HEADER GLYCOSIDE HYDROLASE FAMILY 10 10-APR-00 1E0W TITLE XYLANASE 10A FROM SREPTOMYCES LIVIDANS. NATIVE STRUCTURE AT TITLE 2 1.2 ANGSTROM RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: XYLANASE A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC MODULE; COMPND 5 EC: 3.2.1.8; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS; SOURCE 3 ORGANISM_TAXID: 1916; SOURCE 4 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1916; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: IAF 19 KEYWDS GLYCOSIDE HYDROLASE FAMILY 10, XYLANASE, XYLAN DEGRADATION EXPDTA X-RAY DIFFRACTION AUTHOR V.DUCROS,S.J.CHARNOCK,U.DEREWENDA,Z.S.DEREWENDA,Z.DAUTER, AUTHOR 2 C.DUPONT,F.SHARECK,R.MOROSOLI,D.KLUEPFEL,G.J.DAVIES REVDAT 3 24-FEB-09 1E0W 1 VERSN REVDAT 2 25-MAY-01 1E0W 1 JRNL REVDAT 1 05-APR-01 1E0W 0 JRNL AUTH V.DUCROS,S.J.CHARNOCK,U.DEREWENDA,Z.S.DEREWENDA, JRNL AUTH 2 Z.DAUTER,C.DUPONT,F.SHARECK,R.MOROSOLI,D.KLUEPFEL, JRNL AUTH 3 G.J.DAVIES JRNL TITL SUBSTRATE SPECIFICITY IN GLYCOSIDE HYDROLASE JRNL TITL 2 FAMILY 10. STRUCTURAL AND KINETIC ANALYSIS OF THE JRNL TITL 3 STREPTOMYCES LIVIDANS XYLANASE 10A JRNL REF J.BIOL.CHEM. V. 275 23020 2000 JRNL REFN ISSN 0021-9258 JRNL PMID 10930426 JRNL DOI 10.1074/JBC.M00012900 REMARK 1 REMARK 1 REF J.BIOL.CHEM. V. 275 23027 2000 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 2 REMARK 1 AUTH U.DEREWENDA,L.SWENSON,R.GREEN,Y.WEI,R.MOROSOLI, REMARK 1 AUTH 2 F.SHARECK,D.KLUEPFEL,Z.S.DEREWENDA REMARK 1 TITL CRYSTAL STRUCTURE, AT 2.6 A RESOLUTION, OF THE REMARK 1 TITL 2 STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE REMARK 1 TITL 3 F FAMILY OF B-1,4-D-GLYCANASES REMARK 1 REF J.BIOL.CHEM. V. 269 20811 1994 REMARK 1 REFN ISSN 0021-9258 REMARK 1 PMID 8063693 REMARK 2 REMARK 2 RESOLUTION. 1.2 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.2 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 96 REMARK 3 NUMBER OF REFLECTIONS : 81581 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.098 REMARK 3 FREE R VALUE : 0.124 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 4292 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2385 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 438 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.010 ; 0.02 REMARK 3 ANGLE DISTANCE (A) : 0.025 ; 0.04 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.05 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.028 ; 0.03 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.098 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.15 ; 0.30 REMARK 3 MULTIPLE TORSION (A) : 0.24 ; 0.30 REMARK 3 H-BOND (X...Y) (A) : 0.13 ; 0.30 REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 5.2 ; 7.0 REMARK 3 STAGGERED (DEGREES) : 11.9 ; 15.0 REMARK 3 TRANSVERSE (DEGREES) : 27.3 ; 20.0 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.452 ; 3.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.270 ; 5.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.499 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.741 ; 6.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DOUBLY CONFIGURATED DISULPHIDE BOND REMARK 3 BETWEEN CYS168 AND CYS201 REMARK 4 REMARK 4 1E0W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-00. REMARK 100 THE PDBE ID CODE IS EBI-4838. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-NOV-97 REMARK 200 TEMPERATURE (KELVIN) : 297.0 REMARK 200 PH : 4.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X31 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84936 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.35000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.3 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 60MG/ML WAS CRYSTALLISED REMARK 280 WITH 5% PEG 4000, 100MM SODIUM ACETATE PH 4.6 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-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 35.12500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.19500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.46500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.19500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.12500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.46500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 303 REMARK 465 ASP A 304 REMARK 465 SER A 305 REMARK 465 SER A 306 REMARK 465 GLU A 307 REMARK 465 PRO A 308 REMARK 465 PRO A 309 REMARK 465 ALA A 310 REMARK 465 ASP A 311 REMARK 465 GLY A 312 REMARK 465 GLY A 313 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG A 102 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU A 236 42.08 -143.27 REMARK 500 VAL A 268 -77.11 -99.61 REMARK 500 THR A 279 65.27 31.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ACI REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: CATALYTIC ACID/BASE REMARK 800 REMARK 800 SITE_IDENTIFIER: NUC REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: CATALYTIC NUCLEOPHILE REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XAS RELATED DB: PDB REMARK 900 XYLANASE A REMARK 900 RELATED ID: 1E0V RELATED DB: PDB REMARK 900 XYLANASE 10A FROM SREPTOMYCES LIVIDANS. CELLOBIOSYL-ENZYME REMARK 900 INTERMEDIATE AT 1.7 A REMARK 900 RELATED ID: 1E0X RELATED DB: PDB REMARK 900 XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME REMARK 900 INTERMEDIATE AT 1.65 A REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND REMARK 999 TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE PDB FILE REMARK 999 IF AFTER CLEAVAGE OF THE SIGNAL PEPTIDE. REMARK 999 THE LAST 11 AMINO ACIDS ARE TOO DISORDERED REMARK 999 TO BE BUILT IN DENSITY DBREF 1E0W A 1 302 UNP P26514 XYNA_STRLI 42 343 SEQRES 1 A 313 ALA GLU SER THR LEU GLY ALA ALA ALA ALA GLN SER GLY SEQRES 2 A 313 ARG TYR PHE GLY THR ALA ILE ALA SER GLY ARG LEU SER SEQRES 3 A 313 ASP SER THR TYR THR SER ILE ALA GLY ARG GLU PHE ASN SEQRES 4 A 313 MET VAL THR ALA GLU ASN GLU MET LYS ILE ASP ALA THR SEQRES 5 A 313 GLU PRO GLN ARG GLY GLN PHE ASN PHE SER SER ALA ASP SEQRES 6 A 313 ARG VAL TYR ASN TRP ALA VAL GLN ASN GLY LYS GLN VAL SEQRES 7 A 313 ARG GLY HIS THR LEU ALA TRP HIS SER GLN GLN PRO GLY SEQRES 8 A 313 TRP MET GLN SER LEU SER GLY SER ALA LEU ARG GLN ALA SEQRES 9 A 313 MET ILE ASP HIS ILE ASN GLY VAL MET ALA HIS TYR LYS SEQRES 10 A 313 GLY LYS ILE VAL GLN TRP ASP VAL VAL ASN GLU ALA PHE SEQRES 11 A 313 ALA ASP GLY SER SER GLY ALA ARG ARG ASP SER ASN LEU SEQRES 12 A 313 GLN ARG SER GLY ASN ASP TRP ILE GLU VAL ALA PHE ARG SEQRES 13 A 313 THR ALA ARG ALA ALA ASP PRO SER ALA LYS LEU CYS TYR SEQRES 14 A 313 ASN ASP TYR ASN VAL GLU ASN TRP THR TRP ALA LYS THR SEQRES 15 A 313 GLN ALA MET TYR ASN MET VAL ARG ASP PHE LYS GLN ARG SEQRES 16 A 313 GLY VAL PRO ILE ASP CYS VAL GLY PHE GLN SER HIS PHE SEQRES 17 A 313 ASN SER GLY SER PRO TYR ASN SER ASN PHE ARG THR THR SEQRES 18 A 313 LEU GLN ASN PHE ALA ALA LEU GLY VAL ASP VAL ALA ILE SEQRES 19 A 313 THR GLU LEU ASP ILE GLN GLY ALA PRO ALA SER THR TYR SEQRES 20 A 313 ALA ASN VAL THR ASN ASP CYS LEU ALA VAL SER ARG CYS SEQRES 21 A 313 LEU GLY ILE THR VAL TRP GLY VAL ARG ASP SER ASP SER SEQRES 22 A 313 TRP ARG SER GLU GLN THR PRO LEU LEU PHE ASN ASN ASP SEQRES 23 A 313 GLY SER LYS LYS ALA ALA TYR THR ALA VAL LEU ASP ALA SEQRES 24 A 313 LEU ASN GLY GLY ASP SER SER GLU PRO PRO ALA ASP GLY SEQRES 25 A 313 GLY FORMUL 2 HOH *438(H2 O1) HELIX 1 1 THR A 4 GLN A 11 1 8 HELIX 2 2 ALA A 21 LEU A 25 5 5 HELIX 3 3 ASP A 27 PHE A 38 1 12 HELIX 4 4 LYS A 48 GLU A 53 1 6 HELIX 5 5 PHE A 61 ASN A 74 1 14 HELIX 6 6 PRO A 90 SER A 95 1 6 HELIX 7 7 SER A 97 TYR A 116 1 20 HELIX 8 8 SER A 141 SER A 146 1 6 HELIX 9 9 ASP A 149 ASP A 162 1 14 HELIX 10 10 TRP A 179 GLY A 196 1 18 HELIX 11 11 ASN A 217 ALA A 227 1 11 HELIX 12 12 PRO A 243 ALA A 256 1 14 HELIX 13 13 ASP A 270 SER A 273 5 4 HELIX 14 14 ARG A 275 THR A 279 5 5 HELIX 15 15 LYS A 290 GLY A 302 1 13 SHEET 1 A 4 GLY A 262 VAL A 265 0 SHEET 2 A 4 TYR A 15 ILE A 20 1 N TYR A 15 O ILE A 263 SHEET 3 A 4 MET A 40 ALA A 43 1 N MET A 40 O THR A 18 SHEET 4 A 4 GLN A 77 ARG A 79 1 N GLN A 77 O VAL A 41 SHEET 1 B 4 ASP A 231 ILE A 234 0 SHEET 2 B 4 CYS A 201 PHE A 204 1 N VAL A 202 O ASP A 231 SHEET 3 B 4 LYS A 166 ASP A 171 1 N TYR A 169 O CYS A 201 SHEET 4 B 4 GLN A 122 ASN A 127 1 N TRP A 123 O LYS A 166 SSBOND 1 CYS A 168 CYS A 201 1555 1555 2.08 SSBOND 2 CYS A 168 CYS A 201 1555 1555 1.98 SSBOND 3 CYS A 254 CYS A 260 1555 1555 2.05 CISPEP 1 HIS A 81 THR A 82 0 4.39 SITE 1 ACI 1 GLU A 128 SITE 1 NUC 1 GLU A 236 CRYST1 70.250 46.930 86.390 90.00 90.00 90.00 P 21 21 21 4 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 0.014235 0.000000 0.000000 0.00000 SCALE2 0.000000 0.021308 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011575 0.00000 ATOM 1 N ALA A 1 -0.959 51.810 10.943 1.00 34.68 N ANISOU 1 N ALA A 1 2859 4956 5364 426 -328 -167 N ATOM 2 CA ALA A 1 0.408 51.308 10.636 1.00 28.05 C ANISOU 2 CA ALA A 1 2886 3831 3939 218 -329 -33 C ATOM 3 C ALA A 1 1.439 51.901 11.587 1.00 26.22 C ANISOU 3 C ALA A 1 2532 3291 4141 999 -705 92 C ATOM 4 O ALA A 1 1.295 53.028 12.054 1.00 30.04 O ANISOU 4 O ALA A 1 2971 3551 4890 1320 -1011 -306 O ATOM 5 CB ALA A 1 0.802 51.607 9.200 1.00 27.47 C ANISOU 5 CB ALA A 1 3039 3512 3886 281 -624 251 C ATOM 6 N GLU A 2 2.494 51.136 11.843 1.00 18.37 N ANISOU 6 N GLU A 2 1610 2260 3108 269 -21 249 N ATOM 7 CA GLU A 2 3.582 51.561 12.717 1.00 16.04 C ANISOU 7 CA GLU A 2 1630 1463 3000 275 42 330 C ATOM 8 C GLU A 2 4.854 51.749 11.890 1.00 14.70 C ANISOU 8 C GLU A 2 1694 1488 2403 328 -62 265 C ATOM 9 O GLU A 2 4.946 51.233 10.773 1.00 17.98 O ANISOU 9 O GLU A 2 2000 2055 2774 145 -47 -214 O ATOM 10 CB GLU A 2 3.811 50.568 13.851 1.00 17.85 C ANISOU 10 CB GLU A 2 2121 1821 2839 435 -6 385 C ATOM 11 CG GLU A 2 2.626 50.375 14.767 1.00 23.99 C ANISOU 11 CG GLU A 2 2804 3052 3257 400 530 668 C ATOM 12 CD GLU A 2 2.358 51.502 15.731 1.00 31.61 C ANISOU 12 CD GLU A 2 4147 3402 4460 193 -15 -269 C ATOM 13 OE1 GLU A 2 3.225 52.352 16.000 1.00 33.47 O ANISOU 13 OE1 GLU A 2 4190 3414 5112 37 42 28 O ATOM 14 OE2 GLU A 2 1.219 51.535 16.260 1.00 39.82 O ANISOU 14 OE2 GLU A 2 4350 4661 6117 80 558 11 O ATOM 15 N SER A 3 5.799 52.516 12.424 1.00 14.23 N ANISOU 15 N SER A 3 1538 1484 2385 410 15 180 N ATOM 16 CA SER A 3 6.991 52.881 11.683 1.00 14.39 C ANISOU 16 CA SER A 3 1588 1510 2369 348 -5 393 C ATOM 17 C SER A 3 8.268 52.175 12.090 1.00 12.89 C ANISOU 17 C SER A 3 1435 1295 2169 202 12 217 C ATOM 18 O SER A 3 9.301 52.464 11.475 1.00 15.20 O ANISOU 18 O SER A 3 1604 1744 2428 175 81 749 O ATOM 19 CB SER A 3 7.224 54.401 11.813 1.00 20.36 C ANISOU 19 CB SER A 3 2268 1642 3827 52 -161 451 C ATOM 20 OG SER A 3 7.471 54.695 13.174 1.00 27.51 O ANISOU 20 OG SER A 3 4087 2236 4128 -57 194 -612 O ATOM 21 N THR A 4 8.227 51.289 13.072 1.00 11.47 N ANISOU 21 N THR A 4 1220 1220 1919 197 -88 88 N ATOM 22 CA THR A 4 9.375 50.497 13.508 1.00 10.54 C ANISOU 22 CA THR A 4 1029 1196 1780 110 148 181 C ATOM 23 C THR A 4 8.988 49.015 13.548 1.00 9.70 C ANISOU 23 C THR A 4 1041 1208 1435 154 216 93 C ATOM 24 O THR A 4 7.804 48.691 13.699 1.00 11.14 O ANISOU 24 O THR A 4 1006 1404 1823 208 109 158 O ATOM 25 CB THR A 4 9.942 50.941 14.860 1.00 12.45 C ANISOU 25 CB THR A 4 1300 1577 1855 86 15 95 C ATOM 26 OG1 THR A 4 8.910 50.718 15.844 1.00 14.75 O ANISOU 26 OG1 THR A 4 1438 2386 1780 -50 128 -296 O ATOM 27 CG2 THR A 4 10.393 52.388 14.889 1.00 14.63 C ANISOU 27 CG2 THR A 4 1487 1694 2379 -71 105 -315 C ATOM 28 N LEU A 5 9.977 48.125 13.438 1.00 9.63 N ANISOU 28 N LEU A 5 1063 1053 1544 123 150 53 N ATOM 29 CA LEU A 5 9.708 46.693 13.374 1.00 8.82 C ANISOU 29 CA LEU A 5 866 1121 1364 70 48 -18 C ATOM 30 C LEU A 5 9.008 46.153 14.625 1.00 8.62 C ANISOU 30 C LEU A 5 802 1024 1450 20 52 -23 C ATOM 31 O LEU A 5 8.010 45.424 14.545 1.00 9.52 O ANISOU 31 O LEU A 5 960 1187 1469 -59 101 -46 O ATOM 32 CB LEU A 5 10.986 45.885 13.083 1.00 9.41 C ANISOU 32 CB LEU A 5 1144 1087 1345 220 202 25 C ATOM 33 CG LEU A 5 11.687 46.213 11.746 1.00 10.36 C ANISOU 33 CG LEU A 5 1252 1337 1348 160 227 -6 C ATOM 34 CD1 LEU A 5 13.052 45.523 11.713 1.00 13.29 C ANISOU 34 CD1 LEU A 5 1380 1826 1844 381 513 373 C ATOM 35 CD2 LEU A 5 10.845 45.796 10.555 1.00 15.19 C ANISOU 35 CD2 LEU A 5 1955 2317 1498 -298 93 -243 C ATOM 36 N GLY A 6 9.570 46.491 15.809 1.00 9.40 N ANISOU 36 N GLY A 6 862 1343 1367 -41 50 -7 N ATOM 37 CA GLY A 6 9.000 45.973 17.044 1.00 10.00 C ANISOU 37 CA GLY A 6 1004 1420 1376 7 35 89 C ATOM 38 C GLY A 6 7.563 46.419 17.273 1.00 9.77 C ANISOU 38 C GLY A 6 1103 1322 1287 26 147 29 C ATOM 39 O GLY A 6 6.699 45.620 17.662 1.00 10.65 O ANISOU 39 O GLY A 6 1104 1498 1446 -50 129 167 O ATOM 40 N ALA A 7 7.297 47.711 17.056 1.00 9.69 N ANISOU 40 N ALA A 7 1039 1237 1408 -1 240 -175 N ATOM 41 CA ALA A 7 5.947 48.259 17.234 1.00 11.41 C ANISOU 41 CA ALA A 7 1233 1431 1671 201 288 -252 C ATOM 42 C ALA A 7 4.969 47.638 16.243 1.00 10.00 C ANISOU 42 C ALA A 7 1052 1157 1591 207 337 35 C ATOM 43 O ALA A 7 3.817 47.367 16.603 1.00 11.76 O ANISOU 43 O ALA A 7 1111 1567 1791 61 407 -157 O ATOM 44 CB ALA A 7 5.973 49.782 17.158 1.00 13.64 C ANISOU 44 CB ALA A 7 1653 1439 2090 336 276 -341 C ATOM 45 N ALA A 8 5.403 47.428 14.999 1.00 9.61 N ANISOU 45 N ALA A 8 960 1199 1492 150 176 7 N ATOM 46 CA ALA A 8 4.539 46.801 13.991 1.00 9.92 C ANISOU 46 CA ALA A 8 857 1254 1658 133 119 -20 C ATOM 47 C ALA A 8 4.216 45.360 14.367 1.00 9.84 C ANISOU 47 C ALA A 8 933 1224 1583 82 -24 53 C ATOM 48 O ALA A 8 3.067 44.905 14.227 1.00 11.98 O ANISOU 48 O ALA A 8 1035 1510 2008 22 -115 38 O ATOM 49 CB ALA A 8 5.186 46.932 12.618 1.00 11.11 C ANISOU 49 CB ALA A 8 1227 1480 1515 144 30 -16 C ATOM 50 N ALA A 9 5.205 44.596 14.864 1.00 9.10 N ANISOU 50 N ALA A 9 973 1063 1420 52 45 83 N ATOM 51 CA ALA A 9 4.954 43.233 15.319 1.00 8.23 C ANISOU 51 CA ALA A 9 674 1070 1381 45 166 -95 C ATOM 52 C ALA A 9 4.005 43.183 16.517 1.00 8.63 C ANISOU 52 C ALA A 9 830 938 1511 163 254 59 C ATOM 53 O ALA A 9 3.141 42.292 16.618 1.00 9.94 O ANISOU 53 O ALA A 9 858 1135 1785 86 206 -44 O ATOM 54 CB ALA A 9 6.284 42.529 15.657 1.00 9.25 C ANISOU 54 CB ALA A 9 948 1247 1318 347 200 115 C ATOM 55 N ALA A 10 4.148 44.148 17.433 1.00 9.87 N ANISOU 55 N ALA A 10 965 1251 1533 97 324 -134 N ATOM 56 CA ALA A 10 3.324 44.198 18.646 1.00 10.84 C ANISOU 56 CA ALA A 10 1241 1325 1554 130 411 -60 C ATOM 57 C ALA A 10 1.852 44.386 18.328 1.00 11.54 C ANISOU 57 C ALA A 10 1176 1326 1884 152 557 -76 C ATOM 58 O ALA A 10 0.992 43.911 19.102 1.00 13.00 O ANISOU 58 O ALA A 10 1350 1478 2110 103 841 -137 O ATOM 59 CB ALA A 10 3.816 45.309 19.582 1.00 12.36 C ANISOU 59 CB ALA A 10 1522 1674 1500 -175 532 -185 C ATOM 60 N GLN A 11 1.488 44.974 17.189 1.00 11.59 N ANISOU 60 N GLN A 11 1007 1230 2166 248 486 15 N ATOM 61 CA GLN A 11 0.094 45.108 16.764 1.00 12.91 C ANISOU 61 CA GLN A 11 1128 1321 2456 411 224 -85 C ATOM 62 C GLN A 11 -0.571 43.758 16.514 1.00 12.31 C ANISOU 62 C GLN A 11 1023 1404 2251 267 343 34 C ATOM 63 O GLN A 11 -1.812 43.684 16.489 1.00 14.82 O ANISOU 63 O GLN A 11 1024 1711 2894 344 383 85 O ATOM 64 CB GLN A 11 -0.023 45.900 15.464 1.00 18.16 C ANISOU 64 CB GLN A 11 1251 2394 3255 528 205 821 C ATOM 65 CG GLN A 11 0.459 47.306 15.318 1.00 21.97 C ANISOU 65 CG GLN A 11 2159 2435 3753 140 56 55 C ATOM 66 CD GLN A 11 0.432 47.763 13.864 1.00 30.70 C ANISOU 66 CD GLN A 11 4102 3849 3714 641 12 191 C ATOM 67 OE1 GLN A 11 -0.170 48.812 13.591 1.00 36.49 O ANISOU 67 OE1 GLN A 11 4372 3837 5655 717 -220 257 O ATOM 68 NE2 GLN A 11 1.033 47.055 12.908 1.00 27.13 N ANISOU 68 NE2 GLN A 11 3340 3515 3454 343 -317 213 N ATOM 69 N SER A 12 0.187 42.693 16.258 1.00 11.93 N ANISOU 69 N SER A 12 1003 