CG2 THR A1151 21.377 20.243 63.249 1.00 26.89 C ANISOU 2721 CG2 THR A1151 2984 2954 4279 -1158 -1051 656 C ATOM 2722 N THR A1152 23.699 17.593 63.614 1.00 22.75 N ANISOU 2722 N THR A1152 2851 2278 3515 -1183 -656 195 N ATOM 2723 CA THR A1152 24.725 17.225 62.661 1.00 22.90 C ANISOU 2723 CA THR A1152 3002 2300 3397 -1296 -559 115 C ATOM 2724 C THR A1152 24.631 15.729 62.309 1.00 29.40 C ANISOU 2724 C THR A1152 3963 3128 4081 -1445 -445 -32 C ATOM 2725 O THR A1152 24.776 15.395 61.139 1.00 31.18 O ANISOU 2725 O THR A1152 4282 3435 4128 -1652 -410 -67 O ATOM 2726 CB THR A1152 26.066 17.804 63.115 1.00 21.56 C ANISOU 2726 CB THR A1152 2828 2020 3345 -1132 -480 70 C ATOM 2727 OG1 THR A1152 25.993 19.230 62.953 1.00 22.62 O ANISOU 2727 OG1 THR A1152 2855 2185 3556 -1084 -599 223 O ATOM 2728 CG2 THR A1152 27.254 17.243 62.336 1.00 16.79 C ANISOU 2728 CG2 THR A1152 2353 1392 2635 -1221 -336 -56 C ATOM 2729 N PHE A1153 24.314 14.842 63.293 1.00 25.00 N ANISOU 2729 N PHE A1153 3416 2488 3595 -1363 -391 -114 N ATOM 2730 CA PHE A1153 24.159 13.394 63.053 1.00 24.57 C ANISOU 2730 CA PHE A1153 3487 2407 3440 -1495 -280 -251 C ATOM 2731 C PHE A1153 22.895 13.145 62.272 1.00 31.54 C ANISOU 2731 C PHE A1153 4380 3450 4154 -1718 -374 -192 C ATOM 2732 O PHE A1153 22.893 12.291 61.380 1.00 33.59 O ANISOU 2732 O PHE A1153 4763 3749 4250 -1928 -290 -292 O ATOM 2733 CB PHE A1153 24.100 12.578 64.357 1.00 24.62 C ANISOU 2733 CB PHE A1153 3491 2286 3577 -1356 -222 -318 C ATOM 2734 CG PHE A1153 25.415 12.135 64.951 1.00 25.49 C ANISOU 2734 CG PHE A1153 3643 2226 3816 -1212 -83 -417 C ATOM 2735 CD1 PHE A1153 26.439 11.650 64.143 1.00 30.50 C ANISOU 2735 CD1 PHE A1153 4378 2795 4417 -1277 62 -534 C ATOM 2736 CD2 PHE A1153 25.612 12.145 66.323 1.00 25.42 C ANISOU 2736 CD2 PHE A1153 3565 2130 3962 -1030 -92 -394 C ATOM 2737 CE1 PHE A1153 27.646 11.219 64.701 1.00 30.68 C ANISOU 2737 CE1 PHE A1153 4413 2654 4591 -1135 187 -609 C ATOM 2738 CE2 PHE A1153 26.815 11.715 66.873 1.00 27.47 C ANISOU 2738 CE2 PHE A1153 3846 2245 4346 -909 16 -453 C ATOM 2739 CZ PHE A1153 27.826 11.256 66.062 1.00 26.84 C ANISOU 2739 CZ PHE A1153 3848 2087 4261 -950 152 -554 C ATOM 2740 N ARG A1154 21.823 13.901 62.594 1.00 27.63 N ANISOU 2740 N ARG A1154 3746 3048 3705 -1683 -541 -33 N ATOM 2741 CA ARG A1154 20.531 13.791 61.935 1.00 28.52 C ANISOU 2741 CA ARG A1154 3826 3330 3680 -1882 -662 65 C ATOM 2742 C ARG A1154 20.649 14.082 60.421 1.00 35.09 C ANISOU 2742 C ARG A1154 4712 4310 4311 -2124 -706 126 C ATOM 2743 O ARG A1154 20.451 13.174 59.610 1.00 37.36 O ANISOU 2743 O ARG A1154 5120 4676 4397 -2367 -645 39 O ATOM 2744 CB ARG A1154 19.524 14.731 62.614 1.00 25.97 C ANISOU 2744 CB ARG A1154 3308 3054 3506 -1758 -824 232 C ATOM 2745 CG ARG A1154 18.075 14.541 62.195 1.00 30.66 C ANISOU 2745 CG ARG A1154 3832 3813 4004 -1929 -955 343 C ATOM 2746 CD ARG A1154 17.164 15.463 62.978 1.00 45.75 C ANISOU 2746 CD ARG A1154 5529 5738 6118 -1774 -1083 485 C ATOM 2747 NE ARG A1154 17.275 16.862 62.552 1.00 61.87 N ANISOU 2747 NE ARG A1154 7440 7801 8269 -1713 -1202 664 N ATOM 2748 CZ ARG A1154 16.547 17.414 61.584 1.00 81.45 C ANISOU 2748 CZ ARG A1154 9825 10429 10693 -1862 -1367 868 C ATOM 2749 NH1 ARG A1154 15.642 16.694 60.929 1.00 71.70 N ANISOU 2749 NH1 ARG A1154 8611 9356 9274 -2094 -1433 911 N ATOM 2750 NH2 ARG A1154 16.718 18.690 61.262 1.00 68.27 N ANISOU 2750 NH2 ARG A1154 8036 8750 9155 -1792 -1473 1041 N ATOM 2751 N THR A1155 21.059 15.317 60.061 1.00 29.98 N ANISOU 2751 N THR A1155 3985 3692 3713 -2072 -794 263 N ATOM 2752 CA THR A1155 21.153 15.838 58.698 1.00 30.53 C ANISOU 2752 CA THR A1155 4076 3918 3605 -2298 -873 373 C ATOM 2753 C THR A1155 22.388 15.503 57.888 1.00 35.31 C ANISOU 2753 C THR A1155 4838 4510 4068 -2422 -716 223 C ATOM 2754 O THR A1155 22.313 15.550 56.671 1.00 38.55 O ANISOU 2754 O THR A1155 5304 5086 4258 -2696 -753 270 O ATOM 2755 CB THR A1155 20.943 17.358 58.701 1.00 37.23 C ANISOU 2755 CB THR A1155 4754 4796 4597 -2190 -1055 615 C ATOM 2756 OG1 THR A1155 22.091 18.003 59.253 1.00 32.81 O ANISOU 2756 OG1 THR A1155 4188 4082 4196 -1971 -976 564 O ATOM 2757 CG2 THR A1155 19.681 17.784 59.445 1.00 35.97 C ANISOU 2757 CG2 THR A1155 4411 4647 4610 -2070 -1200 763 C ATOM 2758 N GLY A1156 23.521 15.277 58.522 1.00 30.21 N ANISOU 2758 N GLY A1156 4246 3685 3548 -2235 -553 63 N ATOM 2759 CA GLY A1156 24.774 15.056 57.801 1.00 31.56 C ANISOU 2759 CA GLY A1156 4539 3829 3625 -2326 -391 -83 C ATOM 2760 C GLY A1156 25.315 16.308 57.108 1.00 38.68 C ANISOU 2760 C GLY A1156 5395 4813 4490 -2365 -480 58 C ATOM 2761 O GLY A1156 26.099 16.202 56.152 1.00 40.16 O ANISOU 2761 O GLY A1156 5681 5059 4520 -2544 -380 -30 O ATOM 2762 N THR A1157 24.925 17.510 57.616 1.00 34.76 N ANISOU 2762 N THR A1157 4745 4311 4152 -2198 -657 270 N ATOM 2763 CA THR A1157 25.303 18.844 57.123 1.00 35.18 C ANISOU 2763 CA THR A1157 4728 4415 4225 -2201 -774 448 C ATOM 2764 C THR A1157 25.911 19.685 58.243 1.00 37.61 C ANISOU 2764 C THR A1157 4941 4549 4799 -1885 -767 466 C ATOM 2765 O THR A1157 25.706 19.361 59.415 1.00 37.22 O ANISOU 2765 O THR A1157 4849 4380 4914 -1682 -725 395 O ATOM 2766 CB THR A1157 24.049 19.609 56.609 1.00 46.96 C ANISOU 2766 CB THR A1157 6095 6060 5686 -2322 -1020 729 C ATOM 2767 OG1 THR A1157 23.179 19.963 57.701 1.00 47.14 O ANISOU 2767 OG1 THR A1157 5968 5997 5947 -2096 -1116 820 O ATOM 2768 CG2 THR A1157 23.286 18.859 55.525 1.00 46.20 C ANISOU 2768 CG2 THR A1157 6071 6172 5310 -2664 -1064 749 C ATOM 2769 N TRP A1158 26.544 20.829 57.894 1.00 33.25 N ANISOU 2769 N TRP A1158 4348 4000 4287 -1863 -825 581 N ATOM 2770 CA TRP A1158 27.108 21.763 58.873 1.00 31.19 C ANISOU 2770 CA TRP A1158 3995 3588 4268 -1595 -825 608 C ATOM 2771 C TRP A1158 26.113 22.830 59.347 1.00 37.36 C ANISOU 2771 C TRP A1158 4603 4345 5245 -1478 -1006 820 C ATOM 2772 O TRP A1158 26.524 23.767 60.029 1.00 35.04 O ANISOU 2772 O TRP A1158 4229 3935 5150 -1291 -1012 855 O ATOM 2773 CB TRP A1158 28.349 22.442 58.324 1.00 29.46 C ANISOU 2773 CB TRP A1158 3820 3363 4009 -1625 -777 606 C ATOM 2774 CG TRP A1158 29.466 21.503 58.034 1.00 30.27 C ANISOU 2774 CG TRP A1158 4061 3452 3986 -1689 -571 377 C ATOM 2775 CD1 TRP A1158 29.846 21.043 56.808 1.00 34.88 C ANISOU 2775 CD1 TRP A1158 4759 4161 4333 -1951 -502 311 C ATOM 2776 CD2 TRP A1158 30.374 20.929 58.977 1.00 28.37 C ANISOU 2776 CD2 TRP A1158 3848 3063 3868 -1497 -401 187 C ATOM 2777 NE1 TRP A1158 30.938 20.220 56.929 1.00 34.22 N ANISOU 2777 NE1 TRP A1158 4765 3996 4242 -1917 -282 74 N ATOM 2778 CE2 TRP A1158 31.282 20.128 58.253 1.00 33.13 C ANISOU 2778 CE2 TRP A1158 4569 3687 4330 -1633 -228 11 C ATOM 2779 CE3 TRP A1158 30.487 20.982 60.371 1.00 27.78 C ANISOU 2779 CE3 TRP A1158 3702 2848 4007 -1240 -378 151 C ATOM 2780 CZ2 TRP A1158 32.312 19.412 58.870 1.00 31.09 C ANISOU 2780 CZ2 TRP A1158 4344 3297 4173 -1495 -42 -177 C ATOM 2781 CZ3 TRP A1158 31.503 20.259 60.980 1.00 28.45 C ANISOU 2781 CZ3 TRP A1158 3829 2825 4157 -1125 -211 -21 C ATOM 2782 CH2 TRP A1158 32.414 19.506 60.227 1.00 29.55 C ANISOU 2782 CH2 TRP A1158 4069 2971 4187 -1240 -50 -172 C ATOM 2783 N ASP A1159 24.815 22.669 59.029 1.00 37.80 N ANISOU 2783 N ASP A1159 4594 4504 5264 -1587 -1139 950 N ATOM 2784 CA ASP A1159 23.740 23.602 59.386 1.00 39.51 C ANISOU 2784 CA ASP A1159 4623 4701 5690 -1490 -1308 1158 C ATOM 2785 C ASP A1159 23.793 24.224 60.800 1.00 41.15 C ANISOU 2785 C ASP A1159 4717 4725 6194 -1198 -1261 1106 C ATOM 2786 O ASP A1159 23.646 25.446 60.950 1.00 41.64 O ANISOU 2786 O ASP A1159 4645 4713 6462 -1097 -1351 1255 O ATOM 2787 CB ASP A1159 22.363 22.964 59.123 1.00 44.09 C ANISOU 2787 CB ASP A1159 5153 5407 6193 -1623 -1410 1237 C ATOM 2788 CG ASP A1159 21.737 23.354 57.788 1.00 69.29 C ANISOU 2788 CG ASP A1159 8303 8783 9243 -1878 -1600 1490 C ATOM 2789 OD1 ASP A1159 22.314 22.994 56.729 1.00 73.03 O ANISOU 2789 OD1 ASP A1159 8916 9382 9452 -2115 -1574 1466 O ATOM 2790 OD2 ASP A1159 20.650 23.989 57.800 1.00 78.05 O ANISOU 2790 OD2 ASP A1159 9232 9918 10505 -1856 -1775 1713 O ATOM 2791 N ALA A1160 24.004 23.380 61.823 1.00 35.13 N ANISOU 2791 N ALA A1160 4007 3889 5452 -1081 -1119 895 N ATOM 2792 CA ALA A1160 24.054 23.770 63.234 1.00 33.42 C ANISOU 2792 CA ALA A1160 3702 3530 5464 -848 -1054 812 C ATOM 2793 C ALA A1160 25.180 24.763 63.544 1.00 36.17 C ANISOU 2793 C ALA A1160 4042 3768 5932 -726 -1003 797 C ATOM 2794 O ALA A1160 25.060 25.581 64.467 1.00 35.52 O ANISOU 2794 O ALA A1160 3846 3579 6070 -567 -995 796 O ATOM 2795 CB ALA A1160 24.212 22.526 64.088 1.00 33.10 C ANISOU 2795 CB ALA A1160 3749 3464 5364 -805 -920 609 C ATOM 2796 N TYR A1161 26.259 24.689 62.746 1.00 31.57 N ANISOU 2796 N TYR A1161 3579 3218 5197 -818 -959 774 N ATOM 2797 CA TYR A1161 27.457 25.499 62.859 1.00 30.41 C ANISOU 2797 CA TYR A1161 3448 2993 5113 -741 -904 753 C ATOM 2798 C TYR A1161 27.521 26.616 61.804 1.00 38.25 C ANISOU 2798 C TYR A1161 4403 4019 6110 -837 -1029 956 C ATOM 2799 O TYR A1161 28.576 27.195 61.589 1.00 37.31 O ANISOU 2799 O TYR A1161 4325 3867 5985 -830 -989 949 O ATOM 2800 CB TYR A1161 28.693 24.571 62.838 1.00 29.93 C ANISOU 2800 CB TYR A1161 3534 2935 4904 -763 -747 569 C ATOM 2801 CG TYR A1161 28.682 23.588 63.985 1.00 29.38 C ANISOU 2801 CG TYR A1161 3481 2808 4872 -654 -641 407 C ATOM 2802 CD1 TYR A1161 29.077 23.974 65.262 1.00 29.70 C ANISOU 2802 CD1 TYR A1161 3461 2750 5072 -481 -585 341 C ATOM 2803 CD2 TYR A1161 28.192 22.299 63.816 1.00 30.38 C ANISOU 2803 CD2 TYR A1161 3681 2987 4876 -742 -606 332 C ATOM 2804 CE1 TYR A1161 28.964 23.109 66.350 1.00 28.32 C ANISOU 2804 CE1 TYR A1161 3291 2542 4926 -404 -513 224 C ATOM 2805 CE2 TYR A1161 28.078 21.420 64.895 1.00 30.29 C ANISOU 2805 CE2 TYR A1161 3677 2921 4912 -649 -529 214 C ATOM 2806 CZ TYR A1161 28.482 21.823 66.161 1.00 33.21 C ANISOU 2806 CZ TYR A1161 3982 3205 5433 -483 -488 169 C ATOM 2807 OH TYR A1161 28.398 20.950 67.225 1.00 28.08 O ANISOU 2807 OH TYR A1161 3339 2517 4814 -418 -425 73 O ATOM 2808 N LEU A 405 26.397 26.941 61.162 1.00 35.54 N ANISOU 2808 N LEU A 405 5022 5627 2854 387 -1670 572 N ATOM 2809 CA LEU A 405 26.377 28.007 60.160 1.00 37.36 C ANISOU 2809 CA LEU A 405 5239 5811 3144 343 -1579 498 C ATOM 2810 C LEU A 405 25.262 28.986 60.427 1.00 52.26 C ANISOU 2810 C LEU A 405 7104 7750 5004 252 -1585 480 C ATOM 2811 O LEU A 405 24.229 28.610 60.992 1.00 52.11 O ANISOU 2811 O LEU A 405 7109 7788 4902 212 -1650 549 O ATOM 2812 CB LEU A 405 26.258 27.477 58.714 1.00 36.26 C ANISOU 2812 CB LEU A 405 5259 5507 3009 362 -1529 522 C ATOM 2813 CG LEU A 405 27.333 26.527 58.179 1.00 40.45 C ANISOU 2813 CG LEU A 405 5851 5972 3545 502 -1507 529 C ATOM 2814 CD1 LEU A 405 26.867 25.864 56.902 1.00 40.19 C ANISOU 2814 CD1 LEU A 405 6028 5761 3479 510 -1487 558 C ATOM 2815 CD2 LEU A 405 28.657 27.224 57.964 1.00 42.52 C ANISOU 2815 CD2 LEU A 405 5947 6341 3870 564 -1426 456 C ATOM 2816 N HIS A 406 25.472 30.246 59.996 1.00 57.12 N ANISOU 2816 N HIS A 406 7680 8352 5671 225 -1518 395 N ATOM 2817 CA HIS A 406 24.509 31.345 60.100 1.00 60.31 C ANISOU 2817 CA HIS A 406 8095 8780 6040 187 -1511 360 C ATOM 2818 C HIS A 406 24.015 31.716 58.696 1.00 69.64 C ANISOU 2818 C HIS A 406 9385 9840 7236 169 -1441 367 C ATOM 2819 O HIS A 406 24.625 31.293 57.701 1.00 69.77 O ANISOU 2819 O HIS A 406 9448 9759 7302 173 -1390 377 O ATOM 2820 CB HIS A 406 25.137 32.564 60.796 1.00 62.49 C ANISOU 2820 CB HIS A 406 8294 9105 6345 172 -1507 253 C ATOM 2821 CG HIS A 406 25.651 32.264 62.167 1.00 67.55 C ANISOU 2821 CG HIS A 406 8819 9886 6962 188 -1578 240 C ATOM 2822 ND1 HIS A 406 26.972 31.894 62.377 1.00 70.76 N ANISOU 2822 ND1 HIS A 406 9130 10337 7418 192 -1579 225 N ATOM 2823 CD2 HIS A 406 24.998 32.258 63.355 1.00 70.50 C ANISOU 2823 CD2 HIS A 406 9147 10390 7250 211 -1648 