HEADER LYASE 08-FEB-06 2FYM TITLE CRYSTAL STRUCTURE OF E. COLI ENOLASE COMPLEXED WITH THE TITLE 2 MINIMAL BINDING SEGMENT OF RNASE E. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENOLASE; COMPND 3 CHAIN: A, C, D, F; COMPND 4 SYNONYM: 2-PHOSPHOGLYCERATE DEHYDRATASE, 2-PHOSPHO-D- COMPND 5 GLYCERATE HYDRO-LYASE; COMPND 6 EC: 4.2.1.11; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: RIBONUCLEASE E; COMPND 10 CHAIN: B, E; COMPND 11 FRAGMENT: RESIDUES 833-850; COMPND 12 SYNONYM: RNASE E; COMPND 13 EC: 3.1.4.-; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 GENE: ENO; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: THE E. COLI RNASE E PEPTIDE WAS SYNTHESIZED. KEYWDS RNA DEGRADOSOME, ENOLASE, RNASE E EXPDTA X-RAY DIFFRACTION AUTHOR V.CHANDRAN,B.F.LUISI REVDAT 2 11-APR-06 2FYM 1 JRNL REVDAT 1 28-FEB-06 2FYM 0 JRNL AUTH V.CHANDRAN,B.F.LUISI JRNL TITL RECOGNITION OF ENOLASE IN THE ESCHERICHIA COLI RNA JRNL TITL 2 DEGRADOSOME JRNL REF J.MOL.BIOL. V. 358 8 2006 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9 REMARK 3 NUMBER OF REFLECTIONS : 205585 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) : 0.167 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 10847 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW : 1.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 15113 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.22 REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE SET COUNT : 820 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 14807 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.02000 REMARK 3 B22 (A**2) : -0.02000 REMARK 3 B33 (A**2) : 0.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.01000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.125 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.234 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13050 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17604 ; 1.157 ; 1.969 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1744 ; 5.413 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 517 ;40.267 ;25.745 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2277 ;12.064 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;18.674 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2013 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9690 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7024 ; 0.194 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9218 ; 0.302 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1764 ; 0.137 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 69 ; 0.171 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 78 ; 0.147 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8843 ; 0.844 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13607 ; 1.237 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4702 ; 2.697 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3994 ; 3.078 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 13545 ; 2.495 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 1934 ; 3.556 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 12873 ; 2.843 ; 3.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2FYM COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB036466. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-MAY-2004; 24-FEB-2004; 09- REMARK 200 MAR-2004; 08-MAY-2004 REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100 REMARK 200 PH : 7.0; 8.2; 6.0; 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y; N; Y REMARK 200 RADIATION SOURCE : ESRF; ESRF; ROTATING ANODE; REMARK 200 ESRF REMARK 200 BEAMLINE : ID14-4; ID29; ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 0.9782; 1.54; 1.0 REMARK 200 MONOCHROMATOR : GE(220) CRYSTAL; SI(111) REMARK 200 CRYSTAL; GE(220) CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : Q315R ADSC DETECTOR; ADSC REMARK 200 Q210 2D; IMAGE PLATE; Q315R REMARK 200 ADSC DETECTOR REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM REMARK 200 4; RIGAKU RAXIS IV; ADSC REMARK 200 QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 216432 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 200 DATA REDUNDANCY : 10.300 REMARK 200 R MERGE (I) : 0.03400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3 REMARK 200 DATA REDUNDANCY IN SHELL : 16.51 REMARK 200 R MERGE FOR SHELL (I) : 0.25300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.450 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; REMARK 200 SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: ENOLASE STRUCTURE 1E9I REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M SODIUM MALONATE, PH 7.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K. 40% MPEG 550, REMARK 280 0.1M HEPES, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298.0K. 8% PEG 4K, 0.2 M IMIDAZOLE MALEATE, PH 6.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K. 27% PEG 600, 0.1M REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z 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 62.10050 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F 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 ILE B 16 REMARK 465 VAL B 17 REMARK 465 ARG B 18 REMARK 465 GLY C 263 REMARK 465 ASN C 264 REMARK 465 LYS C 265 REMARK 465 ALA C 431 REMARK 465 GLY D 261 REMARK 465 GLU D 262 REMARK 465 GLY D 263 REMARK 465 ALA D 431 REMARK 465 ILE E 16 REMARK 465 VAL E 17 REMARK 465 ARG E 18 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 2 CG CD CE NZ REMARK 470 LYS A 5 CG CD CE NZ REMARK 470 GLU A 235 CG CD OE1 OE2 REMARK 470 LYS A 256 CG CD CE NZ REMARK 470 ASN A 264 CG OD1 ND2 REMARK 470 LYS A 265 CG CD CE NZ REMARK 470 GLN A 282 CG CD OE1 NE2 REMARK 470 LYS A 310 CG CD CE NZ REMARK 470 LYS A 324 CG CD CE NZ REMARK 470 GLU A 331 CG CD OE1 OE2 REMARK 470 LYS C 305 CG CD CE NZ REMARK 470 GLU C 417 CG CD OE1 OE2 REMARK 470 GLU D 100 CG CD OE1 OE2 REMARK 470 ASP D 160 CG OD1 OD2 REMARK 470 ASN D 162 CG OD1 ND2 REMARK 470 LYS D 197 CG CD CE NZ REMARK 470 LYS D 253 CG CD CE NZ REMARK 470 ASP D 254 CG OD1 OD2 REMARK 470 ASN D 264 CG OD1 ND2 REMARK 470 GLU D 278 CG CD OE1 OE2 REMARK 470 LYS D 305 CG CD CE NZ REMARK 470 LYS D 324 CG CD CE NZ REMARK 470 GLU D 417 CG CD OE1 OE2 REMARK 470 LYS F 2 CG CD CE NZ REMARK 470 GLN F 76 CG CD OE1 NE2 REMARK 470 LYS F 265 CG CD CE NZ REMARK 470 LYS F 310 CG CD CE NZ REMARK 470 LYS F 324 CG CD CE NZ REMARK 470 LYS F 359 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 OG SER F 249 O HOH 1932 1.93 REMARK 500 O HOH 410 O HOH 1940 1.94 REMARK 500 O HOH 485 O HOH 1934 1.98 REMARK 500 O HOH 1236 O HOH 1933 2.11 REMARK 500 O HOH 324 O HOH 1938 2.16 REMARK 500 O HOH 941 O HOH 1937 2.17 REMARK 500 O HOH 303 O HOH 1926 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU C 375 CB GLU C 375 CG 0.060 REMARK 500 GLU D 375 CB GLU D 375 CG 0.076 REMARK 500 PRO F 18 CB PRO F 18 CG -0.062 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLU A 375 CA - CB - CG ANGL. DEV. = 7.6 DEGREES REMARK 500 LYS C 392 N - CA - C ANGL. DEV. = -7.2 DEGREES REMARK 500 LEU F 236 CA - CB - CG ANGL. DEV. = 7.2 DEGREES REMARK 500 LEU F 236 CB - CG - CD2 ANGL. DEV. = 7.4 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ARG A 398 123.79 78.01 REMARK 500 ARG C 398 123.72 75.67 REMARK 500 ARG D 398 123.00 75.87 REMARK 500 ARG F 398 126.88 75.30 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 748 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH 807 DISTANCE = 5.26 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E9I RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH MINIMAL BINDING PEPTIDE REMARK 900 FROM RNASE E. DBREF 2FYM A 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM C 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM D 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM F 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM B 1 18 UNP P21513 RNE_ECOLI 833 850 DBREF 2FYM E 1 18 UNP P21513 RNE_ECOLI 833 850 SEQRES 1 A 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 A 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 A 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 A 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 A 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 A 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 A 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 A 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 A 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 A 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 A 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 A 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 A 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 A 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 A 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 A 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 A 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 A 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 A 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 A 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 A 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 A 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 A 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 A 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 A 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 A 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 A 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 A 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 A 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 A 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 A 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 A 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 A 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 A 431 GLN ALA SEQRES 1 B 18 ALA SER PRO GLU LEU ALA SER GLY LYS VAL TRP ILE ARG SEQRES 2 B 18 TYR PRO ILE VAL ARG SEQRES 1 C 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 C 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 C 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 C 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 C 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 C 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 C 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 C 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 C 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 C 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 C 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 C 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 C 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 C 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 C 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 C 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 C 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 C 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 C 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 C 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 C 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 C 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 C 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 C 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 C 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 C 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 C 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 C 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 C 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 C 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 C 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 C 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 C 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 C 431 GLN ALA SEQRES 1 D 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 D 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 D 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 D 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 D 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 D 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 D 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 D 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 D 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 D 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 D 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 D 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 D 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 D 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 D 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 D 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 D 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 D 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 D 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 D 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 D 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 D 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 D 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 D 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 D 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 D 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 D 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 D 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 D 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 D 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 D 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 D 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 D 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 D 431 GLN ALA SEQRES 1 E 18 ALA SER PRO GLU LEU ALA SER GLY LYS VAL TRP ILE ARG SEQRES 2 E 18 TYR PRO ILE VAL ARG SEQRES 1 F 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 F 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 F 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 F 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 F 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 F 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 F 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 F 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 F 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 F 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 F 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 F 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 F 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 F 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 F 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 F 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 F 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 F 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 F 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 F 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 F 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 F 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 F 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 F 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 F 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 F 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 F 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 F 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 F 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 F 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 F 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 F 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 F 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 F 431 GLN ALA HET MG A1431 1 HET MG C1431 1 HET MG D1431 1 HET MG F1431 1 HETNAM MG MAGNESIUM ION FORMUL 7 MG 4(MG 2+) FORMUL 11 HOH *1930(H2 O) HELIX 1 1 ARG A 57 LYS A 61 5 5 HELIX 2 2 VAL A 63 GLY A 72 1 10 HELIX 3 3 GLY A 72 ILE A 79 1 8 HELIX 4 4 ASP A 85 GLY A 98 1 14 HELIX 5 5 GLY A 106 LYS A 125 1 20 HELIX 6 6 PRO A 128 ASN A 137 1 10 HELIX 7 7 GLY A 156 ALA A 159 5 4 HELIX 8 8 THR A 177 LYS A 199 1 23 HELIX 9 9 SER A 217 ALA A 232 1 16 HELIX 10 10 ALA A 247 GLU A 250 5 4 HELIX 11 11 ALA A 260 GLY A 263 5 4 HELIX 12 12 THR A 268 TYR A 283 1 16 HELIX 13 13 ASP A 296 GLY A 308 1 13 HELIX 14 14 ASN A 322 LYS A 332 1 11 HELIX 15 15 LYS A 341 ILE A 345 5 5 HELIX 16 16 SER A 347 ALA A 361 1 15 HELIX 17 17 ALA A 377 THR A 386 1 10 HELIX 18 18 ARG A 398 GLY A 416 1 19 HELIX 19 19 GLU A 417 ALA A 419 5 3 HELIX 20 20 ASN A 422 ILE A 427 5 6 HELIX 21 21 SER B 2 SER B 7 1 6 HELIX 22 22 ARG C 57 LYS C 61 5 5 HELIX 23 23 VAL C 63 GLY C 72 1 10 HELIX 24 24 GLY C 72 ILE C 79 1 8 HELIX 25 25 ASP C 85 GLY C 98 1 14 HELIX 26 26 GLY C 106 LYS C 125 1 20 HELIX 27 27 PRO C 128 GLY C 138 1 11 HELIX 28 28 GLY C 156 ALA C 159 5 4 HELIX 29 29 THR C 177 LYS C 199 1 23 HELIX 30 30 SER C 217 ALA C 232 1 16 HELIX 31 31 ALA C 247 GLU C 250 5 4 HELIX 32 32 THR C 268 TYR C 283 1 16 HELIX 33 33 ASP C 296 GLY C 308 1 13 HELIX 34 34 ASN C 322 GLY C 333 1 12 HELIX 35 35 LYS C 341 GLY C 346 1 6 HELIX 36 36 SER C 347 ALA C 361 1 15 HELIX 37 37 ALA C 377 THR C 386 1 10 HELIX 38 38 ARG C 398 GLY C 416 1 19 HELIX 39 39 GLU C 417 ALA C 419 5 3 HELIX 40 40 ASN C 422 ILE C 427 5 6 HELIX 41 41 ARG D 57 LYS D 61 5 5 HELIX 42 42 VAL D 63 GLY D 72 1 10 HELIX 43 43 GLY D 72 ILE D 79 1 8 HELIX 44 44 ASP D 85 GLY D 98 1 14 HELIX 45 45 GLY D 106 LYS D 125 1 20 HELIX 46 46 PRO D 128 ASN D 137 1 10 HELIX 47 47 GLY D 156 ALA D 159 5 4 HELIX 48 48 THR D 177 LYS D 199 1 23 HELIX 49 49 SER D 217 ALA D 232 1 16 HELIX 50 50 ALA D 247 GLU D 250 5 4 HELIX 51 51 THR D 268 TYR D 283 1 16 HELIX 52 52 ASP D 296 GLY D 308 1 13 HELIX 53 53 ASN D 322 LYS D 332 1 11 HELIX 54 54 LYS D 341 GLY D 346 1 6 HELIX 55 55 SER D 347 GLY D 362 1 16 HELIX 56 56 ALA D 377 THR D 386 1 10 HELIX 57 57 ARG D 398 GLY D 416 1 19 HELIX 58 58 GLU D 417 ALA D 419 5 3 HELIX 59 59 ASN D 422 ILE D 427 5 6 HELIX 60 60 SER E 2 SER E 7 1 6 HELIX 61 61 ARG F 57 LYS F 61 5 5 HELIX 62 62 VAL F 63 GLY F 72 1 10 HELIX 63 63 GLY F 72 ILE F 79 1 8 HELIX 64 64 ASP F 85 GLY F 98 1 14 HELIX 65 65 GLY F 106 LYS F 125 1 20 HELIX 66 66 PRO F 128 ASN F 137 1 10 HELIX 67 67 GLY F 156 ALA F 159 5 4 HELIX 68 68 THR F 177 LYS F 199 1 23 HELIX 69 69 SER F 217 ALA F 232 1 16 HELIX 70 70 ALA F 247 GLU F 250 5 4 HELIX 71 71 THR F 268 TYR F 283 1 16 HELIX 72 72 ASP F 296 GLY F 308 1 13 HELIX 73 73 ASN F 322 LYS F 332 1 11 HELIX 74 74 LYS F 341 GLY F 346 1 6 HELIX 75 75 SER F 347 ALA F 361 1 15 HELIX 76 76 ALA F 377 THR F 386 1 10 HELIX 77 77 ARG F 398 GLY F 416 1 19 HELIX 78 78 GLU F 417 ALA F 419 5 3 HELIX 79 79 ASN F 422 ILE F 427 5 6 SHEET 1 A 3 ILE A 3 ILE A 12 0 SHEET 2 A 3 PRO A 18 LEU A 26 -1 O HIS A 25 N LYS A 5 SHEET 3 A 3 VAL A 31 ALA A 35 -1 O ALA A 34 N ALA A 22 SHEET 1 B 9 VAL A 147 PRO A 148 0 SHEET 2 B 9 GLY A 389 LYS A 392 1 O GLY A 389 N VAL A 147 SHEET 3 B 9 THR A 364 SER A 368 1 N ILE A 367 O LYS A 392 SHEET 4 B 9 SER A 337 ILE A 340 1 N ILE A 340 O VAL A 366 SHEET 5 B 9 GLN A 312 GLY A 315 1 N GLY A 315 O LEU A 339 SHEET 6 B 9 ILE A 285 GLU A 289 1 N ILE A 288 O GLN A 312 SHEET 7 B 9 THR A 241 ASP A 245 1 N MET A 244 O GLU A 289 SHEET 8 B 9 GLU A 167 GLN A 171 -1 N MET A 169 O ALA A 243 SHEET 9 B 9 MET A 150 ASN A 154 -1 N MET A 150 O ILE A 170 SHEET 1 C 3 TYR A 252 LYS A 253 0 SHEET 2 C 3 LYS A 256 VAL A 258 -1 O LYS A 256 N LYS A 253 SHEET 3 C 3 ALA A 266 PHE A 267 -1 O PHE A 267 N TYR A 257 SHEET 1 D 3 ILE C 3 ILE C 12 0 SHEET 2 D 3 PRO C 18 LEU C 26 -1 O HIS C 25 N LYS C 5 SHEET 3 D 3 VAL C 31 ALA C 35 -1 O ALA C 34 N ALA C 22 SHEET 1 E 9 VAL C 147 PRO C 148 0 SHEET 2 E 9 GLY C 389 LYS C 392 1 O GLY C 389 N VAL C 147 SHEET 3 E 9 THR C 364 SER C 368 1 N ILE C 367 O LYS C 392 SHEET 4 E 9 SER C 337 ILE C 340 1 N ILE C 340 O VAL C 366 SHEET 5 E 9 GLN C 312 GLY C 315 1 N GLY C 315 O LEU C 339 SHEET 6 E 9 ILE C 285 GLU C 289 1 N ILE C 288 O GLN C 312 SHEET 7 E 9 THR C 241 ASP C 245 1 N MET C 244 O GLU C 289 SHEET 8 E 9 GLU C 167 GLN C 171 -1 N MET C 169 O ALA C 243 SHEET 9 E 9 MET C 150 ASN C 154 -1 N MET C 150 O ILE C 170 SHEET 1 F 2 TYR C 252 LYS C 253 0 SHEET 2 F 2 LYS C 256 TYR C 257 -1 O LYS C 256 N LYS C 253 SHEET 1 G 3 ILE D 3 ILE D 12 0 SHEET 2 G 3 PRO D 18 LEU D 26 -1 O HIS D 25 N LYS D 5 SHEET 3 G 3 VAL D 31 ALA D 35 -1 O ALA D 34 N ALA D 22 SHEET 1 H 9 VAL D 147 PRO D 148 0 SHEET 2 H 9 GLY D 389 LYS D 392 1 O GLY D 389 N VAL D 147 SHEET 3 H 9 THR D 364 SER D 368 1 N ILE D 367 O LYS D 392 SHEET 4 H 9 SER D 337 ILE D 340 1 N ILE D 340 O SER D 368 SHEET 5 H 9 GLN D 312 GLY D 315 1 N GLY D 315 O LEU D 339 SHEET 6 H 9 ILE D 285 GLU D 289 1 N ILE D 288 O GLN D 312 SHEET 7 H 9 THR D 241 ASP D 245 1 N LEU D 242 O VAL D 286 SHEET 8 H 9 GLU D 167 GLN D 171 -1 N MET D 169 O ALA D 243 SHEET 9 H 9 MET D 150 ASN D 154 -1 N MET D 150 O ILE D 170 SHEET 1 I 3 TYR D 252 LYS D 253 0 SHEET 2 I 3 LYS D 256 LEU D 259 -1 O LYS D 256 N LYS D 253 SHEET 3 I 3 LYS D 265 PHE D 267 -1 O PHE D 267 N TYR D 257 SHEET 1 J 3 ILE F 3 ILE F 12 0 SHEET 2 J 3 PRO F 18 LEU F 26 -1 O HIS F 25 N VAL F 4 SHEET 3 J 3 VAL F 31 ALA F 35 -1 O ALA F 34 N ALA F 22 SHEET 1 K 9 VAL F 147 PRO F 148 0 SHEET 2 K 9 GLY F 389 LYS F 392 1 O GLY F 389 N VAL F 147 SHEET 3 K 9 THR F 364 SER F 368 1 N ILE F 367 O LYS F 392 SHEET 4 K 9 SER F 337 ILE F 340 1 N ILE F 340 O VAL F 366 SHEET 5 K 9 GLN F 312 GLY F 315 1 N GLY F 315 O SER F 337 SHEET 6 K 9 ILE F 285 GLU F 289 1 N ILE F 288 O GLN F 312 SHEET 7 K 9 THR F 241 ASP F 245 1 N LEU F 242 O VAL F 286 SHEET 8 K 9 GLU F 167 GLN F 171 -1 N MET F 169 O ALA F 243 SHEET 9 K 9 MET F 150 ASN F 154 -1 N MET F 150 O ILE F 170 SHEET 1 L 3 TYR F 252 LYS F 253 0 SHEET 2 L 3 LYS F 256 LEU F 259 -1 O LYS F 256 N LYS F 253 SHEET 3 L 3 LYS F 265 PHE F 267 -1 O PHE F 267 N TYR F 257 LINK MG MG A1431 OD2 ASP A 245 LINK MG MG A1431 OE2 GLU A 289 LINK MG MG A1431 OD2 ASP A 316 LINK MG MG C1431 OD2 ASP C 245 LINK MG MG C1431 OE2 GLU C 289 LINK MG MG C1431 OD2 ASP C 316 LINK MG MG D1431 OD2 ASP D 245 LINK MG MG D1431 OE2 GLU D 289 LINK MG MG D1431 OD2 ASP D 316 LINK MG MG F1431 OD2 ASP F 245 LINK MG MG F1431 OE2 GLU F 289 LINK MG MG F1431 OD2 ASP F 316 CRYST1 77.054 124.201 96.076 90.00 90.58 90.00 P 1 21 1 8 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 0.012978 0.000000 0.000131 0.00000 SCALE2 0.000000 0.008051 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010409 0.00000 ATOM 1 N SER A 1 15.327 19.512 53.255 1.00 29.56 N ANISOU 1 N SER A 1 3771 3717 3744 69 41 -15 N ATOM 2 CA SER A 1 14.274 18.606 52.699 1.00 29.32 C ANISOU 2 CA SER A 1 3766 3672 3700 74 34 4 C ATOM 3 C SER A 1 14.128 17.369 53.579 1.00 28.87 C ANISOU 3 C SER A 1 3705 3614 3647 91 51 -6 C ATOM 4 O SER A 1 14.929 16.434 53.494 1.00 28.78 O ANISOU 4 O SER A 1 3714 3566 3653 151 51 -23 O ATOM 5 CB SER A 1 14.619 18.212 51.262 1.00 29.70 C ANISOU 5 CB SER A 1 3840 3725 3719 69 20 0 C ATOM 6 OG SER A 1 14.867 19.367 50.472 1.00 30.82 O ANISOU 6 OG SER A 1 3973 3857 3879 5 5 26 O ATOM 7 N LYS A 2 13.113 17.376 54.434 1.00 27.87 N ANISOU 7 N LYS A 2 3583 3473 3531 99 64 1 N ATOM 8 CA LYS A 2 12.966 16.338 55.456 1.00 27.36 C ANISOU 8 CA LYS A 2 3518 3430 3444 108 74 -14 C ATOM 9 C LYS A 2 12.580 14.965 54.887 1.00 26.69 C ANISOU 9 C LYS A 2 3415 3379 3346 115 55 -8 C ATOM 10 O LYS A 2 11.692 14.857 54.044 1.00 26.40 O ANISOU 10 O LYS A 2 3412 3333 3282 172 65 -39 O ATOM 11 CB LYS A 2 11.969 16.782 56.534 1.00 27.46 C ANISOU 11 CB LYS A 2 3518 3468 3448 122 102 -9 C ATOM 12 N ILE A 3 13.265 13.924 55.365 1.00 25.93 N ANISOU 12 N ILE A 3 3303 3294 3253 122 45 -6 N ATOM 13 CA ILE A 3 12.922 12.541 55.036 1.00 25.46 C ANISOU 13 CA ILE A 3 3227 3280 3163 113 24 47 C ATOM 14 C ILE A 3 11.641 12.147 55.771 1.00 25.56 C ANISOU 14 C ILE A 3 3224 3290 3194 118 36 10 C ATOM 15 O ILE A 3 11.513 12.388 56.977 1.00 25.76 O ANISOU 15 O ILE A 3 3283 3327 3175 167 32 17 O ATOM 16 CB ILE A 3 14.082 11.570 55.413 1.00 25.40 C ANISOU 16 CB ILE A 3 3167 3285 3196 109 52 22 C ATOM 17 CG1 ILE A 3 15.315 11.856 54.543 1.00 24.18 C ANISOU 17 CG1 ILE A 3 3049 3139 2998 94 48 84 C ATOM 18 CG2 ILE A 3 13.636 10.097 55.323 1.00 24.93 C ANISOU 18 CG2 ILE A 3 3195 3237 3038 90 45 27 C ATOM 19 CD1 ILE A 3 16.595 11.180 55.025 1.00 24.85 C ANISOU 19 CD1 ILE A 3 3162 3201 3075 122 -53 76 C ATOM 20 N VAL A 4 10.699 11.546 55.045 1.00 25.43 N ANISOU 20 N VAL A 4 3210 3302 3148 107 47 13 N ATOM 21 CA VAL A 4 9.435 11.109 55.643 1.00 25.76 C ANISOU 21 CA VAL A 4 3241 3333 3210 92 60 -5 C ATOM 22 C VAL A 4 9.265 9.586 55.703 1.00 25.53 C ANISOU 22 C VAL A 4 3211 3320 3169 110 93 6 C ATOM 23 O VAL A 4 8.630 9.065 56.621 1.00 25.54 O ANISOU 23 O VAL A 4 3167 3356 3179 134 146 27 O ATOM 24 CB VAL A 4 8.202 11.789 54.975 1.00 25.72 C ANISOU 24 CB VAL A 4 3252 3344 3175 81 36 0 C ATOM 25 CG1 VAL A 4 8.306 13.306 55.095 1.00 26.01 C ANISOU 25 CG1 VAL A 4 3319 3342 3222 95 46 -17 C ATOM 26 CG2 VAL A 4 8.052 11.375 53.516 1.00 26.64 C ANISOU 26 CG2 VAL A 4 3402 3429 3292 94 33 -64 C ATOM 27 N LYS A 5 9.833 8.874 54.729 1.00 25.15 N ANISOU 27 N LYS A 5 3116 3283 3156 111 131 -6 N ATOM 28 CA LYS A 5 9.741 7.423 54.689 1.00 24.71 C ANISOU 28 CA LYS A 5 3052 3250 3085 112 141 10 C ATOM 29 C LYS A 5 10.945 6.840 53.970 1.00 24.26 C ANISOU 29 C LYS A 5 3027 3151 3038 130 133 1 C ATOM 30 O LYS A 5 11.441 7.417 53.002 1.00 23.81 O ANISOU 30 O LYS A 5 2971 3098 2978 139 127 22 O ATOM 31 CB LYS A 5 8.465 6.963 53.982 1.00 25.46 C ANISOU 31 CB LYS A 5 3115 3362 3196 74 127 9 C ATOM 32 N ILE A 6 11.416 5.704 54.472 1.00 23.88 N ANISOU 32 N ILE A 6 3010 3121 2939 125 134 39 N ATOM 33 CA ILE A 6 12.444 4.925 53.792 1.00 23.50 C ANISOU 33 CA ILE A 6 2990 3044 2893 112 113 2 C ATOM 34 C ILE A 6 11.952 3.491 53.680 1.00 23.46 C ANISOU 34 C ILE A 6 2963 3044 2907 138 127 45 C ATOM 35 O ILE A 6 11.461 2.904 54.646 1.00 23.99 O ANISOU 35 O ILE A 6 3088 3105 2920 137 154 56 O ATOM 36 CB ILE A 6 13.820 5.008 54.498 1.00 23.84 C ANISOU 36 CB ILE A 6 2991 3097 2969 116 143 42 C ATOM 37 CG1 ILE A 6 14.329 6.453 54.488 1.00 23.78 C ANISOU 37 CG1 ILE A 6 3058 3049 2928 108 144 -99 C ATOM 38 CG2 ILE A 6 14.832 4.085 53.817 1.00 23.48 C ANISOU 38 CG2 ILE A 6 3024 3029 2866 96 87 -66 C ATOM 39 CD1 ILE A 6 15.626 6.685 55.200 1.00 25.09 C ANISOU 39 CD1 ILE A 6 3240 3242 3052 141 89 -39 C ATOM 40 N ILE A 7 12.061 2.946 52.477 1.00 22.64 N ANISOU 40 N ILE A 7 2842 2965 2793 144 108 50 N ATOM 41 CA ILE A 7 11.609 1.602 52.202 1.00 22.40 C ANISOU 41 CA ILE A 7 2782 2926 2803 156 142 51 C ATOM 42 C ILE A 7 12.775 0.804 51.654 1.00 21.30 C ANISOU 42 C ILE A 7 2657 2769 2667 154 153 103 C ATOM 43 O ILE A 7 13.485 1.264 50.759 1.00 21.11 O ANISOU 43 O ILE A 7 2646 2750 2622 225 232 153 O ATOM 44 CB ILE A 7 10.437 1.579 51.190 1.00 22.48 C ANISOU 44 CB ILE A 7 2786 2931 2824 151 108 47 C ATOM 45 CG1 ILE A 7 9.241 2.371 51.736 1.00 23.55 C ANISOU 45 CG1 ILE A 7 2838 3134 2976 156 100 25 C ATOM 46 CG2 ILE A 7 10.018 0.143 50.880 1.00 22.93 C ANISOU 46 CG2 ILE A 7 2783 2985 2943 105 89 60 C ATOM 47 CD1 ILE A 7 8.172 2.679 50.697 1.00 23.99 C ANISOU 47 CD1 ILE A 7 3018 3130 2967 140 110 74 C ATOM 48 N GLY A 8 12.981 -0.372 52.235 1.00 20.02 N ANISOU 48 N GLY A 8 2499 2593 2513 166 188 107 N ATOM 49 CA GLY A 8 13.926 -1.344 51.714 1.00 18.47 C ANISOU 49 CA GLY A 8 2314 2426 2275 128 128 151 C ATOM 50 C GLY A 8 13.184 -2.530 51.156 1.00 18.01 C ANISOU 50 C GLY A 8 2198 2409 2234 120 100 168 C ATOM 51 O GLY A 8 12.122 -2.924 51.671 1.00 17.54 O ANISOU 51 O GLY A 8 2063 2385 2213 129 130 171 O ATOM 52 N ARG A 9 13.748 -3.123 50.108 1.00 16.62 N ANISOU 52 N ARG A 9 2053 2220 2042 121 64 199 N ATOM 53 CA ARG A 9 13.201 -4.352 49.563 1.00 16.89 C ANISOU 53 CA ARG A 9 2115 2218 2081 98 72 222 C ATOM 54 C ARG A 9 14.276 -5.232 48.944 1.00 16.90 C ANISOU 54 C ARG A 9 2128 2186 2104 77 62 238 C ATOM 55 O ARG A 9 15.347 -4.762 48.524 1.00 16.48 O ANISOU 55 O ARG A 9 2103 2136 2020 28 -19 424 O ATOM 56 CB ARG A 9 12.071 -4.083 48.556 1.00 16.92 C ANISOU 56 CB ARG A 9 2098 2253 2074 133 64 228 C ATOM 57 CG ARG A 9 12.510 -3.486 47.217 1.00 16.78 C ANISOU 57 CG ARG A 9 2064 2246 2065 38 130 231 C ATOM 58 CD ARG A 9 11.341 -3.478 46.204 1.00 15.68 C ANISOU 58 CD ARG A 9 1926 2053 1978 112 147 271 C ATOM 59 NE ARG A 9 10.257 -2.623 46.698 1.00 15.91 N ANISOU 59 NE ARG A 9 2016 2143 1885 147 273 249 N ATOM 60 CZ ARG A 9 10.183 -1.310 46.513 1.00 16.07 C ANISOU 60 CZ ARG A 9 1929 2203 1974 56 155 186 C ATOM 61 NH1 ARG A 9 11.120 -0.659 45.816 1.00 16.12 N ANISOU 61 NH1 ARG A 9 1741 2352 2028 -30 223 263 N ATOM 62 NH2 ARG A 9 9.162 -0.640 47.018 1.00 17.20 N ANISOU 62 NH2 ARG A 9 2049 2389 2095 194 229 90 N ATOM 63 N GLU A 10 13.975 -6.520 48.917 1.00 16.85 N ANISOU 63 N GLU A 10 2198 2132 2071 11 78 270 N ATOM 64 CA GLU A 10 14.828 -7.510 48.294 1.00 16.41 C ANISOU 64 CA GLU A 10 2109 2066 2060 -13 113 280 C ATOM 65 C GLU A 10 14.389 -7.681 46.844 1.00 16.62 C ANISOU 65 C GLU A 10 2112 2158 2042 -34 90 287 C ATOM 66 O GLU A 10 13.290 -8.181 46.566 1.00 16.44 O ANISOU 66 O GLU A 10 2068 2198 1979 -81 115 360 O ATOM 67 CB GLU A 10 14.708 -8.834 49.055 1.00 17.06 C ANISOU 67 CB GLU A 10 2216 2123 2142 -16 106 292 C ATOM 68 CG GLU A 10 15.551 -9.957 48.502 1.00 17.67 C ANISOU 68 CG GLU A 10 2295 2067 2352 -53 115 307 C ATOM 69 CD GLU A 10 15.310 -11.261 49.242 1.00 17.62 C ANISOU 69 CD GLU A 10 2242 2240 2211 41 99 389 C ATOM 70 OE1 GLU A 10 14.160 -11.731 49.238 1.00 18.22 O ANISOU 70 OE1 GLU A 10 2408 2066 2448 -79 42 457 O ATOM 71 OE2 GLU A 10 16.269 -11.803 49.811 1.00 18.33 O ANISOU 71 OE2 GLU A 10 2134 2515 2312 -5 114 412 O ATOM 72 N ILE A 11 15.248 -7.250 45.917 1.00 16.04 N ANISOU 72 N ILE A 11 2039 2089 1964 -16 86 303 N ATOM 73 CA ILE A 11 15.008 -7.451 44.485 1.00 15.18 C ANISOU 73 CA ILE A 11 1972 1947 1845 28 72 259 C ATOM 74 C ILE A 11 16.055 -8.435 43.946 1.00 14.50 C ANISOU 74 C ILE A 11 1829 1930 1751 27 48 248 C ATOM 75 O ILE A 11 16.827 -9.016 44.726 1.00 14.71 O ANISOU 75 O ILE A 11 1835 2020 1731 101 106 418 O ATOM 76 CB ILE A 11 15.039 -6.101 43.683 1.00 14.88 C ANISOU 76 CB ILE A 11 1935 1871 1846 6 64 245 C ATOM 77 CG1 ILE A 11 16.376 -5.375 43.892 1.00 15.40 C ANISOU 77 CG1 ILE A 11 1995 1956 1898 -79 36 231 C ATOM 78 CG2 ILE A 11 13.867 -5.189 44.089 1.00 16.04 C ANISOU 78 CG2 ILE A 11 2074 2056 1963 95 78 251 C ATOM 79 CD1 ILE A 11 16.680 -4.290 42.832 1.00 16.15 C ANISOU 79 CD1 ILE A 11 2235 2000 1901 -12 100 239 C ATOM 80 N ILE A 12 16.082 -8.635 42.631 1.00 13.86 N ANISOU 80 N ILE A 12 1692 1861 1711 50 113 305 N ATOM 81 CA ILE A 12 16.941 -9.645 42.023 1.00 13.36 C ANISOU 81 CA ILE A 12 1690 1738 1647 -49 134 271 C ATOM 82 C ILE A 12 17.976 -8.954 41.135 1.00 13.11 C ANISOU 82 C ILE A 12 1611 1710 1659 -29 123 292 C ATOM 83 O ILE A 12 17.643 -8.009 40.405 1.00 12.62 O ANISOU 83 O ILE A 12 1546 1628 1620 -6 37 329 O ATOM 84 CB ILE A 12 16.114 -10.668 41.203 1.00 13.15 C ANISOU 84 CB ILE A 12 1605 1728 1661 -13 126 250 C ATOM 85 CG1 ILE A 12 14.926 -11.200 42.039 1.00 14.92 C ANISOU 85 CG1 ILE A 12 1847 2072 1750 -98 148 282 C ATOM 86 CG2 ILE A 12 17.003 -11.810 40.672 1.00 13.61 C ANISOU 86 CG2 ILE A 12 1793 1757 1621 -19 197 229 C ATOM 87 CD1 ILE A 12 15.347 -11.922 43.339 1.00 16.65 C ANISOU 87 CD1 ILE A 12 2088 2263 1972 28 88 301 C ATOM 88 N ASP A 13 19.217 -9.419 41.219 1.00 12.21 N ANISOU 88 N ASP A 13 1472 1584 1582 -94 100 306 N ATOM 89 CA ASP A 13 20.299 -8.858 40.416 1.00 11.93 C ANISOU 89 CA ASP A 13 1489 1564 1478 -80 78 250 C ATOM 90 C ASP A 13 20.476 -9.582 39.076 1.00 11.20 C ANISOU 90 C ASP A 13 1453 1433 1368 -76 70 278 C ATOM 91 O ASP A 13 19.735 -10.523 38.733 1.00 11.04 O ANISOU 91 O ASP A 13 1438 1456 1298 -71 80 408 O ATOM 92 CB ASP A 13 21.608 -8.703 41.242 1.00 12.10 C ANISOU 92 CB ASP A 13 1479 1623 1493 -77 37 290 C ATOM 93 CG ASP A 13 22.459 -9.994 41.324 1.00 12.30 C ANISOU 93 CG ASP A 13 1570 1620 1484 -92 136 182 C ATOM 94 OD1 ASP A 13 22.141 -11.035 40.701 1.00 12.33 O ANISOU 94 OD1 ASP A 13 1725 1457 1502 53 -16 272 O ATOM 95 OD2 ASP A 13 23.502 -9.950 42.025 1.00 14.04 O ANISOU 95 OD2 ASP A 13 1895 1853 1585 -19 -20 248 O ATOM 96 N SER A 14 21.443 -9.122 38.293 1.00 10.93 N ANISOU 96 N SER A 14 1451 1375 1324 -84 94 257 N ATOM 97 CA SER A 14 21.563 -9.592 36.931 1.00 10.82 C ANISOU 97 CA SER A 14 1475 1327 1306 -143 43 232 C ATOM 98 C SER A 14 22.045 -11.027 36.828 1.00 11.31 C ANISOU 98 C SER A 14 1520 1377 1400 -107 12 212 C ATOM 99 O SER A 14 22.039 -11.593 35.740 1.00 11.76 O ANISOU 99 O SER A 14 1592 1384 1491 -202 21 300 O ATOM 100 CB SER A 14 22.503 -8.668 36.150 1.00 10.60 C ANISOU 100 CB SER A 14 1452 1398 1175 -166 108 264 C ATOM 101 OG SER A 14 23.815 -8.671 36.708 1.00 11.81 O ANISOU 101 OG SER A 14 1464 1439 1583 -98 40 281 O ATOM 102 N ARG A 15 22.488 -11.605 37.954 1.00 11.56 N ANISOU 102 N ARG A 15 1592 1325 1473 -75 15 218 N ATOM 103 CA ARG A 15 22.927 -12.999 37.977 1.00 12.60 C ANISOU 103 CA ARG A 15 1618 1513 1654 -24 -30 191 C ATOM 104 C ARG A 15 21.867 -13.871 38.642 1.00 12.88 C ANISOU 104 C ARG A 15 1643 1539 1708 -13 -6 177 C ATOM 105 O ARG A 15 22.070 -15.076 38.810 1.00 14.35 O ANISOU 105 O ARG A 15 1885 1598 1969 -15 -52 151 O ATOM 106 CB ARG A 15 24.274 -13.120 38.698 1.00 12.75 C ANISOU 106 CB ARG A 15 1519 1531 1791 11 20 202 C ATOM 107 CG ARG A 15 25.394 -12.406 37.936 1.00 14.30 C ANISOU 107 CG ARG A 15 1707 1850 1873 -51 21 154 C ATOM 108 CD ARG A 15 26.738 -12.874 38.408 1.00 17.45 C ANISOU 108 CD ARG A 15 1907 2367 2353 -25 -44 -13 C ATOM 109 NE ARG A 15 27.012 -12.408 39.757 1.00 18.25 N ANISOU 109 NE ARG A 15 2192 2497 2242 -66 0 -13 N ATOM 110 CZ ARG A 15 28.211 -12.455 40.332 1.00 21.69 C ANISOU 110 CZ ARG A 15 2535 2894 2812 -42 -41 -6 C ATOM 111 NH1 ARG A 15 29.255 -12.956 39.674 1.00 23.52 N ANISOU 111 NH1 ARG A 15 2709 3174 3051 10 -9 32 N ATOM 112 NH2 ARG A 15 28.364 -11.988 41.566 1.00 23.95 N ANISOU 112 NH2 ARG A 15 2832 3446 2820 -196 -124 11 N ATOM 113 N GLY A 16 20.734 -13.261 39.011 1.00 12.53 N ANISOU 113 N GLY A 16 1635 1538 1587 -2 -3 191 N ATOM 114 CA GLY A 16 19.619 -14.003 39.598 1.00 13.48 C ANISOU 114 CA GLY A 16 1767 1725 1630 -25 -43 232 C ATOM 115 C GLY A 16 19.724 -14.086 41.109 1.00 14.08 C ANISOU 115 C GLY A 16 1803 1857 1689 -73 -7 225 C ATOM 116 O GLY A 16 18.995 -14.844 41.733 1.00 14.76 O ANISOU 116 O GLY A 16 1912 2022 1674 -156 1 412 O ATOM 117 N ASN A 17 20.638 -13.321 41.696 1.00 14.18 N ANISOU 117 N ASN A 17 1865 1752 1769 -93 3 251 N ATOM 118 CA ASN A 17 20.812 -13.308 43.147 1.00 14.28 C ANISOU 118 CA ASN A 17 1831 1780 1814 -83 11 212 C ATOM 119 C ASN A 17 20.162 -12.100 43.813 1.00 14.62 C ANISOU 119 C ASN A 17 1936 1796 1821 -66 40 194 C ATOM 120 O ASN A 17 20.116 -11.014 43.226 1.00 14.56 O ANISOU 120 O ASN A 17 1992 1718 1822 -29 70 266 O ATOM 121 CB ASN A 17 22.296 -13.380 43.503 1.00 14.46 C ANISOU 121 CB ASN A 17 1809 1834 1851 -52 -14 218 C ATOM 122 CG ASN A 17 22.944 -14.651 43.017 1.00 15.91 C ANISOU 122 CG ASN A 17 2045 1958 2040 -53 19 127 C ATOM 123 OD1 ASN A 17 22.430 -15.765 43.247 1.00 16.48 O ANISOU 123 OD1 ASN A 17 2153 1888 2220 13 126 385 O ATOM 124 ND2 ASN A 17 24.072 -14.504 42.318 1.00 17.70 N ANISOU 124 ND2 ASN A 17 2046 2320 2358 9 53 133 N ATOM 125 N PRO A 18 19.635 -12.274 45.037 1.00 14.10 N ANISOU 125 N PRO A 18 1890 1717 1751 -27 73 267 N ATOM 126 CA PRO A 18 19.026 -11.136 45.729 1.00 13.91 C ANISOU 126 CA PRO A 18 1900 1687 1698 -65 104 232 C ATOM 127 C PRO A 18 19.975 -9.950 45.941 1.00 13.83 C ANISOU 127 C PRO A 18 1845 1710 1700 -35 42 173 C ATOM 128 O PRO A 18 21.187 -10.124 46.133 1.00 13.89 O ANISOU 128 O PRO A 18 1856 1676 1744 -20 116 274 O ATOM 129 CB PRO A 18 18.622 -11.727 47.092 1.00 14.30 C ANISOU 129 CB PRO A 18 1935 1778 1717 -33 95 233 C ATOM 130 CG PRO A 18 18.436 -13.133 46.812 1.00 14.06 C ANISOU 130 CG PRO A 18 1904 1719 1719 -41 85 115 C ATOM 131 CD PRO A 18 19.544 -13.493 45.861 1.00 14.22 C ANISOU 131 CD PRO A 18 1946 1694 1761 -74 95 272 C ATOM 132 N THR A 19 19.412 -8.752 45.870 1.00 13.42 N ANISOU 132 N THR A 19 1803 1729 1564 14 18 206 N ATOM 133 CA THR A 19 20.112 -7.567 46.365 1.00 13.56 C ANISOU 133 CA THR A 19 1838 1711 1604 25 50 202 C ATOM 134 C THR A 19 19.157 -6.558 46.999 1.00 13.72 C ANISOU 134 C THR A 19 1857 1780 1575 65 26 230 C ATOM 135 O THR A 19 17.944 -6.768 46.993 1.00 14.16 O ANISOU 135 O THR A 19 1912 1848 1617 131 49 218 O ATOM 136 CB THR A 19 21.052 -6.918 45.311 1.00 13.89 C ANISOU 136 CB THR A 19 1862 1813 1600 20 -21 237 C ATOM 137 OG1 THR A 19 21.940 -6.026 45.987 1.00 13.21 O ANISOU 137 OG1 THR A 19 1755 1755 1507 64 93 179 O ATOM 138 CG2 THR A 19 20.252 -6.172 44.197 1.00 13.16 C ANISOU 138 CG2 THR A 19 1925 1568 1506 -53 -9 310 C ATOM 139 N VAL A 20 19.722 -5.499 47.577 1.00 13.17 N ANISOU 139 N VAL A 20 1821 1729 1453 124 42 256 N ATOM 140 CA VAL A 20 18.943 -4.489 48.284 1.00 13.50 C ANISOU 140 CA VAL A 20 1813 1760 1557 100 72 263 C ATOM 141 C VAL A 20 18.598 -3.323 47.373 1.00 13.60 C ANISOU 141 C VAL A 20 1748 1864 1556 117 58 251 C ATOM 142 O VAL A 20 19.476 -2.764 46.717 1.00 13.87 O ANISOU 142 O VAL A 20 1626 1974 1667 101 60 291 O ATOM 143 CB VAL A 20 19.715 -3.933 49.486 1.00 12.73 C ANISOU 143 CB VAL A 20 1778 1656 1400 149 76 300 C ATOM 144 CG1 VAL A 20 18.895 -2.856 50.214 1.00 14.77 C ANISOU 144 CG1 VAL A 20 2096 1836 1679 233 85 250 C ATOM 145 CG2 VAL A 20 20.113 -5.072 50.446 1.00 14.21 C ANISOU 145 CG2 VAL A 20 2083 1884 1431 159 30 396 C ATOM 146 N GLU A 21 17.320 -2.950 47.364 1.00 14.11 N ANISOU 146 N GLU A 21 1733 2000 1628 84 73 273 N ATOM 147 CA GLU A 21 16.862 -1.707 46.765 1.00 14.71 C ANISOU 147 CA GLU A 21 1822 2018 1749 93 67 176 C ATOM 148 C GLU A 21 16.278 -0.845 47.884 1.00 15.11 C ANISOU 148 C GLU A 21 1880 2088 1771 121 97 185 C ATOM 149 O GLU A 21 15.606 -1.371 48.788 1.00 15.84 O ANISOU 149 O GLU A 21 2008 2193 1814 109 213 270 O ATOM 150 CB GLU A 21 15.803 -2.001 45.712 1.00 14.90 C ANISOU 150 CB GLU A 21 1814 2067 1779 85 55 195 C ATOM 151 CG GLU A 21 15.147 -0.777 45.089 1.00 14.81 C ANISOU 151 CG GLU A 21 1834 2046 1746 10 19 171 C ATOM 152 CD GLU A 21 14.289 -1.179 43.908 1.00 16.12 C ANISOU 152 CD GLU A 21 1867 2432 1827 -51 -23 173 C ATOM 153 OE1 GLU A 21 14.803 -1.101 42.769 1.00 15.95 O ANISOU 153 OE1 GLU A 21 2008 2299 1752 -31 40 311 O ATOM 154 OE2 GLU A 21 13.134 -1.630 44.123 1.00 16.16 O ANISOU 154 OE2 GLU A 21 1930 2473 1735 -80 218 398 O ATOM 155 N ALA A 22 16.566 0.450 47.845 1.00 15.20 N ANISOU 155 N ALA A 22 1947 2088 1740 164 103 206 N ATOM 156 CA ALA A 22 15.999 1.407 48.802 1.00 15.62 C ANISOU 156 CA ALA A 22 2069 2037 1828 206 88 185 C ATOM 157 C ALA A 22 15.281 2.557 48.118 1.00 16.12 C ANISOU 157 C ALA A 22 2095 2117 1911 221 98 184 C ATOM 158 O ALA A 22 15.694 3.000 47.057 1.00 14.93 O ANISOU 158 O ALA A 22 1959 2017 1695 342 145 132 O ATOM 159 CB ALA A 22 17.076 1.952 49.714 1.00 16.48 C ANISOU 159 CB ALA A 22 2140 2208 1910 146 81 183 C ATOM 160 N GLU A 23 14.217 3.045 48.761 1.00 15.91 N ANISOU 160 N GLU A 23 2052 2100 1893 255 123 176 N ATOM 161 CA GLU A 23 13.549 4.279 48.353 1.00 17.23 C ANISOU 161 CA GLU A 23 2233 2203 2109 185 42 128 C ATOM 162 C GLU A 23 13.641 5.271 49.493 1.00 18.06 C ANISOU 162 C GLU A 23 2335 2335 2190 205 61 107 C ATOM 163 O GLU A 23 13.406 4.919 50.659 1.00 18.85 O ANISOU 163 O GLU A 23 2426 2454 2281 246 42 210 O ATOM 164 CB GLU A 23 12.071 4.043 48.058 1.00 17.37 C ANISOU 164 CB GLU A 23 2261 2206 2132 203 45 151 C ATOM 165 CG GLU A 23 11.787 3.156 46.886 1.00 18.25 C ANISOU 165 CG GLU A 23 2367 2305 2261 123 -2 92 C ATOM 166 CD GLU A 23 10.309 2.852 46.731 1.00 18.97 C ANISOU 166 CD GLU A 23 2290 2472 2445 53 98 42 C ATOM 167 OE1 GLU A 23 9.473 3.531 47.382 1.00 21.95 O ANISOU 167 OE1 GLU A 23 2683 2955 2700 66 184 -109 O ATOM 168 OE2 GLU A 23 9.975 1.956 45.932 1.00 18.96 O ANISOU 168 OE2 GLU A 23 2218 2566 2417 240 230 42 O ATOM 169 N VAL A 24 13.962 6.513 49.161 1.00 17.93 N ANISOU 169 N VAL A 24 2286 2336 2190 203 60 102 N ATOM 170 CA VAL A 24 13.944 7.581 50.148 1.00 18.30 C ANISOU 170 CA VAL A 24 2380 2355 2215 246 11 63 C ATOM 171 C VAL A 24 12.888 8.601 49.701 1.00 19.04 C ANISOU 171 C VAL A 24 2410 2484 2337 256 32 72 C ATOM 172 O VAL A 24 12.970 9.153 48.605 1.00 18.62 O ANISOU 172 O VAL A 24 2294 2495 2285 307 140 72 O ATOM 173 CB VAL A 24 15.336 8.222 50.355 1.00 17.99 C ANISOU 173 CB VAL A 24 2385 2297 2151 229 1 70 C ATOM 174 CG1 VAL A 24 15.244 9.471 51.239 1.00 17.51 C ANISOU 174 CG1 VAL A 24 2413 2217 2023 306 27 89 C ATOM 175 CG2 VAL A 24 16.316 7.206 50.971 1.00 17.82 C ANISOU 175 CG2 VAL A 24 2306 2382 2083 225 -22 10 C ATOM 176 N HIS A 25 11.887 8.797 50.558 1.00 19.88 N ANISOU 176 N HIS A 25 2465 2643 2446 229 46 16 N ATOM 177 CA HIS A 25 10.767 9.703 50.302 1.00 21.03 C ANISOU 177 CA HIS A 25 2636 2720 2633 165 4 31 C ATOM 178 C HIS A 25 10.903 10.958 51.164 1.00 21.50 C ANISOU 178 C HIS A 25 2674 2798 2694 167 33 -11 C ATOM 179 O HIS A 25 11.189 10.865 52.367 1.00 21.71 O ANISOU 179 O HIS A 25 2686 2843 2718 202 66 -8 O ATOM 180 CB HIS A 25 9.437 8.995 50.607 1.00 21.00 C ANISOU 180 CB HIS A 25 2628 2725 2625 116 6 25 C ATOM 181 CG HIS A 25 9.152 7.821 49.715 1.00 21.04 C ANISOU 181 CG HIS A 25 2671 2703 2620 50 35 44 C ATOM 182 ND1 HIS A 25 8.170 7.843 48.746 1.00 20.47 N ANISOU 182 ND1 HIS A 25 2564 2628 2585 67 80 51 N ATOM 183 CD2 HIS A 25 9.729 6.598 49.636 1.00 20.69 C ANISOU 183 CD2 HIS A 25 2610 2683 2565 36 68 42 C ATOM 184 CE1 HIS A 25 8.149 6.683 48.115 1.00 21.85 C ANISOU 184 CE1 HIS A 25 2803 2872 2625 48 32 14 C ATOM 185 NE2 HIS A 25 9.085 5.909 48.637 1.00 20.90 N ANISOU 185 NE2 HIS A 25 2645 2674 2621 119 88 14 N ATOM 186 N LEU A 26 10.703 12.123 50.545 1.00 22.05 N ANISOU 186 N LEU A 26 