1430 2099 328 159 -59 N ATOM 70 CA SER A 12 -0.320 41.334 16.111 1.00 11.84 C ANISOU 70 CA SER A 12 985 1450 2064 295 203 -89 C ATOM 71 C SER A 12 -0.005 40.477 17.340 1.00 11.09 C ANISOU 71 C SER A 12 838 1385 1990 38 72 -167 C ATOM 72 O SER A 12 -0.082 39.235 17.290 1.00 13.04 O ANISOU 72 O SER A 12 1361 1419 2173 26 -66 -72 O ATOM 73 CB SER A 12 0.165 40.642 14.839 1.00 14.28 C ANISOU 73 CB SER A 12 1600 2045 1782 538 99 28 C ATOM 74 OG ASER A 12 -0.099 41.389 13.666 0.50 13.65 O ANISOU 74 OG ASER A 12 1764 1814 1608 150 102 -41 O ATOM 75 OG BSER A 12 1.495 40.218 14.927 0.50 14.87 O ANISOU 75 OG BSER A 12 1464 2081 2104 421 485 -119 O ATOM 76 N GLY A 13 0.335 41.114 18.455 1.00 10.95 N ANISOU 76 N GLY A 13 837 1383 1940 261 109 -142 N ATOM 77 CA GLY A 13 0.667 40.370 19.667 1.00 10.89 C ANISOU 77 CA GLY A 13 1022 1427 1689 49 329 -153 C ATOM 78 C GLY A 13 1.983 39.610 19.625 1.00 11.59 C ANISOU 78 C GLY A 13 1023 1744 1639 124 211 204 C ATOM 79 O GLY A 13 2.208 38.704 20.444 1.00 15.30 O ANISOU 79 O GLY A 13 1484 1970 2357 409 597 618 O ATOM 80 N ARG A 14 2.884 39.983 18.713 1.00 9.69 N ANISOU 80 N ARG A 14 752 1200 1729 73 131 106 N ATOM 81 CA ARG A 14 4.161 39.334 18.492 1.00 9.09 C ANISOU 81 CA ARG A 14 786 1047 1620 78 120 -17 C ATOM 82 C ARG A 14 5.331 40.282 18.734 1.00 8.38 C ANISOU 82 C ARG A 14 845 985 1355 71 247 -46 C ATOM 83 O ARG A 14 5.147 41.453 19.045 1.00 11.79 O ANISOU 83 O ARG A 14 904 1120 2455 175 225 -301 O ATOM 84 CB ARG A 14 4.172 38.743 17.079 1.00 9.65 C ANISOU 84 CB ARG A 14 858 1164 1643 197 -41 -35 C ATOM 85 CG ARG A 14 3.144 37.621 16.915 1.00 11.19 C ANISOU 85 CG ARG A 14 1341 1089 1820 48 -64 -145 C ATOM 86 CD ARG A 14 2.938 37.171 15.509 1.00 13.67 C ANISOU 86 CD ARG A 14 1927 1359 1905 -170 -219 -212 C ATOM 87 NE ARG A 14 2.120 36.003 15.286 1.00 13.05 N ANISOU 87 NE ARG A 14 1364 1230 2363 63 -241 -323 N ATOM 88 CZ ARG A 14 0.789 35.909 15.259 1.00 12.51 C ANISOU 88 CZ ARG A 14 1337 1293 2122 281 -484 -154 C ATOM 89 NH1 ARG A 14 -0.043 36.931 15.485 1.00 12.90 N ANISOU 89 NH1 ARG A 14 1462 1352 2086 282 -378 -278 N ATOM 90 NH2 ARG A 14 0.237 34.746 14.975 1.00 13.19 N ANISOU 90 NH2 ARG A 14 1335 1327 2349 276 -610 -190 N ATOM 91 N TYR A 15 6.553 39.756 18.650 1.00 7.92 N ANISOU 91 N TYR A 15 717 986 1305 33 88 -103 N ATOM 92 CA TYR A 15 7.754 40.565 18.838 1.00 7.57 C ANISOU 92 CA TYR A 15 616 1047 1214 64 35 -104 C ATOM 93 C TYR A 15 8.648 40.517 17.588 1.00 6.61 C ANISOU 93 C TYR A 15 602 851 1060 69 -79 -16 C ATOM 94 O TYR A 15 8.527 39.596 16.764 1.00 7.68 O ANISOU 94 O TYR A 15 887 908 1124 -36 43 -53 O ATOM 95 CB TYR A 15 8.534 40.127 20.091 1.00 8.12 C ANISOU 95 CB TYR A 15 959 976 1149 -23 -4 -91 C ATOM 96 CG TYR A 15 9.087 38.712 20.078 1.00 7.03 C ANISOU 96 CG TYR A 15 753 944 973 -27 -2 -4 C ATOM 97 CD1 TYR A 15 10.237 38.404 19.363 1.00 7.40 C ANISOU 97 CD1 TYR A 15 838 1064 910 -53 22 137 C ATOM 98 CD2 TYR A 15 8.441 37.676 20.745 1.00 8.19 C ANISOU 98 CD2 TYR A 15 909 1159 1042 -61 91 26 C ATOM 99 CE1 TYR A 15 10.752 37.111 19.336 1.00 8.12 C ANISOU 99 CE1 TYR A 15 905 1128 1054 12 -14 167 C ATOM 100 CE2 TYR A 15 8.939 36.387 20.721 1.00 8.36 C ANISOU 100 CE2 TYR A 15 1105 1035 1036 -122 115 99 C ATOM 101 CZ TYR A 15 10.097 36.100 20.020 1.00 7.82 C ANISOU 101 CZ TYR A 15 1106 941 923 -40 -2 40 C ATOM 102 OH TYR A 15 10.574 34.811 20.030 1.00 9.13 O ANISOU 102 OH TYR A 15 1208 1018 1243 -20 117 79 O ATOM 103 N PHE A 16 9.565 41.479 17.509 1.00 6.84 N ANISOU 103 N PHE A 16 608 831 1160 17 122 -97 N ATOM 104 CA PHE A 16 10.614 41.481 16.498 1.00 6.43 C ANISOU 104 CA PHE A 16 582 859 1001 110 98 -85 C ATOM 105 C PHE A 16 11.926 41.797 17.236 1.00 6.58 C ANISOU 105 C PHE A 16 687 741 1072 23 77 -115 C ATOM 106 O PHE A 16 12.075 42.898 17.790 1.00 9.42 O ANISOU 106 O PHE A 16 934 892 1755 50 121 -270 O ATOM 107 CB PHE A 16 10.342 42.462 15.336 1.00 8.61 C ANISOU 107 CB PHE A 16 930 1064 1279 262 16 96 C ATOM 108 CG PHE A 16 10.953 41.973 14.033 1.00 8.06 C ANISOU 108 CG PHE A 16 1030 883 1148 86 7 178 C ATOM 109 CD1 PHE A 16 12.300 42.138 13.776 1.00 10.69 C ANISOU 109 CD1 PHE A 16 1003 1631 1429 56 69 10 C ATOM 110 CD2 PHE A 16 10.187 41.314 13.094 1.00 10.56 C ANISOU 110 CD2 PHE A 16 1308 1493 1213 -203 -106 226 C ATOM 111 CE1 PHE A 16 12.859 41.654 12.608 1.00 12.49 C ANISOU 111 CE1 PHE A 16 1335 1983 1427 42 204 10 C ATOM 112 CE2 PHE A 16 10.743 40.839 11.919 1.00 12.12 C ANISOU 112 CE2 PHE A 16 1630 1884 1091 -57 -239 179 C ATOM 113 CZ PHE A 16 12.086 41.007 11.669 1.00 11.96 C ANISOU 113 CZ PHE A 16 1684 1489 1371 124 112 96 C ATOM 114 N GLY A 17 12.851 40.835 17.249 1.00 6.94 N ANISOU 114 N GLY A 17 740 858 1039 98 -93 -117 N ATOM 115 CA GLY A 17 14.060 40.947 18.054 1.00 7.26 C ANISOU 115 CA GLY A 17 813 1031 915 85 -64 -71 C ATOM 116 C GLY A 17 15.348 40.910 17.231 1.00 5.97 C ANISOU 116 C GLY A 17 753 692 823 29 -46 51 C ATOM 117 O GLY A 17 15.370 40.698 16.039 1.00 6.88 O ANISOU 117 O GLY A 17 847 852 915 32 -11 2 O ATOM 118 N THR A 18 16.453 41.091 17.991 1.00 6.17 N ANISOU 118 N THR A 18 650 911 783 62 74 -1 N ATOM 119 CA THR A 18 17.796 40.987 17.423 1.00 5.99 C ANISOU 119 CA THR A 18 645 798 831 -35 49 -24 C ATOM 120 C THR A 18 18.756 40.330 18.413 1.00 6.04 C ANISOU 120 C THR A 18 790 701 805 -41 53 -99 C ATOM 121 O THR A 18 18.446 40.163 19.590 1.00 9.26 O ANISOU 121 O THR A 18 994 1576 949 320 139 288 O ATOM 122 CB THR A 18 18.346 42.357 16.970 1.00 7.38 C ANISOU 122 CB THR A 18 880 966 958 -133 49 149 C ATOM 123 OG1 THR A 18 19.514 42.189 16.157 1.00 9.01 O ANISOU 123 OG1 THR A 18 1035 1057 1331 -108 253 272 O ATOM 124 CG2 THR A 18 18.680 43.297 18.134 1.00 9.02 C ANISOU 124 CG2 THR A 18 1156 943 1329 -133 -139 20 C ATOM 125 N ALA A 19 19.936 39.963 17.929 1.00 7.58 N ANISOU 125 N ALA A 19 755 1263 862 169 18 53 N ATOM 126 CA ALA A 19 21.072 39.547 18.742 1.00 6.68 C ANISOU 126 CA ALA A 19 770 890 878 -10 -123 54 C ATOM 127 C ALA A 19 21.899 40.798 19.091 1.00 7.01 C ANISOU 127 C ALA A 19 814 878 971 -56 24 29 C ATOM 128 O ALA A 19 22.159 41.625 18.201 1.00 9.86 O ANISOU 128 O ALA A 19 1450 1154 1142 -354 1 159 O ATOM 129 CB ALA A 19 21.959 38.566 17.989 1.00 9.30 C ANISOU 129 CB ALA A 19 1140 945 1450 151 -82 -139 C ATOM 130 N ILE A 20 22.320 40.943 20.341 1.00 7.00 N ANISOU 130 N ILE A 20 824 826 1011 -112 -93 68 N ATOM 131 CA ILE A 20 23.154 42.037 20.817 1.00 7.14 C ANISOU 131 CA ILE A 20 959 767 987 -119 -181 71 C ATOM 132 C ILE A 20 24.484 41.466 21.327 1.00 7.35 C ANISOU 132 C ILE A 20 997 809 988 -65 -67 140 C ATOM 133 O ILE A 20 24.493 40.473 22.061 1.00 8.82 O ANISOU 133 O ILE A 20 1005 956 1392 -152 -197 299 O ATOM 134 CB ILE A 20 22.452 42.834 21.955 1.00 8.09 C ANISOU 134 CB ILE A 20 1051 910 1114 -99 -21 51 C ATOM 135 CG1 ILE A 20 21.201 43.551 21.444 1.00 10.40 C ANISOU 135 CG1 ILE A 20 1240 936 1775 68 -138 -17 C ATOM 136 CG2 ILE A 20 23.402 43.796 22.670 1.00 10.60 C ANISOU 136 CG2 ILE A 20 1349 1333 1346 -256 -102 -155 C ATOM 137 CD1 ILE A 20 21.425 44.673 20.458 1.00 11.79 C ANISOU 137 CD1 ILE A 20 1438 1084 1956 183 -94 127 C ATOM 138 N ALA A 21 25.584 42.132 20.962 1.00 8.02 N ANISOU 138 N ALA A 21 930 825 1292 -46 -137 299 N ATOM 139 CA ALA A 21 26.920 41.784 21.432 1.00 8.87 C ANISOU 139 CA ALA A 21 945 1136 1291 -164 -221 132 C ATOM 140 C ALA A 21 27.481 42.913 22.308 1.00 8.95 C ANISOU 140 C ALA A 21 965 939 1497 -248 -202 190 C ATOM 141 O ALA A 21 27.468 44.086 21.901 1.00 10.35 O ANISOU 141 O ALA A 21 1218 962 1751 -189 -286 242 O ATOM 142 CB ALA A 21 27.874 41.525 20.279 1.00 12.12 C ANISOU 142 CB ALA A 21 1070 1655 1879 -108 61 -255 C ATOM 143 N SER A 22 28.004 42.552 23.486 1.00 9.78 N ANISOU 143 N SER A 22 1162 1185 1370 -173 -141 137 N ATOM 144 CA SER A 22 28.504 43.553 24.432 1.00 10.81 C ANISOU 144 CA SER A 22 1320 1278 1507 -217 -42 -2 C ATOM 145 C SER A 22 29.635 44.404 23.885 1.00 9.93 C ANISOU 145 C SER A 22 1296 1199 1279 -271 -245 67 C ATOM 146 O SER A 22 29.703 45.611 24.227 1.00 12.98 O ANISOU 146 O SER A 22 1823 1294 1816 -424 -22 -111 O ATOM 147 CB SER A 22 28.900 42.872 25.752 1.00 13.27 C ANISOU 147 CB SER A 22 1735 1900 1407 -470 -156 77 C ATOM 148 OG SER A 22 29.922 41.922 25.593 1.00 15.62 O ANISOU 148 OG SER A 22 1917 1943 2076 -270 -604 550 O ATOM 149 N GLY A 23 30.499 43.869 23.044 1.00 10.21 N ANISOU 149 N GLY A 23 1159 1175 1545 -183 -301 34 N ATOM 150 CA GLY A 23 31.609 44.619 22.474 1.00 11.90 C ANISOU 150 CA GLY A 23 1316 1368 1838 -239 -211 231 C ATOM 151 C GLY A 23 31.200 45.709 21.498 1.00 10.30 C ANISOU 151 C GLY A 23 1252 1064 1597 -284 -141 -12 C ATOM 152 O GLY A 23 32.055 46.527 21.120 1.00 12.52 O ANISOU 152 O GLY A 23 1409 1444 1905 -425 -32 81 O ATOM 153 N ARG A 24 29.941 45.729 21.053 1.00 9.65 N ANISOU 153 N ARG A 24 1137 998 1532 -93 -86 115 N ATOM 154 CA ARG A 24 29.422 46.707 20.111 1.00 9.92 C ANISOU 154 CA ARG A 24 1201 1135 1435 -12 40 147 C ATOM 155 C ARG A 24 28.647 47.836 20.785 1.00 10.92 C ANISOU 155 C ARG A 24 1532 1012 1604 39 -87 128 C ATOM 156 O ARG A 24 28.232 48.801 20.115 1.00 11.95 O ANISOU 156 O ARG A 24 1858 924 1757 31 -394 31 O ATOM 157 CB ARG A 24 28.532 46.012 19.062 1.00 9.72 C ANISOU 157 CB ARG A 24 1334 1133 1228 21 145 65 C ATOM 158 CG ARG A 24 29.241 44.912 18.276 1.00 10.47 C ANISOU 158 CG ARG A 24 1212 1474 1290 79 194 -63 C ATOM 159 CD ARG A 24 28.311 44.203 17.280 1.00 10.22 C ANISOU 159 CD ARG A 24 1303 1407 1172 65 241 -113 C ATOM 160 NE ARG A 24 28.974 42.989 16.785 1.00 10.47 N ANISOU 160 NE ARG A 24 1417 1230 1331 -61 269 -37 N ATOM 161 CZ ARG A 24 29.845 42.924 15.800 1.00 9.11 C ANISOU 161 CZ ARG A 24 1057 1222 1182 74 26 -33 C ATOM 162 NH1 ARG A 24 30.104 43.980 15.037 1.00 10.37 N ANISOU 162 NH1 ARG A 24 1221 1359 1358 18 123 64 N ATOM 163 NH2 ARG A 24 30.493 41.781 15.581 1.00 11.49 N ANISOU 163 NH2 ARG A 24 1593 1305 1468 246 189 -25 N ATOM 164 N LEU A 25 28.470 47.792 22.108 1.00 11.29 N ANISOU 164 N LEU A 25 1467 1178 1647 148 100 -92 N ATOM 165 CA LEU A 25 27.671 48.774 22.831 1.00 12.75 C ANISOU 165 CA LEU A 25 1540 1394 1911 318 126 -178 C ATOM 166 C LEU A 25 28.289 50.156 22.954 1.00 14.48 C ANISOU 166 C LEU A 25 1731 1536 2234 205 -66 -512 C ATOM 167 O LEU A 25 27.558 51.091 23.329 1.00 18.76 O ANISOU 167 O LEU A 25 1857 1732 3538 217 72 -855 O ATOM 168 CB LEU A 25 27.233 48.238 24.202 1.00 14.13 C ANISOU 168 CB LEU A 25 1803 1874 1690 183 9 -325 C ATOM 169 CG LEU A 25 26.273 47.045 24.182 1.00 16.31 C ANISOU 169 CG LEU A 25 2593 1614 1991 60 200 -208 C ATOM 170 CD1 LEU A 25 25.977 46.571 25.598 1.00 19.48 C ANISOU 170 CD1 LEU A 25 2799 2320 2283 57 537 102 C ATOM 171 CD2 LEU A 25 24.964 47.407 23.481 1.00 16.70 C ANISOU 171 CD2 LEU A 25 2010 1860 2476 -328 360 -425 C ATOM 172 N SER A 26 29.540 50.362 22.581 1.00 12.09 N ANISOU 172 N SER A 26 1666 1225 1705 231 -297 -214 N ATOM 173 CA SER A 26 30.119 51.701 22.537 1.00 14.32 C ANISOU 173 CA SER A 26 1849 1547 2044 -127 -531 -385 C ATOM 174 C SER A 26 29.866 52.391 21.193 1.00 13.71 C ANISOU 174 C SER A 26 1679 1422 2109 -302 -302 -231 C ATOM 175 O SER A 26 30.213 53.573 21.049 1.00 17.58 O ANISOU 175 O SER A 26 2830 1588 2263 -734 -574 -210 O ATOM 176 CB SER A 26 31.609 51.708 22.859 1.00 21.08 C ANISOU 176 CB SER A 26 1710 2499 3800 -180 -260 -186 C ATOM 177 OG SER A 26 32.299 51.026 21.842 1.00 27.58 O ANISOU 177 OG SER A 26 2355 4404 3721 505 -104 -305 O ATOM 178 N ASP A 27 29.275 51.705 20.209 1.00 10.82 N ANISOU 178 N ASP A 27 1257 856 1999 7 -296 -126 N ATOM 179 CA ASP A 27 28.975 52.266 18.894 1.00 10.15 C ANISOU 179 CA ASP A 27 1061 906 1892 45 -169 -243 C ATOM 180 C ASP A 27 27.577 52.909 18.939 1.00 8.62 C ANISOU 180 C ASP A 27 1103 731 1442 13 53 -54 C ATOM 181 O ASP A 27 26.570 52.191 19.071 1.00 10.02 O ANISOU 181 O ASP A 27 1063 967 1776 -57 -10 -24 O ATOM 182 CB ASP A 27 29.095 51.172 17.830 1.00 10.92 C ANISOU 182 CB ASP A 27 1126 1049 1974 122 -79 -319 C ATOM 183 CG ASP A 27 28.764 51.546 16.410 1.00 11.65 C ANISOU 183 CG ASP A 27 1300 1207 1918 61 119 -207 C ATOM 184 OD1 ASP A 27 27.958 52.469 16.164 1.00 12.89 O ANISOU 184 OD1 ASP A 27 1624 1203 2070 210 209 -16 O ATOM 185 OD2 ASP A 27 29.287 50.851 15.493 1.00 14.87 O ANISOU 185 OD2 ASP A 27 1472 2067 2113 336 -158 -712 O ATOM 186 N SER A 28 27.515 54.237 18.852 1.00 9.53 N ANISOU 186 N SER A 28 1050 742 1829 13 157 -155 N ATOM 187 CA SER A 28 26.257 54.966 18.986 1.00 9.25 C ANISOU 187 CA SER A 28 997 894 1624 11 72 -126 C ATOM 188 C SER A 28 25.259 54.751 17.860 1.00 8.76 C ANISOU 188 C SER A 28 1062 761 1506 64 100 -37 C ATOM 189 O SER A 28 24.037 54.879 18.101 1.00 10.62 O ANISOU 189 O SER A 28 1103 1252 1682 98 66 -108 O ATOM 190 CB SER A 28 26.550 56.446 19.233 1.00 10.91 C ANISOU 190 CB SER A 28 1580 878 1688 72 -91 -378 C ATOM 191 OG SER A 28 27.219 56.654 20.470 1.00 13.37 O ANISOU 191 OG SER A 28 1674 1464 1942 54 -263 -503 O ATOM 192 N THR A 29 25.728 54.416 16.660 1.00 9.01 N ANISOU 192 N THR A 29 1074 814 1537 -19 116 32 N ATOM 193 CA THR A 29 24.826 54.066 15.566 1.00 9.08 C ANISOU 193 CA THR A 29 1215 884 1353 -2 158 109 C ATOM 194 C THR A 29 24.125 52.743 15.888 1.00 8.63 C ANISOU 194 C THR A 29 1121 815 1343 28 87 43 C ATOM 195 O THR A 29 22.887 52.614 15.751 1.00 10.21 O ANISOU 195 O THR A 29 1131 1099 1649 14 -24 193 O ATOM 196 CB THR A 29 25.560 54.003 14.211 1.00 10.20 C ANISOU 196 CB THR A 29 1439 1042 1395 117 218 141 C ATOM 197 OG1 THR A 29 26.170 55.281 13.968 1.00 15.77 O ANISOU 197 OG1 THR A 29 2622 1230 2141 -209 964 202 O ATOM 198 CG2 THR A 29 24.613 53.672 13.071 1.00 13.68 C ANISOU 198 CG2 THR A 29 2031 1824 1343 -83 126 -19 C ATOM 199 N TYR A 30 24.922 51.757 16.306 1.00 8.88 N ANISOU 199 N TYR A 30 969 745 1661 -20 144 116 N ATOM 200 CA TYR A 30 24.390 50.450 16.690 1.00 8.05 C ANISOU 200 CA TYR A 30 1035 677 1348 32 35 40 C ATOM 201 C TYR A 30 23.362 50.540 17.823 1.00 8.01 C ANISOU 201 C TYR A 30 877 706 1460 3 15 105 C ATOM 202 O TYR A 30 22.260 49.972 17.701 1.00 9.53 O ANISOU 202 O TYR A 30 1005 933 1684 -111 -129 52 O ATOM 203 CB TYR A 30 25.560 49.564 17.110 1.00 8.85 C ANISOU 203 CB TYR A 30 1108 764 1489 -7 17 25 C ATOM 204 CG TYR A 30 25.280 48.143 17.534 1.00 8.03 C ANISOU 204 CG TYR A 30 1011 732 1308 19 -123 13 C ATOM 205 CD1 TYR A 30 25.183 47.123 16.593 1.00 8.02 C ANISOU 205 CD1 TYR A 30 1080 762 1205 -117 16 20 C ATOM 206 CD2 TYR A 30 25.175 47.777 18.867 1.00 8.83 C ANISOU 206 CD2 TYR A 30 1314 781 1260 -8 -112 -107 C ATOM 207 CE1 TYR A 30 24.987 45.799 16.974 1.00 7.69 C ANISOU 207 CE1 TYR A 30 1093 752 1077 -80 63 -99 C ATOM 208 CE2 TYR A 30 24.967 46.472 19.269 1.00 8.95 C ANISOU 208 CE2 TYR A 30 1385 855 1162 -46 55 -55 C ATOM 209 CZ TYR A 30 24.901 45.478 18.311 1.00 7.45 C ANISOU 209 CZ TYR A 30 1033 725 1072 -62 48 30 C ATOM 210 OH TYR A 30 24.776 44.161 18.712 1.00 9.14 O ANISOU 210 OH TYR A 30 1363 809 1303 -122 87 35 O ATOM 211 N THR A 31 23.730 51.225 18.928 1.00 8.54 N ANISOU 211 N THR A 31 939 846 1461 19 -73 85 N ATOM 212 CA THR A 31 22.810 51.261 20.066 1.00 8.99 C ANISOU 212 CA THR A 31 1004 811 1601 -74 1 128 C ATOM 213 C THR A 31 21.532 52.051 19.798 1.00 8.14 C ANISOU 213 C THR A 31 1015 877 1200 -20 79 70 C ATOM 214 O THR A 31 20.464 51.684 20.344 1.00 9.43 O ANISOU 214 O THR A 31 1049 1168 1367 -63 164 63 O ATOM 215 CB THR A 31 23.498 51.808 21.334 1.00 11.59 C ANISOU 215 CB THR A 31 1374 1327 1701 -69 -394 158 C ATOM 216 OG1 THR A 31 23.919 53.160 21.088 1.00 13.14 O ANISOU 216 OG1 THR A 31 1745 1506 1743 -270 -47 -36 O ATOM 217 CG2 THR A 31 24.667 50.936 21.724 1.00 14.39 C ANISOU 217 CG2 THR A 31 1583 1612 2274 79 -488 323 C ATOM 218 N SER A 32 21.611 53.124 19.015 1.00 8.53 N ANISOU 