247 C ATOM 2824 CE1 HIS A 406 27.084 31.687 63.681 1.00 71.13 C ANISOU 2824 CE1 HIS A 406 9086 10524 7416 212 -1653 222 C ATOM 2825 NE2 HIS A 406 25.924 31.899 64.313 1.00 71.25 N ANISOU 2825 NE2 HIS A 406 9131 10590 7351 221 -1696 233 N ATOM 2826 N MET A 407 22.905 32.499 58.620 1.00 70.20 N ANISOU 2826 N MET A 407 9493 9935 7246 171 -1438 364 N ATOM 2827 CA MET A 407 22.256 32.959 57.379 1.00 71.85 C ANISOU 2827 CA MET A 407 9799 10058 7444 168 -1379 379 C ATOM 2828 C MET A 407 21.902 31.755 56.515 1.00 76.60 C ANISOU 2828 C MET A 407 10468 10615 8021 135 -1384 467 C ATOM 2829 O MET A 407 22.170 31.774 55.313 1.00 76.34 O ANISOU 2829 O MET A 407 10511 10468 8027 128 -1322 464 O ATOM 2830 CB MET A 407 23.159 33.925 56.560 1.00 75.44 C ANISOU 2830 CB MET A 407 10296 10381 7988 150 -1297 307 C ATOM 2831 CG MET A 407 23.663 35.139 57.307 1.00 81.14 C ANISOU 2831 CG MET A 407 10999 11100 8730 139 -1302 213 C ATOM 2832 SD MET A 407 25.017 35.940 56.394 1.00 87.23 S ANISOU 2832 SD MET A 407 11800 11742 9603 43 -1221 163 S ATOM 2833 CE MET A 407 25.865 36.779 57.766 1.00 85.01 C ANISOU 2833 CE MET A 407 11456 11513 9331 -24 -1279 63 C ATOM 2834 N ASN A 408 21.363 30.685 57.118 1.00 74.04 N ANISOU 2834 N ASN A 408 10136 10371 7626 104 -1463 547 N ATOM 2835 CA ASN A 408 21.045 29.489 56.338 1.00 74.70 C ANISOU 2835 CA ASN A 408 10333 10379 7671 47 -1489 628 C ATOM 2836 C ASN A 408 19.950 29.699 55.268 1.00 79.57 C ANISOU 2836 C ASN A 408 11016 10999 8216 -1 -1468 672 C ATOM 2837 O ASN A 408 19.990 29.035 54.225 1.00 78.93 O ANISOU 2837 O ASN A 408 11058 10801 8132 -38 -1457 696 O ATOM 2838 CB ASN A 408 20.821 28.262 57.226 1.00 77.07 C ANISOU 2838 CB ASN A 408 10648 10731 7904 -6 -1590 713 C ATOM 2839 CG ASN A 408 22.101 27.557 57.642 1.00103.99 C ANISOU 2839 CG ASN A 408 14074 14056 11382 61 -1602 688 C ATOM 2840 OD1 ASN A 408 22.997 27.282 56.828 1.00 99.52 O ANISOU 2840 OD1 ASN A 408 13580 13356 10877 125 -1551 649 O ATOM 2841 ND2 ASN A 408 22.189 27.192 58.914 1.00 96.34 N ANISOU 2841 ND2 ASN A 408 13034 13188 10382 64 -1672 721 N ATOM 2842 N ARG A 409 19.029 30.677 55.499 1.00 76.45 N ANISOU 2842 N ARG A 409 10547 10744 7755 25 -1460 673 N ATOM 2843 CA ARG A 409 17.956 31.034 54.562 1.00 76.01 C ANISOU 2843 CA ARG A 409 10524 10744 7613 11 -1439 718 C ATOM 2844 C ARG A 409 18.512 31.697 53.307 1.00 77.20 C ANISOU 2844 C ARG A 409 10759 10727 7846 56 -1344 658 C ATOM 2845 O ARG A 409 18.050 31.376 52.215 1.00 76.88 O ANISOU 2845 O ARG A 409 10796 10655 7762 11 -1331 702 O ATOM 2846 CB ARG A 409 16.878 31.899 55.229 1.00 78.99 C ANISOU 2846 CB ARG A 409 10793 11345 7874 82 -1454 737 C ATOM 2847 CG ARG A 409 15.877 31.082 56.040 1.00 95.96 C ANISOU 2847 CG ARG A 409 12850 13734 9877 -5 -1548 850 C ATOM 2848 CD ARG A 409 14.811 31.952 56.681 1.00114.78 C ANISOU 2848 CD ARG A 409 15103 16392 12117 106 -1554 870 C ATOM 2849 NE ARG A 409 13.966 31.184 57.603 1.00132.66 N ANISOU 2849 NE ARG A 409 17243 18930 14230 13 -1642 987 N ATOM 2850 CZ ARG A 409 13.982 31.311 58.928 1.00152.76 C ANISOU 2850 CZ ARG A 409 19683 21627 16733 69 -1675 977 C ATOM 2851 NH1 ARG A 409 14.789 32.190 59.511 1.00142.56 N ANISOU 2851 NH1 ARG A 409 18403 20230 15535 218 -1635 844 N ATOM 2852 NH2 ARG A 409 13.180 30.566 59.681 1.00141.53 N ANISOU 2852 NH2 ARG A 409 18143 20474 15158 -40 -1753 1105 N ATOM 2853 N GLU A 410 19.520 32.591 53.460 1.00 72.30 N ANISOU 2853 N GLU A 410 10127 10009 7333 122 -1284 565 N ATOM 2854 CA GLU A 410 20.222 33.264 52.355 1.00 71.38 C ANISOU 2854 CA GLU A 410 10083 9743 7296 139 -1192 517 C ATOM 2855 C GLU A 410 21.051 32.222 51.594 1.00 73.00 C ANISOU 2855 C GLU A 410 10341 9843 7553 101 -1171 525 C ATOM 2856 O GLU A 410 20.967 32.143 50.369 1.00 72.25 O ANISOU 2856 O GLU A 410 10328 9678 7446 93 -1123 541 O ATOM 2857 CB GLU A 410 21.141 34.389 52.875 1.00 73.16 C ANISOU 2857 CB GLU A 410 10281 9910 7605 168 -1155 429 C ATOM 2858 CG GLU A 410 20.421 35.681 53.208 1.00 87.34 C ANISOU 2858 CG GLU A 410 12109 11733 9343 241 -1154 400 C ATOM 2859 CD GLU A 410 20.333 36.008 54.686 1.00118.36 C ANISOU 2859 CD GLU A 410 15971 15759 13241 284 -1216 353 C ATOM 2860 OE1 GLU A 410 20.896 37.051 55.093 1.00122.72 O ANISOU 2860 OE1 GLU A 410 16569 16231 13830 297 -1205 270 O ATOM 2861 OE2 GLU A 410 19.686 35.239 55.435 1.00113.37 O ANISOU 2861 OE2 GLU A 410 15254 15285 12536 293 -1280 401 O ATOM 2862 N ARG A 411 21.821 31.403 52.345 1.00 68.29 N ANISOU 2862 N ARG A 411 9705 9246 6995 101 -1210 514 N ATOM 2863 CA ARG A 411 22.666 30.303 51.879 1.00 67.85 C ANISOU 2863 CA ARG A 411 9709 9105 6965 119 -1204 516 C ATOM 2864 C ARG A 411 21.853 29.402 50.951 1.00 71.29 C ANISOU 2864 C ARG A 411 10290 9482 7315 75 -1233 575 C ATOM 2865 O ARG A 411 22.276 29.158 49.823 1.00 70.83 O ANISOU 2865 O ARG A 411 10321 9329 7261 105 -1178 559 O ATOM 2866 CB ARG A 411 23.159 29.510 53.102 1.00 68.37 C ANISOU 2866 CB ARG A 411 9724 9215 7040 141 -1276 522 C ATOM 2867 CG ARG A 411 24.338 28.572 52.861 1.00 77.21 C ANISOU 2867 CG ARG A 411 10884 10264 8187 226 -1261 506 C ATOM 2868 CD ARG A 411 24.900 28.063 54.182 1.00 81.67 C ANISOU 2868 CD ARG A 411 11370 10898 8762 269 -1326 510 C ATOM 2869 NE ARG A 411 25.374 29.160 55.031 1.00 89.01 N ANISOU 2869 NE ARG A 411 12125 11944 9750 257 -1307 456 N ATOM 2870 CZ ARG A 411 26.588 29.702 54.957 1.00108.94 C ANISOU 2870 CZ ARG A 411 14541 14514 12339 292 -1244 400 C ATOM 2871 NH1 ARG A 411 27.479 29.241 54.084 1.00 96.26 N ANISOU 2871 NH1 ARG A 411 12953 12879 10742 372 -1184 394 N ATOM 2872 NH2 ARG A 411 26.923 30.705 55.758 1.00 99.50 N ANISOU 2872 NH2 ARG A 411 13217 13409 11179 241 -1246 351 N ATOM 2873 N LYS A 412 20.662 28.961 51.417 1.00 68.15 N ANISOU 2873 N LYS A 412 9909 9164 6820 -7 -1322 647 N ATOM 2874 CA LYS A 412 19.727 28.124 50.668 1.00 68.62 C ANISOU 2874 CA LYS A 412 10102 9200 6771 -105 -1377 716 C ATOM 2875 C LYS A 412 19.287 28.843 49.376 1.00 72.17 C ANISOU 2875 C LYS A 412 10580 9643 7196 -102 -1305 709 C ATOM 2876 O LYS A 412 19.488 28.305 48.280 1.00 72.38 O ANISOU 2876 O LYS A 412 10743 9556 7203 -109 -1285 700 O ATOM 2877 CB LYS A 412 18.515 27.747 51.548 1.00 71.80 C ANISOU 2877 CB LYS A 412 10458 9764 7059 -224 -1483 810 C ATOM 2878 CG LYS A 412 18.469 26.274 51.942 1.00 92.79 C ANISOU 2878 CG LYS A 412 13251 12350 9654 -326 -1593 875 C ATOM 2879 CD LYS A 412 17.119 25.633 51.570 1.00107.63 C ANISOU 2879 CD LYS A 412 15208 14312 11372 -526 -1686 984 C ATOM 2880 CE LYS A 412 17.139 24.114 51.536 1.00117.31 C ANISOU 2880 CE LYS A 412 16671 15376 12525 -657 -1797 1042 C ATOM 2881 NZ LYS A 412 15.851 23.540 51.053 1.00120.01 N ANISOU 2881 NZ LYS A 412 17100 15801 12697 -900 -1895 1149 N ATOM 2882 N ALA A 413 18.765 30.089 49.514 1.00 67.61 N ANISOU 2882 N ALA A 413 9892 9179 6616 -66 -1265 706 N ATOM 2883 CA ALA A 413 18.306 30.954 48.419 1.00 67.10 C ANISOU 2883 CA ALA A 413 9848 9122 6523 -38 -1198 709 C ATOM 2884 C ALA A 413 19.386 31.266 47.365 1.00 69.04 C ANISOU 2884 C ALA A 413 10162 9214 6857 17 -1095 649 C ATOM 2885 O ALA A 413 19.044 31.458 46.195 1.00 68.49 O ANISOU 2885 O ALA A 413 10160 9123 6741 13 -1054 668 O ATOM 2886 CB ALA A 413 17.734 32.247 48.978 1.00 67.88 C ANISOU 2886 CB ALA A 413 9847 9342 6603 39 -1179 706 C ATOM 2887 N ALA A 414 20.675 31.315 47.782 1.00 64.53 N ANISOU 2887 N ALA A 414 9553 8569 6395 63 -1056 588 N ATOM 2888 CA ALA A 414 21.828 31.570 46.911 1.00 64.18 C ANISOU 2888 CA ALA A 414 9530 8435 6419 107 -958 543 C ATOM 2889 C ALA A 414 22.110 30.376 45.995 1.00 68.60 C ANISOU 2889 C ALA A 414 10211 8919 6933 124 -957 545 C ATOM 2890 O ALA A 414 22.429 30.578 44.822 1.00 68.48 O ANISOU 2890 O ALA A 414 10247 8864 6907 152 -879 535 O ATOM 2891 CB ALA A 414 23.057 31.896 47.739 1.00 65.00 C ANISOU 2891 CB ALA A 414 9527 8548 6623 136 -932 491 C ATOM 2892 N LYS A 415 21.980 29.137 46.527 1.00 65.35 N ANISOU 2892 N LYS A 415 9868 8481 6480 112 -1048 558 N ATOM 2893 CA LYS A 415 22.163 27.898 45.767 1.00 65.92 C ANISOU 2893 CA LYS A 415 10120 8444 6484 138 -1072 552 C ATOM 2894 C LYS A 415 21.070 27.843 44.698 1.00 69.85 C ANISOU 2894 C LYS A 415 10729 8933 6878 50 -1089 589 C ATOM 2895 O LYS A 415 21.369 27.521 43.548 1.00 69.76 O ANISOU 2895 O LYS A 415 10836 8846 6823 94 -1044 562 O ATOM 2896 CB LYS A 415 22.094 26.670 46.699 1.00 69.05 C ANISOU 2896 CB LYS A 415 10604 8788 6843 119 -1187 573 C ATOM 2897 CG LYS A 415 22.298 25.316 46.006 1.00 88.37 C ANISOU 2897 CG LYS A 415 13302 11073 9200 160 -1233 559 C ATOM 2898 CD LYS A 415 21.315 24.257 46.529 1.00100.05 C ANISOU 2898 CD LYS A 415 14946 12492 10578 8 -1384 628 C ATOM 2899 CE LYS A 415 21.252 23.025 45.653 1.00110.63 C ANISOU 2899 CE LYS A 415 16600 13635 11799 2 -1447 614 C ATOM 2900 NZ LYS A 415 19.850 22.653 45.320 1.00117.67 N ANISOU 2900 NZ LYS A 415 17613 14534 12563 -243 -1554 687 N ATOM 2901 N GLN A 416 19.818 28.206 45.072 1.00 66.27 N ANISOU 2901 N GLN A 416 10220 8590 6369 -63 -1150 652 N ATOM 2902 CA GLN A 416 18.674 28.249 44.160 1.00 66.46 C ANISOU 2902 CA GLN A 416 10306 8670 6275 -155 -1175 703 C ATOM 2903 C GLN A 416 18.917 29.251 43.035 1.00 70.26 C ANISOU 2903 C GLN A 416 10765 9151 6781 -79 -1057 681 C ATOM 2904 O GLN A 416 18.697 28.891 41.881 1.00 70.61 O ANISOU 2904 O GLN A 416 10928 9155 6743 -101 -1048 682 O ATOM 2905 CB GLN A 416 17.376 28.585 44.900 1.00 67.77 C ANISOU 2905 CB GLN A 416 10358 9025 6366 -253 -1250 784 C ATOM 2906 CG GLN A 416 16.127 28.306 44.067 1.00 83.05 C ANISOU 2906 CG GLN A 416 12349 11066 8142 -380 -1308 855 C ATOM 2907 CD GLN A 416 14.967 29.187 44.448 1.00101.60 C ANISOU 2907 CD GLN A 416 14526 13666 10413 -389 -1322 929 C ATOM 2908 OE1 GLN A 416 15.057 30.418 44.424 1.00 98.75 O ANISOU 2908 OE1 GLN A 416 14070 13347 10104 -250 -1236 909 O ATOM 2909 NE2 GLN A 416 13.832 28.577 44.750 1.00 90.08 N ANISOU 2909 NE2 GLN A 416 13036 12386 8804 -550 -1433 1023 N ATOM 2910 N LEU A 417 19.388 30.489 43.361 1.00 66.20 N ANISOU 2910 N LEU A 417 10121 8667 6365 -1 -974 661 N ATOM 2911 CA LEU A 417 19.698 31.519 42.360 1.00 66.13 C ANISOU 2911 CA LEU A 417 10107 8640 6379 55 -864 654 C ATOM 2912 C LEU A 417 20.779 31.028 41.399 1.00 71.90 C ANISOU 2912 C LEU A 417 10915 9277 7126 105 -791 609 C ATOM 2913 O LEU A 417 20.613 31.160 40.184 1.00 71.94 O ANISOU 2913 O LEU A 417 10991 9275 7068 113 -742 622 O ATOM 2914 CB LEU A 417 20.076 32.866 43.000 1.00 65.53 C ANISOU 2914 CB LEU A 417 9925 8577 6397 99 -809 642 C ATOM 2915 CG LEU A 417 20.681 33.954 42.085 1.00 70.34 C ANISOU 2915 CG LEU A 417 10551 9132 7044 131 -696 640 C ATOM 2916 CD1 LEU A 417 19.702 34.408 40.983 1.00 70.45 C ANISOU 2916 CD1 LEU A 417 10635 9178 6955 143 -676 699 C ATOM 2917 CD2 LEU A 417 21.127 35.143 42.895 1.00 72.73 C ANISOU 2917 CD2 LEU A 417 10794 9409 7431 137 -671 621 C ATOM 2918 N GLY A 418 21.832 30.423 41.950 1.00 68.99 N ANISOU 2918 N GLY A 418 10528 8863 6820 156 -788 561 N ATOM 2919 CA GLY A 418 22.924 29.832 41.184 1.00 69.72 C ANISOU 2919 CA GLY A 418 10678 8907 6905 250 -723 515 C ATOM 2920 C GLY A 418 22.456 28.738 40.244 1.00 74.62 C ANISOU 2920 C GLY A 418 11497 9455 7399 255 -767 506 C ATOM 2921 O GLY A 418 22.924 28.665 39.111 1.00 74.81 O ANISOU 2921 O GLY A 418 11585 9466 7375 326 -691 482 O ATOM 2922 N PHE A 419 21.510 27.900 40.700 1.00 72.01 N ANISOU 2922 N PHE A 419 11274 9086 7001 162 -894 529 N ATOM 2923 CA PHE A 419 20.922 26.819 39.914 1.00 73.53 C ANISOU 2923 CA PHE A 419 11692 9191 7055 112 -970 523 C ATOM 2924 C PHE A 419 20.161 27.430 38.728 1.00 76.89 C ANISOU 2924 C PHE A 419 12130 9684 7402 54 -932 555 C ATOM 2925 O PHE A 419 20.376 27.000 37.593 1.00 77.16 O ANISOU 2925 O PHE A 419 12308 9660 7351 101 -902 517 O ATOM 2926 CB PHE A 419 19.981 25.974 40.795 1.00 76.34 C ANISOU 2926 CB PHE A 419 12131 9524 7350 -39 -1125 