2729 2837 2810 171 50 -22 N ATOM 187 CA LEU A 26 10.831 13.414 51.230 1.00 22.41 C ANISOU 187 CA LEU A 26 2766 2876 2872 149 51 -23 C ATOM 188 C LEU A 26 9.508 14.176 51.271 1.00 23.44 C ANISOU 188 C LEU A 26 2880 3006 3019 141 57 -26 C ATOM 189 O LEU A 26 8.614 13.946 50.459 1.00 23.78 O ANISOU 189 O LEU A 26 2976 3071 2986 182 101 -28 O ATOM 190 CB LEU A 26 11.873 14.302 50.543 1.00 21.78 C ANISOU 190 CB LEU A 26 2669 2807 2798 169 25 -42 C ATOM 191 CG LEU A 26 13.231 13.685 50.172 1.00 21.26 C ANISOU 191 CG LEU A 26 2556 2795 2725 165 55 38 C ATOM 192 CD1 LEU A 26 14.158 14.746 49.597 1.00 21.55 C ANISOU 192 CD1 LEU A 26 2652 2753 2781 123 -21 31 C ATOM 193 CD2 LEU A 26 13.863 12.987 51.376 1.00 20.90 C ANISOU 193 CD2 LEU A 26 2610 2697 2633 156 107 -7 C ATOM 194 N GLU A 27 9.399 15.098 52.219 1.00 24.98 N ANISOU 194 N GLU A 27 3139 3180 3169 125 54 -38 N ATOM 195 CA GLU A 27 8.293 16.060 52.204 1.00 26.45 C ANISOU 195 CA GLU A 27 3310 3354 3386 132 35 -21 C ATOM 196 C GLU A 27 8.271 16.757 50.842 1.00 26.42 C ANISOU 196 C GLU A 27 3321 3345 3370 123 38 -22 C ATOM 197 O GLU A 27 9.318 17.131 50.315 1.00 26.83 O ANISOU 197 O GLU A 27 3383 3395 3416 147 64 32 O ATOM 198 CB GLU A 27 8.448 17.085 53.330 1.00 26.78 C ANISOU 198 CB GLU A 27 3365 3383 3424 115 32 -11 C ATOM 199 CG GLU A 27 9.842 17.675 53.429 1.00 28.65 C ANISOU 199 CG GLU A 27 3567 3636 3680 27 22 -66 C ATOM 200 CD GLU A 27 9.955 18.868 54.355 1.00 29.51 C ANISOU 200 CD GLU A 27 3734 3718 3759 71 17 -45 C ATOM 201 OE1 GLU A 27 8.949 19.223 55.031 1.00 32.53 O ANISOU 201 OE1 GLU A 27 3941 4240 4176 85 141 -185 O ATOM 202 OE2 GLU A 27 11.070 19.451 54.399 1.00 30.76 O ANISOU 202 OE2 GLU A 27 3705 3895 4086 15 -1 -40 O ATOM 203 N GLY A 28 7.085 16.908 50.263 1.00 26.64 N ANISOU 203 N GLY A 28 3356 3372 3392 153 41 -5 N ATOM 204 CA GLY A 28 6.975 17.499 48.928 1.00 26.21 C ANISOU 204 CA GLY A 28 3295 3297 3364 160 48 0 C ATOM 205 C GLY A 28 6.775 16.479 47.828 1.00 26.10 C ANISOU 205 C GLY A 28 3306 3273 3336 150 70 11 C ATOM 206 O GLY A 28 6.530 16.844 46.674 1.00 26.43 O ANISOU 206 O GLY A 28 3369 3268 3404 204 41 7 O ATOM 207 N GLY A 29 6.896 15.198 48.183 1.00 25.51 N ANISOU 207 N GLY A 29 3194 3197 3300 133 81 -7 N ATOM 208 CA GLY A 29 6.632 14.098 47.253 1.00 24.54 C ANISOU 208 CA GLY A 29 3017 3146 3160 149 114 -5 C ATOM 209 C GLY A 29 7.834 13.609 46.463 1.00 23.51 C ANISOU 209 C GLY A 29 2868 3037 3029 117 112 0 C ATOM 210 O GLY A 29 7.698 12.753 45.589 1.00 24.21 O ANISOU 210 O GLY A 29 2852 3211 3133 136 197 -25 O ATOM 211 N PHE A 30 9.009 14.136 46.781 1.00 22.76 N ANISOU 211 N PHE A 30 2833 2898 2916 160 144 33 N ATOM 212 CA PHE A 30 10.237 13.754 46.072 1.00 21.68 C ANISOU 212 CA PHE A 30 2722 2706 2810 187 118 68 C ATOM 213 C PHE A 30 10.711 12.366 46.490 1.00 20.50 C ANISOU 213 C PHE A 30 2645 2515 2626 176 109 33 C ATOM 214 O PHE A 30 10.728 12.046 47.677 1.00 19.96 O ANISOU 214 O PHE A 30 2628 2417 2536 263 136 15 O ATOM 215 CB PHE A 30 11.331 14.790 46.321 1.00 21.88 C ANISOU 215 CB PHE A 30 2776 2698 2836 120 77 45 C ATOM 216 CG PHE A 30 10.885 16.195 46.053 1.00 23.19 C ANISOU 216 CG PHE A 30 2957 2833 3019 136 52 78 C ATOM 217 CD1 PHE A 30 10.714 16.643 44.745 1.00 23.63 C ANISOU 217 CD1 PHE A 30 2976 2981 3019 46 97 55 C ATOM 218 CD2 PHE A 30 10.598 17.057 47.108 1.00 24.05 C ANISOU 218 CD2 PHE A 30 3174 2866 3095 83 16 46 C ATOM 219 CE1 PHE A 30 10.282 17.943 44.490 1.00 23.82 C ANISOU 219 CE1 PHE A 30 3081 2933 3036 70 115 24 C ATOM 220 CE2 PHE A 30 10.154 18.365 46.865 1.00 24.12 C ANISOU 220 CE2 PHE A 30 3155 2917 3089 143 43 50 C ATOM 221 CZ PHE A 30 10.002 18.805 45.553 1.00 24.01 C ANISOU 221 CZ PHE A 30 3192 2892 3036 122 73 47 C ATOM 222 N VAL A 31 11.078 11.544 45.509 1.00 19.28 N ANISOU 222 N VAL A 31 2433 2430 2460 240 187 103 N ATOM 223 CA VAL A 31 11.470 10.160 45.787 1.00 18.63 C ANISOU 223 CA VAL A 31 2290 2407 2378 208 147 75 C ATOM 224 C VAL A 31 12.772 9.866 45.055 1.00 17.93 C ANISOU 224 C VAL A 31 2196 2365 2250 233 157 89 C ATOM 225 O VAL A 31 12.932 10.244 43.901 1.00 18.49 O ANISOU 225 O VAL A 31 2227 2463 2334 351 119 202 O ATOM 226 CB VAL A 31 10.383 9.146 45.310 1.00 18.56 C ANISOU 226 CB VAL A 31 2304 2368 2379 161 147 97 C ATOM 227 CG1 VAL A 31 10.740 7.718 45.717 1.00 19.11 C ANISOU 227 CG1 VAL A 31 2408 2382 2470 171 125 49 C ATOM 228 CG2 VAL A 31 9.018 9.511 45.881 1.00 19.88 C ANISOU 228 CG2 VAL A 31 2364 2619 2568 167 109 57 C ATOM 229 N GLY A 32 13.695 9.202 45.743 1.00 17.32 N ANISOU 229 N GLY A 32 2125 2318 2136 242 178 113 N ATOM 230 CA GLY A 32 14.881 8.613 45.103 1.00 16.88 C ANISOU 230 CA GLY A 32 2092 2248 2072 179 154 71 C ATOM 231 C GLY A 32 14.881 7.108 45.315 1.00 16.84 C ANISOU 231 C GLY A 32 2143 2246 2006 182 146 91 C ATOM 232 O GLY A 32 14.450 6.620 46.372 1.00 17.08 O ANISOU 232 O GLY A 32 2223 2302 1963 194 202 146 O ATOM 233 N MET A 33 15.328 6.354 44.309 1.00 15.96 N ANISOU 233 N MET A 33 2018 2107 1939 154 128 67 N ATOM 234 CA MET A 33 15.417 4.914 44.448 1.00 15.71 C ANISOU 234 CA MET A 33 1931 2095 1943 168 127 139 C ATOM 235 C MET A 33 16.733 4.435 43.872 1.00 14.94 C ANISOU 235 C MET A 33 1874 1964 1837 163 122 80 C ATOM 236 O MET A 33 17.167 4.934 42.845 1.00 14.33 O ANISOU 236 O MET A 33 1829 1911 1703 278 192 163 O ATOM 237 CB MET A 33 14.243 4.223 43.745 1.00 16.04 C ANISOU 237 CB MET A 33 2025 2069 2000 54 82 90 C ATOM 238 CG MET A 33 14.155 2.714 43.996 1.00 16.69 C ANISOU 238 CG MET A 33 2194 2092 2052 141 39 162 C ATOM 239 SD MET A 33 12.616 1.965 43.407 1.00 18.86 S ANISOU 239 SD MET A 33 2319 2539 2306 112 55 384 S ATOM 240 CE MET A 33 12.995 1.987 41.657 1.00 16.32 C ANISOU 240 CE MET A 33 1964 2138 2099 262 49 60 C ATOM 241 N ALA A 34 17.374 3.505 44.572 1.00 13.60 N ANISOU 241 N ALA A 34 1695 1741 1729 173 140 63 N ATOM 242 CA ALA A 34 18.651 2.940 44.113 1.00 13.04 C ANISOU 242 CA ALA A 34 1619 1675 1659 174 124 68 C ATOM 243 C ALA A 34 18.817 1.526 44.624 1.00 13.42 C ANISOU 243 C ALA A 34 1737 1708 1650 153 119 124 C ATOM 244 O ALA A 34 18.183 1.121 45.603 1.00 13.63 O ANISOU 244 O ALA A 34 1750 1795 1632 241 160 192 O ATOM 245 CB ALA A 34 19.825 3.788 44.592 1.00 13.58 C ANISOU 245 CB ALA A 34 1701 1735 1723 88 124 26 C ATOM 246 N ALA A 35 19.693 0.781 43.968 1.00 12.75 N ANISOU 246 N ALA A 35 1632 1638 1571 177 83 149 N ATOM 247 CA ALA A 35 19.990 -0.584 44.403 1.00 12.94 C ANISOU 247 CA ALA A 35 1688 1646 1581 129 16 142 C ATOM 248 C ALA A 35 21.481 -0.775 44.553 1.00 13.17 C ANISOU 248 C ALA A 35 1705 1714 1585 112 14 157 C ATOM 249 O ALA A 35 22.272 -0.106 43.893 1.00 14.06 O ANISOU 249 O ALA A 35 1909 1829 1601 174 0 305 O ATOM 250 CB ALA A 35 19.429 -1.603 43.418 1.00 13.10 C ANISOU 250 CB ALA A 35 1724 1673 1579 69 36 65 C ATOM 251 N ALA A 36 21.858 -1.688 45.445 1.00 13.81 N ANISOU 251 N ALA A 36 1798 1858 1590 117 -21 199 N ATOM 252 CA ALA A 36 23.257 -2.072 45.600 1.00 13.59 C ANISOU 252 CA ALA A 36 1789 1817 1558 78 -6 166 C ATOM 253 C ALA A 36 23.618 -3.182 44.615 1.00 13.48 C ANISOU 253 C ALA A 36 1789 1770 1561 31 -2 158 C ATOM 254 O ALA A 36 22.839 -4.116 44.425 1.00 14.13 O ANISOU 254 O ALA A 36 1834 1883 1651 -18 13 122 O ATOM 255 CB ALA A 36 23.524 -2.524 47.038 1.00 14.14 C ANISOU 255 CB ALA A 36 1854 1935 1582 98 -49 224 C ATOM 256 N PRO A 37 24.806 -3.090 43.995 1.00 13.01 N ANISOU 256 N PRO A 37 1817 1637 1486 12 47 185 N ATOM 257 CA PRO A 37 25.293 -4.198 43.184 1.00 12.97 C ANISOU 257 CA PRO A 37 1775 1645 1505 13 83 180 C ATOM 258 C PRO A 37 25.868 -5.284 44.112 1.00 13.62 C ANISOU 258 C PRO A 37 1924 1704 1543 23 3 194 C ATOM 259 O PRO A 37 26.003 -5.049 45.323 1.00 14.16 O ANISOU 259 O PRO A 37 2047 1687 1643 -41 69 163 O ATOM 260 CB PRO A 37 26.406 -3.546 42.342 1.00 12.85 C ANISOU 260 CB PRO A 37 1800 1652 1429 -25 107 168 C ATOM 261 CG PRO A 37 26.951 -2.476 43.224 1.00 12.00 C ANISOU 261 CG PRO A 37 1761 1493 1304 -21 173 178 C ATOM 262 CD PRO A 37 25.755 -1.959 44.022 1.00 13.32 C ANISOU 262 CD PRO A 37 1693 1725 1643 9 54 120 C ATOM 263 N SER A 38 26.225 -6.435 43.544 1.00 14.52 N ANISOU 263 N SER A 38 2069 1723 1722 92 -97 244 N ATOM 264 CA SER A 38 26.803 -7.558 44.313 1.00 15.82 C ANISOU 264 CA SER A 38 2264 1924 1821 127 -131 238 C ATOM 265 C SER A 38 28.167 -7.182 44.876 1.00 16.08 C ANISOU 265 C SER A 38 2238 1984 1885 123 -119 234 C ATOM 266 O SER A 38 28.909 -6.421 44.263 1.00 15.50 O ANISOU 266 O SER A 38 2202 1961 1724 207 -93 302 O ATOM 267 CB SER A 38 26.979 -8.775 43.395 1.00 17.00 C ANISOU 267 CB SER A 38 2383 2066 2009 91 -138 142 C ATOM 268 OG SER A 38 28.081 -8.590 42.505 1.00 19.46 O ANISOU 268 OG SER A 38 2855 2476 2060 137 -162 180 O ATOM 269 N GLY A 39 28.517 -7.738 46.044 1.00 16.53 N ANISOU 269 N GLY A 39 2324 2134 1820 82 -130 290 N ATOM 270 CA GLY A 39 29.823 -7.458 46.653 1.00 17.60 C ANISOU 270 CA GLY A 39 2410 2210 2067 91 -144 278 C ATOM 271 C GLY A 39 30.323 -8.638 47.465 1.00 18.28 C ANISOU 271 C GLY A 39 2479 2255 2209 100 -152 253 C ATOM 272 O GLY A 39 29.788 -9.734 47.361 1.00 20.12 O ANISOU 272 O GLY A 39 2655 2539 2448 76 -184 319 O ATOM 273 N ALA A 40 31.364 -8.404 48.253 1.00 18.95 N ANISOU 273 N ALA A 40 2613 2349 2239 96 -175 277 N ATOM 274 CA ALA A 40 31.928 -9.422 49.159 1.00 19.07 C ANISOU 274 CA ALA A 40 2544 2429 2272 120 -173 241 C ATOM 275 C ALA A 40 31.183 -9.395 50.498 1.00 18.88 C ANISOU 275 C ALA A 40 2497 2407 2267 103 -151 202 C ATOM 276 O ALA A 40 30.844 -8.322 50.996 1.00 18.39 O ANISOU 276 O ALA A 40 2456 2415 2115 134 -253 291 O ATOM 277 CB ALA A 40 33.396 -9.140 49.376 1.00 19.45 C ANISOU 277 CB ALA A 40 2579 2528 2280 116 -135 189 C ATOM 278 N SER A 41 30.957 -10.570 51.095 1.00 19.51 N ANISOU 278 N SER A 41 2572 2483 2357 95 -142 177 N ATOM 279 CA SER A 41 30.316 -10.656 52.412 1.00 19.43 C ANISOU 279 CA SER A 41 2560 2462 2361 115 -117 159 C ATOM 280 C SER A 41 31.306 -11.105 53.484 1.00 19.48 C ANISOU 280 C SER A 41 2563 2485 2351 107 -112 138 C ATOM 281 O SER A 41 30.988 -11.099 54.679 1.00 19.67 O ANISOU 281 O SER A 41 2588 2512 2371 133 -136 225 O ATOM 282 CB SER A 41 29.105 -11.590 52.395 1.00 20.04 C ANISOU 282 CB SER A 41 2671 2515 2427 89 -102 109 C ATOM 283 OG SER A 41 29.492 -12.928 52.119 1.00 20.61 O ANISOU 283 OG SER A 41 2798 2451 2580 110 -43 160 O ATOM 284 N THR A 42 32.497 -11.496 53.039 1.00 19.59 N ANISOU 284 N THR A 42 2587 2491 2364 145 -124 165 N ATOM 285 CA THR A 42 33.582 -11.904 53.942 1.00 19.60 C ANISOU 285 CA THR A 42 2575 2468 2403 109 -94 77 C ATOM 286 C THR A 42 34.875 -11.240 53.498 1.00 20.13 C ANISOU 286 C THR A 42 2614 2565 2470 110 -44 74 C ATOM 287 O THR A 42 34.992 -10.807 52.348 1.00 20.58 O ANISOU 287 O THR A 42 2646 2593 2578 61 52 145 O ATOM 288 CB THR A 42 33.775 -13.439 53.960 1.00 19.83 C ANISOU 288 CB THR A 42 2681 2487 2365 104 -96 67 C ATOM 289 OG1 THR A 42 34.249 -13.895 52.684 1.00 20.29 O ANISOU 289 OG1 THR A 42 2875 2369 2462 225 2 131 O ATOM 290 CG2 THR A 42 32.482 -14.137 54.303 1.00 19.49 C ANISOU 290 CG2 THR A 42 2561 2446 2396 54 -115 20 C ATOM 291 N GLY A 43 35.847 -11.170 54.397 1.00 20.60 N ANISOU 291 N GLY A 43 2659 2585 2581 75 -3 -16 N ATOM 292 CA GLY A 43 37.122 -10.575 54.048 1.00 21.24 C ANISOU 292 CA GLY A 43 2719 2698 2652 61 -56 -44 C ATOM 293 C GLY A 43 37.468 -9.421 54.953 1.00 21.31 C ANISOU 293 C GLY A 43 2776 2752 2567 79 -108 -9 C ATOM 294 O GLY A 43 36.598 -8.878 55.627 1.00 20.41 O ANISOU 294 O GLY A 43 2677 2642 2434 160 -201 -27 O ATOM 295 N SER A 44 38.740 -9.045 54.937 1.00 22.20 N ANISOU 295 N SER A 44 2829 2918 2687 87 -113 -16 N ATOM 296 CA SER A 44 39.283 -8.142 55.943 1.00 23.02 C ANISOU 296 CA SER A 44 2936 3028 2782 67 -122 -24 C ATOM 297 C SER A 44 39.523 -6.736 55.452 1.00 22.70 C ANISOU 297 C SER A 44 2894 3005 2724 70 -88 -1 C ATOM 298 O SER A 44 39.917 -5.889 56.248 1.00 23.18 O ANISOU 298 O SER A 44 3000 3114 2691 43 -140 27 O ATOM 299 CB SER A 44 40.620 -8.678 56.495 1.00 23.33 C ANISOU 299 CB SER A 44 2950 3072 2841 70 -131 -39 C ATOM 300 OG SER A 44 40.587 -10.072 56.730 1.00 25.85 O ANISOU 300 OG SER A 44 3324 3407 3090 58 -102 110 O ATOM 301 N ARG A 45 39.294 -6.465 54.162 1.00 21.91 N ANISOU 301 N ARG A 45 2755 2940 2628 115 -119 8 N ATOM 302 CA ARG A 45 39.808 -5.229 53.561 1.00 21.66 C ANISOU 302 CA ARG A 45 2671 2927 2629 157 -92 26 C ATOM 303 C ARG A 45 38.754 -4.283 53.000 1.00 21.12 C ANISOU 303 C ARG A 45 2656 2818 2549 140 -73 21 C ATOM 304 O ARG A 45 38.993 -3.086 52.900 1.00 22.54 O ANISOU 304 O ARG A 45 2823 2966 2773 144 -94 43 O ATOM 305 CB ARG A 45 40.804 -5.548 52.445 1.00 21.97 C ANISOU 305 CB ARG A 45 2693 2946 2706 187 -52 25 C ATOM 306 CG ARG A 45 41.968 -6.424 52.898 1.00 22.52 C ANISOU 306 CG ARG A 45 2694 3082 2778 206 -65 82 C ATOM 307 CD ARG A 45 42.642 -7.064 51.692 1.00 24.23 C ANISOU 307 CD ARG A 45 2939 3206 3060 100 55 26 C ATOM 308 NE ARG A 45 43.315 -6.025 50.943 1.00 23.72 N ANISOU 308 NE ARG A 45 2956 3252 2803 161 3 222 N ATOM 309 CZ ARG A 45 43.203 -5.813 49.632 1.00 21.43 C ANISOU 309 CZ ARG A 45 2676 2924 2542 64 -113 19 C ATOM 310 NH1 ARG A 45 42.463 -6.608 48.858 1.00 19.25 N ANISOU 310 NH1 ARG A 45 2354 2701 2257 219 -174 144 N ATOM 311 NH2 ARG A 45 43.875 -4.801 49.105 1.00 19.95 N ANISOU 311 NH2 ARG A 45 2512 2724 2341 108 -144 19 N ATOM 312 N GLU A 46 37.606 -4.822 52.618 1.00 20.00 N ANISOU 312 N GLU A 46 2501 2740 2358 182 -49 44 N ATOM 313 CA GLU A 46 36.583 -3.995 51.979 1.00 18.61 C ANISOU 313 CA GLU A 46 2388 2521 2159 184 -72 27 C ATOM 314 C GLU A 46 35.324 -3.941 52.825 1.00 17.39 C ANISOU 314 C GLU A 46 2234 2338 2033 138 -80 39 C ATOM 315 O GLU A 46 35.151 -4.744 53.743 1.00 17.08 O ANISOU 315 O GLU A 46 2247 2276 1967 207 -89 97 O ATOM 316 CB GLU A 46 36.257 -4.516 50.579 1.00 19.13 C ANISOU 316 CB GLU A 46 2428 2610 2231 187 -83 1 C ATOM 317 CG GLU A 46 35.671 -5.885 50.548 1.00 19.98 C ANISOU 317 CG GLU A 46 2555 2749 2287 188 -136 21 C ATOM 318 CD GLU A 46 35.980 -6.585 49.245 1.00 24.25 C ANISOU 318 CD GLU A 46 3281 3142 2789 192 -60 -114 C ATOM 319 OE1 GLU A 46 35.384 -6.223 48.204 1.00 22.39 O ANISOU 319 OE1 GLU A 46 2993 3012 2499 181 -118 -52 O ATOM 320 OE2 GLU A 46 36.829 -7.495 49.270 1.00 26.57 O ANISOU 320 OE2 GLU A 46 3395 3415 3282 381 -212 -54 O ATOM 321 N ALA A 47 34.447 -2.986 52.523 1.00 16.32 N ANISOU 321 N ALA A 47 2195 2212 1792 131 -133 16 N ATOM 322 CA ALA A 47 33.141 -2.963 53.156 1.00 15.45 C ANISOU 322 CA ALA A 47 2106 2082 1681 118 -107 22 C ATOM 323 C ALA A 47 32.417 -4.248 52.790 1.00 15.69 C ANISOU 323 C ALA A 47 2164 2079 1715 131 -83 50 C ATOM 324 O ALA A 47 32.518 -4.721 51.657 1.00 16.03 O ANISOU 324 O ALA A 47 2358 2160 1570 87 -40 47 O ATOM 325 CB ALA A 47 32.344 -1.741 52.721 1.00 15.27 C ANISOU 325 CB ALA A 47 2038 2105 1658 135 -151 56 C ATOM 326 N LEU A 48 31.701 -4.822 53.745 1.00 15.57 N ANISOU 326 N LEU A 48 2140 2144 1631 130 -88 42 N ATOM 327 CA LEU A 48 31.055 -6.100 53.537 1.00 16.03 C ANISOU 327 CA LEU A 48 2158 2160 1769 114 -46 140 C ATOM 328 C LEU A 48 29.552 -5.969 53.388 1.00 16.50 C ANISOU 328 C LEU A 48 2198 2214 1855 80 -62 137 C ATOM 329 O LEU A 48 28.903 -5.312 54.196 1.00 16.65 O ANISOU 329 O LEU A 48 2211 2347 1766 143 -97 100 O ATOM 330 CB LEU A 48 31.375 -7.045 54.701 1.00 16.13 C ANISOU 330 CB LEU A 48 2183 2172 1773 146 -39 138 C ATOM 331 CG LEU A 48 32.861 -7.309 54.949 1.00 16.39 C ANISOU 331 CG LEU A 48 2209 2211 1805 132 -50 171 C ATOM 332 CD1 LEU A 48 33.004 -8.284 56.106 1.00 16.47 C ANISOU 332 CD1 LEU A 48 2488 2151 1617 152 -31 156 C ATOM 333 CD2 LEU A 48 33.557 -7.844 53.710 1.00 17.09 C ANISOU 333 CD2 LEU A 48 2249 2442 1800 128 -94 81 C ATOM 334 N GLU A 49 29.004 -6.605 52.356 1.00 16.48 N ANISOU 334 N GLU A 49 2228 2245 1788 9 -49 215 N ATOM 335 CA GLU A 49 27.553 -6.768 52.247 1.00 17.37 C ANISOU 335 CA GLU A 49 2286 2351 1962 -22 -37 200 C ATOM 336 C GLU A 49 27.102 -7.807 53.262 1.00 17.80 C ANISOU 336 C GLU A 49 2359 2375 2029 5 -7 200 C ATOM 337 O GLU A 49 27.870 -8.706 53.618 1.00 17.99 O ANISOU 337 O GLU A 49 2391 2450 1995 109 58 208 O ATOM 338 CB GLU A 49 27.136 -7.213 50.833 1.00 17.48 C ANISOU 338 CB GLU A 49 2305 2375 1958 -66 -76 191 C ATOM 339 CG GLU A 49 27.812 -8.487 50.356 1.00 18.73 C ANISOU 339 CG GLU A 49 2539 2506 2070 -123 -84 160 C ATOM 340 CD GLU A 49 27.204 -9.089 49.112 1.00 18.83 C ANISOU 340 CD GLU A 49 2346 2621 2185 -119 2 115 C ATOM 341 OE1 GLU A 49 26.712 -8.320 48.271 1.00 20.81 O ANISOU 341 OE1 GLU A 49 2525 3214 2167 -177 -174 193 O ATOM 342 OE2 GLU A 49 27.254 -10.332 48.979 1.00 22.10 O ANISOU 342 OE2 GLU A 49 2765 3121 2509 -206 -107 12 O ATOM 343 N LEU A 50 25.866 -7.674 53.722 1.00 18.01 N ANISOU 343 N LEU A 50 2365 2382 2093 -11 17 234 N ATOM 344 CA LEU A 50 25.253 -8.672 54.601 1.00 18.12 C ANISOU 344 CA LEU A 50 2422 2354 2109 33 33 259 C ATOM 345 C LEU A 50 24.406 -9.662 53.799 1.00 18.06 C ANISOU 345 C LEU A 50 2380 2351 2128 -6 26 284 C ATOM 346 O LEU A 50 23.476 -9.261 53.075 1.00 16.83 O ANISOU 346 O LEU A 50 2304 2210 1881 -18 49 484 O ATOM 347 CB LEU A 50 24.401 -7.983 55.665 1.00 18.59 C ANISOU 347 CB LEU A 50 2511 2374 2178 23 41 240 C ATOM 348 CG LEU A 50 23.805 -8.805 56.811 1.00 19.47 C ANISOU 348 CG LEU A 50 2592 2541 2266 61 90 198 C ATOM 349 CD1 LEU A 50 24.897 -9.495 57.612 1.00 20.95 C ANISOU 349 CD1 LEU A 50 2680 2776 2503 92 -15 84 C ATOM 350 CD2 LEU A 50 23.019 -7.863 57.695 1.00 19.36 C ANISOU 350 CD2 LEU A 50 2593 2581 2179 80 84 193 C ATOM 351 N ARG A 51 24.727 -10.950 53.938 1.00 17.93 N ANISOU 351 N ARG A 51 2380 2348 2082 49 57 266 N ATOM 352 CA ARG A 51 23.936 -12.031 53.359 1.00 18.54 C ANISOU 352 CA ARG A 51 2462 2415 2165 -20 43 283 C ATOM 353 C ARG A 51 23.313 -12.894 54.463 1.00 19.18 C ANISOU 353 C ARG A 51 2539 2485 2263 -68 39 272 C ATOM 354 O ARG A 51 23.910 -13.062 55.526 1.00 19.51 O ANISOU 354 O ARG A 51 2521 2555 2337 -60 25 387 O ATOM 355 CB ARG A 51 24.801 -12.927 52.475 1.00 18.96 C ANISOU 355 CB ARG A 51 2510 2488 2202 0 60 269 C ATOM 356 CG ARG A 51 25.338 -12.253 51.230 1.00 18.64 C ANISOU 356 CG ARG A 51 2472 2517 2091 5 31 249 C ATOM 357 CD ARG A 51 24.344 -12.312 50.074 1.00 18.33 C ANISOU 357 CD ARG A 51 2415 2368 2182 -47 -3 180 C ATOM 358 NE ARG A 51 24.796 -11.411 49.025 1.00 17.67 N ANISOU 358 NE ARG A 51 2303 2427 1982 -3 -12 263 N ATOM 359 CZ ARG A 51 24.116 -11.105 47.923 1.00 16.68 C ANISOU 359 CZ ARG A 51 2063 2391 1880 -67 10 219 C ATOM 360 NH1 ARG A 51 22.926 -11.648 47.680 1.00 15.23 N ANISOU 360 NH1 ARG A 51 2055 2067 1661 75 -69 219 N ATOM 361 NH2 ARG A 51 24.643 -10.231 47.063 1.00 16.25 N ANISOU 361 NH2 ARG A 51 2019 2152 2002 -52 -35 382 N ATOM 362 N ASP A 52 22.142 -13.458 54.187 1.00 19.71 N ANISOU 362 N ASP A 52 2553 2559 2376 -45 26 300 N ATOM 363 CA ASP A 52 21.389 -14.224 55.196 1.00 20.64 C ANISOU 363 CA ASP A 52 2707 2621 2513 -67 23 248 C ATOM 364 C ASP A 52 22.013 -15.567 55.542 1.00 21.58 C ANISOU 364 C ASP A 52 2823 2716 2660 -40 16 202 C ATOM 365 O ASP A 52 22.003 -15.966 56.706 1.00 22.53 O ANISOU 365 O ASP A 52 3032 2817 2708 -62 17 242 O ATOM 366 CB ASP A 52 19.941 -14.442 54.756 1.00 20.31 C ANISOU 366 CB ASP A 52 2629 2634 2451 0 49 256 C ATOM 367 CG ASP A 52 19.179 -13.136 54.563 1.00 19.88 C ANISOU 367 CG ASP A 52 2677 2478 2396 -80 22 270 C ATOM 368 OD1 ASP A 52 19.601 -12.085 55.082 1.00 18.20 O ANISOU 368 OD1 ASP A 52 2512 2314 2089 -45 21 563 O ATOM 369 OD2 ASP A 52 18.128 -13.180 53.901 1.00 20.06 O ANISOU 369 OD2 ASP A 52 2685 2591 2343 15 26 559 O ATOM 370 N GLY A 53 22.516 -16.275 54.535 1.00 22.09 N ANISOU 370 N GLY A 53 2910 2723 2758 -34 44 210 N ATOM 371 CA GLY A 53 23.067 -17.617 54.741 1.00 22.80 C ANISOU 371 CA GLY A 53 2984 2788 2889 15 5 183 C ATOM 372 C GLY A 53 22.012 -18.656 55.079 1.00 23.41 C ANISOU 372 C GLY A 53 3073 2861 2959 -2 -11 197 C ATOM 373 O GLY A 53 22.321 -19.685 55.699 1.00 23.62 O ANISOU 373 O GLY A 53 3174 2862 2937 28 -49 286 O ATOM 374 N ASP A 54 20.770 -18.396 54.674 1.00 23.65 N ANISOU 374 N ASP A 54 3080 2929 2974 -12 -21 209 N ATOM 375 CA ASP A 54 19.675 -19.360 54.823 1.00 24.23 C ANISOU 375 CA ASP A 54 3174 2976 3055 -35 -33 211 C ATOM 376 C ASP A 54 19.620 -20.258 53.586 1.00 24.69 C ANISOU 376 C ASP A 54 3227 3037 3115 -27 -35 194 C ATOM 377 O ASP A 54 19.174 -19.844 52.519 1.00 23.97 O ANISOU 377 O ASP A 54 3168 2939 3001 -60 -78 274 O ATOM 378 CB ASP A 54 18.343 -18.629 55.058 1.00 24.44 C ANISOU 378 CB ASP A 54 3168 3036 3080 -66 9 200 C ATOM 379 CG ASP A 54 17.144 -19.578 55.192 1.00 25.43 C ANISOU 379 CG ASP A 54 3275 3171 3217 -52 38 171 C ATOM 380 OD1 ASP A 54 17.310 -20.812 55.055 1.00 25.69 O ANISOU 380 OD1 ASP A 54 3374 3164 3219 -131 84 291 O ATOM 381 OD2 ASP A 54 16.021 -19.069 55.425 1.00 26.70 O ANISOU 381 OD2 ASP A 54 3347 3341 3455 -135 139 245 O ATOM 382 N LYS A 55 20.053 -21.506 53.745 1.00 25.18 N ANISOU 382 N LYS A 55 3331 3054 3182 -5 -41 194 N ATOM 383 CA LYS A 55 20.145 -22.449 52.632 1.00 25.75 C ANISOU 383 CA LYS A 55 3392 3126 3265 0 -18 167 C ATOM 384 C LYS A 55 18.808 -22.727 51.947 1.00 25.16 C ANISOU 384 C LYS A 55 3363 2995 3199 -16 -22 173 C ATOM 385 O LYS A 55 18.781 -23.119 50.783 1.00 25.55 O ANISOU 385 O LYS A 55 3488 2978 3240 -23 8 207 O ATOM 386 CB LYS A 55 20.835 -23.751 53.072 1.00 26.44 C ANISOU 386 CB LYS A 55 3452 3230 3364 12 -20 130 C ATOM 387 CG LYS A 55 22.344 -23.609 53.265 1.00 28.78 C ANISOU 387 CG LYS A 55 3615 3645 3672 11 -6 93 C ATOM 388 CD LYS A 55 23.012 -23.136 51.973 1.00 32.20 C ANISOU 388 CD LYS A 55 4184 4097 3951 1 83 98 C ATOM 389 CE LYS A 55 24.504 -22.943 52.139 1.00 34.58 C ANISOU 389 CE LYS A 55 4153 4435 4550 -15 -56 -77 C ATOM 390 NZ LYS A 55 25.078 -22.243 50.943 1.00 35.08 N ANISOU 390 NZ LYS A 55 4556 4521 4251 -129 120 182 N ATOM 391 N SER A 56 17.710 -22.495 52.661 1.00 24.74 N ANISOU 391 N SER A 56 3278 2997 3123 -25 -43 212 N ATOM 392 CA SER A 56 16.365 -22.730 52.131 1.00 24.60 C ANISOU 392 CA SER A 56 3220 3009 3117 -63 -10 163 C ATOM 393 C SER A 56 15.826 -21.586 51.254 1.00 23.83 C ANISOU 393 C SER A 56 3101 2958 2995 -66 -34 177 C ATOM 394 O SER A 56 14.725 -21.701 50.699 1.00 24.09 O ANISOU 394 O SER A 56 3125 2993 3034 -86 -7 241 O ATOM 395 CB SER A 56 15.384 -23.000 53.275 1.00 25.11 C ANISOU 395 CB SER A 56 3280 3100 3160 -77 16 99 C ATOM 396 OG SER A 56 14.961 -21.788 53.869 1.00 26.28 O ANISOU 396 OG SER A 56 3415 3219 3350 -39 68 115 O ATOM 397 N ARG A 57 16.567 -20.479 51.159 1.00 22.95 N ANISOU 397 N ARG A 57 3014 2844 2858 -31 -33 193 N ATOM 398 CA ARG A 57 16.189 -19.388 50.236 1.00 22.15 C ANISOU 398 CA ARG A 57 2849 2756 2808 -12 -5 163 C ATOM 399 C ARG A 57 17.382 -18.936 49.414 1.00 21.20 C ANISOU 399 C ARG A 57 2746 2614 2695 -13 -29 165 C ATOM 400 O ARG A 57 18.424 -18.586 49.983 1.00 20.93 O ANISOU 400 O ARG A 57 2746 2541 2666 -35 -17 199 O ATOM 401 CB ARG A 57 15.668 -18.167 50.989 1.00 22.00 C ANISOU 401 CB ARG A 57 2824 2788 2745 -18 -1 116 C ATOM 402 CG ARG A 57 14.374 -18.322 51.743 1.00 22.88 C ANISOU 402 CG ARG A 57 2942 2940 2812 7 26 163 C ATOM 403 CD ARG A 57 13.989 -16.977 52.345 1.00 23.31 C ANISOU 403 CD ARG A 57 2987 2941 2927 5 -4 141 C ATOM 404 NE ARG A 57 13.336 -16.091 51.374 1.00 24.19 N ANISOU 404 NE ARG A 57 3124 3104 2962 -56 26 206 N ATOM 405 CZ ARG A 57 13.883 -15.010 50.815 1.00 23.39 C ANISOU 405 CZ ARG A 57 2926 3016 2944 -45 -83 234 C ATOM 406 NH1 ARG A 57 15.131 -14.618 51.098 1.00 22.99 N ANISOU 406 NH1 ARG A 57 2982 3138 2615 115 -142 308 N ATOM 407 NH2 ARG A 57 13.162 -14.305 49.957 1.00 23.12 N ANISOU 407 NH2 ARG A 57 2893 3070 2822 -70 -40 223 N ATOM 408 N PHE A 58 17.229 -18.946 48.085 1.00 20.44 N ANISOU 408 N PHE A 58 2584 2519 2660 -6 -16 204 N ATOM 409 CA PHE A 58 18.248 -18.423 47.178 1.00 19.95 C ANISOU 409 CA PHE A 58 2507 2485 2588 23 -48 176 C ATOM 410 C PHE A 58 19.641 -19.009 47.448 1.00 19.90 C ANISOU 410 C PHE A 58 2518 2464 2579 41 -38 187 C ATOM 411 O PHE A 58 20.653 -18.315 47.297 1.00 19.76 O ANISOU 411 O PHE A 58 2531 2442 2535 44 -124 209 O ATOM 412 CB PHE A 58 18.322 -16.888 47.299 1.00 19.49 C ANISOU 412 CB PHE A 58 2410 2399 2595 18 -84 143 C ATOM 413 CG PHE A 58 17.125 -16.159 46.756 1.00 18.04 C ANISOU 413 CG PHE A 58 2305 2242 2306 -46 -5 171 C ATOM 414 CD1 PHE A 58 16.944 -16.025 45.383 1.00 17.99 C ANISOU 414 CD1 PHE A 58 2269 2237 2330 -73 -161 212 C ATOM 415 CD2 PHE A 58 16.203 -15.565 47.616 1.00 17.56 C ANISOU 415 CD2 PHE A 58 2241 2090 2338 16 -65 186 C ATOM 416 CE1 PHE A 58 15.839 -15.320 44.869 1.00 17.56 C ANISOU 416 CE1 PHE A 58 2129 2022 2520 -16 5 226 C ATOM 417 CE2 PHE A 58 15.103 -14.858 47.111 1.00 18.23 C ANISOU 417 CE2 PHE A 58 2166 2398 2363 -39 -26 121 C ATOM 418 CZ PHE A 58 14.930 -14.739 45.733 1.00 17.84 C ANISOU 418 CZ PHE A 58 2353 2076 2346 -78 -33 83 C ATOM 419 N LEU A 59 19.690 -20.278 47.856 1.00 20.26 N ANISOU 419 N LEU A 59 2584 2508 2603 41 -28 196 N ATOM 420 CA LEU A 59 20.968 -20.964 48.103 1.00 20.68 C ANISOU 420 CA LEU A 59 2656 2588 2611 50 -33 166 C ATOM 421 C LEU A 59 21.863 -20.184 49.083 1.00 20.28 C ANISOU 421 C LEU A 59 2651 2472 2581 14 -21 222 C ATOM 422 O LEU A 59 23.096 -20.182 48.967 1.00 20.68 O ANISOU 422 O LEU A 59 2681 2592 2582 21 -36 273 O ATOM 423 CB LEU A 59 21.699 -21.262 46.781 1.00 21.02 C ANISOU 423 CB LEU A 59 2691 2602 2691 29 -34 143 C ATOM 424 CG LEU A 59 21.107 -22.308 45.816 1.00 21.60 C ANISOU 424 CG LEU A 59 2799 2708 2699 46 -31 48 C ATOM 425 CD1 LEU A 59 19.750 -21.893 45.246 1.00 23.08 C ANISOU 425 CD1 LEU A 59 2887 2883 3000 64 -36 32 C ATOM 426 CD2 LEU A 59 22.077 -22.598 44.684 1.00 22.22 C ANISOU 426 CD2 LEU A 59 2831 2847 2763 70 -36 106 C ATOM 427 N GLY A 60 21.227 -19.534 50.056 1.00 20.02 N ANISOU 427 N GLY A 60 2705 2364 2536 4 -49 251 N ATOM 428 CA GLY A 60 21.938 -18.815 51.116 1.00 19.72 C ANISOU 428 CA GLY A 60 2712 2288 2491 2 -53 229 C ATOM 429 C GLY A 60 22.232 -17.354 50.828 1.00 19.48 C ANISOU 429 C GLY A 60 2602 2316 2481 -18 -44 177 C ATOM 430 O GLY A 60 22.823 -16.658 51.659 1.00 19.15 O ANISOU 430 O GLY A 60 2625 2272 2375 34 -97 258 O ATOM 431 N LYS A 61 21.790 -16.888 49.662 1.00 19.11 N ANISOU 431 N LYS A 61 2503 2326 2432 17 -27 187 N ATOM 432 CA LYS A 61 22.116 -15.539 49.194 1.00 19.09 C ANISOU 432 CA LYS A 61 2440 2343 2468 42 36 144 C ATOM 433 C LYS A 61 21.010 -14.486 49.430 1.00 18.91 C ANISOU 433 C LYS A 61 2367 2364 2452 51 70 172 C ATOM 434 O LYS A 61 21.063 -13.386 48.876 1.00 17.58 O ANISOU 434 O LYS A 61 2110 2213 2355 15 119 260 O ATOM 435 CB LYS A 61 22.552 -15.569 47.714 1.00 19.55 C ANISOU 435 CB LYS A 61 2504 2447 2476 62 41 80 C ATOM 436 CG LYS A 61 23.771 -16.457 47.409 1.00 21.53 C ANISOU 436 CG LYS A 61 2691 2682 2808 105 17 77 C ATOM 437 CD LYS A 61 25.005 -15.952 48.126 1.00 25.87 C ANISOU 437 CD LYS A 61 3231 3345 3250 -62 -78 -12 C ATOM 438 CE LYS A 61 26.154 -16.946 48.083 1.00 28.68 C ANISOU 438 CE LYS A 61 3660 3609 3625 101 15 2 C ATOM 439 NZ LYS A 61 27.277 -16.515 48.992 1.00 30.84 N ANISOU 439 NZ LYS A 61 3773 4001 3941 -21 -126 -26 N ATOM 440 N GLY A 62 20.017 -14.814 50.256 1.00 18.83 N ANISOU 440 N GLY A 62 2390 2371 2390 74 83 206 N ATOM 441 CA GLY A 62 18.997 -13.832 50.648 1.00 18.64 C ANISOU 441 CA GLY A 62 2415 2354 2312 32 91 159 C ATOM 442 C GLY A 62 19.606 -12.585 51.271 1.00 18.48 C ANISOU 442 C GLY A 62 2368 2378 2275 -5 88 215 C ATOM 443 O GLY A 62 20.695 -12.642 51.858 1.00 18.24 O ANISOU 443 O GLY A 62 2389 2289 2250 -6 130 301 O ATOM 444 N VAL A 63 18.932 -11.442 51.107 1.00 18.23 N ANISOU 444 N VAL A 63 2296 2408 2220 21 100 227 N ATOM 445 CA VAL A 63 19.346 -10.207 51.789 1.00 17.98 C ANISOU 445 CA VAL A 63 2219 2385 2226 -15 48 267 C ATOM 446 C VAL A 63 18.264 -9.644 52.716 1.00 18.53 C ANISOU 446 C VAL A 63 2295 2449 2297 1 35 231 C ATOM 447 O VAL A 63 18.182 -8.428 52.950 1.00 18.01 O ANISOU 447 O VAL A 63 2177 2414 2250 -3 100 316 O ATOM 448 CB VAL A 63 19.895 -9.122 50.812 1.00 18.09 C ANISOU 448 CB VAL A 63 2214 2415 2241 27 26 299 C ATOM 449 CG1 VAL A 63 21.170 -9.621 50.146 1.00 16.79 C ANISOU 449 CG1 VAL A 63 1984 2286 2107 -4 -20 203 C ATOM 450 CG2 VAL A 63 18.826 -8.722 49.772 1.00 17.97 C ANISOU 450 CG2 VAL A 63 2130 2416 2280 68 -55 221 C ATOM 451 N THR A 64 17.456 -10.543 53.284 1.00 19.26 N ANISOU 451 N THR A 64 2362 2548 2406 -5 35 232 N ATOM 452 CA THR A 64 16.375 -10.107 54.170 1.00 20.15 C ANISOU 452 CA THR A 64 2544 2654 2458 -23 61 215 C ATOM 453 C THR A 64 16.906 -9.345 55.390 1.00 19.64 C ANISOU 453 C THR A 64 2518 2569 2375 -27 63 234 C ATOM 454 O THR A 64 16.282 -8.396 55.841 1.00 20.18 O ANISOU 454 O THR A 64 2573 2678 2415 -6 75 302 O ATOM 455 CB THR A 64 15.442 -11.272 54.609 1.00 20.65 C ANISOU 455 CB THR A 64 2560 2704 2582 -37 52 162 C ATOM 456 OG1 THR A 64 16.166 -12.179 55.445 1.00 22.08 O ANISOU 456 OG1 THR A 64 2795 2924 2669 -16 98 337 O ATOM 457 CG2 THR A 64 14.900 -12.032 53.407 1.00 21.63 C ANISOU 457 CG2 THR A 64 2741 2788 2687 -69 20 97 C ATOM 458 N LYS A 65 18.062 -9.750 55.918 1.00 19.69 N ANISOU 458 N LYS A 65 2491 2611 2378 -42 102 226 N ATOM 459 CA LYS A 65 18.649 -9.036 57.064 1.00 19.82 C ANISOU 459 CA LYS A 65 2595 2569 2367 12 74 179 C ATOM 460 C LYS A 65 19.060 -7.604 56.746 1.00 19.83 C ANISOU 460 C LYS A 65 2596 2581 2354 31 73 141 C ATOM 461 O LYS A 65 18.762 -6.687 57.512 1.00 19.54 O ANISOU 461 O LYS A 65 2630 2572 2221 67 57 170 O ATOM 462 CB LYS A 65 19.829 -9.806 57.668 1.00 20.25 C ANISOU 462 CB LYS A 65 2602 2654 2436 46 23 127 C ATOM 463 CG LYS A 65 19.418 -11.093 58.349 1.00 21.87 C ANISOU 463 CG LYS A 65 2835 2823 2651 -50 96 121 C ATOM 464 CD LYS A 65 20.633 -11.901 58.775 1.00 24.25 C ANISOU 464 CD LYS A 65 3095 3136 2979 66 -65 148 C ATOM 465 CE LYS A 65 20.255 -13.335 59.145 1.00 27.53 C ANISOU 465 CE LYS A 65 3552 3451 3456 6 41 88 C ATOM 466 NZ LYS A 65 21.399 -14.007 59.831 1.00 27.96 N ANISOU 466 NZ LYS A 65 3672 3599 3351 84 -63 221 N ATOM 467 N ALA A 66 19.716 -7.416 55.601 1.00 19.06 N ANISOU 467 N ALA A 66 2517 2487 2237 15 104 173 N ATOM 468 CA ALA A 66 20.105 -6.080 55.153 1.00 18.79 C ANISOU 468 CA ALA A 66 2445 2445 2248 121 118 191 C ATOM 469 C ALA A 66 18.870 -5.208 54.878 1.00 18.53 C ANISOU 469 C ALA A 66 2435 2454 2149 73 66 213 C ATOM 470 O ALA A 66 18.836 -4.044 55.277 1.00 18.36 O ANISOU 470 O ALA A 66 2410 2444 2119 176 112 313 O ATOM 471 CB ALA A 66 21.018 -6.169 53.935 1.00 18.66 C ANISOU 471 CB ALA A 66 2444 2466 2179 71 117 227 C ATOM 472 N VAL A 67 17.858 -5.797 54.240 1.00 18.41 N ANISOU 472 N VAL A 67 2362 2428 2203 89 92 216 N ATOM 473 CA VAL A 67 16.586 -5.117 53.978 1.00 18.71 C ANISOU 473 CA VAL A 67 2402 2463 2243 81 77 141 C ATOM 474 C VAL A 67 15.921 -4.716 55.307 1.00 19.04 C ANISOU 474 C VAL A 67 2482 2502 2247 83 92 178 C ATOM 475 O VAL A 67 15.380 -3.620 55.434 1.00 19.00 O ANISOU 475 O VAL A 67 2471 2516 2233 61 167 162 O ATOM 476 CB VAL A 67 15.659 -5.995 53.123 1.00 18.63 C ANISOU 476 CB VAL A 67 2346 2495 2238 98 64 123 C ATOM 477 CG1 VAL A 67 14.232 -5.414 53.051 1.00 18.76 C ANISOU 477 CG1 VAL A 67 2341 2473 2311 96 48 117 C ATOM 478 CG2 VAL A 67 16.249 -6.155 51.720 1.00 18.34 C ANISOU 478 CG2 VAL A 67 2360 2493 2114 44 53 70 C ATOM 479 N ALA A 68 15.997 -5.599 56.304 1.00 19.67 N ANISOU 479 N ALA A 68 2622 2539 2309 62 66 227 N ATOM 480 CA ALA A 68 15.452 -5.301 57.635 1.00 19.85 C ANISOU 480 CA ALA A 68 2653 2554 2333 126 83 225 C ATOM 481 C ALA A 68 16.182 -4.129 58.302 1.00 19.75 C ANISOU 481 C ALA A 68 2667 2577 2258 131 49 257 C ATOM 482 O ALA A 68 15.561 -3.305 58.969 1.00 19.94 O ANISOU 482 O ALA A 68 2767 2643 2167 150 95 320 O ATOM 483 CB ALA A 68 15.503 -6.546 58.522 1.00 20.01 C ANISOU 483 CB ALA A 68 2703 2529 2369 69 69 215 C ATOM 484 N ALA A 69 17.495 -4.026 58.087 1.00 19.91 N ANISOU 484 N ALA A 69 2659 2595 2309 132 26 271 N ATOM 485 CA ALA A 69 18.264 -2.900 58.603 1.00 20.25 C ANISOU 485 CA ALA A 69 2670 2661 2361 109 41 188 C ATOM 486 C ALA A 69 17.768 -1.587 57.987 1.00 20.42 C ANISOU 486 C ALA A 69 2674 2644 2438 121 44 129 C ATOM 487 O ALA A 69 17.639 -0.579 58.680 1.00 20.88 O ANISOU 487 O ALA A 69 2813 2749 2368 118 75 145 O ATOM 488 CB ALA A 69 19.745 -3.084 58.323 1.00 20.68 C ANISOU 488 CB ALA A 69 2679 2713 2463 133 74 164 C ATOM 489 N VAL A 70 17.500 -1.606 56.684 1.00 20.44 N ANISOU 489 N VAL A 70 2636 2698 2431 115 109 98 N ATOM 490 CA VAL A 70 16.962 -0.422 55.997 1.00 20.23 C ANISOU 490 CA VAL A 70 2567 2707 2414 127 103 88 C ATOM 491 C VAL A 70 15.616 -0.013 56.597 1.00 20.42 C ANISOU 491 C VAL A 70 2581 2770 2408 86 77 52 C ATOM 492 O VAL A 70 15.434 1.141 56.974 1.00 20.51 O ANISOU 492 O VAL A 70 2593 2785 2414 71 149 82 O ATOM 493 CB VAL A 70 16.818 -0.622 54.455 1.00 20.23 C ANISOU 493 CB VAL A 70 2550 2679 2457 115 81 87 C ATOM 494 CG1 VAL A 70 16.084 0.570 53.818 1.00 20.48 C ANISOU 494 CG1 VAL A 70 2618 2704 2456 129 84 46 C ATOM 495 CG2 VAL A 70 18.197 -0.815 53.799 1.00 20.76 C ANISOU 495 CG2 VAL A 70 2616 2736 2532 159 115 68 C ATOM 496 N ASN A 71 14.696 -0.972 56.674 1.00 20.67 N ANISOU 496 N ASN A 71 2619 2834 2400 100 144 101 N ATOM 497 CA ASN A 71 13.316 -0.706 57.090 1.00 21.18 C ANISOU 497 CA ASN A 71 2634 2888 2524 108 97 90 C ATOM 498 C ASN A 71 13.180 -0.372 58.566 1.00 21.97 C ANISOU 498 C ASN A 71 2767 2969 2609 107 112 82 C ATOM 499 O ASN A 71 12.241 0.322 58.977 1.00 22.45 O ANISOU 499 O ASN A 71 2758 3056 2714 154 102 183 O ATOM 500 CB ASN A 71 12.435 -1.893 56.737 1.00 21.00 C ANISOU 500 CB ASN A 71 2629 2833 2517 97 123 103 C ATOM 501 CG ASN A 71 12.115 -1.943 55.264 1.00 20.76 C ANISOU 501 CG ASN A 71 2595 2813 2479 15 173 92 C ATOM 502 OD1 ASN A 71 11.819 -0.905 54.653 1.00 22.08 O ANISOU 502 OD1 ASN A 71 2746 3008 2633 136 302 154 O ATOM 503 ND2 ASN A 71 12.155 -3.138 54.681 1.00 20.97 N ANISOU 503 ND2 ASN A 71 2629 2813 2526 3 235 225 N ATOM 504 N GLY A 72 14.132 -0.864 59.351 1.00 22.40 N ANISOU 504 N GLY A 72 2797 3038 2673 111 104 99 N ATOM 505 CA GLY A 72 14.116 -0.698 60.797 1.00 22.99 C ANISOU 505 CA GLY A 72 2943 3103 2688 102 89 69 C ATOM 506 C GLY A 72 14.997 0.419 61.319 1.00 22.89 C ANISOU 506 C GLY A 72 2973 3030 2693 64 140 100 C ATOM 507 O GLY A 72 14.604 1.587 61.280 1.00 23.25 O ANISOU 507 O GLY A 72 3100 3137 2596 72 171 44 O ATOM 508 N PRO A 73 16.198 0.069 61.816 1.00 23.17 N ANISOU 508 N PRO A 73 3023 3050 2728 64 120 93 N ATOM 509 CA PRO A 73 17.069 1.030 62.498 1.00 23.13 C ANISOU 509 CA PRO A 73 3003 2998 2787 64 106 116 C ATOM 510 C PRO A 73 17.573 2.169 61.610 1.00 22.81 C ANISOU 510 C PRO A 73 2980 2945 2738 68 92 110 C ATOM 511 O PRO A 73 17.701 3.287 62.091 1.00 23.04 O ANISOU 511 O PRO A 73 3084 2959 2710 137 103 137 O ATOM 512 CB PRO A 73 18.240 0.170 62.990 1.00 23.39 C ANISOU 512 CB PRO A 73 3031 3017 2838 79 109 103 C ATOM 513 CG PRO A 73 18.237 -1.031 62.089 1.00 22.89 C ANISOU 513 CG PRO A 73 2978 2979 2737 46 62 35 C ATOM 514 CD PRO A 73 16.796 -1.280 61.766 1.00 23.57 C ANISOU 514 CD PRO A 73 3042 3038 2874 35 115 60 C ATOM 515 N ILE A 74 17.858 1.895 60.338 1.00 22.39 N ANISOU 515 N ILE A 74 2945 2888 2673 121 57 101 N ATOM 516 CA ILE A 74 18.279 2.966 59.418 1.00 22.36 C ANISOU 516 CA ILE A 74 2922 2907 2666 111 86 67 C ATOM 517 C ILE A 74 17.129 3.967 59.191 1.00 23.00 C ANISOU 517 C ILE A 74 3008 2975 2755 99 62 89 C ATOM 518 O ILE A 74 17.312 5.168 59.392 1.00 23.05 O ANISOU 518 O ILE A 74 3038 2990 2727 172 98 88 O ATOM 519 CB ILE A 74 18.864 2.410 58.082 1.00 22.08 C ANISOU 519 CB ILE A 74 2883 2907 2597 117 88 113 C ATOM 520 CG1 ILE A 74 20.163 1.643 58.365 1.00 21.94 C ANISOU 520 CG1 ILE A 74 2850 2895 2588 95 85 60 C ATOM 521 CG2 ILE A 74 19.085 3.561 57.064 1.00 21.44 C ANISOU 521 CG2 ILE A 74 2775 2859 2512 88 151 97 C ATOM 522 CD1 ILE A 74 20.714 0.809 57.193 1.00 21.76 C ANISOU 522 CD1 ILE A 74 2896 2850 2521 80 28 52 C ATOM 523 N ALA A 75 15.955 3.462 58.812 1.00 23.51 N ANISOU 523 N ALA A 75 3017 3074 2841 100 51 75 N ATOM 524 CA ALA A 75 14.759 4.304 58.629 1.00 24.63 C ANISOU 524 CA ALA A 75 3170 3182 3002 97 54 49 C ATOM 525 C ALA A 75 14.536 5.173 59.864 1.00 25.37 C ANISOU 525 C ALA A 75 3278 3283 3078 101 70 33 C ATOM 526 O ALA A 75 14.458 6.399 59.767 1.00 25.78 O ANISOU 526 O ALA A 75 3362 3381 3051 120 76 63 O ATOM 527 CB ALA A 75 13.527 3.449 58.350 1.00 24.25 C ANISOU 527 CB ALA A 75 3084 3152 2976 118 58 50 C ATOM 528 N GLN A 76 14.484 4.524 61.028 1.00 26.01 N ANISOU 528 N GLN A 76 3350 3381 3152 114 46 48 N ATOM 529 CA GLN A 76 14.202 5.209 62.294 1.00 27.12 C ANISOU 529 CA GLN A 76 3493 3507 3301 83 39 24 C ATOM 530 C GLN A 76 15.202 6.319 62.597 1.00 26.25 C ANISOU 530 C GLN A 76 3406 3398 3167 120 63 46 C ATOM 531 O GLN A 76 14.824 7.368 63.118 1.00 26.51 O ANISOU 531 O GLN A 76 3482 3428 3163 162 68 34 O ATOM 532 CB GLN A 76 14.126 4.201 63.450 1.00 27.39 C ANISOU 532 CB GLN A 76 3516 3533 3357 91 17 47 C ATOM 533 CG GLN A 76 12.836 3.388 63.464 1.00 29.21 C ANISOU 533 CG GLN A 76 3743 3691 3663 11 6 43 C ATOM 534 CD GLN A 76 12.934 2.067 64.227 1.00 30.68 C ANISOU 534 CD GLN A 76 3971 3886 3799 60 59 -4 C ATOM 535 OE1 GLN A 76 13.932 1.782 64.906 1.00 34.01 O ANISOU 535 OE1 GLN A 76 4330 4423 4166 64 -155 12 O ATOM 536 NE2 GLN A 76 11.889 1.247 64.111 1.00 32.01 N ANISOU 536 NE2 GLN A 76 3977 4045 4137 -128 -15 22 N ATOM 537 N ALA A 77 16.469 6.096 62.246 1.00 25.58 N ANISOU 537 N ALA A 77 3291 3336 3091 125 44 29 N ATOM 538 CA ALA A 77 17.526 7.080 62.465 1.00 24.90 C ANISOU 538 CA ALA A 77 3195 3248 3017 144 68 22 C ATOM 539 C ALA A 77 17.509 8.254 61.484 1.00 24.69 C ANISOU 539 C ALA A 77 3166 3198 3014 140 56 -19 C ATOM 540 O ALA A 77 18.092 9.301 61.763 1.00 24.47 O ANISOU 540 O ALA A 77 3165 3170 2961 147 93 -26 O ATOM 541 CB ALA A 77 18.892 6.400 62.441 1.00 25.04 C ANISOU 541 CB ALA A 77 3191 3271 3050 152 69 17 C ATOM 542 N LEU A 78 16.853 8.074 60.339 1.00 24.10 N ANISOU 542 N LEU A 78 3121 3116 2918 192 80 -41 N ATOM 543 CA LEU A 78 16.898 9.078 59.283 1.00 24.02 C ANISOU 543 CA LEU A 78 3107 3103 2916 145 77 -37 C ATOM 544 C LEU A 78 15.609 9.879 59.095 1.00 24.78 C ANISOU 544 C LEU A 78 3185 3193 3034 136 66 -28 C ATOM 545 O LEU A 78 15.661 10.987 58.554 1.00 24.58 O ANISOU 545 O LEU A 78 3166 3154 3018 159 113 -39 O ATOM 546 CB LEU A 78 17.315 8.446 57.953 1.00 23.58 C ANISOU 546 CB LEU A 78 3033 3091 2835 126 58 -40 C ATOM 547 CG LEU A 78 18.698 7.791 57.859 1.00 22.54 C ANISOU 547 CG LEU A 78 2983 2902 2676 161 2 -26 C ATOM 548 CD1 LEU A 78 18.906 7.259 56.455 1.00 22.27 C ANISOU 548 CD1 LEU A 78 2912 2868 2680 154 20 -92 C ATOM 549 CD2 LEU A 78 19.798 8.750 58.207 1.00 21.01 C ANISOU 549 CD2 LEU A 78 2845 2660 2474 228 -12 -76 C ATOM 550 N ILE A 79 14.468 9.320 59.515 1.00 25.35 N ANISOU 550 N ILE A 79 3260 3253 3117 114 63 -14 N ATOM 551 CA ILE A 79 13.186 10.043 59.452 1.00 26.28 C ANISOU 551 CA ILE A 79 3339 3385 3259 118 26 0 C ATOM 552 C ILE A 79 13.356 11.414 60.110 1.00 26.12 C ANISOU 552 C ILE A 79 3329 3364 3229 125 16 -29 C ATOM 553 O ILE A 79 13.858 11.517 61.235 1.00 26.68 O ANISOU 553 O ILE A 79 3376 3492 3267 202 56 -29 O ATOM 554 CB ILE A 79 12.008 9.279 60.136 1.00 26.57 C ANISOU 554 CB ILE A 79 3381 3419 3292 97 6 6 C ATOM 555 CG1 ILE A 79 11.773 7.891 59.518 1.00 27.56 C ANISOU 555 CG1 ILE A 79 3511 3492 3469 139 4 -15 C ATOM 556 CG2 ILE A 79 10.710 10.099 60.075 1.00 27.30 C ANISOU 556 CG2 ILE A 79 3466 3506 3400 132 27 31 C ATOM 557 CD1 ILE A 79 11.517 7.870 58.026 1.00 28.95 C ANISOU 557 CD1 ILE A 79 3728 3726 3546 135 2 -64 C ATOM 558 N GLY A 80 12.963 12.465 59.393 1.00 26.15 N ANISOU 558 N GLY A 80 3379 3335 3218 98 11 -28 N ATOM 559 CA GLY A 80 13.052 13.833 59.910 1.00 25.84 C ANISOU 559 CA GLY A 80 3356 3274 3187 124 11 -32 C ATOM 560 C GLY A 80 14.342 14.568 59.602 1.00 25.51 C ANISOU 560 C GLY A 80 3318 3247 3125 142 17 -36 C ATOM 561 O GLY A 80 14.445 15.779 59.847 1.00 25.55 O ANISOU 561 O GLY A 80 3364 3263 3081 153 22 -76 O ATOM 562 N LYS A 81 15.328 13.857 59.048 1.00 24.93 N ANISOU 562 N LYS A 81 3269 3188 3013 176 6 -33 N ATOM 563 CA LYS A 81 16.617 14.467 58.726 1.00 24.74 C ANISOU 563 CA LYS A 81 3254 3135 3011 171 27 -23 C ATOM 564 C LYS A 81 16.588 15.124 57.338 1.00 24.22 C ANISOU 564 C LYS A 81 3180 3064 2958 191 60 -57 C ATOM 565 O LYS A 81 15.705 14.840 56.532 1.00 24.59 O ANISOU 565 O LYS A 81 3187 3153 3002 266 100 -53 O ATOM 566 CB LYS A 81 17.759 13.435 58.833 1.00 24.82 C ANISOU 566 CB LYS A 81 3263 3145 3023 143 37 -21 C ATOM 567 CG LYS A 81 17.829 12.689 60.178 1.00 25.61 C ANISOU 567 CG LYS A 81 3368 3228 3135 85 -35 -2 C ATOM 568 CD LYS A 81 18.139 13.635 61.312 1.00 26.68 C ANISOU 568 CD LYS A 81 3470 3410 3256 51 -43 -51 C ATOM 569 CE LYS A 81 18.099 12.928 62.653 1.00 28.45 C ANISOU 569 CE LYS A 81 3724 3596 3488 57 -39 7 C ATOM 570 NZ LYS A 81 18.432 13.900 63.730 1.00 30.41 N ANISOU 570 NZ LYS A 81 4038 3797 3718 61 -32 -84 N ATOM 571 N ASP A 82 17.556 15.994 57.079 1.00 24.21 N ANISOU 571 N ASP A 82 3189 3070 2938 218 73 -72 N ATOM 572 CA ASP A 82 17.636 16.755 55.829 1.00 24.05 C ANISOU 572 CA ASP A 82 3164 3056 2916 144 76 -36 C ATOM 573 C ASP A 82 18.413 15.977 54.774 1.00 23.40 C ANISOU 573 C ASP A 82 3099 2960 2829 102 39 -52 C ATOM 574 O ASP A 82 19.636 15.876 54.848 1.00 23.65 O ANISOU 574 O ASP A 82 3150 3057 2776 107 59 -32 O ATOM 575 CB ASP A 82 18.314 18.106 56.081 1.00 24.65 C ANISOU 575 CB ASP A 82 3240 3126 2999 132 49 -48 C ATOM 576 CG ASP A 82 18.452 18.963 54.820 1.00 25.98 C ANISOU 576 CG ASP A 82 3408 3243 3221 69 46 -6 C ATOM 577 OD1 ASP A 82 17.906 18.612 53.747 1.00 26.03 O ANISOU 577 OD1 ASP A 82 3532 3123 3234 118 -1 -63 O ATOM 578 OD2 ASP A 82 19.127 20.009 54.917 1.00 28.45 O ANISOU 578 OD2 ASP A 82 3829 3371 3609 16 78 -54 O ATOM 579 N ALA A 83 17.700 15.466 53.776 1.00 22.87 N ANISOU 579 N ALA A 83 3048 2895 2744 95 48 -25 N ATOM 580 CA ALA A 83 18.323 14.675 52.708 1.00 21.82 