218 N SER A 32 1130 830 1281 82 176 85 N ATOM 219 CA SER A 32 20.410 53.929 18.767 1.00 8.95 C ANISOU 219 CA SER A 32 1053 783 1563 42 79 35 C ATOM 220 C SER A 32 19.465 53.234 17.792 1.00 8.91 C ANISOU 220 C SER A 32 1016 1008 1361 158 14 76 C ATOM 221 O SER A 32 18.241 53.260 17.996 1.00 10.73 O ANISOU 221 O SER A 32 1077 1191 1809 84 103 85 O ATOM 222 CB SER A 32 20.762 55.363 18.409 1.00 10.34 C ANISOU 222 CB SER A 32 1333 897 1697 19 129 44 C ATOM 223 OG SER A 32 21.492 55.469 17.222 1.00 10.99 O ANISOU 223 OG SER A 32 1527 1056 1595 186 130 382 O ATOM 224 N ILE A 33 19.969 52.568 16.748 1.00 8.73 N ANISOU 224 N ILE A 33 986 1130 1200 -31 40 160 N ATOM 225 CA ILE A 33 19.122 51.814 15.825 1.00 9.08 C ANISOU 225 CA ILE A 33 1081 1245 1124 9 -52 201 C ATOM 226 C ILE A 33 18.512 50.588 16.511 1.00 8.59 C ANISOU 226 C ILE A 33 949 1182 1131 6 87 30 C ATOM 227 O ILE A 33 17.302 50.323 16.408 1.00 10.11 O ANISOU 227 O ILE A 33 987 1485 1369 -79 32 72 O ATOM 228 CB ILE A 33 19.871 51.416 14.543 1.00 11.20 C ANISOU 228 CB ILE A 33 1273 1885 1098 -14 -73 178 C ATOM 229 CG1 ILE A 33 20.268 52.666 13.743 1.00 15.14 C ANISOU 229 CG1 ILE A 33 1856 2484 1413 -509 -6 471 C ATOM 230 CG2 ILE A 33 19.068 50.444 13.693 1.00 14.10 C ANISOU 230 CG2 ILE A 33 1865 2092 1403 -175 -21 -140 C ATOM 231 CD1 ILE A 33 21.154 52.388 12.557 1.00 21.04 C ANISOU 231 CD1 ILE A 33 2457 3665 1873 -452 423 159 C ATOM 232 N ALA A 34 19.322 49.819 17.247 1.00 8.46 N ANISOU 232 N ALA A 34 1021 967 1227 -53 101 89 N ATOM 233 CA ALA A 34 18.815 48.653 17.968 1.00 8.62 C ANISOU 233 CA ALA A 34 1078 834 1361 -114 132 -5 C ATOM 234 C ALA A 34 17.770 49.079 18.997 1.00 8.76 C ANISOU 234 C ALA A 34 1100 908 1320 -124 111 -2 C ATOM 235 O ALA A 34 16.764 48.389 19.211 1.00 10.38 O ANISOU 235 O ALA A 34 1294 1049 1603 -220 181 122 O ATOM 236 CB ALA A 34 19.946 47.866 18.609 1.00 11.06 C ANISOU 236 CB ALA A 34 1368 1038 1798 129 244 308 C ATOM 237 N GLY A 35 18.017 50.183 19.712 1.00 8.44 N ANISOU 237 N GLY A 35 1161 916 1129 54 -10 54 N ATOM 238 CA GLY A 35 17.085 50.698 20.688 1.00 9.40 C ANISOU 238 CA GLY A 35 1219 1208 1146 -94 125 53 C ATOM 239 C GLY A 35 15.735 51.055 20.075 1.00 9.06 C ANISOU 239 C GLY A 35 1207 997 1237 -50 132 7 C ATOM 240 O GLY A 35 14.681 50.746 20.633 1.00 11.39 O ANISOU 240 O GLY A 35 1314 1388 1627 53 369 270 O ATOM 241 N ARG A 36 15.739 51.696 18.919 1.00 9.78 N ANISOU 241 N ARG A 36 1223 1122 1369 -34 -2 146 N ATOM 242 CA ARG A 36 14.527 52.124 18.242 1.00 10.18 C ANISOU 242 CA ARG A 36 1224 1119 1525 4 -70 60 C ATOM 243 C ARG A 36 13.694 50.988 17.653 1.00 9.55 C ANISOU 243 C ARG A 36 991 1219 1421 40 130 -43 C ATOM 244 O ARG A 36 12.463 51.008 17.698 1.00 11.86 O ANISOU 244 O ARG A 36 1036 1531 1939 101 115 -217 O ATOM 245 CB ARG A 36 14.916 53.096 17.095 1.00 11.90 C ANISOU 245 CB ARG A 36 1495 1033 1992 -89 -141 359 C ATOM 246 CG ARG A 36 13.807 53.665 16.234 1.00 14.59 C ANISOU 246 CG ARG A 36 1760 1752 2031 164 -244 458 C ATOM 247 CD ARG A 36 14.392 54.550 15.102 1.00 15.84 C ANISOU 247 CD ARG A 36 2323 1852 1844 105 -279 439 C ATOM 248 NE ARG A 36 14.898 53.756 13.992 1.00 16.58 N ANISOU 248 NE ARG A 36 2267 2271 1763 -260 -26 359 N ATOM 249 CZ ARG A 36 15.853 54.023 13.120 1.00 16.20 C ANISOU 249 CZ ARG A 36 2083 1980 2092 -116 89 100 C ATOM 250 NH1 ARG A 36 16.580 55.134 13.202 1.00 17.74 N ANISOU 250 NH1 ARG A 36 2328 2184 2227 -385 274 225 N ATOM 251 NH2 ARG A 36 16.139 53.155 12.151 1.00 16.45 N ANISOU 251 NH2 ARG A 36 1899 2193 2159 -553 179 -129 N ATOM 252 N GLU A 37 14.352 50.015 17.026 1.00 8.69 N ANISOU 252 N GLU A 37 1001 1063 1239 5 50 28 N ATOM 253 CA GLU A 37 13.672 49.072 16.151 1.00 8.15 C ANISOU 253 CA GLU A 37 1027 1031 1040 128 -58 125 C ATOM 254 C GLU A 37 13.184 47.770 16.765 1.00 8.15 C ANISOU 254 C GLU A 37 787 1088 1222 83 -35 57 C ATOM 255 O GLU A 37 12.286 47.157 16.178 1.00 11.56 O ANISOU 255 O GLU A 37 1307 1344 1741 -211 -415 226 O ATOM 256 CB GLU A 37 14.595 48.731 14.955 1.00 10.13 C ANISOU 256 CB GLU A 37 1194 1465 1191 164 12 100 C ATOM 257 CG GLU A 37 14.863 49.912 14.040 1.00 11.14 C ANISOU 257 CG GLU A 37 1227 1725 1282 15 71 220 C ATOM 258 CD GLU A 37 13.715 50.331 13.151 1.00 10.95 C ANISOU 258 CD GLU A 37 1202 1717 1244 1 35 117 C ATOM 259 OE1 GLU A 37 12.712 49.608 12.932 1.00 11.86 O ANISOU 259 OE1 GLU A 37 1296 1729 1483 -70 48 141 O ATOM 260 OE2 GLU A 37 13.835 51.463 12.624 1.00 14.99 O ANISOU 260 OE2 GLU A 37 1730 1983 1981 -461 -68 518 O ATOM 261 N PHE A 38 13.800 47.294 17.845 1.00 7.86 N ANISOU 261 N PHE A 38 969 900 1119 21 9 73 N ATOM 262 CA PHE A 38 13.522 45.935 18.329 1.00 7.70 C ANISOU 262 CA PHE A 38 1002 760 1162 17 15 -37 C ATOM 263 C PHE A 38 12.907 45.935 19.722 1.00 8.36 C ANISOU 263 C PHE A 38 1200 897 1079 -72 46 -10 C ATOM 264 O PHE A 38 13.237 46.804 20.540 1.00 11.55 O ANISOU 264 O PHE A 38 1764 1407 1217 -497 143 -215 O ATOM 265 CB PHE A 38 14.839 45.114 18.309 1.00 8.15 C ANISOU 265 CB PHE A 38 1013 793 1289 58 40 59 C ATOM 266 CG PHE A 38 15.486 45.024 16.943 1.00 7.62 C ANISOU 266 CG PHE A 38 886 786 1224 99 -1 102 C ATOM 267 CD1 PHE A 38 14.939 44.219 15.963 1.00 8.82 C ANISOU 267 CD1 PHE A 38 962 1089 1301 4 127 -79 C ATOM 268 CD2 PHE A 38 16.608 45.774 16.638 1.00 9.63 C ANISOU 268 CD2 PHE A 38 1004 1054 1600 9 167 37 C ATOM 269 CE1 PHE A 38 15.543 44.133 14.717 1.00 10.31 C ANISOU 269 CE1 PHE A 38 1196 1336 1386 174 261 48 C ATOM 270 CE2 PHE A 38 17.203 45.697 15.396 1.00 10.54 C ANISOU 270 CE2 PHE A 38 1106 1195 1704 7 308 143 C ATOM 271 CZ PHE A 38 16.671 44.872 14.412 1.00 10.48 C ANISOU 271 CZ PHE A 38 1282 1264 1436 212 343 118 C ATOM 272 N ASN A 39 12.060 44.954 20.041 1.00 7.64 N ANISOU 272 N ASN A 39 953 856 1095 52 108 2 N ATOM 273 CA ASN A 39 11.446 44.824 21.365 1.00 7.94 C ANISOU 273 CA ASN A 39 952 927 1136 17 185 -99 C ATOM 274 C ASN A 39 11.839 43.523 22.083 1.00 7.70 C ANISOU 274 C ASN A 39 815 1003 1107 86 120 -83 C ATOM 275 O ASN A 39 11.278 43.222 23.153 1.00 9.96 O ANISOU 275 O ASN A 39 1182 1247 1356 162 367 96 O ATOM 276 CB ASN A 39 9.931 45.094 21.396 1.00 8.74 C ANISOU 276 CB ASN A 39 1076 987 1257 225 109 -54 C ATOM 277 CG ASN A 39 9.131 44.199 20.493 1.00 9.35 C ANISOU 277 CG ASN A 39 983 1415 1153 133 166 -118 C ATOM 278 OD1 ASN A 39 9.642 43.318 19.809 1.00 11.00 O ANISOU 278 OD1 ASN A 39 1084 1372 1725 38 165 -402 O ATOM 279 ND2 ASN A 39 7.828 44.431 20.428 1.00 18.00 N ANISOU 279 ND2 ASN A 39 1153 3133 2552 599 -93 -1187 N ATOM 280 N MET A 40 12.797 42.788 21.561 1.00 7.84 N ANISOU 280 N MET A 40 1011 986 981 173 131 17 N ATOM 281 CA MET A 40 13.289 41.526 22.138 1.00 7.28 C ANISOU 281 CA MET A 40 812 1063 891 88 79 -8 C ATOM 282 C MET A 40 14.781 41.429 21.848 1.00 6.97 C ANISOU 282 C MET A 40 779 1096 772 56 76 -46 C ATOM 283 O MET A 40 15.246 41.827 20.763 1.00 8.24 O ANISOU 283 O MET A 40 941 1352 840 61 9 76 O ATOM 284 CB MET A 40 12.529 40.325 21.532 1.00 8.04 C ANISOU 284 CB MET A 40 992 1139 924 -94 137 -20 C ATOM 285 CG MET A 40 12.924 38.958 22.076 1.00 10.63 C ANISOU 285 CG MET A 40 1222 1056 1760 -231 122 -1 C ATOM 286 SD MET A 40 12.406 38.595 23.755 1.00 11.75 S ANISOU 286 SD MET A 40 1880 1210 1375 -309 -502 190 S ATOM 287 CE MET A 40 10.674 38.181 23.514 1.00 19.65 C ANISOU 287 CE MET A 40 2106 3081 2280 -1165 15 -303 C ATOM 288 N VAL A 41 15.559 40.934 22.818 1.00 6.51 N ANISOU 288 N VAL A 41 760 807 906 81 86 -4 N ATOM 289 CA VAL A 41 17.014 40.788 22.693 1.00 6.58 C ANISOU 289 CA VAL A 41 775 812 914 92 36 -9 C ATOM 290 C VAL A 41 17.457 39.363 23.052 1.00 6.11 C ANISOU 290 C VAL A 41 728 780 815 -32 -13 -56 C ATOM 291 O VAL A 41 16.970 38.787 24.040 1.00 8.48 O ANISOU 291 O VAL A 41 1181 898 1143 37 282 118 O ATOM 292 CB AVAL A 41 17.677 41.767 23.728 0.50 5.40 C ANISOU 292 CB AVAL A 41 518 820 714 49 146 130 C ATOM 293 CG1AVAL A 41 19.172 41.511 23.930 0.50 5.09 C ANISOU 293 CG1AVAL A 41 515 408 1010 -138 -176 -136 C ATOM 294 CG2AVAL A 41 17.464 43.211 23.294 0.50 7.32 C ANISOU 294 CG2AVAL A 41 847 644 1292 -140 -24 -69 C ATOM 295 CB BVAL A 41 17.840 41.826 23.476 0.50 13.23 C ANISOU 295 CB BVAL A 41 1594 826 2608 -455 -335 -76 C ATOM 296 CG1BVAL A 41 17.569 43.255 23.034 0.50 13.47 C ANISOU 296 CG1BVAL A 41 1891 1250 1979 70 20 227 C ATOM 297 CG2BVAL A 41 17.594 41.609 24.952 0.50 24.24 C ANISOU 297 CG2BVAL A 41 3367 3152 2693 -191 39 14 C ATOM 298 N THR A 42 18.431 38.844 22.309 1.00 6.24 N ANISOU 298 N THR A 42 789 743 840 77 -21 73 N ATOM 299 CA THR A 42 19.196 37.647 22.646 1.00 5.99 C ANISOU 299 CA THR A 42 815 715 746 30 -39 75 C ATOM 300 C THR A 42 20.667 38.061 22.794 1.00 6.49 C ANISOU 300 C THR A 42 805 710 949 -50 -62 90 C ATOM 301 O THR A 42 21.181 38.758 21.910 1.00 8.29 O ANISOU 301 O THR A 42 863 1099 1189 -196 -188 336 O ATOM 302 CB THR A 42 19.105 36.549 21.564 1.00 6.85 C ANISOU 302 CB THR A 42 882 759 963 1 -54 -14 C ATOM 303 OG1 THR A 42 17.707 36.311 21.274 1.00 7.71 O ANISOU 303 OG1 THR A 42 941 968 1022 -21 -153 -91 O ATOM 304 CG2 THR A 42 19.766 35.253 21.993 1.00 8.21 C ANISOU 304 CG2 THR A 42 1086 763 1270 111 -139 -34 C ATOM 305 N ALA A 43 21.376 37.619 23.844 1.00 7.06 N ANISOU 305 N ALA A 43 848 927 905 -97 -99 88 N ATOM 306 CA ALA A 43 22.829 37.871 23.924 1.00 7.16 C ANISOU 306 CA ALA A 43 809 912 1000 -82 -165 75 C ATOM 307 C ALA A 43 23.534 36.956 22.932 1.00 7.02 C ANISOU 307 C ALA A 43 819 833 1016 -29 -191 166 C ATOM 308 O ALA A 43 23.295 35.733 22.928 1.00 8.65 O ANISOU 308 O ALA A 43 1034 850 1401 -17 -111 174 O ATOM 309 CB ALA A 43 23.349 37.597 25.330 1.00 9.22 C ANISOU 309 CB ALA A 43 1084 1278 1142 38 -267 30 C ATOM 310 N GLU A 44 24.398 37.504 22.077 1.00 7.75 N ANISOU 310 N GLU A 44 967 874 1104 35 -19 125 N ATOM 311 CA GLU A 44 25.026 36.691 21.032 1.00 8.77 C ANISOU 311 CA GLU A 44 1106 1077 1150 89 7 107 C ATOM 312 C GLU A 44 25.946 35.621 21.598 1.00 8.13 C ANISOU 312 C GLU A 44 1138 962 990 70 -37 15 C ATOM 313 O GLU A 44 25.972 34.495 21.095 1.00 10.19 O ANISOU 313 O GLU A 44 1575 1060 1238 176 -162 -32 O ATOM 314 CB GLU A 44 25.725 37.591 19.997 1.00 9.93 C ANISOU 314 CB GLU A 44 1484 1217 1073 40 38 151 C ATOM 315 CG GLU A 44 26.144 36.829 18.746 1.00 12.01 C ANISOU 315 CG GLU A 44 1811 1375 1375 276 329 108 C ATOM 316 CD GLU A 44 26.763 37.660 17.653 1.00 15.53 C ANISOU 316 CD GLU A 44 2580 1594 1725 350 672 284 C ATOM 317 OE1 GLU A 44 27.028 38.853 17.869 1.00 19.08 O ANISOU 317 OE1 GLU A 44 3458 1758 2034 -167 650 216 O ATOM 318 OE2 GLU A 44 27.004 37.115 16.554 1.00 20.12 O ANISOU 318 OE2 GLU A 44 3487 2495 1663 493 759 146 O ATOM 319 N ASN A 45 26.739 35.947 22.617 1.00 8.19 N ANISOU 319 N ASN A 45 997 938 1174 74 -104 104 N ATOM 320 CA ASN A 45 27.709 35.042 23.222 1.00 9.05 C ANISOU 320 CA ASN A 45 1216 1039 1183 184 26 275 C ATOM 321 C ASN A 45 27.778 34.992 24.742 1.00 8.27 C ANISOU 321 C ASN A 45 1048 917 1176 163 -68 187 C ATOM 322 O ASN A 45 28.311 34.025 25.306 1.00 9.93 O ANISOU 322 O ASN A 45 1317 1090 1367 345 -218 76 O ATOM 323 CB ASN A 45 29.142 35.448 22.754 1.00 12.41 C ANISOU 323 CB ASN A 45 1251 1672 1793 278 291 340 C ATOM 324 CG ASN A 45 29.386 35.246 21.279 1.00 16.13 C ANISOU 324 CG ASN A 45 1731 2504 1894 197 446 185 C ATOM 325 OD1 ASN A 45 29.381 34.112 20.807 1.00 20.88 O ANISOU 325 OD1 ASN A 45 2408 3173 2353 -187 700 -692 O ATOM 326 ND2 ASN A 45 29.582 36.364 20.594 1.00 19.71 N ANISOU 326 ND2 ASN A 45 2376 2990 2123 172 517 634 N ATOM 327 N GLU A 46 27.237 36.010 25.418 1.00 7.82 N ANISOU 327 N GLU A 46 963 948 1059 65 -138 113 N ATOM 328 CA GLU A 46 27.528 36.244 26.835 1.00 8.06 C ANISOU 328 CA GLU A 46 961 958 1145 -61 -129 28 C ATOM 329 C GLU A 46 26.831 35.307 27.820 1.00 8.50 C ANISOU 329 C GLU A 46 1041 1004 1184 31 -130 124 C ATOM 330 O GLU A 46 27.225 35.293 29.000 1.00 10.05 O ANISOU 330 O GLU A 46 1433 1141 1245 -140 -229 56 O ATOM 331 CB GLU A 46 27.199 37.720 27.159 1.00 8.63 C ANISOU 331 CB GLU A 46 1274 978 1027 -42 -170 40 C ATOM 332 CG GLU A 46 28.030 38.760 26.432 1.00 9.89 C ANISOU 332 CG GLU A 46 1410 1096 1252 -115 -118 63 C ATOM 333 CD GLU A 46 27.691 39.058 24.990 1.00 9.17 C ANISOU 333 CD GLU A 46 1236 936 1313 -96 -161 130 C ATOM 334 OE1 GLU A 46 26.777 38.499 24.355 1.00 9.73 O ANISOU 334 OE1 GLU A 46 1327 963 1408 4 -273 98 O ATOM 335 OE2 GLU A 46 28.412 39.925 24.422 1.00 12.41 O ANISOU 335 OE2 GLU A 46 1633 1339 1744 -326 -304 546 O ATOM 336 N MET A 47 25.812 34.562 27.343 1.00 8.23 N ANISOU 336 N MET A 47 1047 946 1136 -33 -154 157 N ATOM 337 CA MET A 47 25.119 33.613 28.217 1.00 8.60 C ANISOU 337 CA MET A 47 1048 1105 1116 -4 -44 178 C ATOM 338 C MET A 47 25.428 32.159 27.863 1.00 8.70 C ANISOU 338 C MET A 47 964 1165 1176 68 -63 164 C ATOM 339 O MET A 47 24.763 31.239 28.406 1.00 10.73 O ANISOU 339 O MET A 47 1396 1112 1571 31 155 247 O ATOM 340 CB MET A 47 23.608 33.883 28.280 1.00 8.95 C ANISOU 340 CB MET A 47 1132 1201 1069 22 31 0 C ATOM 341 CG AMET A 47 23.268 35.210 28.922 0.50 7.78 C ANISOU 341 CG AMET A 47 760 1135 1062 -1 -386 -75 C ATOM 342 SD AMET A 47 21.487 35.435 29.148 0.50 10.21 S ANISOU 342 SD AMET A 47 896 1609 1376 75 11 -451 S ATOM 343 CE AMET A 47 21.462 37.170 29.613 0.50 10.71 C ANISOU 343 CE AMET A 47 1008 1586 1477 420 -140 -573 C ATOM 344 CG BMET A 47 23.277 35.198 28.971 0.50 13.47 C ANISOU 344 CG BMET A 47 1733 1228 2158 357 -29 -199 C ATOM 345 SD BMET A 47 21.500 35.447 29.137 0.50 16.56 S ANISOU 345 SD BMET A 47 1749 2186 2357 152 518 -365 S ATOM 346 CE BMET A 47 20.928 35.133 27.492 0.50 21.10 C ANISOU 346 CE BMET A 47 1746 3155 3118 -493 -319 -592 C ATOM 347 N LYS A 48 26.426 31.917 27.029 1.00 8.39 N ANISOU 347 N LYS A 48 1079 883 1226 119 -82 47 N ATOM 348 CA LYS A 48 26.906 30.565 26.717 1.00 8.30 C ANISOU 348 CA LYS A 48 992 864 1299 185 -83 128 C ATOM 349 C LYS A 48 27.651 29.962 27.909 1.00 7.78 C ANISOU 349 C LYS A 48 1096 750 1109 15 -72 77 C ATOM 350 O LYS A 48 27.944 30.641 28.915 1.00 8.68 O ANISOU 350 O LYS A 48 1237 979 1082 62 -108 10 O ATOM 351 CB LYS A 48 27.759 30.590 25.445 1.00 9.71 C ANISOU 351 CB LYS A 48 1306 1183 1200 172 -95 89 C ATOM 352 CG LYS A 48 26.949 30.917 24.204 1.00 11.70 C ANISOU 352 CG LYS A 48 1867 1301 1279 241 -343 -1 C ATOM 353 CD LYS A 48 27.828 31.137 22.992 1.00 13.01 C ANISOU 353 CD LYS A 48 2107 1436 1399 426 -158 35 C ATOM 354 CE LYS A 48 27.025 31.379 21.715 1.00 15.91 C ANISOU 354 CE LYS A 48 3293 1410 1344 643 -455 -12 C ATOM 355 NZ LYS A 48 27.948 31.724 20.585 1.00 21.20 N ANISOU 355 NZ LYS A 48 4552 1994 1509 410 60 84 N ATOM 356 N ILE A 49 27.972 28.663 27.850 1.00 8.30 N ANISOU 356 N ILE A 49 1225 830 1100 62 -84 39 N ATOM 357 CA ILE A 49 28.533 27.952 28.998 1.00 7.71 C ANISOU 357 CA ILE A 49 1013 815 1102 54 27 180 C ATOM 358 C ILE A 49 29.916 28.473 29.376 1.00 7.97 C ANISOU 358 C ILE A 49 1121 801 1106 -9 -86 145 C ATOM 359 O ILE A 49 30.216 28.674 30.561 1.00 9.94 O ANISOU 359 O ILE A 49 1366 1242 1170 39 -132 14 O ATOM 360 CB ILE A 49 28.548 26.430 28.759 1.00 9.15 C ANISOU 360 CB ILE A 49 1255 843 1379 -12 -23 154 C ATOM 361 CG1 ILE A 49 27.162 25.883 28.376 1.00 11.20 C ANISOU 361 CG1 ILE A 49 1423 974 1860 -133 -77 -17 C ATOM 362 CG2 ILE A 49 29.076 25.684 29.987 1.00 10.44 C ANISOU 362 CG2 ILE A 49 1328 1112 1528 330 189 321 C ATOM 363 CD1 ILE A 49 27.192 24.469 27.838 1.00 15.20 C ANISOU 363 CD1 ILE A 49 1976 1187 2611 -282 -166 -365 C ATOM 364 N ASP A 50 30.788 28.679 28.378 1.00 8.21 N ANISOU 364 N ASP A 50 1019 914 1187 -49 -92 57 N ATOM 365 CA ASP A 50 32.139 29.178 28.615 1.00 9.55 C ANISOU 365 CA ASP A 50 981 1198 1450 -1 -99 -26 C ATOM 366 C ASP A 50 32.159 30.559 29.253 1.00 9.57 C ANISOU 366 C ASP A 50 1097 1190 1350 -81 -157 -21 C ATOM 367 O ASP A 50 32.995 30.830 30.129 1.00 13.85 O ANISOU 367 O ASP A 50 1388 1538 2337 68 -705 -376 O ATOM 368 CB ASP A 50 33.002 29.117 27.351 1.00 11.49 C ANISOU 368 CB ASP A 50 1142 1414 1811 -65 172 -265 C ATOM 369 CG ASP A 50 32.499 29.897 26.151 1.00 12.60 C ANISOU 369 CG ASP A 50 1469 1648 1671 -242 282 -60 C ATOM 370 OD1 ASP A 50 31.336 30.341 26.132 1.00 13.21 O ANISOU 370 OD1 ASP A 50 1684 1780 1557 -58 0 235 O ATOM 371 OD2 ASP A 50 33.306 30.073 25.186 1.00 20.38 O ANISOU 371 OD2 ASP A 50 2354 3034 2354 -430 918 122 O ATOM 372 N ALA A 51 31.248 31.450 28.868 1.00 8.86 N ANISOU 372 N ALA A 51 1129 980 1258 -157 -38 48 N ATOM 373 CA ALA A 51 31.207 32.812 29.376 1.00 10.14 C ANISOU 373 CA ALA A 51 1328 986 1538 -73 111 12 C ATOM 374 C ALA A 51 30.666 32.883 30.796 1.00 10.28 C ANISOU 374 C ALA A 51 1345 1110 1451 -216 32 -37 C ATOM 375 O ALA A 51 31.099 33.740 31.581 1.00 15.84 O ANISOU 375 O ALA A 51 2310 1856 1852 -902 402 -579 O ATOM 376 CB ALA A 51 30.306 33.649 28.453 1.00 12.91 C ANISOU 376 CB ALA A 51 2131 1187 1588 108 46 251 C ATOM 377 N THR A 52 29.731 32.009 31.169 1.00 8.53 N ANISOU 377 N THR A 52 1103 1019 1119 -55 -28 32 N ATOM 378 CA THR A 52 29.057 32.064 32.460 1.00 8.19 C ANISOU 378 CA THR A 52 988 1013 1111 -25 -57 110 C ATOM 379 C THR A 52 29.687 31.168 33.520 1.00 8.44 C ANISOU 379 C THR A 52 1091 976 1138 30 -151 67 C ATOM 380 O THR A 52 29.475 31.467 34.712 1.00 10.56 O ANISOU 380 O THR A 52 1629 1192 1192 268 -221 -70 O ATOM 381 CB THR A 52 27.542 31.771 32.350 1.00 8.77 C ANISOU 381 CB THR A 52 994 1078 1261 146 -225 69 C ATOM 382 OG1 THR A 52 27.325 30.489 31.740 1.00 9.25 O ANISOU 382 OG1 THR A 52 1087 1116 1310 -123 -59 124 O ATOM 383 CG2 THR A 52 26.801 32.860 31.584 1.00 10.66 C ANISOU 383 CG2 THR A 52 1285 1444 1322 399 -301 48 C ATOM 384 N GLU A 53 30.407 30.100 33.184 1.00 7.74 N ANISOU 384 N GLU A 53 944 959 1037 -9 -179 78 N ATOM 385 CA GLU A 53 31.026 29.226 34.192 1.00 7.90 C ANISOU 385 CA GLU A 53 995 947 1059 77 -239 35 C ATOM 386 C GLU A 53 32.431 28.852 33.703 1.00 8.92 C ANISOU 386 C GLU A 53 1066 1004 1318 31 -105 9 C ATOM 387 O GLU A 53 32.694 27.715 33.279 1.00 9.26 O ANISOU 387 O GLU A 53 1067 1044 1408 88 -167 47 O ATOM 388 CB GLU A 53 30.145 27.997 34.485 1.00 8.45 C ANISOU 388 CB GLU A 53 989 1093 1128 88 -199 111 C ATOM 389 CG GLU A 53 30.516 27.251 35.768 1.00 9.55 C ANISOU 389 CG GLU A 53 1241 1236 1153 -123 -359 193 C ATOM 390 CD GLU A 53 29.704 26.006 36.071 1.00 8.82 C ANISOU 390 CD GLU A 53 1028 1234 1091 12 -229 180 C ATOM 391 OE1 GLU A 53 28.746 25.661 35.343 1.00 10.32 O ANISOU 391 OE1 GLU A 53 1195 1419 1308 -217 -368 299 O ATOM 392 OE2 GLU A 53 30.029 25.312 37.068 1.00 11.10 O ANISOU 392 OE2 GLU A 53 1265 1578 1373 -76 -408 407 O ATOM 393 N PRO A 54 33.384 29.806 33.755 1.00 9.58 N ANISOU 393 N PRO A 54 933 1123 1585 -12 -185 -60 N ATOM 394 CA PRO A 54 34.714 29.589 33.214 1.00 10.81 C ANISOU 394 CA PRO A 54 1085 1392 1633 -109 -17 -52 C ATOM 395 C PRO A 54 35.546 28.552 33.952 1.00 10.91 C ANISOU 395 C PRO A 54 1030 1440 1674 -34 -83 -171 C ATOM 396 O PRO A 54 36.451 27.949 33.380 1.00 13.14 O ANISOU 396 O PRO A 54 1377 1502 2113 128 232 -43 O ATOM 397 CB PRO A 54 35.370 30.984 33.196 1.00 14.31 C ANISOU 397 CB PRO A 54 1344 1496 2598 -258 -76 358 C ATOM 398 CG PRO A 54 34.585 31.767 34.174 1.00 17.83 C ANISOU 398 CG PRO A 54 1725 1642 3409 -414 15 -366 C ATOM 399 CD PRO A 54 33.181 31.219 34.174 1.00 11.69 C ANISOU 399 CD PRO A 54 1334 1225 1882 77 -224 -148 C ATOM 400 N GLN A 55 35.266 28.339 35.223 1.00 11.13 N ANISOU 400 N GLN A 55 1332 1323 1575 196 -308 -77 N ATOM 401 CA GLN A 55 35.851 27.295 36.055 1.00 11.61 C ANISOU 401 CA GLN A 55 1151 1743 1517 176 -406 65 C ATOM 402 C GLN A 55 34.695 26.591 36.771 1.00 12.08 C ANISOU 402 C GLN A 55 1463 1655 1472 118 -169 -107 C ATOM 403 O GLN A 55 33.700 27.252 37.071 1.00 13.49 O ANISOU 403 O GLN A 55 1501 1913 1713 269 -132 95 O ATOM 404 CB GLN A 55 36.868 27.831 37.057 1.00 16.26 C ANISOU 404 CB GLN A 55 1546 2601 2031 -76 -709 -124 C ATOM 405 CG GLN A 55 38.079 28.495 36.448 1.00 20.04 C ANISOU 405 CG GLN A 55 1702 3137 2776 -283 -513 -80 C ATOM 406 CD GLN A 55 38.964 27.601 35.622 1.00 24.96 C ANISOU 406 CD GLN A 55 2006 3355 4123 -92 173 -45 C ATOM 407 OE1 GLN A 55 38.879 26.379 35.728 1.00 28.35 O ANISOU 407 OE1 GLN A 55 2544 3324 4904 554 234 183 O ATOM 408 NE2 GLN A 55 39.819 28.214 34.808 1.00 29.63 N ANISOU 408 NE2 GLN A 55 2695 4302 4262 38 658 339 N ATOM 409 N ARG A 56 34.809 25.296 37.062 1.00 13.44 N ANISOU 409 N ARG A 56 1489 1786 1833 -25 -602 268 N ATOM 410 CA ARG A 56 33.693 24.574 37.667 1.00 14.07 C ANISOU 410 CA ARG A 56 1514 2098 1735 -1 -446 197 C ATOM 411 C ARG A 56 33.285 25.204 38.995 1.00 14.41 C ANISOU 411 C ARG A 56 1734 2158 1582 -97 -571 180 C ATOM 412 O ARG A 56 34.106 25.391 39.899 1.00 17.19 O ANISOU 412 O ARG A 56 1734 3194 1603 56 -668 137 O ATOM 413 CB ARG A 56 34.020 23.091 37.862 1.00 16.34 C ANISOU 413 CB ARG A 56 2161 2163 1884 82 -285 373 C ATOM 414 CG ARG A 56 32.802 22.315 38.350 1.00 17.86 C ANISOU 414 CG ARG A 56 2253 2231 2301 56 11 203 C ATOM 415 CD ARG A 56 32.994 20.812 38.334 1.00 21.67 C ANISOU 415 CD ARG A 56 2825 2327 3082 290 47 235 C ATOM 416 NE ARG A 56 31.811 20.106 38.831 1.00 22.21 N ANISOU 416 NE ARG A 56 2800 2804 2835 16 -170 103 N ATOM 417 CZ ARG A 56 31.729 18.786 38.939 1.00 23.17 C ANISOU 417 CZ ARG A 56 2913 2774 3117 -148 -306 -93 C ATOM 418 NH1 ARG A 56 32.757 18.020 38.585 1.00 24.15 N ANISOU 418 NH1 ARG A 56 3224 3075 2878 -99 53 -289 N ATOM 419 NH2 ARG A 56 30.603 18.256 39.401 1.00 27.33 N ANISOU 419 NH2 ARG A 56 3241 3700 3442 -300 174 -54 N ATOM 420 N GLY A 57 32.000 25.564 39.103 1.00 14.45 N ANISOU 420 N GLY A 57 1770 2253 1468 -55 -403 419 N ATOM 421 CA GLY A 57 31.453 26.161 40.302 1.00 15.86 C ANISOU 421 CA GLY A 57 2063 2438 1526 181 -315 439 C ATOM 422 C GLY A 57 31.716 27.637 40.504 1.00 15.49 C ANISOU 422 C GLY A 57 1975 2465 1446 254 -48 184 C ATOM 423 O GLY A 57 31.318 28.193 41.540 1.00 22.08 O ANISOU 423 O GLY A 57 3330 3172 1889 308 259 -290 O ATOM 424 N GLN A 58 32.397 28.287 39.570 1.00 14.04 N ANISOU 424 N GLN A 58 1759 2175 1401 120 -396 183 N ATOM 425 CA GLN A 58 32.751 29.701 39.644 1.00 14.63 C ANISOU 425 CA GLN A 58 1917 2076 1565 327 -392 -21 C ATOM 426 C GLN A 58 32.011 30.424 38.514 1.00 14.51 C ANISOU 426 C GLN A 58 2026 2019 1469 404 -271 -41 C ATOM 427 O GLN A 58 32.418 30.384 37.354 1.00 19.65 O ANISOU 427 O GLN A 58 2452 3310 1703 927 92 162 O ATOM 428 CB GLN A 58 34.256 29.881 39.492 1.00 19.00 C ANISOU 428 CB GLN A 58 2008 2389 2822 -114 -494 -410 C ATOM 429 CG GLN A 58 35.144 29.353 40.598 1.00 27.60 C ANISOU 429 CG GLN A 58 3483 3987 3018 507 -719 168 C ATOM 430 CD GLN A 58 36.621 29.630 40.382 1.00 37.10 C ANISOU 430 CD GLN A 58 3839 5163 5092 -167 -204 115 C ATOM 431 OE1 GLN A 58 37.054 30.473 39.594 1.00 40.77 O ANISOU 431 OE1 GLN A 58 4677 5435 5378 -610 97 99 O ATOM 432 NE2 GLN A 58 37.450 28.883 41.112 1.00 41.09 N ANISOU 432 NE2 GLN A 58 4770 5351 5492 260 -500 139 N ATOM 433 N PHE A 59 30.898 31.056 38.831 1.00 12.04 N ANISOU 433 N PHE A 59 1727 1761 1088 91 -335 -90 N ATOM 434 CA PHE A 59 30.062 31.736 37.840 1.00 11.55 C ANISOU 434 CA PHE A 59 1733 1540 1116 137 -304 -100 C ATOM 435 C PHE A 59 30.506 33.172 37.633 1.00 13.90 C ANISOU 435 C PHE A 59 2231 1552 1498 -12 -295 -235 C ATOM 436 O PHE A 59 30.979 33.846 38.551 1.00 18.95 O ANISOU 436 O PHE A 59 3325 2069 1805 -353 -857 -268 O ATOM 437 CB PHE A 59 28.572 31.625 38.228 1.00 13.70 C ANISOU 437 CB PHE A 59 1747 2116 1342 252 -291 -128 C ATOM 438 CG PHE A 59 28.047 30.208 38.158 1.00 13.55 C ANISOU 438 CG PHE A 59 1698 2144 1307 189 -160 -114 C ATOM 439 CD1 PHE A 59 28.180 29.343 39.230 1.00 15.25 C ANISOU 439 CD1 PHE A 59 2271 2071 1451 5 -227 -52 C ATOM 440 CD2 PHE A 59 27.432 29.732 37.010 1.00 13.39 C ANISOU 440 CD2 PHE A 59 1644 2090 1352 149 -279 2 C ATOM 441 CE1 PHE A 59 27.714 28.046 39.167 1.00 15.64 C ANISOU 441 CE1 PHE A 59 2154 2227 1563 -246 -251 241 C ATOM 442 CE2 PHE A 59 26.960 28.436 36.943 1.00 13.95 C ANISOU 442 CE2 PHE A 59 1573 2305 1421 -151 -99 -58 C ATOM 443 CZ PHE A 59 27.105 27.585 38.012 1.00 14.80 C ANISOU 443 CZ PHE A 59 1754 2336 1533 -148 -3 46 C ATOM 444 N ASN A 60 30.394 33.648 36.403 1.00 12.89 N ANISOU 444 N ASN A 60 1938 1356 1605 87 -495 -103 N ATOM 445 CA ASN A 60 30.745 35.010 36.017 1.00 13.75 C ANISOU 445 CA ASN A 60 1824 1361 2040 175 -376 -39 C ATOM 446 C ASN A 60 29.619 35.591 35.172 1.00 13.05 C ANISOU 446 C ASN A 60 1826 1397 1736 103 -367 -134 C ATOM 447 O ASN A 60 29.413 35.142 34.041 1.00 16.68 O ANISOU 447 O ASN A 60 2750 1862 1725 872 -400 -266 O ATOM 448 CB ASN A 60 32.052 35.045 35.205 1.00 17.19 C ANISOU 448 CB ASN A 60 1888 2027 2617 372 -139 70 C ATOM 449 CG ASN A 60 32.589 36.456 35.074 1.00 24.04 C ANISOU 449 CG ASN A 60 2895 2265 3974 -57 -103 349 C ATOM 450 OD1 ASN A 60 31.862 37.454 35.053 1.00 23.57 O ANISOU 450 OD1 ASN A 60 2236 2200 4521 -364 -123 614 O ATOM 451 ND2 ASN A 60 33.908 36.596 34.978 1.00 32.85 N ANISOU 451 ND2 ASN A 60 2947 3790 5744 -297 -166 -6 N ATOM 452 N PHE A 61 28.859 36.528 35.708 1.00 11.72 N ANISOU 452 N PHE A 61 1431 1400 1624 -89 -421 -249 N ATOM 453 CA PHE A 61 27.731 37.131 34.998 1.00 11.91 C ANISOU 453 CA PHE A 61 1368 1555 1601 -60 -378 -296 C ATOM 454 C PHE A 61 28.016 38.545 34.526 1.00 12.80 C ANISOU 454 C PHE A 61 1615 1464 1784 88 -314 -337 C ATOM 455 O PHE A 61 27.092 39.254 34.105 1.00 14.25 O ANISOU 455 O PHE A 61 1823 1745 1846 153 -336 43 O ATOM 456 CB PHE A 61 26.469 37.110 35.886 1.00 12.81 C ANISOU 456 CB PHE A 61 1624 1454 1790 157 -119 -153 C ATOM 457 CG PHE A 61 26.015 35.713 36.246 1.00 13.34 C ANISOU 457 CG PHE A 61 1471 1556 2040 -44 -232 -241 C ATOM 458 CD1 PHE A 61 25.455 34.882 35.288 1.00 15.73 C ANISOU 458 CD1 PHE A 61 1747 1703 2526 -342 -436 -267 C ATOM 459 CD2 PHE A 61 26.164 35.231 37.533 1.00 14.39 C ANISOU 459 CD2 PHE A 61 1596 1723 2149 83 103 6 C ATOM 460 CE1 PHE A 61 25.051 33.602 35.599 1.00 16.89 C ANISOU 460 CE1 PHE A 61 2023 1762 2632 -334 -311 -131 C ATOM 461 CE2 PHE A 61 25.751 33.955 37.867 1.00 16.83 C ANISOU 461 CE2 PHE A 61 1811 1884 2697 -35 -361 279 C ATOM 462 CZ PHE A 61 25.207 33.144 36.898 1.00 16.71 C ANISOU 462 CZ PHE A 61 1614 1940 2797 -31 -217 127 C ATOM 463 N SER A 62 29.266 39.016 34.577 1.00 13.16 N ANISOU 463 N SER A 62 1758 1521 1721 -85 -583 -46 N ATOM 464 CA SER A 62 29.532 40.414 34.230 1.00 14.93 C ANISOU 464 CA SER A 62 2131 1533 2010 -85 -540 51 C ATOM 465 C SER A 62 29.081 40.793 32.819 1.00 14.62 C ANISOU 465 C SER A 62 2134 1526 1895 -137 -501 -43 C ATOM 466 O SER A 62 28.363 41.790 32.628 1.00 15.57 O ANISOU 466 O SER A 62 2428 1561 1926 -105 -595 68 O ATOM 467 CB SER A 62 30.994 40.794 34.435 1.00 20.13 C ANISOU 467 CB SER A 62 2445 2471 2731 -663 -804 256 C ATOM 468 OG SER A 62 31.876 39.920 33.774 1.00 30.21 O ANISOU 468 OG SER A 62 3299 3707 4472 -199 82 -141 O ATOM 469 N SER A 63 29.540 40.063 31.795 1.00 13.89 N ANISOU 469 N SER A 63 1444 1731 2103 -153 -531 -173 N ATOM 470 CA SER A 63 29.149 40.413 30.424 1.00 14.48 C ANISOU 470 CA SER A 63 1418 2092 1993 -141 -416 -126 C ATOM 471 C SER A 63 27.683 40.096 30.132 1.00 10.68 C ANISOU 471 C SER A 63 1277 1458 1324 21 -55 -179 C ATOM 472 O SER A 63 27.007 40.846 29.430 1.00 12.96 O ANISOU 472 O SER A 63 1645 1538 1739 -161 -228 142 O ATOM 473 CB SER A 63 30.060 39.796 29.371 1.00 18.49 C ANISOU 473 CB SER A 63 1435 3021 2568 -229 -61 -413 C ATOM 474 OG SER A 63 29.931 38.386 29.361 1.00 22.00 O ANISOU 474 OG SER A 63 2350 2996 3014 63 9 -442 O ATOM 475 N ALA A 64 27.156 39.007 30.691 1.00 10.83 N ANISOU 475 N ALA A 64 1253 1427 1435 -65 -137 -175 N ATOM 476 CA ALA A 64 25.748 38.664 30.529 1.00 11.14 C ANISOU 476 CA ALA A 64 1346 1490 1397 -106 -213 -299 C ATOM 477 C ALA A 64 24.844 39.766 31.098 1.00 10.32 C ANISOU 477 C ALA A 64 1406 1209 1308 -145 -268 -101 C ATOM 478 O ALA A 64 23.847 40.140 30.448 1.00 11.22 O ANISOU 478 O ALA A 64 1537 1290 1437 -57 -321 -46 O ATOM 479 CB ALA A 64 25.455 37.329 31.193 1.00 12.54 C ANISOU 479 CB ALA A 64 1470 1216 2078 4 12 -416 C ATOM 480 N ASP A 65 25.175 40.255 32.296 1.00 10.79 N ANISOU 480 N ASP A 65 1389 1293 1418 -29 -338 -232 N ATOM 481 CA ASP A 65 24.380 41.313 32.925 1.00 11.57 C ANISOU 481 CA ASP A 65 1548 1322 1526 45 -304 -216 C ATOM 482 C ASP A 65 24.505 42.637 32.176 1.00 11.86 C ANISOU 482 C ASP A 65 1762 1329 1416 103 -380 -231 C ATOM 483 O ASP A 65 23.542 43.412 32.179 1.00 13.43 O ANISOU 483 O ASP A 65 1938 1422 1742 222 -201 -262 O ATOM 484 CB ASP A 65 24.727 41.459 34.405 1.00 12.14 C ANISOU 484 CB ASP A 65 1935 1132 1547 114 -302 -209 C ATOM 485 CG ASP A 65 24.124 40.371 35.288 1.00 14.00 C ANISOU 485 CG ASP A 65 2102 1422 1796 114 56 -102 C ATOM 486 OD1 ASP A 65 23.271 39.578 34.856 1.00 17.67 O ANISOU 486 OD1 ASP A 65 2539 1956 2219 -413 112 -124 O ATOM 487 OD2 ASP A 65 24.510 40.300 36.476 1.00 18.29 O ANISOU 487 OD2 ASP A 65 3276 1863 1810 215 -42 129 O ATOM 488 N ARG A 66 25.614 42.914 31.490 1.00 12.30 N ANISOU 488 N ARG A 66 1813 1317 1542 -93 -400 -52 N ATOM 489 CA ARG A 66 25.716 44.127 30.669 1.00 13.13 C ANISOU 489 CA ARG A 66 1868 1355 1768 -99 -432 24 C ATOM 490 C ARG A 66 24.636 44.084 29.581 1.00 12.22 C ANISOU 490 C ARG A 66 1750 1227 1664 -120 -321 -54 C ATOM 491 O ARG A 66 23.979 45.105 29.318 1.00 13.78 O ANISOU 491 O ARG A 66 1924 1155 2157 -124 -608 -62 O ATOM 492 CB ARG A 66 27.110 44.241 30.069 1.00 17.30 C ANISOU 492 CB ARG A 66 1824 2301 2448 -170 -394 -127 C ATOM 493 CG ARG A 66 27.509 45.559 29.433 1.00 27.39 C ANISOU 493 CG ARG A 66 3862 3045 3500 -221 13 828 C ATOM 494 CD ARG A 66 29.042 45.685 29.546 1.00 37.34 C ANISOU 494 CD ARG A 66 3903 5108 5176 -302 -61 19 C ATOM 495 NE ARG A 66 29.466 45.556 30.936 1.00 44.60 N ANISOU 495 NE ARG A 66 5714 5997 5233 145 -372 16 N ATOM 496 CZ ARG A 66 30.507 44.880 31.403 1.00 45.11 C ANISOU 496 CZ ARG A 66 5342 6127 5671 142 -157 -60 C ATOM 497 NH1 ARG A 66 31.296 44.205 30.577 1.00 49.51 N ANISOU 497 NH1 ARG A 66 6104 6444 6263 193 311 -368 N ATOM 498 NH2 ARG A 66 30.760 44.860 32.707 1.00 48.08 N ANISOU 498 NH2 ARG A 66 6222 6345 5700 -75 -304 -17 N ATOM 499 N VAL A 67 24.480 42.946 28.901 1.00 10.59 N ANISOU 499 N VAL A 67 1444 1309 1269 59 -83 -91 N ATOM 500 CA VAL A 67 23.469 42.827 27.845 1.00 9.83 C ANISOU 500 CA VAL A 67 1271 1217 1246 61 -25 93 C ATOM 501 C VAL A 67 22.060 42.859 28.430 1.00 9.24 C ANISOU 501 C VAL A 67 1323 1106 1082 -74 -94 -103 C ATOM 502 O VAL A 67 21.170 43.546 27.910 1.00 10.47 O ANISOU 502 O VAL A 67 1453 1212 1314 25 -58 -1 O ATOM 503 CB VAL A 67 23.721 41.588 26.957 1.00 10.78 C ANISOU 503 CB VAL A 67 1486 1406 1202 98 -101 -12 C ATOM 504 CG1 VAL A 67 22.583 41.434 25.947 1.00 12.68 C ANISOU 504 CG1 VAL A 67 1843 1618 1357 200 -308 -205 C ATOM 505 CG2 VAL A 67 25.079 41.644 26.270 1.00 13.66 C ANISOU 505 CG2 VAL A 67 1760 1756 1674 298 172 10 C ATOM 506 N TYR A 68 21.807 42.089 29.491 1.00 10.15 N ANISOU 506 N TYR A 68 1447 1168 1241 20 17 -1 N ATOM 507 CA TYR A 68 20.502 42.061 30.163 1.00 10.00 C ANISOU 507 CA TYR A 68 1497 1177 1124 27 -4 43 C ATOM 508 C TYR A 68 20.066 43.455 30.595 1.00 10.22 C ANISOU 508 C TYR A 68 1621 1191 1070 47 -60 127 C ATOM 509 O TYR A 68 18.930 43.894 30.324 1.00 11.25 O ANISOU 509 O TYR A 68 1601 1357 1317 57 21 80 O ATOM 510 CB TYR A 68 20.502 41.049 31.337 1.00 10.86 C ANISOU 510 CB TYR A 68 1682 1127 1318 90 -89 121 C ATOM 511 CG TYR A 68 19.202 41.107 32.111 1.00 11.64 C ANISOU 511 CG TYR A 68 1822 1228 1374 11 70 196 C ATOM 512 CD1 TYR A 68 18.048 