570 C ATOM 2927 CG PHE A 419 20.184 24.475 40.758 1.00 80.39 C ANISOU 2927 CG PHE A 419 12913 9857 7774 -39 -1222 536 C ATOM 2928 CD1 PHE A 419 19.677 23.712 39.711 1.00 85.31 C ANISOU 2928 CD1 PHE A 419 13782 10382 8249 -112 -1282 521 C ATOM 2929 CD2 PHE A 419 20.832 23.818 41.802 1.00 83.97 C ANISOU 2929 CD2 PHE A 419 13399 10228 8277 31 -1268 522 C ATOM 2930 CE1 PHE A 419 19.839 22.320 39.692 1.00 88.36 C ANISOU 2930 CE1 PHE A 419 14477 10558 8536 -114 -1388 485 C ATOM 2931 CE2 PHE A 419 20.986 22.423 41.789 1.00 88.75 C ANISOU 2931 CE2 PHE A 419 14303 10634 8785 46 -1369 496 C ATOM 2932 CZ PHE A 419 20.496 21.685 40.728 1.00 88.15 C ANISOU 2932 CZ PHE A 419 14503 10429 8560 -26 -1430 474 C ATOM 2933 N ILE A 420 19.321 28.474 38.989 1.00 72.41 N ANISOU 2933 N ILE A 420 11412 9247 6852 -18 -927 621 N ATOM 2934 CA ILE A 420 18.545 29.222 37.982 1.00 71.77 C ANISOU 2934 CA ILE A 420 11316 9259 6696 -48 -891 668 C ATOM 2935 C ILE A 420 19.489 29.819 36.921 1.00 77.16 C ANISOU 2935 C ILE A 420 12000 9908 7410 68 -751 636 C ATOM 2936 O ILE A 420 19.321 29.528 35.738 1.00 76.96 O ANISOU 2936 O ILE A 420 12087 9875 7280 70 -734 629 O ATOM 2937 CB ILE A 420 17.573 30.257 38.645 1.00 73.23 C ANISOU 2937 CB ILE A 420 11342 9595 6887 -85 -910 742 C ATOM 2938 CG1 ILE A 420 16.275 29.559 39.111 1.00 73.24 C ANISOU 2938 CG1 ILE A 420 11350 9712 6764 -233 -1051 804 C ATOM 2939 CG2 ILE A 420 17.254 31.448 37.726 1.00 73.29 C ANISOU 2939 CG2 ILE A 420 11308 9672 6866 -27 -824 784 C ATOM 2940 CD1 ILE A 420 15.359 30.377 40.058 1.00 74.26 C ANISOU 2940 CD1 ILE A 420 11302 10031 6880 -236 -1083 874 C ATOM 2941 N MET A 421 20.516 30.582 37.361 1.00 75.53 N ANISOU 2941 N MET A 421 11672 9692 7333 147 -659 618 N ATOM 2942 CA MET A 421 21.537 31.187 36.500 1.00 76.90 C ANISOU 2942 CA MET A 421 11815 9868 7537 227 -525 606 C ATOM 2943 C MET A 421 22.312 30.129 35.737 1.00 82.61 C ANISOU 2943 C MET A 421 12650 10546 8191 317 -497 543 C ATOM 2944 O MET A 421 22.588 30.334 34.562 1.00 83.33 O ANISOU 2944 O MET A 421 12777 10668 8217 364 -414 546 O ATOM 2945 CB MET A 421 22.505 32.061 37.305 1.00 79.47 C ANISOU 2945 CB MET A 421 11987 10207 7999 245 -460 604 C ATOM 2946 CG MET A 421 22.001 33.467 37.523 1.00 83.68 C ANISOU 2946 CG MET A 421 12458 10760 8575 195 -438 663 C ATOM 2947 SD MET A 421 23.081 34.470 38.581 1.00 89.04 S ANISOU 2947 SD MET A 421 13002 11429 9399 168 -393 651 S ATOM 2948 CE MET A 421 24.403 34.848 37.445 1.00 87.25 C ANISOU 2948 CE MET A 421 12740 11241 9169 171 -253 667 C ATOM 2949 N ALA A 422 22.631 28.986 36.384 1.00 79.87 N ANISOU 2949 N ALA A 422 12378 10128 7841 359 -569 488 N ATOM 2950 CA ALA A 422 23.354 27.881 35.752 1.00 81.35 C ANISOU 2950 CA ALA A 422 12717 10252 7941 493 -557 416 C ATOM 2951 C ALA A 422 22.560 27.251 34.614 1.00 86.76 C ANISOU 2951 C ALA A 422 13619 10881 8467 458 -605 401 C ATOM 2952 O ALA A 422 23.166 26.765 33.666 1.00 87.74 O ANISOU 2952 O ALA A 422 13856 10986 8498 588 -550 344 O ATOM 2953 CB ALA A 422 23.716 26.823 36.778 1.00 82.44 C ANISOU 2953 CB ALA A 422 12927 10298 8097 550 -644 373 C ATOM 2954 N ALA A 423 21.217 27.264 34.701 1.00 83.32 N ANISOU 2954 N ALA A 423 13231 10446 7982 285 -708 451 N ATOM 2955 CA ALA A 423 20.340 26.707 33.671 1.00 84.18 C ANISOU 2955 CA ALA A 423 13530 10529 7925 203 -773 446 C ATOM 2956 C ALA A 423 20.276 27.629 32.452 1.00 88.71 C ANISOU 2956 C ALA A 423 14040 11212 8455 234 -664 477 C ATOM 2957 O ALA A 423 20.478 27.169 31.328 1.00 89.85 O ANISOU 2957 O ALA A 423 14332 11330 8476 297 -637 429 O ATOM 2958 CB ALA A 423 18.945 26.479 34.235 1.00 84.57 C ANISOU 2958 CB ALA A 423 13600 10611 7922 -10 -920 511 C ATOM 2959 N PHE A 424 20.023 28.933 32.688 1.00 84.51 N ANISOU 2959 N PHE A 424 13307 10790 8012 202 -602 557 N ATOM 2960 CA PHE A 424 19.898 29.984 31.673 1.00 84.74 C ANISOU 2960 CA PHE A 424 13273 10916 8010 222 -502 613 C ATOM 2961 C PHE A 424 21.162 30.228 30.840 1.00 90.30 C ANISOU 2961 C PHE A 424 13958 11632 8718 356 -358 584 C ATOM 2962 O PHE A 424 21.050 30.688 29.708 1.00 90.33 O ANISOU 2962 O PHE A 424 13982 11702 8639 373 -290 618 O ATOM 2963 CB PHE A 424 19.412 31.283 32.322 1.00 85.43 C ANISOU 2963 CB PHE A 424 13194 11075 8190 181 -484 700 C ATOM 2964 CG PHE A 424 18.684 32.222 31.394 1.00 87.16 C ANISOU 2964 CG PHE A 424 13399 11389 8330 174 -443 782 C ATOM 2965 CD1 PHE A 424 17.321 32.082 31.167 1.00 90.33 C ANISOU 2965 CD1 PHE A 424 13828 11888 8605 98 -539 831 C ATOM 2966 CD2 PHE A 424 19.350 33.279 30.786 1.00 89.61 C ANISOU 2966 CD2 PHE A 424 13660 11707 8680 237 -314 824 C ATOM 2967 CE1 PHE A 424 16.642 32.961 30.321 1.00 91.63 C ANISOU 2967 CE1 PHE A 424 13973 12161 8682 122 -503 914 C ATOM 2968 CE2 PHE A 424 18.671 34.158 29.939 1.00 92.82 C ANISOU 2968 CE2 PHE A 424 14077 12187 9005 246 -280 910 C ATOM 2969 CZ PHE A 424 17.319 33.998 29.718 1.00 90.97 C ANISOU 2969 CZ PHE A 424 13869 12052 8644 207 -373 952 C ATOM 2970 N ILE A 425 22.351 29.938 31.387 1.00 87.74 N ANISOU 2970 N ILE A 425 13581 11279 8477 452 -309 532 N ATOM 2971 CA ILE A 425 23.602 30.102 30.641 1.00 88.89 C ANISOU 2971 CA ILE A 425 13674 11498 8602 582 -171 514 C ATOM 2972 C ILE A 425 23.895 28.790 29.883 1.00 97.47 C ANISOU 2972 C ILE A 425 14959 12539 9535 718 -189 416 C ATOM 2973 O ILE A 425 24.408 28.828 28.767 1.00 98.42 O ANISOU 2973 O ILE A 425 15101 12741 9552 820 -92 404 O ATOM 2974 CB ILE A 425 24.778 30.625 31.530 1.00 91.12 C ANISOU 2974 CB ILE A 425 13759 11837 9025 616 -98 525 C ATOM 2975 CG1 ILE A 425 24.404 31.886 32.372 1.00 89.68 C ANISOU 2975 CG1 ILE A 425 13441 11653 8981 475 -106 604 C ATOM 2976 CG2 ILE A 425 26.064 30.854 30.733 1.00 93.09 C ANISOU 2976 CG2 ILE A 425 13909 12231 9228 728 49 530 C ATOM 2977 CD1 ILE A 425 23.566 33.008 31.710 1.00 95.08 C ANISOU 2977 CD1 ILE A 425 14136 12351 9639 387 -80 694 C ATOM 2978 N LEU A 426 23.483 27.644 30.464 1.00 96.09 N ANISOU 2978 N LEU A 426 14956 12225 9328 712 -322 350 N ATOM 2979 CA LEU A 426 23.621 26.299 29.893 1.00 98.24 C ANISOU 2979 CA LEU A 426 15497 12387 9443 831 -378 247 C ATOM 2980 C LEU A 426 22.712 26.119 28.668 1.00104.69 C ANISOU 2980 C LEU A 426 16490 13195 10094 754 -416 240 C ATOM 2981 O LEU A 426 23.051 25.361 27.756 1.00105.90 O ANISOU 2981 O LEU A 426 16841 13306 10090 889 -405 154 O ATOM 2982 CB LEU A 426 23.231 25.266 30.962 1.00 98.12 C ANISOU 2982 CB LEU A 426 15640 12199 9444 777 -534 208 C ATOM 2983 CG LEU A 426 23.780 23.861 30.810 1.00104.47 C ANISOU 2983 CG LEU A 426 16729 12843 10123 957 -589 94 C ATOM 2984 CD1 LEU A 426 24.626 23.491 32.008 1.00104.41 C ANISOU 2984 CD1 LEU A 426 16658 12796 10217 1083 -596 76 C ATOM 2985 CD2 LEU A 426 22.654 22.861 30.610 1.00107.28 C ANISOU 2985 CD2 LEU A 426 17411 13010 10340 794 -765 62 C ATOM 2986 N CYS A 427 21.556 26.804 28.665 1.00101.83 N ANISOU 2986 N CYS A 427 16057 12886 9749 554 -466 327 N ATOM 2987 CA CYS A 427 20.533 26.718 27.623 1.00103.21 C ANISOU 2987 CA CYS A 427 16359 13091 9763 446 -521 341 C ATOM 2988 C CYS A 427 20.657 27.722 26.470 1.00107.37 C ANISOU 2988 C CYS A 427 16777 13773 10245 496 -387 398 C ATOM 2989 O CYS A 427 20.305 27.390 25.334 1.00108.04 O ANISOU 2989 O CYS A 427 17009 13883 10159 498 -399 369 O ATOM 2990 CB CYS A 427 19.146 26.778 28.254 1.00103.11 C ANISOU 2990 CB CYS A 427 16327 13095 9754 216 -662 412 C ATOM 2991 SG CYS A 427 18.727 25.338 29.271 1.00107.75 S ANISOU 2991 SG CYS A 427 17130 13500 10310 91 -855 357 S ATOM 2992 N TRP A 428 21.094 28.956 26.771 1.00102.93 N ANISOU 2992 N TRP A 428 15978 13307 9824 514 -273 485 N ATOM 2993 CA TRP A 428 21.181 30.034 25.795 1.00102.88 C ANISOU 2993 CA TRP A 428 15872 13432 9786 534 -152 568 C ATOM 2994 C TRP A 428 22.562 30.351 25.231 1.00109.33 C ANISOU 2994 C TRP A 428 16603 14333 10606 680 11 563 C ATOM 2995 O TRP A 428 22.623 30.731 24.061 1.00110.09 O ANISOU 2995 O TRP A 428 16710 14531 10590 715 93 599 O ATOM 2996 CB TRP A 428 20.501 31.298 26.319 1.00 99.96 C ANISOU 2996 CB TRP A 428 15348 13109 9524 427 -151 689 C ATOM 2997 CG TRP A 428 19.006 31.225 26.336 1.00100.40 C ANISOU 2997 CG TRP A 428 15454 13195 9497 307 -279 730 C ATOM 2998 CD1 TRP A 428 18.205 31.075 27.430 1.00102.28 C ANISOU 2998 CD1 TRP A 428 15657 13415 9790 208 -396 746 C ATOM 2999 CD2 TRP A 428 18.131 31.342 25.210 1.00100.96 C ANISOU 2999 CD2 TRP A 428 15592 13369 9400 272 -300 774 C ATOM 3000 NE1 TRP A 428 16.882 31.095 27.055 1.00101.97 N ANISOU 3000 NE1 TRP A 428 15640 13483 9619 112 -487 803 N ATOM 3001 CE2 TRP A 428 16.806 31.270 25.698 1.00104.41 C ANISOU 3001 CE2 TRP A 428 16012 13866 9792 148 -433 820 C ATOM 3002 CE3 TRP A 428 18.335 31.511 23.831 1.00103.22 C ANISOU 3002 CE3 TRP A 428 15935 13730 9553 334 -218 785 C ATOM 3003 CZ2 TRP A 428 15.691 31.346 24.856 1.00104.45 C ANISOU 3003 CZ2 TRP A 428 16048 14017 9622 83 -491 877 C ATOM 3004 CZ3 TRP A 428 17.230 31.587 22.998 1.00105.44 C ANISOU 3004 CZ3 TRP A 428 16266 14126 9670 272 -277 835 C ATOM 3005 CH2 TRP A 428 15.927 31.500 23.510 1.00105.59 C ANISOU 3005 CH2 TRP A 428 16259 14214 9645 146 -415 881 C ATOM 3006 N ILE A 429 23.611 30.137 26.017 1.00106.76 N ANISOU 3006 N ILE A 429 16190 13993 10382 762 51 523 N ATOM 3007 CA ILE A 429 24.981 30.344 25.567 1.00108.19 C ANISOU 3007 CA ILE A 429 16253 14311 10544 900 201 524 C ATOM 3008 C ILE A 429 25.251 29.750 24.185 1.00114.41 C ANISOU 3008 C ILE A 429 17170 15180 11122 1048 260 468 C ATOM 3009 O ILE A 429 25.646 30.472 23.269 1.00114.81 O ANISOU 3009 O ILE A 429 17127 15388 11110 1063 383 541 O ATOM 3010 CB ILE A 429 25.996 29.758 26.568 1.00111.66 C ANISOU 3010 CB ILE A 429 16621 14741 11064 1010 204 459 C ATOM 3011 CG1 ILE A 429 27.187 30.703 26.735 1.00112.51 C ANISOU 3011 CG1 ILE A 429 16467 15031 11253 1011 344 539 C ATOM 3012 CG2 ILE A 429 26.460 28.382 26.113 1.00114.49 C ANISOU 3012 CG2 ILE A 429 17165 15072 11265 1232 188 329 C ATOM 3013 CD1 ILE A 429 27.138 31.529 28.002 1.00118.90 C ANISOU 3013 CD1 ILE A 429 17127 15790 12258 851 309 601 C ATOM 3014 N PRO A 430 25.050 28.443 24.028 1.00112.12 N ANISOU 3014 N PRO A 430 17113 14776 10710 1154 169 340 N ATOM 3015 CA PRO A 430 25.391 27.797 22.747 1.00114.31 C ANISOU 3015 CA PRO A 430 17545 15119 10767 1331 221 261 C ATOM 3016 C PRO A 430 24.783 28.516 21.534 1.00119.53 C ANISOU 3016 C PRO A 430 18204 15890 11323 1245 270 338 C ATOM 3017 O PRO A 430 25.454 28.632 20.511 1.00120.69 O ANISOU 3017 O PRO A 430 18319 16201 11336 1381 393 340 O ATOM 3018 CB PRO A 430 24.838 26.376 22.908 1.00116.56 C ANISOU 3018 CB PRO A 430 18155 15184 10948 1372 60 122 C ATOM 3019 CG PRO A 430 23.803 26.484 23.962 1.00118.62 C ANISOU 3019 CG PRO A 430 18415 15304 11351 1136 -82 168 C ATOM 3020 CD PRO A 430 24.337 27.494 24.911 1.00112.68 C ANISOU 3020 CD PRO A 430 17364 14638 10811 1092 -2 265 C ATOM 3021 N TYR A 431 23.535 29.030 21.668 1.00115.48 N ANISOU 3021 N TYR A 431 17704 15314 10860 1034 179 412 N ATOM 3022 CA TYR A 431 22.812 29.778 20.632 1.00115.85 C ANISOU 3022 CA TYR A 431 17742 15463 10811 948 207 503 C ATOM 3023 C TYR A 431 23.432 31.158 20.393 1.00120.39 C ANISOU 3023 C TYR A 431 18086 16189 11465 931 364 649 C ATOM 3024 O TYR A 431 23.517 31.586 19.243 1.00121.47 O ANISOU 3024 O TYR A 431 18217 16462 11474 964 453 705 O ATOM 3025 CB TYR A 431 21.313 29.894 20.994 1.00115.77 C ANISOU 3025 CB TYR A 431 17789 15376 10821 753 57 546 C ATOM 3026 CG TYR A 431 20.538 30.946 20.222 1.00117.24 C ANISOU 3026 CG TYR A 431 17908 15685 10952 671 88 677 C ATOM 3027 CD1 TYR A 431 20.116 30.713 18.917 1.00120.59 C ANISOU 3027 CD1 TYR A 431 18453 16201 11165 692 87 665 C ATOM 3028 CD2 TYR A 431 20.190 32.158 20.814 1.00116.59 C ANISOU 3028 CD2 TYR A 431 17664 15621 11013 587 110 811 C ATOM 3029 CE1 TYR A 431 19.401 31.677 18.205 1.00121.48 C ANISOU 3029 CE1 TYR A 431 18504 16439 