C ANISOU 580 CA ALA A 83 2898 2718 2672 116 32 -39 C ATOM 581 C ALA A 83 19.435 15.413 51.942 1.00 21.47 C ANISOU 581 C ALA A 83 2876 2665 2615 109 14 -25 C ATOM 582 O ALA A 83 20.369 14.784 51.436 1.00 20.98 O ANISOU 582 O ALA A 83 2829 2613 2529 164 31 10 O ATOM 583 CB ALA A 83 17.260 14.163 51.744 1.00 21.57 C ANISOU 583 CB ALA A 83 2853 2695 2645 89 41 -55 C ATOM 584 N LYS A 84 19.346 16.741 51.868 1.00 20.97 N ANISOU 584 N LYS A 84 2860 2545 2561 127 8 -54 N ATOM 585 CA LYS A 84 20.355 17.548 51.166 1.00 21.31 C ANISOU 585 CA LYS A 84 2880 2593 2623 113 1 -62 C ATOM 586 C LYS A 84 21.736 17.483 51.817 1.00 21.14 C ANISOU 586 C LYS A 84 2880 2586 2567 110 2 -54 C ATOM 587 O LYS A 84 22.760 17.677 51.152 1.00 20.84 O ANISOU 587 O LYS A 84 2855 2582 2479 101 -49 -31 O ATOM 588 CB LYS A 84 19.909 19.011 51.054 1.00 21.50 C ANISOU 588 CB LYS A 84 2922 2600 2646 117 4 -54 C ATOM 589 CG LYS A 84 18.652 19.244 50.252 1.00 22.93 C ANISOU 589 CG LYS A 84 3031 2826 2852 59 -35 -80 C ATOM 590 CD LYS A 84 18.354 20.740 50.212 1.00 25.16 C ANISOU 590 CD LYS A 84 3348 2962 3250 104 16 15 C ATOM 591 CE LYS A 84 16.994 21.038 49.613 1.00 27.95 C ANISOU 591 CE LYS A 84 3571 3563 3484 -12 -33 28 C ATOM 592 NZ LYS A 84 16.548 22.430 49.955 1.00 29.60 N ANISOU 592 NZ LYS A 84 3966 3363 3918 215 44 -90 N ATOM 593 N ASP A 85 21.759 17.213 53.121 1.00 21.57 N ANISOU 593 N ASP A 85 2940 2676 2576 145 -21 -95 N ATOM 594 CA ASP A 85 23.003 17.087 53.863 1.00 21.74 C ANISOU 594 CA ASP A 85 2957 2710 2593 150 -24 -118 C ATOM 595 C ASP A 85 23.553 15.669 53.719 1.00 21.55 C ANISOU 595 C ASP A 85 2962 2670 2557 128 4 -93 C ATOM 596 O ASP A 85 23.472 14.871 54.649 1.00 21.66 O ANISOU 596 O ASP A 85 3029 2677 2524 145 -18 -134 O ATOM 597 CB ASP A 85 22.759 17.414 55.338 1.00 22.30 C ANISOU 597 CB ASP A 85 3038 2817 2618 148 -22 -91 C ATOM 598 CG ASP A 85 24.035 17.382 56.173 1.00 23.87 C ANISOU 598 CG ASP A 85 3093 3152 2821 78 -56 -111 C ATOM 599 OD1 ASP A 85 25.138 17.200 55.607 1.00 23.10 O ANISOU 599 OD1 ASP A 85 3166 3052 2557 51 -112 -347 O ATOM 600 OD2 ASP A 85 23.925 17.538 57.412 1.00 26.62 O ANISOU 600 OD2 ASP A 85 3598 3583 2933 150 -84 -180 O ATOM 601 N GLN A 86 24.111 15.363 52.546 1.00 20.92 N ANISOU 601 N GLN A 86 2867 2600 2480 140 -11 -112 N ATOM 602 CA GLN A 86 24.552 13.997 52.239 1.00 20.36 C ANISOU 602 CA GLN A 86 2762 2566 2405 136 -40 -62 C ATOM 603 C GLN A 86 25.561 13.447 53.248 1.00 20.09 C ANISOU 603 C GLN A 86 2714 2564 2355 120 -29 -90 C ATOM 604 O GLN A 86 25.416 12.312 53.711 1.00 19.67 O ANISOU 604 O GLN A 86 2678 2613 2181 79 -65 -54 O ATOM 605 CB GLN A 86 25.120 13.916 50.823 1.00 20.15 C ANISOU 605 CB GLN A 86 2739 2509 2407 150 34 -103 C ATOM 606 CG GLN A 86 25.483 12.482 50.366 1.00 19.26 C ANISOU 606 CG GLN A 86 2626 2287 2402 91 -59 -43 C ATOM 607 CD GLN A 86 24.260 11.592 50.155 1.00 17.54 C ANISOU 607 CD GLN A 86 2376 2372 1916 120 5 -44 C ATOM 608 OE1 GLN A 86 23.206 12.062 49.713 1.00 17.33 O ANISOU 608 OE1 GLN A 86 2337 2475 1770 173 63 -52 O ATOM 609 NE2 GLN A 86 24.410 10.292 50.436 1.00 16.15 N ANISOU 609 NE2 GLN A 86 2251 2193 1689 34 -65 -59 N ATOM 610 N ALA A 87 26.565 14.251 53.587 1.00 20.26 N ANISOU 610 N ALA A 87 2723 2611 2365 114 -26 -82 N ATOM 611 CA ALA A 87 27.577 13.839 54.567 1.00 20.57 C ANISOU 611 CA ALA A 87 2746 2633 2435 144 -29 -70 C ATOM 612 C ALA A 87 26.957 13.506 55.922 1.00 21.02 C ANISOU 612 C ALA A 87 2814 2682 2490 133 1 -87 C ATOM 613 O ALA A 87 27.360 12.538 56.575 1.00 20.53 O ANISOU 613 O ALA A 87 2840 2644 2313 171 -15 -124 O ATOM 614 CB ALA A 87 28.649 14.900 54.714 1.00 20.62 C ANISOU 614 CB ALA A 87 2786 2618 2430 107 0 -96 C ATOM 615 N GLY A 88 25.982 14.313 56.342 1.00 21.35 N ANISOU 615 N GLY A 88 2828 2740 2543 137 -8 -75 N ATOM 616 CA GLY A 88 25.275 14.080 57.596 1.00 21.50 C ANISOU 616 CA GLY A 88 2851 2806 2510 152 12 -97 C ATOM 617 C GLY A 88 24.467 12.798 57.618 1.00 21.27 C ANISOU 617 C GLY A 88 2811 2783 2485 148 15 -76 C ATOM 618 O GLY A 88 24.464 12.062 58.615 1.00 21.71 O ANISOU 618 O GLY A 88 2960 2814 2473 214 6 -97 O ATOM 619 N ILE A 89 23.773 12.533 56.511 1.00 20.89 N ANISOU 619 N ILE A 89 2738 2766 2433 139 -10 -76 N ATOM 620 CA ILE A 89 22.986 11.320 56.342 1.00 20.51 C ANISOU 620 CA ILE A 89 2688 2688 2413 141 -39 -21 C ATOM 621 C ILE A 89 23.900 10.098 56.376 1.00 20.51 C ANISOU 621 C ILE A 89 2695 2667 2429 121 -5 -40 C ATOM 622 O ILE A 89 23.639 9.121 57.100 1.00 20.68 O ANISOU 622 O ILE A 89 2768 2672 2418 226 29 -15 O ATOM 623 CB ILE A 89 22.180 11.369 54.997 1.00 20.20 C ANISOU 623 CB ILE A 89 2640 2632 2403 137 -90 -12 C ATOM 624 CG1 ILE A 89 21.156 12.519 55.015 1.00 21.01 C ANISOU 624 CG1 ILE A 89 2673 2732 2574 161 7 -13 C ATOM 625 CG2 ILE A 89 21.521 10.030 54.666 1.00 19.38 C ANISOU 625 CG2 ILE A 89 2481 2620 2261 148 -45 -14 C ATOM 626 CD1 ILE A 89 20.046 12.391 56.062 1.00 19.79 C ANISOU 626 CD1 ILE A 89 2522 2447 2549 33 4 -51 C ATOM 627 N ASP A 90 24.972 10.167 55.597 1.00 20.45 N ANISOU 627 N ASP A 90 2692 2679 2398 122 -35 -31 N ATOM 628 CA ASP A 90 25.947 9.087 55.530 1.00 19.87 C ANISOU 628 CA ASP A 90 2632 2629 2289 111 -44 -7 C ATOM 629 C ASP A 90 26.606 8.859 56.892 1.00 20.26 C ANISOU 629 C ASP A 90 2719 2682 2297 100 -53 1 C ATOM 630 O ASP A 90 26.791 7.716 57.301 1.00 20.17 O ANISOU 630 O ASP A 90 2739 2657 2265 114 -28 -60 O ATOM 631 CB ASP A 90 26.985 9.371 54.438 1.00 19.73 C ANISOU 631 CB ASP A 90 2616 2620 2261 87 -70 -37 C ATOM 632 CG ASP A 90 26.440 9.095 53.041 1.00 18.76 C ANISOU 632 CG ASP A 90 2497 2500 2129 105 -17 -8 C ATOM 633 OD1 ASP A 90 25.485 8.305 52.939 1.00 16.89 O ANISOU 633 OD1 ASP A 90 2459 2369 1587 251 -40 -222 O ATOM 634 OD2 ASP A 90 26.971 9.661 52.060 1.00 18.54 O ANISOU 634 OD2 ASP A 90 2466 2546 2031 113 -111 20 O ATOM 635 N LYS A 91 26.920 9.945 57.593 1.00 20.78 N ANISOU 635 N LYS A 91 2807 2704 2383 104 -85 21 N ATOM 636 CA LYS A 91 27.536 9.846 58.927 1.00 21.84 C ANISOU 636 CA LYS A 91 2953 2862 2482 94 -108 10 C ATOM 637 C LYS A 91 26.606 9.181 59.947 1.00 21.75 C ANISOU 637 C LYS A 91 2945 2824 2495 111 -82 -3 C ATOM 638 O LYS A 91 27.062 8.351 60.747 1.00 21.92 O ANISOU 638 O LYS A 91 3041 2884 2405 148 -102 27 O ATOM 639 CB LYS A 91 28.026 11.209 59.426 1.00 22.24 C ANISOU 639 CB LYS A 91 3019 2875 2555 77 -114 48 C ATOM 640 CG LYS A 91 28.522 11.214 60.892 1.00 23.12 C ANISOU 640 CG LYS A 91 3184 2968 2632 33 -144 15 C ATOM 641 CD LYS A 91 28.887 12.618 61.360 1.00 23.54 C ANISOU 641 CD LYS A 91 3185 3047 2711 45 -125 -62 C ATOM 642 CE LYS A 91 29.294 12.642 62.847 1.00 25.56 C ANISOU 642 CE LYS A 91 3489 3379 2841 21 -91 -46 C ATOM 643 NZ LYS A 91 30.320 11.619 63.198 1.00 28.08 N ANISOU 643 NZ LYS A 91 3661 3589 3418 98 -167 145 N ATOM 644 N ILE A 92 25.317 9.526 59.921 1.00 21.42 N ANISOU 644 N ILE A 92 2912 2829 2396 78 -79 -10 N ATOM 645 CA ILE A 92 24.335 8.875 60.792 1.00 21.48 C ANISOU 645 CA ILE A 92 2877 2828 2457 93 -38 -42 C ATOM 646 C ILE A 92 24.344 7.365 60.602 1.00 20.85 C ANISOU 646 C ILE A 92 2824 2793 2305 110 -13 -36 C ATOM 647 O ILE A 92 24.407 6.610 61.571 1.00 20.49 O ANISOU 647 O ILE A 92 2813 2769 2201 135 26 -8 O ATOM 648 CB ILE A 92 22.905 9.461 60.624 1.00 21.71 C ANISOU 648 CB ILE A 92 2901 2836 2510 85 -57 -16 C ATOM 649 CG1 ILE A 92 22.844 10.866 61.242 1.00 22.53 C ANISOU 649 CG1 ILE A 92 2986 2889 2682 93 -80 -17 C ATOM 650 CG2 ILE A 92 21.851 8.540 61.261 1.00 22.49 C ANISOU 650 CG2 ILE A 92 2952 2956 2634 80 -17 -5 C ATOM 651 CD1 ILE A 92 21.624 11.699 60.799 1.00 22.40 C ANISOU 651 CD1 ILE A 92 2988 2912 2611 148 -1 -6 C ATOM 652 N MET A 93 24.301 6.921 59.349 1.00 19.72 N ANISOU 652 N MET A 93 2738 2696 2059 119 -33 -76 N ATOM 653 CA MET A 93 24.312 5.485 59.079 1.00 19.01 C ANISOU 653 CA MET A 93 2664 2614 1946 162 -11 -55 C ATOM 654 C MET A 93 25.649 4.853 59.461 1.00 18.97 C ANISOU 654 C MET A 93 2626 2608 1971 114 1 -63 C ATOM 655 O MET A 93 25.684 3.760 60.028 1.00 18.70 O ANISOU 655 O MET A 93 2607 2571 1925 159 5 -81 O ATOM 656 CB MET A 93 23.984 5.197 57.612 1.00 18.76 C ANISOU 656 CB MET A 93 2585 2641 1899 171 -6 -34 C ATOM 657 CG MET A 93 22.559 5.575 57.201 1.00 19.31 C ANISOU 657 CG MET A 93 2660 2670 2006 134 -55 -93 C ATOM 658 SD MET A 93 22.229 4.995 55.524 1.00 18.31 S ANISOU 658 SD MET A 93 2733 2584 1639 351 177 -22 S ATOM 659 CE MET A 93 23.161 6.182 54.539 1.00 19.10 C ANISOU 659 CE MET A 93 2771 2433 2052 135 91 -11 C ATOM 660 N ILE A 94 26.741 5.544 59.157 1.00 19.34 N ANISOU 660 N ILE A 94 2654 2661 2032 124 -7 -86 N ATOM 661 CA ILE A 94 28.069 5.042 59.480 1.00 20.13 C ANISOU 661 CA ILE A 94 2734 2724 2190 120 -30 -42 C ATOM 662 C ILE A 94 28.234 4.864 60.989 1.00 20.89 C ANISOU 662 C ILE A 94 2871 2799 2265 129 -48 -44 C ATOM 663 O ILE A 94 28.721 3.828 61.446 1.00 20.88 O ANISOU 663 O ILE A 94 2883 2761 2287 235 -60 -126 O ATOM 664 CB ILE A 94 29.183 5.945 58.898 1.00 20.34 C ANISOU 664 CB ILE A 94 2717 2748 2262 67 -18 -32 C ATOM 665 CG1 ILE A 94 29.265 5.745 57.372 1.00 20.23 C ANISOU 665 CG1 ILE A 94 2761 2655 2269 92 -28 -43 C ATOM 666 CG2 ILE A 94 30.541 5.648 59.558 1.00 20.25 C ANISOU 666 CG2 ILE A 94 2778 2646 2268 70 -62 11 C ATOM 667 CD1 ILE A 94 29.945 6.884 56.633 1.00 21.26 C ANISOU 667 CD1 ILE A 94 2765 2801 2511 15 -3 -1 C ATOM 668 N ASP A 95 27.809 5.868 61.753 1.00 21.63 N ANISOU 668 N ASP A 95 2991 2851 2376 162 -39 -63 N ATOM 669 CA ASP A 95 27.944 5.803 63.217 1.00 22.54 C ANISOU 669 CA ASP A 95 3079 2998 2488 145 -67 -32 C ATOM 670 C ASP A 95 27.016 4.765 63.831 1.00 22.99 C ANISOU 670 C ASP A 95 3105 3030 2600 140 -33 -27 C ATOM 671 O ASP A 95 27.383 4.114 64.820 1.00 24.17 O ANISOU 671 O ASP A 95 3285 3209 2689 179 -22 7 O ATOM 672 CB ASP A 95 27.663 7.163 63.866 1.00 22.87 C ANISOU 672 CB ASP A 95 3131 3016 2542 129 -79 -56 C ATOM 673 CG ASP A 95 28.712 8.207 63.539 1.00 24.60 C ANISOU 673 CG ASP A 95 3280 3277 2787 66 -118 -30 C ATOM 674 OD1 ASP A 95 29.815 7.857 63.060 1.00 26.29 O ANISOU 674 OD1 ASP A 95 3403 3577 3008 83 -40 -208 O ATOM 675 OD2 ASP A 95 28.435 9.401 63.778 1.00 27.74 O ANISOU 675 OD2 ASP A 95 3872 3551 3117 127 -119 -156 O ATOM 676 N LEU A 96 25.813 4.633 63.272 1.00 23.23 N ANISOU 676 N LEU A 96 3097 3067 2659 129 -2 -35 N ATOM 677 CA LEU A 96 24.812 3.705 63.790 1.00 23.35 C ANISOU 677 CA LEU A 96 3060 3092 2720 106 -8 5 C ATOM 678 C LEU A 96 25.226 2.257 63.573 1.00 23.27 C ANISOU 678 C LEU A 96 3052 3079 2709 92 19 -4 C ATOM 679 O LEU A 96 25.085 1.423 64.471 1.00 23.82 O ANISOU 679 O LEU A 96 3127 3096 2826 121 37 44 O ATOM 680 CB LEU A 96 23.431 3.967 63.181 1.00 23.81 C ANISOU 680 CB LEU A 96 3094 3150 2801 65 -1 11 C ATOM 681 CG LEU A 96 22.267 3.275 63.885 1.00 24.93 C ANISOU 681 CG LEU A 96 3175 3348 2949 91 41 -33 C ATOM 682 CD1 LEU A 96 22.069 3.888 65.271 1.00 25.19 C ANISOU 682 CD1 LEU A 96 3273 3350 2947 40 59 -84 C ATOM 683 CD2 LEU A 96 21.005 3.387 63.060 1.00 25.73 C ANISOU 683 CD2 LEU A 96 3201 3360 3214 74 -72 -73 C ATOM 684 N ASP A 97 25.738 1.962 62.381 1.00 22.67 N ANISOU 684 N ASP A 97 2938 3038 2636 130 -7 12 N ATOM 685 CA ASP A 97 26.367 0.669 62.119 1.00 21.75 C ANISOU 685 CA ASP A 97 2810 2949 2503 89 -5 -3 C ATOM 686 C ASP A 97 27.524 0.421 63.107 1.00 21.53 C ANISOU 686 C ASP A 97 2770 2923 2487 100 -23 -1 C ATOM 687 O ASP A 97 27.603 -0.650 63.723 1.00 21.66 O ANISOU 687 O ASP A 97 2763 3039 2426 107 -37 25 O ATOM 688 CB ASP A 97 26.845 0.612 60.662 1.00 21.73 C ANISOU 688 CB ASP A 97 2819 2959 2477 92 6 19 C ATOM 689 CG ASP A 97 27.688 -0.612 60.367 1.00 20.58 C ANISOU 689 CG ASP A 97 2723 2792 2302 25 70 44 C ATOM 690 OD1 ASP A 97 27.138 -1.593 59.843 1.00 20.58 O ANISOU 690 OD1 ASP A 97 2665 2782 2370 55 158 167 O ATOM 691 OD2 ASP A 97 28.910 -0.581 60.638 1.00 20.40 O ANISOU 691 OD2 ASP A 97 2911 2867 1973 197 -56 -45 O ATOM 692 N GLY A 98 28.405 1.414 63.254 1.00 20.90 N ANISOU 692 N GLY A 98 2654 2889 2397 143 -87 8 N ATOM 693 CA GLY A 98 29.506 1.358 64.236 1.00 20.24 C ANISOU 693 CA GLY A 98 2615 2824 2249 143 -80 -65 C ATOM 694 C GLY A 98 30.743 0.560 63.856 1.00 20.08 C ANISOU 694 C GLY A 98 2606 2799 2222 145 -92 -62 C ATOM 695 O GLY A 98 31.723 0.551 64.605 1.00 20.01 O ANISOU 695 O GLY A 98 2559 2829 2214 249 -62 -71 O ATOM 696 N THR A 99 30.712 -0.116 62.703 1.00 19.45 N ANISOU 696 N THR A 99 2613 2706 2071 181 -102 -15 N ATOM 697 CA THR A 99 31.867 -0.904 62.250 1.00 19.12 C ANISOU 697 CA THR A 99 2601 2624 2036 115 -70 37 C ATOM 698 C THR A 99 32.519 -0.243 61.043 1.00 19.11 C ANISOU 698 C THR A 99 2597 2592 2069 136 -62 46 C ATOM 699 O THR A 99 31.823 0.326 60.186 1.00 19.18 O ANISOU 699 O THR A 99 2713 2626 1948 233 -86 44 O ATOM 700 CB THR A 99 31.492 -2.360 61.890 1.00 19.07 C ANISOU 700 CB THR A 99 2527 2646 2072 97 -87 38 C ATOM 701 OG1 THR A 99 30.736 -2.378 60.673 1.00 18.32 O ANISOU 701 OG1 THR A 99 2678 2475 1808 138 -58 38 O ATOM 702 CG2 THR A 99 30.669 -3.002 63.000 1.00 18.31 C ANISOU 702 CG2 THR A 99 2513 2374 2069 74 -95 134 C ATOM 703 N GLU A 100 33.843 -0.325 60.970 1.00 18.39 N ANISOU 703 N GLU A 100 2557 2472 1954 91 -63 38 N ATOM 704 CA GLU A 100 34.579 0.302 59.877 1.00 18.69 C ANISOU 704 CA GLU A 100 2585 2457 2059 62 -45 27 C ATOM 705 C GLU A 100 34.114 -0.198 58.505 1.00 17.54 C ANISOU 705 C GLU A 100 2463 2273 1928 93 -82 69 C ATOM 706 O GLU A 100 33.979 0.592 57.565 1.00 17.88 O ANISOU 706 O GLU A 100 2663 2220 1911 89 -52 122 O ATOM 707 CB GLU A 100 36.090 0.102 60.043 1.00 19.60 C ANISOU 707 CB GLU A 100 2665 2604 2176 64 -91 -7 C ATOM 708 CG GLU A 100 36.922 0.955 59.087 1.00 23.27 C ANISOU 708 CG GLU A 100 3189 2973 2680 -43 16 55 C ATOM 709 CD GLU A 100 36.539 2.438 59.131 1.00 34.63 C ANISOU 709 CD GLU A 100 4045 4049 5062 -80 279 63 C ATOM 710 OE1 GLU A 100 36.117 2.984 58.080 1.00 30.82 O ANISOU 710 OE1 GLU A 100 4273 4165 3269 125 -312 306 O ATOM 711 OE2 GLU A 100 36.651 3.060 60.218 1.00 30.94 O ANISOU 711 OE2 GLU A 100 4475 3967 3312 -79 -92 -419 O ATOM 712 N ASN A 101 33.876 -1.500 58.410 1.00 16.55 N ANISOU 712 N ASN A 101 2337 2188 1763 98 -81 128 N ATOM 713 CA ASN A 101 33.524 -2.167 57.154 1.00 15.72 C ANISOU 713 CA ASN A 101 2234 2047 1689 131 -68 124 C ATOM 714 C ASN A 101 32.008 -2.342 56.934 1.00 15.54 C ANISOU 714 C ASN A 101 2207 2023 1673 145 -57 184 C ATOM 715 O ASN A 101 31.574 -3.134 56.094 1.00 15.82 O ANISOU 715 O ASN A 101 2152 2058 1800 240 -120 177 O ATOM 716 CB ASN A 101 34.258 -3.522 57.052 1.00 15.29 C ANISOU 716 CB ASN A 101 2204 1993 1613 115 -30 189 C ATOM 717 CG ASN A 101 33.871 -4.481 58.177 1.00 15.10 C ANISOU 717 CG ASN A 101 2190 1969 1577 135 -172 167 C ATOM 718 OD1 ASN A 101 33.186 -4.089 59.118 1.00 15.50 O ANISOU 718 OD1 ASN A 101 2389 1979 1519 155 -234 230 O ATOM 719 ND2 ASN A 101 34.296 -5.741 58.071 1.00 15.58 N ANISOU 719 ND2 ASN A 101 2443 2025 1449 98 -307 -9 N ATOM 720 N LYS A 102 31.206 -1.605 57.695 1.00 15.81 N ANISOU 720 N LYS A 102 2226 2151 1628 135 -69 209 N ATOM 721 CA LYS A 102 29.747 -1.614 57.549 1.00 15.92 C ANISOU 721 CA LYS A 102 2235 2200 1613 111 -49 220 C ATOM 722 C LYS A 102 29.136 -3.013 57.631 1.00 16.98 C ANISOU 722 C LYS A 102 2301 2334 1815 95 -37 174 C ATOM 723 O LYS A 102 28.154 -3.308 56.957 1.00 17.07 O ANISOU 723 O LYS A 102 2368 2422 1696 137 -7 206 O ATOM 724 CB LYS A 102 29.340 -0.914 56.236 1.00 15.17 C ANISOU 724 CB LYS A 102 2159 2075 1530 60 -55 200 C ATOM 725 CG LYS A 102 29.702 0.542 56.224 1.00 14.72 C ANISOU 725 CG LYS A 102 2171 1912 1509 89 -71 227 C ATOM 726 CD LYS A 102 29.427 1.174 54.853 1.00 15.75 C ANISOU 726 CD LYS A 102 2398 2064 1522 24 -21 133 C ATOM 727 CE LYS A 102 29.812 2.655 54.857 1.00 15.99 C ANISOU 727 CE LYS A 102 2249 2085 1739 0 19 51 C ATOM 728 NZ LYS A 102 31.262 2.908 55.080 1.00 16.63 N ANISOU 728 NZ LYS A 102 2328 2192 1798 48 44 63 N ATOM 729 N SER A 103 29.712 -3.868 58.489 1.00 17.68 N ANISOU 729 N SER A 103 2423 2444 1851 97 -30 213 N ATOM 730 CA SER A 103 29.370 -5.287 58.509 1.00 18.74 C ANISOU 730 CA SER A 103 2519 2541 2061 78 -48 116 C ATOM 731 C SER A 103 28.261 -5.649 59.495 1.00 19.63 C ANISOU 731 C SER A 103 2628 2581 2248 39 -45 134 C ATOM 732 O SER A 103 27.850 -6.809 59.561 1.00 20.77 O ANISOU 732 O SER A 103 2843 2663 2385 -6 40 162 O ATOM 733 CB SER A 103 30.621 -6.142 58.752 1.00 18.88 C ANISOU 733 CB SER A 103 2561 2534 2077 69 -70 88 C ATOM 734 OG SER A 103 31.265 -5.772 59.967 1.00 18.80 O ANISOU 734 OG SER A 103 2544 2736 1860 160 -169 188 O ATOM 735 N LYS A 104 27.767 -4.664 60.241 1.00 20.25 N ANISOU 735 N LYS A 104 2697 2709 2287 47 -30 122 N ATOM 736 CA LYS A 104 26.584 -4.871 61.078 1.00 21.36 C ANISOU 736 CA LYS A 104 2748 2882 2483 21 -36 84 C ATOM 737 C LYS A 104 25.296 -4.822 60.253 1.00 20.91 C ANISOU 737 C LYS A 104 2694 2809 2442 45 5 65 C ATOM 738 O LYS A 104 24.575 -5.813 60.197 1.00 21.35 O ANISOU 738 O LYS A 104 2828 2874 2410 35 -76 127 O ATOM 739 CB LYS A 104 26.547 -3.894 62.254 1.00 22.12 C ANISOU 739 CB LYS A 104 2851 2946 2608 23 -31 50 C ATOM 740 CG LYS A 104 25.269 -3.953 63.076 1.00 25.03 C ANISOU 740 CG LYS A 104 3116 3366 3027 -16 30 49 C ATOM 741 CD LYS A 104 25.558 -3.811 64.559 1.00 28.69 C ANISOU 741 CD LYS A 104 3747 3768 3385 -14 -6 -50 C ATOM 742 CE LYS A 104 24.515 -2.944 65.217 1.00 32.21 C ANISOU 742 CE LYS A 104 4019 4319 3900 120 -3 -31 C ATOM 743 NZ LYS A 104 24.982 -1.536 65.211 1.00 32.75 N ANISOU 743 NZ LYS A 104 4252 4012 4177 -85 -25 67 N ATOM 744 N PHE A 105 25.035 -3.686 59.602 1.00 20.52 N ANISOU 744 N PHE A 105 2634 2763 2400 98 38 40 N ATOM 745 CA PHE A 105 23.857 -3.521 58.745 1.00 20.49 C ANISOU 745 CA PHE A 105 2640 2762 2380 54 19 34 C ATOM 746 C PHE A 105 24.099 -4.028 57.319 1.00 19.57 C ANISOU 746 C PHE A 105 2515 2647 2271 48 27 59 C ATOM 747 O PHE A 105 23.160 -4.414 56.617 1.00 20.00 O ANISOU 747 O PHE A 105 2620 2687 2290 66 31 66 O ATOM 748 CB PHE A 105 23.447 -2.049 58.642 1.00 21.05 C ANISOU 748 CB PHE A 105 2719 2784 2494 65 45 10 C ATOM 749 CG PHE A 105 22.977 -1.437 59.929 1.00 22.66 C ANISOU 749 CG PHE A 105 2894 3076 2639 66 22 1 C ATOM 750 CD1 PHE A 105 22.266 -2.183 60.870 1.00 23.53 C ANISOU 750 CD1 PHE A 105 3058 3159 2721 83 53 14 C ATOM 751 CD2 PHE A 105 23.205 -0.090 60.172 1.00 24.37 C ANISOU 751 CD2 PHE A 105 3088 3237 2932 42 15 -17 C ATOM 752 CE1 PHE A 105 21.823 -1.580 62.059 1.00 23.49 C ANISOU 752 CE1 PHE A 105 3116 3104 2702 57 21 -49 C ATOM 753 CE2 PHE A 105 22.761 0.516 61.346 1.00 24.79 C ANISOU 753 CE2 PHE A 105 3083 3328 3006 24 66 -20 C ATOM 754 CZ PHE A 105 22.072 -0.236 62.287 1.00 23.80 C ANISOU 754 CZ PHE A 105 3107 3181 2754 44 47 -6 C ATOM 755 N GLY A 106 25.358 -3.991 56.896 1.00 18.20 N ANISOU 755 N GLY A 106 2395 2469 2048 74 17 116 N ATOM 756 CA GLY A 106 25.730 -4.404 55.551 1.00 17.24 C ANISOU 756 CA GLY A 106 2236 2367 1946 46 43 116 C ATOM 757 C GLY A 106 25.950 -3.181 54.676 1.00 15.90 C ANISOU 757 C GLY A 106 2079 2176 1784 62 36 112 C ATOM 758 O GLY A 106 25.141 -2.238 54.682 1.00 15.34 O ANISOU 758 O GLY A 106 2093 2195 1540 116 121 160 O ATOM 759 N ALA A 107 27.054 -3.189 53.932 1.00 15.16 N ANISOU 759 N ALA A 107 1995 2115 1650 99 37 138 N ATOM 760 CA ALA A 107 27.340 -2.114 52.991 1.00 15.00 C ANISOU 760 CA ALA A 107 1874 2053 1770 90 47 130 C ATOM 761 C ALA A 107 26.258 -2.055 51.915 1.00 14.67 C ANISOU 761 C ALA A 107 1879 2005 1687 83 37 97 C ATOM 762 O ALA A 107 26.048 -0.996 51.317 1.00 14.38 O ANISOU 762 O ALA A 107 1842 1991 1631 140 17 101 O ATOM 763 CB ALA A 107 28.714 -2.302 52.354 1.00 15.22 C ANISOU 763 CB ALA A 107 1881 2140 1759 78 103 178 C ATOM 764 N ASN A 108 25.590 -3.188 51.660 1.00 14.52 N ANISOU 764 N ASN A 108 1804 2031 1678 93 25 100 N ATOM 765 CA ASN A 108 24.469 -3.211 50.710 1.00 14.65 C ANISOU 765 CA ASN A 108 1882 2052 1631 97 58 62 C ATOM 766 C ASN A 108 23.277 -2.384 51.199 1.00 15.52 C ANISOU 766 C ASN A 108 1986 2178 1732 135 71 92 C ATOM 767 O ASN A 108 22.636 -1.674 50.422 1.00 15.67 O ANISOU 767 O ASN A 108 2069 2230 1652 191 129 175 O ATOM 768 CB ASN A 108 24.065 -4.637 50.283 1.00 14.61 C ANISOU 768 CB ASN A 108 1875 2023 1653 67 51 120 C ATOM 769 CG ASN A 108 23.898 -5.616 51.450 1.00 14.75 C ANISOU 769 CG ASN A 108 1980 1922 1702 48 -14 54 C ATOM 770 OD1 ASN A 108 24.324 -5.363 52.589 1.00 15.28 O ANISOU 770 OD1 ASN A 108 2224 2038 1541 151 -87 473 O ATOM 771 ND2 ASN A 108 23.290 -6.762 51.152 1.00 13.30 N ANISOU 771 ND2 ASN A 108 1633 1924 1494 71 -10 187 N ATOM 772 N ALA A 109 22.995 -2.464 52.497 1.00 15.30 N ANISOU 772 N ALA A 109 2018 2188 1607 121 38 137 N ATOM 773 CA ALA A 109 21.917 -1.668 53.084 1.00 16.04 C ANISOU 773 CA ALA A 109 2085 2265 1741 139 53 106 C ATOM 774 C ALA A 109 22.265 -0.185 53.075 1.00 16.37 C ANISOU 774 C ALA A 109 2105 2306 1809 134 34 85 C ATOM 775 O ALA A 109 21.479 0.657 52.597 1.00 16.93 O ANISOU 775 O ALA A 109 2171 2351 1907 213 14 100 O ATOM 776 CB ALA A 109 21.616 -2.139 54.517 1.00 16.64 C ANISOU 776 CB ALA A 109 2169 2389 1765 75 77 133 C ATOM 777 N ILE A 110 23.459 0.128 53.577 1.00 16.08 N ANISOU 777 N ILE A 110 2068 2247 1795 104 19 57 N ATOM 778 CA ILE A 110 23.904 1.511 53.722 1.00 15.84 C ANISOU 778 CA ILE A 110 2043 2242 1733 112 -17 60 C ATOM 779 C ILE A 110 24.065 2.207 52.362 1.00 15.22 C ANISOU 779 C ILE A 110 2034 2083 1663 110 -5 68 C ATOM 780 O ILE A 110 23.609 3.343 52.198 1.00 15.52 O ANISOU 780 O ILE A 110 2165 2140 1593 225 40 27 O ATOM 781 CB ILE A 110 25.170 1.619 54.629 1.00 16.14 C ANISOU 781 CB ILE A 110 2022 2276 1835 139 -8 34 C ATOM 782 CG1 ILE A 110 24.792 1.205 56.058 1.00 16.00 C ANISOU 782 CG1 ILE A 110 1910 2324 1844 107 -32 106 C ATOM 783 CG2 ILE A 110 25.766 3.028 54.596 1.00 16.72 C ANISOU 783 CG2 ILE A 110 2040 2368 1941 121 42 15 C ATOM 784 CD1 ILE A 110 25.983 1.003 56.994 1.00 16.07 C ANISOU 784 CD1 ILE A 110 2051 2367 1685 99 -133 51 C ATOM 785 N LEU A 111 24.669 1.525 51.394 1.00 14.19 N ANISOU 785 N LEU A 111 1916 1927 1547 107 -49 89 N ATOM 786 CA LEU A 111 24.841 2.134 50.074 1.00 14.45 C ANISOU 786 CA LEU A 111 1917 2006 1566 109 0 42 C ATOM 787 C LEU A 111 23.506 2.393 49.379 1.00 14.22 C ANISOU 787 C LEU A 111 1849 1928 1624 97 1 -25 C ATOM 788 O LEU A 111 23.325 3.450 48.787 1.00 14.20 O ANISOU 788 O LEU A 111 1892 1936 1565 82 -19 -36 O ATOM 789 CB LEU A 111 25.751 1.305 49.152 1.00 13.97 C ANISOU 789 CB LEU A 111 1918 1895 1494 63 2 18 C ATOM 790 CG LEU A 111 25.944 1.935 47.759 1.00 15.27 C ANISOU 790 CG LEU A 111 2137 2021 1642 53 -9 28 C ATOM 791 CD1 LEU A 111 26.857 3.172 47.792 1.00 14.77 C ANISOU 791 CD1 LEU A 111 2108 1913 1591 86 44 81 C ATOM 792 CD2 LEU A 111 26.481 0.895 46.807 1.00 16.41 C ANISOU 792 CD2 LEU A 111 2365 2026 1842 87 148 33 C ATOM 793 N ALA A 112 22.587 1.434 49.439 1.00 14.58 N ANISOU 793 N ALA A 112 1840 1981 1718 136 -3 -46 N ATOM 794 CA ALA A 112 21.297 1.596 48.744 1.00 14.71 C ANISOU 794 CA ALA A 112 1850 1931 1807 138 -16 -61 C ATOM 795 C ALA A 112 20.604 2.854 49.262 1.00 15.08 C ANISOU 795 C ALA A 112 1917 1970 1842 133 25 12 C ATOM 796 O ALA A 112 20.111 3.674 48.482 1.00 15.38 O ANISOU 796 O ALA A 112 1939 2020 1883 143 37 71 O ATOM 797 CB ALA A 112 20.427 0.386 48.956 1.00 14.82 C ANISOU 797 CB ALA A 112 1838 1945 1846 159 -33 6 C ATOM 798 N VAL A 113 20.611 3.027 50.579 1.00 15.60 N ANISOU 798 N VAL A 113 2080 2010 1836 117 22 33 N ATOM 799 CA VAL A 113 20.001 4.217 51.188 1.00 15.79 C ANISOU 799 CA VAL A 113 2155 2081 1760 145 74 15 C ATOM 800 C VAL A 113 20.782 5.492 50.856 1.00 15.44 C ANISOU 800 C VAL A 113 2115 2052 1699 158 35 -32 C ATOM 801 O VAL A 113 20.183 6.533 50.556 1.00 15.67 O ANISOU 801 O VAL A 113 2168 2093 1693 271 80 38 O ATOM 802 CB VAL A 113 19.822 4.056 52.724 1.00 16.16 C ANISOU 802 CB VAL A 113 2209 2139 1792 112 11 27 C ATOM 803 CG1 VAL A 113 19.265 5.331 53.332 1.00 17.09 C ANISOU 803 CG1 VAL A 113 2375 2240 1878 96 117 10 C ATOM 804 CG2 VAL A 113 18.912 2.875 53.021 1.00 16.47 C ANISOU 804 CG2 VAL A 113 2173 2200 1882 121 65 -55 C ATOM 805 N SER A 114 22.111 5.411 50.895 1.00 15.34 N ANISOU 805 N SER A 114 2082 2019 1726 136 11 -8 N ATOM 806 CA SER A 114 22.973 6.556 50.605 1.00 15.09 C ANISOU 806 CA SER A 114 2033 2033 1667 143 4 20 C ATOM 807 C SER A 114 22.664 7.128 49.216 1.00 14.97 C ANISOU 807 C SER A 114 2069 1972 1645 136 -22 16 C ATOM 808 O SER A 114 22.482 8.330 49.057 1.00 15.30 O ANISOU 808 O SER A 114 2203 2014 1595 202 40 -75 O ATOM 809 CB SER A 114 24.448 6.147 50.685 1.00 15.47 C ANISOU 809 CB SER A 114 2027 2077 1771 112 -14 35 C ATOM 810 OG SER A 114 25.295 7.275 50.552 1.00 15.26 O ANISOU 810 OG SER A 114 1966 2030 1803 89 -119 -25 O ATOM 811 N LEU A 115 22.627 6.247 48.217 1.00 14.91 N ANISOU 811 N LEU A 115 2072 1939 1652 127 -32 20 N ATOM 812 CA LEU A 115 22.332 6.650 46.837 1.00 14.65 C ANISOU 812 CA LEU A 115 1977 1915 1674 114 3 37 C ATOM 813 C LEU A 115 20.891 7.124 46.633 1.00 15.24 C ANISOU 813 C LEU A 115 2070 1935 1784 98 -9 44 C ATOM 814 O LEU A 115 20.659 8.125 45.939 1.00 15.65 O ANISOU 814 O LEU A 115 2133 2012 1799 159 -29 77 O ATOM 815 CB LEU A 115 22.650 5.499 45.882 1.00 14.64 C ANISOU 815 CB LEU A 115 2006 1889 1667 85 -25 4 C ATOM 816 CG LEU A 115 24.094 4.984 45.930 1.00 14.73 C ANISOU 816 CG LEU A 115 1950 1878 1769 30 26 -21 C ATOM 817 CD1 LEU A 115 24.273 3.817 44.981 1.00 13.71 C ANISOU 817 CD1 LEU A 115 1936 1709 1563 -81 -20 -12 C ATOM 818 CD2 LEU A 115 25.123 6.088 45.622 1.00 15.35 C ANISOU 818 CD2 LEU A 115 1989 1965 1878 -101 28 -23 C ATOM 819 N ALA A 116 19.936 6.398 47.213 1.00 15.64 N ANISOU 819 N ALA A 116 2069 2050 1822 118 42 37 N ATOM 820 CA ALA A 116 18.528 6.764 47.106 1.00 15.60 C ANISOU 820 CA ALA A 116 2068 2037 1820 93 46 46 C ATOM 821 C ALA A 116 18.298 8.125 47.754 1.00 15.87 C ANISOU 821 C ALA A 116 2119 2095 1815 93 32 41 C ATOM 822 O ALA A 116 17.556 8.955 47.221 1.00 15.98 O ANISOU 822 O ALA A 116 2246 2112 1713 207 52 65 O ATOM 823 CB ALA A 116 17.623 5.688 47.743 1.00 16.34 C ANISOU 823 CB ALA A 116 2187 2080 1938 67 97 89 C ATOM 824 N ASN A 117 18.941 8.357 48.896 1.00 15.78 N ANISOU 824 N ASN A 117 2155 2102 1737 82 25 10 N ATOM 825 CA ASN A 117 18.881 9.669 49.544 1.00 16.24 C ANISOU 825 CA ASN A 117 2202 2144 1824 118 -31 25 C ATOM 826 C ASN A 117 19.374 10.770 48.624 1.00 15.91 C ANISOU 826 C ASN A 117 2107 2097 1838 119 15 2 C ATOM 827 O ASN A 117 18.722 11.810 48.479 1.00 16.46 O ANISOU 827 O ASN A 117 2253 2179 1821 210 19 -34 O ATOM 828 CB ASN A 117 19.705 9.698 50.839 1.00 16.36 C ANISOU 828 CB ASN A 117 2209 2198 1807 97 -41 -13 C ATOM 829 CG ASN A 117 19.600 11.033 51.545 1.00 17.24 C ANISOU 829 CG ASN A 117 2357 2274 1919 74 -13 15 C ATOM 830 OD1 ASN A 117 18.592 11.318 52.181 1.00 20.05 O ANISOU 830 OD1 ASN A 117 2742 2687 2187 216 122 -117 O ATOM 831 ND2 ASN A 117 20.620 11.863 51.413 1.00 17.97 N ANISOU 831 ND2 ASN A 117 2491 2311 2023 64 -148 0 N ATOM 832 N ALA A 118 20.524 10.537 47.992 1.00 16.12 N ANISOU 832 N ALA A 118 2078 2125 1921 151 14 91 N ATOM 833 CA ALA A 118 21.115 11.531 47.108 1.00 15.98 C ANISOU 833 CA ALA A 118 2022 2099 1949 122 55 55 C ATOM 834 C ALA A 118 20.194 11.830 45.925 1.00 15.96 C ANISOU 834 C ALA A 118 2062 2049 1950 96 27 23 C ATOM 835 O ALA A 118 20.041 12.993 45.534 1.00 15.76 O ANISOU 835 O ALA A 118 2176 1922 1889 67 18 19 O ATOM 836 CB ALA A 118 22.493 11.066 46.634 1.00 15.48 C ANISOU 836 CB ALA A 118 1986 2104 1789 155 131 9 C ATOM 837 N LYS A 119 19.559 10.795 45.374 1.00 15.44 N ANISOU 837 N LYS A 119 1945 2013 1905 111 26 17 N ATOM 838 CA LYS A 119 18.614 11.000 44.266 1.00 15.62 C ANISOU 838 CA LYS A 119 1979 2048 1907 101 49 -10 C ATOM 839 C LYS A 119 17.401 11.819 44.713 1.00 15.97 C ANISOU 839 C LYS A 119 2034 2065 1970 142 65 15 C ATOM 840 O LYS A 119 16.946 12.717 43.992 1.00 16.38 O ANISOU 840 O LYS A 119 2117 2162 1943 167 118 0 O ATOM 841 CB LYS A 119 18.158 9.665 43.686 1.00 14.78 C ANISOU 841 CB LYS A 119 1870 1894 1850 99 59 42 C ATOM 842 CG LYS A 119 19.268 8.893 42.985 1.00 13.84 C ANISOU 842 CG LYS A 119 1839 1706 1713 40 42 -23 C ATOM 843 CD LYS A 119 18.754 7.573 42.446 1.00 12.98 C ANISOU 843 CD LYS A 119 1666 1611 1655 79 118 -70 C ATOM 844 CE LYS A 119 19.882 6.806 41.754 1.00 12.50 C ANISOU 844 CE LYS A 119 1494 1766 1488 119 144 -82 C ATOM 845 NZ LYS A 119 19.382 5.550 41.128 1.00 13.02 N ANISOU 845 NZ LYS A 119 1718 1791 1438 46 98 62 N ATOM 846 N ALA A 120 16.874 11.487 45.895 1.00 16.73 N ANISOU 846 N ALA A 120 2097 2222 2036 139 59 -17 N ATOM 847 CA ALA A 120 15.720 12.200 46.470 1.00 17.10 C ANISOU 847 CA ALA A 120 2160 2236 2099 121 83 -3 C ATOM 848 C ALA A 120 16.046 13.684 46.694 1.00 17.92 C ANISOU 848 C ALA A 120 2292 2315 2202 123 40 7 C ATOM 849 O ALA A 120 15.243 14.579 46.354 1.00 18.56 O ANISOU 849 O ALA A 120 2347 2439 2263 134 30 -7 O ATOM 850 CB ALA A 120 15.292 11.540 47.771 1.00 17.59 C ANISOU 850 CB ALA A 120 2226 2316 2139 149 46 18 C ATOM 851 N ALA A 121 17.232 13.934 47.251 1.00 17.90 N ANISOU 851 N ALA A 121 2268 2299 2232 69 63 2 N ATOM 852 CA ALA A 121 17.720 15.294 47.500 1.00 17.79 C ANISOU 852 CA ALA A 121 2296 2268 2193 96 66 10 C ATOM 853 C ALA A 121 17.853 16.084 46.206 1.00 18.24 C ANISOU 853 C ALA A 121 2362 2308 2260 123 99 17 C ATOM 854 O ALA A 121 17.452 17.254 46.144 1.00 18.43 O ANISOU 854 O ALA A 121 2400 2327 2274 228 135 8 O ATOM 855 CB ALA A 121 19.053 15.265 48.250 1.00 18.11 C ANISOU 855 CB ALA A 121 2282 2323 2274 99 69 29 C ATOM 856 N ALA A 122 18.423 15.450 45.179 1.00 18.06 N ANISOU 856 N ALA A 122 2361 2328 2170 151 92 7 N ATOM 857 CA ALA A 122 18.540 16.087 43.867 1.00 18.49 C ANISOU 857 CA ALA A 122 2396 2371 2255 159 121 30 C ATOM 858 C ALA A 122 17.162 16.526 43.388 1.00 18.65 C ANISOU 858 C ALA A 122 2442 2380 2263 129 79 5 C ATOM 859 O ALA A 122 16.981 17.692 43.018 1.00 18.51 O ANISOU 859 O ALA A 122 2469 2370 2194 191 118 106 O ATOM 860 CB ALA A 122 19.174 15.130 42.856 1.00 17.91 C ANISOU 860 CB ALA A 122 2362 2228 2215 165 104 -21 C ATOM 861 N ALA A 123 16.192 15.605 43.438 1.00 18.81 N ANISOU 861 N ALA A 123 2445 2431 2270 122 120 7 N ATOM 862 CA ALA A 123 14.817 15.891 43.012 1.00 19.10 C ANISOU 862 CA ALA A 123 2478 2424 2354 157 80 -33 C ATOM 863 C ALA A 123 14.235 17.088 43.777 1.00 19.59 C ANISOU 863 C ALA A 123 2524 2469 2450 179 93 -46 C ATOM 864 O ALA A 123 13.600 17.957 43.180 1.00 20.20 O ANISOU 864 O ALA A 123 2594 2553 2525 267 100 -58 O ATOM 865 CB ALA A 123 13.937 14.674 43.184 1.00 19.05 C ANISOU 865 CB ALA A 123 2448 2413 2374 145 50 -33 C ATOM 866 N ALA A 124 14.476 17.136 45.085 1.00 19.86 N ANISOU 866 N ALA A 124 2555 2470 2518 177 83 -39 N ATOM 867 CA ALA A 124 14.002 18.250 45.925 1.00 20.26 C ANISOU 867 CA ALA A 124 2668 2458 2571 153 79 -85 C ATOM 868 C ALA A 124 14.617 19.593 45.515 1.00 20.85 C ANISOU 868 C ALA A 124 2699 2547 2674 151 95 -57 C ATOM 869 O ALA A 124 13.963 20.648 45.596 1.00 21.60 O ANISOU 869 O ALA A 124 2869 2569 2769 220 116 -85 O ATOM 870 CB ALA A 124 14.277 17.964 47.390 1.00 20.33 C ANISOU 870 CB ALA A 124 2674 2481 2568 135 61 -78 C ATOM 871 N LYS A 125 15.865 19.542 45.069 1.00 20.58 N ANISOU 871 N LYS A 125 2657 2495 2668 150 109 -60 N ATOM 872 CA LYS A 125 16.593 20.714 44.600 1.00 20.20 C ANISOU 872 CA LYS A 125 2593 2521 2557 137 101 -25 C ATOM 873 C LYS A 125 16.293 21.061 43.134 1.00 20.06 C ANISOU 873 C LYS A 125 2594 2481 2544 173 100 3 C ATOM 874 O LYS A 125 16.879 22.001 42.593 1.00 20.79 O ANISOU 874 O LYS A 125 2726 2578 2593 206 134 24 O ATOM 875 CB LYS A 125 18.104 20.513 44.815 1.00 20.00 C ANISOU 875 CB LYS A 125 2561 2506 2528 153 61 2 C ATOM 876 CG LYS A 125 18.520 20.383 46.286 1.00 19.62 C ANISOU 876 CG LYS A 125 2515 2454 2484 102 50 -53 C ATOM 877 CD LYS A 125 19.972 19.962 46.465 1.00 19.53 C ANISOU 877 CD LYS A 125 2527 2426 2467 87 101 -52 C ATOM 878 CE LYS A 125 20.942 20.924 45.784 1.00 19.21 C ANISOU 878 CE LYS A 125 2583 2307 2407 24 16 -64 C ATOM 879 NZ LYS A 125 22.348 20.505 46.002 1.00 19.51 N ANISOU 879 NZ LYS A 125 2614 2341 2458 56 87 -211 N ATOM 880 N GLY A 126 15.382 20.307 42.516 1.00 19.94 N ANISOU 880 N GLY A 126 2596 2515 2463 193 96 54 N ATOM 881 CA GLY A 126 14.999 20.478 41.105 1.00 20.44 C ANISOU 881 CA GLY A 126 2671 2565 2527 179 77 61 C ATOM 882 C GLY A 126 16.136 20.264 40.117 1.00 20.50 C ANISOU 882 C GLY A 126 2683 2539 2564 216 84 78 C ATOM 883 O GLY A 126 16.248 20.974 39.115 1.00 21.63 O ANISOU 883 O GLY A 126 2856 2719 2641 267 62 87 O ATOM 884 N MET A 127 16.996 19.291 40.389 1.00 19.80 N ANISOU 884 N MET A 127 2583 2434 2505 186 83 90 N ATOM 885 CA MET A 127 18.141 19.047 39.517 1.00 19.19 C ANISOU 885 CA MET A 127 2542 2282 2466 202 72 47 C ATOM 886 C MET A 127 18.415 17.549 39.410 1.00 18.36 C ANISOU 886 C MET A 127 2423 2207 2344 132 91 42 C ATOM 887 O MET A 127 18.064 16.798 40.316 1.00 18.28 O ANISOU 887 O MET A 127 2402 2167 2375 165 48 111 O ATOM 888 CB MET A 127 19.376 19.777 40.046 1.00 19.49 C ANISOU 888 CB MET A 127 2569 2371 2463 170 81 42 C ATOM 889 CG MET A 127 19.843 19.299 41.432 1.00 19.81 C ANISOU 889 CG MET A 127 2575 2455 2496 249 26 41 C ATOM 890 SD MET A 127 21.320 20.119 42.045 1.00 20.08 S ANISOU 890 SD MET A 127 2699 2264 2664 335 68 -101 S ATOM 891 CE MET A 127 20.830 21.856 42.052 1.00 20.21 C ANISOU 891 CE MET A 127 2803 2298 2576 228 58 -78 C ATOM 892 N PRO A 128 19.047 17.117 38.305 1.00 17.84 N ANISOU 892 N PRO A 128 2363 2138 2277 102 57 61 N ATOM 893 CA PRO A 128 19.400 15.707 38.166 1.00 16.70 C ANISOU 893 CA PRO A 128 2231 2013 2101 74 34 46 C ATOM 894 C PRO A 128 20.520 15.312 39.133 1.00 15.82 C ANISOU 894 C PRO A 128 2072 1910 2027 42 11 57 C ATOM 895 O PRO A 128 21.283 16.174 39.593 1.00 15.26 O ANISOU 895 O PRO A 128 2151 1840 1807 112 6 84 O ATOM 896 CB PRO A 128 19.876 15.602 36.721 1.00 17.07 C ANISOU 896 CB PRO A 128 2257 2077 2152 53 20 29 C ATOM 897 CG PRO A 128 20.290 16.959 36.347 1.00 18.05 C ANISOU 897 CG PRO A 128 2471 2115 2270 95 114 15 C ATOM 898 CD PRO A 128 19.455 17.914 37.134 1.00 18.02 C ANISOU 898 CD PRO A 128 2389 2166 2289 101 99 32 C ATOM 899 N LEU A 129 20.613 14.019 39.434 1.00 15.09 N ANISOU 899 N LEU A 129 1957 1873 1903 62 -13 23 N ATOM 900 CA LEU A 129 21.629 13.534 40.347 1.00 14.55 C ANISOU 900 CA LEU A 129 1947 1752 1829 43 -30 11 C ATOM 901 C LEU A 129 23.037 14.014 39.979 1.00 14.67 C ANISOU 901 C LEU A 129 1939 1799 1835 49 -27 8 C ATOM 902 O LEU A 129 23.781 14.453 40.855 1.00 14.59 O ANISOU 902 O LEU A 129 2040 1733 1768 5 -50 -109 O ATOM 903 CB LEU A 129 21.601 12.002 40.458 1.00 14.72 C ANISOU 903 CB LEU A 129 1965 1756 1872 23 -81 43 C ATOM 904 CG LEU A 129 22.651 11.411 41.407 1.00 14.72 C ANISOU 904 CG LEU A 129 1978 1821 1792 105 -91 -55 C ATOM 905 CD1 LEU A 129 22.481 11.928 42.853 1.00 15.67 C ANISOU 905 CD1 LEU A 129 2043 2035 1874 41 49 -174 C ATOM 906 CD2 LEU A 129 22.628 9.897 41.387 1.00 14.30 C ANISOU 906 CD2 LEU A 129 1986 1706 1738 10 -23 36 C ATOM 907 N TYR A 130 23.421 13.929 38.705 1.00 14.39 N ANISOU 907 N TYR A 130 1903 1798 1765 38 -16 32 N ATOM 908 CA TYR A 130 24.798 14.303 38.349 1.00 14.53 C ANISOU 908 CA TYR A 130 1939 1802 1779 39 -4 8 C ATOM 909 C TYR A 130 25.109 15.757 38.723 1.00 14.93 C ANISOU 909 C TYR A 130 2005 1813 1855 19 -13 58 C ATOM 910 O TYR A 130 26.228 16.059 39.143 1.00 14.81 O ANISOU 910 O TYR A 130 1982 1805 1840 -20 -30 66 O ATOM 911 CB TYR A 130 25.099 14.040 36.864 1.00 14.72 C ANISOU 911 CB TYR A 130 1963 1882 1747 63 10 -14 C ATOM 912 CG TYR A 130 24.150 14.709 35.889 1.00 14.08 C ANISOU 912 CG TYR A 130 1853 1674 1823 36 68 65 C ATOM 913 CD1 TYR A 130 23.065 14.011 35.360 1.00 14.31 C ANISOU 913 CD1 TYR A 130 1812 1983 1642 233 -51 -49 C ATOM 914 CD2 TYR A 130 24.351 16.042 35.481 1.00 14.48 C ANISOU 914 CD2 TYR A 130 1800 1732 1971 75 57 156 C ATOM 915 CE1 TYR A 130 22.195 14.612 34.461 1.00 14.35 C ANISOU 915 CE1 TYR A 130 1934 1950 1567 119 44 97 C ATOM 916 CE2 TYR A 130 23.473 16.652 34.579 1.00 14.49 C ANISOU 916 CE2 TYR A 130 1863 1905 1735 -56 41 192 C ATOM 917 CZ TYR A 130 22.411 15.923 34.071 1.00 14.55 C ANISOU 917 CZ TYR A 130 1876 1868 1783 140 -9 -36 C ATOM 918 OH TYR A 130 21.545 16.509 33.182 1.00 16.17 O ANISOU 918 OH TYR A 130 2129 2218 1795 171 36 66 O ATOM 919 N GLU A 131 24.106 16.634 38.614 1.00 14.88 N ANISOU 919 N GLU A 131 2002 1777 1875 53 -24 29 N ATOM 920 CA GLU A 131 24.287 18.047 38.999 1.00 15.73 C ANISOU 920 CA GLU A 131 2168 1835 1971 118 -27 38 C ATOM 921 C GLU A 131 24.447 18.180 40.518 1.00 15.57 C ANISOU 921 C GLU A 131 2103 1856 1954 114 -5 11 C ATOM 922 O GLU A 131 25.313 18.918 41.004 1.00 15.47 O ANISOU 922 O GLU A 131 2210 1738 1928 122 1 39 O ATOM 923 CB GLU A 131 23.117 18.909 38.526 1.00 15.70 C ANISOU 923 CB GLU A 131 2103 1841 2018 129 -25 41 C ATOM 924 CG GLU A 131 23.402 20.409 38.713 1.00 17.45 C ANISOU 924 CG GLU A 131 2421 1989 2219 138 -4 -4 C ATOM 925 CD GLU A 131 22.277 21.313 38.236 1.00 17.09 C ANISOU 925 CD GLU A 131 2331 1986 2177 69 -24 74 C ATOM 926 OE1 GLU A 131 21.367 20.838 37.516 1.00 18.25 O ANISOU 926 OE1 GLU A 131 2556 2298 2079 71 -52 210 O ATOM 927 OE2 GLU A 131 22.319 22.521 38.595 1.00 19.32 O ANISOU 927 OE2 GLU A 131 2754 2118 2469 64 -2 -159 O ATOM 928 N HIS A 132 23.607 17.455 41.255 1.00 15.91 N ANISOU 928 N HIS A 132 2215 1850 1977 101 8 14 N ATOM 929 CA HIS A 132 23.679 17.425 42.719 1.00 15.96 C ANISOU 929 CA HIS A 132 2155 1963 1945 54 1 -22 C ATOM 930 C HIS A 132 25.028 16.872 43.200 1.00 15.75 C ANISOU 930 C HIS A 132 2164 1905 1913 61 12 -8 C ATOM 931 O HIS A 132 25.639 17.414 44.129 1.00 15.46 O ANISOU 931 O HIS A 132 2068 1965 1842 59 -23 4 O ATOM 932 CB HIS A 132 22.499 16.621 43.283 1.00 16.29 C ANISOU 932 CB HIS A 132 2189 2047 1951 26 30 -6 C ATOM 933 CG HIS A 132 22.467 16.531 44.776 1.00 16.98 C ANISOU 933 CG HIS A 132 2315 2090 2044 43 -8 -78 C ATOM 934 ND1 HIS A 132 22.504 17.642 45.595 1.00 17.87 N ANISOU 934 ND1 HIS A 132 2522 2151 2117 73 0 -118 N ATOM 935 CD2 HIS A 132 22.377 15.458 45.598 1.00 16.68 C ANISOU 935 CD2 HIS A 132 2232 2036 2070 98 26 -71 C ATOM 936 CE1 HIS A 132 22.464 17.253 46.857 1.00 18.28 C ANISOU 936 CE1 HIS A 132 2569 2174 2201 71 5 28 C ATOM 937 NE2 HIS A 132 22.376 15.933 46.886 1.00 17.57 N ANISOU 937 NE2 HIS A 132 2557 2075 2044 115 -12 -96 N ATOM 938 N ILE A 133 25.500 15.813 42.548 1.00 14.96 N ANISOU 938 N ILE A 133 2046 1758 1880 78 23 -2 N ATOM 939 CA ILE A 133 26.809 15.247 42.879 1.00 14.83 C ANISOU 939 CA ILE A 133 2023 1752 1858 58 -14 -60 C ATOM 940 C ILE A 133 27.921 16.276 42.700 1.00 15.39 C ANISOU 940 C ILE A 133 2071 1836 1939 90 -18 -49 C ATOM 941 O ILE A 133 28.798 16.405 43.563 1.00 16.09 O ANISOU 941 O ILE A 133 2251 1901 1959 91 -127 -62 O ATOM 942 CB ILE A 133 27.100 13.950 42.087 1.00 13.74 C ANISOU 942 CB ILE A 133 1878 1627 1715 24 -4 -46 C ATOM 943 CG1 ILE A 133 26.211 12.810 42.616 1.00 14.52 C ANISOU 943 CG1 ILE A 133 2005 1816 1695 -56 30 -65 C ATOM 944 CG2 ILE A 133 28.604 13.595 42.160 1.00 14.35 C ANISOU 944 CG2 ILE A 133 1925 1795 1731 27 -39 -57 C ATOM 945 CD1 ILE A 133 26.332 11.510 41.822 1.00 14.19 C ANISOU 945 CD1 ILE A 133 1925 1710 1755 44 3 -83 C ATOM 946 N ALA A 134 27.880 17.032 41.604 1.00 15.51 N ANISOU 946 N ALA A 134 2122 1852 1919 84 11 -64 N ATOM 947 CA ALA A 134 28.877 18.076 41.388 1.00 15.86 C ANISOU 947 CA ALA A 134 2190 1878 1956 58 0 -86 C ATOM 948 C ALA A 134 28.853 19.124 42.510 1.00 16.22 C ANISOU 948 C ALA A 134 2220 1951 1991 43 -8 -102 C ATOM 949 O ALA A 134 29.907 19.565 42.980 1.00 16.68 O ANISOU 949 O ALA A 134 2253 2044 2041 67 -2 -119 O ATOM 950 CB ALA A 134 28.694 18.716 40.029 1.00 15.37 C ANISOU 950 CB ALA A 134 2145 1804 1888 26 9 -43 C ATOM 951 N GLU A 135 27.653 19.488 42.954 1.00 17.12 N ANISOU 951 N GLU A 135 2333 2074 2097 51 -53 -135 N ATOM 952 CA GLU A 135 27.494 20.421 44.079 1.00 17.81 C ANISOU 952 CA GLU A 135 2415 2142 2211 35 -30 -114 C ATOM 953 C GLU A 135 28.043 19.833 45.383 1.00 18.13 C ANISOU 953 C GLU A 135 2414 2201 2271 40 -37 -116 C ATOM 954 O GLU A 135 28.798 20.498 46.105 1.00 18.86 O ANISOU 954 O GLU A 135 2518 2315 2333 33 -103 -163 O ATOM 955 CB GLU A 135 26.031 20.839 44.231 1.00 17.65 C ANISOU 955 CB GLU A 135 2397 2083 2224 41 -25 -113 C ATOM 956 CG GLU A 135 25.558 21.747 43.092 1.00 18.88 C ANISOU 956 CG GLU A 135 2549 2285 2338 109 -76 -90 C ATOM 957 CD GLU A 135 24.350 22.617 43.446 1.00 20.54 C ANISOU 957 CD GLU A 135 2690 2490 2622 143 32 -76 C ATOM 958 OE1 GLU A 135 23.709 22.395 44.491 1.00 22.51 O ANISOU 958 OE1 GLU A 135 3031 2619 2899 270 110 -86 O ATOM 959 OE2 GLU A 135 24.038 23.532 42.658 1.00 22.77 O ANISOU 959 OE2 GLU A 135 3044 2733 2873 179 -41 -76 O ATOM 960 N LEU A 136 27.681 18.585 45.674 1.00 18.47 N ANISOU 960 N LEU A 136 2460 2287 2270 -18 7 -112 N ATOM 961 CA LEU A 136 28.211 17.885 46.843 1.00 18.71 C ANISOU 961 CA LEU A 136 2454 2299 2355 12 12 -79 C ATOM 962 C LEU A 136 29.728 17.798 46.807 1.00 19.13 C ANISOU 962 C LEU A 136 2517 2369 2381 -8 -13 -85 C ATOM 963 O LEU A 136 30.378 17.808 47.856 1.00 20.52 O ANISOU 963 O LEU A 136 2624 2628 2542 21 -29 -160 O ATOM 964 CB LEU A 136 27.629 16.472 46.946 1.00 18.60 C ANISOU 964 CB LEU A 136 2445 2269 2352 -25 49 -83 C ATOM 965 CG LEU A 136 26.151 16.290 47.308 1.00 18.70 C ANISOU 965 CG LEU A 136 2403 2328 2371 47 64 -63 C ATOM 966 CD1 LEU A 136 25.819 14.816 47.350 1.00 19.96 C ANISOU 966 CD1 LEU A 136 2606 2452 2524 10 29 -76 C ATOM 967 CD2 LEU A 136 25.826 16.938 48.648 1.00 19.18 C ANISOU 967 CD2 LEU A 136 2496 2550 2242 76 -7 -42 C ATOM 968 N ASN A 137 30.272 17.704 45.594 1.00 19.15 N ANISOU 968 N ASN A 137 2535 2338 2402 -5 0 -103 N ATOM 969 CA ASN A 137 31.699 17.559 45.367 1.00 19.29 C ANISOU 969 CA ASN A 137 2551 2399 2378 -39 -29 -98 C ATOM 970 C ASN A 137 32.464 18.878 45.520 1.00 19.30 C ANISOU 970 C ASN A 137 2549 2423 2360 -55 -40 -59 C ATOM 971 O ASN A 137 33.686 18.890 