40.452 31.719 1.00 13.65 C ANISOU 512 CD1 TYR A 68 1964 1659 1565 -332 174 279 C ATOM 513 CD2 TYR A 68 19.132 41.941 33.231 1.00 14.29 C ANISOU 513 CD2 TYR A 68 2332 1629 1469 -160 182 -29 C ATOM 514 CE1 TYR A 68 16.860 40.595 32.426 1.00 14.23 C ANISOU 514 CE1 TYR A 68 1912 1819 1678 -171 131 291 C ATOM 515 CE2 TYR A 68 17.956 42.088 33.942 1.00 16.44 C ANISOU 515 CE2 TYR A 68 2449 1950 1849 -220 406 -7 C ATOM 516 CZ TYR A 68 16.829 41.431 33.522 1.00 14.74 C ANISOU 516 CZ TYR A 68 2110 1610 1879 9 461 252 C ATOM 517 OH TYR A 68 15.655 41.609 34.241 1.00 19.36 O ANISOU 517 OH TYR A 68 2511 2318 2526 41 942 85 O ATOM 518 N ASN A 69 20.959 44.179 31.279 1.00 10.51 N ANISOU 518 N ASN A 69 1641 1342 1012 151 -71 -45 N ATOM 519 CA ASN A 69 20.632 45.524 31.756 1.00 12.12 C ANISOU 519 CA ASN A 69 1972 1381 1253 151 -54 -223 C ATOM 520 C ASN A 69 20.357 46.485 30.607 1.00 10.78 C ANISOU 520 C ASN A 69 1590 1130 1376 -73 111 -154 C ATOM 521 O ASN A 69 19.453 47.342 30.719 1.00 12.85 O ANISOU 521 O ASN A 69 1987 1414 1482 226 140 -155 O ATOM 522 CB ASN A 69 21.705 46.066 32.696 1.00 14.72 C ANISOU 522 CB ASN A 69 2252 1705 1637 50 -313 -291 C ATOM 523 CG ASN A 69 21.724 45.376 34.042 1.00 18.01 C ANISOU 523 CG ASN A 69 3079 2214 1549 204 -139 -291 C ATOM 524 OD1 ASN A 69 20.693 44.921 34.533 1.00 21.65 O ANISOU 524 OD1 ASN A 69 3603 2964 1658 -336 -27 -102 O ATOM 525 ND2 ASN A 69 22.895 45.296 34.663 1.00 23.85 N ANISOU 525 ND2 ASN A 69 3602 3454 2007 521 -685 -296 N ATOM 526 N TRP A 70 21.167 46.425 29.537 1.00 9.88 N ANISOU 526 N TRP A 70 1470 1093 1189 11 -21 26 N ATOM 527 CA TRP A 70 20.900 47.279 28.368 1.00 9.60 C ANISOU 527 CA TRP A 70 1511 908 1229 -58 -94 -61 C ATOM 528 C TRP A 70 19.489 47.018 27.838 1.00 9.85 C ANISOU 528 C TRP A 70 1427 989 1328 -4 -68 127 C ATOM 529 O TRP A 70 18.723 47.944 27.511 1.00 10.49 O ANISOU 529 O TRP A 70 1473 979 1534 70 42 -3 O ATOM 530 CB TRP A 70 21.964 47.058 27.265 1.00 10.38 C ANISOU 530 CB TRP A 70 1393 1065 1484 55 -59 -21 C ATOM 531 CG TRP A 70 21.767 47.972 26.086 1.00 9.99 C ANISOU 531 CG TRP A 70 1274 963 1558 -29 78 24 C ATOM 532 CD1 TRP A 70 22.349 49.206 25.942 1.00 11.29 C ANISOU 532 CD1 TRP A 70 1634 1086 1571 -225 -20 -15 C ATOM 533 CD2 TRP A 70 20.966 47.755 24.919 1.00 9.99 C ANISOU 533 CD2 TRP A 70 1420 1036 1340 -32 157 26 C ATOM 534 NE1 TRP A 70 21.938 49.768 24.762 1.00 12.61 N ANISOU 534 NE1 TRP A 70 2070 1045 1674 -241 0 216 N ATOM 535 CE2 TRP A 70 21.093 48.908 24.110 1.00 10.34 C ANISOU 535 CE2 TRP A 70 1584 1035 1308 2 284 19 C ATOM 536 CE3 TRP A 70 20.150 46.707 24.467 1.00 10.44 C ANISOU 536 CE3 TRP A 70 1476 1070 1419 -4 46 -48 C ATOM 537 CZ2 TRP A 70 20.416 49.049 22.899 1.00 11.71 C ANISOU 537 CZ2 TRP A 70 1883 1238 1330 66 221 -12 C ATOM 538 CZ3 TRP A 70 19.487 46.847 23.266 1.00 11.51 C ANISOU 538 CZ3 TRP A 70 1742 1190 1442 -205 -52 -119 C ATOM 539 CH2 TRP A 70 19.624 48.013 22.497 1.00 12.12 C ANISOU 539 CH2 TRP A 70 1729 1450 1426 2 141 60 C ATOM 540 N ALA A 71 19.097 45.730 27.727 1.00 9.31 N ANISOU 540 N ALA A 71 1335 1010 1191 -1 -2 -29 N ATOM 541 CA ALA A 71 17.780 45.389 27.214 1.00 10.12 C ANISOU 541 CA ALA A 71 1457 1053 1334 13 -151 -132 C ATOM 542 C ALA A 71 16.645 45.963 28.052 1.00 11.22 C ANISOU 542 C ALA A 71 1397 1112 1752 36 60 138 C ATOM 543 O ALA A 71 15.745 46.621 27.512 1.00 11.10 O ANISOU 543 O ALA A 71 1404 1119 1696 48 4 -8 O ATOM 544 CB ALA A 71 17.637 43.867 27.107 1.00 11.63 C ANISOU 544 CB ALA A 71 1684 1032 1704 59 -147 -196 C ATOM 545 N VAL A 72 16.697 45.726 29.357 1.00 12.20 N ANISOU 545 N VAL A 72 1608 1352 1677 118 306 108 N ATOM 546 CA VAL A 72 15.609 46.201 30.229 1.00 14.75 C ANISOU 546 CA VAL A 72 1905 1833 1867 333 615 213 C ATOM 547 C VAL A 72 15.548 47.718 30.296 1.00 13.96 C ANISOU 547 C VAL A 72 1893 1836 1577 389 436 180 C ATOM 548 O VAL A 72 14.456 48.311 30.261 1.00 17.23 O ANISOU 548 O VAL A 72 1949 2136 2460 504 580 -48 O ATOM 549 CB VAL A 72 15.633 45.516 31.609 1.00 18.28 C ANISOU 549 CB VAL A 72 2653 2436 1858 393 868 298 C ATOM 550 CG1AVAL A 72 15.605 44.000 31.427 0.50 21.51 C ANISOU 550 CG1AVAL A 72 2863 2339 2971 228 703 663 C ATOM 551 CG2AVAL A 72 16.818 45.910 32.458 0.50 18.90 C ANISOU 551 CG2AVAL A 72 3174 2555 1450 263 670 273 C ATOM 552 CG1BVAL A 72 14.678 46.167 32.599 0.50 18.12 C ANISOU 552 CG1BVAL A 72 2366 2539 1980 487 834 480 C ATOM 553 CG2BVAL A 72 15.308 44.035 31.447 0.50 21.55 C ANISOU 553 CG2BVAL A 72 2526 2555 3107 146 613 327 C ATOM 554 N GLN A 73 16.696 48.406 30.273 1.00 13.54 N ANISOU 554 N GLN A 73 2075 1395 1674 394 205 -396 N ATOM 555 CA GLN A 73 16.737 49.863 30.285 1.00 14.61 C ANISOU 555 CA GLN A 73 2509 1403 1641 397 108 -355 C ATOM 556 C GLN A 73 16.140 50.463 29.022 1.00 14.38 C ANISOU 556 C GLN A 73 2391 1283 1791 302 -100 -451 C ATOM 557 O GLN A 73 15.654 51.604 29.025 1.00 18.95 O ANISOU 557 O GLN A 73 3226 1609 2367 855 -342 -633 O ATOM 558 CB GLN A 73 18.173 50.344 30.492 1.00 18.56 C ANISOU 558 CB GLN A 73 2715 1800 2537 222 -219 -743 C ATOM 559 CG GLN A 73 18.706 50.105 31.902 1.00 26.17 C ANISOU 559 CG GLN A 73 4105 3186 2652 243 -389 -272 C ATOM 560 CD GLN A 73 20.207 50.267 32.009 1.00 35.13 C ANISOU 560 CD GLN A 73 4154 4696 4497 -50 -408 76 C ATOM 561 OE1 GLN A 73 20.848 50.921 31.187 1.00 40.57 O ANISOU 561 OE1 GLN A 73 5139 5241 5036 -419 -34 332 O ATOM 562 NE2 GLN A 73 20.802 49.659 33.033 1.00 37.51 N ANISOU 562 NE2 GLN A 73 5032 4821 4398 145 -420 147 N ATOM 563 N ASN A 74 16.171 49.721 27.922 1.00 10.93 N ANISOU 563 N ASN A 74 1615 1057 1482 124 82 -207 N ATOM 564 CA ASN A 74 15.640 50.115 26.632 1.00 10.71 C ANISOU 564 CA ASN A 74 1569 892 1609 16 155 1 C ATOM 565 C ASN A 74 14.299 49.492 26.288 1.00 11.28 C ANISOU 565 C ASN A 74 1455 1098 1732 22 177 -48 C ATOM 566 O ASN A 74 13.849 49.562 25.129 1.00 13.58 O ANISOU 566 O ASN A 74 1709 1567 1886 46 -4 -26 O ATOM 567 CB ASN A 74 16.692 49.862 25.555 1.00 10.96 C ANISOU 567 CB ASN A 74 1488 1045 1632 -180 249 17 C ATOM 568 CG ASN A 74 17.834 50.856 25.576 1.00 11.21 C ANISOU 568 CG ASN A 74 1568 1048 1643 -251 -100 -7 C ATOM 569 OD1 ASN A 74 17.687 51.967 25.013 1.00 15.77 O ANISOU 569 OD1 ASN A 74 1767 1406 2819 -378 -137 662 O ATOM 570 ND2 ASN A 74 18.945 50.551 26.243 1.00 11.85 N ANISOU 570 ND2 ASN A 74 1494 1063 1945 -312 -111 81 N ATOM 571 N GLY A 75 13.587 48.934 27.277 1.00 11.71 N ANISOU 571 N GLY A 75 1448 1112 1889 -51 273 -63 N ATOM 572 CA GLY A 75 12.234 48.440 27.119 1.00 13.18 C ANISOU 572 CA GLY A 75 1401 1315 2292 68 203 -299 C ATOM 573 C GLY A 75 12.045 47.135 26.387 1.00 13.19 C ANISOU 573 C GLY A 75 1445 1000 2568 6 177 -125 C ATOM 574 O GLY A 75 10.952 46.872 25.868 1.00 18.07 O ANISOU 574 O GLY A 75 1521 1591 3755 101 -190 -340 O ATOM 575 N LYS A 76 13.049 46.267 26.335 1.00 10.79 N ANISOU 575 N LYS A 76 1447 920 1734 32 272 93 N ATOM 576 CA LYS A 76 12.992 44.982 25.676 1.00 9.66 C ANISOU 576 CA LYS A 76 1229 990 1449 -103 88 126 C ATOM 577 C LYS A 76 12.909 43.813 26.676 1.00 9.44 C ANISOU 577 C LYS A 76 1251 1071 1266 -116 32 94 C ATOM 578 O LYS A 76 13.440 43.878 27.790 1.00 13.11 O ANISOU 578 O LYS A 76 2275 1322 1383 -407 -308 85 O ATOM 579 CB LYS A 76 14.229 44.748 24.770 1.00 9.94 C ANISOU 579 CB LYS A 76 1398 1007 1371 -215 167 -6 C ATOM 580 CG LYS A 76 14.340 45.680 23.575 1.00 11.39 C ANISOU 580 CG LYS A 76 1462 1436 1431 -92 99 141 C ATOM 581 CD LYS A 76 15.440 46.706 23.710 1.00 12.36 C ANISOU 581 CD LYS A 76 1484 1417 1794 -113 72 231 C ATOM 582 CE LYS A 76 15.537 47.696 22.559 1.00 11.54 C ANISOU 582 CE LYS A 76 1692 1137 1555 -230 28 11 C ATOM 583 NZ LYS A 76 14.335 48.584 22.448 1.00 11.17 N ANISOU 583 NZ LYS A 76 1729 1073 1441 -278 84 75 N ATOM 584 N GLN A 77 12.268 42.755 26.216 1.00 8.84 N ANISOU 584 N GLN A 77 1263 921 1176 61 112 -2 N ATOM 585 CA GLN A 77 12.323 41.456 26.893 1.00 8.68 C ANISOU 585 CA GLN A 77 1339 908 1051 49 184 43 C ATOM 586 C GLN A 77 13.569 40.707 26.392 1.00 7.78 C ANISOU 586 C GLN A 77 1151 964 841 -51 50 76 C ATOM 587 O GLN A 77 14.222 41.133 25.421 1.00 8.51 O ANISOU 587 O GLN A 77 1230 1023 981 121 156 118 O ATOM 588 CB GLN A 77 11.050 40.632 26.673 1.00 11.27 C ANISOU 588 CB GLN A 77 1381 1094 1805 -93 454 24 C ATOM 589 CG GLN A 77 9.793 41.235 27.279 1.00 16.61 C ANISOU 589 CG GLN A 77 1535 1799 2976 324 601 256 C ATOM 590 CD GLN A 77 8.563 40.415 26.925 1.00 26.29 C ANISOU 590 CD GLN A 77 1972 3836 4182 -306 -51 -109 C ATOM 591 OE1 GLN A 77 8.215 40.206 25.761 1.00 32.57 O ANISOU 591 OE1 GLN A 77 3039 4859 4478 -845 -378 -599 O ATOM 592 NE2 GLN A 77 7.881 39.944 27.958 1.00 35.11 N ANISOU 592 NE2 GLN A 77 4371 4471 4497 -630 541 366 N ATOM 593 N VAL A 78 13.941 39.612 27.070 1.00 8.29 N ANISOU 593 N VAL A 78 1160 1030 961 92 140 79 N ATOM 594 CA VAL A 78 15.165 38.857 26.790 1.00 7.73 C ANISOU 594 CA VAL A 78 1097 988 850 -50 88 -61 C ATOM 595 C VAL A 78 14.905 37.359 26.636 1.00 8.09 C ANISOU 595 C VAL A 78 1036 981 1058 26 79 238 C ATOM 596 O VAL A 78 14.191 36.740 27.443 1.00 10.25 O ANISOU 596 O VAL A 78 1465 1208 1223 -141 277 228 O ATOM 597 CB VAL A 78 16.205 39.108 27.910 1.00 9.91 C ANISOU 597 CB VAL A 78 1303 1302 1161 -12 -135 65 C ATOM 598 CG1 VAL A 78 17.473 38.324 27.659 1.00 12.00 C ANISOU 598 CG1 VAL A 78 1183 1883 1493 46 -293 -98 C ATOM 599 CG2 VAL A 78 16.513 40.600 28.041 1.00 13.35 C ANISOU 599 CG2 VAL A 78 2063 1428 1580 -194 -500 -95 C ATOM 600 N ARG A 79 15.505 36.768 25.588 1.00 7.84 N ANISOU 600 N ARG A 79 1141 816 1023 27 13 176 N ATOM 601 CA ARG A 79 15.562 35.315 25.407 1.00 8.07 C ANISOU 601 CA ARG A 79 1094 804 1170 -40 -66 173 C ATOM 602 C ARG A 79 16.944 34.836 25.889 1.00 7.67 C ANISOU 602 C ARG A 79 1044 888 982 -88 -38 153 C ATOM 603 O ARG A 79 17.952 35.413 25.447 1.00 10.88 O ANISOU 603 O ARG A 79 1125 1330 1679 -123 -36 555 O ATOM 604 CB ARG A 79 15.456 34.857 23.933 1.00 11.74 C ANISOU 604 CB ARG A 79 1693 1145 1622 -190 -493 -330 C ATOM 605 CG ARG A 79 14.330 35.350 23.088 1.00 12.31 C ANISOU 605 CG ARG A 79 2029 1304 1343 63 -268 54 C ATOM 606 CD ARG A 79 14.262 34.708 21.711 1.00 9.71 C ANISOU 606 CD ARG A 79 1499 1059 1133 -89 -176 150 C ATOM 607 NE ARG A 79 13.840 33.308 21.824 1.00 8.85 N ANISOU 607 NE ARG A 79 1183 1031 1151 8 9 107 N ATOM 608 CZ ARG A 79 14.624 32.227 21.826 1.00 7.80 C ANISOU 608 CZ ARG A 79 1059 992 911 -24 5 22 C ATOM 609 NH1 ARG A 79 15.910 32.288 21.502 1.00 8.68 N ANISOU 609 NH1 ARG A 79 1159 962 1179 -33 143 114 N ATOM 610 NH2 ARG A 79 14.061 31.053 22.127 1.00 9.40 N ANISOU 610 NH2 ARG A 79 1193 1127 1250 -98 246 133 N ATOM 611 N GLY A 80 17.016 33.787 26.687 1.00 7.59 N ANISOU 611 N GLY A 80 1030 820 1036 -29 -2 166 N ATOM 612 CA GLY A 80 18.280 33.243 27.188 1.00 8.13 C ANISOU 612 CA GLY A 80 1063 953 1072 27 -12 138 C ATOM 613 C GLY A 80 18.867 32.213 26.231 1.00 7.35 C ANISOU 613 C GLY A 80 1011 753 1028 -132 16 111 C ATOM 614 O GLY A 80 18.155 31.315 25.769 1.00 10.18 O ANISOU 614 O GLY A 80 1187 1172 1508 -354 125 -240 O ATOM 615 N HIS A 81 20.154 32.300 25.935 1.00 8.36 N ANISOU 615 N HIS A 81 933 814 1430 7 -77 -73 N ATOM 616 CA HIS A 81 20.832 31.430 24.960 1.00 7.81 C ANISOU 616 CA HIS A 81 1037 725 1205 58 -142 69 C ATOM 617 C HIS A 81 22.240 31.145 25.465 1.00 6.96 C ANISOU 617 C HIS A 81 1016 645 985 -68 -144 136 C ATOM 618 O HIS A 81 23.033 32.094 25.542 1.00 9.34 O ANISOU 618 O HIS A 81 1249 846 1453 -186 -176 215 O ATOM 619 CB HIS A 81 20.850 32.224 23.633 1.00 10.26 C ANISOU 619 CB HIS A 81 1258 1260 1381 136 -264 363 C ATOM 620 CG HIS A 81 21.463 31.468 22.518 1.00 11.18 C ANISOU 620 CG HIS A 81 1352 1760 1135 122 -225 330 C ATOM 621 ND1 HIS A 81 20.805 30.443 21.831 1.00 11.98 N ANISOU 621 ND1 HIS A 81 1760 1754 1038 112 -137 176 N ATOM 622 CD2 HIS A 81 22.658 31.603 21.899 1.00 13.61 C ANISOU 622 CD2 HIS A 81 1487 2286 1396 76 -84 112 C ATOM 623 CE1 HIS A 81 21.587 29.981 20.874 1.00 14.20 C ANISOU 623 CE1 HIS A 81 1747 2249 1398 221 -2 51 C ATOM 624 NE2 HIS A 81 22.710 30.669 20.892 1.00 14.70 N ANISOU 624 NE2 HIS A 81 1771 2544 1272 103 -183 -22 N ATOM 625 N THR A 82 22.610 29.935 25.835 1.00 7.24 N ANISOU 625 N THR A 82 859 709 1182 -67 -127 223 N ATOM 626 CA THR A 82 21.916 28.660 25.793 1.00 6.80 C ANISOU 626 CA THR A 82 866 766 953 -58 -146 168 C ATOM 627 C THR A 82 22.511 27.793 26.924 1.00 7.05 C ANISOU 627 C THR A 82 861 851 967 -23 -128 113 C ATOM 628 O THR A 82 23.687 27.971 27.282 1.00 8.51 O ANISOU 628 O THR A 82 1016 1024 1193 -115 -262 244 O ATOM 629 CB THR A 82 22.034 27.945 24.450 1.00 8.20 C ANISOU 629 CB THR A 82 1191 933 991 36 -89 125 C ATOM 630 OG1 THR A 82 21.354 26.682 24.443 1.00 9.52 O ANISOU 630 OG1 THR A 82 1475 1093 1049 -132 -85 -161 O ATOM 631 CG2 THR A 82 23.464 27.687 24.012 1.00 10.64 C ANISOU 631 CG2 THR A 82 1285 1373 1386 -1 139 -105 C ATOM 632 N LEU A 83 21.738 26.863 27.510 1.00 6.73 N ANISOU 632 N LEU A 83 932 890 735 -84 -168 134 N ATOM 633 CA LEU A 83 22.151 26.162 28.717 1.00 7.34 C ANISOU 633 CA LEU A 83 1106 853 830 -26 -210 159 C ATOM 634 C LEU A 83 22.912 24.864 28.543 1.00 7.11 C ANISOU 634 C LEU A 83 928 927 847 -90 -173 191 C ATOM 635 O LEU A 83 23.716 24.544 29.435 1.00 9.95 O ANISOU 635 O LEU A 83 1427 1204 1152 263 -487 83 O ATOM 636 CB LEU A 83 20.900 25.920 29.599 1.00 8.08 C ANISOU 636 CB LEU A 83 1371 981 717 17 -110 128 C ATOM 637 CG LEU A 83 20.217 27.191 30.123 1.00 9.53 C ANISOU 637 CG LEU A 83 1536 1196 889 258 -56 93 C ATOM 638 CD1 LEU A 83 18.859 26.868 30.730 1.00 12.13 C ANISOU 638 CD1 LEU A 83 1778 1704 1128 296 286 -79 C ATOM 639 CD2 LEU A 83 21.073 27.929 31.144 1.00 13.06 C ANISOU 639 CD2 LEU A 83 2047 1396 1522 108 -179 -365 C ATOM 640 N ALA A 84 22.721 24.147 27.448 1.00 7.79 N ANISOU 640 N ALA A 84 1019 1128 812 110 -196 55 N ATOM 641 CA ALA A 84 23.357 22.853 27.225 1.00 8.31 C ANISOU 641 CA ALA A 84 1008 1068 1080 119 -93 110 C ATOM 642 C ALA A 84 23.586 22.700 25.722 1.00 8.57 C ANISOU 642 C ALA A 84 933 1329 996 165 -172 -13 C ATOM 643 O ALA A 84 22.654 22.761 24.916 1.00 10.56 O ANISOU 643 O ALA A 84 1020 1879 1112 275 -224 -64 O ATOM 644 CB ALA A 84 22.501 21.720 27.774 1.00 10.16 C ANISOU 644 CB ALA A 84 1535 960 1366 70 41 157 C ATOM 645 N TRP A 85 24.844 22.510 25.319 1.00 8.74 N ANISOU 645 N TRP A 85 938 1245 1136 99 -85 -46 N ATOM 646 CA TRP A 85 25.287 22.539 23.926 1.00 8.94 C ANISOU 646 CA TRP A 85 970 1193 1233 134 13 -99 C ATOM 647 C TRP A 85 26.630 21.843 23.796 1.00 8.16 C ANISOU 647 C TRP A 85 786 1117 1197 -45 -57 -54 C ATOM 648 O TRP A 85 27.470 21.917 24.719 1.00 9.75 O ANISOU 648 O TRP A 85 956 1446 1304 64 -169 -89 O ATOM 649 CB TRP A 85 25.425 24.018 23.494 1.00 9.96 C ANISOU 649 CB TRP A 85 1301 1191 1293 51 -39 -131 C ATOM 650 CG TRP A 85 25.631 24.363 22.067 1.00 8.98 C ANISOU 650 CG TRP A 85 932 1145 1336 24 -257 -7 C ATOM 651 CD1 TRP A 85 25.285 23.633 20.959 1.00 9.18 C ANISOU 651 CD1 TRP A 85 1142 1050 1297 -66 -67 53 C ATOM 652 CD2 TRP A 85 26.130 25.611 21.554 1.00 9.90 C ANISOU 652 CD2 TRP A 85 1184 1069 1508 87 -186 -39 C ATOM 653 NE1 TRP A 85 25.555 24.333 19.800 1.00 9.73 N ANISOU 653 NE1 TRP A 85 1295 1145 1257 -28 -247 -20 N ATOM 654 CE2 TRP A 85 26.068 25.548 20.149 1.00 10.33 C ANISOU 654 CE2 TRP A 85 1380 1023 1524 92 -252 89 C ATOM 655 CE3 TRP A 85 26.645 26.762 22.153 1.00 12.94 C ANISOU 655 CE3 TRP A 85 1734 1250 1934 -66 -418 -143 C ATOM 656 CZ2 TRP A 85 26.508 26.597 19.323 1.00 14.07 C ANISOU 656 CZ2 TRP A 85 2033 1438 1874 -173 -246 367 C ATOM 657 CZ3 TRP A 85 27.076 27.797 21.341 1.00 16.81 C ANISOU 657 CZ3 TRP A 85 2702 1397 2289 -298 -286 74 C ATOM 658 CH2 TRP A 85 27.000 27.706 19.944 1.00 16.70 C ANISOU 658 CH2 TRP A 85 2783 1338 2225 -370 -224 398 