11214 635 114 795 C ATOM 3030 CE2 TYR A 431 19.464 33.124 20.116 1.00117.53 C ANISOU 3030 CE2 TYR A 431 17749 15841 11067 547 134 937 C ATOM 3031 CZ TYR A 431 19.062 32.874 18.815 1.00125.96 C ANISOU 3031 CZ TYR A 431 18918 17016 11927 572 136 934 C ATOM 3032 OH TYR A 431 18.352 33.821 18.118 1.00126.38 O ANISOU 3032 OH TYR A 431 18937 17181 11903 551 158 1066 O ATOM 3033 N PHE A 432 23.822 31.863 21.473 1.00116.07 N ANISOU 3033 N PHE A 432 17370 15614 11119 861 388 714 N ATOM 3034 CA PHE A 432 24.436 33.187 21.379 1.00116.28 C ANISOU 3034 CA PHE A 432 17210 15745 11224 800 517 856 C ATOM 3035 C PHE A 432 25.865 33.126 20.876 1.00123.29 C ANISOU 3035 C PHE A 432 17980 16817 12047 916 665 857 C ATOM 3036 O PHE A 432 26.332 34.088 20.261 1.00123.62 O ANISOU 3036 O PHE A 432 17911 16997 12062 862 783 983 O ATOM 3037 CB PHE A 432 24.314 33.972 22.690 1.00116.39 C ANISOU 3037 CB PHE A 432 17117 15655 11450 669 476 918 C ATOM 3038 CG PHE A 432 22.992 34.690 22.810 1.00116.67 C ANISOU 3038 CG PHE A 432 17209 15607 11512 562 394 997 C ATOM 3039 CD1 PHE A 432 21.923 34.106 23.478 1.00118.33 C ANISOU 3039 CD1 PHE A 432 17500 15720 11742 529 247 939 C ATOM 3040 CD2 PHE A 432 22.806 35.940 22.230 1.00119.08 C ANISOU 3040 CD2 PHE A 432 17492 15952 11803 503 462 1140 C ATOM 3041 CE1 PHE A 432 20.696 34.766 23.577 1.00118.42 C ANISOU 3041 CE1 PHE A 432 17533 15715 11748 460 177 1019 C ATOM 3042 CE2 PHE A 432 21.574 36.595 22.323 1.00121.08 C ANISOU 3042 CE2 PHE A 432 17802 16147 12055 456 388 1214 C ATOM 3043 CZ PHE A 432 20.531 36.006 23.003 1.00117.97 C ANISOU 3043 CZ PHE A 432 17453 15697 11671 446 249 1152 C ATOM 3044 N ILE A 433 26.557 31.995 21.112 1.00122.02 N ANISOU 3044 N ILE A 433 17849 16674 11840 1085 659 725 N ATOM 3045 CA ILE A 433 27.908 31.787 20.598 1.00124.59 C ANISOU 3045 CA ILE A 433 18050 17228 12059 1251 800 714 C ATOM 3046 C ILE A 433 27.829 31.323 19.121 1.00132.41 C ANISOU 3046 C ILE A 433 19172 18334 12803 1397 853 672 C ATOM 3047 O ILE A 433 28.817 31.416 18.394 1.00134.13 O ANISOU 3047 O ILE A 433 19268 18802 12893 1520 994 703 O ATOM 3048 CB ILE A 433 28.789 30.905 21.534 1.00127.92 C ANISOU 3048 CB ILE A 433 18423 17655 12526 1409 784 607 C ATOM 3049 CG1 ILE A 433 30.274 31.290 21.453 1.00130.06 C ANISOU 3049 CG1 ILE A 433 18422 18230 12766 1487 942 674 C ATOM 3050 CG2 ILE A 433 28.568 29.404 21.349 1.00129.22 C ANISOU 3050 CG2 ILE A 433 18849 17697 12552 1628 696 429 C ATOM 3051 CD1 ILE A 433 30.711 32.282 22.502 1.00136.67 C ANISOU 3051 CD1 ILE A 433 19031 19094 13803 1278 958 786 C ATOM 3052 N PHE A 434 26.627 30.865 18.688 1.00129.75 N ANISOU 3052 N PHE A 434 19069 17840 12388 1367 737 611 N ATOM 3053 CA PHE A 434 26.296 30.444 17.319 1.00131.64 C ANISOU 3053 CA PHE A 434 19473 18154 12391 1466 753 564 C ATOM 3054 C PHE A 434 25.938 31.683 16.491 1.00136.22 C ANISOU 3054 C PHE A 434 19954 18859 12944 1326 832 735 C ATOM 3055 O PHE A 434 26.028 31.659 15.263 1.00137.60 O ANISOU 3055 O PHE A 434 20173 19187 12921 1411 905 744 O ATOM 3056 CB PHE A 434 25.116 29.457 17.336 1.00133.20 C ANISOU 3056 CB PHE A 434 19960 18130 12519 1437 571 437 C ATOM 3057 CG PHE A 434 25.008 28.547 16.138 1.00137.22 C ANISOU 3057 CG PHE A 434 20706 18672 12761 1593 558 314 C ATOM 3058 CD1 PHE A 434 25.901 27.496 15.959 1.00142.41 C ANISOU 3058 CD1 PHE A 434 21486 19343 13281 1862 588 165 C ATOM 3059 CD2 PHE A 434 23.982 28.703 15.216 1.00140.08 C ANISOU 3059 CD2 PHE A 434 21187 19047 12990 1487 503 340 C ATOM 3060 CE1 PHE A 434 25.794 26.646 14.854 1.00145.58 C ANISOU 3060 CE1 PHE A 434 22146 19752 13415 2023 567 35 C ATOM 3061 CE2 PHE A 434 23.872 27.845 14.115 1.00145.06 C ANISOU 3061 CE2 PHE A 434 22058 19701 13358 1620 478 214 C ATOM 3062 CZ PHE A 434 24.769 26.813 13.950 1.00144.93 C ANISOU 3062 CZ PHE A 434 22188 19671 13208 1886 507 56 C ATOM 3063 N PHE A 435 25.523 32.758 17.182 1.00131.61 N ANISOU 3063 N PHE A 435 19258 18199 12548 1126 813 868 N ATOM 3064 CA PHE A 435 25.196 34.066 16.627 1.00131.74 C ANISOU 3064 CA PHE A 435 19202 18285 12570 990 877 1049 C ATOM 3065 C PHE A 435 26.502 34.804 16.370 1.00137.98 C ANISOU 3065 C PHE A 435 19789 19278 13359 981 1046 1165 C ATOM 3066 O PHE A 435 26.593 35.576 15.420 1.00138.49 O ANISOU 3066 O PHE A 435 19818 19480 13323 935 1140 1299 O ATOM 3067 CB PHE A 435 24.329 34.848 17.622 1.00131.56 C ANISOU 3067 CB PHE A 435 19169 18078 12738 819 781 1126 C ATOM 3068 CG PHE A 435 22.970 35.249 17.104 1.00132.73 C ANISOU 3068 CG PHE A 435 19431 18184 12817 757 703 1190 C ATOM 3069 CD1 PHE A 435 22.632 36.590 16.960 1.00135.73 C ANISOU 3069 CD1 PHE A 435 19773 18558 13240 661 741 1364 C ATOM 3070 CD2 PHE A 435 22.023 34.287 16.764 1.00134.96 C ANISOU 3070 CD2 PHE A 435 19869 18437 12974 793 584 1081 C ATOM 3071 CE1 PHE A 435 21.373 36.963 16.480 1.00136.56 C ANISOU 3071 CE1 PHE A 435 19970 18657 13260 643 670 1430 C ATOM 3072 CE2 PHE A 435 20.771 34.661 16.269 1.00137.75 C ANISOU 3072 CE2 PHE A 435 20291 18808 13239 734 511 1151 C ATOM 3073 CZ PHE A 435 20.450 35.996 16.139 1.00135.68 C ANISOU 3073 CZ PHE A 435 19967 18567 13019 679 558 1326 C ATOM 3074 N MET A 436 27.519 34.541 17.218 1.00136.06 N ANISOU 3074 N MET A 436 19407 19077 13213 1017 1080 1122 N ATOM 3075 CA MET A 436 28.886 35.064 17.130 1.00138.20 C ANISOU 3075 CA MET A 436 19446 19595 13471 1000 1230 1221 C ATOM 3076 C MET A 436 29.569 34.435 15.892 1.00145.03 C ANISOU 3076 C MET A 436 20289 20738 14078 1214 1346 1181 C ATOM 3077 O MET A 436 30.465 35.049 15.309 1.00146.43 O ANISOU 3077 O MET A 436 20284 21188 14167 1178 1489 1311 O ATOM 3078 CB MET A 436 29.656 34.704 18.423 1.00140.36 C ANISOU 3078 CB MET A 436 19587 19852 13890 1018 1207 1155 C ATOM 3079 CG MET A 436 31.020 35.380 18.573 1.00145.80 C ANISOU 3079 CG MET A 436 19998 20809 14590 933 1340 1278 C ATOM 3080 SD MET A 436 31.964 34.796 20.020 1.00149.75 S ANISOU 3080 SD MET A 436 20328 21349 15220 998 1310 1187 S ATOM 3081 CE MET A 436 32.726 33.321 19.351 1.00148.53 C ANISOU 3081 CE MET A 436 20172 21437 14826 1397 1377 1032 C ATOM 3082 N VAL A 437 29.129 33.213 15.498 1.00142.40 N ANISOU 3082 N VAL A 437 20156 20337 13610 1427 1278 1002 N ATOM 3083 CA VAL A 437 29.614 32.508 14.322 1.00144.94 C ANISOU 3083 CA VAL A 437 20524 20883 13666 1669 1366 929 C ATOM 3084 C VAL A 437 29.101 32.908 12.946 1.00150.40 C ANISOU 3084 C VAL A 437 21294 21678 14174 1648 1415 1003 C ATOM 3085 O VAL A 437 29.908 33.131 12.042 1.00152.24 O ANISOU 3085 O VAL A 437 21396 22217 14230 1735 1563 1075 O ATOM 3086 CB VAL A 437 29.307 30.938 14.420 1.00149.16 C ANISOU 3086 CB VAL A 437 21322 21252 14098 1916 1251 684 C ATOM 3087 CG1 VAL A 437 29.660 30.210 13.124 1.00151.73 C ANISOU 3087 CG1 VAL A 437 21760 21771 14119 2185 1325 588 C ATOM 3088 CG2 VAL A 437 30.026 30.288 15.595 1.00148.65 C ANISOU 3088 CG2 VAL A 437 21197 21137 14144 2034 1222 590 C ATOM 3089 N ILE A 438 27.761 33.080 12.819 1.00145.86 N ANISOU 3089 N ILE A 438 20904 20880 13634 1519 1292 1007 N ATOM 3090 CA ILE A 438 26.983 33.499 11.610 1.00146.47 C ANISOU 3090 CA ILE A 438 21082 21016 13554 1474 1301 1082 C ATOM 3091 C ILE A 438 27.285 34.928 11.211 1.00153.05 C ANISOU 3091 C ILE A 438 21742 21997 14415 1305 1422 1325 C ATOM 3092 O ILE A 438 27.375 35.209 10.013 1.00154.21 O ANISOU 3092 O ILE A 438 21885 22343 14366 1343 1513 1405 O ATOM 3093 CB ILE A 438 25.468 33.128 11.791 1.00147.43 C ANISOU 3093 CB ILE A 438 21432 20881 13705 1393 1113 1004 C ATOM 3094 CG1 ILE A 438 25.232 31.598 11.892 1.00147.59 C ANISOU 3094 CG1 ILE A 438 21679 20775 13624 1549 995 765 C ATOM 3095 CG2 ILE A 438 24.603 33.737 10.673 1.00148.66 C ANISOU 3095 CG2 ILE A 438 21656 21112 13717 1324 1114 1113 C ATOM 3096 CD1 ILE A 438 23.895 31.177 12.503 1.00150.43 C ANISOU 3096 CD1 ILE A 438 22216 20881 14061 1411 793 696 C ATOM 3097 N ALA A 439 27.467 35.836 12.204 1.00150.26 N ANISOU 3097 N ALA A 439 21263 21539 14289 1113 1420 1446 N ATOM 3098 CA ALA A 439 27.747 37.276 12.040 1.00151.57 C ANISOU 3098 CA ALA A 439 21311 21768 14509 905 1509 1685 C ATOM 3099 C ALA A 439 28.779 37.594 10.949 1.00160.63 C ANISOU 3099 C ALA A 439 22311 23265 15457 931 1686 1807 C ATOM 3100 O ALA A 439 28.496 38.397 10.057 1.00161.46 O ANISOU 3100 O ALA A 439 22448 23438 15461 843 1738 1968 O ATOM 3101 CB ALA A 439 28.176 37.882 13.369 1.00151.12 C ANISOU 3101 CB ALA A 439 21142 21581 14697 735 1487 1740 C ATOM 3102 N PHE A 440 29.922 36.908 10.948 1.00160.05 N ANISOU 3102 N PHE A 440 22080 23436 15296 1078 1777 1730 N ATOM 3103 CA PHE A 440 30.947 37.136 9.916 1.00163.61 C ANISOU 3103 CA PHE A 440 22353 24286 15526 1123 1952 1845 C ATOM 3104 C PHE A 440 31.096 36.015 8.866 1.00172.03 C ANISOU 3104 C PHE A 440 23484 25567 16311 1444 2002 1691 C ATOM 3105 O PHE A 440 31.684 36.222 7.804 1.00174.72 O ANISOU 3105 O PHE A 440 23714 26242 16428 1500 2141 1789 O ATOM 3106 CB PHE A 440 32.303 37.417 10.570 1.00166.42 C ANISOU 3106 CB PHE A 440 22421 24872 15939 1040 2050 1927 C ATOM 3107 CG PHE A 440 33.257 38.170 9.688 1.00170.84 C ANISOU 3107 CG PHE A 440 22762 25829 16320 930 2222 2144 C ATOM 3108 CD1 PHE A 440 32.877 39.361 9.092 1.00174.29 C ANISOU 3108 CD1 PHE A 440 23254 26224 16746 678 2249 2368 C ATOM 3109 CD2 PHE A 440 34.534 37.688 9.454 1.00175.42 C ANISOU 3109 CD2 PHE A 440 23080 26844 16726 1085 2356 2136 C ATOM 3110 CE1 PHE A 440 33.752 40.057 8.279 1.00178.03 C ANISOU 3110 CE1 PHE A 440 23534 27066 17044 544 2403 2587 C ATOM 3111 CE2 PHE A 440 35.413 38.379 8.642 1.00181.07 C ANISOU 3111 CE2 PHE A 440 23566 27974 17257 962 2515 2354 C ATOM 3112 CZ PHE A 440 35.021 39.565 8.054 1.00179.54 C ANISOU 3112 CZ PHE A 440 23438 27718 17060 671 2537 2583 C ATOM 3113 N CYS A 441 30.529 34.842 9.128 1.00168.60 N ANISOU 3113 N CYS A 441 23252 24938 15871 1646 1883 1453 N ATOM 3114 CA CYS A 441 30.697 33.702 8.216 1.00170.86 C ANISOU 3114 CA CYS A 441 23655 25382 15882 1966 1912 1278 C ATOM 3115 C CYS A 441 29.735 33.646 7.014 1.00175.30 C ANISOU 3115 C CYS A 441 24428 25922 16256 1992 1877 1264 C ATOM 3116 O CYS A 441 30.138 33.308 5.902 1.00177.34 O ANISOU 3116 O CYS A 441 24689 26452 16239 2184 1976 1236 O ATOM 3117 CB CYS A 441 30.624 32.386 8.996 1.00170.38 C ANISOU 3117 CB CYS A 441 23759 25113 15863 2177 1794 1024 C ATOM 3118 SG CYS A 441 32.217 31.559 9.216 1.00177.02 S ANISOU 3118 SG CYS A 441 24414 26274 16570 2511 1919 924 S ATOM 3119 N LYS A 442 28.472 33.981 7.255 1.00169.87 N ANISOU 3119 N LYS A 442 23904 24939 15701 1810 1737 1285 N ATOM 3120 CA LYS A 442 27.467 33.988 6.198 1.00170.33 C ANISOU 3120 CA LYS A 442 24146 24984 15589 1807 1686 1285 C ATOM 3121 C LYS A 442 26.735 32.653 6.109 1.00174.75 C ANISOU 3121 C LYS A 442 24990 25366 16041 1961 1534 1028 C ATOM 3122 O LYS A 442 26.161 32.318 5.073 1.00175.63 O ANISOU 3122 O LYS A 442 25264 25537 15929 2028 1503 972 O ATOM 3123 CB LYS A 442 28.109 34.326 4.851 1.00175.65 C ANISOU 3123 CB LYS A 442 24718 26026 15996 1899 1855 1395 C ATOM 3124 N ASN A 443 26.760 31.894 7.199 1.00170.29 N ANISOU 3124 N ASN A 443 24498 24581 15624 1999 1433 877 N ATOM 3125 CA ASN A 443 26.090 30.600 7.245 1.00170.19 C ANISOU 3125 CA ASN A 443 24788 24357 15519 2104 1270 639 C ATOM 3126 C ASN A 443 27.073 29.434 7.217 1.00175.50 C ANISOU 3126 C ASN A 443 25550 25088 16044 2418 1310 441 C ATOM 3127 O ASN A 443 26.988 28.559 6.355 1.00177.29 O ANISOU 3127 O ASN A 443 26009 25344 16008 2612 1283 281 O ATOM 3128 CB ASN A 443 25.091 30.473 6.093 1.00172.89 C ANISOU 3128 CB ASN A 443 25324 24725 15641 2074 1201 615 C ATOM 3129 CG ASN A 443 23.676 30.824 6.507 1.00193.66 C ANISOU 3129 CG ASN A 443 28030 27148 18403 1816 1035 672 C ATOM 3130 OD1 ASN A 443 23.389 31.002 7.691 1.00185.09 O ANISOU 3130 OD1 ASN A 443 26892 25869 17564 1680 957 698 O ATOM 3131 ND2 ASN A 443 22.781 30.926 5.531 1.00186.55 