45.503 1.00 19.88 O ANISOU 971 O ASN A 137 2648 2580 2323 -59 -107 -47 O ATOM 972 CB ASN A 137 31.950 16.962 43.974 1.00 18.98 C ANISOU 972 CB ASN A 137 2481 2379 2351 -8 -24 -113 C ATOM 973 CG ASN A 137 33.361 16.435 43.809 1.00 18.80 C ANISOU 973 CG ASN A 137 2466 2341 2335 -45 -57 -94 C ATOM 974 OD1 ASN A 137 34.074 16.803 42.869 1.00 20.60 O ANISOU 974 OD1 ASN A 137 2709 2424 2690 -43 16 14 O ATOM 975 ND2 ASN A 137 33.782 15.584 44.732 1.00 18.36 N ANISOU 975 ND2 ASN A 137 2429 2099 2447 -82 -110 -33 N ATOM 976 N GLY A 138 31.731 19.983 45.658 1.00 19.55 N ANISOU 976 N GLY A 138 2608 2443 2376 -55 -68 -68 N ATOM 977 CA GLY A 138 32.338 21.312 45.706 1.00 19.64 C ANISOU 977 CA GLY A 138 2628 2450 2382 -83 -66 -63 C ATOM 978 C GLY A 138 32.874 21.778 44.365 1.00 19.88 C ANISOU 978 C GLY A 138 2639 2482 2429 -115 -55 -73 C ATOM 979 O GLY A 138 33.699 22.692 44.295 1.00 20.54 O ANISOU 979 O GLY A 138 2801 2549 2454 -159 -96 -83 O ATOM 980 N THR A 139 32.394 21.148 43.294 1.00 19.33 N ANISOU 980 N THR A 139 2575 2390 2380 -48 -41 -78 N ATOM 981 CA THR A 139 32.832 21.457 41.942 1.00 18.74 C ANISOU 981 CA THR A 139 2479 2260 2379 13 -56 -103 C ATOM 982 C THR A 139 31.594 21.669 41.062 1.00 19.15 C ANISOU 982 C THR A 139 2579 2304 2392 33 -74 -98 C ATOM 983 O THR A 139 31.423 20.998 40.043 1.00 19.13 O ANISOU 983 O THR A 139 2615 2211 2441 21 -100 -156 O ATOM 984 CB THR A 139 33.714 20.327 41.389 1.00 18.55 C ANISOU 984 CB THR A 139 2433 2272 2341 10 -63 -60 C ATOM 985 OG1 THR A 139 33.020 19.087 41.539 1.00 16.58 O ANISOU 985 OG1 THR A 139 2197 1946 2154 146 -4 -180 O ATOM 986 CG2 THR A 139 35.030 20.247 42.152 1.00 18.41 C ANISOU 986 CG2 THR A 139 2384 2197 2413 -60 -71 -125 C ATOM 987 N PRO A 140 30.721 22.620 41.447 1.00 19.29 N ANISOU 987 N PRO A 140 2631 2280 2419 69 -76 -141 N ATOM 988 CA PRO A 140 29.458 22.764 40.717 1.00 19.68 C ANISOU 988 CA PRO A 140 2615 2347 2514 79 -51 -128 C ATOM 989 C PRO A 140 29.693 23.110 39.252 1.00 20.00 C ANISOU 989 C PRO A 140 2643 2400 2555 40 -69 -80 C ATOM 990 O PRO A 140 30.592 23.899 38.923 1.00 20.67 O ANISOU 990 O PRO A 140 2688 2517 2645 -13 -99 -99 O ATOM 991 CB PRO A 140 28.754 23.923 41.440 1.00 19.46 C ANISOU 991 CB PRO A 140 2611 2292 2490 75 -33 -99 C ATOM 992 CG PRO A 140 29.866 24.669 42.119 1.00 19.71 C ANISOU 992 CG PRO A 140 2637 2323 2526 105 -113 -144 C ATOM 993 CD PRO A 140 30.856 23.630 42.519 1.00 19.35 C ANISOU 993 CD PRO A 140 2659 2304 2387 65 -97 -145 C ATOM 994 N GLY A 141 28.908 22.487 38.377 1.00 19.77 N ANISOU 994 N GLY A 141 2628 2366 2515 18 -86 -102 N ATOM 995 CA GLY A 141 28.958 22.781 36.947 1.00 19.82 C ANISOU 995 CA GLY A 141 2654 2343 2534 -22 -57 -48 C ATOM 996 C GLY A 141 30.150 22.202 36.214 1.00 19.34 C ANISOU 996 C GLY A 141 2630 2263 2455 -57 -63 -50 C ATOM 997 O GLY A 141 30.340 22.488 35.030 1.00 20.02 O ANISOU 997 O GLY A 141 2793 2330 2480 -8 -103 -70 O ATOM 998 N LYS A 142 30.955 21.402 36.918 1.00 18.26 N ANISOU 998 N LYS A 142 2512 2059 2364 -98 -83 -65 N ATOM 999 CA LYS A 142 32.130 20.758 36.340 1.00 18.24 C ANISOU 999 CA LYS A 142 2560 2055 2314 -129 -65 -52 C ATOM 1000 C LYS A 142 31.788 19.320 35.973 1.00 17.07 C ANISOU 1000 C LYS A 142 2442 1930 2110 -130 -66 -81 C ATOM 1001 O LYS A 142 31.528 18.498 36.852 1.00 16.98 O ANISOU 1001 O LYS A 142 2541 1905 2005 -166 -103 -135 O ATOM 1002 CB LYS A 142 33.316 20.791 37.318 1.00 18.27 C ANISOU 1002 CB LYS A 142 2541 2092 2309 -102 -57 -70 C ATOM 1003 CG LYS A 142 33.893 22.188 37.580 1.00 22.09 C ANISOU 1003 CG LYS A 142 3000 2511 2882 -101 -103 -68 C ATOM 1004 CD LYS A 142 34.261 22.843 36.257 1.00 25.52 C ANISOU 1004 CD LYS A 142 3453 3129 3113 -82 10 63 C ATOM 1005 CE LYS A 142 35.162 24.044 36.419 1.00 28.56 C ANISOU 1005 CE LYS A 142 3657 3378 3815 -98 -20 -3 C ATOM 1006 NZ LYS A 142 35.264 24.712 35.091 1.00 30.14 N ANISOU 1006 NZ LYS A 142 4064 3832 3554 -57 93 175 N ATOM 1007 N TYR A 143 31.775 19.028 34.673 1.00 15.64 N ANISOU 1007 N TYR A 143 2226 1764 1953 -130 -45 -59 N ATOM 1008 CA TYR A 143 31.382 17.705 34.183 1.00 14.84 C ANISOU 1008 CA TYR A 143 2046 1676 1915 -87 -46 -36 C ATOM 1009 C TYR A 143 32.289 17.202 33.073 1.00 13.90 C ANISOU 1009 C TYR A 143 1948 1521 1811 -91 -13 -27 C ATOM 1010 O TYR A 143 32.943 17.979 32.359 1.00 14.45 O ANISOU 1010 O TYR A 143 2155 1534 1800 -119 32 35 O ATOM 1011 CB TYR A 143 29.964 17.742 33.597 1.00 15.16 C ANISOU 1011 CB TYR A 143 2038 1698 2023 -17 -36 -18 C ATOM 1012 CG TYR A 143 28.911 18.390 34.458 1.00 15.03 C ANISOU 1012 CG TYR A 143 1991 1768 1949 -53 -44 -37 C ATOM 1013 CD1 TYR A 143 28.464 17.776 35.623 1.00 15.10 C ANISOU 1013 CD1 TYR A 143 1933 1945 1857 -31 -32 -68 C ATOM 1014 CD2 TYR A 143 28.326 19.602 34.076 1.00 16.51 C ANISOU 1014 CD2 TYR A 143 2186 1930 2156 -36 -121 -59 C ATOM 1015 CE1 TYR A 143 27.472 18.353 36.412 1.00 16.39 C ANISOU 1015 CE1 TYR A 143 2119 2121 1985 33 -8 -68 C ATOM 1016 CE2 TYR A 143 27.330 20.191 34.855 1.00 16.00 C ANISOU 1016 CE2 TYR A 143 2138 1931 2010 -46 -6 21 C ATOM 1017 CZ TYR A 143 26.912 19.558 36.029 1.00 15.43 C ANISOU 1017 CZ TYR A 143 2037 1916 1909 -22 47 -76 C ATOM 1018 OH TYR A 143 25.922 20.119 36.805 1.00 19.00 O ANISOU 1018 OH TYR A 143 2394 2471 2352 170 60 -128 O ATOM 1019 N SER A 144 32.305 15.888 32.902 1.00 13.12 N ANISOU 1019 N SER A 144 1821 1443 1718 -81 -15 19 N ATOM 1020 CA SER A 144 32.770 15.314 31.650 1.00 12.45 C ANISOU 1020 CA SER A 144 1729 1375 1624 -109 -50 -17 C ATOM 1021 C SER A 144 32.001 14.030 31.409 1.00 12.08 C ANISOU 1021 C SER A 144 1648 1377 1564 -148 -34 16 C ATOM 1022 O SER A 144 31.430 13.451 32.348 1.00 12.09 O ANISOU 1022 O SER A 144 1708 1417 1465 -72 -122 72 O ATOM 1023 CB SER A 144 34.263 15.000 31.681 1.00 13.10 C ANISOU 1023 CB SER A 144 1760 1508 1709 -132 -63 -4 C ATOM 1024 OG SER A 144 34.554 14.033 32.670 1.00 12.99 O ANISOU 1024 OG SER A 144 1850 1390 1694 -199 -159 78 O ATOM 1025 N MET A 145 31.964 13.609 30.148 1.00 11.59 N ANISOU 1025 N MET A 145 1575 1288 1540 -77 11 15 N ATOM 1026 CA MET A 145 31.445 12.280 29.822 1.00 11.00 C ANISOU 1026 CA MET A 145 1458 1213 1506 -24 -3 39 C ATOM 1027 C MET A 145 32.629 11.331 29.821 1.00 10.63 C ANISOU 1027 C MET A 145 1410 1208 1420 -51 -26 111 C ATOM 1028 O MET A 145 33.626 11.568 29.114 1.00 11.78 O ANISOU 1028 O MET A 145 1443 1337 1694 8 -18 157 O ATOM 1029 CB MET A 145 30.763 12.266 28.459 1.00 11.10 C ANISOU 1029 CB MET A 145 1474 1215 1528 45 -9 107 C ATOM 1030 CG MET A 145 29.621 13.299 28.277 1.00 11.63 C ANISOU 1030 CG MET A 145 1412 1364 1643 168 49 116 C ATOM 1031 SD MET A 145 28.386 13.290 29.608 1.00 12.37 S ANISOU 1031 SD MET A 145 1629 1561 1510 -131 -17 256 S ATOM 1032 CE MET A 145 27.810 11.580 29.534 1.00 12.42 C ANISOU 1032 CE MET A 145 1583 1360 1773 17 -13 84 C ATOM 1033 N PRO A 146 32.530 10.240 30.598 1.00 10.60 N ANISOU 1033 N PRO A 146 1339 1295 1392 -52 -47 154 N ATOM 1034 CA PRO A 146 33.670 9.355 30.778 1.00 10.38 C ANISOU 1034 CA PRO A 146 1404 1200 1339 -24 -10 165 C ATOM 1035 C PRO A 146 33.996 8.538 29.537 1.00 10.52 C ANISOU 1035 C PRO A 146 1405 1287 1301 -11 -6 190 C ATOM 1036 O PRO A 146 33.101 8.157 28.773 1.00 10.25 O ANISOU 1036 O PRO A 146 1407 1246 1241 79 -55 174 O ATOM 1037 CB PRO A 146 33.220 8.426 31.903 1.00 10.65 C ANISOU 1037 CB PRO A 146 1376 1340 1330 -53 13 190 C ATOM 1038 CG PRO A 146 31.718 8.362 31.762 1.00 9.65 C ANISOU 1038 CG PRO A 146 1256 1094 1317 2 -52 185 C ATOM 1039 CD PRO A 146 31.339 9.791 31.342 1.00 10.24 C ANISOU 1039 CD PRO A 146 1337 1181 1371 -81 -25 227 C ATOM 1040 N VAL A 147 35.287 8.272 29.369 1.00 10.39 N ANISOU 1040 N VAL A 147 1367 1293 1288 -51 42 200 N ATOM 1041 CA VAL A 147 35.766 7.358 28.358 1.00 11.06 C ANISOU 1041 CA VAL A 147 1428 1361 1412 -56 13 161 C ATOM 1042 C VAL A 147 35.556 5.930 28.862 1.00 10.84 C ANISOU 1042 C VAL A 147 1411 1316 1390 -72 -18 125 C ATOM 1043 O VAL A 147 36.163 5.527 29.879 1.00 11.25 O ANISOU 1043 O VAL A 147 1472 1387 1413 -81 5 93 O ATOM 1044 CB VAL A 147 37.251 7.611 28.049 1.00 11.17 C ANISOU 1044 CB VAL A 147 1420 1353 1470 -35 16 169 C ATOM 1045 CG1 VAL A 147 37.784 6.520 27.135 1.00 12.17 C ANISOU 1045 CG1 VAL A 147 1600 1545 1478 -58 193 100 C ATOM 1046 CG2 VAL A 147 37.432 9.007 27.421 1.00 13.02 C ANISOU 1046 CG2 VAL A 147 1677 1590 1678 -199 69 218 C ATOM 1047 N PRO A 148 34.681 5.166 28.177 1.00 10.83 N ANISOU 1047 N PRO A 148 1363 1365 1387 -78 -91 170 N ATOM 1048 CA PRO A 148 34.400 3.787 28.633 1.00 10.48 C ANISOU 1048 CA PRO A 148 1318 1314 1349 -26 -72 146 C ATOM 1049 C PRO A 148 35.497 2.789 28.267 1.00 11.14 C ANISOU 1049 C PRO A 148 1392 1467 1374 -3 -10 125 C ATOM 1050 O PRO A 148 36.018 2.819 27.155 1.00 11.70 O ANISOU 1050 O PRO A 148 1536 1502 1405 101 92 147 O ATOM 1051 CB PRO A 148 33.103 3.426 27.898 1.00 10.82 C ANISOU 1051 CB PRO A 148 1313 1454 1344 -110 -51 192 C ATOM 1052 CG PRO A 148 33.109 4.307 26.661 1.00 12.12 C ANISOU 1052 CG PRO A 148 1672 1397 1536 -60 -146 146 C ATOM 1053 CD PRO A 148 33.882 5.545 26.990 1.00 10.56 C ANISOU 1053 CD PRO A 148 1329 1390 1291 -135 -26 116 C ATOM 1054 N MET A 149 35.842 1.910 29.203 1.00 10.47 N ANISOU 1054 N MET A 149 1260 1445 1270 38 -32 131 N ATOM 1055 CA MET A 149 36.601 0.707 28.852 1.00 10.64 C ANISOU 1055 CA MET A 149 1269 1511 1260 -44 -70 106 C ATOM 1056 C MET A 149 35.592 -0.430 28.895 1.00 10.83 C ANISOU 1056 C MET A 149 1305 1511 1299 -8 -12 83 C ATOM 1057 O MET A 149 34.992 -0.687 29.944 1.00 10.78 O ANISOU 1057 O MET A 149 1385 1510 1201 -42 41 32 O ATOM 1058 CB MET A 149 37.814 0.487 29.783 1.00 10.37 C ANISOU 1058 CB MET A 149 1267 1567 1106 51 -71 36 C ATOM 1059 CG MET A 149 37.533 0.511 31.275 1.00 10.74 C ANISOU 1059 CG MET A 149 1262 1566 1249 -45 -26 101 C ATOM 1060 SD MET A 149 39.014 0.084 32.224 1.00 12.03 S ANISOU 1060 SD MET A 149 1402 1789 1379 -230 -205 272 S ATOM 1061 CE MET A 149 40.087 1.491 31.953 1.00 12.05 C ANISOU 1061 CE MET A 149 1386 1654 1539 -95 99 -13 C ATOM 1062 N MET A 150 35.395 -1.074 27.746 1.00 10.68 N ANISOU 1062 N MET A 150 1260 1441 1355 3 46 10 N ATOM 1063 CA MET A 150 34.265 -1.975 27.527 1.00 12.60 C ANISOU 1063 CA MET A 150 1638 1644 1505 -11 -40 24 C ATOM 1064 C MET A 150 34.727 -3.406 27.448 1.00 12.08 C ANISOU 1064 C MET A 150 1600 1561 1426 -78 7 31 C ATOM 1065 O MET A 150 35.475 -3.767 26.543 1.00 12.42 O ANISOU 1065 O MET A 150 1650 1602 1466 -90 95 106 O ATOM 1066 CB MET A 150 33.568 -1.629 26.214 1.00 12.99 C ANISOU 1066 CB MET A 150 1711 1682 1542 23 -38 38 C ATOM 1067 CG MET A 150 33.031 -0.238 26.151 1.00 13.56 C ANISOU 1067 CG MET A 150 1754 1780 1617 -7 -146 73 C ATOM 1068 SD MET A 150 32.333 0.042 24.531 1.00 16.28 S ANISOU 1068 SD MET A 150 2277 2228 1678 147 -133 40 S ATOM 1069 CE MET A 150 31.673 1.683 24.786 1.00 15.55 C ANISOU 1069 CE MET A 150 2165 1943 1797 119 -95 104 C ATOM 1070 N ASN A 151 34.272 -4.228 28.394 1.00 11.59 N ANISOU 1070 N ASN A 151 1480 1551 1373 -149 -16 38 N ATOM 1071 CA ASN A 151 34.559 -5.649 28.366 1.00 12.09 C ANISOU 1071 CA ASN A 151 1564 1622 1405 -58 20 24 C ATOM 1072 C ASN A 151 34.301 -6.191 26.972 1.00 11.70 C ANISOU 1072 C ASN A 151 1523 1563 1357 -60 53 37 C ATOM 1073 O ASN A 151 33.290 -5.845 26.350 1.00 11.90 O ANISOU 1073 O ASN A 151 1732 1580 1208 53 98 141 O ATOM 1074 CB ASN A 151 33.651 -6.379 29.364 1.00 12.41 C ANISOU 1074 CB ASN A 151 1645 1615 1453 -88 61 30 C ATOM 1075 CG ASN A 151 33.936 -7.853 29.438 1.00 14.64 C ANISOU 1075 CG ASN A 151 1932 1909 1718 -54 44 60 C ATOM 1076 OD1 ASN A 151 34.810 -8.300 30.198 1.00 19.56 O ANISOU 1076 OD1 ASN A 151 2500 2606 2325 129 -213 148 O ATOM 1077 ND2 ASN A 151 33.226 -8.620 28.640 1.00 11.70 N ANISOU 1077 ND2 ASN A 151 1707 1368 1370 -36 137 52 N ATOM 1078 N ILE A 152 35.181 -7.068 26.501 1.00 11.81 N ANISOU 1078 N ILE A 152 1580 1537 1367 -45 71 17 N ATOM 1079 CA ILE A 152 34.998 -7.680 25.184 1.00 12.98 C ANISOU 1079 CA ILE A 152 1837 1603 1492 -27 50 16 C ATOM 1080 C ILE A 152 35.353 -9.186 25.144 1.00 12.35 C ANISOU 1080 C ILE A 152 1688 1589 1414 25 67 33 C ATOM 1081 O ILE A 152 34.625 -9.979 24.559 1.00 12.11 O ANISOU 1081 O ILE A 152 1727 1550 1320 107 99 55 O ATOM 1082 CB ILE A 152 35.727 -6.833 24.074 1.00 13.89 C ANISOU 1082 CB ILE A 152 1890 1722 1662 -52 70 3 C ATOM 1083 CG1 ILE A 152 35.265 -7.239 22.683 1.00 16.87 C ANISOU 1083 CG1 ILE A 152 2262 2235 1910 -46 -39 -95 C ATOM 1084 CG2 ILE A 152 37.233 -6.886 24.209 1.00 15.37 C ANISOU 1084 CG2 ILE A 152 1971 1924 1944 -10 85 -87 C ATOM 1085 CD1 ILE A 152 33.902 -6.687 22.308 1.00 19.86 C ANISOU 1085 CD1 ILE A 152 2412 2675 2459 85 -144 -171 C ATOM 1086 N ILE A 153 36.444 -9.565 25.805 1.00 12.10 N ANISOU 1086 N ILE A 153 1717 1516 1365 74 64 118 N ATOM 1087 CA ILE A 153 36.878 -10.963 25.866 1.00 12.24 C ANISOU 1087 CA ILE A 153 1724 1544 1382 68 4 84 C ATOM 1088 C ILE A 153 37.251 -11.287 27.307 1.00 12.81 C ANISOU 1088 C ILE A 153 1736 1625 1503 48 -8 60 C ATOM 1089 O ILE A 153 37.993 -10.544 27.952 1.00 13.33 O ANISOU 1089 O ILE A 153 1845 1664 1555 -91 -41 43 O ATOM 1090 CB ILE A 153 38.099 -11.253 24.944 1.00 12.10 C ANISOU 1090 CB ILE A 153 1680 1505 1410 73 11 95 C ATOM 1091 CG1 ILE A 153 37.709 -11.174 23.455 1.00 13.12 C ANISOU 1091 CG1 ILE A 153 1840 1592 1552 0 -8 93 C ATOM 1092 CG2 ILE A 153 38.727 -12.615 25.268 1.00 11.93 C ANISOU 1092 CG2 ILE A 153 1684 1534 1312 36 29 106 C ATOM 1093 CD1 ILE A 153 36.799 -12.284 22.945 1.00 14.64 C ANISOU 1093 CD1 ILE A 153 1952 1836 1774 17 -231 -61 C ATOM 1094 N ASN A 154 36.764 -12.425 27.781 1.00 12.98 N ANISOU 1094 N ASN A 154 1685 1691 1553 -9 -2 130 N ATOM 1095 CA ASN A 154 37.047 -12.872 29.134 1.00 13.76 C ANISOU 1095 CA ASN A 154 1767 1789 1670 3 29 88 C ATOM 1096 C ASN A 154 37.924 -14.104 29.187 1.00 13.57 C ANISOU 1096 C ASN A 154 1831 1689 1633 -8 4 79 C ATOM 1097 O ASN A 154 37.887 -14.947 28.285 1.00 13.50 O ANISOU 1097 O ASN A 154 1896 1655 1575 0 81 61 O ATOM 1098 CB ASN A 154 35.720 -13.083 29.838 1.00 14.20 C ANISOU 1098 CB ASN A 154 1869 1820 1705 0 81 87 C ATOM 1099 CG ASN A 154 34.972 -11.793 29.943 1.00 16.70 C ANISOU 1099 CG ASN A 154 2051 2133 2159 55 94 -67 C ATOM 1100 OD1 ASN A 154 34.083 -11.457 29.111 1.00 19.91 O ANISOU 1100 OD1 ASN A 154 2532 2540 2490 99 107 70 O ATOM 1101 ND2 ASN A 154 35.402 -10.993 30.894 1.00 14.32 N ANISOU 1101 ND2 ASN A 154 1856 1839 1746 -47 -2 -14 N ATOM 1102 N GLY A 155 38.729 -14.190 30.242 1.00 14.11 N ANISOU 1102 N GLY A 155 1948 1759 1652 -3 0 74 N ATOM 1103 CA GLY A 155 39.579 -15.343 30.462 1.00 14.58 C ANISOU 1103 CA GLY A 155 2049 1796 1694 12 -66 136 C ATOM 1104 C GLY A 155 39.772 -15.613 31.943 1.00 15.67 C ANISOU 1104 C GLY A 155 2158 1977 1819 -1 -29 150 C ATOM 1105 O GLY A 155 38.980 -15.168 32.767 1.00 14.89 O ANISOU 1105 O GLY A 155 2169 1829 1657 -53 -53 221 O ATOM 1106 N GLY A 156 40.824 -16.360 32.265 1.00 17.20 N ANISOU 1106 N GLY A 156 2324 2148 2060 -26 -78 179 N ATOM 1107 CA GLY A 156 41.133 -16.709 33.656 1.00 18.05 C ANISOU 1107 CA GLY A 156 2383 2287 2185 -24 -82 177 C ATOM 1108 C GLY A 156 39.929 -17.287 34.376 1.00 18.57 C ANISOU 1108 C GLY A 156 2427 2345 2283 -4 -69 153 C ATOM 1109 O GLY A 156 39.220 -18.133 33.824 1.00 18.54 O ANISOU 1109 O GLY A 156 2494 2274 2273 -64 -82 142 O ATOM 1110 N GLU A 157 39.687 -16.816 35.600 1.00 18.97 N ANISOU 1110 N GLU A 157 2477 2360 2370 17 -63 118 N ATOM 1111 CA GLU A 157 38.559 -17.297 36.402 1.00 19.90 C ANISOU 1111 CA GLU A 157 2562 2517 2481 -6 -38 97 C ATOM 1112 C GLU A 157 37.189 -16.903 35.835 1.00 19.92 C ANISOU 1112 C GLU A 157 2569 2505 2493 -22 -30 121 C ATOM 1113 O GLU A 157 36.160 -17.428 36.273 1.00 20.66 O ANISOU 1113 O GLU A 157 2648 2628 2572 -20 -2 177 O ATOM 1114 CB GLU A 157 38.686 -16.833 37.860 1.00 20.27 C ANISOU 1114 CB GLU A 157 2647 2549 2505 -37 -29 108 C ATOM 1115 CG GLU A 157 39.893 -17.421 38.578 1.00 23.20 C ANISOU 1115 CG GLU A 157 2902 3035 2878 15 -59 98 C ATOM 1116 CD GLU A 157 39.786 -18.920 38.711 1.00 27.25 C ANISOU 1116 CD GLU A 157 3510 3371 3470 19 -8 119 C ATOM 1117 OE1 GLU A 157 38.797 -19.395 39.307 1.00 31.08 O ANISOU 1117 OE1 GLU A 157 3961 3970 3875 -63 23 148 O ATOM 1118 OE2 GLU A 157 40.677 -19.623 38.202 1.00 30.11 O ANISOU 1118 OE2 GLU A 157 3997 3637 3804 130 31 104 O ATOM 1119 N HIS A 158 37.182 -16.007 34.847 1.00 19.06 N ANISOU 1119 N HIS A 158 2551 2367 2323 3 -68 63 N ATOM 1120 CA HIS A 158 35.923 -15.570 34.251 1.00 19.20 C ANISOU 1120 CA HIS A 158 2542 2349 2404 19 1 64 C ATOM 1121 C HIS A 158 35.598 -16.276 32.932 1.00 18.99 C ANISOU 1121 C HIS A 158 2511 2317 2387 6 -10 45 C ATOM 1122 O HIS A 158 34.754 -15.812 32.161 1.00 18.72 O ANISOU 1122 O HIS A 158 2560 2235 2315 22 -18 63 O ATOM 1123 CB HIS A 158 35.905 -14.041 34.122 1.00 18.69 C ANISOU 1123 CB HIS A 158 2461 2328 2309 -1 2 42 C ATOM 1124 CG HIS A 158 35.807 -13.338 35.441 1.00 19.95 C ANISOU 1124 CG HIS A 158 2579 2512 2485 -10 4 -5 C ATOM 1125 ND1 HIS A 158 35.660 -11.975 35.551 1.00 19.79 N ANISOU 1125 ND1 HIS A 158 2568 2478 2472 -89 50 -47 N ATOM 1126 CD2 HIS A 158 35.805 -13.822 36.708 1.00 19.40 C ANISOU 1126 CD2 HIS A 158 2544 2467 2358 -35 40 -23 C ATOM 1127 CE1 HIS A 158 35.593 -11.643 36.828 1.00 20.62 C ANISOU 1127 CE1 HIS A 158 2667 2621 2546 -76 61 -4 C ATOM 1128 NE2 HIS A 158 35.679 -12.745 37.552 1.00 20.60 N ANISOU 1128 NE2 HIS A 158 2720 2586 2518 4 21 -49 N ATOM 1129 N ALA A 159 36.260 -17.406 32.677 1.00 19.13 N ANISOU 1129 N ALA A 159 2582 2296 2389 6 -26 45 N ATOM 1130 CA ALA A 159 36.008 -18.188 31.469 1.00 19.64 C ANISOU 1130 CA ALA A 159 2668 2334 2460 -11 -34 45 C ATOM 1131 C ALA A 159 36.420 -19.643 31.681 1.00 20.36 C ANISOU 1131 C ALA A 159 2776 2399 2560 -15 -40 53 C ATOM 1132 O ALA A 159 36.910 -20.007 32.755 1.00 20.35 O ANISOU 1132 O ALA A 159 2795 2386 2548 -39 -75 70 O ATOM 1133 CB ALA A 159 36.770 -17.596 30.276 1.00 19.15 C ANISOU 1133 CB ALA A 159 2568 2294 2413 -5 2 18 C ATOM 1134 N ASP A 160 36.234 -20.458 30.646 1.00 20.93 N ANISOU 1134 N ASP A 160 2822 2461 2668 -46 -55 33 N ATOM 1135 CA ASP A 160 36.746 -21.822 30.622 1.00 22.16 C ANISOU 1135 CA ASP A 160 2941 2633 2843 -6 -35 26 C ATOM 1136 C ASP A 160 37.541 -22.023 29.335 1.00 22.03 C ANISOU 1136 C ASP A 160 2946 2616 2807 1 -51 5 C ATOM 1137 O ASP A 160 37.229 -22.898 28.524 1.00 23.29 O ANISOU 1137 O ASP A 160 3142 2782 2923 -16 -40 -33 O ATOM 1138 CB ASP A 160 35.597 -22.831 30.750 1.00 22.59 C ANISOU 1138 CB ASP A 160 3019 2640 2924 -31 -6 28 C ATOM 1139 CG ASP A 160 36.086 -24.273 30.882 1.00 24.61 C ANISOU 1139 CG ASP A 160 3271 2877 3201 -12 1 62 C ATOM 1140 OD1 ASP A 160 37.258 -24.502 31.256 1.00 27.62 O ANISOU 1140 OD1 ASP A 160 3687 3167 3639 17 -18 82 O ATOM 1141 OD2 ASP A 160 35.284 -25.179 30.589 1.00 28.28 O ANISOU 1141 OD2 ASP A 160 3822 3306 3617 -173 91 -42 O ATOM 1142 N ASN A 161 38.563 -21.185 29.159 1.00 21.57 N ANISOU 1142 N ASN A 161 2907 2546 2741 34 -46 22 N ATOM 1143 CA ASN A 161 39.455 -21.219 28.000 1.00 20.97 C ANISOU 1143 CA ASN A 161 2828 2472 2666 44 -74 65 C ATOM 1144 C ASN A 161 40.916 -21.246 28.456 1.00 21.47 C ANISOU 1144 C ASN A 161 2874 2554 2727 51 -55 24 C ATOM 1145 O ASN A 161 41.186 -21.453 29.645 1.00 21.49 O ANISOU 1145 O ASN A 161 2929 2537 2696 119 -76 10 O ATOM 1146 CB ASN A 161 39.176 -20.024 27.065 1.00 20.13 C ANISOU 1146 CB ASN A 161 2796 2341 2511 25 -101 21 C ATOM 1147 CG ASN A 161 39.248 -18.682 27.777 1.00 18.54 C ANISOU 1147 CG ASN A 161 2530 2193 2319 48 -141 90 C ATOM 1148 OD1 ASN A 161 40.008 -18.506 28.734 1.00 17.38 O ANISOU 1148 OD1 ASN A 161 2393 1934 2273 110 -198 -27 O ATOM 1149 ND2 ASN A 161 38.454 -17.725 27.307 1.00 16.46 N ANISOU 1149 ND2 ASN A 161 2238 1877 2136 11 -157 -15 N ATOM 1150 N ASN A 162 41.854 -21.066 27.528 1.00 21.91 N ANISOU 1150 N ASN A 162 2898 2602 2821 62 -33 7 N ATOM 1151 CA ASN A 162 43.275 -21.049 27.888 1.00 22.82 C ANISOU 1151 CA ASN A 162 2970 2788 2910 58 5 9 C ATOM 1152 C ASN A 162 43.882 -19.646 27.892 1.00 21.94 C ANISOU 1152 C ASN A 162 2812 2709 2813 65 -13 -14 C ATOM 1153 O ASN A 162 45.085 -19.467 27.677 1.00 22.44 O ANISOU 1153 O ASN A 162 2876 2806 2842 57 21 -5 O ATOM 1154 CB ASN A 162 44.080 -22.010 27.001 1.00 24.23 C ANISOU 1154 CB ASN A 162 3143 2989 3071 87 25 -37 C ATOM 1155 CG ASN A 162 43.819 -23.482 27.330 1.00 27.07 C ANISOU 1155 CG ASN A 162 3559 3282 3444 5 42 22 C ATOM 1156 OD1 ASN A 162 43.989 -24.354 26.472 1.00 32.11 O ANISOU 1156 OD1 ASN A 162 4290 3938 3972 63 116 -112 O ATOM 1157 ND2 ASN A 162 43.406 -23.766 28.570 1.00 28.77 N ANISOU 1157 ND2 ASN A 162 3792 3635 3504 66 81 -26 N ATOM 1158 N VAL A 163 43.032 -18.651 28.133 1.00 20.82 N ANISOU 1158 N VAL A 163 2684 2559 2666 65 -23 22 N ATOM 1159 CA VAL A 163 43.466 -17.273 28.306 1.00 19.86 C ANISOU 1159 CA VAL A 163 2581 2434 2529 66 -30 45 C ATOM 1160 C VAL A 163 43.668 -17.028 29.807 1.00 19.97 C ANISOU 1160 C VAL A 163 2605 2428 2555 59 -59 52 C ATOM 1161 O VAL A 163 42.764 -17.285 30.600 1.00 20.26 O ANISOU 1161 O VAL A 163 2716 2499 2483 34 -47 88 O ATOM 1162 CB VAL A 163 42.400 -16.293 27.730 1.00 19.22 C ANISOU 1162 CB VAL A 163 2481 2364 2455 55 -55 52 C ATOM 1163 CG1 VAL A 163 42.794 -14.831 27.981 1.00 18.92 C ANISOU 1163 CG1 VAL A 163 2478 2324 2386 32 -24 54 C ATOM 1164 CG2 VAL A 163 42.162 -16.572 26.240 1.00 19.43 C ANISOU 1164 CG2 VAL A 163 2548 2344 2490 70 -37 48 C ATOM 1165 N ASP A 164 44.855 -16.564 30.196 1.00 20.09 N ANISOU 1165 N ASP A 164 2661 2388 2582 0 -43 68 N ATOM 1166 CA ASP A 164 45.159 -16.313 31.618 1.00 20.35 C ANISOU 1166 CA ASP A 164 2645 2501 2584 -25 -35 65 C ATOM 1167 C ASP A 164 44.618 -14.974 32.127 1.00 19.93 C ANISOU 1167 C ASP A 164 2596 2483 2493 -35 -15 75 C ATOM 1168 O ASP A 164 44.145 -14.869 33.265 1.00 20.26 O ANISOU 1168 O ASP A 164 2659 2539 2497 -99 -8 144 O ATOM 1169 CB ASP A 164 46.664 -16.382 31.869 1.00 20.85 C ANISOU 1169 CB ASP A 164 2676 2581 2665 7 -12 49 C ATOM 1170 CG ASP A 164 47.264 -17.706 31.454 1.00 22.41 C ANISOU 1170 CG ASP A 164 2837 2802 2874 6 -70 -20 C ATOM 1171 OD1 ASP A 164 46.799 -18.769 31.922 1.00 25.48 O ANISOU 1171 OD1 ASP A 164 3276 3046 3357 102 10 119 O ATOM 1172 OD2 ASP A 164 48.207 -17.676 30.654 1.00 26.02 O ANISOU 1172 OD2 ASP A 164 3281 3356 3249 -19 102 -43 O ATOM 1173 N ILE A 165 44.715 -13.945 31.283 1.00 19.20 N ANISOU 1173 N ILE A 165 2524 2391 2381 -33 -42 88 N ATOM 1174 CA ILE A 165 44.226 -12.610 31.607 1.00 18.40 C ANISOU 1174 CA ILE A 165 2390 2306 2294 -22 -11 106 C ATOM 1175 C ILE A 165 42.710 -12.645 31.818 1.00 17.61 C ANISOU 1175 C ILE A 165 2311 2213 2166 -26 -11 104 C ATOM 1176 O ILE A 165 41.984 -13.244 31.016 1.00 17.33 O ANISOU 1176 O ILE A 165 2332 2196 2055 -30 42 23 O ATOM 1177 CB ILE A 165 44.618 -11.592 30.493 1.00 18.72 C ANISOU 1177 CB ILE A 165 2436 2336 2338 7 15 91 C ATOM 1178 CG1 ILE A 165 46.145 -11.530 30.326 1.00 20.50 C ANISOU 1178 CG1 ILE A 165 2621 2575 2590 29 41 79 C ATOM 1179 CG2 ILE A 165 44.008 -10.208 30.763 1.00 17.78 C ANISOU 1179 CG2 ILE A 165 2319 2116 2319 -62 -14 -4 C ATOM 1180 CD1 ILE A 165 46.908 -11.208 31.579 1.00 23.71 C ANISOU 1180 CD1 ILE A 165 2973 3154 2881 -66 -16 16 C ATOM 1181 N GLN A 166 42.235 -12.030 32.901 1.00 16.23 N ANISOU 1181 N GLN A 166 2170 2044 1950 -61 -34 157 N ATOM 1182 CA GLN A 166 40.809 -12.102 33.253 1.00 16.30 C ANISOU 1182 CA GLN A 166 2186 2096 1910 -75 -2 145 C ATOM 1183 C GLN A 166 39.902 -11.394 32.249 1.00 15.55 C ANISOU 1183 C GLN A 166 2072 1985 1849 -108 -8 166 C ATOM 1184 O GLN A 166 38.846 -11.904 31.886 1.00 16.30 O ANISOU 1184 O GLN A 166 2224 2103 1867 -172 20 150 O ATOM 1185 CB GLN A 166 40.551 -11.538 34.645 1.00 15.95 C ANISOU 1185 CB GLN A 166 2140 2016 1902 -62 0 97 C ATOM 1186 CG GLN A 166 39.156 -11.860 35.170 1.00 17.13 C ANISOU 1186 CG GLN A 166 2324 2228 1954 -140 87 87 C ATOM 1187 CD GLN A 166 39.090 -11.777 36.687 1.00 17.52 C ANISOU 1187 CD GLN A 166 2391 2267 1996 -30 -27 48 C ATOM 1188 OE1 GLN A 166 39.383 -12.752 37.386 1.00 19.50 O ANISOU 1188 OE1 GLN A 166 2702 2499 2207 -101 96 210 O ATOM 1189 NE2 GLN A 166 38.713 -10.611 37.202 1.00 17.24 N ANISOU 1189 NE2 GLN A 166 2395 2105 2050 -63 13 43 N ATOM 1190 N GLU A 167 40.282 -10.194 31.821 1.00 15.13 N ANISOU 1190 N GLU A 167 2021 1902 1823 -160 7 127 N ATOM 1191 CA GLU A 167 39.504 -9.562 30.763 1.00 14.71 C ANISOU 1191 CA GLU A 167 1947 1893 1747 -65 41 141 C ATOM 1192 C GLU A 167 40.293 -8.595 29.916 1.00 13.47 C ANISOU 1192 C GLU A 167 1820 1709 1589 -88 53 131 C ATOM 1193 O GLU A 167 41.255 -7.970 30.376 1.00 13.58 O ANISOU 1193 O GLU A 167 1899 1849 1411 -10 -40 150 O ATOM 1194 CB GLU A 167 38.232 -8.881 31.281 1.00 15.74 C ANISOU 1194 CB GLU A 167 2111 1988 1879 -80 122 137 C ATOM 1195 CG GLU A 167 38.485 -7.690 32.179 1.00 16.33 C ANISOU 1195 CG GLU A 167 2087 2089 2029 4 77 -23 C ATOM 1196 CD GLU A 167 37.212 -6.944 32.556 1.00 17.36 C ANISOU 1196 CD GLU A 167 2111 2386 2099 62 44 25 C ATOM 1197 OE1 GLU A 167 36.473 -6.502 31.652 1.00 19.24 O ANISOU 1197 OE1 GLU A 167 2591 2557 2159 87 -51 2 O ATOM 1198 OE2 GLU A 167 36.963 -6.792 33.766 1.00 18.85 O ANISOU 1198 OE2 GLU A 167 2139 2827 2194 246 225 -60 O ATOM 1199 N PHE A 168 39.857 -8.497 28.665 1.00 13.12 N ANISOU 1199 N PHE A 168 1746 1615 1621 -5 44 178 N ATOM 1200 CA PHE A 168 40.356 -7.502 27.736 1.00 13.03 C ANISOU 1200 CA PHE A 168 1698 1591 1659 27 34 191 C ATOM 1201 C PHE A 168 39.183 -6.585 27.408 1.00 12.84 C ANISOU 1201 C PHE A 168 1610 1581 1688 2 25 179 C ATOM 1202 O PHE A 168 38.034 -7.036 27.312 1.00 12.86 O ANISOU 1202 O PHE A 168 1565 1566 1754 25 -27 232 O ATOM 1203 CB PHE A 168 40.840 -8.173 26.456 1.00 13.82 C ANISOU 1203 CB PHE A 168 1788 1714 1747 57 57 143 C ATOM 1204 CG PHE A 168 42.035 -9.063 26.652 1.00 15.65 C ANISOU 1204 CG PHE A 168 2022 1963 1962 126 -3 144 C ATOM 1205 CD1 PHE A 168 43.323 -8.561 26.525 1.00 17.70 C ANISOU 1205 CD1 PHE A 168 2166 2359 2201 246 20 155 C ATOM 1206 CD2 PHE A 168 41.861 -10.400 26.965 1.00 16.42 C ANISOU 1206 CD2 PHE A 168 2323 1986 1928 209 -59 62 C ATOM 1207 CE1 PHE A 168 44.442 -9.404 26.708 1.00 17.75 C ANISOU 1207 CE1 PHE A 168 2210 2464 2068 256 51 57 C ATOM 1208 CE2 PHE A 168 42.973 -11.234 27.152 1.00 18.13 C ANISOU 1208 CE2 PHE A 168 2287 2366 2234 214 -35 -20 C ATOM 1209 CZ PHE A 168 44.246 -10.728 27.023 1.00 17.37 C ANISOU 1209 CZ PHE A 168 2150 2320 2127 258 34 -22 C ATOM 1210 N MET A 169 39.491 -5.303 27.240 1.00 12.23 N ANISOU 1210 N MET A 169 1579 1494 1573 -2 55 181 N ATOM 1211 CA MET A 169 38.486 -4.278 27.027 1.00 11.60 C ANISOU 1211 CA MET A 169 1512 1451 1445 -69 25 207 C ATOM 1212 C MET A 169 38.904 -3.386 25.889 1.00 11.86 C ANISOU 1212 C MET A 169 1515 1525 1465 -59 -8 177 C ATOM 1213 O MET A 169 40.094 -3.237 25.638 1.00 12.02 O ANISOU 1213 O MET A 169 1481 1569 1515 -157 -9 287 O ATOM 1214 CB MET A 169 38.360 -3.412 28.279 1.00 11.67 C ANISOU 1214 CB MET A 169 1590 1485 1356 -64 78 212 C ATOM 1215 CG MET A 169 37.795 -4.153 29.492 1.00 11.02 C ANISOU 1215 CG MET A 169 1477 1383 1325 -102 109 259 C ATOM 1216 SD MET A 169 37.982 -3.179 30.991 1.00 12.58 S ANISOU 1216 SD MET A 169 1671 1642 1467 -147 -50 191 S ATOM 1217 CE MET A 169 39.618 -3.724 31.503 1.00 13.16 C ANISOU 1217 CE MET A 169 1456 1995 1546 -199 132 190 C ATOM 1218 N ILE A 170 37.918 -2.804 25.210 1.00 11.77 N ANISOU 1218 N ILE A 170 1502 1518 1452 -72 -50 127 N ATOM 1219 CA ILE A 170 38.186 -1.752 24.223 1.00 11.95 C ANISOU 1219 CA ILE A 170 1549 1581 1409 -57 -26 85 C ATOM 1220 C ILE A 170 37.822 -0.371 24.756 1.00 12.52 C ANISOU 1220 C ILE A 170 1577 1666 1512 -74 20 84 C ATOM 1221 O ILE A 170 36.865 -0.225 25.518 1.00 11.77 O ANISOU 1221 O ILE A 170 1483 1592 1395 -75 119 34 O ATOM 1222 CB ILE A 170 37.440 -2.003 22.886 1.00 11.82 C ANISOU 1222 CB ILE A 170 1503 1595 1390 -37 -17 43 C ATOM 1223 CG1 ILE A 170 35.936 -2.215 23.111 1.00 12.64 C ANISOU 1223 CG1 ILE A 170 1489 1786 1527 19 -116 66 C ATOM 1224 CG2 ILE A 170 38.063 -3.191 22.139 1.00 12.67 C ANISOU 1224 CG2 ILE A 170 1743 1685 1385 -21 78 28 C ATOM 1225 CD1 ILE A 170 35.119 -2.255 21.806 1.00 13.20 C ANISOU 1225 CD1 ILE A 170 1674 1932 1411 -11 -48 -23 C ATOM 1226 N GLN A 171 38.584 0.646 24.335 1.00 12.12 N ANISOU 1226 N GLN A 171 1471 1602 1531 -151 -43 71 N ATOM 1227 CA GLN A 171 38.293 2.034 24.720 1.00 12.42 C ANISOU 1227 CA GLN A 171 1568 1660 1489 -67 -32 130 C ATOM 1228 C GLN A 171 38.201 2.855 23.452 1.00 12.82 C ANISOU 1228 C GLN A 171 1616 1737 1515 -90 39 158 C ATOM 1229 O GLN A 171 39.202 2.979 22.753 1.00 13.49 O ANISOU 1229 O GLN A 171 1640 1817 1666 -76 125 218 O ATOM 1230 CB GLN A 171 39.414 2.614 25.579 1.00 13.19 C ANISOU 1230 CB GLN A 171 1718 1804 1486 -79 -52 102 C ATOM 1231 CG GLN A 171 39.632 1.908 26.912 1.00 12.72 C ANISOU 1231 CG GLN A 171 1629 1797 1405 -3 -129 227 C ATOM 1232 CD GLN A 171 40.931 2.343 27.579 1.00 13.26 C ANISOU 1232 CD GLN A 171 1676 1787 1574 -60 -44 35 C ATOM 1233 OE1 GLN A 171 40.931 2.892 28.698 1.00 15.23 O ANISOU 1233 OE1 GLN A 171 2107 2126 1551 -183 -153 65 O ATOM 1234 NE2 GLN A 171 42.047 2.104 26.898 1.00 11.60 N ANISOU 1234 NE2 GLN A 171 1387 1766 1252 -141 -86 195 N ATOM 1235 N PRO A 172 37.007 3.381 23.135 1.00 12.97 N ANISOU 1235 N PRO A 172 1584 1819 1524 -75 64 202 N ATOM 1236 CA PRO A 172 36.826 4.228 21.943 1.00 13.07 C ANISOU 1236 CA PRO A 172 1626 1793 1547 -43 16 219 C ATOM 1237 C PRO A 172 37.363 5.641 22.163 1.00 13.51 C ANISOU 1237 C PRO A 172 1728 1803 1602 12 59 158 C ATOM 1238 O PRO A 172 36.605 6.618 22.226 1.00 13.59 O ANISOU 1238 O PRO A 172 1693 1844 1626 29 123 219 O ATOM 1239 CB PRO A 172 35.309 4.220 21.699 1.00 13.28 C ANISOU 1239 CB PRO A 172 1658 1811 1575 -44 81 218 C ATOM 1240 CG PRO A 172 34.710 3.390 22.782 1.00 15.01 C ANISOU 1240 CG PRO A 172 1809 2190 1701 -99 -1 325 C ATOM 1241 CD PRO A 172 35.735 3.151 23.845 1.00 12.86 C ANISOU 1241 CD PRO A 172 1477 1866 1540 -98 19 210 C ATOM 1242 N VAL A 173 38.678 5.744 22.276 1.00 13.32 N ANISOU 1242 N VAL A 173 1712 1782 1565 0 28 111 N ATOM 1243 CA VAL A 173 39.292 7.026 22.573 1.00 14.98 C ANISOU 1243 CA VAL A 173 1858 1927 1907 -16 67 173 C ATOM 1244 C VAL A 173 39.100 8.035 21.442 1.00 15.08 C ANISOU 1244 C VAL A 173 1847 1958 1923 27 80 173 C ATOM 1245 O VAL A 173 39.079 9.245 21.701 1.00 16.28 O ANISOU 1245 O VAL A 173 2078 1948 2158 -52 126 253 O ATOM 1246 CB VAL A 173 40.794 6.894 22.943 1.00 14.86 C ANISOU 1246 CB VAL A 173 1835 2002 1808 5 1 134 C ATOM 1247 CG1 VAL A 173 40.945 6.154 24.279 1.00 15.82 C ANISOU 1247 CG1 VAL A 173 2006 2074 1927 8 40 286 C ATOM 1248 CG2 VAL A 173 41.591 6.205 21.841 1.00 15.06 C ANISOU 1248 CG2 VAL A 173 1935 1889 1896 -81 106 90 C ATOM 1249 N GLY A 174 38.927 7.533 20.218 1.00 15.24 N ANISOU 1249 N GLY A 174 1861 1979 1948 7 115 280 N ATOM 1250 CA GLY A 174 38.811 8.380 19.024 1.00 15.81 C ANISOU 1250 CA GLY A 174 1926 2095 1983 38 127 293 C ATOM 1251 C GLY A 174 37.453 9.018 18.824 1.00 14.90 C ANISOU 1251 C GLY A 174 1876 1917 1869 33 154 272 C ATOM 1252 O GLY A 174 37.301 9.896 17.967 1.00 15.67 O ANISOU 1252 O GLY A 174 1976 2030 1948 60 174 355 O ATOM 1253 N ALA A 175 36.456 8.556 19.586 1.00 14.28 N ANISOU 1253 N ALA A 175 1837 1805 1781 -11 170 238 N ATOM 1254 CA ALA A 175 35.129 9.160 19.581 1.00 13.95 C ANISOU 1254 CA ALA A 175 1776 1771 1753 -102 206 233 C ATOM 1255 C ALA A 175 35.178 10.614 20.024 1.00 13.52 C ANISOU 1255 C ALA A 175 1769 1682 1684 -126 189 297 C ATOM 1256 O ALA A 175 36.034 10.993 20.822 1.00 13.61 O ANISOU 1256 O ALA A 175 1793 1596 1782 -142 181 404 O ATOM 1257 CB ALA A 175 34.193 8.376 20.502 1.00 13.62 C ANISOU 1257 CB ALA A 175 1735 1771 1666 -132 203 260 C ATOM 1258 N LYS A 176 34.237 11.421 19.533 1.00 14.01 N ANISOU 1258 N LYS A 176 1785 1702 1834 -113 200 229 N ATOM 1259 CA LYS A 176 34.174 12.823 19.943 1.00 14.35 C ANISOU 1259 CA LYS A 176 1891 1724 1836 -35 148 182 C ATOM 1260 C LYS A 176 33.066 13.143 20.949 1.00 13.35 C ANISOU 1260 C LYS A 176 1764 1590 1717 -73 81 163 C ATOM 1261 O LYS A 176 33.032 14.245 21.508 1.00 13.85 O ANISOU 1261 O LYS A 176 1732 1610 1917 -94 74 201 O ATOM 1262 CB LYS A 176 34.092 13.745 18.715 1.00 15.60 C ANISOU 1262 CB LYS A 176 2101 1912 1911 -17 177 184 C ATOM 1263 CG LYS A 176 35.214 13.537 17.704 1.00 18.45 C ANISOU 1263 CG LYS A 176 2475 2289 2245 31 281 180 C ATOM 1264 CD LYS A 176 36.587 13.533 18.349 1.00 22.88 C ANISOU 1264 CD LYS A 176 2881 2964 2846 -4 61 101 C ATOM 1265 CE LYS A 176 37.009 14.894 18.884 1.00 26.40 C ANISOU 1265 CE LYS A 176 3441 3233 3355 -60 1 -35 C ATOM 1266 NZ LYS A 176 38.414 14.868 19.414 1.00 29.11 N ANISOU 1266 NZ LYS A 176 3541 3831 3688 -20 -68 11 N ATOM 1267 N THR A 177 32.187 12.162 21.189 1.00 12.71 N ANISOU 1267 N THR A 177 1652 1556 1621 -75 88 184 N ATOM 1268 CA THR A 177 31.121 12.250 22.184 1.00 12.04 C ANISOU 1268 CA THR A 177 1640 1372 1560 -82 63 226 C ATOM 1269 C THR A 177 30.943 10.848 22.767 1.00 11.79 C ANISOU 1269 C THR A 177 1658 1322 1499 -115 66 172 C ATOM 1270 O THR A 177 31.365 9.862 22.141 1.00 11.16 O ANISOU 1270 O THR A 177 1609 1125 1506 -141 149 345 O ATOM 1271 CB THR A 177 29.772 12.649 21.545 1.00 11.99 C ANISOU 1271 CB THR A 177 1692 1365 1496 -74 51 160 C ATOM 1272 OG1 THR A 177 29.410 11.683 20.539 1.00 11.45 O ANISOU 1272 OG1 THR A 177 1543 1215 1590 31 79 153 O ATOM 1273 CG2 THR A 177 29.856 14.065 20.933 1.00 12.56 C ANISOU 1273 CG2 THR A 177 1774 1393 1605 3 -29 260 C ATOM 1274 N VAL A 178 30.290 10.759 23.931 1.00 11.93 N ANISOU 1274 N VAL A 178 1662 1404 1464 -107 33 143 N ATOM 1275 CA VAL A 178 30.020 9.431 24.531 1.00 12.21 C ANISOU 1275 CA VAL A 178 1631 1463 1544 -77 43 106 C ATOM 1276 C VAL A 178 29.037 8.635 23.669 1.00 12.22 C ANISOU 1276 C VAL A 178 1625 1505 1511 -24 3 112 C ATOM 1277 O VAL A 178 29.131 7.411 23.589 1.00 12.43 O ANISOU 1277 O VAL A 178 1721 1491 1509 -42 -34 97 O ATOM 1278 CB VAL A 178 29.583 9.497 26.021 1.00 12.45 C ANISOU 1278 CB VAL A 178 1680 1497 1553 -30 -12 120 C ATOM 1279 CG1 VAL A 178 28.064 9.652 26.163 1.00 13.26 C ANISOU 1279 CG1 VAL A 178 1771 1592 1674 -58 170 85 C ATOM 1280 CG2 VAL A 178 30.078 8.272 26.777 1.00 12.67 C ANISOU 1280 CG2 VAL A 178 1623 1571 1617 -95 81 179 C ATOM 1281 N LYS A 179 28.112 9.328 23.000 1.00 12.00 N ANISOU 1281 N LYS A 179 1544 1515 1499 -18 -29 92 N ATOM 1282 CA ALYS A 179 27.180 8.654 22.099 0.25 11.62 C ANISOU 1282 CA ALYS A 179 1511 1437 1465 -15 -15 103 C ATOM 1283 CA BLYS A 179 27.177 8.673 22.088 0.25 11.78 C ANISOU 1283 CA BLYS A 179 1539 1455 1480 -13 -20 98 C ATOM 1284 CA CLYS A 179 27.181 8.644 22.102 0.50 11.96 C ANISOU 1284 CA CLYS A 179 1560 1477 1504 -23 -16 101 C ATOM 1285 C LYS A 179 27.949 7.950 20.980 1.00 11.69 C ANISOU 1285 C LYS A 179 1557 1437 1446 -29 -26 110 C ATOM 1286 O LYS A 179 27.670 6.792 20.654 1.00 11.55 O ANISOU 1286 O LYS A 179 1578 1344 1467 -36 9 233 O ATOM 1287 CB ALYS A 179 26.150 9.633 21.536 0.25 11.82 C ANISOU 1287 CB ALYS A 179 1526 1455 1510 -18 -41 73 C ATOM 1288 CB BLYS A 179 26.222 9.712 21.502 0.25 12.19 C ANISOU 1288 CB BLYS A 179 1578 1503 1548 -14 -36 70 C ATOM 1289 CB CLYS A 179 26.129 9.605 21.544 0.50 12.48 C ANISOU 1289 CB CLYS A 179 1615 1515 1612 -12 -58 80 C ATOM 1290 CG ALYS A 179 25.348 9.077 20.379 0.25 11.83 C ANISOU 1290 CG ALYS A 179 1540 1470 1485 -56 39 49 C ATOM 1291 CG BLYS A 179 25.096 9.155 20.666 0.25 13.23 C ANISOU 1291 CG BLYS A 179 1741 1682 1605 -100 32 -8 C ATOM 1292 CG CLYS A 179 25.095 8.965 20.624 0.50 13.67 C ANISOU 1292 CG CLYS A 179 1758 1756 1680 34 -54 -3 C ATOM 1293 CD ALYS A 179 24.091 9.886 20.112 0.25 8.42 C ANISOU 1293 CD ALYS A 179 1177 1184 835 13 -299 -52 C ATOM 1294 CD BLYS A 179 24.119 10.261 20.298 0.25 9.01 C ANISOU 1294 CD BLYS A 179 1133 1270 1017 -2 -495 -71 C ATOM 1295 CD CLYS A 179 24.477 7.731 21.261 0.50 13.74 C ANISOU 1295 CD CLYS A 179 1796 1742 1683 -15 6 27 C ATOM 1296 CE ALYS A 179 23.353 9.346 18.896 0.25 12.04 C ANISOU 1296 CE ALYS A 179 1532 1470 1570 178 182 65 C ATOM 1297 CE BLYS A 179 23.158 9.822 19.210 0.25 19.61 C ANISOU 1297 CE BLYS A 179 2411 2833 2204 -458 521 -423 C ATOM 1298 CE CLYS A 179 23.008 7.551 20.951 0.50 16.49 C ANISOU 1298 CE CLYS A 179 2099 2093 2074 63 -113 52 C ATOM 1299 NZ ALYS A 179 22.679 8.051 19.135 0.25 7.20 N ANISOU 1299 NZ ALYS A 179 970 852 912 -20 -44 -17 N ATOM 1300 NZ BLYS A 179 22.450 10.988 18.610 0.25 7.98 N ANISOU 1300 NZ BLYS A 179 1167 628 1236 400 -315 279 N ATOM 1301 NZ CLYS A 179 22.709 6.541 19.899 0.50 15.66 N ANISOU 1301 NZ CLYS A 179 2116 1918 1916 170 -177 -8 N ATOM 1302 N GLU A 180 28.930 8.643 20.401 1.00 11.52 N ANISOU 1302 N GLU A 180 1535 1413 1426 -27 11 146 N ATOM 1303 CA GLU A 180 29.751 8.024 19.379 1.00 11.33 C ANISOU 1303 CA GLU A 180 1552 1383 1367 -8 38 216 C ATOM 1304 C GLU A 180 30.559 6.849 19.949 1.00 10.96 C ANISOU 1304 C GLU A 180 1435 1360 1368 -15 29 137 C ATOM 1305 O GLU A 180 30.691 5.819 19.291 1.00 12.05 O ANISOU 1305 O GLU A 180 1673 1423 1481 16 -18 210 O ATOM 1306 CB GLU A 180 30.693 9.058 18.740 1.00 11.64 C ANISOU 1306 CB GLU A 180 1471 1473 1478 -89 99 208 C ATOM 1307 CG GLU A 180 31.478 8.492 17.545 1.00 12.38 C ANISOU 1307 CG GLU A 180 1804 1405 1494 -98 153 114 C ATOM 1308 CD GLU A 180 32.447 9.488 16.908 1.00 13.28 C ANISOU 1308 CD GLU A 180 1862 1650 1534 -26 139 210 C ATOM 1309 OE1 GLU A 180 32.588 10.615 17.404 1.00 16.14 O ANISOU 1309 OE1 GLU A 180 2324 2094 1712 -143 61 242 O ATOM 1310 OE2 GLU A 180 33.069 9.117 15.881 1.00 18.95 O ANISOU 1310 OE2 GLU A 180 2645 2466 2087 -18 347 91 O ATOM 1311 N ALA A 181 31.093 7.015 21.159 1.00 10.62 N ANISOU 1311 N ALA A 181 1396 1348 1291 -13 83 173 N ATOM 1312 CA ALA A 181 31.882 5.951 21.806 1.00 10.10 C ANISOU 1312 CA ALA A 181 1363 1325 1147 -83 -24 121 C ATOM 1313 C ALA A 181 31.042 4.688 21.954 1.00 9.88 C ANISOU 1313 C ALA A 181 1325 1309 1120 -33 26 116 C ATOM 1314 O ALA A 181 31.491 3.577 21.667 1.00 10.03 O ANISOU 1314 O ALA A 181 1376 1356 1079 -48 61 122 O ATOM 1315 CB ALA A 181 32.383 6.420 23.159 1.00 10.79 C ANISOU 1315 CB ALA A 181 1511 1418 1168 -98 -16 73 C ATOM 1316 N ILE A 182 29.802 4.881 22.379 1.00 10.09 N ANISOU 1316 N ILE A 182 1319 1413 1099 -97 16 113 N ATOM 1317 CA ILE A 182 28.863 3.780 22.541 1.00 9.95 C ANISOU 1317 CA ILE A 182 1406 1273 1101 -72 41 61 C ATOM 1318 C ILE A 182 28.565 3.106 21.202 1.00 9.94 C ANISOU 1318 C ILE A 182 1387 1305 1083 -45 12 133 C ATOM 1319 O ILE A 182 28.564 1.878 21.114 1.00 9.76 O ANISOU 1319 O ILE A 182 1450 1288 968 -52 40 125 O ATOM 1320 CB ILE A 182 27.597 4.261 23.296 1.00 10.16 C ANISOU 1320 CB ILE A 182 1257 1433 1168 -71 -42 100 C ATOM 1321 CG1 ILE A 182 27.983 4.572 24.758 1.00 10.85 C ANISOU 1321 CG1 ILE A 182 1603 1365 1152 -83 166 2 C ATOM 1322 CG2 ILE A 182 26.444 3.234 23.182 1.00 10.62 C ANISOU 1322 CG2 ILE A 182 1352 1404 1276 -73 87 106 C ATOM 1323 CD1 ILE A 182 26.982 5.465 25.504 1.00 11.85 C ANISOU 1323 CD1 ILE A 182 1374 1497 1632 50 137 38 C ATOM 1324 N ARG A 183 28.347 3.903 20.155 1.00 9.76 N ANISOU 1324 N ARG A 183 1462 1282 965 -47 -16 130 N ATOM 1325 CA ARG A 183 28.104 3.317 18.831 1.00 10.57 C ANISOU 1325 CA ARG A 183 1587 1352 1077 -25 -54 163 C ATOM 1326 C ARG A 183 29.323 2.512 18.351 1.00 10.56 C ANISOU 1326 C ARG A 183 1567 1346 1098 -28 -27 138 C ATOM 1327 O ARG A 183 29.187 1.406 17.842 1.00 11.16 O ANISOU 1327 O ARG A 183 1596 1361 1282 -44 -19 246 O ATOM 1328 CB ARG A 183 27.716 4.387 17.804 1.00 10.54 C ANISOU 1328 CB ARG A 183 1598 1334 1070 18 -87 136 C ATOM 1329 CG ARG A 183 27.575 3.785 16.428 1.00 11.08 C ANISOU 1329 CG ARG A 183 1772 1340 1097 80 -114 137 C ATOM 1330 CD ARG A 183 27.047 4.787 15.407 1.00 12.04 C ANISOU 1330 CD ARG A 183 1817 1481 1276 94 -170 359 C ATOM 1331 NE ARG A 183 27.931 5.937 15.229 1.00 15.15 N ANISOU 1331 NE ARG A 183 2093 1892 1771 -31 2 295 N ATOM 1332 CZ ARG A 183 29.014 5.941 14.460 1.00 15.36 C ANISOU 1332 CZ ARG A 183 1997 1965 1870 -10 -40 168 C ATOM 1333 NH1 ARG A 183 29.366 4.842 13.792 1.00 16.65 N ANISOU 1333 NH1 ARG A 183 2393 2032 1900 36 56 240 N ATOM 1334 NH2 ARG A 183 29.738 7.056 14.352 1.00 16.45 N ANISOU 1334 NH2 ARG A 183 2209 2062 1978 -143 78 306 N ATOM 1335 N MET A 184 30.519 3.081 18.496 1.00 11.28 N ANISOU 1335 N MET A 184 1597 1416 1273 -57 2 112 N ATOM 1336 CA MET A 184 31.748 2.375 18.129 1.00 13.02 C ANISOU 1336 CA MET A 184 1710 1670 1566 -37 39 100 C ATOM 1337 C MET A 184 31.857 1.044 18.855 1.00 12.21 C ANISOU 1337 C MET A 184 1618 1524 1496 14 -21 33 C ATOM 1338 O MET A 184 32.143 0.000 18.240 1.00 12.91 O ANISOU 1338 O MET A 184 1696 1562 1648 37 0 8 O ATOM 1339 CB MET A 184 32.975 3.227 18.419 1.00 12.79 C ANISOU 1339 CB MET A 184 1717 1586 1554 -46 18 71 C ATOM 1340 CG MET A 184 32.996 4.497 17.587 1.00 14.98 C ANISOU 1340 CG MET A 184 2062 1848 1780 7 69 141 C ATOM 1341 SD MET A 184 34.348 5.572 18.054 1.00 17.48 S ANISOU 1341 SD MET A 184 2238 2366 2036 -230 100 197 S ATOM 1342 CE MET A 184 35.756 4.485 17.851 1.00 17.94 C ANISOU 1342 CE MET A 184 2180 2427 2209 -149 16 6 C ATOM 1343 N GLY A 185 31.603 1.088 20.160 1.00 11.72 N ANISOU 1343 N GLY A 185 1518 1475 1458 4 41 28 N ATOM 1344 CA GLY A 185 31.585 -0.119 20.992 1.00 11.25 C ANISOU 1344 CA GLY A 185 1566 1390 1318 -3 14 35 C ATOM 1345 C GLY A 185 30.603 -1.171 20.477 1.00 11.45 C ANISOU 1345 C GLY A 185 1604 1413 1332 30 17 -11 C ATOM 1346 O GLY A 185 30.956 -2.362 20.320 1.00 12.28 O ANISOU 1346 O GLY A 185 1724 1514 1425 102 38 -60 O ATOM 1347 N SER A 186 29.373 -0.741 20.216 1.00 10.75 N ANISOU 1347 N SER A 186 1533 1323 1227 51 106 14 N ATOM 1348 CA SER A 186 28.343 -1.618 19.658 1.00 11.29 C ANISOU 1348 CA SER A 186 1583 1423 1283 40 79 14 C ATOM 1349 C SER A 186 28.801 -2.295 18.359 1.00 10.72 C ANISOU 1349 C SER A 186 1498 1340 1233 38 141 18 C ATOM 1350 O SER A 186 28.665 -3.512 18.199 1.00 9.95 O ANISOU 