C ATOM 659 N HIS A 86 26.900 21.218 22.654 1.00 8.54 N ANISOU 659 N HIS A 86 967 1068 1211 239 -131 -100 N ATOM 660 CA HIS A 86 28.189 20.578 22.401 1.00 9.09 C ANISOU 660 CA HIS A 86 885 1124 1446 136 -69 -48 C ATOM 661 C HIS A 86 29.303 21.578 22.117 1.00 9.03 C ANISOU 661 C HIS A 86 1008 1030 1394 111 -110 -65 C ATOM 662 O HIS A 86 30.487 21.219 22.255 1.00 12.26 O ANISOU 662 O HIS A 86 1051 1408 2198 147 -135 35 O ATOM 663 CB HIS A 86 28.102 19.616 21.196 1.00 9.85 C ANISOU 663 CB HIS A 86 1134 916 1692 87 -5 -107 C ATOM 664 CG HIS A 86 27.877 20.294 19.875 1.00 9.81 C ANISOU 664 CG HIS A 86 1063 1210 1456 91 -23 -241 C ATOM 665 ND1 HIS A 86 26.652 20.824 19.502 1.00 10.48 N ANISOU 665 ND1 HIS A 86 1200 1266 1515 150 -98 -226 N ATOM 666 CD2 HIS A 86 28.755 20.574 18.879 1.00 11.72 C ANISOU 666 CD2 HIS A 86 1206 1692 1556 109 98 -184 C ATOM 667 CE1 HIS A 86 26.813 21.381 18.320 1.00 11.88 C ANISOU 667 CE1 HIS A 86 1488 1594 1432 78 -9 -245 C ATOM 668 NE2 HIS A 86 28.068 21.236 17.901 1.00 12.17 N ANISOU 668 NE2 HIS A 86 1602 1689 1334 -60 169 -29 N ATOM 669 N SER A 87 28.989 22.784 21.684 1.00 9.10 N ANISOU 669 N SER A 87 1024 1096 1338 98 -70 -10 N ATOM 670 CA SER A 87 29.955 23.782 21.247 1.00 10.24 C ANISOU 670 CA SER A 87 1166 1320 1404 -20 16 49 C ATOM 671 C SER A 87 30.226 24.829 22.336 1.00 9.77 C ANISOU 671 C SER A 87 1242 1320 1152 -136 -236 282 C ATOM 672 O SER A 87 29.391 25.067 23.204 1.00 11.56 O ANISOU 672 O SER A 87 1556 1394 1442 -17 -120 -49 O ATOM 673 CB SER A 87 29.408 24.489 19.996 1.00 12.80 C ANISOU 673 CB SER A 87 1763 1634 1467 -114 -111 225 C ATOM 674 OG SER A 87 30.413 25.237 19.355 1.00 20.09 O ANISOU 674 OG SER A 87 2556 2910 2168 -724 77 681 O ATOM 675 N GLN A 88 31.414 25.421 22.294 1.00 12.66 N ANISOU 675 N GLN A 88 1514 1763 1533 -367 -236 207 N ATOM 676 CA GLN A 88 31.792 26.475 23.229 1.00 13.76 C ANISOU 676 CA GLN A 88 1752 1719 1757 -399 -708 279 C ATOM 677 C GLN A 88 31.729 26.038 24.683 1.00 13.65 C ANISOU 677 C GLN A 88 2389 1148 1650 32 -774 132 C ATOM 678 O GLN A 88 31.340 26.820 25.572 1.00 15.22 O ANISOU 678 O GLN A 88 2731 1284 1767 -214 -599 6 O ATOM 679 CB GLN A 88 31.038 27.777 22.942 1.00 17.04 C ANISOU 679 CB GLN A 88 2747 1546 2181 -418 -745 657 C ATOM 680 CG GLN A 88 31.538 28.464 21.668 1.00 20.91 C ANISOU 680 CG GLN A 88 2627 2239 3079 -337 258 867 C ATOM 681 CD GLN A 88 30.868 29.813 21.471 1.00 22.83 C ANISOU 681 CD GLN A 88 3336 2103 3236 -86 114 87 C ATOM 682 OE1 GLN A 88 29.976 29.917 20.647 1.00 23.44 O ANISOU 682 OE1 GLN A 88 3745 2642 2518 -340 248 259 O ATOM 683 NE2 GLN A 88 31.268 30.825 22.239 1.00 28.05 N ANISOU 683 NE2 GLN A 88 4292 2364 4001 -408 154 -319 N ATOM 684 N GLN A 89 32.114 24.760 24.945 1.00 11.89 N ANISOU 684 N GLN A 89 1622 1191 1706 -125 -525 253 N ATOM 685 CA GLN A 89 32.238 24.322 26.334 1.00 10.26 C ANISOU 685 CA GLN A 89 1184 1042 1673 -65 -295 311 C ATOM 686 C GLN A 89 33.600 24.790 26.871 1.00 9.20 C ANISOU 686 C GLN A 89 1137 949 1410 46 -165 88 C ATOM 687 O GLN A 89 34.610 24.687 26.140 1.00 11.28 O ANISOU 687 O GLN A 89 1269 1497 1518 -214 -85 34 O ATOM 688 CB GLN A 89 32.182 22.797 26.445 1.00 9.95 C ANISOU 688 CB GLN A 89 1133 1054 1591 -36 -224 144 C ATOM 689 CG GLN A 89 30.809 22.186 26.171 1.00 11.08 C ANISOU 689 CG GLN A 89 1203 1206 1799 -115 -381 301 C ATOM 690 CD GLN A 89 30.795 20.679 26.348 1.00 10.97 C ANISOU 690 CD GLN A 89 1216 1226 1725 -136 -392 295 C ATOM 691 OE1 GLN A 89 31.750 20.052 26.811 1.00 13.93 O ANISOU 691 OE1 GLN A 89 1644 1097 2552 0 -886 171 O ATOM 692 NE2 GLN A 89 29.676 20.058 25.986 1.00 11.71 N ANISOU 692 NE2 GLN A 89 1310 1130 2009 -153 -508 95 N ATOM 693 N PRO A 90 33.677 25.213 28.114 1.00 9.44 N ANISOU 693 N PRO A 90 1103 1035 1448 118 -241 87 N ATOM 694 CA PRO A 90 34.973 25.500 28.729 1.00 9.48 C ANISOU 694 CA PRO A 90 1131 988 1483 71 -295 59 C ATOM 695 C PRO A 90 35.763 24.202 28.842 1.00 8.96 C ANISOU 695 C PRO A 90 1010 964 1431 -26 -66 84 C ATOM 696 O PRO A 90 35.207 23.095 28.926 1.00 9.42 O ANISOU 696 O PRO A 90 984 968 1629 -38 -102 69 O ATOM 697 CB PRO A 90 34.592 26.107 30.065 1.00 11.05 C ANISOU 697 CB PRO A 90 1379 1301 1519 184 -284 -41 C ATOM 698 CG PRO A 90 33.274 25.503 30.410 1.00 11.81 C ANISOU 698 CG PRO A 90 1446 1473 1568 94 -213 -33 C ATOM 699 CD PRO A 90 32.571 25.297 29.096 1.00 10.36 C ANISOU 699 CD PRO A 90 1189 1179 1569 13 -196 67 C ATOM 700 N GLY A 91 37.101 24.315 28.872 1.00 10.26 N ANISOU 700 N GLY A 91 1005 1127 1768 -135 -34 119 N ATOM 701 CA GLY A 91 37.977 23.150 28.922 1.00 10.41 C ANISOU 701 CA GLY A 91 935 1317 1703 -86 212 116 C ATOM 702 C GLY A 91 37.666 22.165 30.037 1.00 8.62 C ANISOU 702 C GLY A 91 746 1019 1509 -76 24 -40 C ATOM 703 O GLY A 91 37.706 20.948 29.825 1.00 9.44 O ANISOU 703 O GLY A 91 971 1035 1580 -13 63 -74 O ATOM 704 N TRP A 92 37.299 22.669 31.228 1.00 8.58 N ANISOU 704 N TRP A 92 861 917 1484 -40 9 -76 N ATOM 705 CA TRP A 92 37.031 21.749 32.342 1.00 8.21 C ANISOU 705 CA TRP A 92 754 917 1447 38 -102 -32 C ATOM 706 C TRP A 92 35.854 20.831 32.047 1.00 7.96 C ANISOU 706 C TRP A 92 737 963 1325 -24 -50 108 C ATOM 707 O TRP A 92 35.850 19.675 32.519 1.00 9.95 O ANISOU 707 O TRP A 92 1061 989 1732 -60 -174 149 O ATOM 708 CB TRP A 92 36.808 22.534 33.658 1.00 9.56 C ANISOU 708 CB TRP A 92 1018 1146 1467 191 -196 -151 C ATOM 709 CG TRP A 92 35.600 23.428 33.693 1.00 8.77 C ANISOU 709 CG TRP A 92 966 942 1423 60 -135 -126 C ATOM 710 CD1 TRP A 92 35.558 24.765 33.428 1.00 9.05 C ANISOU 710 CD1 TRP A 92 1040 1032 1368 -20 -99 -61 C ATOM 711 CD2 TRP A 92 34.249 23.044 34.005 1.00 9.47 C ANISOU 711 CD2 TRP A 92 1105 1068 1424 14 76 -150 C ATOM 712 NE1 TRP A 92 34.271 25.256 33.541 1.00 10.15 N ANISOU 712 NE1 TRP A 92 1160 1058 1639 213 -5 -4 N ATOM 713 CE2 TRP A 92 33.450 24.210 33.895 1.00 9.70 C ANISOU 713 CE2 TRP A 92 1141 1199 1348 120 -70 -80 C ATOM 714 CE3 TRP A 92 33.637 21.836 34.346 1.00 11.89 C ANISOU 714 CE3 TRP A 92 1362 1080 2076 90 326 33 C ATOM 715 CZ2 TRP A 92 32.070 24.180 34.108 1.00 11.63 C ANISOU 715 CZ2 TRP A 92 1188 1520 1711 231 8 -280 C ATOM 716 CZ3 TRP A 92 32.273 21.815 34.575 1.00 13.48 C ANISOU 716 CZ3 TRP A 92 1380 1546 2196 -123 293 -231 C ATOM 717 CH2 TRP A 92 31.512 22.980 34.448 1.00 13.33 C ANISOU 717 CH2 TRP A 92 992 1912 2160 16 93 -89 C ATOM 718 N MET A 93 34.851 21.305 31.302 1.00 7.99 N ANISOU 718 N MET A 93 841 887 1309 -39 -125 86 N ATOM 719 CA MET A 93 33.673 20.494 30.994 1.00 8.11 C ANISOU 719 CA MET A 93 814 917 1351 -33 -150 80 C ATOM 720 C MET A 93 33.951 19.511 29.857 1.00 8.12 C ANISOU 720 C MET A 93 807 908 1371 -58 -156 91 C ATOM 721 O MET A 93 33.433 18.380 29.832 1.00 9.07 O ANISOU 721 O MET A 93 1038 925 1484 -128 -90 5 O ATOM 722 CB MET A 93 32.467 21.388 30.675 1.00 8.53 C ANISOU 722 CB MET A 93 933 847 1459 -11 -116 176 C ATOM 723 CG MET A 93 31.185 20.627 30.382 1.00 10.84 C ANISOU 723 CG MET A 93 889 1174 2057 32 -251 55 C ATOM 724 SD MET A 93 29.763 21.698 30.058 1.00 12.17 S ANISOU 724 SD MET A 93 982 1456 2188 201 -320 254 S ATOM 725 CE MET A 93 29.208 22.104 31.693 1.00 18.70 C ANISOU 725 CE MET A 93 2130 2779 2196 672 -316 38 C ATOM 726 N GLN A 94 34.824 19.911 28.902 1.00 8.65 N ANISOU 726 N GLN A 94 1008 1051 1226 -65 -132 35 N ATOM 727 CA GLN A 94 35.202 18.996 27.817 1.00 9.54 C ANISOU 727 CA GLN A 94 1038 1215 1370 -11 -55 -48 C ATOM 728 C GLN A 94 35.860 17.732 28.365 1.00 10.12 C ANISOU 728 C GLN A 94 1265 1177 1404 6 -58 -73 C ATOM 729 O GLN A 94 35.783 16.653 27.746 1.00 13.49 O ANISOU 729 O GLN A 94 2146 1320 1658 108 -207 -228 O ATOM 730 CB GLN A 94 36.194 19.670 26.853 1.00 9.88 C ANISOU 730 CB GLN A 94 1064 1430 1259 45 -69 21 C ATOM 731 CG GLN A 94 35.616 20.849 26.074 1.00 10.55 C ANISOU 731 CG GLN A 94 1144 1505 1360 85 -160 78 C ATOM 732 CD GLN A 94 36.597 21.402 25.060 1.00 13.27 C ANISOU 732 CD GLN A 94 1531 1625 1886 249 299 255 C ATOM 733 OE1 GLN A 94 37.377 20.668 24.442 1.00 16.88 O ANISOU 733 OE1 GLN A 94 2143 1996 2273 498 660 185 O ATOM 734 NE2 GLN A 94 36.581 22.711 24.884 1.00 15.44 N ANISOU 734 NE2 GLN A 94 1825 1706 2336 79 432 489 N ATOM 735 N SER A 95 36.542 17.804 29.516 1.00 8.68 N ANISOU 735 N SER A 95 871 1007 1419 29 27 -36 N ATOM 736 CA SER A 95 37.227 16.693 30.138 1.00 9.70 C ANISOU 736 CA SER A 95 864 1137 1686 81 87 70 C ATOM 737 C SER A 95 36.331 15.718 30.883 1.00 10.50 C ANISOU 737 C SER A 95 1079 1021 1890 14 67 154 C ATOM 738 O SER A 95 36.818 14.654 31.302 1.00 15.08 O ANISOU 738 O SER A 95 1410 1322 2997 154 189 700 O ATOM 739 CB SER A 95 38.311 17.196 31.112 1.00 10.21 C ANISOU 739 CB SER A 95 1058 1344 1477 -51 64 225 C ATOM 740 OG SER A 95 39.226 18.021 30.416 1.00 10.63 O ANISOU 740 OG SER A 95 1173 1465 1402 -193 145 66 O ATOM 741 N LEU A 96 35.073 16.047 31.132 1.00 9.98 N ANISOU 741 N LEU A 96 1038 1106 1648 -58 90 53 N ATOM 742 CA LEU A 96 34.153 15.213 31.883 1.00 9.73 C ANISOU 742 CA LEU A 96 1171 1111 1414 -53 -25 159 C ATOM 743 C LEU A 96 33.329 14.286 30.986 1.00 10.31 C ANISOU 743 C LEU A 96 1260 1066 1593 11 15 10 C ATOM 744 O LEU A 96 33.004 14.596 29.847 1.00 12.17 O ANISOU 744 O LEU A 96 1572 1353 1700 -307 -201 69 O ATOM 745 CB LEU A 96 33.216 16.077 32.743 1.00 10.99 C ANISOU 745 CB LEU A 96 1185 1280 1712 -115 40 -26 C ATOM 746 CG LEU A 96 33.852 16.999 33.780 1.00 11.44 C ANISOU 746 CG LEU A 96 1145 1351 1850 -325 54 -5 C ATOM 747 CD1 LEU A 96 32.797 17.849 34.484 1.00 13.70 C ANISOU 747 CD1 LEU A 96 1580 1540 2086 -43 89 -214 C ATOM 748 CD2 LEU A 96 34.699 16.237 34.784 1.00 17.30 C ANISOU 748 CD2 LEU A 96 2098 2114 2363 202 -595 -102 C ATOM 749 N SER A 97 32.933 13.148 31.575 1.00 11.28 N ANISOU 749 N SER A 97 1361 1124 1800 -198 -90 79 N ATOM 750 CA SER A 97 32.088 12.166 30.910 1.00 11.83 C ANISOU 750 CA SER A 97 1379 1134 1984 -205 -22 -55 C ATOM 751 C SER A 97 31.122 11.542 31.925 1.00 11.50 C ANISOU 751 C SER A 97 1596 939 1834 -94 5 -5 C ATOM 752 O SER A 97 31.268 11.686 33.146 1.00 12.88 O ANISOU 752 O SER A 97 1681 1316 1898 -166 -193 91 O ATOM 753 CB SER A 97 32.897 11.043 30.245 1.00 16.07 C ANISOU 753 CB SER A 97 1865 1653 2587 179 23 -331 C ATOM 754 OG SER A 97 33.692 10.373 31.191 1.00 21.11 O ANISOU 754 OG SER A 97 2558 2190 3272 553 -318 -175 O ATOM 755 N GLY A 98 30.118 10.823 31.431 1.00 12.65 N ANISOU 755 N GLY A 98 1525 1147 2133 -195 63 -10 N ATOM 756 CA GLY A 98 29.248 10.026 32.272 1.00 12.88 C ANISOU 756 CA GLY A 98 1505 1177 2214 -250 77 28 C ATOM 757 C GLY A 98 28.534 10.761 33.384 1.00 12.23 C ANISOU 757 C GLY A 98 1625 1048 1974 -161 -20 167 C ATOM 758 O GLY A 98 28.049 11.876 33.189 1.00 12.50 O ANISOU 758 O GLY A 98 1690 1095 1965 -30 -21 148 O ATOM 759 N SER A 99 28.445 10.124 34.565 1.00 13.66 N ANISOU 759 N SER A 99 1999 1025 2165 -76 -24 402 N ATOM 760 CA SER A 99 27.728 10.708 35.695 1.00 14.56 C ANISOU 760 CA SER A 99 2092 1416 2024 -103 -1 389 C ATOM 761 C SER A 99 28.323 12.019 36.190 1.00 12.65 C ANISOU 761 C SER A 99 1897 1413 1498 -40 -6 360 C ATOM 762 O SER A 99 27.579 12.882 36.648 1.00 13.90 O ANISOU 762 O SER A 99 1949 1555 1778 7 44 340 O ATOM 763 CB SER A 99 27.599 9.694 36.848 1.00 19.65 C ANISOU 763 CB SER A 99 3018 1830 2620 -343 172 818 C ATOM 764 OG ASER A 99 28.877 9.304 37.304 0.50 22.11 O ANISOU 764 OG ASER A 99 3644 1986 2771 4 -373 1178 O ATOM 765 OG BSER A 99 26.846 8.582 36.387 0.50 23.73 O ANISOU 765 OG BSER A 99 3417 2564 3036 -804 337 323 O ATOM 766 N ALA A 100 29.642 12.185 36.132 1.00 12.92 N ANISOU 766 N ALA A 100 1823 1201 1885 151 -177 321 N ATOM 767 CA ALA A 100 30.294 13.429 36.525 1.00 12.19 C ANISOU 767 CA ALA A 100 1682 1458 1490 129 -449 183 C ATOM 768 C ALA A 100 29.866 14.590 35.608 1.00 10.69 C ANISOU 768 C ALA A 100 1351 1421 1291 148 -277 81 C ATOM 769 O ALA A 100 29.558 15.684 36.078 1.00 11.35 O ANISOU 769 O ALA A 100 1584 1451 1279 120 -276 16 O ATOM 770 CB ALA A 100 31.813 13.307 36.528 1.00 15.22 C ANISOU 770 CB ALA A 100 1707 1862 2213 213 -497 270 C ATOM 771 N LEU A 101 29.801 14.312 34.316 1.00 9.31 N ANISOU 771 N LEU A 101 1228 1050 1259 109 -132 81 N ATOM 772 CA LEU A 101 29.306 15.309 33.358 1.00 9.21 C ANISOU 772 CA LEU A 101 1230 970 1298 85 -140 78 C ATOM 773 C LEU A 101 27.842 15.643 33.601 1.00 8.74 C ANISOU 773 C LEU A 101 1218 1028 1076 -7 -168 58 C ATOM 774 O LEU A 101 27.440 16.811 33.542 1.00 9.59 O ANISOU 774 O LEU A 101 1250 1098 1296 57 -49 15 O ATOM 775 CB LEU A 101 29.534 14.818 31.927 1.00 9.32 C ANISOU 775 CB LEU A 101 1070 1082 1388 14 33 65 C ATOM 776 CG LEU A 101 29.005 15.734 30.813 1.00 9.43 C ANISOU 776 CG LEU A 101 1254 1039 1289 6 -104 -37 C ATOM 777 CD1 LEU A 101 29.662 17.110 30.792 1.00 11.14 C ANISOU 777 CD1 LEU A 101 1711 1164 1359 -168 -211 137 C ATOM 778 CD2 LEU A 101 29.178 15.051 29.460 1.00 11.61 C ANISOU 778 CD2 LEU A 101 1715 1413 1285 -111 69 -20 C ATOM 779 N ARG A 102 27.016 14.621 33.855 1.00 9.36 N ANISOU 779 N ARG A 102 1217 1058 1281 -10 -81 175 N ATOM 780 CA ARG A 102 25.594 14.858 34.124 1.00 10.06 C ANISOU 780 CA ARG A 102 1158 1291 1374 -94 -153 110 C ATOM 781 C ARG A 102 25.375 15.795 35.316 1.00 9.19 C ANISOU 781 C ARG A 102 1101 1195 1195 -145 -33 274 C ATOM 782 O ARG A 102 24.576 16.745 35.222 1.00 10.11 O ANISOU 782 O ARG A 102 1140 1462 1238 -12 -95 220 O ATOM 783 CB ARG A 102 24.894 13.517 34.354 1.00 13.40 C ANISOU 783 CB ARG A 102 1597 1579 1917 -411 148 3 C ATOM 784 CG AARG A 102 23.410 13.464 34.518 0.50 14.38 C ANISOU 784 CG AARG A 102 1729 1667 2068 -295 831 -202 C ATOM 785 CD AARG A 102 22.643 13.835 33.286 0.50 19.50 C ANISOU 785 CD AARG A 102 2207 1985 3217 246 126 278 C ATOM 786 NE AARG A 102 22.828 13.088 32.065 0.50 20.77 N ANISOU 786 NE AARG A 102 2801 2599 2491 28 -677 406 N ATOM 787 CZ AARG A 102 22.174 12.003 31.660 0.50 18.18 C ANISOU 787 CZ AARG A 102 2189 2316 2404 214 -622 725 C ATOM 788 NH1AARG A 102 21.245 11.441 32.420 0.50 18.46 N ANISOU 788 NH1AARG A 102 1493 3237 2284 408 -544 381 N ATOM 789 NH2AARG A 102 22.375 11.394 30.500 0.50 13.96 N ANISOU 789 NH2AARG A 102 633 2020 2650 422 343 958 N ATOM 790 CG BARG A 102 24.418 12.843 33.087 0.50 17.03 C ANISOU 790 CG BARG A 102 2305 1796 2368 -263 -113 -386 C ATOM 791 CD BARG A 102 23.180 13.529 32.492 0.50 18.92 C ANISOU 791 CD BARG A 102 2556 2279 2354 -295 -253 220 C ATOM 792 NE BARG A 102 22.848 12.765 31.285 0.50 23.26 N ANISOU 792 NE BARG A 102 3107 3239 2490 -895 -392 56 N ATOM 793 CZ BARG A 102 21.839 11.895 31.279 0.50 21.78 C ANISOU 793 CZ BARG A 102 2214 3233 2829 -415 -492 119 C ATOM 794 NH1BARG A 102 21.056 11.685 32.322 0.50 22.48 N ANISOU 794 NH1BARG A 102 2730 2916 2895 -510 -350 421 N ATOM 795 NH2BARG A 102 21.658 11.252 30.134 0.50 23.05 N ANISOU 795 NH2BARG A 102 2944 3395 2418 -373 -228 389 N ATOM 796 N GLN A 103 26.090 15.557 36.430 1.00 8.70 N ANISOU 796 N GLN A 103 1070 1097 1136 -56 17 187 N ATOM 797 CA GLN A 103 25.950 16.446 37.582 1.00 9.48 C ANISOU 797 CA GLN A 103 1414 1016 1172 30 -73 225 C ATOM 798 C GLN A 103 26.431 17.858 37.262 1.00 7.93 C ANISOU 798 C GLN A 103 1113 1087 814 82 -106 174 C ATOM 799 O GLN A 103 25.789 18.827 37.696 1.00 9.23 O ANISOU 799 O GLN A 103 1253 1196 1059 147 50 189 O ATOM 800 CB GLN A 103 26.662 15.892 38.819 1.00 10.60 C ANISOU 800 CB GLN A 103 1543 1293 1192 15 -139 274 C ATOM 801 CG GLN A 103 26.350 16.704 40.080 1.00 12.92 C ANISOU 801 CG GLN A 103 2327 1464 1117 23 -274 212 C ATOM 802 CD GLN A 103 24.904 16.591 40.509 1.00 15.42 C ANISOU 802 CD GLN A 103 2676 1573 1611 -161 339 225 C ATOM 803 OE1 GLN A 103 24.387 15.482 40.681 1.00 21.22 O ANISOU 803 OE1 GLN A 103 3801 1944 2317 -742 1027 121 O ATOM 804 NE2 GLN A 103 24.217 17.705 40.709 1.00 15.80 N ANISOU 804 NE2 GLN A 