N ANISOU 3131 ND2 ASN A 443 27241 26320 17321 1759 981 697 N ATOM 3132 N CYS A 444 28.003 29.428 8.166 1.00170.71 N ANISOU 3132 N CYS A 444 24770 24502 15591 2482 1370 450 N ATOM 3133 CA CYS A 444 29.002 28.358 8.261 1.00172.04 C ANISOU 3133 CA CYS A 444 25001 24743 15623 2820 1413 276 C ATOM 3134 C CYS A 444 28.541 26.917 8.544 1.00174.36 C ANISOU 3134 C CYS A 444 25687 24724 15838 2977 1238 16 C ATOM 3135 O CYS A 444 29.309 25.969 8.381 1.00176.17 O ANISOU 3135 O CYS A 444 26042 25009 15887 3315 1271 -144 O ATOM 3136 CB CYS A 444 30.098 28.759 9.252 1.00171.74 C ANISOU 3136 CB CYS A 444 24653 24835 15766 2835 1515 368 C ATOM 3137 SG CYS A 444 31.380 29.827 8.557 1.00177.97 S ANISOU 3137 SG CYS A 444 25024 26149 16449 2858 1773 592 S ATOM 3138 N CYS A 445 27.290 26.767 8.968 1.00167.67 N ANISOU 3138 N CYS A 445 25040 23559 15109 2732 1049 -15 N ATOM 3139 CA CYS A 445 26.699 25.476 9.308 1.00167.34 C ANISOU 3139 CA CYS A 445 25390 23186 15007 2782 855 -231 C ATOM 3140 C CYS A 445 25.217 25.391 8.942 1.00169.26 C ANISOU 3140 C CYS A 445 25857 23247 15207 2513 678 -247 C ATOM 3141 O CYS A 445 24.563 26.415 8.717 1.00166.98 O ANISOU 3141 O CYS A 445 25388 23056 15001 2277 695 -75 O ATOM 3142 CB CYS A 445 26.941 25.122 10.774 1.00165.92 C ANISOU 3142 CB CYS A 445 25191 22790 15062 2764 782 -264 C ATOM 3143 SG CYS A 445 27.878 23.590 11.018 1.00172.47 S ANISOU 3143 SG CYS A 445 26311 23500 15721 3190 756 -509 S ATOM 3144 N ASN A 446 24.702 24.152 8.886 1.00166.71 N ANISOU 3144 N ASN A 446 25940 22665 14736 2553 503 -451 N ATOM 3145 CA ASN A 446 23.326 23.787 8.555 1.00166.19 C ANISOU 3145 CA ASN A 446 26140 22428 14578 2297 304 -500 C ATOM 3146 C ASN A 446 22.307 24.359 9.540 1.00166.06 C ANISOU 3146 C ASN A 446 25980 22294 14822 1936 187 -362 C ATOM 3147 O ASN A 446 22.671 24.846 10.612 1.00163.44 O ANISOU 3147 O ASN A 446 25416 21935 14750 1897 235 -267 O ATOM 3148 CB ASN A 446 23.204 22.256 8.543 1.00169.57 C ANISOU 3148 CB ASN A 446 27056 22560 14812 2411 133 -751 C ATOM 3149 CG ASN A 446 22.970 21.636 7.190 1.00195.09 C ANISOU 3149 CG ASN A 446 30609 25826 17691 2520 90 -899 C ATOM 3150 OD1 ASN A 446 23.843 21.657 6.316 1.00191.58 O ANISOU 3150 OD1 ASN A 446 30137 25599 17057 2835 249 -945 O ATOM 3151 ND2 ASN A 446 21.767 21.122 6.966 1.00186.72 N ANISOU 3151 ND2 ASN A 446 29839 24585 16519 2247 -124 -965 N ATOM 3152 N GLU A 447 21.020 24.273 9.171 1.00162.18 N ANISOU 3152 N GLU A 447 25628 21753 14239 1677 28 -354 N ATOM 3153 CA GLU A 447 19.900 24.702 10.006 1.00159.57 C ANISOU 3153 CA GLU A 447 25185 21350 14094 1347 -102 -234 C ATOM 3154 C GLU A 447 19.321 23.479 10.751 1.00163.51 C ANISOU 3154 C GLU A 447 26007 21543 14576 1202 -328 -376 C ATOM 3155 O GLU A 447 18.221 23.557 11.302 1.00161.70 O ANISOU 3155 O GLU A 447 25753 21267 14420 904 -478 -305 O ATOM 3156 CB GLU A 447 18.823 25.437 9.174 1.00160.88 C ANISOU 3156 CB GLU A 447 25254 21716 14156 1151 -134 -107 C ATOM 3157 CG GLU A 447 19.310 26.681 8.443 1.00170.75 C ANISOU 3157 CG GLU A 447 26215 23246 15417 1265 75 58 C ATOM 3158 CD GLU A 447 19.778 27.832 9.312 1.00186.05 C ANISOU 3158 CD GLU A 447 27812 25232 17645 1254 205 238 C ATOM 3159 OE1 GLU A 447 20.998 27.920 9.580 1.00180.95 O ANISOU 3159 OE1 GLU A 447 27063 24605 17085 1440 349 227 O ATOM 3160 OE2 GLU A 447 18.927 28.659 9.710 1.00177.43 O ANISOU 3160 OE2 GLU A 447 26561 24174 16678 1065 161 391 O ATOM 3161 N HIS A 448 20.080 22.350 10.761 1.00161.88 N ANISOU 3161 N HIS A 448 26111 21140 14256 1425 -352 -571 N ATOM 3162 CA HIS A 448 19.715 21.110 11.456 1.00162.35 C ANISOU 3162 CA HIS A 448 26539 20864 14281 1321 -562 -713 C ATOM 3163 C HIS A 448 20.131 21.186 12.935 1.00164.27 C ANISOU 3163 C HIS A 448 26624 20979 14812 1323 -549 -657 C ATOM 3164 O HIS A 448 19.447 20.625 13.795 1.00163.32 O ANISOU 3164 O HIS A 448 26652 20645 14756 1091 -729 -669 O ATOM 3165 CB HIS A 448 20.217 19.837 10.712 1.00166.31 C ANISOU 3165 CB HIS A 448 27522 21181 14489 1566 -618 -954 C ATOM 3166 CG HIS A 448 21.598 19.337 11.054 1.00170.55 C ANISOU 3166 CG HIS A 448 28135 21628 15040 1977 -502 -1064 C ATOM 3167 ND1 HIS A 448 22.783 19.991 11.083 1.00171.66 N ANISOU 3167 ND1 HIS A 448 27948 21998 15276 2280 -268 -1002 N ATOM 3168 CD2 HIS A 448 21.827 17.998 11.335 1.00174.41 C ANISOU 3168 CD2 HIS A 448 29098 21774 15395 2111 -640 -1260 C ATOM 3169 CE1 HIS A 448 23.744 19.066 11.420 1.00172.81 C ANISOU 3169 CE1 HIS A 448 28327 21981 15353 2621 -256 -1155 C ATOM 3170 NE2 HIS A 448 23.128 17.893 11.558 1.00174.76 N ANISOU 3170 NE2 HIS A 448 29069 21867 15465 2521 -482 -1308 N ATOM 3171 N LEU A 449 21.228 21.931 13.219 1.00159.70 N ANISOU 3171 N LEU A 449 25724 20559 14396 1558 -339 -581 N ATOM 3172 CA LEU A 449 21.755 22.182 14.563 1.00157.43 C ANISOU 3172 CA LEU A 449 25226 20209 14380 1581 -298 -515 C ATOM 3173 C LEU A 449 21.279 23.545 15.087 1.00158.01 C ANISOU 3173 C LEU A 449 24887 20456 14692 1358 -238 -301 C ATOM 3174 O LEU A 449 21.031 23.680 16.284 1.00155.95 O ANISOU 3174 O LEU A 449 24519 20097 14640 1218 -300 -240 O ATOM 3175 CB LEU A 449 23.294 22.019 14.637 1.00158.47 C ANISOU 3175 CB LEU A 449 25291 20406 14515 1973 -128 -579 C ATOM 3176 CG LEU A 449 24.207 23.073 13.980 1.00163.03 C ANISOU 3176 CG LEU A 449 25514 21332 15100 2151 114 -472 C ATOM 3177 CD1 LEU A 449 25.504 23.202 14.745 1.00162.79 C ANISOU 3177 CD1 LEU A 449 25263 21388 15203 2383 249 -453 C ATOM 3178 CD2 LEU A 449 24.517 22.718 12.530 1.00168.39 C ANISOU 3178 CD2 LEU A 449 26366 22142 15471 2374 182 -574 C ATOM 3179 N HIS A 450 21.110 24.536 14.173 1.00153.80 N ANISOU 3179 N HIS A 450 24155 20171 14112 1333 -127 -188 N ATOM 3180 CA HIS A 450 20.603 25.884 14.456 1.00151.22 C ANISOU 3180 CA HIS A 450 23495 20001 13962 1154 -72 15 C ATOM 3181 C HIS A 450 19.172 25.790 15.000 1.00153.21 C ANISOU 3181 C HIS A 450 23795 20168 14248 850 -265 61 C ATOM 3182 O HIS A 450 18.755 26.632 15.796 1.00150.49 O ANISOU 3182 O HIS A 450 23217 19867 14096 719 -263 198 O ATOM 3183 CB HIS A 450 20.632 26.740 13.180 1.00152.86 C ANISOU 3183 CB HIS A 450 23580 20460 14042 1203 58 109 C ATOM 3184 CG HIS A 450 20.117 28.132 13.376 1.00154.55 C ANISOU 3184 CG HIS A 450 23508 20807 14406 1051 112 317 C ATOM 3185 ND1 HIS A 450 20.948 29.151 13.806 1.00155.31 N ANISOU 3185 ND1 HIS A 450 23338 20985 14687 1109 270 441 N ATOM 3186 CD2 HIS A 450 18.882 28.639 13.155 1.00155.71 C ANISOU 3186 CD2 HIS A 450 23619 21025 14519 861 25 419 C ATOM 3187 CE1 HIS A 450 20.193 30.236 13.846 1.00153.57 C ANISOU 3187 CE1 HIS A 450 22969 20838 14544 963 269 606 C ATOM 3188 NE2 HIS A 450 18.943 29.977 13.464 1.00154.10 N ANISOU 3188 NE2 HIS A 450 23153 20916 14482 833 130 601 N ATOM 3189 N MET A 451 18.424 24.757 14.561 1.00150.93 N ANISOU 3189 N MET A 451 23819 19774 13754 737 -436 -54 N ATOM 3190 CA MET A 451 17.057 24.466 15.001 1.00149.98 C ANISOU 3190 CA MET A 451 23767 19609 13610 422 -641 -19 C ATOM 3191 C MET A 451 17.079 23.910 16.433 1.00151.82 C ANISOU 3191 C MET A 451 24041 19630 14014 336 -740 -44 C ATOM 3192 O MET A 451 16.084 24.015 17.153 1.00150.32 O ANISOU 3192 O MET A 451 23769 19459 13886 85 -865 42 O ATOM 3193 CB MET A 451 16.405 23.447 14.050 1.00154.79 C ANISOU 3193 CB MET A 451 24730 20163 13920 309 -799 -145 C ATOM 3194 CG MET A 451 15.037 23.873 13.527 1.00158.60 C ANISOU 3194 CG MET A 451 25125 20858 14278 43 -903 -34 C ATOM 3195 SD MET A 451 13.712 23.967 14.766 1.00161.33 S ANISOU 3195 SD MET A 451 25319 21243 14737 -312 -1083 97 S ATOM 3196 CE MET A 451 13.789 22.304 15.465 1.00159.68 C ANISOU 3196 CE MET A 451 25532 20672 14468 -448 -1283 -77 C ATOM 3197 N PHE A 452 18.216 23.313 16.842 1.00148.05 N ANISOU 3197 N PHE A 452 23682 18976 13593 559 -684 -156 N ATOM 3198 CA PHE A 452 18.365 22.751 18.181 1.00146.56 C ANISOU 3198 CA PHE A 452 23547 18582 13557 514 -769 -182 C ATOM 3199 C PHE A 452 18.794 23.774 19.232 1.00145.52 C ANISOU 3199 C PHE A 452 23043 18540 13710 551 -650 -54 C ATOM 3200 O PHE A 452 18.326 23.689 20.365 1.00143.65 O ANISOU 3200 O PHE A 452 22751 18224 13604 390 -748 -6 O ATOM 3201 CB PHE A 452 19.283 21.523 18.178 1.00150.59 C ANISOU 3201 CB PHE A 452 24401 18848 13968 742 -793 -364 C ATOM 3202 CG PHE A 452 18.920 20.528 19.253 1.00152.58 C ANISOU 3202 CG PHE A 452 24890 18828 14255 589 -980 -412 C ATOM 3203 CD1 PHE A 452 17.857 19.647 19.079 1.00157.35 C ANISOU 3203 CD1 PHE A 452 25820 19283 14682 304 -1202 -459 C ATOM 3204 CD2 PHE A 452 19.626 20.485 20.449 1.00153.69 C ANISOU 3204 CD2 PHE A 452 24926 18875 14596 703 -940 -398 C ATOM 3205 CE1 PHE A 452 17.509 18.739 20.083 1.00158.76 C ANISOU 3205 CE1 PHE A 452 26227 19210 14883 128 -1380 -482 C ATOM 3206 CE2 PHE A 452 19.280 19.573 21.451 1.00156.92 C ANISOU 3206 CE2 PHE A 452 25558 19034 15030 556 -1114 -427 C ATOM 3207 CZ PHE A 452 18.223 18.706 21.261 1.00156.66 C ANISOU 3207 CZ PHE A 452 25859 18844 14820 264 -1333 -464 C ATOM 3208 N THR A 453 19.663 24.741 18.861 1.00139.99 N ANISOU 3208 N THR A 453 22095 18008 13087 743 -448 7 N ATOM 3209 CA THR A 453 20.127 25.790 19.777 1.00137.14 C ANISOU 3209 CA THR A 453 21403 17728 12977 762 -336 127 C ATOM 3210 C THR A 453 18.997 26.756 20.149 1.00139.29 C ANISOU 3210 C THR A 453 21477 18106 13343 536 -383 279 C ATOM 3211 O THR A 453 19.050 27.361 21.222 1.00137.43 O ANISOU 3211 O THR A 453 21046 17865 13306 492 -365 356 O ATOM 3212 CB THR A 453 21.422 26.482 19.306 1.00141.73 C ANISOU 3212 CB THR A 453 21800 18458 13594 993 -122 154 C ATOM 3213 OG1 THR A 453 21.139 27.428 18.278 1.00140.46 O ANISOU 3213 OG1 THR A 453 21521 18489 13361 963 -32 256 O ATOM 3214 CG2 THR A 453 22.508 25.503 18.875 1.00140.91 C ANISOU 3214 CG2 THR A 453 21877 18306 13354 1264 -71 4 C ATOM 3215 N ILE A 454 17.973 26.891 19.272 1.00136.14 N ANISOU 3215 N ILE A 454 21129 17816 12781 409 -446 319 N ATOM 3216 CA ILE A 454 16.786 27.710 19.542 1.00134.79 C ANISOU 3216 CA ILE A 454 20786 17781 12646 227 -504 462 C ATOM 3217 C ILE A 454 15.829 26.923 20.439 1.00138.10 C ANISOU 3217 C ILE A 454 21295 18122 13056 9 -702 444 C ATOM 3218 O ILE A 454 15.138 27.524 21.262 1.00136.45 O ANISOU 3218 O ILE A 454 20899 17997 12950 -98 -741 552 O ATOM 3219 CB ILE A 454 16.076 28.302 18.287 1.00138.88 C ANISOU 3219 CB ILE A 454 21275 18503 12990 196 -484 540 C ATOM 3220 CG1 ILE A 454 15.560 27.225 17.315 1.00141.71 C ANISOU 3220 CG1 ILE A 454 21904 18854 13084 112 -606 432 C ATOM 3221 CG2 ILE A 454 16.936 29.326 17.572 1.00139.45 C ANISOU 3221 CG2 ILE A 454 21212 18676 13098 377 -284 608 C ATOM 3222 CD1 ILE A 454 14.072 27.249 17.121 1.00150.94 C ANISOU 3222 CD1 ILE A 454 23054 20185 14113 -121 -758 511 C ATOM 3223 N TRP A 455 15.805 25.577 20.285 1.00135.83 N ANISOU 3223 N TRP A 455 21308 17671 12631 -53 -828 310 N ATOM 3224 CA TRP A 455 14.979 24.674 21.086 1.00135.75 C ANISOU 3224 CA TRP A 455 21433 17561 12583 -295 -1028 293 C ATOM 3225 C TRP A 455 15.604 24.371 22.437 1.00136.19 C ANISOU 3225 C TRP A 455 21470 17441 12835 -247 -1031 268 C ATOM 3226 O TRP A 455 14.877 24.056 23.377 1.00135.48 O ANISOU 3226 O TRP A 455 21364 17333 12777 -450 -1164 316 O ATOM 3227 CB TRP A 455 14.604 23.400 20.319 1.00137.41 C ANISOU 3227 CB TRP A 455 22021 17649 12541 -422 -1183 171 C ATOM 3228 CG TRP A 455 13.283 23.530 19.626 1.00139.67 C ANISOU 3228 CG TRP A 455 22283 18152 12633 -669 -1297 246 C ATOM 3229 CD1 TRP A 455 13.064 24.029 18.378 1.00143.45 C ANISOU 3229 CD1 TRP A 455 22724 18815 12966 -618 -1237 267 C ATOM 3230 CD2 TRP A 455 11.987 23.277 20.192 1.00139.86 C ANISOU 3230 CD2 TRP A 455 22262 18293 12588 -1001 -1481 337 C ATOM 3231 NE1 TRP A 455 11.715 24.047 18.104 1.00143.92 N ANISOU 3231 NE1 TRP A 455 22733 19091 12860 -891 -1380 354 N ATOM 3232 CE2 TRP A 455 11.029 23.594 19.201 1.00145.00 C ANISOU 3232 CE2 TRP A 455 22852 19207 13035 -1135 -1531 402 