1350 O SER A 186 1343 1294 1144 65 76 192 O ATOM 1351 CB SER A 186 27.037 -0.868 19.419 1.00 11.82 C ANISOU 1351 CB SER A 186 1559 1452 1479 40 80 -90 C ATOM 1352 OG SER A 186 26.102 -1.684 18.716 1.00 14.99 O ANISOU 1352 OG SER A 186 1851 1853 1992 -94 51 -17 O ATOM 1353 N GLU A 187 29.339 -1.501 17.430 1.00 10.66 N ANISOU 1353 N GLU A 187 1584 1242 1223 0 103 86 N ATOM 1354 CA GLU A 187 29.749 -2.048 16.128 1.00 11.15 C ANISOU 1354 CA GLU A 187 1526 1410 1298 -5 120 107 C ATOM 1355 C GLU A 187 30.870 -3.064 16.261 1.00 11.28 C ANISOU 1355 C GLU A 187 1562 1421 1303 -33 68 118 C ATOM 1356 O GLU A 187 30.830 -4.109 15.637 1.00 12.34 O ANISOU 1356 O GLU A 187 1727 1622 1338 63 75 11 O ATOM 1357 CB GLU A 187 30.150 -0.911 15.183 1.00 11.27 C ANISOU 1357 CB GLU A 187 1537 1411 1334 -34 98 175 C ATOM 1358 CG GLU A 187 28.951 0.015 14.893 1.00 12.13 C ANISOU 1358 CG GLU A 187 1642 1491 1475 40 19 50 C ATOM 1359 CD GLU A 187 29.332 1.306 14.213 1.00 14.75 C ANISOU 1359 CD GLU A 187 1972 1822 1808 -8 71 154 C ATOM 1360 OE1 GLU A 187 30.545 1.578 14.087 1.00 17.48 O ANISOU 1360 OE1 GLU A 187 2093 2173 2374 56 -31 251 O ATOM 1361 OE2 GLU A 187 28.410 2.065 13.840 1.00 13.60 O ANISOU 1361 OE2 GLU A 187 2098 1844 1225 -25 -38 126 O ATOM 1362 N VAL A 188 31.865 -2.759 17.087 1.00 11.38 N ANISOU 1362 N VAL A 188 1452 1553 1318 28 56 132 N ATOM 1363 CA VAL A 188 32.956 -3.719 17.320 1.00 11.35 C ANISOU 1363 CA VAL A 188 1469 1528 1313 17 68 139 C ATOM 1364 C VAL A 188 32.442 -5.008 17.966 1.00 11.24 C ANISOU 1364 C VAL A 188 1460 1498 1311 24 25 97 C ATOM 1365 O VAL A 188 32.827 -6.115 17.577 1.00 11.46 O ANISOU 1365 O VAL A 188 1461 1582 1310 21 98 113 O ATOM 1366 CB VAL A 188 34.102 -3.087 18.139 1.00 11.36 C ANISOU 1366 CB VAL A 188 1488 1442 1387 -54 25 183 C ATOM 1367 CG1 VAL A 188 35.167 -4.134 18.490 1.00 11.67 C ANISOU 1367 CG1 VAL A 188 1498 1514 1419 99 119 160 C ATOM 1368 CG2 VAL A 188 34.721 -1.888 17.380 1.00 11.83 C ANISOU 1368 CG2 VAL A 188 1461 1542 1489 -140 224 201 C ATOM 1369 N PHE A 189 31.572 -4.850 18.958 1.00 11.57 N ANISOU 1369 N PHE A 189 1490 1528 1376 17 87 134 N ATOM 1370 CA PHE A 189 30.927 -5.977 19.644 1.00 11.87 C ANISOU 1370 CA PHE A 189 1587 1499 1422 -10 14 86 C ATOM 1371 C PHE A 189 30.228 -6.915 18.655 1.00 11.94 C ANISOU 1371 C PHE A 189 1608 1524 1405 22 34 82 C ATOM 1372 O PHE A 189 30.384 -8.134 18.724 1.00 12.54 O ANISOU 1372 O PHE A 189 1766 1573 1426 139 -86 72 O ATOM 1373 CB PHE A 189 29.953 -5.414 20.693 1.00 12.52 C ANISOU 1373 CB PHE A 189 1650 1593 1513 -36 54 68 C ATOM 1374 CG PHE A 189 29.112 -6.455 21.386 1.00 13.12 C ANISOU 1374 CG PHE A 189 1782 1577 1625 -20 5 112 C ATOM 1375 CD1 PHE A 189 29.619 -7.194 22.455 1.00 13.54 C ANISOU 1375 CD1 PHE A 189 1878 1577 1688 45 -37 25 C ATOM 1376 CD2 PHE A 189 27.790 -6.655 21.006 1.00 14.05 C ANISOU 1376 CD2 PHE A 189 1860 1853 1624 -120 -50 63 C ATOM 1377 CE1 PHE A 189 28.825 -8.151 23.097 1.00 13.49 C ANISOU 1377 CE1 PHE A 189 1828 1714 1582 38 9 23 C ATOM 1378 CE2 PHE A 189 26.994 -7.609 21.649 1.00 13.67 C ANISOU 1378 CE2 PHE A 189 1898 1700 1594 -33 0 26 C ATOM 1379 CZ PHE A 189 27.520 -8.354 22.697 1.00 14.03 C ANISOU 1379 CZ PHE A 189 1914 1660 1756 -10 41 71 C ATOM 1380 N HIS A 190 29.492 -6.346 17.704 1.00 11.61 N ANISOU 1380 N HIS A 190 1515 1510 1386 38 -12 31 N ATOM 1381 CA HIS A 190 28.805 -7.165 16.700 1.00 12.29 C ANISOU 1381 CA HIS A 190 1605 1617 1445 19 3 -9 C ATOM 1382 C HIS A 190 29.738 -7.815 15.688 1.00 12.71 C ANISOU 1382 C HIS A 190 1676 1633 1518 17 14 15 C ATOM 1383 O HIS A 190 29.567 -8.992 15.326 1.00 13.21 O ANISOU 1383 O HIS A 190 1798 1721 1498 -52 31 -39 O ATOM 1384 CB HIS A 190 27.686 -6.382 16.030 1.00 12.37 C ANISOU 1384 CB HIS A 190 1614 1607 1479 52 7 52 C ATOM 1385 CG HIS A 190 26.554 -6.085 16.963 1.00 13.17 C ANISOU 1385 CG HIS A 190 1653 1751 1596 60 72 -49 C ATOM 1386 ND1 HIS A 190 26.162 -4.807 17.293 1.00 14.98 N ANISOU 1386 ND1 HIS A 190 1975 1930 1787 -36 13 91 N ATOM 1387 CD2 HIS A 190 25.769 -6.917 17.686 1.00 15.48 C ANISOU 1387 CD2 HIS A 190 1887 1979 2016 -10 197 -44 C ATOM 1388 CE1 HIS A 190 25.157 -4.863 18.150 1.00 15.63 C ANISOU 1388 CE1 HIS A 190 2023 1894 2021 67 107 -198 C ATOM 1389 NE2 HIS A 190 24.895 -6.131 18.403 1.00 16.67 N ANISOU 1389 NE2 HIS A 190 2125 2114 2094 139 231 23 N ATOM 1390 N HIS A 191 30.745 -7.061 15.255 1.00 12.60 N ANISOU 1390 N HIS A 191 1685 1642 1458 14 6 2 N ATOM 1391 CA HIS A 191 31.730 -7.638 14.349 1.00 13.33 C ANISOU 1391 CA HIS A 191 1784 1685 1596 60 11 53 C ATOM 1392 C HIS A 191 32.498 -8.778 15.017 1.00 13.22 C ANISOU 1392 C HIS A 191 1788 1708 1526 90 -33 24 C ATOM 1393 O HIS A 191 32.811 -9.772 14.366 1.00 14.22 O ANISOU 1393 O HIS A 191 1990 1755 1656 94 -85 -7 O ATOM 1394 CB HIS A 191 32.638 -6.573 13.754 1.00 13.82 C ANISOU 1394 CB HIS A 191 1826 1792 1630 35 -46 73 C ATOM 1395 CG HIS A 191 32.033 -5.922 12.553 1.00 13.87 C ANISOU 1395 CG HIS A 191 1930 1803 1537 4 -32 158 C ATOM 1396 ND1 HIS A 191 31.455 -4.671 12.583 1.00 15.61 N ANISOU 1396 ND1 HIS A 191 2070 2198 1662 123 -58 -14 N ATOM 1397 CD2 HIS A 191 31.838 -6.401 11.301 1.00 14.93 C ANISOU 1397 CD2 HIS A 191 2037 1997 1636 -24 -73 -39 C ATOM 1398 CE1 HIS A 191 30.972 -4.385 11.382 1.00 15.29 C ANISOU 1398 CE1 HIS A 191 2152 2043 1614 145 -120 -15 C ATOM 1399 NE2 HIS A 191 31.195 -5.417 10.588 1.00 16.55 N ANISOU 1399 NE2 HIS A 191 2256 2163 1865 103 -125 70 N ATOM 1400 N LEU A 192 32.758 -8.658 16.319 1.00 13.13 N ANISOU 1400 N LEU A 192 1797 1689 1501 87 -5 22 N ATOM 1401 CA LEU A 192 33.419 -9.742 17.035 1.00 12.70 C ANISOU 1401 CA LEU A 192 1703 1690 1430 47 -19 -38 C ATOM 1402 C LEU A 192 32.584 -11.012 17.071 1.00 12.38 C ANISOU 1402 C LEU A 192 1704 1622 1377 44 14 -8 C ATOM 1403 O LEU A 192 33.125 -12.101 16.915 1.00 13.15 O ANISOU 1403 O LEU A 192 1758 1750 1487 70 100 -22 O ATOM 1404 CB LEU A 192 33.814 -9.319 18.445 1.00 12.54 C ANISOU 1404 CB LEU A 192 1740 1663 1360 47 -16 -84 C ATOM 1405 CG LEU A 192 34.628 -10.340 19.231 1.00 13.39 C ANISOU 1405 CG LEU A 192 1728 1851 1506 56 -18 -29 C ATOM 1406 CD1 LEU A 192 35.898 -10.774 18.503 1.00 14.91 C ANISOU 1406 CD1 LEU A 192 1877 1997 1790 244 76 -9 C ATOM 1407 CD2 LEU A 192 34.994 -9.723 20.550 1.00 15.12 C ANISOU 1407 CD2 LEU A 192 2084 2037 1623 12 -92 -177 C ATOM 1408 N ALA A 193 31.274 -10.883 17.272 1.00 12.18 N ANISOU 1408 N ALA A 193 1660 1603 1363 -23 6 -19 N ATOM 1409 CA ALA A 193 30.403 -12.067 17.224 1.00 12.87 C ANISOU 1409 CA ALA A 193 1753 1691 1445 -36 20 -50 C ATOM 1410 C ALA A 193 30.557 -12.791 15.883 1.00 13.46 C ANISOU 1410 C ALA A 193 1860 1746 1508 -3 -5 -57 C ATOM 1411 O ALA A 193 30.681 -14.011 15.850 1.00 13.97 O ANISOU 1411 O ALA A 193 2048 1767 1494 -43 32 -27 O ATOM 1412 CB ALA A 193 28.957 -11.688 17.465 1.00 13.14 C ANISOU 1412 CB ALA A 193 1734 1748 1509 13 2 -53 C ATOM 1413 N LYS A 194 30.558 -12.033 14.783 1.00 13.86 N ANISOU 1413 N LYS A 194 1960 1781 1525 16 34 -62 N ATOM 1414 CA LYS A 194 30.706 -12.628 13.439 1.00 14.84 C ANISOU 1414 CA LYS A 194 2044 1942 1648 30 11 -72 C ATOM 1415 C LYS A 194 32.059 -13.337 13.278 1.00 14.12 C ANISOU 1415 C LYS A 194 1978 1809 1578 20 56 -34 C ATOM 1416 O LYS A 194 32.133 -14.475 12.792 1.00 13.91 O ANISOU 1416 O LYS A 194 1918 1852 1513 -26 104 -123 O ATOM 1417 CB LYS A 194 30.539 -11.553 12.355 1.00 14.74 C ANISOU 1417 CB LYS A 194 2051 1862 1687 105 -9 -50 C ATOM 1418 CG LYS A 194 29.190 -10.837 12.398 1.00 16.05 C ANISOU 1418 CG LYS A 194 2176 2053 1867 136 -87 -73 C ATOM 1419 CD LYS A 194 29.142 -9.694 11.387 1.00 17.75 C ANISOU 1419 CD LYS A 194 2426 2287 2031 79 3 -19 C ATOM 1420 CE LYS A 194 27.849 -8.891 11.529 1.00 22.32 C ANISOU 1420 CE LYS A 194 2716 2907 2856 164 23 -15 C ATOM 1421 NZ LYS A 194 26.614 -9.700 11.310 1.00 26.51 N ANISOU 1421 NZ LYS A 194 3221 3522 3326 -31 -62 -71 N ATOM 1422 N VAL A 195 33.114 -12.673 13.740 1.00 14.15 N ANISOU 1422 N VAL A 195 1891 1874 1611 29 84 8 N ATOM 1423 CA VAL A 195 34.481 -13.196 13.685 1.00 14.76 C ANISOU 1423 CA VAL A 195 1988 1875 1745 48 50 24 C ATOM 1424 C VAL A 195 34.614 -14.505 14.481 1.00 14.26 C ANISOU 1424 C VAL A 195 1928 1809 1681 55 42 21 C ATOM 1425 O VAL A 195 35.213 -15.475 14.005 1.00 14.35 O ANISOU 1425 O VAL A 195 2099 1743 1609 107 100 71 O ATOM 1426 CB VAL A 195 35.489 -12.131 14.184 1.00 15.34 C ANISOU 1426 CB VAL A 195 1970 1967 1890 35 80 43 C ATOM 1427 CG1 VAL A 195 36.854 -12.756 14.498 1.00 16.52 C ANISOU 1427 CG1 VAL A 195 1998 2257 2019 23 -41 44 C ATOM 1428 CG2 VAL A 195 35.615 -11.007 13.150 1.00 16.19 C ANISOU 1428 CG2 VAL A 195 2248 1899 2004 -27 23 21 C ATOM 1429 N LEU A 196 34.029 -14.530 15.672 1.00 14.48 N ANISOU 1429 N LEU A 196 1966 1809 1727 17 59 24 N ATOM 1430 CA LEU A 196 34.061 -15.725 16.518 1.00 14.80 C ANISOU 1430 CA LEU A 196 2011 1872 1740 75 70 0 C ATOM 1431 C LEU A 196 33.212 -16.856 15.951 1.00 15.52 C ANISOU 1431 C LEU A 196 2083 1962 1850 66 67 -17 C ATOM 1432 O LEU A 196 33.626 -18.023 15.974 1.00 15.52 O ANISOU 1432 O LEU A 196 2073 1939 1884 131 19 -38 O ATOM 1433 CB LEU A 196 33.625 -15.386 17.951 1.00 14.66 C ANISOU 1433 CB LEU A 196 1993 1835 1740 118 69 -12 C ATOM 1434 CG LEU A 196 34.551 -14.483 18.754 1.00 13.96 C ANISOU 1434 CG LEU A 196 1790 1840 1671 135 95 13 C ATOM 1435 CD1 LEU A 196 33.894 -14.135 20.089 1.00 15.41 C ANISOU 1435 CD1 LEU A 196 2127 1955 1772 271 188 -97 C ATOM 1436 CD2 LEU A 196 35.912 -15.142 18.987 1.00 13.61 C ANISOU 1436 CD2 LEU A 196 1659 1580 1929 77 7 -162 C ATOM 1437 N LYS A 197 32.029 -16.523 15.441 1.00 15.89 N ANISOU 1437 N LYS A 197 2066 1985 1985 70 82 -99 N ATOM 1438 CA LYS A 197 31.172 -17.517 14.790 1.00 16.58 C ANISOU 1438 CA LYS A 197 2139 2115 2043 54 114 -115 C ATOM 1439 C LYS A 197 31.892 -18.244 13.662 1.00 16.43 C ANISOU 1439 C LYS A 197 2177 2046 2019 60 168 -98 C ATOM 1440 O LYS A 197 31.845 -19.488 13.580 1.00 16.48 O ANISOU 1440 O LYS A 197 2215 2060 1983 17 291 -105 O ATOM 1441 CB LYS A 197 29.892 -16.865 14.265 1.00 17.10 C ANISOU 1441 CB LYS A 197 2213 2130 2154 136 95 -131 C ATOM 1442 CG LYS A 197 28.819 -16.778 15.323 1.00 20.40 C ANISOU 1442 CG LYS A 197 2555 2661 2532 -55 170 -61 C ATOM 1443 CD LYS A 197 27.635 -15.982 14.836 1.00 24.07 C ANISOU 1443 CD LYS A 197 3001 3105 3037 162 83 41 C ATOM 1444 CE LYS A 197 27.559 -14.634 15.533 1.00 27.38 C ANISOU 1444 CE LYS A 197 3476 3351 3574 0 -6 -69 C ATOM 1445 NZ LYS A 197 26.995 -14.754 16.913 1.00 28.67 N ANISOU 1445 NZ LYS A 197 3748 3594 3549 86 115 80 N ATOM 1446 N ALA A 198 32.565 -17.466 12.807 1.00 15.77 N ANISOU 1446 N ALA A 198 2059 2011 1921 73 167 -135 N ATOM 1447 CA ALA A 198 33.298 -18.030 11.669 1.00 16.20 C ANISOU 1447 CA ALA A 198 2127 2094 1933 80 142 -105 C ATOM 1448 C ALA A 198 34.426 -18.957 12.112 1.00 16.22 C ANISOU 1448 C ALA A 198 2138 2101 1923 67 87 -110 C ATOM 1449 O ALA A 198 34.806 -19.876 11.374 1.00 16.05 O ANISOU 1449 O ALA A 198 2140 2050 1905 110 136 -151 O ATOM 1450 CB ALA A 198 33.816 -16.926 10.763 1.00 16.19 C ANISOU 1450 CB ALA A 198 2107 2067 1976 76 148 -74 C ATOM 1451 N LYS A 199 34.963 -18.714 13.310 1.00 15.82 N ANISOU 1451 N LYS A 199 2122 2082 1804 72 83 -129 N ATOM 1452 CA LYS A 199 36.003 -19.574 13.886 1.00 16.18 C ANISOU 1452 CA LYS A 199 2187 2093 1866 30 13 -102 C ATOM 1453 C LYS A 199 35.422 -20.842 14.542 1.00 16.49 C ANISOU 1453 C LYS A 199 2296 2065 1905 63 3 -87 C ATOM 1454 O LYS A 199 36.171 -21.726 14.976 1.00 17.35 O ANISOU 1454 O LYS A 199 2454 2150 1986 122 -29 -110 O ATOM 1455 CB LYS A 199 36.832 -18.800 14.919 1.00 15.97 C ANISOU 1455 CB LYS A 199 2184 2072 1810 -42 17 -80 C ATOM 1456 CG LYS A 199 37.723 -17.694 14.349 1.00 15.97 C ANISOU 1456 CG LYS A 199 2121 2148 1798 -124 -33 -95 C ATOM 1457 CD LYS A 199 38.289 -16.803 15.454 1.00 16.54 C ANISOU 1457 CD LYS A 199 2214 2183 1886 15 0 -148 C ATOM 1458 CE LYS A 199 39.061 -15.637 14.869 1.00 17.92 C ANISOU 1458 CE LYS A 199 2314 2360 2131 8 -25 -113 C ATOM 1459 NZ LYS A 199 40.415 -16.013 14.346 1.00 17.69 N ANISOU 1459 NZ LYS A 199 2292 2469 1961 122 -40 -13 N ATOM 1460 N GLY A 200 34.097 -20.917 14.626 1.00 16.77 N ANISOU 1460 N GLY A 200 2344 2035 1993 50 24 -78 N ATOM 1461 CA GLY A 200 33.403 -22.024 15.293 1.00 17.69 C ANISOU 1461 CA GLY A 200 2492 2140 2087 38 42 -42 C ATOM 1462 C GLY A 200 33.396 -21.891 16.800 1.00 18.57 C ANISOU 1462 C GLY A 200 2612 2225 2218 37 47 -11 C ATOM 1463 O GLY A 200 33.255 -22.884 17.530 1.00 19.30 O ANISOU 1463 O GLY A 200 2806 2310 2214 55 88 -3 O ATOM 1464 N MET A 201 33.528 -20.656 17.266 1.00 18.20 N ANISOU 1464 N MET A 201 2506 2260 2149 88 24 -76 N ATOM 1465 CA MET A 201 33.596 -20.397 18.683 1.00 18.92 C ANISOU 1465 CA MET A 201 2531 2407 2248 102 74 -78 C ATOM 1466 C MET A 201 32.250 -19.912 19.202 1.00 18.09 C ANISOU 1466 C MET A 201 2425 2263 2183 84 50 -40 C ATOM 1467 O MET A 201 31.416 -19.420 18.446 1.00 17.57 O ANISOU 1467 O MET A 201 2319 2212 2141 129 85 -46 O ATOM 1468 CB MET A 201 34.708 -19.392 18.965 1.00 19.53 C ANISOU 1468 CB MET A 201 2583 2502 2335 84 38 -52 C ATOM 1469 CG MET A 201 36.088 -19.966 18.718 1.00 20.33 C ANISOU 1469 CG MET A 201 2714 2688 2321 109 181 -172 C ATOM 1470 SD MET A 201 37.375 -18.756 18.961 1.00 22.33 S ANISOU 1470 SD MET A 201 2829 3026 2627 156 137 -152 S ATOM 1471 CE MET A 201 38.816 -19.824 18.782 1.00 21.48 C ANISOU 1471 CE MET A 201 2693 2951 2517 137 75 -125 C ATOM 1472 N ASN A 202 32.062 -20.073 20.504 1.00 17.70 N ANISOU 1472 N ASN A 202 2350 2221 2151 76 85 33 N ATOM 1473 CA ASN A 202 30.808 -19.768 21.185 1.00 17.82 C ANISOU 1473 CA ASN A 202 2360 2252 2158 51 65 14 C ATOM 1474 C ASN A 202 30.668 -18.266 21.390 1.00 17.36 C ANISOU 1474 C ASN A 202 2266 2253 2075 24 44 -25 C ATOM 1475 O ASN A 202 31.625 -17.599 21.783 1.00 17.38 O ANISOU 1475 O ASN A 202 2221 2207 2173 -5 19 -31 O ATOM 1476 CB ASN A 202 30.783 -20.533 22.515 1.00 18.22 C ANISOU 1476 CB ASN A 202 2429 2273 2221 7 101 58 C ATOM 1477 CG ASN A 202 29.461 -20.404 23.253 1.00 20.80 C ANISOU 1477 CG ASN A 202 2696 2606 2598 37 175 13 C ATOM 1478 OD1 ASN A 202 29.114 -19.331 23.741 1.00 23.49 O ANISOU 1478 OD1 ASN A 202 3170 2862 2891 162 260 121 O ATOM 1479 ND2 ASN A 202 28.733 -21.511 23.365 1.00 23.53 N ANISOU 1479 ND2 ASN A 202 2923 2930 3087 -75 159 21 N ATOM 1480 N THR A 203 29.484 -17.734 21.093 1.00 16.95 N ANISOU 1480 N THR A 203 2207 2204 2027 30 51 -42 N ATOM 1481 CA THR A 203 29.235 -16.299 21.238 1.00 16.68 C ANISOU 1481 CA THR A 203 2132 2207 1998 26 80 7 C ATOM 1482 C THR A 203 28.179 -15.956 22.286 1.00 16.05 C ANISOU 1482 C THR A 203 2074 2080 1944 -19 55 -9 C ATOM 1483 O THR A 203 27.723 -14.816 22.345 1.00 16.71 O ANISOU 1483 O THR A 203 2034 2174 2138 35 109 12 O ATOM 1484 CB THR A 203 28.853 -15.631 19.895 1.00 16.94 C ANISOU 1484 CB THR A 203 2127 2330 1979 20 87 0 C ATOM 1485 OG1 THR A 203 27.722 -16.310 19.338 1.00 18.53 O ANISOU 1485 OG1 THR A 203 2295 2594 2148 -79 58 125 O ATOM 1486 CG2 THR A 203 30.019 -15.715 18.919 1.00 17.91 C ANISOU 1486 CG2 THR A 203 2276 2499 2029 36 177 6 C ATOM 1487 N ALA A 204 27.814 -16.919 23.131 1.00 15.76 N ANISOU 1487 N ALA A 204 2022 2069 1895 -58 33 -61 N ATOM 1488 CA ALA A 204 26.972 -16.610 24.284 1.00 15.10 C ANISOU 1488 CA ALA A 204 1963 1885 1886 -68 25 -87 C ATOM 1489 C ALA A 204 27.792 -15.725 25.222 1.00 14.61 C ANISOU 1489 C ALA A 204 1901 1823 1825 -36 19 -91 C ATOM 1490 O ALA A 204 29.025 -15.750 25.199 1.00 14.90 O ANISOU 1490 O ALA A 204 1933 1842 1887 31 40 -227 O ATOM 1491 CB ALA A 204 26.525 -17.889 24.994 1.00 15.71 C ANISOU 1491 CB ALA A 204 2037 1993 1938 -70 60 -16 C ATOM 1492 N VAL A 205 27.108 -14.943 26.045 1.00 13.72 N ANISOU 1492 N VAL A 205 1798 1610 1805 -37 61 -41 N ATOM 1493 CA VAL A 205 27.795 -13.916 26.829 1.00 13.01 C ANISOU 1493 CA VAL A 205 1739 1582 1620 -11 22 -11 C ATOM 1494 C VAL A 205 27.927 -14.229 28.321 1.00 12.99 C ANISOU 1494 C VAL A 205 1723 1569 1644 14 68 3 C ATOM 1495 O VAL A 205 27.154 -15.019 28.873 1.00 13.28 O ANISOU 1495 O VAL A 205 1764 1642 1638 -33 107 59 O ATOM 1496 CB VAL A 205 27.117 -12.540 26.668 1.00 13.23 C ANISOU 1496 CB VAL A 205 1695 1557 1774 16 16 61 C ATOM 1497 CG1 VAL A 205 27.080 -12.107 25.209 1.00 13.93 C ANISOU 1497 CG1 VAL A 205 1812 1809 1670 -99 73 -90 C ATOM 1498 CG2 VAL A 205 25.717 -12.521 27.297 1.00 13.46 C ANISOU 1498 CG2 VAL A 205 1704 1638 1768 191 54 71 C ATOM 1499 N GLY A 206 28.922 -13.608 28.950 1.00 11.70 N ANISOU 1499 N GLY A 206 1678 1404 1363 23 21 -25 N ATOM 1500 CA GLY A 206 29.154 -13.766 30.388 1.00 11.91 C ANISOU 1500 CA GLY A 206 1685 1414 1426 33 56 44 C ATOM 1501 C GLY A 206 28.453 -12.699 31.210 1.00 11.67 C ANISOU 1501 C GLY A 206 1637 1415 1379 13 19 29 C ATOM 1502 O GLY A 206 27.570 -11.965 30.713 1.00 11.42 O ANISOU 1502 O GLY A 206 1538 1392 1407 -53 69 75 O ATOM 1503 N ASP A 207 28.869 -12.597 32.469 1.00 11.83 N ANISOU 1503 N ASP A 207 1696 1405 1394 15 39 40 N ATOM 1504 CA ASP A 207 28.201 -11.727 33.418 1.00 12.27 C ANISOU 1504 CA ASP A 207 1708 1471 1480 -6 14 -9 C ATOM 1505 C ASP A 207 28.189 -10.270 32.966 1.00 12.31 C ANISOU 1505 C ASP A 207 1691 1508 1477 5 -18 62 C ATOM 1506 O ASP A 207 27.232 -9.545 33.247 1.00 12.67 O ANISOU 1506 O ASP A 207 1765 1532 1516 -9 1 0 O ATOM 1507 CB ASP A 207 28.895 -11.803 34.768 1.00 12.97 C ANISOU 1507 CB ASP A 207 1833 1661 1431 13 17 106 C ATOM 1508 CG ASP A 207 28.680 -13.137 35.482 1.00 15.50 C ANISOU 1508 CG ASP A 207 2168 1821 1901 2 20 20 C ATOM 1509 OD1 ASP A 207 27.816 -13.953 35.066 1.00 17.74 O ANISOU 1509 OD1 ASP A 207 2414 2100 2226 -80 106 160 O ATOM 1510 OD2 ASP A 207 29.400 -13.353 36.479 1.00 17.69 O ANISOU 1510 OD2 ASP A 207 2446 2286 1986 116 15 68 O ATOM 1511 N GLU A 208 29.270 -9.847 32.308 1.00 12.00 N ANISOU 1511 N GLU A 208 1683 1453 1422 -10 -6 36 N ATOM 1512 CA GLU A 208 29.424 -8.450 31.879 1.00 12.90 C ANISOU 1512 CA GLU A 208 1712 1612 1575 -56 -28 123 C ATOM 1513 C GLU A 208 29.001 -8.233 30.437 1.00 11.99 C ANISOU 1513 C GLU A 208 1583 1500 1472 -31 8 59 C ATOM 1514 O GLU A 208 29.221 -7.143 29.890 1.00 11.17 O ANISOU 1514 O GLU A 208 1454 1404 1385 -7 31 250 O ATOM 1515 CB GLU A 208 30.871 -7.972 32.047 1.00 14.52 C ANISOU 1515 CB GLU A 208 1963 1835 1717 -130 -134 92 C ATOM 1516 CG GLU A 208 31.493 -8.328 33.370 1.00 19.41 C ANISOU 1516 CG GLU A 208 2664 2426 2283 -92 -175 174 C ATOM 1517 CD GLU A 208 32.360 -9.563 33.276 1.00 22.78 C ANISOU 1517 CD GLU A 208 2731 3105 2816 191 -48 -61 C ATOM 1518 OE1 GLU A 208 32.029 -10.533 32.540 1.00 23.01 O ANISOU 1518 OE1 GLU A 208 2590 3317 2833 101 -175 -15 O ATOM 1519 OE2 GLU A 208 33.383 -9.570 33.972 1.00 27.34 O ANISOU 1519 OE2 GLU A 208 3134 3944 3308 -61 -130 -130 O ATOM 1520 N GLY A 209 28.416 -9.260 29.810 1.00 10.60 N ANISOU 1520 N GLY A 209 1361 1383 1281 25 0 25 N ATOM 1521 CA GLY A 209 27.842 -9.099 28.465 1.00 10.84 C ANISOU 1521 CA GLY A 209 1372 1494 1251 135 73 -72 C ATOM 1522 C GLY A 209 28.799 -9.268 27.303 1.00 11.18 C ANISOU 1522 C GLY A 209 1432 1496 1319 19 57 -12 C ATOM 1523 O GLY A 209 28.420 -9.038 26.155 1.00 11.19 O ANISOU 1523 O GLY A 209 1447 1510 1294 35 34 -104 O ATOM 1524 N GLY A 210 30.034 -9.657 27.615 1.00 11.07 N ANISOU 1524 N GLY A 210 1391 1422 1390 47 111 -29 N ATOM 1525 CA GLY A 210 31.056 -9.935 26.608 1.00 11.37 C ANISOU 1525 CA GLY A 210 1532 1372 1417 69 103 -47 C ATOM 1526 C GLY A 210 31.211 -11.418 26.353 1.00 11.85 C ANISOU 1526 C GLY A 210 1638 1445 1419 -2 71 -21 C ATOM 1527 O GLY A 210 30.428 -12.241 26.851 1.00 11.37 O ANISOU 1527 O GLY A 210 1575 1319 1425 -13 -5 -25 O ATOM 1528 N TYR A 211 32.239 -11.756 25.583 1.00 12.08 N ANISOU 1528 N TYR A 211 1592 1447 1548 94 93 47 N ATOM 1529 CA TYR A 211 32.406 -13.124 25.097 1.00 12.76 C ANISOU 1529 CA TYR A 211 1707 1561 1577 28 82 -33 C ATOM 1530 C TYR A 211 33.489 -13.844 25.865 1.00 13.07 C ANISOU 1530 C TYR A 211 1798 1554 1612 0 36 34 C ATOM 1531 O TYR A 211 34.431 -13.227 26.356 1.00 13.11 O ANISOU 1531 O TYR A 211 1763 1503 1714 -6 13 14 O ATOM 1532 CB TYR A 211 32.734 -13.132 23.602 1.00 12.91 C ANISOU 1532 CB TYR A 211 1743 1609 1553 89 25 13 C ATOM 1533 CG TYR A 211 31.787 -12.312 22.752 1.00 13.28 C ANISOU 1533 CG TYR A 211 1768 1677 1599 32 15 -43 C ATOM 1534 CD1 TYR A 211 30.499 -12.768 22.472 1.00 14.00 C ANISOU 1534 CD1 TYR A 211 1678 1888 1753 196 -52 -65 C ATOM 1535 CD2 TYR A 211 32.198 -11.089 22.214 1.00 13.43 C ANISOU 1535 CD2 TYR A 211 1839 1604 1658 163 -9 10 C ATOM 1536 CE1 TYR A 211 29.616 -12.005 21.675 1.00 14.64 C ANISOU 1536 CE1 TYR A 211 1961 1956 1644 123 -126 67 C ATOM 1537 CE2 TYR A 211 31.335 -10.325 21.414 1.00 14.11 C ANISOU 1537 CE2 TYR A 211 1895 1896 1569 96 -145 85 C ATOM 1538 CZ TYR A 211 30.047 -10.798 21.152 1.00 13.63 C ANISOU 1538 CZ TYR A 211 1808 1764 1605 91 -59 -56 C ATOM 1539 OH TYR A 211 29.191 -10.047 20.359 1.00 15.18 O ANISOU 1539 OH TYR A 211 2064 1949 1755 55 -215 -22 O ATOM 1540 N ALA A 212 33.358 -15.164 25.962 1.00 14.00 N ANISOU 1540 N ALA A 212 1908 1654 1756 -7 36 0 N ATOM 1541 CA ALA A 212 34.389 -15.995 26.578 1.00 14.24 C ANISOU 1541 CA ALA A 212 1971 1711 1725 22 34 1 C ATOM 1542 C ALA A 212 34.655 -17.219 25.700 1.00 14.83 C ANISOU 1542 C ALA A 212 2056 1761 1818 0 55 -37 C ATOM 1543 O ALA A 212 34.468 -18.361 26.139 1.00 15.01 O ANISOU 1543 O ALA A 212 2205 1772 1725 1 59 -19 O ATOM 1544 CB ALA A 212 33.966 -16.415 27.972 1.00 14.46 C ANISOU 1544 CB ALA A 212 1979 1784 1729 7 57 28 C ATOM 1545 N PRO A 213 35.109 -16.988 24.456 1.00 14.99 N ANISOU 1545 N PRO A 213 2109 1794 1790 38 46 -63 N ATOM 1546 CA PRO A 213 35.303 -18.110 23.523 1.00 15.98 C ANISOU 1546 CA PRO A 213 2203 1921 1947 49 55 -70 C ATOM 1547 C PRO A 213 36.513 -18.946 23.925 1.00 16.80 C ANISOU 1547 C PRO A 213 2261 2035 2085 48 39 -53 C ATOM 1548 O PRO A 213 37.336 -18.512 24.743 1.00 16.44 O ANISOU 1548 O PRO A 213 2166 1939 2140 65 52 -94 O ATOM 1549 CB PRO A 213 35.553 -17.403 22.192 1.00 16.11 C ANISOU 1549 CB PRO A 213 2231 1975 1912 46 22 -70 C ATOM 1550 CG PRO A 213 36.211 -16.118 22.591 1.00 15.93 C ANISOU 1550 CG PRO A 213 2230 1960 1862 41 80 -61 C ATOM 1551 CD PRO A 213 35.506 -15.701 23.849 1.00 14.85 C ANISOU 1551 CD PRO A 213 2027 1762 1852 54 101 -81 C ATOM 1552 N ASN A 214 36.609 -20.138 23.343 1.00 17.91 N ANISOU 1552 N ASN A 214 2414 2112 2276 105 0 -104 N ATOM 1553 CA ASN A 214 37.660 -21.095 23.672 1.00 19.32 C ANISOU 1553 CA ASN A 214 2526 2363 2452 91 11 -69 C ATOM 1554 C ASN A 214 38.969 -20.784 22.968 1.00 19.37 C ANISOU 1554 C ASN A 214 2520 2370 2468 89 27 -86 C ATOM 1555 O ASN A 214 39.468 -21.601 22.181 1.00 19.08 O ANISOU 1555 O ASN A 214 2551 2280 2416 116 85 -210 O ATOM 1556 CB ASN A 214 37.200 -22.510 23.319 1.00 20.03 C ANISOU 1556 CB ASN A 214 2646 2414 2548 83 -23 -87 C ATOM 1557 CG ASN A 214 36.311 -23.118 24.387 1.00 24.50 C ANISOU 1557 CG ASN A 214 3205 3050 3054 15 54 0 C ATOM 1558 OD1 ASN A 214 36.396 -22.752 25.561 1.00 28.46 O ANISOU 1558 OD1 ASN A 214 3886 3621 3303 -58 -47 -44 O ATOM 1559 ND2 ASN A 214 35.444 -24.053 23.987 1.00 28.14 N ANISOU 1559 ND2 ASN A 214 3623 3483 3586 -90 -40 -80 N ATOM 1560 N LEU A 215 39.513 -19.598 23.235 1.00 18.95 N ANISOU 1560 N LEU A 215 2460 2341 2396 66 13 -114 N ATOM 1561 CA LEU A 215 40.805 -19.193 22.691 1.00 19.56 C ANISOU 1561 CA LEU A 215 2511 2436 2483 38 -28 -9 C ATOM 1562 C LEU A 215 41.941 -19.899 23.413 1.00 19.64 C ANISOU 1562 C LEU A 215 2495 2450 2514 31 -42 11 C ATOM 1563 O LEU A 215 41.818 -20.263 24.589 1.00 20.27 O ANISOU 1563 O LEU A 215 2574 2550 2575 53 -7 47 O ATOM 1564 CB LEU A 215 40.993 -17.678 22.786 1.00 19.66 C ANISOU 1564 CB LEU A 215 2554 2426 2489 22 -45 -16 C ATOM 1565 CG LEU A 215 39.905 -16.831 22.124 1.00 20.15 C ANISOU 1565 CG LEU A 215 2532 2519 2602 57 -53 16 C ATOM 1566 CD1 LEU A 215 39.884 -15.431 22.709 1.00 21.42 C ANISOU 1566 CD1 LEU A 215 2831 2510 2794 58 -4 36 C ATOM 1567 CD2 LEU A 215 40.072 -16.791 20.618 1.00 22.35 C ANISOU 1567 CD2 LEU A 215 2787 2909 2795 204 68 -28 C ATOM 1568 N GLY A 216 43.056 -20.055 22.714 1.00 19.74 N ANISOU 1568 N GLY A 216 2480 2483 2536 52 -60 12 N ATOM 1569 CA GLY A 216 44.156 -20.875 23.212 1.00 20.12 C ANISOU 1569 CA GLY A 216 2461 2556 2625 61 -64 60 C ATOM 1570 C GLY A 216 45.315 -20.125 23.836 1.00 20.67 C ANISOU 1570 C GLY A 216 2548 2632 2672 65 -79 52 C ATOM 1571 O GLY A 216 46.270 -20.761 24.310 1.00 21.35 O ANISOU 1571 O GLY A 216 2648 2692 2768 129 -142 153 O ATOM 1572 N SER A 217 45.262 -18.791 23.808 1.00 19.96 N ANISOU 1572 N SER A 217 2452 2589 2542 114 -17 27 N ATOM 1573 CA SER A 217 46.320 -17.955 24.381 1.00 19.89 C ANISOU 1573 CA SER A 217 2444 2621 2492 61 75 4 C ATOM 1574 C SER A 217 45.867 -16.521 24.611 1.00 19.94 C ANISOU 1574 C SER A 217 2458 2635 2483 34 42 -51 C ATOM 1575 O SER A 217 44.888 -16.061 24.005 1.00 19.19 O ANISOU 1575 O SER A 217 2343 2515 2431 100 93 -154 O ATOM 1576 CB SER A 217 47.569 -17.945 23.481 1.00 19.98 C ANISOU 1576 CB SER A 217 2423 2626 2541 96 85 35 C ATOM 1577 OG SER A 217 47.351 -17.141 22.334 1.00 20.46 O ANISOU 1577 OG SER A 217 2484 2799 2488 160 132 102 O ATOM 1578 N ASN A 218 46.597 -15.814 25.479 1.00 20.18 N ANISOU 1578 N ASN A 218 2425 2718 2523 -37 11 -63 N ATOM 1579 CA ASN A 218 46.434 -14.365 25.620 1.00 20.38 C ANISOU 1579 CA ASN A 218 2468 2741 2532 3 -35 -72 C ATOM 1580 C ASN A 218 46.606 -13.638 24.292 1.00 20.38 C ANISOU 1580 C ASN A 218 2470 2713 2559 18 -18 -68 C ATOM 1581 O ASN A 218 45.805 -12.774 23.949 1.00 20.43 O ANISOU 1581 O ASN A 218 2420 2722 2621 32 -16 -70 O ATOM 1582 CB ASN A 218 47.421 -13.800 26.656 1.00 20.89 C ANISOU 1582 CB ASN A 218 2510 2822 2605 -27 -49 -77 C ATOM 1583 CG ASN A 218 47.248 -14.434 28.022 1.00 21.79 C ANISOU 1583 CG ASN A 218 2616 3009 2654 28 -57 -32 C ATOM 1584 OD1 ASN A 218 46.145 -14.490 28.561 1.00 21.63 O ANISOU 1584 OD1 ASN A 218 2480 2987 2751 201 -124 -244 O ATOM 1585 ND2 ASN A 218 48.346 -14.938 28.585 1.00 23.93 N ANISOU 1585 ND2 ASN A 218 2772 3424 2895 156 -139 -99 N ATOM 1586 N ALA A 219 47.636 -14.021 23.532 1.00 20.61 N ANISOU 1586 N ALA A 219 2441 2783 2605 16 4 -27 N ATOM 1587 CA ALA A 219 47.882 -13.444 22.205 1.00 20.78 C ANISOU 1587 CA ALA A 219 2494 2769 2630 41 11 -13 C ATOM 1588 C ALA A 219 46.715 -13.639 21.237 1.00 20.54 C ANISOU 1588 C ALA A 219 2485 2707 2610 42 5 -16 C ATOM 1589 O ALA A 219 46.432 -12.766 20.415 1.00 21.48 O ANISOU 1589 O ALA A 219 2621 2849 2691 -21 -21 3 O ATOM 1590 CB ALA A 219 49.186 -14.003 21.596 1.00 21.07 C ANISOU 1590 CB ALA A 219 2487 2829 2688 78 40 0 C ATOM 1591 N GLU A 220 46.028 -14.772 21.338 1.00 19.98 N ANISOU 1591 N GLU A 220 2388 2687 2514 41 -6 -27 N ATOM 1592 CA GLU A 220 44.895 -15.026 20.443 1.00 19.25 C ANISOU 1592 CA GLU A 220 2363 2584 2367 77 -27 -24 C ATOM 1593 C GLU A 220 43.738 -14.083 20.756 1.00 18.50 C ANISOU 1593 C GLU A 220 2284 2466 2279 44 10 -6 C ATOM 1594 O GLU A 220 43.065 -13.607 19.837 1.00 18.04 O ANISOU 1594 O GLU A 220 2203 2349 2303 105 -30 -1 O ATOM 1595 CB GLU A 220 44.447 -16.485 20.479 1.00 19.17 C ANISOU 1595 CB GLU A 220 2369 2574 2338 52 -13 2 C ATOM 1596 CG GLU A 220 43.634 -16.904 19.238 1.00 19.56 C ANISOU 1596 CG GLU A 220 2476 2650 2304 96 -53 -15 C ATOM 1597 CD GLU A 220 43.115 -18.331 19.283 1.00 20.06 C ANISOU 1597 CD GLU A 220 2485 2695 2441 137 -4 -75 C ATOM 1598 OE1 GLU A 220 43.553 -19.109 20.167 1.00 20.52 O ANISOU 1598 OE1 GLU A 220 2938 2593 2265 166 -26 -40 O ATOM 1599 OE2 GLU A 220 42.269 -18.693 18.415 1.00 20.27 O ANISOU 1599 OE2 GLU A 220 2634 2915 2152 299 -21 -154 O ATOM 1600 N ALA A 221 43.538 -13.776 22.036 1.00 17.86 N ANISOU 1600 N ALA A 221 2200 2346 2238 5 -2 -14 N ATOM 1601 CA ALA A 221 42.463 -12.857 22.439 1.00 17.17 C ANISOU 1601 CA ALA A 221 2126 2248 2149 -47 11 -11 C ATOM 1602 C ALA A 221 42.705 -11.464 21.861 1.00 16.74 C ANISOU 1602 C ALA A 221 2057 2233 2070 -36 26 -19 C ATOM 1603 O ALA A 221 41.790 -10.823 21.349 1.00 17.44 O ANISOU 1603 O ALA A 221 2126 2314 2186 -74 19 41 O ATOM 1604 CB ALA A 221 42.358 -12.788 23.960 1.00 17.11 C ANISOU 1604 CB ALA A 221 2083 2265 2150 -115 78 -34 C ATOM 1605 N LEU A 222 43.951 -11.006 21.936 1.00 16.22 N ANISOU 1605 N LEU A 222 1999 2186 1977 -59 -8 -37 N ATOM 1606 CA LEU A 222 44.297 -9.681 21.442 1.00 16.43 C ANISOU 1606 CA LEU A 222 1998 2252 1992 -30 -54 8 C ATOM 1607 C LEU A 222 44.115 -9.654 19.930 1.00 16.37 C ANISOU 1607 C LEU A 222 2025 2225 1970 -26 -10 -31 C ATOM 1608 O LEU A 222 43.579 -8.686 19.390 1.00 16.23 O ANISOU 1608 O LEU A 222 2015 2233 1918 22 -16 0 O ATOM 1609 CB LEU A 222 45.732 -9.310 21.839 1.00 16.21 C ANISOU 1609 CB LEU A 222 1970 2191 1999 -130 9 1 C ATOM 1610 CG LEU A 222 45.886 -8.981 23.333 1.00 15.51 C ANISOU 1610 CG LEU A 222 1799 2162 1932 -36 -46 -46 C ATOM 1611 CD1 LEU A 222 47.330 -9.179 23.849 1.00 15.55 C ANISOU 1611 CD1 LEU A 222 1851 2193 1864 -85 -136 14 C ATOM 1612 CD2 LEU A 222 45.351 -7.586 23.646 1.00 15.88 C ANISOU 1612 CD2 LEU A 222 1960 2115 1958 -126 -95 20 C ATOM 1613 N ALA A 223 44.525 -10.734 19.267 1.00 16.66 N ANISOU 1613 N ALA A 223 2041 2254 2034 -20 -28 -28 N ATOM 1614 CA ALA A 223 44.404 -10.840 17.816 1.00 16.81 C ANISOU 1614 CA ALA A 223 2078 2267 2041 3 1 -75 C ATOM 1615 C ALA A 223 42.943 -10.802 17.338 1.00 16.83 C ANISOU 1615 C ALA A 223 2110 2209 2076 8 25 -57 C ATOM 1616 O ALA A 223 42.623 -10.126 16.351 1.00 17.50 O ANISOU 1616 O ALA A 223 2193 2319 2135 36 5 -78 O ATOM 1617 CB ALA A 223 45.109 -12.112 17.314 1.00 17.37 C ANISOU 1617 CB ALA A 223 2191 2325 2084 77 4 -93 C ATOM 1618 N VAL A 224 42.055 -11.515 18.029 1.00 16.82 N ANISOU 1618 N VAL A 224 2152 2151 2084 -5 29 -75 N ATOM 1619 CA AVAL A 224 40.648 -11.543 17.622 0.50 16.39 C ANISOU 1619 CA AVAL A 224 2096 2090 2039 -5 24 -67 C ATOM 1620 CA BVAL A 224 40.636 -11.533 17.616 0.50 16.15 C ANISOU 1620 CA BVAL A 224 2077 2063 1993 -4 22 -67 C ATOM 1621 C VAL A 224 39.977 -10.173 17.841 1.00 16.15 C ANISOU 1621 C VAL A 224 2075 2088 1973 -3 27 -58 C ATOM 1622 O VAL A 224 39.133 -9.746 17.059 1.00 15.76 O ANISOU 1622 O VAL A 224 2057 2042 1888 39 16 -128 O ATOM 1623 CB AVAL A 224 39.865 -12.682 18.318 0.50 16.58 C ANISOU 1623 CB AVAL A 224 2163 2071 2063 18 40 -48 C ATOM 1624 CB BVAL A 224 39.777 -12.690 18.250 0.50 16.21 C ANISOU 1624 CB BVAL A 224 2120 2037 1999 20 34 -49 C ATOM 1625 CG1AVAL A 224 38.578 -12.921 17.600 0.50 17.38 C ANISOU 1625 CG1AVAL A 224 2201 2154 2246 -10 -10 -37 C ATOM 1626 CG1BVAL A 224 40.362 -14.060 17.925 0.50 17.01 C ANISOU 1626 CG1BVAL A 224 2220 2126 2116 41 -1 -97 C ATOM 1627 CG2AVAL A 224 40.672 -13.976 18.320 0.50 17.35 C ANISOU 1627 CG2AVAL A 224 2241 2188 2160 34 38 -79 C ATOM 1628 CG2BVAL A 224 39.579 -12.509 19.758 0.50 15.83 C ANISOU 1628 CG2BVAL A 224 2097 1985 1930 9 18 -24 C ATOM 1629 N ILE A 225 40.375 -9.473 18.904 1.00 15.71 N ANISOU 1629 N ILE A 225 2038 2053 1875 -23 8 -32 N ATOM 1630 CA ILE A 225 39.828 -8.133 19.144 1.00 15.32 C ANISOU 1630 CA ILE A 225 1992 2033 1795 -44 55 -33 C ATOM 1631 C ILE A 225 40.300 -7.210 18.028 1.00 15.58 C ANISOU 1631 C ILE A 225 1951 2084 1882 -5 56 25 C ATOM 1632 O ILE A 225 39.512 -6.431 17.474 1.00 15.32 O ANISOU 1632 O ILE A 225 1854 2119 1846 -3 32 53 O ATOM 1633 CB ILE A 225 40.240 -7.577 20.529 1.00 15.30 C ANISOU 1633 CB ILE A 225 2005 2014 1794 -72 55 -3 C ATOM 1634 CG1 ILE A 225 39.628 -8.453 21.634 1.00 15.03 C ANISOU 1634 CG1 ILE A 225 1885 2157 1667 -72 129 -63 C ATOM 1635 CG2 ILE A 225 39.824 -6.108 20.653 1.00 15.81 C ANISOU 1635 CG2 ILE A 225 2047 2043 1915 -78 56 13 C ATOM 1636 CD1 ILE A 225 40.281 -8.254 23.013 1.00 15.92 C ANISOU 1636 CD1 ILE A 225 1921 2339 1786 -21 -82 23 C ATOM 1637 N ALA A 226 41.582 -7.312 17.675 1.00 16.15 N ANISOU 1637 N ALA A 226 2005 2189 1941 11 77 46 N ATOM 1638 CA ALA A 226 42.110 -6.467 16.603 1.00 16.33 C ANISOU 1638 CA ALA A 226 2019 2266 1920 14 118 74 C ATOM 1639 C ALA A 226 41.338 -6.692 15.294 1.00 16.72 C ANISOU 1639 C ALA A 226 2033 2352 1965 27 124 52 C ATOM 1640 O ALA A 226 41.000 -5.729 14.579 1.00 17.45 O ANISOU 1640 O ALA A 226 2162 2491 1974 67 164 82 O ATOM 1641 CB ALA A 226 43.588 -6.703 16.410 1.00 16.62 C ANISOU 1641 CB ALA A 226 2009 2340 1964 -2 107 100 C ATOM 1642 N GLU A 227 41.030 -7.951 15.006 1.00 16.80 N ANISOU 1642 N GLU A 227 2011 2403 1967 44 130 29 N ATOM 1643 CA GLU A 227 40.284 -8.299 13.797 1.00 17.73 C ANISOU 1643 CA GLU A 227 2185 2508 2043 57 70 -9 C ATOM 1644 C GLU A 227 38.875 -7.708 13.775 1.00 17.37 C ANISOU 1644 C GLU A 227 2133 2441 2025 46 52 14 C ATOM 1645 O GLU A 227 38.419 -7.216 12.741 1.00 17.25 O ANISOU 1645 O GLU A 227 2224 2454 1875 99 98 78 O ATOM 1646 CB GLU A 227 40.202 -9.813 13.614 1.00 18.20 C ANISOU 1646 CB GLU A 227 2231 2536 2146 29 56 0 C ATOM 1647 CG GLU A 227 39.827 -10.229 12.179 1.00 21.74 C ANISOU 1647 CG GLU A 227 2776 2970 2513 19 -32 -81 C ATOM 1648 CD GLU A 227 40.800 -9.708 11.100 1.00 25.43 C ANISOU 1648 CD GLU A 227 3182 3319 3159 16 108 -30 C ATOM 1649 OE1 GLU A 227 40.350 -9.553 9.940 1.00 26.67 O ANISOU 1649 OE1 GLU A 227 3501 3479 3153 -25 131 -40 O ATOM 1650 OE2 GLU A 227 41.993 -9.439 11.399 1.00 28.16 O ANISOU 1650 OE2 GLU A 227 3435 3578 3684 104 95 -270 O ATOM 1651 N ALA A 228 38.185 -7.764 14.909 1.00 17.15 N ANISOU 1651 N ALA A 228 2121 2415 1978 40 58 41 N ATOM 1652 CA ALA A 228 36.856 -7.153 15.015 1.00 16.54 C ANISOU 1652 CA ALA A 228 2028 2333 1921 30 68 70 C ATOM 1653 C ALA A 228 36.918 -5.623 14.865 1.00 16.58 C ANISOU 1653 C ALA A 228 2020 2326 1953 13 61 52 C ATOM 1654 O ALA A 228 36.065 -5.010 14.216 1.00 16.43 O ANISOU 1654 O ALA A 228 2019 2305 1918 -31 -24 161 O ATOM 1655 CB ALA A 228 36.198 -7.542 16.343 1.00 16.28 C ANISOU 1655 CB ALA A 228 1997 2341 1846 66 100 40 C ATOM 1656 N VAL A 229 37.932 -5.003 15.462 1.00 15.83 N ANISOU 1656 N VAL A 229 1938 2200 1874 -3 6 19 N ATOM 1657 CA VAL A 229 38.106 -3.552 15.350 1.00 15.96 C ANISOU 1657 CA VAL A 229 1987 2218 1858 -16 35 32 C ATOM 1658 C VAL A 229 38.275 -3.170 13.866 1.00 16.68 C ANISOU 1658 C VAL A 229 2155 2259 1923 -8 22 33 C ATOM 1659 O VAL A 229 37.646 -2.229 13.387 1.00 16.60 O ANISOU 1659 O VAL A 229 2150 2361 1794 -2 -15 19 O ATOM 1660 CB VAL A 229 39.281 -3.056 16.235 1.00 16.05 C ANISOU 1660 CB VAL A 229 2017 2143 1937 -29 29 22 C ATOM 1661 CG1 VAL A 229 39.705 -1.632 15.877 1.00 15.20 C ANISOU 1661 CG1 VAL A 229 1899 1977 1896 -78 128 73 C ATOM 1662 CG2 VAL A 229 38.894 -3.130 17.705 1.00 16.46 C ANISOU 1662 CG2 VAL A 229 2001 2334 1919 7 54 -30 C ATOM 1663 N LYS A 230 39.099 -3.934 13.150 1.00 17.35 N ANISOU 1663 N LYS A 230 2228 2380 1982 -38 47 32 N ATOM 1664 CA LYS A 230 39.293 -3.720 11.714 1.00 18.56 C ANISOU 1664 CA LYS A 230 2402 2551 2098 29 28 54 C ATOM 1665 C LYS A 230 38.006 -3.923 10.909 1.00 18.90 C ANISOU 1665 C LYS A 230 2474 2551 2155 15 16 72 C ATOM 1666 O LYS A 230 37.663 -3.089 10.039 1.00 18.64 O ANISOU 1666 O LYS A 230 2469 2612 1999 85 17 147 O ATOM 1667 CB LYS A 230 40.393 -4.641 11.176 1.00 19.16 C ANISOU 1667 CB LYS A 230 2496 2591 2191 79 64 -6 C ATOM 1668 CG LYS A 230 40.868 -4.213 9.803 1.00 21.68 C ANISOU 1668 CG LYS A 230 2832 2971 2433 61 31 86 C ATOM 1669 CD LYS A 230 41.930 -5.145 9.276 1.00 26.16 C ANISOU 1669 CD LYS A 230 3329 3480 3129 158 80 -95 C ATOM 1670 CE LYS A 230 42.944 -4.363 8.451 1.00 28.13 C ANISOU 1670 CE LYS A 230 3489 3654 3544 -89 90 -14 C ATOM 1671 NZ LYS A 230 43.954 -3.644 9.316 1.00 30.59 N ANISOU 1671 NZ LYS A 230 3886 4056 3678 -32 81 -168 N ATOM 1672 N ALA A 231 37.305 -5.022 11.207 1.00 18.63 N ANISOU 1672 N ALA A 231 2461 2553 2061 -34 33 60 N ATOM 1673 CA ALA A 231 36.031 -5.350 10.563 1.00 19.22 C ANISOU 1673 CA ALA A 231 2524 2595 2182 -74 -6 90 C ATOM 1674 C ALA A 231 35.024 -4.205 10.677 1.00 19.50 C ANISOU 1674 C ALA A 231 2583 2624 2202 -65 -39 82 C ATOM 1675 O ALA A 231 34.277 -3.907 9.730 1.00 20.05 O ANISOU 1675 O ALA A 231 2619 2771 2226 -71 -101 89 O ATOM 1676 CB ALA A 231 35.452 -6.629 11.167 1.00 19.64 C ANISOU 1676 CB ALA A 231 2632 2590 2238 -55 -5 103 C ATOM 1677 N ALA A 232 35.030 -3.553 11.834 1.00 19.01 N ANISOU 1677 N ALA A 232 2571 2569 2080 -46 -35 72 N ATOM 1678 CA ALA A 232 34.126 -2.451 12.127 1.00 18.87 C ANISOU 1678 CA ALA A 232 2561 2558 2050 -45 -20 48 C ATOM 1679 C ALA A 232 34.570 -1.162 11.434 1.00 18.58 C ANISOU 1679 C ALA A 232 2524 2524 2010 -7 -20 81 C ATOM 1680 O ALA A 232 33.863 -0.153 11.485 1.00 18.46 O ANISOU 1680 O ALA A 232 2554 2494 1966 -22 -9 109 O ATOM 1681 CB ALA A 232 34.039 -2.239 13.642 1.00 18.99 C ANISOU 1681 CB ALA A 232 2593 2607 2012 -60 -10 18 C ATOM 1682 N GLY A 233 35.759 -1.198 10.830 1.00 18.97 N ANISOU 1682 N GLY A 233 2534 2562 2112 -46 -50 132 N ATOM 1683 CA GLY A 233 36.302 -0.060 10.098 1.00 19.48 C ANISOU 1683 CA GLY A 233 2572 2625 2202 -16 -17 160 C ATOM 1684 C GLY A 233 37.018 0.972 10.938 1.00 19.37 C ANISOU 1684 C GLY A 233 2528 2571 2261 -7 15 137 C ATOM 1685 O GLY A 233 37.158 2.126 10.529 1.00 20.38 O ANISOU 1685 O GLY A 233 2649 2743 2348 10 26 154 O ATOM 1686 N TYR A 234 37.474 0.564 12.121 1.00 18.94 N ANISOU 1686 N TYR A 234 2356 2606 2234 16 10 93 N ATOM 1687 CA TYR A 234 38.210 1.457 13.004 1.00 18.89 C ANISOU 1687 CA TYR A 234 2278 2613 2284 23 32 68 C ATOM 1688 C TYR A 234 39.690 1.125 13.015 1.00 19.04 C ANISOU 1688 C TYR A 234 2296 2625 2313 29 63 63 C ATOM 1689 O TYR A 234 40.095 0.017 12.650 1.00 19.15 O ANISOU 1689 O TYR A 234 2243 2637 2393 13 38 26 O ATOM 1690 CB TYR A 234 37.618 1.442 14.422 1.00 18.44 C ANISOU 1690 CB TYR A 234 2241 2546 2218 29 28 85 C ATOM 1691 CG TYR A 234 36.201 1.964 14.420 1.00 17.63 C ANISOU 1691 CG TYR A 234 2139 2413 2144 -3 46 79 C ATOM 1692 CD1 TYR A 234 35.945 3.307 14.111 1.00 18.18 C ANISOU 1692 CD1 TYR A 234 2234 2457 2217 37 33 69 C ATOM 1693 CD2 TYR A 234 35.113 1.122 14.690 1.00 17.75 C ANISOU 1693 CD2 TYR A 234 2264 2381 2099 56 19 196 C ATOM 1694 CE1 TYR A 234 34.664 3.806 14.065 1.00 17.56 C ANISOU 1694 CE1 TYR A 234 2192 2356 2123 -9 80 75 C ATOM 1695 CE2 TYR A 234 33.807 1.618 14.646 1.00 17.06 C ANISOU 1695 CE2 TYR A 234 2137 2342 2001 4 95 143 C ATOM 1696 CZ TYR A 234 33.600 2.965 14.335 1.00 17.82 C ANISOU 1696 CZ TYR A 234 2193 2353 2223 -6 3 20 C ATOM 1697 OH TYR A 234 32.338 3.495 14.286 1.00 18.39 O ANISOU 1697 OH TYR A 234 2204 2581 2199 64 12 -7 O ATOM 1698 N GLU A 235 40.503 2.089 13.436 1.00 19.13 N ANISOU 1698 N GLU A 235 2288 2657 2321 39 36 46 N ATOM 1699 CA GLU A 235 41.948 1.903 13.491 1.00 19.48 C ANISOU 1699 CA GLU A 235 2344 2713 2345 14 89 56 C ATOM 1700 C GLU A 235 42.417 1.655 14.921 1.00 19.30 C ANISOU 1700 C GLU A 235 2349 2648 2334 -4 87 35 C ATOM 1701 O GLU A 235 42.369 2.550 15.764 1.00 19.20 O ANISOU 1701 O GLU A 235 2397 2615 2281 33 150 47 O ATOM 1702 CB GLU A 235 42.667 3.119 12.905 1.00 19.78 C ANISOU 1702 CB GLU A 235 2415 2719 2381 0 108 63 C ATOM 1703 N LEU A 236 42.871 0.434 15.186 1.00 19.39 N ANISOU 1703 N LEU A 236 2385 2646 2335 -17 110 35 N ATOM 1704 CA LEU A 236 43.516 0.115 16.454 1.00 20.16 C ANISOU 1704 CA LEU A 236 2525 2702 2433 5 99 76 C ATOM 1705 C LEU A 236 44.618 1.117 16.779 1.00 20.39 C ANISOU 1705 C LEU A 236 2568 2742 2435 -13 72 46 C ATOM 1706 O LEU A 236 45.500 1.373 15.959 1.00 20.94 O ANISOU 1706 O LEU A 236 2567 2901 2487 -65 123 39 O ATOM 1707 CB LEU A 236 44.088 -1.304 16.421 1.00 20.70 C ANISOU 1707 CB LEU A 236 2618 2781 2466 26 99 71 C ATOM 1708 CG LEU A 236 44.191 -2.024 17.767 1.00 20.69 C ANISOU 1708 CG LEU A 236 2658 2751 2451 51 50 140 C ATOM 1709 CD1 LEU A 236 42.836 -2.070 18.457 1.00 21.05 C ANISOU 1709 CD1 LEU A 236 2766 2751 2481 74 67 159 C ATOM 1710 CD2 LEU A 236 44.751 -3.426 17.585 1.00 21.17 C ANISOU 1710 CD2 LEU A 236 2728 2787 2529 41 82 89 C ATOM 1711 N GLY A 237 44.561 1.682 17.981 1.00 20.40 N ANISOU 1711 N GLY A 237 2628 2709 2414 13 64 102 N ATOM 1712 CA GLY A 237 45.578 2.616 18.435 1.00 20.86 C ANISOU 1712 CA GLY A 237 2745 2766 2415 -30 52 78 C ATOM 1713 C GLY A 237 45.193 4.071 18.273 1.00 21.94 C ANISOU 1713 C GLY A 237 2948 2819 2568 -83 18 58 C ATOM 1714 O GLY A 237 45.564 4.897 19.100 1.00 23.83 O ANISOU 1714 O GLY A 237 3344 2987 2721 -90 1 55 O ATOM 1715 N LYS A 238 44.472 4.393 17.199 1.00 21.51 N ANISOU 1715 N LYS A 238 2815 2782 2575 -73 39 91 N ATOM 1716 CA LYS A 238 43.980 5.745 16.980 1.00 21.43 C ANISOU 1716 CA LYS A 238 2767 2822 2552 -45 41 91 C ATOM 1717 C LYS A 238 42.526 5.870 17.443 1.00 20.38 C ANISOU 1717 C LYS A 238 2696 2641 2404 -61 51 141 C ATOM 1718 O LYS A 238 42.197 6.724 18.272 1.00 20.89 O ANISOU 1718 O LYS A 238 2764 2662 2510 -111 110 114 O ATOM 1719 CB LYS A 238 44.098 6.127 15.500 1.00 22.24 C ANISOU 1719 CB LYS A 238 2864 2924 2661 -78 93 106 C ATOM 1720 CG LYS A 238 43.679 7.547 15.182 1.00 25.18 C ANISOU 1720 CG LYS A 238 3149 3230 3186 53 50 18 C ATOM 1721 CD LYS A 238 43.015 7.591 13.824 1.00 29.38 C ANISOU 1721 CD LYS A 238 3838 3824 3499 26 -70 29 C ATOM 1722 CE LYS A 238 41.761 8.446 13.861 1.00 31.87 C ANISOU 1722 CE LYS A 238 4000 4074 4035 85 2 -4 C ATOM 1723 NZ LYS A 238 40.689 7.932 12.958 1.00 31.98 N ANISOU 1723 NZ LYS A 238 4097 4086 3966 -127 -113 -35 N ATOM 1724 N ASP A 239 41.661 5.020 16.899 1.00 19.24 N ANISOU 1724 N ASP A 239 2571 2490 2248 -36 29 180 N ATOM 1725 CA ASP A 239 40.243 5.071 17.216 1.00 17.86 C ANISOU 1725 CA ASP A 239 2402 2283 2101 -27 51 198 C ATOM 1726 C ASP A 239 39.965 4.329 18.518 1.00 16.99 C ANISOU 1726 C ASP A 239 2277 2197 1981 -6 52 210 C ATOM 1727 O ASP A 239 39.129 4.756 19.331 1.00 16.87 O ANISOU 1727 O ASP A 239 2258 2114 2036 -44 71 302 O ATOM 1728 CB ASP A 239 39.414 4.417 16.108 1.00 18.47 C ANISOU 1728 CB ASP A 239 2480 2389 2145 15 5 155 C ATOM 1729 CG ASP A 239 39.369 5.239 14.836 1.00 19.68 C ANISOU 1729 CG ASP A 239 2696 2468 2313 -42 -20 162 C ATOM 1730 OD1 ASP A 239 39.340 6.480 14.926 1.00 24.01 