103 2548 1787 1670 44 656 515 N ATOM 805 N ALA A 104 27.525 18.006 36.506 1.00 8.13 N ANISOU 805 N ALA A 104 1016 1028 1045 57 -84 121 N ATOM 806 CA ALA A 104 27.995 19.346 36.141 1.00 8.45 C ANISOU 806 CA ALA A 104 1056 1003 1152 -88 -174 91 C ATOM 807 C ALA A 104 26.993 20.053 35.241 1.00 7.56 C ANISOU 807 C ALA A 104 810 1053 1010 -134 28 106 C ATOM 808 O ALA A 104 26.816 21.288 35.351 1.00 8.85 O ANISOU 808 O ALA A 104 1172 1037 1155 -86 -46 69 O ATOM 809 CB ALA A 104 29.359 19.257 35.445 1.00 10.45 C ANISOU 809 CB ALA A 104 1044 1191 1735 -78 -76 80 C ATOM 810 N MET A 105 26.330 19.336 34.311 1.00 8.03 N ANISOU 810 N MET A 105 1061 1038 952 -78 -201 169 N ATOM 811 CA MET A 105 25.294 19.918 33.450 1.00 7.90 C ANISOU 811 CA MET A 105 1049 1165 789 -11 -87 242 C ATOM 812 C MET A 105 24.138 20.462 34.292 1.00 7.72 C ANISOU 812 C MET A 105 1074 906 955 -63 -70 203 C ATOM 813 O MET A 105 23.656 21.586 34.090 1.00 8.69 O ANISOU 813 O MET A 105 1217 995 1091 -12 49 269 O ATOM 814 CB MET A 105 24.792 18.878 32.443 1.00 8.97 C ANISOU 814 CB MET A 105 1196 1412 799 54 -11 26 C ATOM 815 CG MET A 105 23.731 19.380 31.480 1.00 11.64 C ANISOU 815 CG MET A 105 1404 1866 1153 -115 -368 115 C ATOM 816 SD MET A 105 22.898 18.126 30.466 1.00 12.64 S ANISOU 816 SD MET A 105 1457 2107 1240 -156 -267 -173 S ATOM 817 CE MET A 105 21.785 17.412 31.674 1.00 14.87 C ANISOU 817 CE MET A 105 1540 2032 2076 -284 -173 219 C ATOM 818 N ILE A 106 23.661 19.649 35.243 1.00 7.84 N ANISOU 818 N ILE A 106 942 1146 889 48 3 244 N ATOM 819 CA ILE A 106 22.576 20.018 36.148 1.00 7.81 C ANISOU 819 CA ILE A 106 1012 1112 844 75 -28 211 C ATOM 820 C ILE A 106 22.940 21.231 36.988 1.00 7.67 C ANISOU 820 C ILE A 106 913 1073 928 -50 6 241 C ATOM 821 O ILE A 106 22.167 22.206 37.108 1.00 9.15 O ANISOU 821 O ILE A 106 1072 1220 1183 36 -27 215 O ATOM 822 CB ILE A 106 22.145 18.803 37.010 1.00 9.13 C ANISOU 822 CB ILE A 106 994 1308 1168 -178 54 224 C ATOM 823 CG1 ILE A 106 21.464 17.743 36.130 1.00 11.21 C ANISOU 823 CG1 ILE A 106 1350 1385 1526 -300 1 108 C ATOM 824 CG2 ILE A 106 21.274 19.210 38.187 1.00 10.32 C ANISOU 824 CG2 ILE A 106 1310 1463 1149 -112 144 290 C ATOM 825 CD1 ILE A 106 21.294 16.373 36.767 1.00 14.74 C ANISOU 825 CD1 ILE A 106 2124 1381 2095 -358 95 181 C ATOM 826 N ASP A 107 24.140 21.218 37.596 1.00 7.57 N ANISOU 826 N ASP A 107 1003 1061 812 0 -50 168 N ATOM 827 CA ASP A 107 24.610 22.350 38.408 1.00 7.71 C ANISOU 827 CA ASP A 107 1096 1020 814 38 -84 164 C ATOM 828 C ASP A 107 24.694 23.624 37.567 1.00 7.62 C ANISOU 828 C ASP A 107 942 1035 919 65 -57 174 C ATOM 829 O ASP A 107 24.405 24.728 38.058 1.00 8.53 O ANISOU 829 O ASP A 107 1306 1081 853 47 14 125 O ATOM 830 CB ASP A 107 25.946 22.048 39.087 1.00 8.17 C ANISOU 830 CB ASP A 107 1190 1071 842 -1 -193 145 C ATOM 831 CG ASP A 107 25.933 20.997 40.188 1.00 9.68 C ANISOU 831 CG ASP A 107 1463 1256 957 -25 -197 220 C ATOM 832 OD1 ASP A 107 24.856 20.603 40.671 1.00 11.82 O ANISOU 832 OD1 ASP A 107 1810 1620 1061 -93 88 440 O ATOM 833 OD2 ASP A 107 27.043 20.549 40.563 1.00 13.33 O ANISOU 833 OD2 ASP A 107 1729 1742 1593 104 -452 543 O ATOM 834 N HIS A 108 25.178 23.517 36.320 1.00 7.47 N ANISOU 834 N HIS A 108 1061 980 797 -56 -58 231 N ATOM 835 CA HIS A 108 25.267 24.693 35.448 1.00 7.01 C ANISOU 835 CA HIS A 108 922 876 864 -129 -54 161 C ATOM 836 C HIS A 108 23.887 25.306 35.165 1.00 7.07 C ANISOU 836 C HIS A 108 1047 875 764 -20 -121 150 C ATOM 837 O HIS A 108 23.709 26.530 35.262 1.00 8.55 O ANISOU 837 O HIS A 108 1247 959 1044 -51 -12 113 O ATOM 838 CB HIS A 108 25.979 24.328 34.123 1.00 7.39 C ANISOU 838 CB HIS A 108 955 1006 846 -11 -25 213 C ATOM 839 CG HIS A 108 26.122 25.529 33.226 1.00 7.00 C ANISOU 839 CG HIS A 108 917 954 788 -83 -26 152 C ATOM 840 ND1 HIS A 108 27.108 26.462 33.461 1.00 7.93 N ANISOU 840 ND1 HIS A 108 1042 1007 964 -195 -2 178 N ATOM 841 CD2 HIS A 108 25.384 25.992 32.190 1.00 7.98 C ANISOU 841 CD2 HIS A 108 1016 1119 898 -76 -31 250 C ATOM 842 CE1 HIS A 108 26.979 27.462 32.585 1.00 8.20 C ANISOU 842 CE1 HIS A 108 1188 1015 912 -159 35 151 C ATOM 843 NE2 HIS A 108 25.939 27.188 31.807 1.00 7.81 N ANISOU 843 NE2 HIS A 108 1058 1045 864 -111 -42 173 N ATOM 844 N ILE A 109 22.908 24.475 34.790 1.00 7.33 N ANISOU 844 N ILE A 109 977 918 889 19 -131 67 N ATOM 845 CA ILE A 109 21.539 24.940 34.549 1.00 7.67 C ANISOU 845 CA ILE A 109 1015 907 992 54 -2 214 C ATOM 846 C ILE A 109 20.991 25.653 35.792 1.00 7.88 C ANISOU 846 C ILE A 109 1076 979 937 50 -8 161 C ATOM 847 O ILE A 109 20.418 26.751 35.714 1.00 9.23 O ANISOU 847 O ILE A 109 1243 1030 1235 98 -63 103 O ATOM 848 CB ILE A 109 20.613 23.775 34.123 1.00 8.04 C ANISOU 848 CB ILE A 109 974 1036 1046 28 -98 161 C ATOM 849 CG1 ILE A 109 21.037 23.226 32.756 1.00 9.22 C ANISOU 849 CG1 ILE A 109 1190 1257 1055 65 -164 98 C ATOM 850 CG2 ILE A 109 19.134 24.194 34.132 1.00 9.84 C ANISOU 850 CG2 ILE A 109 1086 1282 1373 -1 -188 130 C ATOM 851 CD1 ILE A 109 20.388 21.903 32.365 1.00 11.78 C ANISOU 851 CD1 ILE A 109 1374 1610 1494 -121 -197 -271 C ATOM 852 N ASN A 110 21.113 24.999 36.956 1.00 8.06 N ANISOU 852 N ASN A 110 1139 1061 860 118 107 112 N ATOM 853 CA ASN A 110 20.574 25.571 38.193 1.00 9.47 C ANISOU 853 CA ASN A 110 1329 1319 949 167 234 133 C ATOM 854 C ASN A 110 21.223 26.902 38.553 1.00 9.96 C ANISOU 854 C ASN A 110 1359 1277 1148 195 65 137 C ATOM 855 O ASN A 110 20.556 27.847 38.991 1.00 11.70 O ANISOU 855 O ASN A 110 1573 1421 1450 165 219 -60 O ATOM 856 CB ASN A 110 20.676 24.563 39.354 1.00 9.98 C ANISOU 856 CB ASN A 110 1334 1516 942 23 146 219 C ATOM 857 CG ASN A 110 19.663 23.436 39.293 1.00 10.81 C ANISOU 857 CG ASN A 110 1227 1616 1263 8 50 200 C ATOM 858 OD1 ASN A 110 19.888 22.263 39.675 1.00 13.61 O ANISOU 858 OD1 ASN A 110 1785 1648 1737 -30 87 256 O ATOM 859 ND2 ASN A 110 18.493 23.765 38.840 1.00 14.88 N ANISOU 859 ND2 ASN A 110 1343 1667 2645 -333 -358 809 N ATOM 860 N GLY A 111 22.547 27.005 38.372 1.00 9.39 N ANISOU 860 N GLY A 111 1365 1122 1079 66 -41 97 N ATOM 861 CA GLY A 111 23.253 28.244 38.719 1.00 10.14 C ANISOU 861 CA GLY A 111 1708 1200 945 4 -119 18 C ATOM 862 C GLY A 111 22.896 29.430 37.840 1.00 9.79 C ANISOU 862 C GLY A 111 1545 1134 1042 -1 -99 29 C ATOM 863 O GLY A 111 22.701 30.561 38.327 1.00 11.88 O ANISOU 863 O GLY A 111 2098 1363 1052 43 -186 -118 O ATOM 864 N VAL A 112 22.834 29.206 36.528 1.00 8.58 N ANISOU 864 N VAL A 112 1220 1049 992 64 -88 41 N ATOM 865 CA VAL A 112 22.491 30.305 35.596 1.00 8.77 C ANISOU 865 CA VAL A 112 1296 1082 955 34 -5 67 C ATOM 866 C VAL A 112 21.036 30.708 35.757 1.00 8.78 C ANISOU 866 C VAL A 112 1275 967 1095 4 -27 1 C ATOM 867 O VAL A 112 20.721 31.913 35.818 1.00 10.32 O ANISOU 867 O VAL A 112 1583 1024 1315 83 -33 -30 O ATOM 868 CB VAL A 112 22.862 29.916 34.157 1.00 8.91 C ANISOU 868 CB VAL A 112 1361 1008 1018 -25 98 16 C ATOM 869 CG1 VAL A 112 22.371 30.971 33.166 1.00 11.47 C ANISOU 869 CG1 VAL A 112 1823 1441 1096 166 -45 77 C ATOM 870 CG2 VAL A 112 24.352 29.682 33.977 1.00 10.67 C ANISOU 870 CG2 VAL A 112 1412 1309 1333 40 166 57 C ATOM 871 N MET A 113 20.116 29.726 35.801 1.00 8.77 N ANISOU 871 N MET A 113 1107 967 1258 43 -35 28 N ATOM 872 CA MET A 113 18.693 30.086 35.902 1.00 9.82 C ANISOU 872 CA MET A 113 1246 1060 1426 139 -17 -122 C ATOM 873 C MET A 113 18.354 30.783 37.218 1.00 10.91 C ANISOU 873 C MET A 113 1472 1348 1325 254 38 -54 C ATOM 874 O MET A 113 17.495 31.673 37.254 1.00 13.25 O ANISOU 874 O MET A 113 1789 1644 1602 530 -26 -255 O ATOM 875 CB MET A 113 17.780 28.884 35.619 1.00 9.26 C ANISOU 875 CB MET A 113 1151 1173 1196 76 5 -18 C ATOM 876 CG MET A 113 17.863 28.402 34.168 1.00 11.03 C ANISOU 876 CG MET A 113 1663 1286 1239 -128 120 -170 C ATOM 877 SD MET A 113 16.693 27.090 33.784 1.00 10.30 S ANISOU 877 SD MET A 113 1205 1279 1431 -44 7 -34 S ATOM 878 CE MET A 113 15.160 28.018 33.601 1.00 13.87 C ANISOU 878 CE MET A 113 1526 1570 2175 211 -323 107 C ATOM 879 N ALA A 114 19.030 30.440 38.325 1.00 10.76 N ANISOU 879 N ALA A 114 1652 1214 1223 337 89 -65 N ATOM 880 CA ALA A 114 18.792 31.100 39.606 1.00 12.08 C ANISOU 880 CA ALA A 114 1706 1715 1170 189 102 -93 C ATOM 881 C ALA A 114 19.117 32.585 39.513 1.00 11.39 C ANISOU 881 C ALA A 114 1564 1702 1061 217 148 -193 C ATOM 882 O ALA A 114 18.392 33.413 40.089 1.00 13.83 O ANISOU 882 O ALA A 114 2069 1684 1500 244 378 -312 O ATOM 883 CB ALA A 114 19.604 30.437 40.720 1.00 14.55 C ANISOU 883 CB ALA A 114 2376 1985 1167 533 -7 -108 C ATOM 884 N HIS A 115 20.172 32.958 38.811 1.00 10.95 N ANISOU 884 N HIS A 115 1533 1437 1191 21 24 -161 N ATOM 885 CA HIS A 115 20.559 34.362 38.702 1.00 11.50 C ANISOU 885 CA HIS A 115 1637 1426 1305 1 -102 -277 C ATOM 886 C HIS A 115 19.513 35.181 37.962 1.00 11.35 C ANISOU 886 C HIS A 115 1441 1446 1426 -82 -88 -177 C ATOM 887 O HIS A 115 19.354 36.389 38.243 1.00 14.64 O ANISOU 887 O HIS A 115 2015 1698 1849 306 -283 -582 O ATOM 888 CB HIS A 115 21.920 34.443 38.003 1.00 12.75 C ANISOU 888 CB HIS A 115 1592 1654 1598 -25 -98 -307 C ATOM 889 CG HIS A 115 22.516 35.812 37.953 1.00 12.60 C ANISOU 889 CG HIS A 115 1534 1579 1675 78 -155 -98 C ATOM 890 ND1 HIS A 115 23.166 36.372 39.040 1.00 15.85 N ANISOU 890 ND1 HIS A 115 2259 1914 1849 -214 -365 -162 N ATOM 891 CD2 HIS A 115 22.611 36.740 36.966 1.00 15.33 C ANISOU 891 CD2 HIS A 115 2099 2015 1711 205 -143 95 C ATOM 892 CE1 HIS A 115 23.614 37.574 38.734 1.00 17.57 C ANISOU 892 CE1 HIS A 115 2658 1784 2235 -187 -111 -296 C ATOM 893 NE2 HIS A 115 23.288 37.819 37.480 1.00 16.37 N ANISOU 893 NE2 HIS A 115 2173 1761 2287 -24 280 253 N ATOM 894 N TYR A 116 18.794 34.575 37.020 1.00 10.84 N ANISOU 894 N TYR A 116 1466 1548 1106 -44 -69 0 N ATOM 895 CA TYR A 116 17.806 35.236 36.186 1.00 11.65 C ANISOU 895 CA TYR A 116 1501 1722 1205 45 -66 95 C ATOM 896 C TYR A 116 16.365 34.815 36.462 1.00 10.95 C ANISOU 896 C TYR A 116 1544 1407 1211 94 71 84 C ATOM 897 O TYR A 116 15.480 35.040 35.624 1.00 12.09 O ANISOU 897 O TYR A 116 1529 1878 1185 102 145 154 O ATOM 898 CB TYR A 116 18.148 34.983 34.701 1.00 11.86 C ANISOU 898 CB TYR A 116 1515 1814 1177 -157 -88 21 C ATOM 899 CG TYR A 116 19.419 35.684 34.264 1.00 11.09 C ANISOU 899 CG TYR A 116 1500 1610 1104 -49 -70 75 C ATOM 900 CD1 TYR A 116 19.506 37.071 34.193 1.00 12.47 C ANISOU 900 CD1 TYR A 116 1497 1650 1592 92 118 166 C ATOM 901 CD2 TYR A 116 20.555 34.955 33.921 1.00 11.85 C ANISOU 901 CD2 TYR A 116 1682 1584 1238 -34 47 -67 C ATOM 902 CE1 TYR A 116 20.682 37.706 33.815 1.00 11.83 C ANISOU 902 CE1 TYR A 116 1746 1367 1383 -44 104 177 C ATOM 903 CE2 TYR A 116 21.721 35.570 33.534 1.00 13.18 C ANISOU 903 CE2 TYR A 116 1558 1685 1765 101 338 -312 C ATOM 904 CZ TYR A 116 21.786 36.945 33.485 1.00 12.65 C ANISOU 904 CZ TYR A 116 1669 1741 1397 -123 228 -159 C ATOM 905 OH TYR A 116 22.977 37.546 33.124 1.00 16.57 O ANISOU 905 OH TYR A 116 1806 2317 2174 -426 343 -232 O ATOM 906 N LYS A 117 16.087 34.221 37.626 1.00 11.62 N ANISOU 906 N LYS A 117 1607 1577 1231 94 196 118 N ATOM 907 CA LYS A 117 14.746 33.694 37.911 1.00 11.60 C ANISOU 907 CA LYS A 117 1582 1607 1218 130 187 193 C ATOM 908 C LYS A 117 13.684 34.769 37.816 1.00 11.16 C ANISOU 908 C LYS A 117 1580 1471 1190 48 161 13 C ATOM 909 O LYS A 117 13.775 35.816 38.451 1.00 14.82 O ANISOU 909 O LYS A 117 2461 1641 1529 296 52 -263 O ATOM 910 CB LYS A 117 14.721 32.995 39.287 1.00 13.58 C ANISOU 910 CB LYS A 117 2072 1830 1259 110 251 220 C ATOM 911 CG LYS A 117 13.426 32.263 39.611 1.00 16.58 C ANISOU 911 CG LYS A 117 2183 2752 1363 -161 408 175 C ATOM 912 CD LYS A 117 13.480 31.566 40.965 1.00 18.94 C ANISOU 912 CD LYS A 117 2837 2436 1924 125 -32 512 C ATOM 913 CE LYS A 117 12.254 30.686 41.161 1.00 25.18 C ANISOU 913 CE LYS A 117 3119 3544 2902 -441 424 47 C ATOM 914 NZ LYS A 117 12.244 30.036 42.500 1.00 33.41 N ANISOU 914 NZ LYS A 117 4929 4622 3145 -258 387 503 N ATOM 915 N GLY A 118 12.671 34.511 37.004 1.00 11.33 N ANISOU 915 N GLY A 118 1498 1580 1227 186 166 2 N ATOM 916 CA GLY A 118 11.569 35.424 36.758 1.00 12.78 C ANISOU 916 CA GLY A 118 1555 1702 1600 263 171 112 C ATOM 917 C GLY A 118 11.876 36.585 35.833 1.00 13.61 C ANISOU 917 C GLY A 118 1857 1717 1598 317 300 126 C ATOM 918 O GLY A 118 11.003 37.442 35.591 1.00 18.86 O ANISOU 918 O GLY A 118 2288 2347 2531 768 186 357 O ATOM 919 N LYS A 119 13.065 36.657 35.238 1.00 11.94 N ANISOU 919 N LYS A 119 1899 1435 1204 222 265 21 N ATOM 920 CA LYS A 119 13.516 37.784 34.451 1.00 13.38 C ANISOU 920 CA LYS A 119 2233 1350 1499 -19 56 33 C ATOM 921 C LYS A 119 13.663 37.512 32.964 1.00 12.80 C ANISOU 921 C LYS A 119 2145 1294 1425 48 182 94 C ATOM 922 O LYS A 119 13.790 38.463 32.172 1.00 14.64 O ANISOU 922 O LYS A 119 2610 1402 1549 80 -70 227 O ATOM 923 CB LYS A 119 14.876 38.292 34.988 1.00 15.23 C ANISOU 923 CB LYS A 119 2506 1616 1663 -291 -72 -8 C ATOM 924 CG LYS A 119 14.826 38.812 36.413 1.00 20.71 C ANISOU 924 CG LYS A 119 3453 2699 1717 -455 52 -256 C ATOM 925 CD LYS A 119 16.187 39.254 36.935 1.00 27.80 C ANISOU 925 CD LYS A 119 3752 3472 3339 -470 -622 -406 C ATOM 926 CE LYS A 119 16.040 39.800 38.355 1.00 33.99 C ANISOU 926 CE LYS A 119 5125 4481 3310 -180 -26 -344 C ATOM 927 NZ LYS A 119 17.363 40.144 38.939 1.00 42.29 N ANISOU 927 NZ LYS A 119 5005 5998 5065 -205 -384 -143 N ATOM 928 N ILE A 120 13.686 36.266 32.548 1.00 12.96 N ANISOU 928 N ILE A 120 2377 1306 1241 261 264 77 N ATOM 929 CA ILE A 120 13.934 35.848 31.151 1.00 11.54 C ANISOU 929 CA ILE A 120 1911 1190 1284 206 285 3 C ATOM 930 C ILE A 120 12.712 35.098 30.660 1.00 11.45 C ANISOU 930 C ILE A 120 1822 1071 1458 165 359 118 C ATOM 931 O ILE A 120 12.264 34.099 31.255 1.00 15.92 O ANISOU 931 O ILE A 120 2538 1570 1942 -181 607 403 O ATOM 932 CB ILE A 120 15.290 35.103 31.052 1.00 14.03 C ANISOU 932 CB ILE A 120 2238 1731 1362 583 295 -177 C ATOM 933 CG1 ILE A 120 16.448 36.124 31.153 1.00 18.48 C ANISOU 933 CG1 ILE A 120 2243 2828 1951 270 -476 -593 C ATOM 934 CG2 ILE A 120 15.351 34.309 29.749 1.00 13.89 C ANISOU 934 CG2 ILE A 120 2018 2040 1219 671 53 -187 C ATOM 935 CD1 ILE A 120 17.854 35.691 30.900 1.00 21.89 C ANISOU 935 CD1 ILE A 120 2443 3375 2497 200 396 182 C ATOM 936 N VAL A 121 12.075 35.528 29.565 1.00 10.67 N ANISOU 936 N VAL A 121 1514 1114 1427 95 245 -94 N ATOM 937 CA VAL A 121 10.799 34.979 29.118 1.00 11.75 C ANISOU 937 CA VAL A 121 1534 1261 1668 76 211 -124 C ATOM 938 C VAL A 121 10.898 33.631 28.426 1.00 9.75 C ANISOU 938 C VAL A 121 1120 1050 1534 86 365 23 C ATOM 939 O VAL A 121 9.939 32.836 28.524 1.00 11.15 O ANISOU 939 O VAL A 121 1187 1224 1825 56 481 2 O ATOM 940 CB VAL A 121 9.995 36.013 28.301 1.00 15.51 C ANISOU 940 CB VAL A 121 1744 1441 2708 508 227 72 C ATOM 941 CG1AVAL A 121 10.659 36.335 26.977 0.50 13.11 C ANISOU 941 CG1AVAL A 121 1237 1340 2406 175 -420 358 C ATOM 942 CG2AVAL A 121 8.565 35.561 28.056 0.50 20.22 C ANISOU 942 CG2AVAL A 121 2076 2565 3040 95 -175 -24 C ATOM 943 CG1BVAL A 121 9.532 37.152 29.213 0.50 18.93 C ANISOU 943 CG1BVAL A 121 2340 1672 3182 900 179 -134 C ATOM 944 CG2BVAL A 121 10.804 36.560 27.144 0.50 16.41 C ANISOU 944 CG2BVAL A 121 2456 1398 2381 312 131 81 C ATOM 945 N GLN A 122 11.966 33.351 27.697 1.00 8.93 N ANISOU 945 N GLN A 122 1122 938 1333 160 305 92 N ATOM 946 CA GLN A 122 12.198 32.101 26.997 1.00 8.48 C ANISOU 946 CA GLN A 122 1026 881 1315 53 169 64 C ATOM 947 C GLN A 122 13.654 31.700 27.212 1.00 7.65 C ANISOU 947 C GLN A 122 992 902 1014 -70 62 27 C ATOM 948 O GLN A 122 14.535 32.585 27.158 1.00 9.74 O ANISOU 948 O GLN A 122 1046 854 1802 -36 209 53 O ATOM 949 CB GLN A 122 11.999 32.210 25.479 1.00 