C ATOM 3233 CE3 TRP A 455 11.540 22.783 21.431 1.00140.73 C ANISOU 3233 CE3 TRP A 455 22369 18334 12766 -1205 -1612 376 C ATOM 3234 CZ2 TRP A 455 9.651 23.438 19.411 1.00145.08 C ANISOU 3234 CZ2 TRP A 455 22780 19442 12904 -1464 -1706 507 C ATOM 3235 CZ3 TRP A 455 10.176 22.622 21.635 1.00142.99 C ANISOU 3235 CZ3 TRP A 455 22581 18837 12914 -1543 -1784 483 C ATOM 3236 CH2 TRP A 455 9.248 22.955 20.636 1.00144.85 C ANISOU 3236 CH2 TRP A 455 22734 19359 12941 -1669 -1829 549 C ATOM 3237 N LEU A 456 16.943 24.512 22.551 1.00130.64 N ANISOU 3237 N LEU A 456 20737 16646 12252 18 -882 209 N ATOM 3238 CA LEU A 456 17.669 24.335 23.810 1.00128.64 C ANISOU 3238 CA LEU A 456 20429 16261 12188 99 -865 192 C ATOM 3239 C LEU A 456 17.363 25.512 24.733 1.00128.55 C ANISOU 3239 C LEU A 456 20078 16392 12374 37 -814 330 C ATOM 3240 O LEU A 456 17.313 25.343 25.946 1.00127.38 O ANISOU 3240 O LEU A 456 19874 16175 12349 -26 -874 349 O ATOM 3241 CB LEU A 456 19.177 24.209 23.580 1.00129.20 C ANISOU 3241 CB LEU A 456 20528 16264 12298 405 -716 101 C ATOM 3242 CG LEU A 456 19.933 23.489 24.685 1.00133.88 C ANISOU 3242 CG LEU A 456 21196 16676 12995 507 -746 36 C ATOM 3243 CD1 LEU A 456 19.824 21.977 24.536 1.00136.33 C ANISOU 3243 CD1 LEU A 456 21929 16738 13130 503 -899 -95 C ATOM 3244 CD2 LEU A 456 21.372 23.904 24.701 1.00136.09 C ANISOU 3244 CD2 LEU A 456 21315 17024 13369 792 -563 14 C ATOM 3245 N GLY A 457 17.140 26.681 24.138 1.00122.87 N ANISOU 3245 N GLY A 457 19159 15861 11666 62 -711 425 N ATOM 3246 CA GLY A 457 16.730 27.885 24.843 1.00120.22 C ANISOU 3246 CA GLY A 457 18549 15654 11476 22 -670 555 C ATOM 3247 C GLY A 457 15.289 27.746 25.294 1.00122.37 C ANISOU 3247 C GLY A 457 18791 16027 11676 -199 -827 627 C ATOM 3248 O GLY A 457 14.913 28.269 26.344 1.00120.58 O ANISOU 3248 O GLY A 457 18392 15857 11567 -243 -848 701 O ATOM 3249 N TYR A 458 14.476 27.007 24.507 1.00119.89 N ANISOU 3249 N TYR A 458 18647 15758 11149 -345 -946 605 N ATOM 3250 CA TYR A 458 13.080 26.699 24.823 1.00120.08 C ANISOU 3250 CA TYR A 458 18647 15925 11053 -597 -1115 677 C ATOM 3251 C TYR A 458 13.044 25.589 25.891 1.00122.39 C ANISOU 3251 C TYR A 458 19078 16051 11374 -747 -1253 628 C ATOM 3252 O TYR A 458 12.014 25.398 26.538 1.00121.83 O ANISOU 3252 O TYR A 458 18933 16108 11247 -964 -1385 708 O ATOM 3253 CB TYR A 458 12.284 26.272 23.559 1.00123.83 C ANISOU 3253 CB TYR A 458 19262 16517 11269 -733 -1202 671 C ATOM 3254 CG TYR A 458 12.138 27.309 22.454 1.00126.44 C ANISOU 3254 CG TYR A 458 19466 17041 11533 -609 -1088 739 C ATOM 3255 CD1 TYR A 458 11.970 28.661 22.750 1.00127.29 C ANISOU 3255 CD1 TYR A 458 19304 17305 11754 -488 -983 864 C ATOM 3256 CD2 TYR A 458 12.053 26.923 21.116 1.00129.03 C ANISOU 3256 CD2 TYR A 458 19965 17399 11659 -624 -1102 684 C ATOM 3257 CE1 TYR A 458 11.812 29.613 21.738 1.00128.47 C ANISOU 3257 CE1 TYR A 458 19367 17614 11830 -373 -886 940 C ATOM 3258 CE2 TYR A 458 11.894 27.866 20.096 1.00130.15 C ANISOU 3258 CE2 TYR A 458 19994 17730 11729 -512 -1001 759 C ATOM 3259 CZ TYR A 458 11.765 29.209 20.412 1.00135.54 C ANISOU 3259 CZ TYR A 458 20415 18551 12534 -390 -894 894 C ATOM 3260 OH TYR A 458 11.602 30.139 19.413 1.00135.19 O ANISOU 3260 OH TYR A 458 20288 18672 12408 -277 -800 980 O ATOM 3261 N ILE A 459 14.173 24.859 26.065 1.00118.38 N ANISOU 3261 N ILE A 459 18766 15278 10935 -621 -1223 505 N ATOM 3262 CA ILE A 459 14.346 23.804 27.070 1.00118.26 C ANISOU 3262 CA ILE A 459 18920 15059 10956 -712 -1339 454 C ATOM 3263 C ILE A 459 14.433 24.437 28.478 1.00119.49 C ANISOU 3263 C ILE A 459 18813 15270 11319 -686 -1303 533 C ATOM 3264 O ILE A 459 13.895 23.863 29.424 1.00119.45 O ANISOU 3264 O ILE A 459 18835 15242 11309 -868 -1435 570 O ATOM 3265 CB ILE A 459 15.508 22.821 26.693 1.00122.64 C ANISOU 3265 CB ILE A 459 19790 15328 11479 -533 -1318 297 C ATOM 3266 CG1 ILE A 459 14.997 21.704 25.750 1.00125.53 C ANISOU 3266 CG1 ILE A 459 20529 15579 11590 -686 -1465 215 C ATOM 3267 CG2 ILE A 459 16.242 22.229 27.915 1.00122.80 C ANISOU 3267 CG2 ILE A 459 19878 15146 11636 -457 -1341 256 C ATOM 3268 CD1 ILE A 459 16.076 21.031 24.824 1.00132.90 C ANISOU 3268 CD1 ILE A 459 21766 16305 12425 -428 -1404 51 C ATOM 3269 N ASN A 460 15.042 25.649 28.594 1.00113.36 N ANISOU 3269 N ASN A 460 17790 14578 10705 -485 -1135 568 N ATOM 3270 CA ASN A 460 15.152 26.428 29.838 1.00110.79 C ANISOU 3270 CA ASN A 460 17219 14311 10567 -443 -1090 634 C ATOM 3271 C ASN A 460 13.759 26.770 30.369 1.00113.55 C ANISOU 3271 C ASN A 460 17408 14883 10854 -629 -1192 754 C ATOM 3272 O ASN A 460 13.562 26.812 31.580 1.00112.55 O ANISOU 3272 O ASN A 460 17168 14783 10814 -678 -1236 795 O ATOM 3273 CB ASN A 460 15.939 27.721 29.602 1.00109.73 C ANISOU 3273 CB ASN A 460 16898 14227 10568 -235 -905 654 C ATOM 3274 CG ASN A 460 16.129 28.564 30.839 1.00130.87 C ANISOU 3274 CG ASN A 460 19362 16937 13427 -188 -862 706 C ATOM 3275 OD1 ASN A 460 17.037 28.337 31.643 1.00125.01 O ANISOU 3275 OD1 ASN A 460 18610 16075 12815 -116 -835 655 O ATOM 3276 ND2 ASN A 460 15.255 29.540 31.029 1.00122.09 N ANISOU 3276 ND2 ASN A 460 18081 15997 12308 -215 -861 806 N ATOM 3277 N SER A 461 12.804 27.019 29.458 1.00110.34 N ANISOU 3277 N SER A 461 16978 14666 10281 -719 -1226 814 N ATOM 3278 CA SER A 461 11.410 27.326 29.761 1.00110.22 C ANISOU 3278 CA SER A 461 16792 14936 10153 -879 -1322 939 C ATOM 3279 C SER A 461 10.697 26.115 30.384 1.00114.06 C ANISOU 3279 C SER A 461 17384 15430 10525 -1165 -1512 955 C ATOM 3280 O SER A 461 9.761 26.281 31.168 1.00113.42 O ANISOU 3280 O SER A 461 17118 15578 10396 -1293 -1590 1062 O ATOM 3281 CB SER A 461 10.696 27.771 28.493 1.00115.34 C ANISOU 3281 CB SER A 461 17411 15786 10627 -890 -1313 991 C ATOM 3282 OG SER A 461 9.328 28.047 28.732 1.00126.08 O ANISOU 3282 OG SER A 461 18584 17475 11845 -1027 -1407 1120 O ATOM 3283 N THR A 462 11.151 24.906 30.026 1.00111.08 N ANISOU 3283 N THR A 462 17316 14804 10087 -1260 -1588 854 N ATOM 3284 CA THR A 462 10.638 23.632 30.529 1.00111.88 C ANISOU 3284 CA THR A 462 17611 14828 10073 -1550 -1779 859 C ATOM 3285 C THR A 462 11.431 23.233 31.789 1.00114.44 C ANISOU 3285 C THR A 462 17979 14934 10571 -1481 -1775 822 C ATOM 3286 O THR A 462 10.875 22.600 32.690 1.00114.83 O ANISOU 3286 O THR A 462 18048 15006 10576 -1704 -1911 885 O ATOM 3287 CB THR A 462 10.770 22.543 29.440 1.00118.60 C ANISOU 3287 CB THR A 462 18840 15473 10751 -1660 -1868 755 C ATOM 3288 OG1 THR A 462 10.511 23.097 28.148 1.00116.99 O ANISOU 3288 OG1 THR A 462 18594 15419 10437 -1600 -1807 753 O ATOM 3289 CG2 THR A 462 9.869 21.344 29.693 1.00117.95 C ANISOU 3289 CG2 THR A 462 18969 15372 10475 -2050 -2098 794 C ATOM 3290 N LEU A 463 12.731 23.605 31.835 1.00108.94 N ANISOU 3290 N LEU A 463 17285 14050 10056 -1182 -1622 730 N ATOM 3291 CA LEU A 463 13.670 23.279 32.909 1.00107.53 C ANISOU 3291 CA LEU A 463 17142 13672 10042 -1065 -1599 683 C ATOM 3292 C LEU A 463 13.510 24.074 34.205 1.00109.05 C ANISOU 3292 C LEU A 463 17032 14022 10382 -1037 -1564 768 C ATOM 3293 O LEU A 463 13.639 23.481 35.272 1.00108.27 O ANISOU 3293 O LEU A 463 16974 13832 10331 -1102 -1637 777 O ATOM 3294 CB LEU A 463 15.124 23.317 32.397 1.00107.23 C ANISOU 3294 CB LEU A 463 17208 13430 10104 -766 -1456 558 C ATOM 3295 CG LEU A 463 15.779 21.996 31.906 1.00113.59 C ANISOU 3295 CG LEU A 463 18407 13943 10810 -718 -1518 435 C ATOM 3296 CD1 LEU A 463 16.477 21.260 33.035 1.00113.83 C ANISOU 3296 CD1 LEU A 463 18548 13771 10931 -652 -1562 401 C ATOM 3297 CD2 LEU A 463 14.814 21.081 31.132 1.00117.48 C ANISOU 3297 CD2 LEU A 463 19184 14390 11064 -980 -1685 428 C ATOM 3298 N ASN A 464 13.240 25.393 34.131 1.00104.51 N ANISOU 3298 N ASN A 464 16179 13665 9866 -930 -1457 828 N ATOM 3299 CA ASN A 464 13.060 26.237 35.325 1.00103.02 C ANISOU 3299 CA ASN A 464 15724 13623 9796 -876 -1423 896 C ATOM 3300 C ASN A 464 11.946 25.790 36.295 1.00107.99 C ANISOU 3300 C ASN A 464 16269 14434 10328 -1107 -1571 999 C ATOM 3301 O ASN A 464 12.243 25.711 37.489 1.00106.70 O ANISOU 3301 O ASN A 464 16039 14234 10269 -1087 -1583 1005 O ATOM 3302 CB ASN A 464 13.006 27.738 35.003 1.00101.39 C ANISOU 3302 CB ASN A 464 15301 13571 9650 -697 -1288 933 C ATOM 3303 CG ASN A 464 14.359 28.368 34.737 1.00115.56 C ANISOU 3303 CG ASN A 464 17103 15193 11611 -471 -1131 853 C ATOM 3304 OD1 ASN A 464 15.422 27.858 35.125 1.00107.50 O ANISOU 3304 OD1 ASN A 464 16168 13981 10695 -404 -1106 774 O ATOM 3305 ND2 ASN A 464 14.345 29.508 34.072 1.00105.86 N ANISOU 3305 ND2 ASN A 464 15779 14047 10394 -351 -1024 883 N ATOM 3306 N PRO A 465 10.714 25.405 35.848 1.00106.68 N ANISOU 3306 N PRO A 465 16106 14475 9952 -1345 -1691 1084 N ATOM 3307 CA PRO A 465 9.702 24.931 36.824 1.00107.50 C ANISOU 3307 CA PRO A 465 16109 14790 9947 -1591 -1834 1199 C ATOM 3308 C PRO A 465 10.113 23.674 37.607 1.00112.20 C ANISOU 3308 C PRO A 465 16926 15143 10563 -1749 -1945 1173 C ATOM 3309 O PRO A 465 9.587 23.423 38.692 1.00111.54 O ANISOU 3309 O PRO A 465 16734 15199 10448 -1896 -2030 1264 O ATOM 3310 CB PRO A 465 8.448 24.703 35.970 1.00111.09 C ANISOU 3310 CB PRO A 465 16545 15512 10152 -1830 -1939 1288 C ATOM 3311 CG PRO A 465 8.943 24.571 34.572 1.00115.83 C ANISOU 3311 CG PRO A 465 17361 15921 10727 -1762 -1892 1190 C ATOM 3312 CD PRO A 465 10.168 25.416 34.472 1.00109.43 C ANISOU 3312 CD PRO A 465 16523 14918 10137 -1413 -1706 1092 C ATOM 3313 N LEU A 466 11.079 22.914 37.059 1.00110.17 N ANISOU 3313 N LEU A 466 16982 14529 10348 -1690 -1940 1053 N ATOM 3314 CA LEU A 466 11.658 21.702 37.630 1.00111.32 C ANISOU 3314 CA LEU A 466 17411 14375 10510 -1767 -2034 1008 C ATOM 3315 C LEU A 466 12.748 22.062 38.662 1.00115.55 C ANISOU 3315 C LEU A 466 17845 14791 11268 -1511 -1930 959 C ATOM 3316 O LEU A 466 12.980 21.278 39.583 1.00115.86 O ANISOU 3316 O LEU A 466 18002 14693 11326 -1582 -2014 973 O ATOM 3317 CB LEU A 466 12.254 20.853 36.491 1.00112.62 C ANISOU 3317 CB LEU A 466 17957 14230 10602 -1737 -2057 886 C ATOM 3318 CG LEU A 466 12.489 19.368 36.745 1.00119.06 C ANISOU 3318 CG LEU A 466 19181 14725 11332 -1888 -2211 851 C ATOM 3319 CD1 LEU A 466 12.046 18.544 35.553 1.00121.51 C ANISOU 3319 CD1 LEU A 466 19832 14909 11427 -2082 -2328 808 C ATOM 3320 CD2 LEU A 466 13.955 19.085 37.050 1.00120.73 C ANISOU 3320 CD2 LEU A 466 19544 14631 11697 -1564 -2122 730 C ATOM 3321 N ILE A 467 13.410 23.236 38.509 1.00111.63 N ANISOU 3321 N ILE A 467 17140 14347 10925 -1232 -1756 909 N ATOM 3322 CA ILE A 467 14.488 23.707 39.397 1.00110.48 C ANISOU 3322 CA ILE A 467 16878 14119 10982 -1001 -1652 859 C ATOM 3323 C ILE A 467 13.990 24.095 40.790 1.00115.84 C ANISOU 3323 C ILE A 467 17322 14987 11705 -1061 -1687 948 C ATOM 3324 O ILE A 467 14.580 23.647 41.773 1.00115.53 O ANISOU 3324 O ILE A 467 17316 14833 11747 -1025 -1712 933 O ATOM 3325 CB ILE A 467 15.398 24.796 38.730 1.00112.15 C ANISOU 3325 CB ILE A 467 16976 14316 11322 -733 -1469 784 C ATOM 3326 CG1 ILE A 467 16.114 24.285 37.444 1.00113.54 C ANISOU 3326 CG1 ILE A 467 17390 14301 11451 -635 -1424 686 C ATOM 3327 CG2 ILE A 467 16.392 25.446 39.702 1.00111.06 C ANISOU 3327 CG2 ILE A 467 16671 14152 11375 -544 -1371 750 C ATOM 3328 CD1 ILE A 467 16.914 22.907 37.514 1.00121.96 C ANISOU 3328 CD1 ILE A 467 18769 15083 12487 -591 -1490 603 C ATOM 3329 N TYR A 468 12.909 24.907 40.872 1.00113.90 N ANISOU 3329 N TYR A 468 16842 15045 11388 -1129 -1689 1040 N ATOM 3330 CA TYR A 468 12.311 25.404 42.127 1.00114.20 C ANISOU 3330 CA TYR A 468 16634 15324 11434 -1154 -1713 1126 C ATOM 3331 C TYR A 468 12.131 24.373 43.276 1.00120.76 C ANISOU 3331 C TYR A 468 17523 16134 12225 -1338 -1845 1186 C ATOM 3332 O TYR A 468 12.625 24.658 44.368 1.00119.02 O ANISOU 3332 O TYR A 468 17192 15910 12122 -1225 -1812 1173 O ATOM 3333 CB TYR A 468 11.038 26.255 