O ANISOU 1730 OD1 ASP A 239 3476 2876 2770 152 -85 83 O ATOM 1731 OD2 ASP A 239 39.354 4.634 13.740 1.00 20.01 O ANISOU 1731 OD2 ASP A 239 2789 2587 2224 -46 0 314 O ATOM 1732 N ILE A 240 40.640 3.198 18.682 1.00 16.19 N ANISOU 1732 N ILE A 240 2131 2146 1873 -75 59 209 N ATOM 1733 CA ILE A 240 40.367 2.297 19.809 1.00 15.73 C ANISOU 1733 CA ILE A 240 2053 2081 1842 -26 19 238 C ATOM 1734 C ILE A 240 41.661 1.825 20.444 1.00 15.42 C ANISOU 1734 C ILE A 240 1995 2053 1808 -36 58 199 C ATOM 1735 O ILE A 240 42.541 1.340 19.753 1.00 15.82 O ANISOU 1735 O ILE A 240 2088 2143 1779 21 86 305 O ATOM 1736 CB ILE A 240 39.526 1.089 19.348 1.00 16.03 C ANISOU 1736 CB ILE A 240 2079 2138 1871 -31 104 224 C ATOM 1737 CG1 ILE A 240 38.143 1.586 18.904 1.00 17.81 C ANISOU 1737 CG1 ILE A 240 2290 2363 2114 -25 -50 214 C ATOM 1738 CG2 ILE A 240 39.447 0.023 20.461 1.00 16.59 C ANISOU 1738 CG2 ILE A 240 2259 2100 1941 -50 24 178 C ATOM 1739 CD1 ILE A 240 37.234 0.539 18.363 1.00 21.05 C ANISOU 1739 CD1 ILE A 240 2638 2701 2658 -168 -95 111 C ATOM 1740 N THR A 241 41.782 2.009 21.758 1.00 14.11 N ANISOU 1740 N THR A 241 1765 1967 1630 -42 76 257 N ATOM 1741 CA THR A 241 42.894 1.430 22.504 1.00 13.53 C ANISOU 1741 CA THR A 241 1695 1844 1600 -71 55 250 C ATOM 1742 C THR A 241 42.375 0.272 23.345 1.00 13.40 C ANISOU 1742 C THR A 241 1607 1882 1599 -70 57 263 C ATOM 1743 O THR A 241 41.157 0.019 23.397 1.00 12.79 O ANISOU 1743 O THR A 241 1439 1899 1518 -60 56 286 O ATOM 1744 CB THR A 241 43.592 2.450 23.392 1.00 13.24 C ANISOU 1744 CB THR A 241 1685 1792 1553 -71 121 234 C ATOM 1745 OG1 THR A 241 42.624 3.061 24.261 1.00 13.49 O ANISOU 1745 OG1 THR A 241 1665 1970 1490 0 -31 50 O ATOM 1746 CG2 THR A 241 44.273 3.541 22.511 1.00 13.80 C ANISOU 1746 CG2 THR A 241 1855 1728 1658 -101 81 261 C ATOM 1747 N LEU A 242 43.304 -0.439 23.976 1.00 12.97 N ANISOU 1747 N LEU A 242 1597 1771 1560 -22 64 271 N ATOM 1748 CA LEU A 242 42.968 -1.650 24.728 1.00 13.13 C ANISOU 1748 CA LEU A 242 1620 1772 1593 -73 32 183 C ATOM 1749 C LEU A 242 43.314 -1.482 26.190 1.00 12.93 C ANISOU 1749 C LEU A 242 1616 1757 1539 -77 25 216 C ATOM 1750 O LEU A 242 44.292 -0.828 26.547 1.00 13.26 O ANISOU 1750 O LEU A 242 1661 1850 1526 -121 51 279 O ATOM 1751 CB LEU A 242 43.695 -2.869 24.152 1.00 13.71 C ANISOU 1751 CB LEU A 242 1718 1816 1674 -45 7 154 C ATOM 1752 CG LEU A 242 43.431 -3.184 22.671 1.00 14.37 C ANISOU 1752 CG LEU A 242 1823 1846 1790 -48 -30 68 C ATOM 1753 CD1 LEU A 242 44.337 -4.301 22.159 1.00 17.08 C ANISOU 1753 CD1 LEU A 242 2179 2207 2102 13 47 9 C ATOM 1754 CD2 LEU A 242 41.943 -3.512 22.452 1.00 15.45 C ANISOU 1754 CD2 LEU A 242 1777 2148 1943 -163 92 58 C ATOM 1755 N ALA A 243 42.477 -2.062 27.043 1.00 12.51 N ANISOU 1755 N ALA A 243 1474 1780 1496 -101 53 192 N ATOM 1756 CA ALA A 243 42.728 -2.092 28.465 1.00 12.61 C ANISOU 1756 CA ALA A 243 1619 1683 1486 -65 33 162 C ATOM 1757 C ALA A 243 42.582 -3.547 28.911 1.00 12.65 C ANISOU 1757 C ALA A 243 1621 1675 1509 -76 79 160 C ATOM 1758 O ALA A 243 41.842 -4.308 28.315 1.00 12.08 O ANISOU 1758 O ALA A 243 1682 1528 1378 -51 16 235 O ATOM 1759 CB ALA A 243 41.741 -1.199 29.191 1.00 12.57 C ANISOU 1759 CB ALA A 243 1555 1736 1484 -52 21 84 C ATOM 1760 N MET A 244 43.303 -3.938 29.945 1.00 12.75 N ANISOU 1760 N MET A 244 1634 1714 1496 -96 65 193 N ATOM 1761 CA MET A 244 43.201 -5.316 30.422 1.00 15.31 C ANISOU 1761 CA MET A 244 1986 2003 1827 -65 74 156 C ATOM 1762 C MET A 244 43.139 -5.341 31.934 1.00 14.02 C ANISOU 1762 C MET A 244 1806 1861 1659 -75 35 176 C ATOM 1763 O MET A 244 43.591 -4.403 32.590 1.00 12.90 O ANISOU 1763 O MET A 244 1680 1748 1472 -149 33 265 O ATOM 1764 CB MET A 244 44.386 -6.160 29.928 1.00 15.60 C ANISOU 1764 CB MET A 244 1982 2047 1898 -50 82 141 C ATOM 1765 CG MET A 244 45.743 -5.605 30.317 1.00 18.23 C ANISOU 1765 CG MET A 244 2289 2390 2247 -11 98 100 C ATOM 1766 SD MET A 244 47.129 -6.492 29.572 1.00 22.38 S ANISOU 1766 SD MET A 244 2666 3051 2785 127 301 142 S ATOM 1767 CE MET A 244 46.314 -7.449 28.311 1.00 19.94 C ANISOU 1767 CE MET A 244 2380 2542 2652 81 266 114 C ATOM 1768 N ASP A 245 42.548 -6.417 32.462 1.00 13.53 N ANISOU 1768 N ASP A 245 1732 1858 1549 -173 44 204 N ATOM 1769 CA ASP A 245 42.578 -6.730 33.895 1.00 14.05 C ANISOU 1769 CA ASP A 245 1773 2002 1562 -93 -31 141 C ATOM 1770 C ASP A 245 43.246 -8.097 34.015 1.00 14.72 C ANISOU 1770 C ASP A 245 1916 2012 1665 -146 13 120 C ATOM 1771 O ASP A 245 42.689 -9.114 33.585 1.00 14.50 O ANISOU 1771 O ASP A 245 1947 1977 1583 -162 -96 76 O ATOM 1772 CB ASP A 245 41.146 -6.762 34.470 1.00 14.52 C ANISOU 1772 CB ASP A 245 1839 2113 1564 -194 -21 144 C ATOM 1773 CG ASP A 245 41.084 -7.219 35.930 1.00 16.67 C ANISOU 1773 CG ASP A 245 1994 2488 1851 -74 -3 173 C ATOM 1774 OD1 ASP A 245 42.139 -7.392 36.582 1.00 18.56 O ANISOU 1774 OD1 ASP A 245 2231 2693 2128 -166 -155 168 O ATOM 1775 OD2 ASP A 245 39.947 -7.402 36.426 1.00 18.44 O ANISOU 1775 OD2 ASP A 245 2154 2787 2062 -255 -136 102 O ATOM 1776 N CYS A 246 44.434 -8.121 34.613 1.00 14.54 N ANISOU 1776 N CYS A 246 1893 1977 1652 -113 13 140 N ATOM 1777 CA CYS A 246 45.180 -9.368 34.757 1.00 16.03 C ANISOU 1777 CA CYS A 246 2094 2124 1872 -171 59 193 C ATOM 1778 C CYS A 246 44.596 -10.258 35.842 1.00 16.29 C ANISOU 1778 C CYS A 246 2160 2081 1946 -172 37 166 C ATOM 1779 O CYS A 246 44.742 -11.478 35.780 1.00 17.79 O ANISOU 1779 O CYS A 246 2405 2199 2154 -173 117 49 O ATOM 1780 CB CYS A 246 46.631 -9.083 35.098 1.00 15.55 C ANISOU 1780 CB CYS A 246 2033 2071 1801 -142 54 253 C ATOM 1781 SG CYS A 246 47.514 -8.218 33.805 1.00 18.26 S ANISOU 1781 SG CYS A 246 2321 2616 1998 -403 248 550 S ATOM 1782 N ALA A 247 43.995 -9.634 36.855 1.00 16.01 N ANISOU 1782 N ALA A 247 2031 2108 1943 -186 58 197 N ATOM 1783 CA ALA A 247 43.622 -10.332 38.094 1.00 16.82 C ANISOU 1783 CA ALA A 247 2159 2243 1987 -169 -4 214 C ATOM 1784 C ALA A 247 44.763 -11.267 38.523 1.00 16.97 C ANISOU 1784 C ALA A 247 2256 2172 2018 -130 14 175 C ATOM 1785 O ALA A 247 44.574 -12.471 38.714 1.00 17.23 O ANISOU 1785 O ALA A 247 2344 2230 1970 -153 33 243 O ATOM 1786 CB ALA A 247 42.308 -11.099 37.904 1.00 16.62 C ANISOU 1786 CB ALA A 247 2150 2204 1961 -192 -26 166 C ATOM 1787 N ALA A 248 45.958 -10.687 38.660 1.00 16.88 N ANISOU 1787 N ALA A 248 2213 2176 2022 -122 17 233 N ATOM 1788 CA ALA A 248 47.191 -11.445 38.806 1.00 17.62 C ANISOU 1788 CA ALA A 248 2330 2184 2181 -98 39 234 C ATOM 1789 C ALA A 248 47.255 -12.264 40.100 1.00 18.07 C ANISOU 1789 C ALA A 248 2394 2268 2201 -65 -10 242 C ATOM 1790 O ALA A 248 48.059 -13.195 40.191 1.00 18.79 O ANISOU 1790 O ALA A 248 2648 2209 2280 -124 30 276 O ATOM 1791 CB ALA A 248 48.412 -10.523 38.679 1.00 17.64 C ANISOU 1791 CB ALA A 248 2227 2240 2233 -35 12 180 C ATOM 1792 N SER A 249 46.429 -11.911 41.085 1.00 18.80 N ANISOU 1792 N SER A 249 2538 2321 2283 -126 -13 267 N ATOM 1793 CA SER A 249 46.291 -12.753 42.297 1.00 20.32 C ANISOU 1793 CA SER A 249 2726 2571 2423 -95 -37 234 C ATOM 1794 C SER A 249 45.878 -14.180 41.951 1.00 21.13 C ANISOU 1794 C SER A 249 2822 2637 2567 -88 -52 183 C ATOM 1795 O SER A 249 46.213 -15.131 42.683 1.00 21.24 O ANISOU 1795 O SER A 249 2912 2656 2500 -111 -41 279 O ATOM 1796 CB SER A 249 45.313 -12.146 43.316 1.00 20.83 C ANISOU 1796 CB SER A 249 2693 2700 2519 -105 -23 219 C ATOM 1797 OG SER A 249 43.964 -12.242 42.894 1.00 22.55 O ANISOU 1797 OG SER A 249 2774 3060 2733 -215 11 373 O ATOM 1798 N GLU A 250 45.170 -14.338 40.833 1.00 21.96 N ANISOU 1798 N GLU A 250 2974 2733 2637 -97 -58 150 N ATOM 1799 CA GLU A 250 44.675 -15.665 40.446 1.00 23.07 C ANISOU 1799 CA GLU A 250 3096 2841 2826 -100 -57 125 C ATOM 1800 C GLU A 250 45.781 -16.607 39.986 1.00 24.32 C ANISOU 1800 C GLU A 250 3269 2967 3003 -62 -46 112 C ATOM 1801 O GLU A 250 45.584 -17.824 39.991 1.00 25.40 O ANISOU 1801 O GLU A 250 3490 2988 3169 -4 -14 109 O ATOM 1802 CB GLU A 250 43.543 -15.580 39.401 1.00 22.49 C ANISOU 1802 CB GLU A 250 2989 2783 2771 -132 -52 132 C ATOM 1803 CG GLU A 250 42.381 -14.686 39.804 1.00 23.12 C ANISOU 1803 CG GLU A 250 2984 2920 2877 -153 -41 56 C ATOM 1804 CD GLU A 250 41.559 -15.217 40.981 1.00 23.61 C ANISOU 1804 CD GLU A 250 3035 2992 2942 -52 -40 109 C ATOM 1805 OE1 GLU A 250 41.856 -16.315 41.514 1.00 24.51 O ANISOU 1805 OE1 GLU A 250 3171 3147 2995 -216 -36 261 O ATOM 1806 OE2 GLU A 250 40.612 -14.511 41.380 1.00 25.32 O ANISOU 1806 OE2 GLU A 250 3236 3355 3028 -122 47 148 O ATOM 1807 N PHE A 251 46.939 -16.068 39.602 1.00 25.05 N ANISOU 1807 N PHE A 251 3349 3075 3091 -11 16 127 N ATOM 1808 CA PHE A 251 48.066 -16.939 39.267 1.00 26.43 C ANISOU 1808 CA PHE A 251 3481 3232 3330 -20 38 129 C ATOM 1809 C PHE A 251 49.327 -16.774 40.141 1.00 26.64 C ANISOU 1809 C PHE A 251 3478 3230 3411 -30 60 118 C ATOM 1810 O PHE A 251 50.399 -17.271 39.807 1.00 27.37 O ANISOU 1810 O PHE A 251 3565 3289 3543 -20 55 93 O ATOM 1811 CB PHE A 251 48.334 -17.021 37.743 1.00 26.89 C ANISOU 1811 CB PHE A 251 3532 3294 3389 -5 51 107 C ATOM 1812 CG PHE A 251 48.145 -15.715 36.982 1.00 27.19 C ANISOU 1812 CG PHE A 251 3554 3340 3436 -10 51 125 C ATOM 1813 CD1 PHE A 251 47.054 -15.533 36.129 1.00 27.46 C ANISOU 1813 CD1 PHE A 251 3637 3302 3493 -66 28 100 C ATOM 1814 CD2 PHE A 251 49.080 -14.695 37.093 1.00 28.12 C ANISOU 1814 CD2 PHE A 251 3651 3504 3529 -34 7 -16 C ATOM 1815 CE1 PHE A 251 46.893 -14.328 35.408 1.00 27.46 C ANISOU 1815 CE1 PHE A 251 3525 3487 3419 -1 -75 28 C ATOM 1816 CE2 PHE A 251 48.930 -13.505 36.393 1.00 26.75 C ANISOU 1816 CE2 PHE A 251 3516 3287 3360 -41 -6 67 C ATOM 1817 CZ PHE A 251 47.837 -13.318 35.551 1.00 26.30 C ANISOU 1817 CZ PHE A 251 3427 3229 3333 0 13 96 C ATOM 1818 N TYR A 252 49.154 -16.135 41.297 1.00 26.85 N ANISOU 1818 N TYR A 252 3526 3263 3410 -17 48 145 N ATOM 1819 CA TYR A 252 50.217 -15.942 42.278 1.00 27.54 C ANISOU 1819 CA TYR A 252 3581 3381 3502 -13 53 140 C ATOM 1820 C TYR A 252 50.349 -17.178 43.159 1.00 28.45 C ANISOU 1820 C TYR A 252 3695 3503 3609 21 35 155 C ATOM 1821 O TYR A 252 49.386 -17.581 43.819 1.00 28.06 O ANISOU 1821 O TYR A 252 3639 3413 3610 27 43 184 O ATOM 1822 CB TYR A 252 49.887 -14.733 43.147 1.00 27.17 C ANISOU 1822 CB TYR A 252 3528 3363 3431 -23 26 131 C ATOM 1823 CG TYR A 252 51.035 -14.101 43.911 1.00 26.65 C ANISOU 1823 CG TYR A 252 3483 3286 3356 10 31 150 C ATOM 1824 CD1 TYR A 252 52.276 -13.878 43.316 1.00 26.09 C ANISOU 1824 CD1 TYR A 252 3426 3223 3262 29 -23 132 C ATOM 1825 CD2 TYR A 252 50.851 -13.666 45.219 1.00 26.78 C ANISOU 1825 CD2 TYR A 252 3530 3255 3391 26 -21 95 C ATOM 1826 CE1 TYR A 252 53.309 -13.262 44.018 1.00 25.96 C ANISOU 1826 CE1 TYR A 252 3393 3222 3248 32 -17 135 C ATOM 1827 CE2 TYR A 252 51.874 -13.049 45.928 1.00 26.57 C ANISOU 1827 CE2 TYR A 252 3425 3279 3392 1 17 131 C ATOM 1828 CZ TYR A 252 53.095 -12.845 45.323 1.00 27.07 C ANISOU 1828 CZ TYR A 252 3504 3348 3432 64 -11 117 C ATOM 1829 OH TYR A 252 54.093 -12.225 46.035 1.00 27.54 O ANISOU 1829 OH TYR A 252 3532 3480 3450 -71 -47 123 O ATOM 1830 N LYS A 253 51.540 -17.771 43.161 1.00 29.87 N ANISOU 1830 N LYS A 253 3857 3696 3793 23 33 146 N ATOM 1831 CA LYS A 253 51.828 -18.922 44.016 1.00 31.53 C ANISOU 1831 CA LYS A 253 4051 3922 4005 45 15 127 C ATOM 1832 C LYS A 253 53.302 -18.956 44.395 1.00 32.07 C ANISOU 1832 C LYS A 253 4095 4006 4083 47 22 96 C ATOM 1833 O LYS A 253 54.179 -18.926 43.522 1.00 32.34 O ANISOU 1833 O LYS A 253 4142 4026 4118 57 27 131 O ATOM 1834 CB LYS A 253 51.418 -20.224 43.333 1.00 31.64 C ANISOU 1834 CB LYS A 253 4091 3937 3993 41 13 94 C ATOM 1835 CG LYS A 253 51.642 -21.458 44.200 1.00 33.30 C ANISOU 1835 CG LYS A 253 4413 3999 4241 32 -76 91 C ATOM 1836 CD LYS A 253 51.347 -22.745 43.450 1.00 37.78 C ANISOU 1836 CD LYS A 253 4577 4947 4829 -90 53 -226 C ATOM 1837 CE LYS A 253 51.684 -23.977 44.300 1.00 30.59 C ANISOU 1837 CE LYS A 253 3902 4446 3272 131 1005 488 C ATOM 1838 NZ LYS A 253 50.918 -24.050 45.588 1.00 42.86 N ANISOU 1838 NZ LYS A 253 5740 4666 5879 53 -790 -23 N ATOM 1839 N ASP A 254 53.556 -19.018 45.702 1.00 32.65 N ANISOU 1839 N ASP A 254 4167 4096 4141 28 20 87 N ATOM 1840 CA ASP A 254 54.908 -19.051 46.272 1.00 33.35 C ANISOU 1840 CA ASP A 254 4249 4189 4231 1 22 69 C ATOM 1841 C ASP A 254 55.762 -17.867 45.839 1.00 33.31 C ANISOU 1841 C ASP A 254 4215 4206 4233 6 37 79 C ATOM 1842 O ASP A 254 56.969 -18.007 45.609 1.00 34.05 O ANISOU 1842 O ASP A 254 4301 4329 4306 15 49 95 O ATOM 1843 CB ASP A 254 55.606 -20.382 45.967 1.00 33.81 C ANISOU 1843 CB ASP A 254 4317 4242 4284 -2 22 46 C ATOM 1844 CG ASP A 254 54.911 -21.557 46.614 1.00 35.31 C ANISOU 1844 CG ASP A 254 4550 4396 4468 -16 25 61 C ATOM 1845 OD1 ASP A 254 54.629 -21.482 47.831 1.00 35.71 O ANISOU 1845 OD1 ASP A 254 4661 4511 4394 32 67 74 O ATOM 1846 OD2 ASP A 254 54.642 -22.551 45.904 1.00 36.43 O ANISOU 1846 OD2 ASP A 254 4807 4505 4527 -31 -9 -41 O ATOM 1847 N GLY A 255 55.122 -16.702 45.742 1.00 32.74 N ANISOU 1847 N GLY A 255 4165 4124 4151 0 28 90 N ATOM 1848 CA GLY A 255 55.803 -15.453 45.397 1.00 31.97 C ANISOU 1848 CA GLY A 255 4051 4035 4058 5 21 82 C ATOM 1849 C GLY A 255 56.081 -15.277 43.915 1.00 31.26 C ANISOU 1849 C GLY A 255 3960 3928 3988 19 -3 75 C ATOM 1850 O GLY A 255 56.754 -14.322 43.518 1.00 31.21 O ANISOU 1850 O GLY A 255 3942 3935 3982 21 27 129 O ATOM 1851 N LYS A 256 55.562 -16.192 43.098 1.00 30.50 N ANISOU 1851 N LYS A 256 3898 3815 3876 50 6 79 N ATOM 1852 CA LYS A 256 55.727 -16.122 41.646 1.00 29.64 C ANISOU 1852 CA LYS A 256 3796 3683 3780 38 27 96 C ATOM 1853 C LYS A 256 54.383 -16.132 40.908 1.00 29.04 C ANISOU 1853 C LYS A 256 3729 3596 3708 41 35 122 C ATOM 1854 O LYS A 256 53.347 -16.476 41.489 1.00 28.80 O ANISOU 1854 O LYS A 256 3705 3526 3710 56 48 183 O ATOM 1855 CB LYS A 256 56.626 -17.262 41.155 1.00 29.83 C ANISOU 1855 CB LYS A 256 3862 3711 3758 19 35 67 C ATOM 1856 N TYR A 257 54.412 -15.747 39.631 1.00 27.98 N ANISOU 1856 N TYR A 257 3609 3447 3573 32 30 98 N ATOM 1857 CA TYR A 257 53.217 -15.697 38.780 1.00 27.02 C ANISOU 1857 CA TYR A 257 3515 3310 3441 36 49 129 C ATOM 1858 C TYR A 257 53.264 -16.799 37.743 1.00 28.61 C ANISOU 1858 C TYR A 257 3715 3516 3638 31 37 92 C ATOM 1859 O TYR A 257 54.059 -16.763 36.800 1.00 28.94 O ANISOU 1859 O TYR A 257 3757 3524 3715 31 78 113 O ATOM 1860 CB TYR A 257 53.053 -14.308 38.135 1.00 24.75 C ANISOU 1860 CB TYR A 257 3227 3071 3106 40 49 125 C ATOM 1861 CG TYR A 257 52.902 -13.246 39.190 1.00 21.00 C ANISOU 1861 CG TYR A 257 2794 2593 2590 19 18 264 C ATOM 1862 CD1 TYR A 257 51.638 -12.884 39.659 1.00 18.08 C ANISOU 1862 CD1 TYR A 257 2454 2130 2286 61 -81 290 C ATOM 1863 CD2 TYR A 257 54.024 -12.655 39.785 1.00 19.68 C ANISOU 1863 CD2 TYR A 257 2722 2306 2448 -48 89 246 C ATOM 1864 CE1 TYR A 257 51.492 -11.939 40.658 1.00 18.25 C ANISOU 1864 CE1 TYR A 257 2530 2237 2165 -8 -4 388 C ATOM 1865 CE2 TYR A 257 53.889 -11.708 40.808 1.00 18.37 C ANISOU 1865 CE2 TYR A 257 2573 2109 2297 -34 63 333 C ATOM 1866 CZ TYR A 257 52.614 -11.355 41.233 1.00 19.07 C ANISOU 1866 CZ TYR A 257 2499 2284 2460 -13 -2 341 C ATOM 1867 OH TYR A 257 52.448 -10.428 42.236 1.00 19.11 O ANISOU 1867 OH TYR A 257 2514 2419 2328 2 -36 504 O ATOM 1868 N VAL A 258 52.409 -17.792 37.944 1.00 30.38 N ANISOU 1868 N VAL A 258 3896 3760 3884 9 20 97 N ATOM 1869 CA VAL A 258 52.389 -18.975 37.111 1.00 32.03 C ANISOU 1869 CA VAL A 258 4130 3939 4099 10 25 49 C ATOM 1870 C VAL A 258 51.251 -18.856 36.111 1.00 33.06 C ANISOU 1870 C VAL A 258 4243 4081 4236 -1 7 42 C ATOM 1871 O VAL A 258 50.088 -18.789 36.499 1.00 33.36 O ANISOU 1871 O VAL A 258 4298 4114 4262 37 42 39 O ATOM 1872 CB VAL A 258 52.226 -20.258 37.972 1.00 31.90 C ANISOU 1872 CB VAL A 258 4094 3951 4073 -6 21 73 C ATOM 1873 CG1 VAL A 258 52.242 -21.498 37.090 1.00 32.53 C ANISOU 1873 CG1 VAL A 258 4188 3999 4170 7 6 20 C ATOM 1874 CG2 VAL A 258 53.323 -20.333 39.039 1.00 31.91 C ANISOU 1874 CG2 VAL A 258 4101 3936 4086 -7 22 56 C ATOM 1875 N LEU A 259 51.583 -18.814 34.824 1.00 34.27 N ANISOU 1875 N LEU A 259 4423 4230 4367 7 40 26 N ATOM 1876 CA LEU A 259 50.553 -18.728 33.796 1.00 35.82 C ANISOU 1876 CA LEU A 259 4605 4453 4551 -14 7 13 C ATOM 1877 C LEU A 259 50.364 -20.060 33.071 1.00 36.96 C ANISOU 1877 C LEU A 259 4761 4584 4696 0 16 1 C ATOM 1878 O LEU A 259 51.199 -20.465 32.258 1.00 37.37 O ANISOU 1878 O LEU A 259 4833 4591 4773 2 27 -3 O ATOM 1879 CB LEU A 259 50.820 -17.571 32.815 1.00 35.71 C ANISOU 1879 CB LEU A 259 4581 4453 4533 0 9 19 C ATOM 1880 CG LEU A 259 50.379 -16.174 33.284 1.00 35.63 C ANISOU 1880 CG LEU A 259 4571 4455 4510 -41 1 20 C ATOM 1881 CD1 LEU A 259 51.302 -15.614 34.366 1.00 36.34 C ANISOU 1881 CD1 LEU A 259 4672 4558 4576 -68 11 21 C ATOM 1882 CD2 LEU A 259 50.296 -15.209 32.118 1.00 35.77 C ANISOU 1882 CD2 LEU A 259 4591 4468 4531 -26 -19 -5 C ATOM 1883 N ALA A 260 49.259 -20.729 33.397 1.00 38.34 N ANISOU 1883 N ALA A 260 4916 4782 4869 -6 11 9 N ATOM 1884 CA ALA A 260 48.877 -21.996 32.775 1.00 39.62 C ANISOU 1884 CA ALA A 260 5082 4928 5041 -4 2 -1 C ATOM 1885 C ALA A 260 48.845 -21.869 31.255 1.00 40.69 C ANISOU 1885 C ALA A 260 5228 5092 5141 10 2 -5 C ATOM 1886 O ALA A 260 49.558 -22.594 30.551 1.00 41.02 O ANISOU 1886 O ALA A 260 5266 5109 5209 28 0 19 O ATOM 1887 CB ALA A 260 47.526 -22.454 33.303 1.00 39.63 C ANISOU 1887 CB ALA A 260 5071 4941 5046 0 0 2 C ATOM 1888 N GLY A 261 48.040 -20.924 30.766 1.00 41.64 N ANISOU 1888 N GLY A 261 5333 5204 5283 25 -8 0 N ATOM 1889 CA GLY A 261 47.878 -20.670 29.332 1.00 42.86 C ANISOU 1889 CA GLY A 261 5488 5388 5407 13 -9 4 C ATOM 1890 C GLY A 261 49.080 -20.070 28.623 1.00 43.52 C ANISOU 1890 C GLY A 261 5564 5482 5491 6 6 15 C ATOM 1891 O GLY A 261 48.959 -19.583 27.496 1.00 44.13 O ANISOU 1891 O GLY A 261 5641 5551 5574 27 5 14 O ATOM 1892 N GLU A 262 50.235 -20.096 29.286 1.00 43.92 N ANISOU 1892 N GLU A 262 5605 5530 5551 9 -5 17 N ATOM 1893 CA GLU A 262 51.504 -19.675 28.690 1.00 44.82 C ANISOU 1893 CA GLU A 262 5667 5594 5767 9 -17 -27 C ATOM 1894 C GLU A 262 52.551 -20.768 28.897 1.00 44.57 C ANISOU 1894 C GLU A 262 5677 5608 5647 15 6 21 C ATOM 1895 O GLU A 262 53.737 -20.484 29.103 1.00 44.76 O ANISOU 1895 O GLU A 262 5697 5632 5675 10 12 26 O ATOM 1896 CB GLU A 262 51.987 -18.344 29.293 1.00 44.54 C ANISOU 1896 CB GLU A 262 5646 5604 5670 31 28 -12 C ATOM 1897 CG GLU A 262 51.146 -17.114 28.922 1.00 40.79 C ANISOU 1897 CG GLU A 262 5711 5471 4313 59 229 383 C ATOM 1898 CD GLU A 262 51.396 -16.598 27.505 1.00 54.04 C ANISOU 1898 CD GLU A 262 6951 6775 6805 -1231 -767 -270 C ATOM 1899 OE1 GLU A 262 52.252 -17.163 26.787 1.00 36.41 O ANISOU 1899 OE1 GLU A 262 4273 5052 4506 949 898 -557 O ATOM 1900 OE2 GLU A 262 50.729 -15.619 27.104 1.00 38.16 O ANISOU 1900 OE2 GLU A 262 4709 4330 5457 949 -285 551 O ATOM 1901 N GLY A 263 52.097 -22.019 28.842 1.00 44.67 N ANISOU 1901 N GLY A 263 5678 5625 5669 19 15 4 N ATOM 1902 CA GLY A 263 52.959 -23.178 29.072 1.00 44.63 C ANISOU 1902 CA GLY A 263 5677 5614 5666 21 10 5 C ATOM 1903 C GLY A 263 53.312 -23.390 30.534 1.00 44.47 C ANISOU 1903 C GLY A 263 5651 5609 5635 27 11 0 C ATOM 1904 O GLY A 263 54.356 -23.969 30.846 1.00 44.69 O ANISOU 1904 O GLY A 263 5667 5639 5674 31 28 -2 O ATOM 1905 N ASN A 264 52.436 -22.922 31.425 1.00 44.09 N ANISOU 1905 N ASN A 264 5613 5547 5590 20 15 8 N ATOM 1906 CA ASN A 264 52.620 -23.027 32.883 1.00 43.61 C ANISOU 1906 CA ASN A 264 5556 5465 5546 11 13 11 C ATOM 1907 C ASN A 264 53.969 -22.515 33.417 1.00 43.06 C ANISOU 1907 C ASN A 264 5493 5391 5474 4 16 17 C ATOM 1908 O ASN A 264 54.502 -23.042 34.392 1.00 43.26 O ANISOU 1908 O ASN A 264 5542 5405 5489 10 9 8 O ATOM 1909 CB ASN A 264 52.329 -24.458 33.369 1.00 43.76 C ANISOU 1909 CB ASN A 264 5582 5476 5568 6 19 18 C ATOM 1910 N LYS A 265 54.503 -21.475 32.774 1.00 42.37 N ANISOU 1910 N LYS A 265 5395 5296 5407 0 13 0 N ATOM 1911 CA LYS A 265 55.754 -20.835 33.195 1.00 41.50 C ANISOU 1911 CA LYS A 265 5289 5199 5278 5 37 0 C ATOM 1912 C LYS A 265 55.568 -19.978 34.448 1.00 40.63 C ANISOU 1912 C LYS A 265 5169 5082 5183 -3 16 7 C ATOM 1913 O LYS A 265 54.520 -19.349 34.625 1.00 40.80 O ANISOU 1913 O LYS A 265 5194 5104 5202 -21 39 -9 O ATOM 1914 CB LYS A 265 56.311 -19.971 32.060 1.00 41.56 C ANISOU 1914 CB LYS A 265 5311 5180 5298 1 39 16 C ATOM 1915 N ALA A 266 56.597 -19.938 35.293 1.00 39.48 N ANISOU 1915 N ALA A 266 5038 4916 5046 9 29 15 N ATOM 1916 CA ALA A 266 56.539 -19.239 36.583 1.00 38.28 C ANISOU 1916 CA ALA A 266 4869 4770 4906 11 14 37 C ATOM 1917 C ALA A 266 57.388 -17.960 36.632 1.00 37.26 C ANISOU 1917 C ALA A 266 4724 4654 4779 40 14 49 C ATOM 1918 O ALA A 266 58.573 -17.995 36.985 1.00 37.57 O ANISOU 1918 O ALA A 266 4758 4696 4818 44 6 47 O ATOM 1919 CB ALA A 266 56.926 -20.184 37.716 1.00 38.52 C ANISOU 1919 CB ALA A 266 4898 4809 4927 13 0 34 C ATOM 1920 N PHE A 267 56.760 -16.832 36.302 1.00 35.47 N ANISOU 1920 N PHE A 267 4499 4421 4557 36 30 67 N ATOM 1921 CA PHE A 267 57.433 -15.529 36.246 1.00 33.68 C ANISOU 1921 CA PHE A 267 4258 4218 4319 64 37 67 C ATOM 1922 C PHE A 267 57.647 -14.951 37.636 1.00 32.17 C ANISOU 1922 C PHE A 267 4053 4005 4165 73 28 127 C ATOM 1923 O PHE A 267 56.755 -15.034 38.478 1.00 32.08 O ANISOU 1923 O PHE A 267 4038 4012 4140 124 52 151 O ATOM 1924 CB PHE A 267 56.584 -14.519 35.459 1.00 33.66 C ANISOU 1924 CB PHE A 267 4257 4210 4322 62 30 65 C ATOM 1925 CG PHE A 267 56.231 -14.949 34.062 1.00 34.24 C ANISOU 1925 CG PHE A 267 4336 4284 4389 63 32 41 C ATOM 1926 CD1 PHE A 267 56.846 -14.348 32.963 1.00 34.29 C ANISOU 1926 CD1 PHE A 267 4366 4276 4386 48 37 49 C ATOM 1927 CD2 PHE A 267 55.257 -15.919 33.835 1.00 34.91 C ANISOU 1927 CD2 PHE A 267 4442 4376 4443 36 -2 18 C ATOM 1928 CE1 PHE A 267 56.516 -14.726 31.664 1.00 34.85 C ANISOU 1928 CE1 PHE A 267 4434 4350 4455 3 28 13 C ATOM 1929 CE2 PHE A 267 54.922 -16.311 32.534 1.00 34.84 C ANISOU 1929 CE2 PHE A 267 4449 4411 4376 7 -5 25 C ATOM 1930 CZ PHE A 267 55.552 -15.708 31.447 1.00 35.03 C ANISOU 1930 CZ PHE A 267 4445 4406 4459 28 15 -3 C ATOM 1931 N THR A 268 58.812 -14.345 37.870 1.00 30.23 N ANISOU 1931 N THR A 268 3815 3753 3918 100 29 154 N ATOM 1932 CA THR A 268 59.005 -13.465 39.028 1.00 28.59 C ANISOU 1932 CA THR A 268 3552 3573 3738 107 56 169 C ATOM 1933 C THR A 268 58.161 -12.195 38.829 1.00 27.40 C ANISOU 1933 C THR A 268 3389 3447 3574 68 65 145 C ATOM 1934 O THR A 268 57.639 -11.976 37.734 1.00 26.56 O ANISOU 1934 O THR A 268 3278 3322 3490 105 93 184 O ATOM 1935 CB THR A 268 60.483 -13.042 39.228 1.00 28.79 C ANISOU 1935 CB THR A 268 3589 3600 3749 84 60 167 C ATOM 1936 OG1 THR A 268 60.938 -12.289 38.096 1.00 28.84 O ANISOU 1936 OG1 THR A 268 3547 3650 3759 136 115 215 O ATOM 1937 CG2 THR A 268 61.389 -14.257 39.426 1.00 28.78 C ANISOU 1937 CG2 THR A 268 3549 3596 3790 95 43 134 C ATOM 1938 N SER A 269 58.041 -11.372 39.874 1.00 26.26 N ANISOU 1938 N SER A 269 3199 3344 3433 45 96 187 N ATOM 1939 CA SER A 269 57.303 -10.109 39.773 1.00 25.32 C ANISOU 1939 CA SER A 269 3059 3256 3303 25 92 178 C ATOM 1940 C SER A 269 57.868 -9.264 38.639 1.00 24.80 C ANISOU 1940 C SER A 269 2949 3234 3236 16 82 181 C ATOM 1941 O SER A 269 57.120 -8.703 37.835 1.00 23.88 O ANISOU 1941 O SER A 269 2756 3134 3182 5 116 232 O ATOM 1942 CB SER A 269 57.359 -9.308 41.082 1.00 25.50 C ANISOU 1942 CB SER A 269 3102 3303 3282 2 103 162 C ATOM 1943 OG SER A 269 56.830 -10.047 42.176 1.00 25.94 O ANISOU 1943 OG SER A 269 3157 3452 3245 75 85 212 O ATOM 1944 N GLU A 270 59.196 -9.194 38.577 1.00 24.46 N ANISOU 1944 N GLU A 270 2879 3187 3228 26 70 205 N ATOM 1945 CA GLU A 270 59.896 -8.428 37.547 1.00 24.60 C ANISOU 1945 CA GLU A 270 2919 3206 3222 27 50 173 C ATOM 1946 C GLU A 270 59.684 -9.024 36.167 1.00 24.05 C ANISOU 1946 C GLU A 270 2831 3132 3172 33 77 157 C ATOM 1947 O GLU A 270 59.363 -8.313 35.234 1.00 23.56 O ANISOU 1947 O GLU A 270 2738 3071 3141 113 114 214 O ATOM 1948 CB GLU A 270 61.397 -8.334 37.858 1.00 24.57 C ANISOU 1948 CB GLU A 270 2898 3218 3217 -15 30 194 C ATOM 1949 CG GLU A 270 61.721 -7.503 39.090 1.00 26.66 C ANISOU 1949 CG GLU A 270 3248 3437 3443 -7 -3 91 C ATOM 1950 CD GLU A 270 61.571 -8.269 40.405 1.00 28.97 C ANISOU 1950 CD GLU A 270 3589 3744 3674 3 -7 90 C ATOM 1951 OE1 GLU A 270 61.286 -9.492 40.384 1.00 29.21 O ANISOU 1951 OE1 GLU A 270 3473 3745 3879 52 -12 162 O ATOM 1952 OE2 GLU A 270 61.732 -7.632 41.464 1.00 30.50 O ANISOU 1952 OE2 GLU A 270 3811 4021 3754 11 -34 1 O ATOM 1953 N GLU A 271 59.841 -10.335 36.040 1.00 24.06 N ANISOU 1953 N GLU A 271 2892 3104 3146 78 63 134 N ATOM 1954 CA GLU A 271 59.599 -11.011 34.768 1.00 24.19 C ANISOU 1954 CA GLU A 271 2935 3095 3161 75 69 130 C ATOM 1955 C GLU A 271 58.161 -10.835 34.262 1.00 23.78 C ANISOU 1955 C GLU A 271 2904 3034 3095 80 96 121 C ATOM 1956 O GLU A 271 57.941 -10.676 33.057 1.00 22.97 O ANISOU 1956 O GLU A 271 2774 2900 3051 153 129 165 O ATOM 1957 CB GLU A 271 59.972 -12.486 34.867 1.00 24.95 C ANISOU 1957 CB GLU A 271 3090 3183 3205 64 75 107 C ATOM 1958 CG GLU A 271 61.471 -12.710 34.921 1.00 26.49 C ANISOU 1958 CG GLU A 271 3253 3429 3381 96 32 124 C ATOM 1959 CD GLU A 271 61.842 -14.096 35.417 1.00 26.96 C ANISOU 1959 CD GLU A 271 3133 3339 3769 94 65 199 C ATOM 1960 OE1 GLU A 271 60.931 -14.879 35.767 1.00 29.92 O ANISOU 1960 OE1 GLU A 271 3863 3689 3814 281 38 112 O ATOM 1961 OE2 GLU A 271 63.058 -14.390 35.449 1.00 30.57 O ANISOU 1961 OE2 GLU A 271 3946 3797 3872 170 -6 182 O ATOM 1962 N PHE A 272 57.187 -10.869 35.176 1.00 23.01 N ANISOU 1962 N PHE A 272 2805 2917 3021 102 114 147 N ATOM 1963 CA PHE A 272 55.799 -10.693 34.754 1.00 22.18 C ANISOU 1963 CA PHE A 272 2725 2786 2914 48 116 146 C ATOM 1964 C PHE A 272 55.548 -9.258 34.263 1.00 21.31 C ANISOU 1964 C PHE A 272 2592 2705 2797 45 110 150 C ATOM 1965 O PHE A 272 54.840 -9.047 33.276 1.00 21.43 O ANISOU 1965 O PHE A 272 2593 2711 2838 28 120 200 O ATOM 1966 CB PHE A 272 54.781 -11.120 35.823 1.00 22.32 C ANISOU 1966 CB PHE A 272 2776 2801 2900 41 105 127 C ATOM 1967 CG PHE A 272 53.372 -11.181 35.298 1.00 21.92 C ANISOU 1967 CG PHE A 272 2750 2748 2829 -39 115 125 C ATOM 1968 CD1 PHE A 272 53.036 -12.065 34.273 1.00 22.49 C ANISOU 1968 CD1 PHE A 272 2820 2805 2919 -68 109 95 C ATOM 1969 CD2 PHE A 272 52.390 -10.327 35.795 1.00 21.92 C ANISOU 1969 CD2 PHE A 272 2800 2680 2849 -5 128 119 C ATOM 1970 CE1 PHE A 272 51.736 -12.113 33.764 1.00 22.55 C ANISOU 1970 CE1 PHE A 272 2798 2855 2912 -44 101 55 C ATOM 1971 CE2 PHE A 272 51.088 -10.366 35.291 1.00 22.19 C ANISOU 1971 CE2 PHE A 272 2816 2767 2845 -94 107 9 C ATOM 1972 CZ PHE A 272 50.762 -11.255 34.269 1.00 22.24 C ANISOU 1972 CZ PHE A 272 2783 2769 2895 -109 137 -2 C ATOM 1973 N THR A 273 56.146 -8.290 34.946 1.00 20.78 N ANISOU 1973 N THR A 273 2504 2683 2705 87 136 166 N ATOM 1974 CA THR A 273 56.121 -6.889 34.499 1.00 20.50 C ANISOU 1974 CA THR A 273 2402 2678 2709 94 112 123 C ATOM 1975 C THR A 273 56.635 -6.768 33.064 1.00 20.94 C ANISOU 1975 C THR A 273 2456 2766 2733 136 108 133 C ATOM 1976 O THR A 273 56.016 -6.101 32.217 1.00 20.92 O ANISOU 1976 O THR A 273 2401 2830 2715 159 120 164 O ATOM 1977 CB THR A 273 56.920 -6.002 35.459 1.00 20.52 C ANISOU 1977 CB THR A 273 2435 2704 2658 117 111 109 C ATOM 1978 OG1 THR A 273 56.164 -5.818 36.659 1.00 20.13 O ANISOU 1978 OG1 THR A 273 2128 2855 2662 33 181 197 O ATOM 1979 CG2 THR A 273 57.225 -4.627 34.847 1.00 19.86 C ANISOU 1979 CG2 THR A 273 2326 2608 2609 -9 81 15 C ATOM 1980 N HIS A 274 57.753 -7.430 32.777 1.00 21.53 N ANISOU 1980 N HIS A 274 2558 2812 2810 134 110 98 N ATOM 1981 CA HIS A 274 58.308 -7.387 31.421 1.00 21.52 C ANISOU 1981 CA HIS A 274 2537 2829 2811 115 116 90 C ATOM 1982 C HIS A 274 57.502 -8.163 30.383 1.00 21.66 C ANISOU 1982 C HIS A 274 2585 2840 2804 113 119 80 C ATOM 1983 O HIS A 274 57.459 -7.773 29.220 1.00 21.97 O ANISOU 1983 O HIS A 274 2584 2934 2828 89 87 135 O ATOM 1984 CB HIS A 274 59.806 -7.721 31.427 1.00 21.74 C ANISOU 1984 CB HIS A 274 2578 2846 2833 109 100 84 C ATOM 1985 CG HIS A 274 60.614 -6.719 32.183 1.00 21.64 C ANISOU 1985 CG HIS A 274 2535 2847 2839 92 119 73 C ATOM 1986 ND1 HIS A 274 60.786 -5.423 31.743 1.00 22.60 N ANISOU 1986 ND1 HIS A 274 2734 2864 2987 50 89 75 N ATOM 1987 CD2 HIS A 274 61.267 -6.805 33.365 1.00 23.14 C ANISOU 1987 CD2 HIS A 274 2829 3035 2926 11 83 58 C ATOM 1988 CE1 HIS A 274 61.520 -4.757 32.617 1.00 22.97 C ANISOU 1988 CE1 HIS A 274 2703 3000 3022 80 49 107 C ATOM 1989 NE2 HIS A 274 61.822 -5.572 33.613 1.00 22.61 N ANISOU 1989 NE2 HIS A 274 2616 3004 2968 35 106 136 N ATOM 1990 N PHE A 275 56.855 -9.248 30.811 1.00 21.22 N ANISOU 1990 N PHE A 275 2567 2741 2752 95 135 81 N ATOM 1991 CA PHE A 275 55.878 -9.967 29.990 1.00 21.95 C ANISOU 1991 CA PHE A 275 2735 2785 2820 61 138 64 C ATOM 1992 C PHE A 275 54.772 -8.998 29.544 1.00 21.12 C ANISOU 1992 C PHE A 275 2644 2701 2676 7 97 64 C ATOM 1993 O PHE A 275 54.410 -8.939 28.365 1.00 21.50 O ANISOU 1993 O PHE A 275 2709 2780 2677 62 205 143 O ATOM 1994 CB PHE A 275 55.300 -11.164 30.782 1.00 22.71 C ANISOU 1994 CB PHE A 275 2850 2865 2911 47 119 71 C ATOM 1995 CG PHE A 275 54.119 -11.839 30.118 1.00 24.55 C ANISOU 1995 CG PHE A 275 3121 3014 3191 1 76 47 C ATOM 1996 CD1 PHE A 275 54.313 -12.822 29.144 1.00 25.73 C ANISOU 1996 CD1 PHE A 275 3310 3242 3223 -1 54 -51 C ATOM 1997 CD2 PHE A 275 52.815 -11.505 30.478 1.00 26.04 C ANISOU 1997 CD2 PHE A 275 3258 3242 3393 -12 67 -8 C ATOM 1998 CE1 PHE A 275 53.226 -13.454 28.529 1.00 26.63 C ANISOU 1998 CE1 PHE A 275 3307 3378 3432 29 109 -65 C ATOM 1999 CE2 PHE A 275 51.716 -12.122 29.867 1.00 26.63 C ANISOU 1999 CE2 PHE A 275 3315 3380 3422 -40 38 -63 C ATOM 2000 CZ PHE A 275 51.920 -13.095 28.886 1.00 26.57 C ANISOU 2000 CZ PHE A 275 3225 3385 3485 -76 18 12 C ATOM 2001 N LEU A 276 54.255 -8.228 30.498 1.00 20.00 N ANISOU 2001 N LEU A 276 2478 2549 2570 14 139 119 N ATOM 2002 CA LEU A 276 53.211 -7.254 30.215 1.00 19.19 C ANISOU 2002 CA LEU A 276 2441 2386 2461 -25 114 113 C ATOM 2003 C LEU A 276 53.738 -6.160 29.307 1.00 19.27 C ANISOU 2003 C LEU A 276 2396 2471 2455 -22 95 120 C ATOM 2004 O LEU A 276 53.071 -5.769 28.348 1.00 19.19 O ANISOU 2004 O LEU A 276 2343 2537 2408 -52 38 131 O ATOM 2005 CB LEU A 276 52.667 -6.661 31.515 1.00 18.96 C ANISOU 2005 CB LEU A 276 2400 2377 2425 -27 95 107 C ATOM 2006 CG LEU A 276 51.903 -7.655 32.392 1.00 18.58 C ANISOU 2006 CG LEU A 276 2421 2268 2369 -97 85 41 C ATOM 2007 CD1 LEU A 276 51.556 -7.005 33.727 1.00 17.69 C ANISOU 2007 CD1 LEU A 276 2311 2184 2224 -11 88 79 C ATOM 2008 CD2 LEU A 276 50.644 -8.173 31.673 1.00 19.56 C ANISOU 2008 CD2 LEU A 276 2437 2492 2500 -11 74 -10 C ATOM 2009 N GLU A 277 54.945 -5.691 29.605 1.00 18.95 N ANISOU 2009 N GLU A 277 2330 2422 2446 -44 75 146 N ATOM 2010 CA GLU A 277 55.579 -4.638 28.813 1.00 19.19 C ANISOU 2010 CA GLU A 277 2347 2454 2490 -75 90 152 C ATOM 2011 C GLU A 277 55.641 -5.049 27.349 1.00 19.83 C ANISOU 2011 C GLU A 277 2393 2533 2605 -77 85 115 C ATOM 2012 O GLU A 277 55.258 -4.278 26.466 1.00 20.18 O ANISOU 2012 O GLU A 277 2437 2554 2674 -47 58 137 O ATOM 2013 CB GLU A 277 56.970 -4.341 29.348 1.00 18.95 C ANISOU 2013 CB GLU A 277 2347 2438 2413 -70 87 157 C ATOM 2014 CG GLU A 277 57.727 -3.261 28.583 1.00 20.11 C ANISOU 2014 CG GLU A 277 2470 2606 2565 -96 121 165 C ATOM 2015 CD GLU A 277 59.145 -3.117 29.083 1.00 22.13 C ANISOU 2015 CD GLU A 277 2660 2890 2857 -19 83 119 C ATOM 2016 OE1 GLU A 277 59.799 -4.146 29.352 1.00 23.50 O ANISOU 2016 OE1 GLU A 277 2951 3052 2926 -10 197 299 O ATOM 2017 OE2 GLU A 277 59.609 -1.971 29.207 1.00 25.06 O ANISOU 2017 OE2 GLU A 277 3028 3120 3371 -67 -50 24 O ATOM 2018 N GLU A 278 56.089 -6.274 27.086 1.00 20.22 N ANISOU 2018 N GLU A 278 2472 2527 2684 -54 88 141 N ATOM 2019 CA GLU A 278 56.112 -6.767 25.714 1.00 21.45 C ANISOU 2019 CA GLU A 278 2665 2727 2755 -11 104 105 C ATOM 2020 C GLU A 278 54.727 -6.764 25.056 1.00 21.41 C ANISOU 2020 C GLU A 278 2629 2768 2737 -30 119 107 C ATOM 2021 O GLU A 278 54.590 -6.397 23.884 1.00 21.28 O ANISOU 2021 O GLU A 278 2552 2822 2711 -25 94 192 O ATOM 2022 CB GLU A 278 56.798 -8.132 25.607 1.00 22.72 C ANISOU 2022 CB GLU A 278 2855 2837 2940 31 105 76 C ATOM 2023 CG GLU A 278 57.509 -8.335 24.249 1.00 27.83 C ANISOU 2023 CG GLU A 278 3670 3597 3307 230 77 -50 C ATOM 2024 CD GLU A 278 58.592 -7.279 23.934 1.00 26.41 C ANISOU 2024 CD GLU A 278 3681 3665 2687 -243 48 -61 C ATOM 2025 OE1 GLU A 278 58.870 -7.091 22.733 1.00 34.82 O ANISOU 2025 OE1 GLU A 278 4494 4326 4406 137 -76 -77 O ATOM 2026 OE2 GLU A 278 59.179 -6.640 24.856 1.00 34.83 O ANISOU 2026 OE2 GLU A 278 4337 4448 4447 186 277 123 O ATOM 2027 N LEU A 279 53.693 -7.146 25.805 1.00 20.98 N ANISOU 2027 N LEU A 279 2568 2743 2659 -23 139 137 N ATOM 2028 CA LEU A 279 52.337 -7.077 25.262 1.00 21.08 C ANISOU 2028 CA LEU A 279 2540 2754 2715 -50 180 118 C ATOM 2029 C LEU A 279 51.974 -5.650 24.835 1.00 20.75 C ANISOU 2029 C LEU A 279 2460 2765 2657 -30 186 110 C ATOM 2030 O LEU A 279 51.313 -5.456 23.821 1.00 20.79 O ANISOU 2030 O LEU A 279 2467 2796 2636 -56 233 156 O ATOM 2031 CB LEU A 279 51.301 -7.614 26.263 1.00 21.32 C ANISOU 2031 CB LEU A 279 2561 2801 2736 -44 192 110 C ATOM 2032 CG LEU A 279 51.306 -9.121 26.529 1.00 21.66 C ANISOU 2032 CG LEU A 279 2680 2805 2743 -78 174 82 C ATOM 2033 CD1 LEU A 279 50.223 -9.457 27.543 1.00 21.65 C ANISOU 2033 CD1 LEU A 279 2648 2847 2728 -100 225 75 C ATOM 2034 CD2 LEU A 279 51.112 -9.924 25.248 1.00 22.73 C ANISOU 2034 CD2 LEU A 279 2856 2920 2857 -23 56 52 C ATOM 2035 N THR A 280 52.426 -4.663 25.609 1.00 20.49 N ANISOU 2035 N THR A 280 2374 2723 2689 -52 201 103 N ATOM 2036 CA THR A 280 52.092 -3.268 25.347 1.00 20.87 C ANISOU 2036 CA THR A 280 2482 2752 2693 -35 158 118 C ATOM 2037 C THR A 280 52.860 -2.711 24.148 1.00 21.58 C ANISOU 2037 C THR A 280 2582 2843 2772 -19 184 115 C ATOM 2038 O THR A 280 52.513 -1.655 23.635 1.00 21.22 O ANISOU 2038 O THR A 280 2487 2865 2710 -39 147 157 O ATOM 2039 CB THR A 280 52.331 -2.348 26.569 1.00 20.59 C ANISOU 2039 CB THR A 280 2436 2708 2677 -33 133 85 C ATOM 2040 OG1 THR A 280 53.742 -2.176 26.800 1.00 20.52 O ANISOU 2040 OG1 THR A 280 2394 2657 2746 -44 179 62 O ATOM 2041 CG2 THR A 280 51.639 -2.892 27.822 1.00 20.67 C ANISOU 2041 CG2 THR A 280 2546 2726 2579 -29 96 80 C ATOM 2042 N LYS A 281 53.901 -3.424 23.720 1.00 22.54 N ANISOU 2042 N LYS A 281 2705 2986 2873 13 147 107 N ATOM 2043 CA LYS A 281 54.641 -3.035 22.519 1.00 23.40 C ANISOU 2043 CA LYS A 281 2831 3120 2940 12 115 92 C ATOM 2044 C LYS A 281 54.006 -3.651 21.285 1.00 23.80 C ANISOU 2044 C LYS A 281 2927 3155 2959 23 114 78 C ATOM 2045 O LYS A 281 54.116 -3.096 20.190 1.00 24.84 O ANISOU 2045 O LYS A 281 3094 3285 3057 -1 98 193 O ATOM 2046 CB LYS A 281 56.101 -3.488 22.611 1.00 23.96 C ANISOU 2046 CB LYS A 281 2892 3171 3041 16 101 86 C ATOM 2047 CG LYS A 281 56.827 -2.993 23.831 1.00 25.45 C ANISOU 2047 CG LYS A 281 3081 3425 3161 20 50 35 C ATOM 2048 CD LYS A 281 56.836 -1.489 23.912 1.00 28.42 C ANISOU 2048 CD LYS A 281 3461 3672 3664 19 78 23 C ATOM 2049 CE LYS A 281 57.746 -1.029 25.029 1.00 30.98 C ANISOU 2049 CE LYS A 281 3909 4124 3736 -71 -43 -50 C ATOM 2050 NZ LYS A 281 59.055 -1.771 25.015 1.00 32.13 N ANISOU 2050 NZ LYS A 281 3902 4260 4045 120 49 -5 N ATOM 2051 N GLN A 282 53.355 -4.797 21.471 1.00 23.41 N ANISOU 2051 N GLN A 282 2846 3114 2933 22 129 50 N ATOM 2052 CA GLN A 282 52.731 -5.564 20.389 1.00 23.02 C ANISOU 2052 CA GLN A 282 2808 3082 2853 17 147 45 C ATOM 2053 C GLN A 282 51.318 -5.084 20.052 1.00 22.63 C ANISOU 2053 C GLN A 282 2785 3039 2775 11 139 24 C ATOM 2054 O GLN A 282 50.858 -5.220 18.914 1.00 23.07 O ANISOU 2054 O GLN A 282 2766 3176 2822 14 190 84 O ATOM 2055 CB GLN A 282 52.695 -7.048 20.765 1.00 23.75 C ANISOU 2055 CB GLN A 282 2935 3115 2974 18 104 12 C ATOM 2056 N TYR A 283 50.627 -4.543 21.054 1.00 21.38 N ANISOU 2056 N TYR A 283 2612 2887 2622 -21 198 96 N ATOM 2057 CA TYR A 283 49.256 -4.069 20.897 1.00 20.55 C ANISOU 2057 CA TYR A 283 2536 2752 2517 -40 153 86 C ATOM 2058 C TYR A 283 49.111 -2.760 21.652 1.00 19.12 C ANISOU 2058 C TYR A 283 2338 2565 2360 -67 150 93 C ATOM 2059 O TYR A 283 49.858 -2.529 22.610 1.00 18.73 O ANISOU 2059 O TYR A 283 2211 2612 2293 -20 169 55 O ATOM 2060 CB TYR A 283 48.254 -5.101 21.440 1.00 20.86 C ANISOU 2060 CB TYR A 283 2578 2743 2605 -56 194 73 C ATOM 2061 CG TYR A 283 48.118 -6.323 20.562 1.00 21.85 C ANISOU 2061 CG TYR A 283 2665 2957 2676 -88 123 39 C ATOM 2062 CD1 TYR A 283 47.221 -6.341 19.487 1.00 23.03 C ANISOU 2062 CD1 TYR A 283 2805 3081 2864 -88 81 25 C ATOM 2063 CD2 TYR A 283 48.894 -7.452 20.793 1.00 21.29 C ANISOU 2063 CD2 TYR A 283 2569 2849 2670 -125 210 29 C ATOM 2064 CE1 TYR A 283 47.100 -7.455 18.674 1.00 23.25 C ANISOU 2064 CE1 TYR A 283 2945 2987 2900 -25 119 7 C ATOM 2065 CE2 TYR A 283 48.782 -8.573 19.986 1.00 22.36 C ANISOU 2065 CE2 TYR A 283 2694 2932 2869 -44 183 -57 C ATOM 2066 CZ TYR A 283 47.888 -8.567 18.925 1.00 23.00 C ANISOU 2066 CZ TYR A 283 2887 2955 2894 -62 140 -49 C ATOM 2067 OH TYR A 283 47.772 -9.685 18.122 1.00 25.35 O ANISOU 2067 OH TYR A 283 3157 3308 3167 -55 164 -166 O ATOM 2068 N PRO A 284 48.167 -1.893 21.227 1.00 18.17 N ANISOU 2068 N PRO A 284 2210 2459 2234 -98 125 108 N ATOM 2069 CA PRO A 284 47.988 -0.640 21.945 1.00 17.45 C ANISOU 2069 CA PRO A 284 2123 2374 2129 -47 101 121 C ATOM 2070 C PRO A 284 47.201 -0.809 23.245 1.00 16.25 C ANISOU 2070 C PRO A 284 1975 2201 1999 -43 98 133 C ATOM 2071 O PRO A 284 46.123 -0.191 23.429 1.00 15.85 O ANISOU 2071 O PRO A 284 1850 2245 1924 -26 130 211 O ATOM 2072 CB PRO A 284 47.215 0.222 20.942 1.00 17.39 C ANISOU 2072 CB PRO A 284 2164 2341 2102 -111 73 180 C ATOM 2073 CG PRO A 284 46.403 -0.750 20.201 1.00 18.62 C ANISOU 2073 CG PRO A 284 2365 2484 2225 -76 49 100 C ATOM 2074 CD PRO A 284 47.249 -1.982 20.072 1.00 18.01 C ANISOU 2074 CD PRO A 284 2237 2430 2175 -40 116 98 C ATOM 2075 N ILE A 285 47.765 -1.623 24.137 1.00 15.62 N ANISOU 2075 N ILE A 285 1864 2166 1902 -52 130 61 N ATOM 2076 CA ILE A 285 47.308 -1.747 25.523 1.00 14.59 C ANISOU 2076 CA ILE A 285 1761 2010 1771 -58 80 91 C ATOM 2077 C ILE A 285 47.837 -0.541 26.298 1.00 14.26 C ANISOU 2077 C ILE A 285 1700 1992 1724 -39 94 85 C ATOM 2078 O ILE A 285 49.057 -0.365 26.425 1.00 15.32 O ANISOU 2078 O ILE A 285 1771 2162 1886 -160 50 14 O ATOM 2079 CB ILE A 285 47.805 -3.062 26.163 1.00 14.95 C ANISOU 2079 CB ILE A 285 1839 2010 1830 -46 74 16 C ATOM 2080 CG1 ILE A 285 47.261 -4.277 25.399 1.00 14.81 C ANISOU 2080 CG1 ILE A 285 1852 1948 1825 -33 48 26 C ATOM 2081 CG2 ILE A 285 47.412 -3.135 27.635 1.00 14.33 C ANISOU 2081 CG2 ILE A 285 1654 2065 1723 -23 81 67 C ATOM 2082 CD1 ILE A 285 48.088 -5.526 25.636 1.00 15.77 C ANISOU 2082 CD1 ILE A 285 2015 1896 2080 24 39 113 C ATOM 2083 N VAL A 286 46.925 0.287 26.802 1.00 13.32 N ANISOU 2083 N VAL A 286 1645 1847 1568 -49 108 144 N ATOM 2084 CA VAL A 286 47.295 1.503 27.533 1.00 13.01 C ANISOU 2084 CA VAL A 286 1603 1783 1554 -28 124 138 C ATOM 2085 C VAL A 286 46.865 1.513 29.002 1.00 12.85 C ANISOU 2085 C VAL A 286 1593 1731 1557 -43 77 124 C ATOM 2086 O VAL A 286 47.098 2.487 29.716 1.00 13.74 O ANISOU 2086 O VAL A 286 1709 1844 1668 -80 159 162 O ATOM 2087 CB VAL A 286 46.749 2.779 26.835 1.00 12.87 C ANISOU 2087 CB VAL A 286 1590 1855 1443 -38 87 155 C ATOM 2088 CG1 VAL A 286 47.381 2.913 25.437 1.00 13.89 C ANISOU 2088 CG1 VAL A 286 1793 1977 1506 -71 189 131 C ATOM 2089 CG2 VAL A 286 45.214 2.745 26.785 1.00 13.75 C ANISOU 2089 CG2 VAL A 286 1672 1888 1662 43 24 134 C ATOM 2090 N SER A 287 46.221 0.435 29.445 1.00 12.83 N ANISOU 2090 N SER A 287 1520 1774 1581 1 99 136 N ATOM 2091 CA SER A 287 45.751 0.376 30.823 1.00 12.21 C ANISOU 2091 CA SER A 287 1421 1688 1528 -26 33 97 C ATOM 2092 C SER A 287 45.795 -1.068 31.273 1.00 12.26 C ANISOU 2092 C SER A 287 1455 1655 1548 -23 40 97 C ATOM 2093 O SER A 287 45.336 -1.965 30.548 1.00 12.07 O ANISOU 2093 O SER A 287 1441 1600 1543 -71 3 112 O ATOM 2094 CB SER A 287 44.321 0.919 30.935 1.00 12.47 C ANISOU 2094 CB SER A 287 1442 1720 1573 46 -22 99 C ATOM 2095 OG SER A 287 43.877 0.925 32.282 1.00 11.59 O ANISOU 2095 OG SER A 287 1187 1678 1536 -83 -118 89 O ATOM 2096 N ILE A 288 46.382 -1.290 32.448 1.00 12.07 N ANISOU 2096 N ILE A 288 1384 1647 1553 -15 53 104 N ATOM 2097 CA ILE A 288 46.539 -2.638 33.000 1.00 12.84 C ANISOU 2097 CA ILE A 288 1475 1753 1648 -20 75 94 C ATOM 2098 C ILE A 288 46.092 -2.626 34.442 1.00 12.47 C ANISOU 2098 C ILE A 288 1456 1709 1570 -62 54 82 C ATOM 2099 O ILE A 288 46.693 -1.952 35.276 1.00 12.62 O ANISOU 2099 O ILE A 288 1479 1655 1662 -178 96 110 O ATOM 2100 CB ILE A 288 48.009 -3.160 32.916 1.00 13.15 C ANISOU 2100 CB ILE A 288 1560 1778 1655 23 77 123 C ATOM 2101 CG1 ILE A 288 48.485 -3.184 31.462 1.00 14.17 C ANISOU 2101 CG1 ILE A 288 1619 1929 1833 112 206 -30 C ATOM 2102 CG2 ILE A 288 48.119 -4.550 33.583 1.00 13.65 C ANISOU 2102 CG2 ILE A 288 1715 1827 1645 108 125 197 C ATOM 2103 CD1 ILE A 288 49.999 -3.476 31.301 1.00 14.18 C ANISOU 2103 CD1 ILE A 288 1430 2038 1920 -29 76 84 C ATOM 2104 N GLU A 289 45.041 -3.397 34.720 1.00 12.41 N ANISOU 2104 N GLU A 289 1471 1755 1488 -110 75 95 N ATOM 2105 CA GLU A 289 44.448 -3.492 36.051 1.00 12.33 C ANISOU 2105 CA GLU A 289 1406 1775 1501 -56 20 122 C ATOM 2106 C GLU A 289 44.991 -4.721 36.790 1.00 12.42 C ANISOU 2106 C GLU A 289 1512 1712 1492 -91 52 115 C ATOM 2107 O GLU A 289 45.118 -5.814 36.213 1.00 11.81 O ANISOU 2107 O GLU A 289 1455 1695 1337 -86 -5 107 O ATOM 2108 CB GLU A 289 42.928 -3.552 35.914 1.00 12.56 C ANISOU 2108 CB GLU A 289 1409 1844 1517 -70 76 61 C ATOM 2109 CG GLU A 289 42.149 -3.688 37.232 1.00 12.86 C ANISOU 2109 CG GLU A 289 1351 1966 1566 -64 66 159 C ATOM 2110 CD GLU A 289 40.660 -3.838 36.977 1.00 13.18 C ANISOU 2110 CD GLU A 289 1466 1896 1645 -158 -56 159 C ATOM 2111 OE1 GLU A 289 40.143 -3.198 36.038 1.00 13.01 O ANISOU 2111 OE1 GLU A 289 1549 1840 1551 -205 90 393 O ATOM 2112 OE2 GLU A 289 40.002 -4.594 37.719 1.00 13.23 O ANISOU 2112 OE2 GLU A 289 1517 2061 1447 -217 -100 224 O ATOM 2113 N ASP A 290 45.331 -4.516 38.063 1.00 12.57 N ANISOU 2113 N ASP A 290 1507 1757 1513 -85 37 137 N ATOM 2114 CA ASP A 290 45.840 -5.595 38.935 1.00 13.53 C ANISOU 2114 CA ASP A 290 1627 1800 1714 -112 111 167 C ATOM 2115 C ASP A 290 46.883 -6.474 38.243 1.00 13.98 C ANISOU 2115 C ASP A 290 1721 1839 1748 -84 94 149 C ATOM 2116 O ASP A 290 46.739 -7.699 38.158 1.00 14.51 O ANISOU 2116 O ASP A 290 1796 1905 1810 -64 134 181 O ATOM 2117 CB ASP A 290 44.683 -6.441 39.499 1.00 13.28 C ANISOU 2117 CB ASP A 290 1559 1796 1687 -170 159 165 C ATOM 2118 CG ASP A 290 43.929 -5.747 40.621 1.00 13.97 C ANISOU 2118 CG ASP A 290 1619 1918 1769 -126 67 97 C ATOM 2119 OD1 ASP A 290 44.470 -4.816 41.257 1.00 15.63 O ANISOU 2119 OD1 ASP A 290 1760 2249 1930 -279 169 226 O ATOM 2120 OD2 ASP A 290 42.770 -6.158 40.877 1.00 15.05 O ANISOU 2120 OD2 ASP A 290 1593 2407 1717 -183 42 242 O ATOM 2121 N GLY A 291 47.938 -5.824 37.749 1.00 13.89 N ANISOU 2121 N GLY A 291 1664 1866 1748 -105 115 238 N ATOM 2122 CA GLY A 291 49.017 -6.505 37.016 1.00 14.43 C ANISOU 2122 CA GLY A 291 1775 1868 1837 3 65 223 C ATOM 2123 C GLY A 291 49.942 -7.341 37.895 1.00 15.31 C ANISOU 2123 C GLY A 291 1891 1978 1946 29 64 210 C ATOM 2124 O GLY A 291 50.774 -8.092 37.388 1.00 16.51 O ANISOU 2124 O GLY A 291 2055 2165 2053 64 62 243 O ATOM 2125 N LEU A 292 49.801 -7.191 39.209 1.00 15.40 N ANISOU 2125 N LEU A 292 1905 2000 1945 13 -35 225 N ATOM 2126 CA LEU A 292 50.476 -8.052 40.190 1.00 15.64 C ANISOU 2126 CA LEU A 292 1962 2030 1949 6 19 242 C ATOM 2127 C LEU A 292 49.519 -8.295 41.357 1.00 15.60 C ANISOU 2127 C LEU A 292 1957 2048 1920 -11 35 260 C ATOM 2128 O LEU A 292 48.455 -7.684 41.418 1.00 15.20 O ANISOU 2128 O LEU A 292 1972 1971 1833 -58 84 348 O ATOM 2129 CB LEU A 292 51.784 -7.423 40.679 1.00 15.74 C ANISOU 2129 CB LEU A 292 1983 1963 2034 20 -27 227 C ATOM 2130 CG LEU A 292 52.875 -7.182 39.622 1.00 15.32 C ANISOU 2130 CG LEU A 292 1863 1933 2024 51 -3 55 C ATOM 2131 CD1 LEU A 292 53.902 -6.189 40.126 1.00 17.37 C ANISOU 2131 CD1 LEU A 292 2039 2137 2421 15 -85 73 C ATOM 2132 CD2 LEU A 292 53.549 -8.474 39.164 1.00 16.57 C ANISOU 2132 CD2 LEU A 292 2046 1953 2296 125 108 126 C ATOM 2133 N ASP A 293 49.890 -9.199 42.266 1.00 15.78 N ANISOU 2133 N ASP A 293 2004 2103 1887 -7 -26 259 N ATOM 2134 CA ASP A 293 49.049 -9.498 43.435 1.00 16.81 C ANISOU 2134 CA ASP A 293 2082 2271 2031 -49 -47 258 C ATOM 2135 C ASP A 293 48.942 -8.277 44.359 1.00 17.08 C ANISOU 2135 C ASP A 293 2148 2333 2008 -59 -83 228 C ATOM 2136 O ASP A 293 49.896 -7.493 44.481 1.00 17.56 O ANISOU 2136 O ASP A 293 2203 2401 2067 -192 -70 308 O ATOM 2137 CB ASP A 293 49.643 -10.669 44.226 1.00 17.02 C ANISOU 2137 CB ASP A 293 2130 2299 2037 -3 -95 263 C ATOM 2138 CG ASP A 293 48.726 -11.142 45.356 1.00 18.28 C ANISOU 2138 CG ASP A 293 2287 2434 2222 -89 -62 245 C ATOM 2139 OD1 ASP A 293 47.748 -11.849 45.068 1.00 20.77 O ANISOU 2139 OD1 ASP A 293 2684 2811 2395 -271 -231 268 O ATOM 2140 OD2 ASP A 293 48.987 -10.816 46.541 1.00 19.67 O ANISOU 2140 OD2 ASP A 293 2630 2549 2294 -145 -51 286 O ATOM 2141 N GLU A 294 47.807 -8.136 45.045 1.00 17.41 N ANISOU 2141 N GLU A 294 2171 2391 2053 -59 -84 246 N ATOM 2142 CA GLU A 294 47.588 -6.976 45.924 1.00 17.81 C ANISOU 2142 CA GLU A 294 2244 2458 2064 -62 -103 216 C ATOM 2143 C GLU A 294 48.637 -6.871 47.041 1.00 18.33 C ANISOU 2143 C GLU A 294 2308 2512 2144 -59 -126 178 C ATOM 2144 O GLU A 294 48.935 -5.777 47.504 1.00 18.42 O ANISOU 2144 O GLU A 294 2402 2539 2055 -74 -149 255 O ATOM 2145 CB GLU A 294 46.163 -6.944 46.502 1.00 18.27 C ANISOU 2145 CB GLU A 294 2258 2510 2172 -18 -130 200 C ATOM 2146 CG GLU A 294 45.803 -8.113 47.417 1.00 19.39 C ANISOU 2146 CG GLU A 294 2458 2597 2310 -75 -57 190 C ATOM 2147 CD GLU A 294 46.261 -7.932 48.871 1.00 21.58 C ANISOU 2147 CD GLU A 294 2715 2903 2579 4 -66 94 C ATOM 2148 OE1 GLU A 294 46.295 -8.948 49.593 1.00 22.83 O ANISOU 2148 OE1 GLU A 294 2935 3038 2699 67 97 250 O ATOM 2149 OE2 GLU A 294 46.573 -6.795 49.295 1.00 22.38 O ANISOU 2149 OE2 GLU A 294 2836 2990 2677 -67 -65 139 O ATOM 2150 N SER A 295 49.198 -8.009 47.447 1.00 18.74 N ANISOU 2150 N SER A 295 2316 2554 2247 -88 -122 202 N ATOM 2151 CA SER A 295 50.206 -8.023 48.522 1.00 19.30 C ANISOU 2151 CA SER A 295 2390 2621 2319 -83 -119 187 C ATOM 2152 C SER A 295 51.600 -7.681 48.022 1.00 19.59 C ANISOU 2152 C SER A 295 2401 2638 2404 -59 -88 128 C ATOM 2153 O SER A 295 52.511 -7.440 48.827 1.00 20.43 O ANISOU 2153 O SER A 295 2484 2846 2430 -58 -117 170 O ATOM 2154 CB SER A 295 50.246 -9.393 49.206 1.00 19.23 C ANISOU 2154 CB SER A 295 2398 2540 2367 -42 -135 152 C ATOM 2155 OG SER A 295 50.778 -10.373 48.338 1.00 19.62 O ANISOU 2155 OG SER A 295 2448 2638 2369 -167 -149 215 O ATOM 2156 N ASP A 296 51.771 -7.683 46.700 1.00 19.30 N ANISOU 2156 N ASP A 296 2321 2615 2395 -34 -36 180 N ATOM 2157 CA ASP A 296 53.103 -7.585 46.089 1.00 19.34 C ANISOU 2157 CA ASP A 296 2361 2527 2459 -11 -9 153 C ATOM 2158 C ASP A 296 53.496 -6.131 45.811 1.00 19.52 C ANISOU 2158 C ASP A 296 2354 2563 2498 -17 -11 147 C ATOM 2159 O ASP A 296 53.654 -5.731 44.654 1.00 19.25 O ANISOU 2159 O ASP A 296 2381 2506 2426 -48 -122 153 O ATOM 2160 CB ASP A 296 53.154 -8.454 44.822 1.00 19.59 C ANISOU 2160 CB ASP A 296 2408 2536 2497 -9 23 178 C ATOM 2161 CG ASP A 296 54.561 -8.589 44.242 1.00 19.74 C ANISOU 2161 CG ASP A 296 2417 2490 2591 -40 -3 165 C ATOM 2162 OD1 ASP A 296 55.549 -8.136 44.874 1.00 21.81 O ANISOU 2162 OD1 ASP A 296 2659 2741 2886 -96 -69 377 O ATOM 2163 OD2 ASP A 296 54.668 -9.166 43.142 1.00 19.57 O ANISOU 2163 OD2 ASP A 296 2242 2624 2569 -32 158 421 O ATOM 2164 N TRP A 297 53.670 -5.358 46.881 1.00 19.63 N ANISOU 2164 N TRP A 297 2376 2549 2532 -3 -36 146 N ATOM 2165 CA TRP A 297 53.989 -3.932 46.769 1.00 20.51 C ANISOU 2165 CA TRP A 297 2440 2699 2651 -30 -12 120 C ATOM 2166 C TRP A 297 55.398 -3.655 46.259 1.00 20.84 C ANISOU 2166 C TRP A 297 2436 2732 2747 -6 -3 138 C ATOM 2167 O TRP A 297 55.604 -2.689 45.519 1.00 21.14 O ANISOU 2167 O TRP A 297 2416 2813 2803 -25 32 189 O ATOM 2168 CB TRP A 297 53.699 -3.190 48.077 1.00 20.40 C ANISOU 2168 CB TRP A 297 2446 2688 2616 -10 -40 71 C ATOM 2169 CG TRP A 297 52.232 -2.952 48.271 1.00 20.59 C ANISOU 2169 CG TRP A 297 2558 2720 2544 6 -88 53 C ATOM 2170 CD1 TRP A 297 51.221 -3.846 48.043 1.00 20.92 C ANISOU 2170 CD1 TRP A 297 2498 2812 2636 7 -74 54 C ATOM 2171 CD2 TRP A 297 51.606 -1.755 48.737 1.00 20.51 C ANISOU 2171 CD2 TRP A 297 2508 2755 2530 44 -99 46 C ATOM 2172 NE1 TRP A 297 50.010 -3.276 48.334 1.00 20.04 N ANISOU 2172 NE1 TRP A 297 2503 2727 2382 101 -137 104 N ATOM 2173 CE2 TRP A 297 50.214 -1.991 48.754 1.00 20.71 C ANISOU 2173 CE2 TRP A 297 2570 2809 2488 -9 -79 22 C ATOM 2174 CE3 TRP A 297 52.083 -0.494 49.128 1.00 20.91 C ANISOU 2174 CE3 TRP A 297 2599 2718 2625 66 -114 -6 C ATOM 2175 CZ2 TRP A 297 49.294 -1.018 49.147 1.00 20.90 C ANISOU 2175 CZ2 TRP A 297 2591 2743 2604 46 -104 5 C ATOM 2176 CZ3 TRP A 297 51.164 0.476 49.526 1.00 21.18 C ANISOU 2176 CZ3 TRP A 297 2515 2874 2656 -2 -87 -9 C ATOM 2177 CH2 TRP A 297 49.784 0.207 49.529 1.00 21.50 C ANISOU 2177 CH2 TRP A 297 2562 2873 2733 -56 1 44 C ATOM 2178 N ASP A 298 56.362 -4.494 46.633 1.00 21.23 N ANISOU 2178 N ASP A 298 2476 2815 2773 -17 -5 163 N ATOM 2179 CA ASP A 298 57.691 -4.389 46.026 1.00 21.48 C ANISOU 2179 CA ASP A 298 2497 2851 2814 -5 -12 142 C ATOM 2180 C ASP A 298 57.596 -4.552 44.509 1.00 20.76 C ANISOU 2180 C ASP A 298 2408 2733 2747 -35 -42 149 C ATOM 2181 O ASP A 298 58.202 -3.783 43.748 1.00 21.18 O ANISOU 2181 O ASP A 298 2349 2899 2797 -89 -50 175 O ATOM 2182 CB ASP A 298 58.653 -5.424 46.624 1.00 22.17 C ANISOU 2182 CB ASP A 298 2632 2919 2869 16 -30 169 C ATOM 2183 CG ASP A 298 59.128 -5.043 48.021 1.00 24.87 C ANISOU 2183 CG ASP A 298 3010 3303 3134 -46 -29 68 C ATOM 2184 OD1 ASP A 298 58.785 -3.949 48.515 1.00 27.79 O ANISOU 2184 OD1 ASP A 298 3423 3739 3395 74 -47 -79 O ATOM 2185 OD2 ASP A 298 59.861 -5.845 48.624 1.00 29.29 O ANISOU 2185 OD2 ASP A 298 3665 3844 3618 147 -71 210 O ATOM 2186 N GLY A 299 56.806 -5.535 44.075 1.00 19.95 N ANISOU 2186 N GLY A 299 2269 2686 2623 -38 -56 132 N ATOM 2187 CA GLY A 299 56.581 -5.783 42.662 1.00 18.96 C ANISOU 2187 CA GLY A 299 2154 2509 2541 -3 -23 131 C ATOM 2188 C GLY A 299 55.879 -4.605 42.008 1.00 18.80 C ANISOU 2188 C GLY A 299 2145 2499 2497 16 -35 127 C ATOM 2189 O GLY A 299 56.259 -4.183 40.913 1.00 18.51 O ANISOU 2189 O GLY A 299 1994 2502 2537 79 -40 208 O ATOM 2190 N PHE A 300 54.864 -4.066 42.682 1.00 18.11 N ANISOU 2190 N PHE A 300 2064 2395 2421 -50 -45 126 N ATOM 2191 CA PHE A 300 54.119 -2.928 42.129 1.00 18.32 C ANISOU 2191 CA PHE A 300 2141 2399 2420 -67 -45 125 C ATOM 2192 C PHE A 300 54.985 -1.690 42.008 1.00 18.25 C ANISOU 2192 C PHE A 300 2147 2400 2386 -98 -104 100 C ATOM 2193 O PHE A 300 54.833 -0.934 41.056 1.00 18.44 O ANISOU 2193 O PHE A 300 2192 2446 2368 -130 -74 151 O ATOM 2194 CB PHE A 300 52.848 -2.609 42.923 1.00 18.21 C ANISOU 2194 CB PHE A 300 2087 2420 2409 -65 -59 64 C ATOM 2195 CG PHE A 300 51.597 -3.238 42.352 1.00 18.18 C ANISOU 2195 CG PHE A 300 2131 2438 2337 -70 -100 130 C ATOM 2196 CD1 PHE A 300 51.122 -2.863 41.097 1.00 17.26 C ANISOU 2196 CD1 PHE A 300 2000 2434 2121 -146 -16 58 C ATOM 2197 CD2 PHE A 300 50.881 -4.182 43.087 1.00 17.10 C ANISOU 2197 CD2 PHE A 300 1940 2350 2207 -95 -36 13 C ATOM 2198 CE1 PHE A 300 49.962 -3.431 40.580 1.00 17.34 C ANISOU 2198 CE1 PHE A 300 2115 2436 2035 -61 -143 50 C ATOM 2199 CE2 PHE A 300 49.728 -4.755 42.570 1.00 17.72 C ANISOU 2199 CE2 PHE A 300 2017 2552 2162 -105 -25 38 C ATOM 2200 CZ PHE A 300 49.266 -4.376 41.314 1.00 17.50 C ANISOU 2200 CZ PHE A 300 2077 2418 2152 -38 -64 91 C ATOM 2201 N ALA A 301 55.890 -1.490 42.966 1.00 18.33 N ANISOU 2201 N ALA A 301 2134 2464 2364 -128 -126 145 N ATOM 2202 CA ALA A 301 56.828 -0.372 42.894 1.00 18.29 C ANISOU 2202 CA ALA A 301 2163 2462 2325 -146 -183 124 C ATOM 2203 C ALA A 301 57.646 -0.466 41.616 1.00 18.27 C ANISOU 2203 C ALA A 301 2128 2498 2312 -125 -192 160 C ATOM 2204 O ALA A 301 57.788 0.525 40.896 1.00 18.92 O ANISOU 2204 O ALA A 301 2238 2570 2380 -142 -211 280 O ATOM 2205 CB ALA A 301 57.741 -0.355 44.117 1.00 18.45 C ANISOU 2205 CB ALA A 301 2149 2515 2346 -126 -189 146 C ATOM 2206 N TYR A 302 58.164 -1.657 41.327 1.00 17.98 N ANISOU 2206 N TYR A 302 2118 2477 2234 -124 -146 157 N ATOM 2207 CA TYR A 302 58.945 -1.902 40.099 1.00 18.03 C ANISOU 2207 CA TYR A 302 2072 2455 2324 -54 -54 173 C ATOM 2208 C TYR A 302 58.096 -1.728 38.835 1.00 18.06 C ANISOU 2208 C TYR A 302 2023 2480 2357 -99 -52 214 C ATOM 2209 O TYR A 302 58.510 -1.054 37.881 1.00 17.81 O ANISOU 2209 O TYR A 302 1919 2503 2343 -77 -7 304 O ATOM 2210 CB TYR A 302 59.561 -3.300 40.134 1.00 18.33 C ANISOU 2210 CB TYR A 302 2148 2428 2387 -76 -31 195 C ATOM 2211 CG TYR A 302 60.436 -3.665 38.963 1.00 18.29 C ANISOU 2211 CG TYR A 302 2197 2343 2409 -18 -21 216 C ATOM 2212 CD1 TYR A 302 61.757 -3.186 38.866 1.00 18.41 C ANISOU 2212 CD1 TYR A 302 2111 2420 2464 5 -32 236 C ATOM 2213 CD2 TYR A 302 59.975 -4.519 37.970 1.00 18.54 C ANISOU 2213 CD2 TYR A 302 2185 2463 2396 -17 7 194 C ATOM 2214 CE1 TYR A 302 62.575 -3.551 37.783 1.00 18.67 C ANISOU 2214 CE1 TYR A 302 2306 2383 2404 -34 3 212 C ATOM 2215 CE2 TYR A 302 60.782 -4.887 36.891 1.00 19.64 C ANISOU 2215 CE2 TYR A 302 2350 2560 2550 -50 51 114 C ATOM 2216 CZ TYR A 302 62.082 -4.400 36.809 1.00 19.14 C ANISOU 2216 CZ TYR A 302 2361 2455 2455 34 21 211 C ATOM 2217 OH TYR A 302 62.856 -4.782 35.743 1.00 19.73 O ANISOU 2217 OH TYR A 302 2403 2599 2492 -38 136 307 O ATOM 2218 N GLN A 303 56.900 -2.311 38.839 1.00 17.66 N ANISOU 2218 N GLN A 303 1937 2407 2362 -111 -61 220 N ATOM 2219 CA GLN A 303 56.013 -2.213 37.688 1.00 17.10 C ANISOU 2219 CA GLN A 303 1864 2333 2297 -140 -48 187 C ATOM 2220 C GLN A 303 55.677 -0.756 37.391 1.00 16.94 C ANISOU 2220 C GLN A 303 1751 2338 2348 -151 -27 145 C ATOM 2221 O GLN A 303 55.574 -0.362 36.232 1.00 16.92 O ANISOU 2221 O GLN A 303 1678 2388 2360 -127 15 160 O ATOM 2222 CB GLN A 303 54.724 -3.025 37.906 1.00 17.35 C ANISOU 2222 CB GLN A 303 1904 2362 2325 -146 -85 210 C ATOM 2223 CG GLN A 303 53.814 -3.058 36.667 1.00 16.59 C ANISOU 2223 CG GLN A 303 1999 2244 2058 -164 -56 213 C ATOM 2224 CD GLN A 303 52.766 -4.155 36.736 1.00 17.04 C ANISOU 2224 CD GLN A 303 2022 2269 2183 -117 0 161 C ATOM 2225 OE1 GLN A 303 53.089 -5.362 36.747 1.00 19.71 O ANISOU 2225 OE1 GLN A 303 2475 2413 2599 -38 112 233 O ATOM 2226 NE2 GLN A 303 51.506 -3.752 36.780 1.00 15.66 N ANISOU 2226 NE2 GLN A 303 1982 1985 1981 -115 31 274 N ATOM 2227 N THR A 304 55.496 0.036 38.440 1.00 16.66 N ANISOU 2227 N THR A 304 1678 2334 2318 -193 -52 158 N ATOM 2228 CA THR A 304 55.144 1.430 38.275 1.00 17.64 C ANISOU 2228 CA THR A 304 1845 2399 2457 -148 -86 134 C ATOM 2229 C THR A 304 56.329 2.217 37.697 1.00 18.16 C ANISOU 2229 C THR A 304 1926 2471 2503 -156 -93 189 C ATOM 2230 O THR A 304 56.151 3.077 36.835 1.00 18.47 O ANISOU 2230 O THR A 304 1922 2494 2602 -268 -201 192 O ATOM 2231 CB THR A 304 54.604 2.038 39.594 1.00 17.19 C ANISOU 2231 CB THR A 304 1868 2351 2310 -151 -70 141 C ATOM 2232 OG1 THR A 304 53.520 1.226 40.085 1.00 16.96 O ANISOU 2232 OG1 THR A 304 1756 2309 2378 -181 -77 93 O ATOM 2233 CG2 THR A 304 54.075 3.451 39.383 1.00 17.96 C ANISOU 2233 CG2 THR A 304 2034 2350 2439 -100 -108 139 C ATOM 2234 N LYS A 305 57.542 1.899 38.148 1.00 19.17 N ANISOU 2234 N LYS A 305 2039 2590 2652 -88 -88 195 N ATOM 2235 CA LYS A 305 58.727 2.557 37.593 1.00 19.69 C ANISOU 2235 CA LYS A 305 2101 2727 2653 -61 -82 208 C ATOM 2236 C LYS A 305 58.921 2.225 36.111 1.00 19.49 C ANISOU 2236 C LYS A 305 2063 2689 2651 -24 -55 212 C ATOM 2237 O LYS A 305 59.220 3.113 35.296 1.00 20.83 O ANISOU 2237 O LYS A 305 2269 2805 2839 -62 -109 309 O ATOM 2238 CB LYS A 305 59.988 2.215 38.408 1.00 20.14 C ANISOU 2238 CB LYS A 305 2199 2749 2705 -31 -79 184 C ATOM 2239 CG LYS A 305 59.998 2.886 39.775 1.00 22.41 C ANISOU 2239 CG LYS A 305 2640 3042 2833 -45 -102 130 C ATOM 2240 CD LYS A 305 61.394 2.897 40.407 1.00 27.07 C ANISOU 2240 CD LYS A 305 3058 3894 3330 -126 -106 48 C ATOM 2241 CE LYS A 305 61.865 1.497 40.693 1.00 29.26 C ANISOU 2241 CE LYS A 305 3628 3644 3845 41 2 60 C ATOM 2242 NZ LYS A 305 62.811 1.465 41.845 1.00 31.14 N ANISOU 2242 NZ LYS A 305 3893 4198 3737 -22 -168 78 N ATOM 2243 N VAL A 306 58.734 0.956 35.774 1.00 18.96 N ANISOU 2243 N VAL A 306 1957 2660 2588 2 -47 230 N ATOM 2244 CA VAL A 306 58.953 0.436 34.432 1.00 18.84 C ANISOU 2244 CA VAL A 306 2062 2583 2513 -8 -20 222 C ATOM 2245 C VAL A 306 57.861 0.892 33.443 1.00 18.74 C ANISOU 2245 C VAL A 306 2036 2591 2494 -38 -8 215 C ATOM 2246 O VAL A 306 58.165 1.290 32.314 1.00 18.89 O ANISOU 2246 O VAL A 306 1961 2635 2579 -46 50 285 O ATOM 2247 CB VAL A 306 59.077 -1.118 34.444 1.00 18.95 C ANISOU 2247 CB VAL A 306 2097 2620 2482 -7 -8 180 C ATOM 2248 CG1 VAL A 306 59.094 -1.685 33.050 1.00 19.35 C ANISOU 2248 CG1 VAL A 306 2134 2758 2460 77 -10 153 C ATOM 2249 CG2 VAL A 306 60.333 -1.555 35.182 1.00 19.61 C ANISOU 2249 CG2 VAL A 306 2212 2663 2573 26 -60 240 C ATOM 2250 N LEU A 307 56.596 0.826 33.862 1.00 18.71 N ANISOU 2250 N LEU A 307 2074 2525 2508 -39 37 244 N ATOM 2251 CA LEU A 307 55.470 1.026 32.943 1.00 18.38 C ANISOU 2251 CA LEU A 307 2153 2331 2497 -74 -7 162 C ATOM 2252 C LEU A 307 54.670 2.313 33.159 1.00 17.91 C ANISOU 2252 C LEU A 307 2081 2295 2429 -93 11 179 C ATOM 2253 O LEU A 307 53.954 2.743 32.253 1.00 17.61 O ANISOU 2253 O LEU A 307 1993 2270 2428 -46 -16 234 O ATOM 2254 CB LEU A 307 54.505 -0.168 33.027 1.00 18.80 C ANISOU 2254 CB LEU A 307 2198 2415 2530 -86 -1 142 C ATOM 2255 CG LEU A 307 54.806 -1.450 32.230 1.00 20.74 C ANISOU 2255 CG LEU A 307 2573 2516 2791 -52 -16 92 C ATOM 2256 CD1 LEU A 307 56.209 -1.923 32.337 1.00 24.43 C ANISOU 2256 CD1 LEU A 307 2970 3126 3186 -15 61 -14 C ATOM 2257 CD2 LEU A 307 53.840 -2.568 32.622 1.00 19.52 C ANISOU 2257 CD2 LEU A 307 2434 2349 2631 -47 4 94 C ATOM 2258 N GLY A 308 54.782 2.901 34.347 1.00 17.45 N ANISOU 2258 N GLY A 308 2054 2199 2377 -127 17 204 N ATOM 2259 CA GLY A 308 53.852 3.939 34.816 1.00 18.12 C ANISOU 2259 CA GLY A 308 2162 2265 2454 -118 -5 209 C ATOM 2260 C GLY A 308 53.854 5.258 34.063 1.00 18.98 C ANISOU 2260 C GLY A 308 2276 2372 2561 -96 2 197 C ATOM 2261 O GLY A 308 52.848 5.974 34.064 1.00 18.35 O ANISOU 2261 O GLY A 308 2133 2265 2573 -141 -13 284 O ATOM 2262 N ASP A 309 54.976 5.582 33.420 1.00 19.69 N ANISOU 2262 N ASP A 309 2319 2515 2647 -132 -44 185 N ATOM 2263 CA ASP A 309 55.057 6.827 32.647 1.00 20.74 C ANISOU 2263 CA ASP A 309 2458 2662 2758 -97 -9 161 C ATOM 2264 C ASP A 309 54.209 6.809 31.375 1.00 20.52 C ANISOU 2264 C ASP A 309 2426 2630 2737 -71 6 154 C ATOM 2265 O ASP A 309 53.785 7.867 30.906 1.00 21.43 O ANISOU 2265 O ASP A 309 2568 2685 2887 -50 -58 200 O ATOM 2266 CB ASP A 309 56.517 7.178 32.330 1.00 21.68 C ANISOU 2266 CB ASP A 309 2569 2781 2887 -100 15 160 C ATOM 2267 CG ASP A 309 57.290 7.607 33.564 1.00 25.50 C ANISOU 2267 CG ASP A 309 3109 3274 3303 -90 -28 29 C ATOM 2268 OD1 ASP A 309 56.660 7.947 34.594 1.00 30.35 O ANISOU 2268 OD1 ASP A 309 3689 4108 3732 -148 88 -131 O ATOM 2269 OD2 ASP A 309 58.535 7.611 33.513 1.00 29.72 O ANISOU 2269 OD2 ASP A 309 3369 3942 3979 -30 6 62 O ATOM 2270 N LYS A 310 53.942 5.618 30.841 1.00 19.69 N ANISOU 2270 N LYS A 310 2298 2591 2592 -96 -3 143 N ATOM 2271 CA LYS A 310 53.290 5.463 29.538 1.00 19.13 C ANISOU 2271 CA LYS A 310 2226 2531 2511 -130 34 126 C ATOM 2272 C LYS A 310 52.042 4.570 29.585 1.00 18.21 C ANISOU 2272 C LYS A 310 2074 2471 2373 -135 25 133 C ATOM 2273 O LYS A 310 51.350 4.405 28.569 1.00 17.86 O ANISOU 2273 O LYS A 310 2039 2436 2309 -138 62 187 O ATOM 2274 CB LYS A 310 54.279 4.870 28.534 1.00 19.87 C ANISOU 2274 CB LYS A 310 2346 2643 2559 -93 14 86 C ATOM 2275 N ILE A 311 51.789 3.969 30.748 1.00 16.59 N ANISOU 2275 N ILE A 311 1822 2273 2206 -123 81 131 N ATOM 2276 CA ILE A 311 50.678 3.007 30.914 1.00 15.72 C ANISOU 2276 CA ILE A 311 1768 2124 2081 -102 66 91 C ATOM 2277 C ILE A 311 49.895 3.323 32.178 1.00 14.48 C ANISOU 2277 C ILE A 311 1600 1980 1919 -98 45 103 C ATOM 2278 O ILE A 311 50.474 3.625 33.220 1.00 14.58 O ANISOU 2278 O ILE A 311 1486 2096 1956 -192 94 214 O ATOM 2279 CB ILE A 311 51.196 1.527 30.997 1.00 15.85 C ANISOU 2279 CB ILE A 311 1816 2122 2083 -56 106 86 C ATOM 2280 CG1 ILE A 311 52.089 1.188 29.798 1.00 16.28 C ANISOU 2280 CG1 ILE A 311 1921 2189 2074 -17 113 -13 C ATOM 2281 CG2 ILE A 311 50.039 0.508 31.120 1.00 16.63 C ANISOU 2281 CG2 ILE A 311 1952 2209 2155 -78 23 48 C ATOM 2282 CD1 ILE A 311 51.328 1.091 28.459 1.00 15.75 C ANISOU 2282 CD1 ILE A 311 1795 2327 1862 80 167 71 C ATOM 2283 N GLN A 312 48.566 3.257 32.080 1.00 13.84 N ANISOU 2283 N GLN A 312 1507 1947 1801 -80 41 108 N ATOM 2284 CA GLN A 312 47.708 3.410 33.253 1.00 13.23 C ANISOU 2284 CA GLN A 312 1513 1843 1669 -30 -38 117 C ATOM 2285 C GLN A 312 47.696 2.084 34.024 1.00 13.49 C ANISOU 2285 C GLN A 312 1591 1845 1689 -52 -91 98 C ATOM 2286 O GLN A 312 47.403 1.032 33.457 1.00 14.22 O ANISOU 2286 O GLN A 312 1708 1966 1728 -36 -158 174 O ATOM 2287 CB GLN A 312 46.299 3.789 32.798 1.00 13.32 C ANISOU 2287 CB GLN A 312 1471 1885 1702 -10 -34 67 C ATOM 2288 CG GLN A 312 45.290 3.938 33.900 1.00 13.55 C ANISOU 2288 CG GLN A 312 1561 1841 1745 21 -17 65 C ATOM 2289 CD GLN A 312 44.001 4.548 33.399 1.00 14.68 C ANISOU 2289 CD GLN A 312 1745 1933 1896 -11 -122 85 C ATOM 2290 OE1 GLN A 312 43.809 5.762 33.489 1.00 14.46 O ANISOU 2290 OE1 GLN A 312 1676 1826 1992 -103 -262 88 O ATOM 2291 NE2 GLN A 312 43.117 3.711 32.846 1.00 13.42 N ANISOU 2291 NE2 GLN A 312 1770 1608 1720 -99 -27 158 N ATOM 2292 N LEU A 313 48.060 2.152 35.302 1.00 13.37 N ANISOU 2292 N LEU A 313 1579 1865 1636 -104 -58 125 N ATOM 2293 CA LEU A 313 48.182 0.977 36.160 1.00 12.83 C ANISOU 2293 CA LEU A 313 1443 1811 1617 -40 -109 76 C ATOM 2294 C LEU A 313 47.086 1.081 37.211 1.00 13.04 C ANISOU 2294 C LEU A 313 1528 1826 1600 -41 -98 48 C ATOM 2295 O LEU A 313 47.162 1.883 38.142 1.00 13.28 O ANISOU 2295 O LEU A 313 1505 1988 1551 -34 -170 44 O ATOM 2296 CB LEU A 313 49.596 0.890 36.775 1.00 13.30 C ANISOU 2296 CB LEU A 313 1492 1906 1654 -82 -39 98 C ATOM 2297 CG LEU A 313 50.746 0.739 35.764 1.00 13.30 C ANISOU 2297 CG LEU A 313 1519 1805 1729 41 -87 8 C ATOM 2298 CD1 LEU A 313 52.087 0.922 36.470 1.00 13.37 C ANISOU 2298 CD1 LEU A 313 1413 1836 1830 -133 -26 121 C ATOM 2299 CD2 LEU A 313 50.699 -0.589 34.996 1.00 14.38 C ANISOU 2299 CD2 LEU A 313 1845 1705 1911 -165 10 2 C ATOM 2300 N VAL A 314 46.018 0.311 37.008 1.00 13.00 N ANISOU 2300 N VAL A 314 1549 1820 1570 0 -94 110 N ATOM 2301 CA VAL A 314 44.800 0.461 37.784 1.00 13.10 C ANISOU 2301 CA VAL A 314 1569 1863 1543 -28 -75 156 C ATOM 2302 C VAL A 314 44.773 -0.544 38.939 1.00 12.97 C ANISOU 2302 C VAL A 314 1572 1851 1503 8 -55 130 C ATOM 2303 O VAL A 314 44.832 -1.749 38.717 1.00 13.29 O ANISOU 2303 O VAL A 314 1681 1936 1431 -7 -30 109 O ATOM 2304 CB VAL A 314 43.541 0.211 36.910 1.00 12.79 C ANISOU 2304 CB VAL A 314 1545 1844 1471 38 -105 157 C ATOM 2305 CG1 VAL A 314 42.295 0.530 37.725 1.00 13.51 C ANISOU 2305 CG1 VAL A 314 1518 2003 1611 28 27 38 C ATOM 2306 CG2 VAL A 314 43.557 1.091 35.659 1.00 12.90 C ANISOU 2306 CG2 VAL A 314 1578 1788 1534 9 -22 211 C ATOM 2307 N GLY A 315 44.682 -0.036 40.161 1.00 13.55 N ANISOU 2307 N GLY A 315 1628 1989 1530 19 -39 132 N ATOM 2308 CA GLY A 315 44.458 -0.904 41.310 1.00 14.55 C ANISOU 2308 CA GLY A 315 1744 2132 1650 -37 0 107 C ATOM 2309 C GLY A 315 42.981 -1.171 41.510 1.00 15.09 C ANISOU 2309 C GLY A 315 1799 2221 1714 12 3 93 C ATOM 2310 O GLY A 315 42.189 -0.231 41.659 1.00 16.19 O ANISOU 2310 O GLY A 315 1928 2320 1902 16 67 161 O ATOM 2311 N ASP A 316 42.621 -2.452 41.495 1.00 14.96 N ANISOU 2311 N ASP A 316 1710 2281 1693 -23 -14 112 N ATOM 2312 CA ASP A 316 41.270 -2.916 41.830 1.00 15.80 C ANISOU 2312 CA ASP A 316 1863 2349 1787 -66 16 108 C ATOM 2313 C ASP A 316 41.384 -3.649 43.162 1.00 15.75 C ANISOU 2313 C ASP A 316 1818 2338 1828 -46 -20 111 C ATOM 2314 O ASP A 316 41.203 -3.026 44.211 1.00 17.23 O ANISOU 2314 O ASP A 316 1941 2654 1951 -11 11 92 O ATOM 2315 CB ASP A 316 40.686 -3.810 40.726 1.00 15.75 C ANISOU 2315 CB ASP A 316 1864 2311 1809 -36 17 86 C ATOM 2316 CG ASP A 316 39.407 -4.527 41.154 1.00 15.83 C ANISOU 2316 CG ASP A 316 1943 2259 1812 -7 32 69 C ATOM 2317 OD1 ASP A 316 38.723 -4.009 42.060 1.00 16.95 O ANISOU 2317 OD1 ASP A 316 1797 2757 1885 24 162 69 O ATOM 2318 OD2 ASP A 316 39.089 -5.604 40.589 1.00 16.64 O ANISOU 2318 OD2 ASP A 316 1992 2487 1841 -76 158 25 O ATOM 2319 N ASP A 317 41.723 -4.937 43.121 1.00 15.90 N ANISOU 2319 N ASP A 317 1878 2340 1823 -59 -40 142 N ATOM 2320 CA ASP A 317 42.028 -5.700 44.345 1.00 15.91 C ANISOU 2320 CA ASP A 317 1924 2285 1833 -88 9 175 C ATOM 2321 C ASP A 317 43.144 -5.006 45.159 1.00 16.01 C ANISOU 2321 C ASP A 317 1947 2298 1838 -68 2 123 C ATOM 2322 O ASP A 317 43.195 -5.108 46.385 1.00 16.50 O ANISOU 2322 O ASP A 317 1999 2383 1885 -114 60 181 O ATOM 2323 CB ASP A 317 42.436 -7.135 43.992 1.00 16.84 C ANISOU 2323 CB ASP A 317 2072 2404 1921 -24 0 186 C ATOM 2324 CG ASP A 317 42.543 -8.040 45.218 1.00 18.52 C ANISOU 2324 CG ASP A 317 2357 2520 2157 5 27 225 C ATOM 2325 OD1 ASP A 317 41.717 -7.890 46.156 1.00 21.80 O ANISOU 2325 OD1 ASP A 317 2731 3138 2414 -71 -16 183 O ATOM 2326 OD2 ASP A 317 43.443 -8.913 45.224 1.00 20.26 O ANISOU 2326 OD2 ASP A 317 2563 2787 2345 36 68 411 O ATOM 2327 N LEU A 318 44.027 -4.284 44.471 1.00 15.16 N ANISOU 2327 N LEU A 318 1861 2180 1718 -97 -24 106 N ATOM 2328 CA LEU A 318 45.119 -3.583 45.129 1.00 15.91 C ANISOU 2328 CA LEU A 318 1914 2238 1892 -50 -20 97 C ATOM 2329 C LEU A 318 44.626 -2.591 46.181 1.00 16.37 C ANISOU 2329 C LEU A 318 2007 2345 1868 -55 -48 28 C ATOM 2330 O LEU A 318 45.181 -2.524 47.287 1.00 17.34 O ANISOU 2330 O LEU A 318 2093 2573 1921 9 -123 13 O ATOM 2331 CB LEU A 318 45.953 -2.841 44.090 1.00 15.35 C ANISOU 2331 CB LEU A 318 1879 2140 1813 -99 -16 130 C ATOM 2332 CG LEU A 318 47.110 -1.969 44.583 1.00 15.16 C ANISOU 2332 CG LEU A 318 1781 2101 1876 -57 -94 127 C ATOM 2333 CD1 LEU A 318 48.098 -2.740 45.466 1.00 15.47 C ANISOU 2333 CD1 LEU A 318 1865 2129 1881 -34 -133 192 C ATOM 2334 CD2 LEU A 318 47.824 -1.342 43.379 1.00 15.64 C ANISOU 2334 CD2 LEU A 318 1892 2209 1839 -52 -22 161 C ATOM 2335 N PHE A 319 43.585 -1.829 45.841 1.00 16.61 N ANISOU 2335 N PHE A 319 2044 2341 1925 0 -70 14 N ATOM 2336 CA PHE A 319 43.124 -0.739 46.707 1.00 17.22 C ANISOU 2336 CA PHE A 319 2066 2457 2019 41 -63 5 C ATOM 2337 C PHE A 319 41.745 -0.960 47.340 1.00 17.58 C ANISOU 2337 C PHE A 319 2143 2499 2037 54 -61 17 C ATOM 2338 O PHE A 319 41.411 -0.300 48.327 1.00 18.07 O ANISOU 2338 O PHE A 319 2199 2648 2019 161 -153 -27 O ATOM 2339 CB PHE A 319 43.105 0.600 45.961 1.00 17.73 C ANISOU 2339 CB PHE A 319 2138 2480 2116 -25 -42 2 C ATOM 2340 CG PHE A 319 44.456 1.063 45.455 1.00 17.02 C ANISOU 2340 CG PHE A 319 1964 2400 2100 -42 -101 12 C ATOM 2341 CD1 PHE A 319 45.555 1.159 46.311 1.00 17.60 C ANISOU 2341 CD1 PHE A 319 2091 2532 2064 -70 -144 -90 C ATOM 2342 CD2 PHE A 319 44.610 1.455 44.129 1.00 17.77 C ANISOU 2342 CD2 PHE A 319 2165 2432 2151 66 -13 -74 C ATOM 2343 CE1 PHE A 319 46.795 1.609 45.837 1.00 17.87 C ANISOU 2343 CE1 PHE A 319 2190 2507 2090 -132 -62 10 C ATOM 2344 CE2 PHE A 319 45.841 1.912 43.635 1.00 17.34 C ANISOU 2344 CE2 PHE A 319 2104 2296 2186 -46 -208 -59 C ATOM 2345 CZ PHE A 319 46.946 1.988 44.495 1.00 18.05 C ANISOU 2345 CZ PHE A 319 2141 2532 2186 -42 -159 -50 C ATOM 2346 N VAL A 320 40.945 -1.851 46.750 1.00 17.32 N ANISOU 2346 N VAL A 320 2095 2464 2019 29 -17 71 N ATOM 2347 CA VAL A 320 39.542 -2.077 47.146 1.00 17.37 C ANISOU 2347 CA VAL A 320 2127 2448 2024 33 -31 56 C ATOM 2348 C VAL A 320 38.785 -0.804 47.588 1.00 17.79 C ANISOU 2348 C VAL A 320 2222 2525 2011 29 -35 17 C ATOM 2349 O VAL A 320 38.063 -0.794 48.601 1.00 18.20 O ANISOU 2349 O VAL A 320 2229 2696 1989 24 -40 143 O ATOM 2350 CB VAL A 320 39.384 -3.273 48.147 1.00 17.00 C ANISOU 2350 CB VAL A 320 2075 2376 2006 57 -14 25 C ATOM 2351 CG1 VAL A 320 39.798 -4.591 47.471 1.00 17.29 C ANISOU 2351 CG1 VAL A 320 2175 2348 2045 20 -42 55 C ATOM 2352 CG2 VAL A 320 40.162 -3.033 49.451 1.00 17.61 C ANISOU 2352 CG2 VAL A 320 2239 2436 2015 16 3 85 C ATOM 2353 N THR A 321 38.942 0.262 46.797 1.00 17.93 N ANISOU 2353 N THR A 321 2251 2570 1990 1 -48 -13 N ATOM 2354 CA THR A 321 38.245 1.537 46.991 1.00 18.71 C ANISOU 2354 CA THR A 321 2368 2666 2074 11 -125 -43 C ATOM 2355 C THR A 321 38.449 2.059 48.427 1.00 19.52 C ANISOU 2355 C THR A 321 2475 2778 2163 26 -128 -63 C ATOM 2356 O THR A 321 37.563 2.676 49.014 1.00 19.81 O ANISOU 2356 O THR A 321 2509 2904 2113 48 -202 -91 O ATOM 2357 CB THR A 321 36.730 1.427 46.615 1.00 18.43 C ANISOU 2357 CB THR A 321 2287 2595 2120 34 -108 -102 C ATOM 2358 OG1 THR A 321 36.589 0.670 45.400 1.00 18.01 O ANISOU 2358 OG1 THR A 321 2334 2692 1816 -11 -226 12 O ATOM 2359 CG2 THR A 321 36.124 2.814 46.388 1.00 19.05 C ANISOU 2359 CG2 THR A 321 2483 2574 2179 -11 -119 -8 C ATOM 2360 N ASN A 322 39.646 1.803 48.961 1.00 20.32 N ANISOU 2360 N ASN A 322 2576 2892 2250 2 -175 -42 N ATOM 2361 CA ASN A 322 39.989 2.110 50.354 1.00 21.17 C ANISOU 2361 CA ASN A 322 2744 2933 2364 22 -130 -29 C ATOM 2362 C ASN A 322 41.008 3.259 50.420 1.00 21.25 C ANISOU 2362 C ASN A 322 2738 2984 2349 52 -171 4 C ATOM 2363 O ASN A 322 42.135 3.109 49.960 1.00 21.20 O ANISOU 2363 O ASN A 322 2720 3047 2288 45 -234 14 O ATOM 2364 CB ASN A 322 40.516 0.830 51.012 1.00 21.23 C ANISOU 2364 CB ASN A 322 2777 2934 2353 2 -141 -31 C ATOM 2365 CG ASN A 322 40.675 0.951 52.508 1.00 23.40 C ANISOU 2365 CG ASN A 322 3121 3172 2597 -17 -82 -18 C ATOM 2366 OD1 ASN A 322 41.206 1.934 53.015 1.00 24.35 O ANISOU 2366 OD1 ASN A 322 3369 3195 2685 -148 -75 -66 O ATOM 2367 ND2 ASN A 322 40.244 -0.076 53.221 1.00 26.11 N ANISOU 2367 ND2 ASN A 322 3513 3487 2919 -162 -40 51 N ATOM 2368 N THR A 323 40.597 4.403 50.976 1.00 21.80 N ANISOU 2368 N THR A 323 2824 2996 2460 60 -176 10 N ATOM 2369 CA THR A 323 41.428 5.615 50.986 1.00 22.45 C ANISOU 2369 CA THR A 323 2879 3051 2598 70 -146 -9 C ATOM 2370 C THR A 323 42.674 5.437 51.848 1.00 22.36 C ANISOU 2370 C THR A 323 2846 3025 2622 33 -141 -14 C ATOM 2371 O THR A 323 43.722 6.041 51.578 1.00 22.25 O ANISOU 2371 O THR A 323 2909 3014 2529 10 -174 -16 O ATOM 2372 CB THR A 323 40.663 6.868 51.488 1.00 22.80 C ANISOU 2372 CB THR A 323 2869 3114 2680 115 -159 28 C ATOM 2373 OG1 THR A 323 39.943 6.544 52.680 1.00 23.18 O ANISOU 2373 OG1 THR A 323 2966 3193 2646 156 -116 -12 O ATOM 2374 CG2 THR A 323 39.679 7.379 50.426 1.00 23.58 C ANISOU 2374 CG2 THR A 323 2909 3251 2799 112 -183 70 C ATOM 2375 N LYS A 324 42.554 4.603 52.878 1.00 22.67 N ANISOU 2375 N LYS A 324 2882 3056 2675 11 -127 -36 N ATOM 2376 CA LYS A 324 43.685 4.287 53.743 1.00 22.72 C ANISOU 2376 CA LYS A 324 2835 3053 2742 22 -123 -44 C ATOM 2377 C LYS A 324 44.769 3.541 52.975 1.00 22.66 C ANISOU 2377 C LYS A 324 2842 3021 2745 0 -108 -42 C ATOM 2378 O LYS A 324 45.956 3.829 53.135 1.00 23.14 O ANISOU 2378 O LYS A 324 2900 3108 2784 -21 -159 -57 O ATOM 2379 CB LYS A 324 43.244 3.479 54.967 1.00 22.77 C ANISOU 2379 CB LYS A 324 2830 3022 2799 2 -107 -13 C ATOM 2380 N ILE A 325 44.354 2.594 52.133 1.00 22.02 N ANISOU 2380 N ILE A 325 2772 2959 2636 4 -159 -46 N ATOM 2381 CA ILE A 325 45.295 1.849 51.306 1.00 21.87 C ANISOU 2381 CA ILE A 325 2743 2908 2658 2 -158 -19 C ATOM 2382 C ILE A 325 45.797 2.723 50.156 1.00 21.99 C ANISOU 2382 C ILE A 325 2770 2885 2700 10 -157 -18 C ATOM 2383 O ILE A 325 46.995 2.779 49.897 1.00 21.85 O ANISOU 2383 O ILE A 325 2702 2962 2639 5 -189 28 O ATOM 2384 CB ILE A 325 44.684 0.534 50.753 1.00 21.49 C ANISOU 2384 CB ILE A 325 2735 2821 2608 11 -160 3 C ATOM 2385 CG1 ILE A 325 44.042 -0.268 51.890 1.00 22.09 C ANISOU 2385 CG1 ILE A 325 2799 2865 2725 -3 -121 21 C ATOM 2386 CG2 ILE A 325 45.747 -0.269 49.988 1.00 21.42 C ANISOU 2386 CG2 ILE A 325 2688 2894 2555 23 -152 58 C ATOM 2387 CD1 ILE A 325 43.359 -1.564 51.466 1.00 21.88 C ANISOU 2387 CD1 ILE A 325 2716 2904 2690 -4 -108 -44 C ATOM 2388 N LEU A 326 44.877 3.405 49.472 1.00 22.41 N ANISOU 2388 N LEU A 326 2800 2918 2797 24 -185 -44 N ATOM 2389 CA LEU A 326 45.245 4.330 48.398 1.00 22.39 C ANISOU 2389 CA LEU A 326 2789 2921 2795 4 -154 -58 C ATOM 2390 C LEU A 326 46.299 5.365 48.838 1.00 23.00 C ANISOU 2390 C LEU A 326 2838 3007 2891 -9 -142 -50 C ATOM 2391 O LEU A 326 47.288 5.586 48.137 1.00 22.80 O ANISOU 2391 O LEU A 326 2795 3018 2847 -72 -214 -78 O ATOM 2392 CB LEU A 326 43.997 5.038 47.840 1.00 21.96 C ANISOU 2392 CB LEU A 326 2733 2852 2759 19 -164 -82 C ATOM 2393 CG LEU A 326 44.231 6.093 46.748 1.00 21.97 C ANISOU 2393 CG LEU A 326 2731 2855 2759 -1 -82 -73 C ATOM 2394 CD1 LEU A 326 44.896 5.521 45.491 1.00 20.77 C ANISOU 2394 CD1 LEU A 326 2638 2576 2676 93 -107 -62 C ATOM 2395 CD2 LEU A 326 42.938 6.817 46.374 1.00 22.28 C ANISOU 2395 CD2 LEU A 326 2785 2876 2802 50 -144 -60 C ATOM 2396 N LYS A 327 46.089 5.974 50.003 1.00 23.77 N ANISOU 2396 N LYS A 327 2919 3128 2981 1 -106 -63 N ATOM 2397 CA LYS A 327 47.018 6.984 50.533 1.00 24.61 C ANISOU 2397 CA LYS A 327 3045 3219 3087 -25 -74 -59 C ATOM 2398 C LYS A 327 48.441 6.426 50.656 1.00 24.06 C ANISOU 2398 C LYS A 327 2989 3153 2997 -29 -91 -25 C ATOM 2399 O LYS A 327 49.408 7.055 50.183 1.00 24.60 O ANISOU 2399 O LYS A 327 2997 3334 3014 -8 -125 -51 O ATOM 2400 CB LYS A 327 46.522 7.536 51.877 1.00 24.59 C ANISOU 2400 CB LYS A 327 3052 3208 3081 -23 -63 -40 C ATOM 2401 CG LYS A 327 47.413 8.610 52.501 1.00 25.97 C ANISOU 2401 CG LYS A 327 3284 3368 3214 -22 -3 -88 C ATOM 2402 CD LYS A 327 46.829 9.095 53.822 1.00 27.06 C ANISOU 2402 CD LYS A 327 3453 3522 3304 -9 -24 -79 C ATOM 2403 CE LYS A 327 47.808 10.015 54.535 1.00 31.77 C ANISOU 2403 CE LYS A 327 3952 3823 4294 -143 -199 5 C ATOM 2404 NZ LYS A 327 47.321 10.374 55.900 1.00 32.40 N ANISOU 2404 NZ LYS A 327 4295 4333 3679 83 206 -183 N ATOM 2405 N GLU A 328 48.562 5.249 51.271 1.00 23.67 N ANISOU 2405 N GLU A 328 2904 3146 2943 -23 -113 -66 N ATOM 2406 CA GLU A 328 49.852 4.573 51.396 1.00 23.70 C ANISOU 2406 CA GLU A 328 2937 3127 2940 -35 -109 -37 C ATOM 2407 C GLU A 328 50.443 4.201 50.032 1.00 22.90 C ANISOU 2407 C GLU A 328 2806 3067 2826 -50 -154 -45 C ATOM 2408 O GLU A 328 51.648 4.325 49.811 1.00 22.27 O ANISOU 2408 O GLU A 328 2735 3051 2676 -136 -240 -34 O ATOM 2409 CB GLU A 328 49.738 3.339 52.296 1.00 23.55 C ANISOU 2409 CB GLU A 328 2907 3078 2962 -41 -106 -3 C ATOM 2410 CG GLU A 328 51.098 2.742 52.677 1.00 25.41 C ANISOU 2410 CG GLU A 328 3091 3359 3202 15 -52 -7 C ATOM 2411 CD GLU A 328 50.996 1.424 53.429 1.00 25.38 C ANISOU 2411 CD GLU A 328 3079 3304 3257 25 -56 92 C ATOM 2412 OE1 GLU A 328 49.861 0.951 53.676 1.00 30.94 O ANISOU 2412 OE1 GLU A 328 3651 4190 3914 -68 -88 15 O ATOM 2413 OE2 GLU A 328 52.059 0.853 53.781 1.00 30.78 O ANISOU 2413 OE2 GLU A 328 3756 4115 3821 91 -91 45 O ATOM 2414 N GLY A 329 49.594 3.742 49.110 1.00 22.54 N ANISOU 2414 N GLY A 329 2739 3067 2757 -71 -219 -79 N ATOM 2415 CA GLY A 329 50.050 3.457 47.756 1.00 22.28 C ANISOU 2415 CA GLY A 329 2710 3007 2748 -48 -193 -51 C ATOM 2416 C GLY A 329 50.668 4.676 47.093 1.00 22.42 C ANISOU 2416 C GLY A 329 2721 3055 2741 -60 -220 -82 C ATOM 2417 O GLY A 329 51.761 4.602 46.542 1.00 22.80 O ANISOU 2417 O GLY A 329 2673 3108 2882 -43 -272 -36 O ATOM 2418 N ILE A 330 49.962 5.800 47.150 1.00 22.49 N ANISOU 2418 N ILE A 330 2750 3040 2753 -77 -275 -45 N ATOM 2419 CA ILE A 330 50.448 7.065 46.609 1.00 22.37 C ANISOU 2419 CA ILE A 330 2690 3040 2769 -97 -243 -65 C ATOM 2420 C ILE A 330 51.820 7.424 47.207 1.00 22.85 C ANISOU 2420 C ILE A 330 2733 3114 2835 -78 -229 -52 C ATOM 2421 O ILE A 330 52.746 7.788 46.487 1.00 22.71 O ANISOU 2421 O ILE A 330 2675 3175 2776 -84 -299 -102 O ATOM 2422 CB ILE A 330 49.431 8.200 46.876 1.00 22.14 C ANISOU 2422 CB ILE A 330 2630 3040 2741 -94 -223 -33 C ATOM 2423 CG1 ILE A 330 48.138 7.944 46.094 1.00 21.63 C ANISOU 2423 CG1 ILE A 330 2602 2920 2693 -95 -186 -91 C ATOM 2424 CG2 ILE A 330 50.009 9.569 46.506 1.00 21.97 C ANISOU 2424 CG2 ILE A 330 2798 2885 2662 -29 -203 -70 C ATOM 2425 CD1 ILE A 330 46.953 8.750 46.624 1.00 21.86 C ANISOU 2425 CD1 ILE A 330 2385 3044 2876 -84 -34 -29 C ATOM 2426 N GLU A 331 51.933 7.301 48.523 1.00 23.72 N ANISOU 2426 N GLU A 331 2847 3199 2966 -66 -192 -23 N ATOM 2427 CA GLU A 331 53.191 7.604 49.212 1.00 24.13 C ANISOU 2427 CA GLU A 331 2901 3229 3038 -82 -157 -37 C ATOM 2428 C GLU A 331 54.353 6.743 48.702 1.00 24.59 C ANISOU 2428 C GLU A 331 2963 3271 3108 -60 -132 -12 C ATOM 2429 O GLU A 331 55.494 7.220 48.621 1.00 25.22 O ANISOU 2429 O GLU A 331 3022 3370 3190 -80 -107 -36 O ATOM 2430 CB GLU A 331 53.016 7.457 50.726 1.00 24.36 C ANISOU 2430 CB GLU A 331 2931 3245 3078 -116 -164 5 C ATOM 2431 N LYS A 332 54.053 5.495 48.334 1.00 24.14 N ANISOU 2431 N LYS A 332 2905 3207 3057 -48 -138 -35 N ATOM 2432 CA LYS A 332 55.073 4.513 47.941 1.00 24.38 C ANISOU 2432 CA LYS A 332 2980 3203 3077 -33 -105 -16 C ATOM 2433 C LYS A 332 55.258 4.303 46.428 1.00 23.91 C ANISOU 2433 C LYS A 332 2915 3112 3056 -10 -90 -10 C ATOM 2434 O LYS A 332 55.985 3.392 46.005 1.00 24.07 O ANISOU 2434 O LYS A 332 2948 3132 3065 30 -56 10 O ATOM 2435 CB LYS A 332 54.836 3.188 48.674 1.00 24.88 C ANISOU 2435 CB LYS A 332 3029 3291 3131 -21 -119 -2 C ATOM 2436 CG LYS A 332 55.014 3.336 50.176 1.00 26.93 C ANISOU 2436 CG LYS A 332 3381 3552 3297 -3 -85 -73 C ATOM 2437 CD LYS A 332 54.825 2.046 50.916 1.00 29.75 C ANISOU 2437 CD LYS A 332 3841 3790 3671 -70 -40 78 C ATOM 2438 CE LYS A 332 55.186 2.234 52.388 1.00 32.23 C ANISOU 2438 CE LYS A 332 4056 4330 3858 9 -63 -102 C ATOM 2439 NZ LYS A 332 54.795 1.046 53.195 1.00 33.15 N ANISOU 2439 NZ LYS A 332 4372 4135 4088 -42 18 193 N ATOM 2440 N GLY A 333 54.609 5.150 45.625 1.00 22.88 N ANISOU 2440 N GLY A 333 2785 3016 2889 -34 -118 0 N ATOM 2441 CA GLY A 333 54.725 5.095 44.166 1.00 21.63 C ANISOU 2441 CA GLY A 333 2575 2867 2775 -31 -82 -3 C ATOM 2442 C GLY A 333 54.151 3.811 43.598 1.00 20.82 C ANISOU 2442 C GLY A 333 2477 2825 2605 -41 -136 -7 C ATOM 2443 O GLY A 333 54.752 3.189 42.714 1.00 20.25 O ANISOU 2443 O GLY A 333 2376 2708 2608 -74 -170 -10 O ATOM 2444 N ILE A 334 52.988 3.427 44.128 1.00 19.99 N ANISOU 2444 N ILE A 334 2419 2695 2479 -56 -135 3 N ATOM 2445 CA ILE A 334 52.305 2.178 43.793 1.00 19.20 C ANISOU 2445 CA ILE A 334 2322 2619 2354 -29 -176 39 C ATOM 2446 C ILE A 334 51.124 2.484 42.873 1.00 18.37 C ANISOU 2446 C ILE A 334 2248 2490 2240 -17 -181 54 C ATOM 2447 O ILE A 334 50.172 3.142 43.299 1.00 18.08 O ANISOU 2447 O ILE A 334 2180 2546 2141 -55 -275 8 O ATOM 2448 CB ILE A 334 51.785 1.480 45.083 1.00 19.18 C ANISOU 2448 CB ILE A 334 2347 2604 2336 -44 -171 67 C ATOM 2449 CG1 ILE A 334 52.938 1.203 46.063 1.00 19.95 C ANISOU 2449 CG1 ILE A 334 2414 2730 2436 6 -201 1 C ATOM 2450 CG2 ILE A 334 51.014 0.201 44.763 1.00 19.04 C ANISOU 2450 CG2 ILE A 334 2409 2534 2292 19 -148 -38 C ATOM 2451 CD1 ILE A 334 54.032 0.321 45.505 1.00 20.87 C ANISOU 2451 CD1 ILE A 334 2520 2903 2506 115 -198 -6 C ATOM 2452 N ALA A 335 51.221 2.015 41.623 1.00 17.70 N ANISOU 2452 N ALA A 335 2126 2406 2191 -17 -248 79 N ATOM 2453 CA ALA A 335 50.214 2.245 40.560 1.00 16.89 C ANISOU 2453 CA ALA A 335 2054 2302 2061 -38 -182 100 C ATOM 2454 C ALA A 335 49.990 3.732 40.244 1.00 16.14 C ANISOU 2454 C ALA A 335 1958 2200 1974 -49 -186 59 C ATOM 2455 O ALA A 335 50.696 4.601 40.754 1.00 16.15 O ANISOU 2455 O ALA A 335 1949 2259 1925 -106 -178 110 O ATOM 2456 CB ALA A 335 48.893 1.522 40.885 1.00 17.10 C ANISOU 2456 CB ALA A 335 2096 2316 2083 -25 -161 81 C ATOM 2457 N ASN A 336 49.016 4.037 39.385 1.00 15.55 N ANISOU 2457 N ASN A 336 1818 2116 1971 -73 -152 50 N ATOM 2458 CA ASN A 336 48.703 5.432 39.112 1.00 14.38 C ANISOU 2458 CA ASN A 336 1654 1991 1817 -65 -148 -3 C ATOM 2459 C ASN A 336 47.220 5.645 38.795 1.00 14.38 C ANISOU 2459 C ASN A 336 1670 1970 1822 -49 -119 -19 C ATOM 2460 O ASN A 336 46.839 6.672 38.250 1.00 14.50 O ANISOU 2460 O ASN A 336 1662 1905 1939 -64 -164 -79 O ATOM 2461 CB ASN A 336 49.599 5.972 37.981 1.00 14.99 C ANISOU 2461 CB ASN A 336 1768 2026 1902 -121 -129 11 C ATOM 2462 CG ASN A 336 49.484 5.167 36.703 1.00 14.97 C ANISOU 2462 CG ASN A 336 1786 2082 1819 -55 -58 47 C ATOM 2463 OD1 ASN A 336 48.451 4.543 36.441 1.00 16.35 O ANISOU 2463 OD1 ASN A 336 1819 2292 2098 -113 -142 1 O ATOM 2464 ND2 ASN A 336 50.545 5.176 35.892 1.00 14.84 N ANISOU 2464 ND2 ASN A 336 1748 1993 1897 -71 -63 197 N ATOM 2465 N SER A 337 46.401 4.671 39.172 1.00 14.07 N ANISOU 2465 N SER A 337 1557 1966 1820 -46 -147 -42 N ATOM 2466 CA SER A 337 44.972 4.703 38.873 1.00 14.43 C ANISOU 2466 CA SER A 337 1610 1992 1881 -53 -111 23 C ATOM 2467 C SER A 337 44.250 3.807 39.861 1.00 14.43 C ANISOU 2467 C SER A 337 1663 1982 1838 -48 -108 39 C ATOM 2468 O SER A 337 44.839 2.876 40.403 1.00 14.40 O ANISOU 2468 O SER A 337 1604 1967 1898 23 -159 121 O ATOM 2469 CB SER A 337 44.733 4.218 37.438 1.00 14.52 C ANISOU 2469 CB SER A 337 1619 2026 1868 -51 -97 5 C ATOM 2470 OG SER A 337 43.355 4.278 37.064 1.00 14.68 O ANISOU 2470 OG SER A 337 1647 2065 1862 -43 -259 0 O ATOM 2471 N ILE A 338 42.966 4.064 40.073 1.00 13.97 N ANISOU 2471 N ILE A 338 1668 1928 1712 2 -52 38 N ATOM 2472 CA ILE A 338 42.180 3.251 41.012 1.00 14.43 C ANISOU 2472 CA ILE A 338 1775 1939 1768 -85 -66 -10 C ATOM 2473 C ILE A 338 40.785 3.007 40.452 1.00 14.44 C ANISOU 2473 C ILE A 338 1801 1901 1783 -58 -114 11 C ATOM 2474 O ILE A 338 40.152 3.919 39.910 1.00 14.73 O ANISOU 2474 O ILE A 338 1873 1905 1815 -20 -86 -2 O ATOM 2475 CB ILE A 338 42.069 3.930 42.409 1.00 14.64 C ANISOU 2475 CB ILE A 338 1810 1972 1777 -97 -47 -4 C ATOM 2476 CG1 ILE A 338 41.259 3.058 43.392 1.00 14.26 C ANISOU 2476 CG1 ILE A 338 1799 1961 1657 -98 -38 -9 C ATOM 2477 CG2 ILE A 338 41.474 5.348 42.281 1.00 14.76 C ANISOU 2477 CG2 ILE A 338 1934 1907 1767 -47 -103 89 C ATOM 2478 CD1 ILE A 338 41.325 3.550 44.851 1.00 15.42 C ANISOU 2478 CD1 ILE A 338 2014 2135 1707 -43 -116 -26 C ATOM 2479 N LEU A 339 40.334 1.763 40.569 1.00 14.85 N ANISOU 2479 N LEU A 339 1887 1917 1835 -70 -111 31 N ATOM 2480 CA LEU A 339 38.961 1.403 40.226 1.00 15.12 C ANISOU 2480 CA LEU A 339 1990 1886 1869 -106 -77 29 C ATOM 2481 C LEU A 339 38.065 1.818 41.398 1.00 15.11 C ANISOU 2481 C LEU A 339 1942 2000 1796 -80 -86 43 C ATOM 2482 O LEU A 339 38.382 1.528 42.561 1.00 16.04 O ANISOU 2482 O LEU A 339 2020 2271 1801 -96 -124 108 O ATOM 2483 CB LEU A 339 38.882 -0.111 40.000 1.00 15.99 C ANISOU 2483 CB LEU A 339 2179 1950 1944 -128 -60 30 C ATOM 2484 CG LEU A 339 37.836 -0.602 39.022 1.00 17.03 C ANISOU 2484 CG LEU A 339 2367 2017 2086 -121 -67 109 C ATOM 2485 CD1 LEU A 339 38.067 0.024 37.646 1.00 16.63 C ANISOU 2485 CD1 LEU A 339 2445 1907 1966 -258 -109 133 C ATOM 2486 CD2 LEU A 339 37.842 -2.119 38.958 1.00 15.80 C ANISOU 2486 CD2 LEU A 339 2142 1870 1992 -136 -95 -13 C ATOM 2487 N ILE A 340 36.963 2.505 