41.902 1.00115.87 C ANISOU 3333 CB TYR A 468 16615 15898 11512 -1190 -1713 1225 C ATOM 3334 CG TYR A 468 11.019 27.124 40.657 1.00117.86 C ANISOU 3334 CG TYR A 468 16848 16177 11756 -1049 -1611 1193 C ATOM 3335 CD1 TYR A 468 12.073 27.991 40.365 1.00118.67 C ANISOU 3335 CD1 TYR A 468 16952 16106 12029 -799 -1465 1099 C ATOM 3336 CD2 TYR A 468 9.907 27.154 39.821 1.00120.13 C ANISOU 3336 CD2 TYR A 468 17092 16701 11852 -1174 -1663 1274 C ATOM 3337 CE1 TYR A 468 12.055 28.798 39.227 1.00119.91 C ANISOU 3337 CE1 TYR A 468 17104 16285 12170 -682 -1373 1086 C ATOM 3338 CE2 TYR A 468 9.863 27.980 38.697 1.00121.15 C ANISOU 3338 CE2 TYR A 468 17201 16867 11963 -1032 -1570 1256 C ATOM 3339 CZ TYR A 468 10.943 28.794 38.397 1.00128.15 C ANISOU 3339 CZ TYR A 468 18119 17545 13025 -786 -1425 1164 C ATOM 3340 OH TYR A 468 10.900 29.592 37.277 1.00129.82 O ANISOU 3340 OH TYR A 468 18328 17787 13209 -662 -1337 1162 O ATOM 3341 N PRO A 469 11.508 23.173 43.084 1.00121.04 N ANISOU 3341 N PRO A 469 17755 16137 12098 -1627 -1998 1251 N ATOM 3342 CA PRO A 469 11.394 22.226 44.214 1.00122.37 C ANISOU 3342 CA PRO A 469 18001 16266 12229 -1808 -2123 1322 C ATOM 3343 C PRO A 469 12.708 21.579 44.685 1.00126.90 C ANISOU 3343 C PRO A 469 18791 16481 12945 -1660 -2109 1228 C ATOM 3344 O PRO A 469 12.826 21.275 45.875 1.00126.59 O ANISOU 3344 O PRO A 469 18709 16453 12936 -1691 -2157 1278 O ATOM 3345 CB PRO A 469 10.394 21.183 43.706 1.00126.41 C ANISOU 3345 CB PRO A 469 18702 16817 12513 -2180 -2294 1417 C ATOM 3346 CG PRO A 469 10.534 21.213 42.232 1.00130.83 C ANISOU 3346 CG PRO A 469 19424 17249 13037 -2136 -2256 1331 C ATOM 3347 CD PRO A 469 10.845 22.637 41.873 1.00124.25 C ANISOU 3347 CD PRO A 469 18331 16547 12332 -1827 -2075 1271 C ATOM 3348 N LEU A 470 13.687 21.372 43.765 1.00123.76 N ANISOU 3348 N LEU A 470 18610 15798 12616 -1485 -2043 1100 N ATOM 3349 CA LEU A 470 14.997 20.760 44.051 1.00123.79 C ANISOU 3349 CA LEU A 470 18816 15491 12728 -1292 -2019 1006 C ATOM 3350 C LEU A 470 15.799 21.547 45.091 1.00126.56 C ANISOU 3350 C LEU A 470 18915 15912 13260 -1065 -1912 977 C ATOM 3351 O LEU A 470 16.529 20.945 45.883 1.00126.53 O ANISOU 3351 O LEU A 470 19006 15759 13311 -986 -1942 962 O ATOM 3352 CB LEU A 470 15.823 20.621 42.756 1.00124.21 C ANISOU 3352 CB LEU A 470 19075 15323 12795 -1107 -1940 877 C ATOM 3353 CG LEU A 470 16.946 19.574 42.756 1.00130.28 C ANISOU 3353 CG LEU A 470 20164 15759 13579 -943 -1962 789 C ATOM 3354 CD1 LEU A 470 17.071 18.923 41.398 1.00132.07 C ANISOU 3354 CD1 LEU A 470 20716 15779 13684 -925 -1984 707 C ATOM 3355 CD2 LEU A 470 18.290 20.175 43.164 1.00131.63 C ANISOU 3355 CD2 LEU A 470 20163 15920 13929 -611 -1814 709 C ATOM 3356 N CYS A 471 15.671 22.887 45.069 1.00121.90 N ANISOU 3356 N CYS A 471 18027 15541 12750 -957 -1796 969 N ATOM 3357 CA CYS A 471 16.396 23.794 45.957 1.00120.22 C ANISOU 3357 CA CYS A 471 17582 15398 12696 -762 -1696 931 C ATOM 3358 C CYS A 471 15.523 24.364 47.066 1.00122.63 C ANISOU 3358 C CYS A 471 17643 15975 12976 -847 -1732 1022 C ATOM 3359 O CYS A 471 15.987 24.467 48.201 1.00121.42 O ANISOU 3359 O CYS A 471 17390 15840 12902 -775 -1730 1017 O ATOM 3360 CB CYS A 471 17.076 24.899 45.155 1.00119.66 C ANISOU 3360 CB CYS A 471 17409 15324 12732 -560 -1540 844 C ATOM 3361 SG CYS A 471 17.856 24.337 43.616 1.00124.34 S ANISOU 3361 SG CYS A 471 18255 15686 13302 -464 -1488 752 S ATOM 3362 N ASN A 472 14.271 24.742 46.744 1.00119.21 N ANISOU 3362 N ASN A 472 17102 15777 12416 -982 -1764 1104 N ATOM 3363 CA ASN A 472 13.336 25.307 47.718 1.00118.92 C ANISOU 3363 CA ASN A 472 16817 16054 12313 -1034 -1793 1196 C ATOM 3364 C ASN A 472 12.479 24.224 48.386 1.00124.38 C ANISOU 3364 C ASN A 472 17550 16859 12848 -1311 -1950 1327 C ATOM 3365 O ASN A 472 11.886 23.386 47.700 1.00125.28 O ANISOU 3365 O ASN A 472 17828 16947 12825 -1538 -2046 1386 O ATOM 3366 CB ASN A 472 12.471 26.404 47.086 1.00118.70 C ANISOU 3366 CB ASN A 472 16617 16270 12213 -980 -1734 1223 C ATOM 3367 CG ASN A 472 11.766 27.292 48.080 1.00134.84 C ANISOU 3367 CG ASN A 472 18395 18627 14210 -905 -1722 1279 C ATOM 3368 OD1 ASN A 472 10.573 27.134 48.351 1.00128.38 O ANISOU 3368 OD1 ASN A 472 17449 18118 13213 -1047 -1800 1399 O ATOM 3369 ND2 ASN A 472 12.479 28.266 48.627 1.00124.89 N ANISOU 3369 ND2 ASN A 472 17049 17315 13090 -678 -1627 1193 N ATOM 3370 N GLU A 473 12.430 24.255 49.736 1.00120.42 N ANISOU 3370 N GLU A 473 16908 16489 12357 -1308 -1980 1375 N ATOM 3371 CA GLU A 473 11.695 23.318 50.594 1.00121.23 C ANISOU 3371 CA GLU A 473 17019 16729 12315 -1568 -2122 1517 C ATOM 3372 C GLU A 473 10.176 23.520 50.514 1.00124.85 C ANISOU 3372 C GLU A 473 17280 17598 12558 -1765 -2183 1659 C ATOM 3373 O GLU A 473 9.451 22.547 50.303 1.00125.83 O ANISOU 3373 O GLU A 473 17518 17775 12516 -2080 -2314 1775 O ATOM 3374 CB GLU A 473 12.184 23.437 52.051 1.00122.15 C ANISOU 3374 CB GLU A 473 17014 16887 12510 -1463 -2116 1517 C ATOM 3375 CG GLU A 473 12.158 22.132 52.833 1.00134.59 C ANISOU 3375 CG GLU A 473 18750 18376 14011 -1683 -2254 1620 C ATOM 3376 CD GLU A 473 13.359 21.222 52.645 1.00153.86 C ANISOU 3376 CD GLU A 473 21509 20390 16560 -1617 -2274 1541 C ATOM 3377 OE1 GLU A 473 14.502 21.673 52.892 1.00142.94 O ANISOU 3377 OE1 GLU A 473 20096 18867 15348 -1346 -2176 1421 O ATOM 3378 OE2 GLU A 473 13.150 20.039 52.291 1.00150.31 O ANISOU 3378 OE2 GLU A 473 21348 19757 16007 -1837 -2395 1605 O ATOM 3379 N ASN A 474 9.703 24.779 50.682 1.00120.20 N ANISOU 3379 N ASN A 474 16408 17309 11955 -1578 -2093 1653 N ATOM 3380 CA ASN A 474 8.288 25.170 50.633 1.00121.15 C ANISOU 3380 CA ASN A 474 16286 17889 11857 -1676 -2126 1783 C ATOM 3381 C ASN A 474 7.619 24.809 49.304 1.00126.79 C ANISOU 3381 C ASN A 474 17093 18642 12439 -1869 -2175 1831 C ATOM 3382 O ASN A 474 6.427 24.504 49.290 1.00128.72 O ANISOU 3382 O ASN A 474 17203 19249 12455 -2107 -2268 1983 O ATOM 3383 CB ASN A 474 8.129 26.662 50.909 1.00120.84 C ANISOU 3383 CB ASN A 474 15999 18069 11844 -1348 -2004 1729 C ATOM 3384 CG ASN A 474 8.080 27.005 52.372 1.00145.54 C ANISOU 3384 CG ASN A 474 18940 21396 14962 -1241 -2000 1751 C ATOM 3385 OD1 ASN A 474 9.110 27.177 53.029 1.00138.81 O ANISOU 3385 OD1 ASN A 474 18151 20306 14286 -1093 -1955 1646 O ATOM 3386 ND2 ASN A 474 6.876 27.129 52.910 1.00139.49 N ANISOU 3386 ND2 ASN A 474 17926 21104 13972 -1307 -2048 1890 N ATOM 3387 N PHE A 475 8.388 24.853 48.196 1.00122.12 N ANISOU 3387 N PHE A 475 16716 17709 11974 -1770 -2114 1707 N ATOM 3388 CA PHE A 475 7.932 24.502 46.850 1.00122.47 C ANISOU 3388 CA PHE A 475 16890 17732 11909 -1928 -2154 1723 C ATOM 3389 C PHE A 475 7.815 22.984 46.711 1.00127.70 C ANISOU 3389 C PHE A 475 17828 18221 12470 -2291 -2314 1786 C ATOM 3390 O PHE A 475 6.820 22.507 46.170 1.00128.72 O ANISOU 3390 O PHE A 475 17964 18552 12391 -2580 -2421 1894 O ATOM 3391 CB PHE A 475 8.902 25.053 45.788 1.00122.76 C ANISOU 3391 CB PHE A 475 17073 17457 12115 -1682 -2028 1566 C ATOM 3392 CG PHE A 475 8.439 26.317 45.106 1.00123.60 C ANISOU 3392 CG PHE A 475 16993 17779 12191 -1481 -1925 1557 C ATOM 3393 CD1 PHE A 475 7.701 26.261 43.931 1.00127.27 C ANISOU 3393 CD1 PHE A 475 17477 18376 12505 -1595 -1955 1603 C ATOM 3394 CD2 PHE A 475 8.758 27.566 45.628 1.00124.43 C ANISOU 3394 CD2 PHE A 475 16929 17939 12408 -1175 -1805 1503 C ATOM 3395 CE1 PHE A 475 7.273 27.431 43.300 1.00127.82 C ANISOU 3395 CE1 PHE A 475 17387 18643 12535 -1386 -1861 1606 C ATOM 3396 CE2 PHE A 475 8.334 28.737 44.992 1.00126.94 C ANISOU 3396 CE2 PHE A 475 17124 18421 12687 -973 -1717 1500 C ATOM 3397 CZ PHE A 475 7.592 28.661 43.834 1.00125.83 C ANISOU 3397 CZ PHE A 475 16993 18422 12395 -1069 -1743 1556 C ATOM 3398 N LYS A 476 8.830 22.236 47.212 1.00124.28 N ANISOU 3398 N LYS A 476 17633 17418 12168 -2275 -2337 1721 N ATOM 3399 CA LYS A 476 8.939 20.770 47.179 1.00126.06 C ANISOU 3399 CA LYS A 476 18204 17375 12318 -2564 -2489 1759 C ATOM 3400 C LYS A 476 7.713 20.051 47.775 1.00133.62 C ANISOU 3400 C LYS A 476 19098 18633 13038 -2976 -2658 1962 C ATOM 3401 O LYS A 476 7.286 19.028 47.232 1.00135.21 O ANISOU 3401 O LYS A 476 19562 18725 13085 -3311 -2803 2023 O ATOM 3402 CB LYS A 476 10.235 20.324 47.883 1.00127.09 C ANISOU 3402 CB LYS A 476 18525 17134 12630 -2386 -2464 1668 C ATOM 3403 CG LYS A 476 10.649 18.876 47.615 1.00134.88 C ANISOU 3403 CG LYS A 476 19961 17721 13564 -2565 -2595 1659 C ATOM 3404 CD LYS A 476 11.567 18.332 48.706 1.00140.29 C ANISOU 3404 CD LYS A 476 20770 18174 14358 -2451 -2611 1644 C ATOM 3405 CE LYS A 476 10.803 17.802 49.900 1.00148.60 C ANISOU 3405 CE LYS A 476 21749 19427 15283 -2736 -2742 1823 C ATOM 3406 NZ LYS A 476 11.691 17.563 51.066 1.00153.50 N ANISOU 3406 NZ LYS A 476 22398 19900 16026 -2566 -2729 1809 N ATOM 3407 N LYS A 477 7.155 20.594 48.879 1.00130.87 N ANISOU 3407 N LYS A 477 18408 18670 12645 -2957 -2642 2066 N ATOM 3408 CA LYS A 477 5.985 20.058 49.589 1.00133.16 C ANISOU 3408 CA LYS A 477 18553 19342 12698 -3327 -2783 2278 C ATOM 3409 C LYS A 477 4.668 20.467 48.911 1.00140.27 C ANISOU 3409 C LYS A 477 19204 20723 13371 -3496 -2812 2391 C ATOM 3410 O LYS A 477 3.754 19.646 48.834 1.00142.16 O ANISOU 3410 O LYS A 477 19477 21160 13376 -3927 -2971 2553 O ATOM 3411 CB LYS A 477 6.002 20.499 51.065 1.00134.21 C ANISOU 3411 CB LYS A 477 18413 19715 12867 -3190 -2741 2334 C ATOM 3412 CG LYS A 477 5.198 19.610 52.002 1.00139.50 C ANISOU 3412 CG LYS A 477 19038 20638 13328 -3583 -2899 2548 C ATOM 3413 CD LYS A 477 5.267 20.132 53.422 1.00143.78 C ANISOU 3413 CD LYS A 477 19298 21427 13903 -3400 -2841 2586 C ATOM 3414 CE LYS A 477 4.491 19.269 54.382 1.00153.24 C ANISOU 3414 CE LYS A 477 20435 22902 14885 -3791 -2991 2813 C ATOM 3415 NZ LYS A 477 4.446 19.869 55.740 1.00160.32 N ANISOU 3415 NZ LYS A 477 21015 24116 15784 -3594 -2927 2853 N ATOM 3416 N THR A 478 4.577 21.732 48.430 1.00137.20 N ANISOU 3416 N THR A 478 18570 20524 13034 -3164 -2666 2313 N ATOM 3417 CA THR A 478 3.403 22.288 47.737 1.00138.99 C ANISOU 3417 CA THR A 478 18535 21222 13051 -3226 -2670 2407 C ATOM 3418 C THR A 478 3.197 21.586 46.378 1.00145.75 C ANISOU 3418 C THR A 478 19656 21911 13811 -3496 -2761 2398 C ATOM 3419 O THR A 478 2.054 21.374 45.968 1.00147.47 O ANISOU 3419 O THR A 478 19736 22524 13772 -3790 -2861 2543 O ATOM 3420 CB THR A 478 3.491 23.834 47.649 1.00146.07 C ANISOU 3420 CB THR A 478 19164 22291 14042 -2752 -2489 2316 C ATOM 3421 OG1 THR A 478 3.790 24.372 48.941 1.00144.62 O ANISOU 3421 OG1 THR A 478 18807 22192 13949 -2521 -2421 2302 O ATOM 3422 CG2 THR A 478 2.202 24.479 47.130 1.00146.31 C ANISOU 3422 CG2 THR A 478 18882 22883 13828 -2756 -2489 2434 C ATOM 3423 N PHE A 479 4.306 21.204 45.707 1.00142.53 N ANISOU 3423 N PHE A 479 19624 20941 13589 -3399 -2731 2231 N ATOM 3424 CA PHE A 479 4.297 20.483 44.431 1.00144.22 C ANISOU 3424 CA PHE A 479 20156 20915 13726 -3613 -2814 2188 C ATOM 3425 C PHE A 479 3.893 19.020 44.640 1.00152.09 C ANISOU 3425 C PHE A 479 21434 21806 14547 -4115 -3031 2303 C ATOM 3426 O PHE A 479 3.204 18.457 43.790 1.00153.95 O ANISOU 3426 O PHE A 479 21797 22114 14582 -4450 -3156 2361 O ATOM 3427 CB PHE A 479 5.673 20.575 43.740 1.00144.24 C ANISOU 3427 CB PHE A 479 20455 20379 13971 -3298 -2701 1971 C ATOM 3428 CG PHE A 479 5.912 21.767 42.831 1.00144.14 C ANISOU 3428 CG PHE A 479 20299 20416 14053 -2951 -2535 1865 C ATOM 3429 CD1 PHE A 479 5.226 22.965 43.023 1.00146.61 C ANISOU 3429 CD1 PHE A 479 20217 21168 14322 -2772 -2446 1930 C ATOM 3430 CD2 PHE A 479 6.856 21.705 41.812 1.00145.46 C ANISOU 3430 CD2 PHE A 479 20736 20188 14342 -2781 -2465 1705 C ATOM 3431 CE1 PHE A 479 5.452 24.062 42.188 1.00146.15 C ANISOU 3431 CE1 PHE A 479 20067 21122 14342 -2457 -2301 1843 C ATOM 3432 CE2 PHE A 479 7.089 22.807 40.984 1.00146.84 C ANISOU 3432 CE2 PHE A 479 20786 20410 14597 -2483 -2313 1625 C ATOM 3433 CZ PHE A 479 6.385 23.976 41.179 1.00144.37 C ANISOU 3433 CZ PHE A 479 20109 20502 14244 -2333 -2237 1698 C ATOM 3434 N LYS A 480 4.313 18.414 45.774 1.00149.48 N ANISOU 3434 N LYS A 480 21212 21303 14280 -4181 -3082 2341 N ATOM 3435 CA LYS A 480 3.981 17.035 46.145 1.00152.33 C ANISOU 3435 CA LYS A 480 21869 21531 14479 -4655 -3293 2467 C ATOM 3436 C LYS A 480 2.506 16.926 46.569 1.00159.38 C ANISOU 3436 C LYS A 480 22445 23033 15078 -5077 -3418 2714 C ATOM 3437 O LYS A 480 1.816 16.002 46.134 1.00161.76 O ANISOU 3437 O LYS A 480 22948 23362 15153 -5561 -3603 2826 O ATOM 3438 CB LYS A 480 4.899 16.531 47.275 1.00154.06 C ANISOU 3438 CB LYS A 480 22269 21410 14854 -4548 -3295 2442 C ATOM 3439 CG LYS A 480 6.222 15.939 46.806 1.00166.72 C ANISOU 3439 CG LYS A 480 24350 22358 16636 -4339 -3275 2252 C ATOM 3440 CD LYS A 480 7.058 15.484 47.998 1.00175.76 C ANISOU 3440 CD LYS A 480 25627 23242 17913 -4218 -3280 2250 C ATOM 3441 CE LYS A 480 8.388 14.898 47.598 1.00183.10 C ANISOU 3441 CE LYS A 480 27004 23571 18996 -3964 -3255 2070 C ATOM 3442 NZ LYS A 480 9.120 14.350 48.772 1.00188.32 N ANISOU 3442 NZ LYS A 480 27804 24003 19746 -3873 -3283 2093 N ATOM 3443 N ARG A 481 2.029 17.878 47.406 1.00155.58 N ANISOU 3443 N ARG A 481 21474 23055 14584 -4891 -3319 2799 N ATOM 3444 CA ARG A 481 0.656 17.919 47.920 1.00157.91 C ANISOU 3444 CA ARG A 481 21385 24024 14590 -5211 -3408 3040 C ATOM 3445 C ARG A 481 -0.408 18.163 46.851 1.00163.40 C ANISOU 3445 C ARG A 481 21898 25138 15049 -5404 -3455 3118 C ATOM 3446 O ARG A 481 -1.513 17.630 46.977 1.00165.55 O ANISOU 3446 O ARG A 481 22030 25847 15026 -5874 -3610 3333 O ATOM 3447 CB ARG A 481 0.520 18.903 49.096 1.00157.26 C ANISOU 3447 CB ARG A 481 20852 24349 14552 -4884 -3278 3085 C ATOM 3448 N ILE A 482 -0.075 18.947 45.800 1.00158.93 N ANISOU 3448 N ILE A 482 21331 24457 14599 -5062 -3327 2955 N ATOM 3449 CA ILE A 482 -0.976 19.256 44.679 1.00160.57 C ANISOU 3449 CA ILE A 482 21381 25031 14600 -5180 -3356 3007 C ATOM 3450 C ILE A 482 -1.091 18.094 43.666 1.00167.73 C ANISOU 3450 C ILE A 482 22711 25644 15374 -5645 -3537 3004 C ATOM 3451 O ILE A 482 -2.131 17.962 43.011 1.00169.88 O ANISOU 3451 O ILE A 482 22844 26327 15374 -5967 -3643 3129 O ATOM 3452 CB ILE A 482 -0.664 20.634 44.021 1.00161.12 C ANISOU 3452 CB ILE A 482 21257 25144 14818 -4626 -3148 2860 C ATOM 3453 CG1 ILE A 482 -1.918 21.252 43.376 1.00163.16 C ANISOU 3453 CG1 ILE A 482 21135 26054 14803 -4672 -3158 2990 C ATOM 3454 CG2 ILE A 482 0.517 20.578 43.040 1.00159.90 C ANISOU 3454 CG2 ILE A 482 21510 24342 14904 -4408 -3074 2629 C ATOM 3455 CD1 ILE A 482 -2.249 22.635 43.869 1.00168.84 C ANISOU 3455 CD1 ILE A 482 21407 27217 15528 -4201 -2994 3011 C ATOM 3456 N LEU A 483 -0.025 17.263 43.544 1.00164.26 N ANISOU 3456 N LEU A 483 22792 24508 15109 -5663 -3576 2860 N ATOM 3457 CA LEU A 483 0.008 16.102 42.647 1.00166.49 C ANISOU 3457 CA LEU A 483 23571 24413 15276 -6060 -3752 2827 C ATOM 3458 C LEU A 483 -0.868 14.969 43.192 1.00173.31 C ANISOU 3458 C LEU A 483 24535 25452 15862 -6714 -3997 3051 C ATOM 3459 O LEU A 483 -1.587 14.323 42.423 1.00175.70 O ANISOU 3459 O LEU A 483 24996 25847 15916 -7176 -4170 3126 O ATOM 3460 CB LEU A 483 1.451 15.611 42.414 1.00165.16 C ANISOU 3460 CB LEU A 483 23922 23467 15363 -5803 -3706 2601 C ATOM 3461 CG LEU A 483 2.272 16.346 41.345 1.00167.55 C ANISOU 3461 CG LEU A 483 24291 23513 15856 -5335 -3531 2377 C ATOM 3462 CD1 LEU A 483 3.750 16.035 41.491 1.00165.94 C ANISOU 3462 CD1 LEU A 483 24463 22669 15917 -5000 -3450 2184 C ATOM 3463 CD2 LEU A 483 1.804 16.000 39.929 1.00172.33 C ANISOU 3463 CD2 LEU A 483 25099 24105 16273 -5573 -3627 2343 C ATOM 3464 N HIS A 484 -0.840 14.767 44.526 1.00169.19 N ANISOU 3464 N HIS A 484 23907 25011 15368 -6770 -4014 3168 N ATOM 3465 CA HIS A 484 -1.636 13.755 45.223 1.00172.17 C ANISOU 3465 CA HIS A 484 24346 25583 15488 -7386 -4234 3408 C ATOM 3466 C HIS A 484 -2.966 14.356 45.726 1.00175.98 C ANISOU 3466 C HIS A 484 24188 26962 15716 -7566 -4240 3653 C ATOM 3467 O HIS A 484 -3.608 13.817 46.634 1.00177.90 O ANISOU 3467 O HIS A 484 24311 27514 15767 -7972 -4367 3878 O ATOM 3468 CB HIS A 484 -0.800 13.086 46.328 1.00172.59 C ANISOU 3468 CB HIS A 484 24700 25180 15698 -7355 -4261 3401 C ATOM 3469 CG HIS A 484 0.489 12.530 45.807 1.00174.92 C ANISOU 3469 CG HIS A 484 25593 24656 16213 -7125 -4248 3165 C ATOM 3470 ND1 HIS A 484 1.667 13.248 45.890 1.00172.95 N ANISOU 3470 ND1 HIS A 484 25325 24102 16285 -6495 -4033 2951 N ATOM 3471 CD2 HIS A 484 0.725 11.382 45.131 1.00179.11 C ANISOU 3471 CD2 HIS A 484 26734 24662 16658 -7432 -4422 3111 C ATOM 3472 CE1 HIS A 484 2.585 12.502 45.300 1.00172.61 C ANISOU 3472 CE1 HIS A 484 25848 23400 16338 -6424 -4076 2785 C ATOM 3473 NE2 HIS A 484 2.065 11.370 44.826 1.00176.65 N ANISOU 3473 NE2 HIS A 484 26770 23737 16612 -6956 -4307 2865 N ATOM 3474 N ILE A 485 -3.379 15.468 45.068 1.00170.33 N ANISOU 3474 N ILE A 485 23070 26668 14978 -7255 -4103 3611 N ATOM 3475 CA ILE A 485 -4.599 16.269 45.243 1.00178.37 C ANISOU 3475 CA ILE A 485 23457 28563 15752 -7270 -4070 3798 C ATOM 3476 C ILE A 485 -4.946 16.607 46.705 1.00175.36 C ANISOU 3476 C ILE A 485 22663 28642 15325 -7191 -4020 3959 C ATOM 3477 O ILE A 485 -4.548 17.656 47.209 1.00117.73 O ANISOU 3477 O ILE A 485 15101 21424 8209 -6627 -3821 3863 O ATOM 3478 CB ILE A 485 -5.790 15.711 44.380 1.00185.13 C ANISOU 3478 CB ILE A 485 24261 29847 16234 -7865 -4269 3970 C ATOM 3479 CG1 ILE A 485 -5.434 15.701 42.871 1.00184.47 C ANISOU 3479 CG1 ILE A 485 24502 29379 16210 -7792 -4268 3778 C ATOM 3480 CG2 ILE A 485 -7.087 16.498 44.616 1.00187.42 C ANISOU 3480 CG2 ILE A 485 23858 31120 16232 -7874 -4240 4188 C ATOM 3481 CD1 ILE A 485 -5.673 14.399 42.167 1.00191.86 C ANISOU 3481 CD1 ILE A 485 25906 29946 17048 -8270 -4461 3743 C TER 3482 ILE A 485 HETATM 3483 C01A5EH A1200 14.569 31.755 20.378 0.50128.73 C HETATM 3484 N02A5EH A1200 14.525 32.943 19.512 0.50135.70 N HETATM 3485 C03A5EH A1200 14.452 32.511 18.106 0.50 23.95 C HETATM 3486 C04A5EH A1200 15.730 33.765 19.724 0.50108.61 C HETATM 3487 C05A5EH A1200 15.364 35.138 20.280 0.50 60.67 C HETATM 3488 C06A5EH A1200 15.773 35.211 21.734 0.50113.33 C HETATM 3489 C07A5EH A1200 16.751 36.014 22.195 0.50165.91 C HETATM 3490 C08A5EH A1200 17.526 36.943 21.311 0.50153.27 C HETATM 3491 C09A5EH A1200 18.420 36.473 20.347 0.50127.97 C HETATM 3492 C10A5EH A1200 19.149 37.384 19.580 0.50131.79 C HETATM 3493 C11A5EH A1200 18.997 38.757 19.793 0.50 91.15 C HETATM 3494 C12A5EH A1200 18.119 39.218 20.775 0.50 77.62 C HETATM 3495 C13A5EH A1200 17.392 38.303 21.537 0.50 99.53 C HETATM 3496 C14A5EH A1200 16.426 38.762 22.605 0.50 29.88 C HETATM 3497 O15A5EH A1200 16.962 38.468 23.894 0.50129.74 O HETATM 3498 C16A5EH A1200 17.176 37.205 24.405 0.50141.60 C HETATM 3499 C17A5EH A1200 17.517 37.134 25.758 0.50123.84 C HETATM 3500 C18A5EH A1200 17.770 35.908 26.373 0.50140.03 C HETATM 3501 C19A5EH A1200 17.686 34.733 25.630 0.50137.78 C HETATM 3502 C20A5EH A1200 17.350 34.796 24.279 0.50113.47 C HETATM 3503 C21A5EH A1200 17.092 36.021 23.659 0.50159.27 C HETATM 3504 C1 BD7V A1201 14.808 32.837 18.106 0.50 73.17 C HETATM 3505 N1 BD7V A1201 14.677 33.217 19.522 0.50134.26 N HETATM 3506 O1 BD7V A1201 17.822 39.257 22.374 0.50 60.56 O HETATM 3507 C2 BD7V A1201 14.643 32.000 20.349 0.50132.98 C HETATM 3508 C3 BD7V A1201 15.818 34.061 19.915 0.50101.39 C HETATM 3509 C4 BD7V A1201 15.343 35.458 20.304 0.50 63.13 C HETATM 3510 C5 BD7V A1201 15.754 35.727 21.733 0.50 97.28 C HETATM 3511 C6 BD7V A1201 16.832 36.440 22.115 0.50159.20 C HETATM 3512 C7 BD7V A1201 17.090 36.591 23.581 0.50151.60 C HETATM 3513 C8 BD7V A1201 17.401 35.486 24.375 0.50133.41 C HETATM 3514 C9 BD7V A1201 17.654 35.666 25.736 0.50144.02 C HETATM 3515 C10BD7V A1201 17.597 36.946 26.291 0.50124.82 C HETATM 3516 C11BD7V A1201 17.280 38.046 25.491 0.50 95.05 C HETATM 3517 C12BD7V A1201 17.027 37.857 24.132 0.50118.35 C HETATM 3518 C13BD7V A1201 16.702 39.017 23.224 0.50 79.50 C HETATM 3519 C14BD7V A1201 18.247 38.425 21.362 0.50105.70 C HETATM 3520 C15BD7V A1201 17.803 37.105 21.170 0.50154.58 C HETATM 3521 C16BD7V A1201 19.189 38.972 20.486 0.50 61.44 C HETATM 3522 C17BD7V A1201 19.706 38.223 19.432 0.50 50.85 C HETATM 3523 C18BD7V A1201 19.279 36.910 19.253 0.50146.65 C HETATM 3524 C19BD7V A1201 18.351 36.351 20.130 0.50111.98 C HETATM 3525 P PO4 A1202 17.536 33.739 14.081 1.00172.63 P HETATM 3526 O1 PO4 A1202 18.998 33.196 13.827 1.00178.54 O HETATM 3527 O2 PO4 A1202 17.291 35.061 13.244 1.00178.73 O HETATM 3528 O3 PO4 A1202 16.485 32.632 13.656 1.00178.41 O HETATM 3529 O4 PO4 A1202 17.396 34.078 15.613 1.00178.53 O HETATM 3530 P PO4 A1203 51.496 6.331 66.907 1.00143.96 P HETATM 3531 O1 PO4 A1203 53.021 5.935 67.064 1.00149.83 O HETATM 3532 O2 PO4 A1203 51.337 7.382 65.738 1.00150.20 O HETATM 3533 O3 PO4 A1203 50.683 5.022 66.529 1.00150.31 O HETATM 3534 O4 PO4 A1203 50.955 6.979 68.247 1.00149.40 O HETATM 3535 P PO4 A1204 25.747 24.023 77.021 1.00 69.14 P HETATM 3536 O1 PO4 A1204 27.311 23.734 77.255 1.00 74.51 O HETATM 3537 O2 PO4 A1204 25.477 25.488 76.470 1.00 76.27 O HETATM 3538 O3 PO4 A1204 25.267 22.981 75.940 1.00 75.67 O HETATM 3539 O4 PO4 A1204 24.945 23.988 78.383 1.00 74.92 O HETATM 3540 C8 OLC A1205 62.015 33.472 79.867 1.00 34.29 C HETATM 3541 C24 OLC A1205 51.982 39.310 76.308 1.00105.76 C HETATM 3542 C7 OLC A1205 61.432 34.438 78.825 1.00 40.65 C HETATM 3543 C6 OLC A1205 59.949 34.737 79.110 1.00208.83 C HETATM 3544 C5 OLC A1205 59.096 34.762 77.838 1.00 30.82 C HETATM 3545 C4 OLC A1205 59.629 35.766 76.821 1.00 13.00 C HETATM 3546 C3 OLC A1205 58.638 36.046 75.698 1.00 13.00 C HETATM 3547 C2 OLC A1205 57.684 37.193 76.015 1.00 13.00 C HETATM 3548 C21 OLC A1205 54.192 38.181 75.565 1.00 10.03 C HETATM 3549 C1 OLC A1205 56.421 37.116 75.166 1.00 39.72 C HETATM 3550 C22 OLC A1205 53.223 38.518 76.714 1.00106.62 C HETATM 3551 O19 OLC A1205 56.417 36.853 73.967 1.00209.66 O HETATM 3552 O25 OLC A1205 51.232 39.626 77.491 1.00114.22 O HETATM 3553 O23 OLC A1205 52.841 37.354 77.461 1.00 74.71 O HETATM 3554 O20 OLC A1205 55.313 37.370 75.955 1.00 58.15 O HETATM 3555 O HOH A1206 40.008 27.360 59.025 1.00 23.71 O HETATM 3556 O HOH A1207 49.908 39.518 80.325 1.00 64.64 O CONECT 556 1173 CONECT 1173 556 CONECT 3118 3137 CONECT 3137 3118 CONECT 3483 3484 CONECT 3484 3483 3485 3486 CONECT 3485 3484 CONECT 3486 3484 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 3503 CONECT 3490 3489 3491 3495 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3490 3494 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 3503 CONECT 3499 3498 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3489 3498 3502 CONECT 3504 3505 CONECT 3505 3504 3507 3508 CONECT 3506 3518 3519 CONECT 3507 3505 CONECT 3508 3505 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 3520 CONECT 3512 3511 3513 3517 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3512 3516 3518 CONECT 3518 3506 3517 CONECT 3519 3506 3520 3521 CONECT 3520 3511 3519 3524 CONECT 3521 3519 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3520 3523 CONECT 3525 3526 3527 3528 3529 CONECT 3526 3525 CONECT 3527 3525 CONECT 3528 3525 CONECT 3529 3525 CONECT 3530 3531 3532 3533 3534 CONECT 3531 3530 CONECT 3532 3530 CONECT 3533 3530 CONECT 3534 3530 CONECT 3535 3536 3537 3538 3539 CONECT 3536 3535 CONECT 3537 3535 CONECT 3538 3535 CONECT 3539 3535 CONECT 3540 3542 CONECT 3541 3550 3552 CONECT 3542 3540 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3549 CONECT 3548 3550 3554 CONECT 3549 3547 3551 3554 CONECT 3550 3541 3548 3553 CONECT 3551 3549 CONECT 3552 3541 CONECT 3553 3550 CONECT 3554 3548 3549 MASTER 400 0 6 24 3 0 11 6 3555 1 76 35 END