41.108 1.00 13.89 N ANISOU 2487 N ILE A 340 1845 1857 1575 -60 -123 44 N ATOM 2488 CA ILE A 340 36.051 2.956 42.153 1.00 14.10 C ANISOU 2488 CA ILE A 340 1778 1904 1674 -43 -126 37 C ATOM 2489 C ILE A 340 34.794 2.088 42.155 1.00 14.69 C ANISOU 2489 C ILE A 340 1844 2036 1698 -70 -73 77 C ATOM 2490 O ILE A 340 33.977 2.161 41.236 1.00 14.53 O ANISOU 2490 O ILE A 340 1815 2132 1572 -38 -120 36 O ATOM 2491 CB ILE A 340 35.687 4.463 42.007 1.00 13.66 C ANISOU 2491 CB ILE A 340 1810 1836 1544 -37 -81 4 C ATOM 2492 CG1 ILE A 340 36.963 5.332 42.007 1.00 13.06 C ANISOU 2492 CG1 ILE A 340 1646 1905 1409 -7 -113 -42 C ATOM 2493 CG2 ILE A 340 34.634 4.889 43.074 1.00 14.75 C ANISOU 2493 CG2 ILE A 340 1822 1987 1794 -40 -68 10 C ATOM 2494 CD1 ILE A 340 37.726 5.481 43.368 1.00 14.75 C ANISOU 2494 CD1 ILE A 340 2012 2043 1548 -47 -172 2 C ATOM 2495 N LYS A 341 34.675 1.247 43.178 1.00 14.91 N ANISOU 2495 N LYS A 341 1919 2051 1695 -90 -81 99 N ATOM 2496 CA LYS A 341 33.488 0.417 43.369 1.00 14.96 C ANISOU 2496 CA LYS A 341 1899 2086 1698 -56 -18 69 C ATOM 2497 C LYS A 341 32.766 0.940 44.600 1.00 14.90 C ANISOU 2497 C LYS A 341 1909 2020 1730 -68 -26 115 C ATOM 2498 O LYS A 341 33.186 0.649 45.714 1.00 14.93 O ANISOU 2498 O LYS A 341 1913 2139 1621 -9 -10 156 O ATOM 2499 CB LYS A 341 33.891 -1.046 43.536 1.00 15.03 C ANISOU 2499 CB LYS A 341 1981 2079 1649 -100 -14 64 C ATOM 2500 CG LYS A 341 34.420 -1.692 42.259 1.00 15.68 C ANISOU 2500 CG LYS A 341 1988 2119 1848 -41 44 -49 C ATOM 2501 CD LYS A 341 34.990 -3.088 42.470 1.00 15.71 C ANISOU 2501 CD LYS A 341 1964 2196 1806 -15 -29 21 C ATOM 2502 CE LYS A 341 35.150 -3.791 41.129 1.00 18.12 C ANISOU 2502 CE LYS A 341 2295 2407 2181 30 10 -151 C ATOM 2503 NZ LYS A 341 36.051 -4.969 41.162 1.00 17.34 N ANISOU 2503 NZ LYS A 341 1925 2556 2105 13 57 32 N ATOM 2504 N PHE A 342 31.709 1.739 44.412 1.00 14.11 N ANISOU 2504 N PHE A 342 1803 1892 1664 -44 17 119 N ATOM 2505 CA PHE A 342 31.109 2.402 45.562 1.00 14.75 C ANISOU 2505 CA PHE A 342 1900 1889 1815 -30 10 100 C ATOM 2506 C PHE A 342 30.566 1.474 46.636 1.00 14.62 C ANISOU 2506 C PHE A 342 1927 1867 1760 -41 19 106 C ATOM 2507 O PHE A 342 30.457 1.881 47.786 1.00 15.13 O ANISOU 2507 O PHE A 342 2008 1947 1794 30 94 128 O ATOM 2508 CB PHE A 342 30.157 3.591 45.245 1.00 14.05 C ANISOU 2508 CB PHE A 342 1843 1803 1693 -24 0 59 C ATOM 2509 CG PHE A 342 28.982 3.285 44.310 1.00 14.49 C ANISOU 2509 CG PHE A 342 1904 1759 1840 -54 -75 -36 C ATOM 2510 CD1 PHE A 342 28.531 1.974 44.037 1.00 13.35 C ANISOU 2510 CD1 PHE A 342 1695 1687 1689 -92 -76 -87 C ATOM 2511 CD2 PHE A 342 28.298 4.354 43.728 1.00 15.44 C ANISOU 2511 CD2 PHE A 342 1940 1982 1943 -42 -79 -41 C ATOM 2512 CE1 PHE A 342 27.421 1.765 43.178 1.00 13.50 C ANISOU 2512 CE1 PHE A 342 1725 1757 1647 43 -79 103 C ATOM 2513 CE2 PHE A 342 27.208 4.154 42.863 1.00 14.88 C ANISOU 2513 CE2 PHE A 342 1914 1880 1859 -62 -93 80 C ATOM 2514 CZ PHE A 342 26.764 2.860 42.593 1.00 14.18 C ANISOU 2514 CZ PHE A 342 1868 1777 1742 14 34 -40 C ATOM 2515 N ASN A 343 30.285 0.215 46.281 1.00 14.88 N ANISOU 2515 N ASN A 343 2008 1880 1762 19 20 83 N ATOM 2516 CA ASN A 343 29.787 -0.732 47.295 1.00 15.04 C ANISOU 2516 CA ASN A 343 2008 1928 1776 7 -15 95 C ATOM 2517 C ASN A 343 30.910 -1.367 48.134 1.00 15.40 C ANISOU 2517 C ASN A 343 2047 1995 1809 14 -54 116 C ATOM 2518 O ASN A 343 30.624 -2.067 49.119 1.00 16.22 O ANISOU 2518 O ASN A 343 2178 2129 1853 45 -61 192 O ATOM 2519 CB ASN A 343 28.824 -1.784 46.717 1.00 15.68 C ANISOU 2519 CB ASN A 343 2076 2031 1847 -20 -1 73 C ATOM 2520 CG ASN A 343 29.531 -2.903 45.987 1.00 14.35 C ANISOU 2520 CG ASN A 343 1818 1908 1727 -9 -65 109 C ATOM 2521 OD1 ASN A 343 30.559 -2.692 45.347 1.00 14.83 O ANISOU 2521 OD1 ASN A 343 1952 2024 1660 133 -6 31 O ATOM 2522 ND2 ASN A 343 28.957 -4.112 46.056 1.00 14.80 N ANISOU 2522 ND2 ASN A 343 2011 1990 1620 -68 -120 142 N ATOM 2523 N GLN A 344 32.160 -1.132 47.729 1.00 15.18 N ANISOU 2523 N GLN A 344 2034 1976 1757 52 -90 95 N ATOM 2524 CA GLN A 344 33.343 -1.555 48.500 1.00 15.91 C ANISOU 2524 CA GLN A 344 2067 2087 1890 47 -16 103 C ATOM 2525 C GLN A 344 33.661 -0.556 49.581 1.00 15.70 C ANISOU 2525 C GLN A 344 2020 2111 1832 51 -37 84 C ATOM 2526 O GLN A 344 34.457 -0.833 50.488 1.00 16.09 O ANISOU 2526 O GLN A 344 2081 2208 1823 114 -22 134 O ATOM 2527 CB GLN A 344 34.566 -1.696 47.597 1.00 16.56 C ANISOU 2527 CB GLN A 344 2159 2147 1985 33 10 44 C ATOM 2528 CG GLN A 344 34.641 -3.004 46.880 1.00 18.39 C ANISOU 2528 CG GLN A 344 2471 2286 2227 84 34 74 C ATOM 2529 CD GLN A 344 35.949 -3.186 46.159 1.00 18.03 C ANISOU 2529 CD GLN A 344 2315 2329 2204 77 -19 18 C ATOM 2530 OE1 GLN A 344 36.556 -2.227 45.672 1.00 17.20 O ANISOU 2530 OE1 GLN A 344 2170 2187 2175 223 -83 0 O ATOM 2531 NE2 GLN A 344 36.395 -4.425 46.079 1.00 19.62 N ANISOU 2531 NE2 GLN A 344 2635 2455 2363 99 -157 47 N ATOM 2532 N ILE A 345 33.071 0.627 49.477 1.00 15.74 N ANISOU 2532 N ILE A 345 2090 2092 1795 51 -45 51 N ATOM 2533 CA ILE A 345 33.260 1.637 50.504 1.00 16.70 C ANISOU 2533 CA ILE A 345 2225 2170 1948 49 -88 0 C ATOM 2534 C ILE A 345 31.939 1.931 51.245 1.00 16.48 C ANISOU 2534 C ILE A 345 2208 2205 1845 38 -77 -12 C ATOM 2535 O ILE A 345 31.924 2.034 52.481 1.00 17.95 O ANISOU 2535 O ILE A 345 2376 2467 1977 66 -116 6 O ATOM 2536 CB ILE A 345 34.030 2.877 49.974 1.00 17.51 C ANISOU 2536 CB ILE A 345 2332 2294 2026 32 -50 -18 C ATOM 2537 CG1 ILE A 345 34.537 3.732 51.144 1.00 18.98 C ANISOU 2537 CG1 ILE A 345 2607 2327 2274 -20 -78 -43 C ATOM 2538 CG2 ILE A 345 33.200 3.662 48.961 1.00 18.71 C ANISOU 2538 CG2 ILE A 345 2586 2311 2210 68 -123 -64 C ATOM 2539 CD1 ILE A 345 35.529 3.007 52.056 1.00 22.73 C ANISOU 2539 CD1 ILE A 345 3056 2954 2626 71 -85 -29 C ATOM 2540 N GLY A 346 30.834 2.017 50.500 1.00 15.82 N ANISOU 2540 N GLY A 346 2132 2112 1767 113 -68 65 N ATOM 2541 CA GLY A 346 29.499 1.890 51.089 1.00 15.56 C ANISOU 2541 CA GLY A 346 2152 2102 1657 109 -114 55 C ATOM 2542 C GLY A 346 28.657 3.140 51.261 1.00 15.41 C ANISOU 2542 C GLY A 346 2165 2095 1595 89 -123 48 C ATOM 2543 O GLY A 346 27.502 3.051 51.659 1.00 15.72 O ANISOU 2543 O GLY A 346 2268 2123 1579 111 -153 84 O ATOM 2544 N SER A 347 29.227 4.305 50.987 1.00 15.07 N ANISOU 2544 N SER A 347 2189 2050 1485 98 -132 8 N ATOM 2545 CA SER A 347 28.433 5.531 51.009 1.00 15.23 C ANISOU 2545 CA SER A 347 2186 2022 1576 71 -110 19 C ATOM 2546 C SER A 347 28.873 6.484 49.911 1.00 14.77 C ANISOU 2546 C SER A 347 2069 1994 1546 61 -109 -25 C ATOM 2547 O SER A 347 30.025 6.448 49.477 1.00 14.83 O ANISOU 2547 O SER A 347 2118 2018 1497 107 -150 -20 O ATOM 2548 CB SER A 347 28.542 6.226 52.365 1.00 15.45 C ANISOU 2548 CB SER A 347 2220 2061 1589 23 -98 23 C ATOM 2549 OG SER A 347 29.815 6.820 52.505 1.00 16.08 O ANISOU 2549 OG SER A 347 2323 2198 1588 -21 -35 114 O ATOM 2550 N LEU A 348 27.952 7.340 49.466 1.00 14.06 N ANISOU 2550 N LEU A 348 2021 1860 1458 125 -112 -78 N ATOM 2551 CA LEU A 348 28.302 8.353 48.482 1.00 14.81 C ANISOU 2551 CA LEU A 348 2023 1929 1674 141 -70 -21 C ATOM 2552 C LEU A 348 29.377 9.320 48.989 1.00 14.71 C ANISOU 2552 C LEU A 348 2046 1929 1615 114 -55 -62 C ATOM 2553 O LEU A 348 30.318 9.634 48.284 1.00 14.77 O ANISOU 2553 O LEU A 348 2091 1889 1631 168 -92 -118 O ATOM 2554 CB LEU A 348 27.055 9.099 47.973 1.00 14.77 C ANISOU 2554 CB LEU A 348 1945 2002 1663 134 -71 12 C ATOM 2555 CG LEU A 348 27.307 10.149 46.876 1.00 14.82 C ANISOU 2555 CG LEU A 348 1908 2008 1713 147 11 67 C ATOM 2556 CD1 LEU A 348 27.929 9.506 45.629 1.00 14.13 C ANISOU 2556 CD1 LEU A 348 2038 1865 1463 258 -11 108 C ATOM 2557 CD2 LEU A 348 26.008 10.841 46.481 1.00 15.25 C ANISOU 2557 CD2 LEU A 348 1995 1969 1830 179 -55 70 C ATOM 2558 N THR A 349 29.247 9.786 50.228 1.00 15.71 N ANISOU 2558 N THR A 349 2160 2101 1707 85 -99 -47 N ATOM 2559 CA THR A 349 30.230 10.726 50.759 1.00 15.87 C ANISOU 2559 CA THR A 349 2219 2034 1776 58 -84 -60 C ATOM 2560 C THR A 349 31.650 10.161 50.704 1.00 15.75 C ANISOU 2560 C THR A 349 2206 2053 1725 23 -97 -34 C ATOM 2561 O THR A 349 32.571 10.826 50.241 1.00 15.99 O ANISOU 2561 O THR A 349 2234 2029 1810 33 -146 -16 O ATOM 2562 CB THR A 349 29.858 11.151 52.183 1.00 16.16 C ANISOU 2562 CB THR A 349 2245 2170 1725 47 -72 -29 C ATOM 2563 OG1 THR A 349 28.559 11.751 52.171 1.00 16.65 O ANISOU 2563 OG1 THR A 349 2356 2204 1765 94 -118 -148 O ATOM 2564 CG2 THR A 349 30.858 12.136 52.745 1.00 16.54 C ANISOU 2564 CG2 THR A 349 2231 2087 1964 -39 5 -56 C ATOM 2565 N GLU A 350 31.815 8.917 51.150 1.00 15.76 N ANISOU 2565 N GLU A 350 2188 2053 1746 82 -159 0 N ATOM 2566 CA GLU A 350 33.131 8.283 51.134 1.00 15.86 C ANISOU 2566 CA GLU A 350 2208 2051 1764 68 -71 1 C ATOM 2567 C GLU A 350 33.634 8.043 49.722 1.00 15.80 C ANISOU 2567 C GLU A 350 2159 2076 1767 18 -126 -22 C ATOM 2568 O GLU A 350 34.831 8.143 49.466 1.00 16.39 O ANISOU 2568 O GLU A 350 2228 2201 1796 10 -188 -67 O ATOM 2569 CB GLU A 350 33.102 6.984 51.934 1.00 15.63 C ANISOU 2569 CB GLU A 350 2201 2050 1686 102 -113 31 C ATOM 2570 CG GLU A 350 32.918 7.222 53.419 1.00 17.09 C ANISOU 2570 CG GLU A 350 2390 2292 1809 52 -33 -31 C ATOM 2571 CD GLU A 350 32.642 5.935 54.172 1.00 18.04 C ANISOU 2571 CD GLU A 350 2461 2329 2061 -3 -116 83 C ATOM 2572 OE1 GLU A 350 31.580 5.313 53.938 1.00 18.16 O ANISOU 2572 OE1 GLU A 350 2401 2600 1899 54 17 218 O ATOM 2573 OE2 GLU A 350 33.502 5.550 55.000 1.00 20.60 O ANISOU 2573 OE2 GLU A 350 2772 2816 2235 109 -205 239 O ATOM 2574 N THR A 351 32.710 7.737 48.805 1.00 15.50 N ANISOU 2574 N THR A 351 2133 2028 1728 -3 -127 -17 N ATOM 2575 CA THR A 351 33.062 7.555 47.401 1.00 15.02 C ANISOU 2575 CA THR A 351 2051 1940 1713 -3 -101 3 C ATOM 2576 C THR A 351 33.648 8.842 46.809 1.00 14.68 C ANISOU 2576 C THR A 351 1999 1896 1683 -3 -82 11 C ATOM 2577 O THR A 351 34.684 8.805 46.134 1.00 13.98 O ANISOU 2577 O THR A 351 1914 1731 1666 -17 -86 61 O ATOM 2578 CB THR A 351 31.846 7.070 46.601 1.00 14.95 C ANISOU 2578 CB THR A 351 2050 1974 1656 -53 -96 -33 C ATOM 2579 OG1 THR A 351 31.445 5.792 47.104 1.00 15.19 O ANISOU 2579 OG1 THR A 351 2154 2017 1601 66 -91 -61 O ATOM 2580 CG2 THR A 351 32.175 6.956 45.104 1.00 15.03 C ANISOU 2580 CG2 THR A 351 1996 2022 1691 31 4 -19 C ATOM 2581 N LEU A 352 33.007 9.976 47.094 1.00 14.97 N ANISOU 2581 N LEU A 352 2077 1916 1692 -15 -70 17 N ATOM 2582 CA LEU A 352 33.543 11.265 46.660 1.00 15.63 C ANISOU 2582 CA LEU A 352 2108 1952 1879 40 -55 -16 C ATOM 2583 C LEU A 352 34.950 11.503 47.212 1.00 15.71 C ANISOU 2583 C LEU A 352 2092 1991 1885 8 -50 -7 C ATOM 2584 O LEU A 352 35.831 11.965 46.484 1.00 16.23 O ANISOU 2584 O LEU A 352 2111 2057 1999 41 -47 -39 O ATOM 2585 CB LEU A 352 32.608 12.410 47.052 1.00 15.74 C ANISOU 2585 CB LEU A 352 2061 2005 1911 94 -23 -17 C ATOM 2586 CG LEU A 352 31.225 12.430 46.400 1.00 17.24 C ANISOU 2586 CG LEU A 352 2221 2258 2069 109 -96 -87 C ATOM 2587 CD1 LEU A 352 30.526 13.733 46.737 1.00 18.76 C ANISOU 2587 CD1 LEU A 352 2514 2296 2319 175 -16 -67 C ATOM 2588 CD2 LEU A 352 31.327 12.280 44.896 1.00 18.72 C ANISOU 2588 CD2 LEU A 352 2469 2532 2111 67 19 35 C ATOM 2589 N ALA A 353 35.161 11.163 48.488 1.00 16.03 N ANISOU 2589 N ALA A 353 2094 2096 1900 -14 -115 -17 N ATOM 2590 CA ALA A 353 36.484 11.290 49.110 1.00 16.58 C ANISOU 2590 CA ALA A 353 2134 2242 1921 -50 -100 -4 C ATOM 2591 C ALA A 353 37.558 10.457 48.406 1.00 16.52 C ANISOU 2591 C ALA A 353 2122 2166 1989 -54 -124 -4 C ATOM 2592 O ALA A 353 38.666 10.944 48.208 1.00 17.52 O ANISOU 2592 O ALA A 353 2183 2360 2111 -45 -76 -40 O ATOM 2593 CB ALA A 353 36.418 10.960 50.616 1.00 16.30 C ANISOU 2593 CB ALA A 353 2092 2223 1878 -64 -129 41 C ATOM 2594 N ALA A 354 37.221 9.232 47.980 1.00 15.50 N ANISOU 2594 N ALA A 354 2038 2026 1824 -54 -146 -20 N ATOM 2595 CA ALA A 354 38.189 8.372 47.282 1.00 15.67 C ANISOU 2595 CA ALA A 354 2115 1991 1845 -60 -128 13 C ATOM 2596 C ALA A 354 38.549 8.950 45.916 1.00 15.57 C ANISOU 2596 C ALA A 354 2068 1955 1891 -37 -90 -21 C ATOM 2597 O ALA A 354 39.724 9.002 45.535 1.00 16.58 O ANISOU 2597 O ALA A 354 2184 2099 2013 -22 -103 79 O ATOM 2598 CB ALA A 354 37.654 6.951 47.144 1.00 16.39 C ANISOU 2598 CB ALA A 354 2220 2070 1937 -51 -119 -40 C ATOM 2599 N ILE A 355 37.532 9.393 45.186 1.00 15.59 N ANISOU 2599 N ILE A 355 2025 1940 1957 -15 -81 9 N ATOM 2600 CA ILE A 355 37.761 9.984 43.874 1.00 15.70 C ANISOU 2600 CA ILE A 355 2021 1979 1964 -10 -88 -9 C ATOM 2601 C ILE A 355 38.663 11.219 44.006 1.00 16.78 C ANISOU 2601 C ILE A 355 2113 2130 2132 -28 -93 -39 C ATOM 2602 O ILE A 355 39.593 11.398 43.230 1.00 17.61 O ANISOU 2602 O ILE A 355 2266 2155 2269 -140 -59 -101 O ATOM 2603 CB ILE A 355 36.413 10.314 43.178 1.00 15.47 C ANISOU 2603 CB ILE A 355 1976 1941 1959 24 -100 57 C ATOM 2604 CG1 ILE A 355 35.654 9.009 42.908 1.00 14.46 C ANISOU 2604 CG1 ILE A 355 1884 1879 1730 -20 -64 -32 C ATOM 2605 CG2 ILE A 355 36.629 11.104 41.887 1.00 16.22 C ANISOU 2605 CG2 ILE A 355 2117 2110 1935 60 35 38 C ATOM 2606 CD1 ILE A 355 34.164 9.179 42.567 1.00 15.33 C ANISOU 2606 CD1 ILE A 355 1942 1939 1941 34 -43 -21 C ATOM 2607 N LYS A 356 38.384 12.049 45.006 1.00 17.53 N ANISOU 2607 N LYS A 356 2261 2200 2198 -36 -96 -92 N ATOM 2608 CA LYS A 356 39.173 13.253 45.244 1.00 18.81 C ANISOU 2608 CA LYS A 356 2397 2350 2399 -75 -43 -124 C ATOM 2609 C LYS A 356 40.629 12.944 45.606 1.00 19.06 C ANISOU 2609 C LYS A 356 2431 2406 2404 -64 -41 -122 C ATOM 2610 O LYS A 356 41.545 13.586 45.079 1.00 19.30 O ANISOU 2610 O LYS A 356 2448 2429 2455 -94 -22 -161 O ATOM 2611 CB LYS A 356 38.526 14.117 46.332 1.00 19.25 C ANISOU 2611 CB LYS A 356 2428 2407 2477 -23 -11 -120 C ATOM 2612 CG LYS A 356 39.256 15.424 46.538 1.00 21.84 C ANISOU 2612 CG LYS A 356 2811 2631 2852 -114 -19 -118 C ATOM 2613 CD LYS A 356 38.438 16.414 47.353 1.00 24.94 C ANISOU 2613 CD LYS A 356 3186 2979 3308 46 76 -180 C ATOM 2614 CE LYS A 356 39.179 17.759 47.492 1.00 26.63 C ANISOU 2614 CE LYS A 356 3502 3204 3412 -105 30 -67 C ATOM 2615 NZ LYS A 356 40.510 17.623 48.171 1.00 27.91 N ANISOU 2615 NZ LYS A 356 3414 3572 3618 -12 -18 -115 N ATOM 2616 N MET A 357 40.843 11.968 46.488 1.00 19.18 N ANISOU 2616 N MET A 357 2428 2447 2412 -49 -79 -154 N ATOM 2617 CA MET A 357 42.204 11.556 46.852 1.00 20.02 C ANISOU 2617 CA MET A 357 2569 2591 2446 -25 -124 -162 C ATOM 2618 C MET A 357 43.013 11.162 45.618 1.00 19.76 C ANISOU 2618 C MET A 357 2501 2540 2466 -42 -103 -140 C ATOM 2619 O MET A 357 44.169 11.560 45.471 1.00 20.30 O ANISOU 2619 O MET A 357 2542 2650 2521 -70 -81 -149 O ATOM 2620 CB MET A 357 42.192 10.421 47.873 1.00 19.82 C ANISOU 2620 CB MET A 357 2503 2553 2471 -16 -61 -147 C ATOM 2621 CG MET A 357 43.578 9.901 48.208 1.00 21.04 C ANISOU 2621 CG MET A 357 2674 2767 2552 -26 -148 -152 C ATOM 2622 SD MET A 357 43.575 8.681 49.516 1.00 21.96 S ANISOU 2622 SD MET A 357 3032 2908 2401 48 -389 -315 S ATOM 2623 CE MET A 357 43.276 9.731 50.953 1.00 22.82 C ANISOU 2623 CE MET A 357 3020 3079 2570 73 -111 -200 C ATOM 2624 N ALA A 358 42.394 10.398 44.717 1.00 19.23 N ANISOU 2624 N ALA A 358 2426 2454 2425 -76 -127 -141 N ATOM 2625 CA ALA A 358 43.074 9.987 43.494 1.00 18.98 C ANISOU 2625 CA ALA A 358 2388 2410 2410 -70 -141 -151 C ATOM 2626 C ALA A 358 43.448 11.211 42.660 1.00 19.19 C ANISOU 2626 C ALA A 358 2406 2429 2454 -100 -123 -175 C ATOM 2627 O ALA A 358 44.598 11.370 42.256 1.00 19.20 O ANISOU 2627 O ALA A 358 2396 2427 2470 -86 -78 -230 O ATOM 2628 CB ALA A 358 42.192 9.040 42.695 1.00 19.09 C ANISOU 2628 CB ALA A 358 2395 2446 2411 -94 -155 -177 C ATOM 2629 N LYS A 359 42.471 12.081 42.408 1.00 19.20 N ANISOU 2629 N LYS A 359 2384 2420 2490 -98 -123 -147 N ATOM 2630 CA LYS A 359 42.700 13.257 41.569 1.00 19.73 C ANISOU 2630 CA LYS A 359 2479 2476 2539 -114 -126 -118 C ATOM 2631 C LYS A 359 43.779 14.170 42.135 1.00 19.58 C ANISOU 2631 C LYS A 359 2471 2422 2544 -125 -96 -134 C ATOM 2632 O LYS A 359 44.651 14.626 41.401 1.00 19.47 O ANISOU 2632 O LYS A 359 2517 2379 2499 -143 -151 -130 O ATOM 2633 CB LYS A 359 41.413 14.034 41.350 1.00 19.96 C ANISOU 2633 CB LYS A 359 2522 2474 2587 -63 -108 -116 C ATOM 2634 CG LYS A 359 40.501 13.368 40.359 1.00 22.38 C ANISOU 2634 CG LYS A 359 2892 2816 2794 -99 -102 -71 C ATOM 2635 CD LYS A 359 39.443 14.328 39.923 1.00 25.26 C ANISOU 2635 CD LYS A 359 3151 3262 3183 34 -105 5 C ATOM 2636 CE LYS A 359 38.269 13.597 39.345 1.00 26.55 C ANISOU 2636 CE LYS A 359 3403 3419 3265 -99 -88 -17 C ATOM 2637 NZ LYS A 359 37.046 14.245 39.831 1.00 27.03 N ANISOU 2637 NZ LYS A 359 3502 3471 3297 -14 -5 -99 N ATOM 2638 N ASP A 360 43.724 14.415 43.438 1.00 20.18 N ANISOU 2638 N ASP A 360 2533 2542 2590 -130 -149 -69 N ATOM 2639 CA ASP A 360 44.714 15.281 44.086 1.00 21.00 C ANISOU 2639 CA ASP A 360 2606 2616 2754 -140 -123 -110 C ATOM 2640 C ASP A 360 46.137 14.761 43.893 1.00 21.22 C ANISOU 2640 C ASP A 360 2621 2682 2760 -130 -109 -80 C ATOM 2641 O ASP A 360 47.085 15.552 43.833 1.00 22.61 O ANISOU 2641 O ASP A 360 2805 2777 3007 -189 -102 -95 O ATOM 2642 CB ASP A 360 44.431 15.408 45.584 1.00 21.26 C ANISOU 2642 CB ASP A 360 2661 2669 2747 -114 -86 -58 C ATOM 2643 CG ASP A 360 43.198 16.239 45.895 1.00 22.60 C ANISOU 2643 CG ASP A 360 2838 2789 2960 -114 -93 -86 C ATOM 2644 OD1 ASP A 360 42.719 16.982 45.015 1.00 24.37 O ANISOU 2644 OD1 ASP A 360 3183 2864 3212 -90 -108 -2 O ATOM 2645 OD2 ASP A 360 42.705 16.149 47.040 1.00 24.52 O ANISOU 2645 OD2 ASP A 360 3219 2978 3118 -194 -36 -172 O ATOM 2646 N ALA A 361 46.285 13.441 43.810 1.00 20.78 N ANISOU 2646 N ALA A 361 2538 2665 2690 -125 -126 -142 N ATOM 2647 CA ALA A 361 47.594 12.792 43.667 1.00 20.86 C ANISOU 2647 CA ALA A 361 2590 2667 2666 -94 -77 -111 C ATOM 2648 C ALA A 361 47.985 12.582 42.200 1.00 20.46 C ANISOU 2648 C ALA A 361 2526 2611 2634 -89 -53 -115 C ATOM 2649 O ALA A 361 49.050 12.030 41.897 1.00 21.51 O ANISOU 2649 O ALA A 361 2609 2821 2740 -73 -67 -116 O ATOM 2650 CB ALA A 361 47.602 11.478 44.415 1.00 20.67 C ANISOU 2650 CB ALA A 361 2519 2678 2656 -134 -46 -115 C ATOM 2651 N GLY A 362 47.113 13.008 41.290 1.00 20.02 N ANISOU 2651 N GLY A 362 2528 2521 2557 -68 -6 -80 N ATOM 2652 CA GLY A 362 47.346 12.833 39.855 1.00 18.86 C ANISOU 2652 CA GLY A 362 2417 2343 2405 -135 -55 -72 C ATOM 2653 C GLY A 362 47.010 11.437 39.356 1.00 18.30 C ANISOU 2653 C GLY A 362 2355 2284 2312 -99 -34 -52 C ATOM 2654 O GLY A 362 47.232 11.119 38.189 1.00 18.28 O ANISOU 2654 O GLY A 362 2380 2268 2295 -164 -4 -80 O ATOM 2655 N TYR A 363 46.484 10.602 40.245 1.00 17.37 N ANISOU 2655 N TYR A 363 2221 2164 2215 -110 -73 -28 N ATOM 2656 CA TYR A 363 45.955 9.298 39.845 1.00 17.13 C ANISOU 2656 CA TYR A 363 2140 2193 2173 -74 -118 -70 C ATOM 2657 C TYR A 363 44.623 9.494 39.129 1.00 16.88 C ANISOU 2657 C TYR A 363 2119 2179 2114 -49 -123 -61 C ATOM 2658 O TYR A 363 43.917 10.475 39.373 1.00 16.39 O ANISOU 2658 O TYR A 363 2041 2187 1998 -21 -227 -130 O ATOM 2659 CB TYR A 363 45.721 8.411 41.067 1.00 17.48 C ANISOU 2659 CB TYR A 363 2159 2281 2199 -71 -103 -6 C ATOM 2660 CG TYR A 363 46.948 7.733 41.656 1.00 16.80 C ANISOU 2660 CG TYR A 363 2084 2217 2081 -14 -50 -72 C ATOM 2661 CD1 TYR A 363 48.169 8.411 41.774 1.00 17.75 C ANISOU 2661 CD1 TYR A 363 2098 2390 2254 42 -55 -63 C ATOM 2662 CD2 TYR A 363 46.876 6.423 42.120 1.00 17.75 C ANISOU 2662 CD2 TYR A 363 2146 2309 2288 4 -155 -16 C ATOM 2663 CE1 TYR A 363 49.288 7.785 42.327 1.00 17.31 C ANISOU 2663 CE1 TYR A 363 2159 2305 2111 69 -213 -78 C ATOM 2664 CE2 TYR A 363 47.997 5.781 42.682 1.00 18.15 C ANISOU 2664 CE2 TYR A 363 2158 2379 2359 30 -145 -27 C ATOM 2665 CZ TYR A 363 49.196 6.480 42.778 1.00 17.78 C ANISOU 2665 CZ TYR A 363 2151 2431 2172 -38 -119 -37 C ATOM 2666 OH TYR A 363 50.316 5.879 43.314 1.00 19.40 O ANISOU 2666 OH TYR A 363 2472 2542 2356 84 -149 93 O ATOM 2667 N THR A 364 44.285 8.563 38.238 1.00 16.21 N ANISOU 2667 N THR A 364 1956 2076 2125 -121 -120 -54 N ATOM 2668 CA THR A 364 42.968 8.578 37.612 1.00 16.37 C ANISOU 2668 CA THR A 364 1945 2145 2130 -84 -95 18 C ATOM 2669 C THR A 364 41.997 7.658 38.349 1.00 16.24 C ANISOU 2669 C THR A 364 1913 2118 2137 -66 -78 36 C ATOM 2670 O THR A 364 42.391 6.609 38.892 1.00 16.51 O ANISOU 2670 O THR A 364 1957 2161 2154 28 -99 76 O ATOM 2671 CB THR A 364 43.030 8.161 36.147 1.00 15.96 C ANISOU 2671 CB THR A 364 1851 2109 2103 -112 -88 -6 C ATOM 2672 OG1 THR A 364 43.714 6.907 36.046 1.00 16.41 O ANISOU 2672 OG1 THR A 364 1848 2185 2200 -181 -118 23 O ATOM 2673 CG2 THR A 364 43.768 9.219 35.328 1.00 16.57 C ANISOU 2673 CG2 THR A 364 1953 2239 2102 -126 -23 13 C ATOM 2674 N ALA A 365 40.727 8.049 38.348 1.00 15.52 N ANISOU 2674 N ALA A 365 1813 2014 2070 -61 -107 21 N ATOM 2675 CA ALA A 365 39.668 7.252 38.949 1.00 14.85 C ANISOU 2675 CA ALA A 365 1714 2006 1920 -114 -133 -33 C ATOM 2676 C ALA A 365 38.807 6.663 37.838 1.00 14.24 C ANISOU 2676 C ALA A 365 1755 1886 1770 -142 -85 -35 C ATOM 2677 O ALA A 365 38.320 7.391 36.970 1.00 14.99 O ANISOU 2677 O ALA A 365 1771 2014 1908 -157 -152 -58 O ATOM 2678 CB ALA A 365 38.811 8.117 39.863 1.00 14.41 C ANISOU 2678 CB ALA A 365 1648 1969 1858 -173 -79 -36 C ATOM 2679 N VAL A 366 38.613 5.349 37.884 1.00 13.58 N ANISOU 2679 N VAL A 366 1629 1846 1681 -147 -85 -88 N ATOM 2680 CA VAL A 366 37.783 4.673 36.892 1.00 11.98 C ANISOU 2680 CA VAL A 366 1433 1656 1463 -109 -80 -43 C ATOM 2681 C VAL A 366 36.545 4.160 37.611 1.00 11.65 C ANISOU 2681 C VAL A 366 1409 1564 1453 -53 -57 -31 C ATOM 2682 O VAL A 366 36.660 3.282 38.468 1.00 12.20 O ANISOU 2682 O VAL A 366 1410 1762 1462 -37 10 53 O ATOM 2683 CB VAL A 366 38.542 3.496 36.245 1.00 11.77 C ANISOU 2683 CB VAL A 366 1369 1657 1446 -110 -40 -10 C ATOM 2684 CG1 VAL A 366 37.672 2.782 35.208 1.00 12.54 C ANISOU 2684 CG1 VAL A 366 1538 1726 1500 -119 -113 -21 C ATOM 2685 CG2 VAL A 366 39.862 3.971 35.631 1.00 12.01 C ANISOU 2685 CG2 VAL A 366 1323 1652 1584 -214 25 -97 C ATOM 2686 N ILE A 367 35.366 4.706 37.280 1.00 11.39 N ANISOU 2686 N ILE A 367 1403 1489 1433 -61 -29 12 N ATOM 2687 CA ILE A 367 34.136 4.301 37.973 1.00 11.19 C ANISOU 2687 CA ILE A 367 1408 1453 1388 -37 -40 6 C ATOM 2688 C ILE A 367 33.694 2.945 37.466 1.00 11.08 C ANISOU 2688 C ILE A 367 1460 1398 1352 -48 13 73 C ATOM 2689 O ILE A 367 33.554 2.768 36.259 1.00 11.33 O ANISOU 2689 O ILE A 367 1517 1480 1305 -173 51 60 O ATOM 2690 CB ILE A 367 32.991 5.336 37.781 1.00 11.12 C ANISOU 2690 CB ILE A 367 1413 1393 1419 -1 21 -1 C ATOM 2691 CG1 ILE A 367 33.503 6.754 38.090 1.00 12.64 C ANISOU 2691 CG1 ILE A 367 1662 1551 1590 -32 -107 -67 C ATOM 2692 CG2 ILE A 367 31.773 4.965 38.630 1.00 11.10 C ANISOU 2692 CG2 ILE A 367 1329 1376 1511 -62 -69 6 C ATOM 2693 CD1 ILE A 367 34.146 6.932 39.491 1.00 13.67 C ANISOU 2693 CD1 ILE A 367 1870 1871 1453 -5 -112 -10 C ATOM 2694 N SER A 368 33.454 1.998 38.382 1.00 10.98 N ANISOU 2694 N SER A 368 1440 1371 1358 -34 9 118 N ATOM 2695 CA SER A 368 33.255 0.603 38.000 1.00 10.76 C ANISOU 2695 CA SER A 368 1327 1462 1296 -34 -21 73 C ATOM 2696 C SER A 368 31.877 0.051 38.373 1.00 10.65 C ANISOU 2696 C SER A 368 1365 1412 1268 -56 36 50 C ATOM 2697 O SER A 368 31.315 0.391 39.416 1.00 10.72 O ANISOU 2697 O SER A 368 1431 1533 1109 -107 49 82 O ATOM 2698 CB SER A 368 34.309 -0.276 38.698 1.00 11.25 C ANISOU 2698 CB SER A 368 1495 1437 1340 18 -41 105 C ATOM 2699 OG SER A 368 34.210 -1.624 38.272 1.00 12.64 O ANISOU 2699 OG SER A 368 1493 1713 1595 56 -105 171 O ATOM 2700 N HIS A 369 31.379 -0.832 37.518 1.00 10.01 N ANISOU 2700 N HIS A 369 1265 1445 1092 -137 -40 61 N ATOM 2701 CA HIS A 369 30.305 -1.770 37.867 1.00 10.70 C ANISOU 2701 CA HIS A 369 1423 1451 1191 -107 0 40 C ATOM 2702 C HIS A 369 30.798 -2.896 38.795 1.00 10.77 C ANISOU 2702 C HIS A 369 1422 1522 1148 -61 1 26 C ATOM 2703 O HIS A 369 31.973 -2.931 39.179 1.00 10.60 O ANISOU 2703 O HIS A 369 1417 1543 1065 -16 -19 1 O ATOM 2704 CB HIS A 369 29.698 -2.383 36.585 1.00 10.79 C ANISOU 2704 CB HIS A 369 1431 1519 1148 -101 2 24 C ATOM 2705 CG HIS A 369 30.622 -3.260 35.769 1.00 11.41 C ANISOU 2705 CG HIS A 369 1441 1497 1395 -132 64 118 C ATOM 2706 ND1 HIS A 369 31.934 -3.554 36.096 1.00 13.80 N ANISOU 2706 ND1 HIS A 369 1803 1736 1703 0 85 31 N ATOM 2707 CD2 HIS A 369 30.376 -3.926 34.615 1.00 9.97 C ANISOU 2707 CD2 HIS A 369 1324 1220 1244 -136 -47 41 C ATOM 2708 CE1 HIS A 369 32.451 -4.360 35.178 1.00 10.68 C ANISOU 2708 CE1 HIS A 369 1101 1497 1459 -158 -110 132 C ATOM 2709 NE2 HIS A 369 31.527 -4.591 34.263 1.00 13.88 N ANISOU 2709 NE2 HIS A 369 1781 1764 1727 -79 17 77 N ATOM 2710 N ARG A 370 29.889 -3.817 39.129 1.00 10.63 N ANISOU 2710 N ARG A 370 1463 1362 1214 -58 12 29 N ATOM 2711 CA ARG A 370 30.249 -5.119 39.703 1.00 11.38 C ANISOU 2711 CA ARG A 370 1534 1520 1267 -60 45 100 C ATOM 2712 C ARG A 370 29.755 -6.245 38.791 1.00 12.04 C ANISOU 2712 C ARG A 370 1652 1526 1393 17 52 106 C ATOM 2713 O ARG A 370 28.930 -6.020 37.902 1.00 12.32 O ANISOU 2713 O ARG A 370 1708 1602 1370 9 28 81 O ATOM 2714 CB ARG A 370 29.621 -5.271 41.099 1.00 11.05 C ANISOU 2714 CB ARG A 370 1497 1516 1184 -84 61 63 C ATOM 2715 CG ARG A 370 30.018 -4.192 42.121 1.00 11.36 C ANISOU 2715 CG ARG A 370 1475 1596 1244 -66 64 -29 C ATOM 2716 CD ARG A 370 31.528 -4.153 42.382 1.00 11.97 C ANISOU 2716 CD ARG A 370 1610 1654 1282 -5 -169 -36 C ATOM 2717 NE ARG A 370 32.097 -5.449 42.754 1.00 12.58 N ANISOU 2717 NE ARG A 370 1664 1786 1329 93 -69 37 N ATOM 2718 CZ ARG A 370 32.429 -5.804 44.000 1.00 14.68 C ANISOU 2718 CZ ARG A 370 1889 2013 1673 135 -117 16 C ATOM 2719 NH1 ARG A 370 32.214 -4.980 45.022 1.00 15.36 N ANISOU 2719 NH1 ARG A 370 2041 2071 1724 99 -140 0 N ATOM 2720 NH2 ARG A 370 32.941 -7.008 44.222 1.00 17.42 N ANISOU 2720 NH2 ARG A 370 2336 2269 2013 239 -172 137 N ATOM 2721 N SER A 371 30.200 -7.473 39.047 1.00 13.21 N ANISOU 2721 N SER A 371 1759 1581 1677 66 20 25 N ATOM 2722 CA SER A 371 29.738 -8.613 38.263 1.00 13.54 C ANISOU 2722 CA SER A 371 1889 1588 1668 73 -44 63 C ATOM 2723 C SER A 371 28.234 -8.801 38.384 1.00 13.40 C ANISOU 2723 C SER A 371 1903 1568 1618 17 -34 96 C ATOM 2724 O SER A 371 27.575 -9.081 37.392 1.00 13.62 O ANISOU 2724 O SER A 371 1885 1767 1522 8 -68 105 O ATOM 2725 CB SER A 371 30.478 -9.886 38.660 1.00 14.36 C ANISOU 2725 CB SER A 371 1959 1686 1808 94 -59 89 C ATOM 2726 OG SER A 371 31.843 -9.744 38.347 1.00 18.26 O ANISOU 2726 OG SER A 371 2329 2175 2432 64 74 108 O ATOM 2727 N GLY A 372 27.703 -8.667 39.602 1.00 13.01 N ANISOU 2727 N GLY A 372 1843 1588 1511 23 -9 84 N ATOM 2728 CA GLY A 372 26.253 -8.667 39.837 1.00 12.80 C ANISOU 2728 CA GLY A 372 1869 1571 1422 51 -50 144 C ATOM 2729 C GLY A 372 25.745 -7.238 39.835 1.00 12.90 C ANISOU 2729 C GLY A 372 1859 1591 1452 -13 -32 115 C ATOM 2730 O GLY A 372 26.034 -6.453 40.752 1.00 13.80 O ANISOU 2730 O GLY A 372 2064 1715 1465 -51 -81 186 O ATOM 2731 N GLU A 373 25.020 -6.886 38.777 1.00 12.48 N ANISOU 2731 N GLU A 373 1743 1571 1426 -25 -20 131 N ATOM 2732 CA GLU A 373 24.483 -5.542 38.628 1.00 11.54 C ANISOU 2732 CA GLU A 373 1599 1478 1308 -47 38 175 C ATOM 2733 C GLU A 373 22.954 -5.524 38.702 1.00 12.51 C ANISOU 2733 C GLU A 373 1713 1545 1495 -42 38 143 C ATOM 2734 O GLU A 373 22.318 -6.570 38.879 1.00 12.42 O ANISOU 2734 O GLU A 373 1728 1477 1511 -64 87 264 O ATOM 2735 CB GLU A 373 24.980 -4.932 37.295 1.00 11.73 C ANISOU 2735 CB GLU A 373 1593 1481 1381 -94 66 163 C ATOM 2736 CG GLU A 373 26.288 -4.154 37.459 1.00 10.52 C ANISOU 2736 CG GLU A 373 1414 1340 1242 -15 24 28 C ATOM 2737 CD GLU A 373 26.130 -2.940 38.372 1.00 11.05 C ANISOU 2737 CD GLU A 373 1453 1366 1377 61 13 21 C ATOM 2738 OE1 GLU A 373 24.993 -2.432 38.516 1.00 11.18 O ANISOU 2738 OE1 GLU A 373 1450 1475 1322 46 109 135 O ATOM 2739 OE2 GLU A 373 27.147 -2.494 38.936 1.00 11.60 O ANISOU 2739 OE2 GLU A 373 1637 1506 1264 28 -106 68 O ATOM 2740 N THR A 374 22.366 -4.337 38.589 1.00 12.00 N ANISOU 2740 N THR A 374 1664 1540 1352 32 22 209 N ATOM 2741 CA THR A 374 20.924 -4.218 38.401 1.00 12.49 C ANISOU 2741 CA THR A 374 1723 1582 1441 22 14 174 C ATOM 2742 C THR A 374 20.660 -3.223 37.286 1.00 11.94 C ANISOU 2742 C THR A 374 1711 1446 1379 -3 -16 134 C ATOM 2743 O THR A 374 21.612 -2.712 36.667 1.00 12.34 O ANISOU 2743 O THR A 374 1738 1458 1492 22 -6 88 O ATOM 2744 CB THR A 374 20.202 -3.713 39.671 1.00 13.28 C ANISOU 2744 CB THR A 374 1877 1710 1458 69 -10 128 C ATOM 2745 OG1 THR A 374 20.589 -2.365 39.942 1.00 13.07 O ANISOU 2745 OG1 THR A 374 1762 1662 1540 -23 66 267 O ATOM 2746 CG2 THR A 374 20.544 -4.576 40.889 1.00 12.27 C ANISOU 2746 CG2 THR A 374 1761 1413 1486 144 142 282 C ATOM 2747 N GLU A 375 19.373 -2.939 37.077 1.00 12.42 N ANISOU 2747 N GLU A 375 1794 1510 1412 -11 -95 167 N ATOM 2748 CA GLU A 375 18.879 -1.871 36.186 1.00 13.57 C ANISOU 2748 CA GLU A 375 1919 1675 1561 -11 -111 187 C ATOM 2749 C GLU A 375 19.367 -0.471 36.595 1.00 13.03 C ANISOU 2749 C GLU A 375 1873 1630 1448 -43 -83 168 C ATOM 2750 O GLU A 375 19.257 0.482 35.820 1.00 13.52 O ANISOU 2750 O GLU A 375 2118 1575 1444 -112 -97 147 O ATOM 2751 CB GLU A 375 17.338 -1.791 36.213 1.00 14.83 C ANISOU 2751 CB GLU A 375 1947 1935 1753 44 -176 165 C ATOM 2752 CG GLU A 375 16.495 -3.010 36.232 1.00 19.41 C ANISOU 2752 CG GLU A 375 2619 2445 2311 -59 -73 288 C ATOM 2753 CD GLU A 375 16.318 -3.634 37.612 1.00 20.17 C ANISOU 2753 CD GLU A 375 2613 2604 2443 -94 70 253 C ATOM 2754 OE1 GLU A 375 17.238 -4.345 37.983 1.00 21.67 O ANISOU 2754 OE1 GLU A 375 2512 2695 3026 -41 -19 171 O ATOM 2755 OE2 GLU A 375 15.262 -3.450 38.288 1.00 18.89 O ANISOU 2755 OE2 GLU A 375 2513 2185 2479 45 203 295 O ATOM 2756 N ASP A 376 19.854 -0.338 37.821 1.00 11.95 N ANISOU 2756 N ASP A 376 1651 1550 1339 -123 -43 220 N ATOM 2757 CA ASP A 376 20.302 0.943 38.359 1.00 11.25 C ANISOU 2757 CA ASP A 376 1557 1439 1278 -27 -53 207 C ATOM 2758 C ASP A 376 21.422 1.512 37.493 1.00 11.87 C ANISOU 2758 C ASP A 376 1633 1422 1452 -28 0 174 C ATOM 2759 O ASP A 376 22.269 0.755 37.031 1.00 13.02 O ANISOU 2759 O ASP A 376 1717 1580 1650 -38 38 172 O ATOM 2760 CB ASP A 376 20.808 0.725 39.788 1.00 11.78 C ANISOU 2760 CB ASP A 376 1658 1545 1270 -63 -95 177 C ATOM 2761 CG ASP A 376 21.227 1.994 40.456 1.00 11.99 C ANISOU 2761 CG ASP A 376 1636 1394 1523 7 -15 254 C ATOM 2762 OD1 ASP A 376 22.434 2.308 40.413 1.00 12.04 O ANISOU 2762 OD1 ASP A 376 1565 1629 1378 -25 236 173 O ATOM 2763 OD2 ASP A 376 20.358 2.664 41.059 1.00 14.97 O ANISOU 2763 OD2 ASP A 376 1781 1798 2108 60 189 166 O ATOM 2764 N ALA A 377 21.446 2.841 37.301 1.00 11.49 N ANISOU 2764 N ALA A 377 1567 1373 1422 -74 -22 180 N ATOM 2765 CA ALA A 377 22.505 3.460 36.495 1.00 10.48 C ANISOU 2765 CA ALA A 377 1426 1314 1239 -56 -4 124 C ATOM 2766 C ALA A 377 23.233 4.596 37.225 1.00 11.01 C ANISOU 2766 C ALA A 377 1515 1419 1248 -63 4 101 C ATOM 2767 O ALA A 377 23.814 5.506 36.589 1.00 10.45 O ANISOU 2767 O ALA A 377 1439 1537 992 -141 64 140 O ATOM 2768 CB ALA A 377 21.940 3.953 35.161 1.00 11.06 C ANISOU 2768 CB ALA A 377 1530 1416 1254 -52 -58 60 C ATOM 2769 N THR A 378 23.219 4.540 38.555 1.00 10.82 N ANISOU 2769 N THR A 378 1511 1385 1215 -46 33 102 N ATOM 2770 CA THR A 378 23.825 5.590 39.373 1.00 11.01 C ANISOU 2770 CA THR A 378 1460 1445 1277 24 29 77 C ATOM 2771 C THR A 378 25.292 5.837 39.018 1.00 10.74 C ANISOU 2771 C THR A 378 1409 1381 1290 73 22 76 C ATOM 2772 O THR A 378 25.747 6.973 39.088 1.00 10.41 O ANISOU 2772 O THR A 378 1374 1343 1239 124 80 75 O ATOM 2773 CB THR A 378 23.726 5.274 40.868 1.00 11.06 C ANISOU 2773 CB THR A 378 1480 1412 1307 47 43 80 C ATOM 2774 OG1 THR A 378 22.383 4.896 41.180 1.00 11.23 O ANISOU 2774 OG1 THR A 378 1519 1515 1233 3 139 59 O ATOM 2775 CG2 THR A 378 24.144 6.484 41.717 1.00 12.40 C ANISOU 2775 CG2 THR A 378 1692 1612 1406 -34 6 60 C ATOM 2776 N ILE A 379 26.047 4.786 38.655 1.00 10.33 N ANISOU 2776 N ILE A 379 1343 1355 1223 109 38 58 N ATOM 2777 CA ILE A 379 27.466 5.029 38.335 1.00 10.77 C ANISOU 2777 CA ILE A 379 1487 1383 1222 74 2 83 C ATOM 2778 C ILE A 379 27.663 5.977 37.150 1.00 10.60 C ANISOU 2778 C ILE A 379 1427 1398 1202 15 -1 96 C ATOM 2779 O ILE A 379 28.701 6.644 37.074 1.00 10.42 O ANISOU 2779 O ILE A 379 1452 1261 1244 -87 -80 15 O ATOM 2780 CB ILE A 379 28.318 3.746 38.145 1.00 9.97 C ANISOU 2780 CB ILE A 379 1474 1288 1023 122 18 23 C ATOM 2781 CG1 ILE A 379 27.804 2.860 37.001 1.00 11.47 C ANISOU 2781 CG1 ILE A 379 1516 1578 1263 111 -62 -100 C ATOM 2782 CG2 ILE A 379 28.418 2.957 39.448 1.00 11.25 C ANISOU 2782 CG2 ILE A 379 1732 1439 1100 26 -139 165 C ATOM 2783 CD1 ILE A 379 28.791 1.722 36.676 1.00 11.24 C ANISOU 2783 CD1 ILE A 379 1539 1429 1302 99 125 98 C ATOM 2784 N ALA A 380 26.676 6.042 36.242 1.00 10.04 N ANISOU 2784 N ALA A 380 1446 1331 1037 9 5 109 N ATOM 2785 CA ALA A 380 26.761 6.995 35.131 1.00 10.61 C ANISOU 2785 CA ALA A 380 1453 1418 1160 68 -37 102 C ATOM 2786 C ALA A 380 26.732 8.433 35.670 1.00 10.58 C ANISOU 2786 C ALA A 380 1459 1416 1143 34 -57 77 C ATOM 2787 O ALA A 380 27.609 9.250 35.362 1.00 10.99 O ANISOU 2787 O ALA A 380 1502 1470 1201 18 -39 -6 O ATOM 2788 CB ALA A 380 25.634 6.760 34.149 1.00 10.07 C ANISOU 2788 CB ALA A 380 1530 1349 945 5 -37 35 C ATOM 2789 N ASP A 381 25.740 8.737 36.501 1.00 11.12 N ANISOU 2789 N ASP A 381 1491 1467 1263 74 -16 31 N ATOM 2790 CA ASP A 381 25.662 10.070 37.128 1.00 11.61 C ANISOU 2790 CA ASP A 381 1536 1451 1421 57 -19 27 C ATOM 2791 C ASP A 381 26.900 10.375 37.958 1.00 11.84 C ANISOU 2791 C ASP A 381 1626 1466 1406 54 -28 39 C ATOM 2792 O ASP A 381 27.393 11.509 37.966 1.00 12.15 O ANISOU 2792 O ASP A 381 1664 1566 1385 -13 26 91 O ATOM 2793 CB ASP A 381 24.428 10.179 38.023 1.00 12.45 C ANISOU 2793 CB ASP A 381 1596 1634 1501 19 11 31 C ATOM 2794 CG ASP A 381 23.132 10.125 37.240 1.00 13.67 C ANISOU 2794 CG ASP A 381 1714 1767 1713 4 -43 18 C ATOM 2795 OD1 ASP A 381 22.840 9.060 36.640 1.00 13.82 O ANISOU 2795 OD1 ASP A 381 1710 1809 1732 123 80 -107 O ATOM 2796 OD2 ASP A 381 22.401 11.156 37.225 1.00 16.49 O ANISOU 2796 OD2 ASP A 381 2034 2013 2215 150 -9 -100 O ATOM 2797 N LEU A 382 27.406 9.354 38.658 1.00 11.26 N ANISOU 2797 N LEU A 382 1542 1469 1265 57 -74 86 N ATOM 2798 CA LEU A 382 28.590 9.528 39.487 1.00 11.63 C ANISOU 2798 CA LEU A 382 1594 1413 1411 55 -91 97 C ATOM 2799 C LEU A 382 29.803 9.909 38.646 1.00 11.43 C ANISOU 2799 C LEU A 382 1579 1384 1379 47 -65 58 C ATOM 2800 O LEU A 382 30.519 10.855 38.986 1.00 12.07 O ANISOU 2800 O LEU A 382 1674 1507 1403 -35 -60 15 O ATOM 2801 CB LEU A 382 28.869 8.241 40.259 1.00 11.27 C ANISOU 2801 CB LEU A 382 1611 1425 1246 94 -160 161 C ATOM 2802 CG LEU A 382 30.132 8.245 41.125 1.00 11.51 C ANISOU 2802 CG LEU A 382 1518 1442 1412 103 -109 20 C ATOM 2803 CD1 LEU A 382 30.103 9.336 42.167 1.00 13.50 C ANISOU 2803 CD1 LEU A 382 1857 1656 1613 -12 -114 -84 C ATOM 2804 CD2 LEU A 382 30.310 6.868 41.764 1.00 11.91 C ANISOU 2804 CD2 LEU A 382 1759 1300 1464 46 -105 93 C ATOM 2805 N ALA A 383 30.025 9.185 37.546 1.00 11.09 N ANISOU 2805 N ALA A 383 1567 1362 1282 2 -75 60 N ATOM 2806 CA ALA A 383 31.166 9.466 36.674 1.00 11.24 C ANISOU 2806 CA ALA A 383 1545 1384 1343 46 -64 52 C ATOM 2807 C ALA A 383 31.086 10.872 36.085 1.00 11.41 C ANISOU 2807 C ALA A 383 1541 1393 1400 -11 -65 55 C ATOM 2808 O ALA A 383 32.078 11.604 36.071 1.00 12.25 O ANISOU 2808 O ALA A 383 1557 1624 1474 -82 -93 134 O ATOM 2809 CB ALA A 383 31.269 8.425 35.563 1.00 11.22 C ANISOU 2809 CB ALA A 383 1554 1412 1297 -5 -115 -17 C ATOM 2810 N VAL A 384 29.902 11.262 35.618 1.00 11.14 N ANISOU 2810 N VAL A 384 1508 1315 1408 20 -63 77 N ATOM 2811 CA VAL A 384 29.734 12.627 35.068 1.00 11.55 C ANISOU 2811 CA VAL A 384 1576 1330 1480 -5 -92 35 C ATOM 2812 C VAL A 384 29.878 13.720 36.131 1.00 12.24 C ANISOU 2812 C VAL A 384 1660 1433 1556 -8 -63 4 C ATOM 2813 O VAL A 384 30.614 14.715 35.919 1.00 12.46 O ANISOU 2813 O VAL A 384 1716 1452 1566 -106 -54 -62 O ATOM 2814 CB VAL A 384 28.396 12.767 34.336 1.00 11.87 C ANISOU 2814 CB VAL A 384 1623 1354 1533 38 -101 62 C ATOM 2815 CG1 VAL A 384 28.202 14.208 33.858 1.00 11.68 C ANISOU 2815 CG1 VAL A 384 1509 1309 1621 -57 -120 138 C ATOM 2816 CG2 VAL A 384 28.354 11.782 33.153 1.00 11.44 C ANISOU 2816 CG2 VAL A 384 1670 1169 1507 54 -54 56 C ATOM 2817 N GLY A 385 29.190 13.529 37.252 1.00 12.87 N ANISOU 2817 N GLY A 385 1735 1528 1624 12 -78 -108 N ATOM 2818 CA GLY A 385 29.132 14.536 38.325 1.00 12.83 C ANISOU 2818 CA GLY A 385 1694 1570 1609 19 -58 -123 C ATOM 2819 C GLY A 385 30.440 14.781 39.043 1.00 13.46 C ANISOU 2819 C GLY A 385 1783 1606 1722 41 -100 -131 C ATOM 2820 O GLY A 385 30.609 15.823 39.688 1.00 14.00 O ANISOU 2820 O GLY A 385 1910 1550 1857 28 -210 -103 O ATOM 2821 N THR A 386 31.364 13.824 38.960 1.00 12.98 N ANISOU 2821 N THR A 386 1723 1535 1673 26 -94 -86 N ATOM 2822 CA THR A 386 32.691 14.028 39.543 1.00 13.34 C ANISOU 2822 CA THR A 386 1804 1576 1685 -23 -83 -72 C ATOM 2823 C THR A 386 33.744 14.272 38.473 1.00 13.89 C ANISOU 2823 C THR A 386 1858 1620 1800 -62 -63 -32 C ATOM 2824 O THR A 386 34.927 14.391 38.792 1.00 14.25 O ANISOU 2824 O THR A 386 1872 1706 1833 -150 -85 -139 O ATOM 2825 CB THR A 386 33.147 12.797 40.372 1.00 12.94 C ANISOU 2825 CB THR A 386 1816 1480 1619 23 -69 -89 C ATOM 2826 OG1 THR A 386 33.185 11.630 39.530 1.00 12.94 O ANISOU 2826 OG1 THR A 386 1874 1343 1699 -5 -81 -94 O ATOM 2827 CG2 THR A 386 32.223 12.565 41.549 1.00 13.95 C ANISOU 2827 CG2 THR A 386 1794 1715 1789 -67 -16 -42 C ATOM 2828 N ALA A 387 33.316 14.310 37.205 1.00 13.95 N ANISOU 2828 N ALA A 387 1907 1568 1824 -116 -58 -47 N ATOM 2829 CA ALA A 387 34.230 14.418 36.056 1.00 13.90 C ANISOU 2829 CA ALA A 387 1866 1564 1852 -70 -19 -13 C ATOM 2830 C ALA A 387 35.390 13.427 36.198 1.00 14.08 C ANISOU 2830 C ALA A 387 1810 1675 1862 -80 1 -21 C ATOM 2831 O ALA A 387 36.562 13.791 36.038 1.00 14.56 O ANISOU 2831 O ALA A 387 1848 1817 1865 -85 82 -19 O ATOM 2832 CB ALA A 387 34.753 15.851 35.906 1.00 14.43 C ANISOU 2832 CB ALA A 387 1899 1616 1965 -86 -63 -17 C ATOM 2833 N ALA A 388 35.051 12.184 36.556 1.00 13.44 N ANISOU 2833 N ALA A 388 1753 1549 1803 -105 -14 -14 N ATOM 2834 CA ALA A 388 36.058 11.139 36.825 1.00 13.27 C ANISOU 2834 CA ALA A 388 1613 1623 1804 -100 -1 55 C ATOM 2835 C ALA A 388 36.895 10.867 35.592 1.00 13.47 C ANISOU 2835 C ALA A 388 1640 1679 1795 -62 -53 24 C ATOM 2836 O ALA A 388 38.106 10.660 35.690 1.00 14.28 O ANISOU 2836 O ALA A 388 1617 1951 1854 -77 -66 109 O ATOM 2837 CB ALA A 388 35.388 9.842 37.316 1.00 13.58 C ANISOU 2837 CB ALA A 388 1688 1650 1822 -134 23 69 C ATOM 2838 N GLY A 389 36.232 10.845 34.440 1.00 12.72 N ANISOU 2838 N GLY A 389 1515 1618 1699 -85 -82 48 N ATOM 2839 CA GLY A 389 36.889 10.751 33.158 1.00 12.16 C ANISOU 2839 CA GLY A 389 1400 1568 1649 -80 -41 15 C ATOM 2840 C GLY A 389 36.883 9.372 32.522 1.00 11.43 C ANISOU 2840 C GLY A 389 1329 1499 1514 -134 6 21 C ATOM 2841 O GLY A 389 37.089 9.254 31.324 1.00 11.83 O ANISOU 2841 O GLY A 389 1376 1634 1482 -168 -51 61 O ATOM 2842 N GLN A 390 36.668 8.329 33.324 1.00 10.73 N ANISOU 2842 N GLN A 390 1263 1378 1434 -6 -40 68 N ATOM 2843 CA GLN A 390 36.591 6.962 32.812 1.00 10.22 C ANISOU 2843 CA GLN A 390 1180 1336 1364 -114 31 45 C ATOM 2844 C GLN A 390 35.531 6.137 33.536 1.00 10.31 C ANISOU 2844 C GLN A 390 1317 1274 1324 -113 39 79 C ATOM 2845 O GLN A 390 35.218 6.394 34.700 1.00 10.61 O ANISOU 2845 O GLN A 390 1399 1209 1422 -98 45 117 O ATOM 2846 CB GLN A 390 37.943 6.247 32.933 1.00 10.68 C ANISOU 2846 CB GLN A 390 1230 1447 1381 -82 49 75 C ATOM 2847 CG GLN A 390 39.050 6.839 32.037 1.00 10.09 C ANISOU 2847 CG GLN A 390 1101 1485 1246 -57 -1 155 C ATOM 2848 CD GLN A 390 40.379 6.135 32.258 1.00 10.84 C ANISOU 2848 CD GLN A 390 1173 1503 1441 -44 -7 -2 C ATOM 2849 OE1 GLN A 390 40.647 5.064 31.685 1.00 13.66 O ANISOU 2849 OE1 GLN A 390 1413 1962 1813 -48 -92 27 O ATOM 2850 NE2 GLN A 390 41.220 6.728 33.115 1.00 12.80 N ANISOU 2850 NE2 GLN A 390 1404 1913 1544 -135 -29 -106 N ATOM 2851 N ILE A 391 35.012 5.133 32.829 1.00 9.92 N ANISOU 2851 N ILE A 391 1233 1258 1275 -139 7 81 N ATOM 2852 CA ILE A 391 34.009 4.220 33.379 1.00 9.54 C ANISOU 2852 CA ILE A 391 1162 1242 1218 -88 -9 99 C ATOM 2853 C ILE A 391 34.284 2.810 32.852 1.00 10.04 C ANISOU 2853 C ILE A 391 1266 1277 1271 -113 -10 25 C ATOM 2854 O ILE A 391 34.779 2.630 31.727 1.00 10.20 O ANISOU 2854 O ILE A 391 1447 1221 1207 -229 -42 102 O ATOM 2855 CB ILE A 391 32.561 4.673 33.023 1.00 9.41 C ANISOU 2855 CB ILE A 391 1108 1293 1172 -97 38 95 C ATOM 2856 CG1 ILE A 391 31.512 3.922 33.863 1.00 9.66 C ANISOU 2856 CG1 ILE A 391 1037 1428 1205 -21 89 111 C ATOM 2857 CG2 ILE A 391 32.287 4.594 31.504 1.00 9.90 C ANISOU 2857 CG2 ILE A 391 1204 1418 1140 -139 -4 171 C ATOM 2858 CD1 ILE A 391 30.119 4.573 33.836 1.00 10.33 C ANISOU 2858 CD1 ILE A 391 1140 1496 1287 46 -24 75 C ATOM 2859 N LYS A 392 34.004 1.823 33.700 1.00 10.24 N ANISOU 2859 N LYS A 392 1324 1280 1287 -109 -50 48 N ATOM 2860 CA LYS A 392 34.136 0.417 33.348 1.00 10.47 C ANISOU 2860 CA LYS A 392 1278 1337 1362 -68 -11 12 C ATOM 2861 C LYS A 392 32.796 -0.201 33.729 1.00 10.76 C ANISOU 2861 C LYS A 392 1352 1405 1328 -127 6 19 C ATOM 2862 O LYS A 392 32.564 -0.509 34.907 1.00 10.77 O ANISOU 2862 O LYS A 392 1357 1424 1309 -210 27 107 O ATOM 2863 CB LYS A 392 35.262 -0.237 34.154 1.00 10.58 C ANISOU 2863 CB LYS A 392 1355 1376 1287 -65 -14 -46 C ATOM 2864 CG LYS A 392 35.511 -1.708 33.852 1.00 11.03 C ANISOU 2864 CG LYS A 392 1400 1384 1405 29 -109 160 C ATOM 2865 CD LYS A 392 36.610 -2.265 34.784 1.00 11.91 C ANISOU 2865 CD LYS A 392 1267 1573 1684 32 -159 37 C ATOM 2866 CE LYS A 392 36.744 -3.751 34.664 1.00 13.96