9.71 C ANISOU 949 CB GLN A 122 1044 1325 1319 -9 136 104 C ATOM 950 CG GLN A 122 10.613 32.512 24.935 1.00 10.57 C ANISOU 950 CG GLN A 122 1152 1509 1354 35 38 229 C ATOM 951 CD GLN A 122 10.660 32.813 23.456 1.00 10.26 C ANISOU 951 CD GLN A 122 1204 1395 1298 85 19 97 C ATOM 952 OE1 GLN A 122 11.367 32.155 22.685 1.00 10.79 O ANISOU 952 OE1 GLN A 122 1383 1455 1263 208 129 222 O ATOM 953 NE2 GLN A 122 9.931 33.834 23.003 1.00 12.39 N ANISOU 953 NE2 GLN A 122 1539 1660 1508 396 179 175 N ATOM 954 N TRP A 123 13.929 30.411 27.355 1.00 7.37 N ANISOU 954 N TRP A 123 840 801 1159 -35 205 -13 N ATOM 955 CA TRP A 123 15.282 29.878 27.351 1.00 7.17 C ANISOU 955 CA TRP A 123 867 929 928 -28 13 22 C ATOM 956 C TRP A 123 15.460 28.856 26.222 1.00 6.85 C ANISOU 956 C TRP A 123 794 828 982 -11 18 -26 C ATOM 957 O TRP A 123 14.628 27.944 26.087 1.00 8.97 O ANISOU 957 O TRP A 123 851 1008 1551 -150 97 -166 O ATOM 958 CB TRP A 123 15.637 29.143 28.669 1.00 8.15 C ANISOU 958 CB TRP A 123 1069 967 1061 -11 -82 147 C ATOM 959 CG TRP A 123 16.117 30.024 29.778 1.00 8.97 C ANISOU 959 CG TRP A 123 1403 1007 997 105 -101 107 C ATOM 960 CD1 TRP A 123 15.420 30.516 30.850 1.00 11.41 C ANISOU 960 CD1 TRP A 123 1581 1517 1235 86 78 64 C ATOM 961 CD2 TRP A 123 17.454 30.544 29.946 1.00 9.72 C ANISOU 961 CD2 TRP A 123 1628 896 1168 -71 -306 114 C ATOM 962 NE1 TRP A 123 16.239 31.303 31.641 1.00 12.54 N ANISOU 962 NE1 TRP A 123 2248 1432 1086 235 -76 -137 N ATOM 963 CE2 TRP A 123 17.487 31.351 31.093 1.00 12.00 C ANISOU 963 CE2 TRP A 123 1933 1236 1392 -15 -422 -30 C ATOM 964 CE3 TRP A 123 18.633 30.410 29.195 1.00 10.86 C ANISOU 964 CE3 TRP A 123 1459 1254 1411 -5 -354 379 C ATOM 965 CZ2 TRP A 123 18.657 31.985 31.533 1.00 13.87 C ANISOU 965 CZ2 TRP A 123 2150 1537 1581 -145 -756 156 C ATOM 966 CZ3 TRP A 123 19.789 31.063 29.590 1.00 14.47 C ANISOU 966 CZ3 TRP A 123 1658 1789 2053 -222 -623 699 C ATOM 967 CH2 TRP A 123 19.761 31.841 30.745 1.00 15.15 C ANISOU 967 CH2 TRP A 123 1822 1921 2015 -196 -784 649 C ATOM 968 N ASP A 124 16.575 28.930 25.496 1.00 6.53 N ANISOU 968 N ASP A 124 843 843 794 46 17 67 N ATOM 969 CA ASP A 124 17.051 27.841 24.635 1.00 6.65 C ANISOU 969 CA ASP A 124 662 919 948 56 12 20 C ATOM 970 C ASP A 124 17.774 26.861 25.584 1.00 6.46 C ANISOU 970 C ASP A 124 755 928 771 -47 -43 50 C ATOM 971 O ASP A 124 18.952 27.048 25.944 1.00 8.02 O ANISOU 971 O ASP A 124 778 1189 1080 -146 -36 194 O ATOM 972 CB ASP A 124 17.988 28.334 23.546 1.00 7.46 C ANISOU 972 CB ASP A 124 1021 932 882 30 119 34 C ATOM 973 CG ASP A 124 17.329 29.200 22.484 1.00 8.88 C ANISOU 973 CG ASP A 124 1337 1055 982 154 94 19 C ATOM 974 OD1 ASP A 124 16.110 29.064 22.278 1.00 10.76 O ANISOU 974 OD1 ASP A 124 1455 1351 1282 260 -293 99 O ATOM 975 OD2 ASP A 124 18.070 29.997 21.860 1.00 11.22 O ANISOU 975 OD2 ASP A 124 1787 1349 1125 53 126 356 O ATOM 976 N VAL A 125 17.028 25.872 26.110 1.00 6.27 N ANISOU 976 N VAL A 125 604 943 836 36 1 130 N ATOM 977 CA VAL A 125 17.593 24.947 27.103 1.00 6.58 C ANISOU 977 CA VAL A 125 740 904 856 -44 39 162 C ATOM 978 C VAL A 125 18.648 24.044 26.469 1.00 6.75 C ANISOU 978 C VAL A 125 773 930 859 -53 -47 75 C ATOM 979 O VAL A 125 19.737 23.866 27.032 1.00 8.89 O ANISOU 979 O VAL A 125 936 1433 1008 206 -187 -172 O ATOM 980 CB VAL A 125 16.474 24.143 27.791 1.00 7.46 C ANISOU 980 CB VAL A 125 823 1061 952 -3 177 174 C ATOM 981 CG1 VAL A 125 17.046 23.151 28.792 1.00 9.58 C ANISOU 981 CG1 VAL A 125 1316 1027 1296 83 272 345 C ATOM 982 CG2 VAL A 125 15.452 25.080 28.450 1.00 9.67 C ANISOU 982 CG2 VAL A 125 1300 1022 1351 141 440 179 C ATOM 983 N VAL A 126 18.276 23.406 25.352 1.00 6.85 N ANISOU 983 N VAL A 126 737 1006 861 49 0 -39 N ATOM 984 CA VAL A 126 19.160 22.514 24.601 1.00 6.59 C ANISOU 984 CA VAL A 126 758 996 748 29 24 -42 C ATOM 985 C VAL A 126 19.258 23.056 23.190 1.00 6.45 C ANISOU 985 C VAL A 126 844 891 714 112 -32 7 C ATOM 986 O VAL A 126 18.240 23.435 22.574 1.00 8.04 O ANISOU 986 O VAL A 126 796 1329 929 115 -36 170 O ATOM 987 CB VAL A 126 18.681 21.057 24.613 1.00 7.89 C ANISOU 987 CB VAL A 126 1038 969 990 12 -29 84 C ATOM 988 CG1 VAL A 126 19.554 20.181 23.727 1.00 10.52 C ANISOU 988 CG1 VAL A 126 1782 985 1228 194 123 52 C ATOM 989 CG2 VAL A 126 18.657 20.510 26.050 1.00 10.85 C ANISOU 989 CG2 VAL A 126 1848 1203 1071 -297 -61 197 C ATOM 990 N ASN A 127 20.479 23.078 22.647 1.00 6.69 N ANISOU 990 N ASN A 127 842 913 788 143 32 70 N ATOM 991 CA ASN A 127 20.776 23.592 21.314 1.00 6.46 C ANISOU 991 CA ASN A 127 810 829 814 44 50 -10 C ATOM 992 C ASN A 127 21.452 22.542 20.440 1.00 6.33 C ANISOU 992 C ASN A 127 775 705 923 123 -7 30 C ATOM 993 O ASN A 127 22.399 21.894 20.896 1.00 7.66 O ANISOU 993 O ASN A 127 971 993 947 206 -103 -58 O ATOM 994 CB ASN A 127 21.740 24.800 21.478 1.00 7.65 C ANISOU 994 CB ASN A 127 1143 726 1036 7 139 -64 C ATOM 995 CG ASN A 127 21.708 25.827 20.381 1.00 8.83 C ANISOU 995 CG ASN A 127 1121 795 1438 109 -22 146 C ATOM 996 OD1 ASN A 127 20.658 26.134 19.798 1.00 13.62 O ANISOU 996 OD1 ASN A 127 976 1449 2750 -116 -202 1255 O ATOM 997 ND2 ASN A 127 22.826 26.418 19.985 1.00 12.52 N ANISOU 997 ND2 ASN A 127 1286 1625 1847 -126 115 243 N ATOM 998 N GLU A 128 20.971 22.357 19.204 1.00 6.58 N ANISOU 998 N GLU A 128 744 879 878 48 69 -100 N ATOM 999 CA GLU A 128 21.725 21.628 18.170 1.00 6.33 C ANISOU 999 CA GLU A 128 731 803 869 130 -9 -41 C ATOM 1000 C GLU A 128 22.100 20.190 18.497 1.00 7.08 C ANISOU 1000 C GLU A 128 869 863 958 133 -38 -1 C ATOM 1001 O GLU A 128 23.233 19.741 18.259 1.00 8.79 O ANISOU 1001 O GLU A 128 941 1072 1326 164 51 1 O ATOM 1002 CB GLU A 128 22.977 22.450 17.748 1.00 6.92 C ANISOU 1002 CB GLU A 128 898 913 817 98 35 11 C ATOM 1003 CG GLU A 128 22.628 23.808 17.166 1.00 7.81 C ANISOU 1003 CG GLU A 128 1010 964 994 1 -31 148 C ATOM 1004 CD GLU A 128 23.816 24.679 16.800 1.00 8.29 C ANISOU 1004 CD GLU A 128 992 975 1184 -22 -15 82 C ATOM 1005 OE1 GLU A 128 24.971 24.213 16.907 1.00 10.36 O ANISOU 1005 OE1 GLU A 128 970 1519 1448 50 87 341 O ATOM 1006 OE2 GLU A 128 23.552 25.839 16.384 1.00 10.35 O ANISOU 1006 OE2 GLU A 128 1239 1175 1520 -56 -76 311 O ATOM 1007 N ALA A 129 21.126 19.395 18.974 1.00 7.30 N ANISOU 1007 N ALA A 129 998 743 1033 134 -30 36 N ATOM 1008 CA ALA A 129 21.368 18.003 19.333 1.00 7.23 C ANISOU 1008 CA ALA A 129 1031 744 972 130 17 -7 C ATOM 1009 C ALA A 129 21.307 17.009 18.185 1.00 6.68 C ANISOU 1009 C ALA A 129 907 644 988 122 33 23 C ATOM 1010 O ALA A 129 21.749 15.852 18.387 1.00 9.27 O ANISOU 1010 O ALA A 129 1615 716 1193 242 -268 -6 O ATOM 1011 CB ALA A 129 20.378 17.591 20.419 1.00 9.60 C ANISOU 1011 CB ALA A 129 1508 1097 1043 205 209 122 C ATOM 1012 N PHE A 130 20.745 17.339 17.025 1.00 7.12 N ANISOU 1012 N PHE A 130 1022 757 927 94 -24 47 N ATOM 1013 CA PHE A 130 20.651 16.404 15.920 1.00 7.68 C ANISOU 1013 CA PHE A 130 1225 805 890 90 2 110 C ATOM 1014 C PHE A 130 21.779 16.577 14.918 1.00 7.35 C ANISOU 1014 C PHE A 130 1219 744 830 -30 -30 7 C ATOM 1015 O PHE A 130 22.307 17.671 14.689 1.00 9.06 O ANISOU 1015 O PHE A 130 1260 860 1322 -46 176 -9 O ATOM 1016 CB PHE A 130 19.273 16.499 15.213 1.00 8.60 C ANISOU 1016 CB PHE A 130 1182 999 1087 106 6 9 C ATOM 1017 CG PHE A 130 18.180 15.962 16.098 1.00 8.93 C ANISOU 1017 CG PHE A 130 979 1108 1307 -140 -89 -68 C ATOM 1018 CD1 PHE A 130 18.056 14.585 16.294 1.00 11.04 C ANISOU 1018 CD1 PHE A 130 1379 1174 1641 -237 87 125 C ATOM 1019 CD2 PHE A 130 17.332 16.792 16.805 1.00 12.19 C ANISOU 1019 CD2 PHE A 130 1213 1584 1836 -96 149 -343 C ATOM 1020 CE1 PHE A 130 17.103 14.057 17.140 1.00 12.70 C ANISOU 1020 CE1 PHE A 130 1268 1634 1925 -362 -2 310 C ATOM 1021 CE2 PHE A 130 16.376 16.274 17.660 1.00 14.68 C ANISOU 1021 CE2 PHE A 130 1359 2110 2109 -164 319 -244 C ATOM 1022 CZ PHE A 130 16.276 14.910 17.821 1.00 14.14 C ANISOU 1022 CZ PHE A 130 1194 2257 1921 -460 240 106 C ATOM 1023 N ALA A 131 22.185 15.473 14.280 1.00 8.86 N ANISOU 1023 N ALA A 131 1400 865 1103 4 164 -86 N ATOM 1024 CA ALA A 131 23.187 15.481 13.220 1.00 9.80 C ANISOU 1024 CA ALA A 131 1417 1004 1301 210 284 -124 C ATOM 1025 C ALA A 131 22.566 16.010 11.917 1.00 9.63 C ANISOU 1025 C ALA A 131 1438 976 1245 85 340 -109 C ATOM 1026 O ALA A 131 21.373 15.868 11.659 1.00 11.14 O ANISOU 1026 O ALA A 131 1537 1414 1281 82 163 139 O ATOM 1027 CB ALA A 131 23.708 14.050 13.020 1.00 13.32 C ANISOU 1027 CB ALA A 131 2132 1306 1624 740 423 8 C ATOM 1028 N ASP A 132 23.414 16.557 11.038 1.00 10.03 N ANISOU 1028 N ASP A 132 1235 1208 1368 45 252 39 N ATOM 1029 CA ASP A 132 23.001 16.913 9.686 1.00 10.52 C ANISOU 1029 CA ASP A 132 1500 1180 1315 40 406 66 C ATOM 1030 C ASP A 132 23.025 15.664 8.796 1.00 12.27 C ANISOU 1030 C ASP A 132 1910 1281 1472 68 454 -12 C ATOM 1031 O ASP A 132 23.663 14.657 9.137 1.00 15.00 O ANISOU 1031 O ASP A 132 2431 1321 1946 297 21 -289 O ATOM 1032 CB ASP A 132 23.926 17.987 9.106 1.00 11.30 C ANISOU 1032 CB ASP A 132 1651 1214 1427 -45 585 -87 C ATOM 1033 CG ASP A 132 23.716 19.328 9.786 1.00 11.97 C ANISOU 1033 CG ASP A 132 1617 1183 1750 89 486 -70 C ATOM 1034 OD1 ASP A 132 22.543 19.773 9.913 1.00 12.40 O ANISOU 1034 OD1 ASP A 132 1657 1203 1852 79 630 -120 O ATOM 1035 OD2 ASP A 132 24.741 19.950 10.180 1.00 14.78 O ANISOU 1035 OD2 ASP A 132 1757 1590 2270 111 196 -498 O ATOM 1036 N GLY A 133 22.314 15.713 7.685 1.00 13.49 N ANISOU 1036 N GLY A 133 2328 1286 1511 26 273 -171 N ATOM 1037 CA GLY A 133 22.301 14.610 6.732 1.00 13.95 C ANISOU 1037 CA GLY A 133 2494 1372 1436 -230 485 -139 C ATOM 1038 C GLY A 133 21.034 13.783 6.774 1.00 12.72 C ANISOU 1038 C GLY A 133 2129 1392 1312 0 218 -159 C ATOM 1039 O GLY A 133 19.986 14.198 7.295 1.00 14.81 O ANISOU 1039 O GLY A 133 2190 1603 1833 109 275 -269 O ATOM 1040 N SER A 134 21.074 12.580 6.196 1.00 14.15 N ANISOU 1040 N SER A 134 2400 1353 1623 -107 424 -183 N ATOM 1041 CA SER A 134 19.904 11.744 5.999 1.00 14.33 C ANISOU 1041 CA SER A 134 2428 1426 1589 -59 35 -128 C ATOM 1042 C SER A 134 19.566 10.789 7.120 1.00 14.07 C ANISOU 1042 C SER A 134 2253 1492 1601 -46 245 -185 C ATOM 1043 O SER A 134 18.511 10.134 7.025 1.00 16.60 O ANISOU 1043 O SER A 134 2502 1878 1927 -318 -109 -188 O ATOM 1044 CB SER A 134 20.123 10.904 4.707 1.00 18.86 C ANISOU 1044 CB SER A 134 3540 2177 1449 -259 184 -233 C ATOM 1045 OG ASER A 134 21.322 10.168 4.883 0.50 20.14 O ANISOU 1045 OG ASER A 134 3883 1930 1840 99 746 -414 O ATOM 1046 OG BSER A 134 20.135 11.766 3.585 0.50 24.22 O ANISOU 1046 OG BSER A 134 4586 2741 1874 -211 101 235 O ATOM 1047 N SER A 135 20.392 10.652 8.157 1.00 12.60 N ANISOU 1047 N SER A 135 2126 1224 1435 -95 347 -223 N ATOM 1048 CA SER A 135 20.139 9.622 9.164 1.00 12.84 C ANISOU 1048 CA SER A 135 2099 1203 1576 109 513 -162 C ATOM 1049 C SER A 135 19.108 9.955 10.221 1.00 10.93 C ANISOU 1049 C SER A 135 1591 1303 1258 8 145 -161 C ATOM 1050 O SER A 135 18.520 9.033 10.823 1.00 13.95 O ANISOU 1050 O SER A 135 2239 1368 1694 -280 361 -183 O ATOM 1051 CB SER A 135 21.464 9.280 9.884 1.00 14.53 C ANISOU 1051 CB SER A 135 2140 1380 2001 369 571 32 C ATOM 1052 OG SER A 135 21.885 10.360 10.714 1.00 14.84 O ANISOU 1052 OG SER A 135 1833 2048 1759 227 -64 41 O ATOM 1053 N GLY A 136 18.950 11.235 10.571 1.00 10.88 N ANISOU 1053 N GLY A 136 1486 1339 1308 179 35 -139 N ATOM 1054 CA GLY A 136 18.090 11.595 11.695 1.00 10.78 C ANISOU 1054 CA GLY A 136 1258 1507 1332 334 -58 -94 C ATOM 1055 C GLY A 136 18.726 11.219 13.036 1.00 9.63 C ANISOU 1055 C GLY A 136 1349 1004 1306 159 -37 -143 C ATOM 1056 O GLY A 136 18.012 11.227 14.045 1.00 13.34 O ANISOU 1056 O GLY A 136 1723 1971 1375 445 178 69 O ATOM 1057 N ALA A 137 20.019 10.926 13.081 1.00 9.37 N ANISOU 1057 N ALA A 137 1355 973 1234 34 -166 -132 N ATOM 1058 CA ALA A 137 20.679 10.546 14.326 1.00 9.27 C ANISOU 1058 CA ALA A 137 1577 824 1122 224 -37 -9 C ATOM 1059 C ALA A 137 20.947 11.757 15.222 1.00 8.37 C ANISOU 1059 C ALA A 137 1177 850 1153 75 -93 27 C ATOM 1060 O ALA A 137 20.949 12.908 14.766 1.00 10.27 O ANISOU 1060 O ALA A 137 1809 809 1283 79 -145 33 O ATOM 1061 CB ALA A 137 21.990 9.815 14.055 1.00 12.96 C ANISOU 1061 CB ALA A 137 2014 1283 1627 687 -22 -226 C ATOM 1062 N ARG A 138 21.264 11.478 16.479 1.00 8.79 N ANISOU 1062 N ARG A 138 1424 729 1187 14 -241 20 N ATOM 1063 CA ARG A 138 21.795 12.480 17.384 1.00 8.37 C ANISOU 1063 CA ARG A 138 1157 696 1327 90 -139 -33 C ATOM 1064 C ARG A 138 23.247 12.759 17.002 1.00 8.73 C ANISOU 1064 C ARG A 138 1265 898 1154 1 0 -125 C ATOM 1065 O ARG A 138 24.013 11.870 16.610 1.00 11.62 O ANISOU 1065 O ARG A 138 1473 1033 1909 77 179 -217 O ATOM 1066 CB ARG A 138 21.761 11.988 18.837 1.00 9.52 C ANISOU 1066 CB ARG A 138 1330 1104 1182 -50 -87 -177 C ATOM 1067 CG ARG A 138 20.390 11.745 19.435 1.00 10.24 C ANISOU 1067 CG ARG A 138 1357 1083 1449 -4 5 -8 C ATOM 1068 CD ARG A 138 19.702 12.979 19.975 1.00 10.80 C ANISOU 1068 CD ARG A 138 1455 1193 1453 -11 131 -28 C ATOM 1069 NE ARG A 138 18.420 12.654 20.596 1.00 11.50 N ANISOU 1069 NE ARG A 138 1369 1655 1347 44 83 25 N ATOM 1070 CZ ARG A 138 18.239 12.243 21.842 1.00 11.07 C ANISOU 1070 CZ ARG A 138 1274 1569 1365 -9 26 57 C ATOM 1071 NH1 ARG A 138 19.237 12.114 22.701 1.00 11.13 N ANISOU 1071 NH1 ARG A 138 1283 1541 1404 98 9 155 N ATOM 1072 NH2 ARG A 138 17.000 11.974 22.260 1.00 15.04 N ANISOU 1072 NH2 ARG A 138 1366 2468 1881 -168 169 259 N ATOM 1073 N ARG A 139 23.677 14.000 17.167 1.00 8.84 N ANISOU 1073 N ARG A 139 1143 925 1290 -49 -2 -65 N ATOM 1074 CA ARG A 139 25.046 14.448 17.017 1.00 9.65 C ANISOU 1074 CA ARG A 139 1248 1106 1311 -78 57 211 C ATOM 1075 C ARG A 139 25.924 13.802 18.100 1.00 9.24 C ANISOU 1075 C ARG A 139 1102 1100 1308 -37 -16 -94 C ATOM 1076 O ARG A 139 25.488 13.669 19.264 1.00 10.29 O ANISOU 1076 O ARG A 139 1285 1260 1364 108 10 92 O ATOM 1077 CB ARG A 139 25.082 15.988 17.158 1.00 13.76 C ANISOU 1077 CB ARG A 139 1904 1158 2166 -233 -413 344 C ATOM 1078 CG ARG A 139 26.415 16.682 17.108 1.00 13.85 C ANISOU 1078 CG ARG A 139 1933 1232 2097 -168 -264 -118 C ATOM 1079 CD ARG A 139 26.263 18.144 17.453 1.00 11.01 C ANISOU 1079 CD ARG A 139 1451 1101 1632 -64 -49 94 C ATOM 1080 NE ARG A 139 25.465 18.931 16.532 1.00 10.09 N ANISOU 1080 NE ARG A 139 1127 1200 1507 57 89 -62 N ATOM 1081 CZ ARG A 139 25.914 19.431 15.377 1.00 11.16 C ANISOU 1081 CZ ARG A 139 1138 1565 1539 -105 96 -25 C ATOM 1082 NH1 ARG A 139 27.153 19.195 14.952 1.00 15.49 N ANISOU 1082 NH1 ARG A 139 1335 2661 1888 56 382 102 N ATOM 1083 NH2 ARG A 139 25.091 20.167 14.636 1.00 13.29 N ANISOU 1083 NH2 ARG A 139 1248 2039 1761 46 293 428 N ATOM 1084 N ASP A 140 27.149 13.425 17.745 1.00 9.60 N ANISOU 1084 N ASP A 140 1248 1183 1218 48 -20 -124 N ATOM 1085 CA ASP A 140 28.096 12.908 18.734 1.00 9.72 C ANISOU 1085 CA ASP A 140 1311 1255 1126 117 56 -128 C ATOM 1086 C ASP A 140 28.668 14.028 19.612 1.00 10.04 C ANISOU 1086 C ASP A 140 1394 1158 1261 -41 31 -23 C ATOM 1087 O ASP A 140 29.063 15.086 19.087 1.00 13.48 O ANISOU 1087 O ASP A 140 2041 1567 1512 -426 -22 223 O ATOM 1088 CB ASP A 140 29.252 12.171 18.044 1.00 12.69 C ANISOU 1088 CB ASP A 140 1552 1660 1610 392 206 -131 C ATOM 1089 CG ASP A 140 30.157 11.423 18.989 1.00 15.08 C ANISOU 1089 CG ASP A 140 1738 1993 2000 415 -53 -15 C ATOM 1090 OD1 ASP A 140 29.718 10.872 20.011 1.00 14.71 O ANISOU 1090 OD1 ASP A 140 1774 1710 2107 372 -254 132 O ATOM 1091 OD2 ASP A 140 31.375 11.338 18.704 1.00 25.18 O ANISOU 1091 OD2 ASP A 140 1936 4241 3390 877 426 460 O ATOM 1092 N SER A 141 28.680 13.860 20.910 1.00 9.06 N ANISOU 1092 N SER A 141 1093 1118 1231 -44 5 -91 N ATOM 1093 CA SER A 141 29.252 14.803 21.864 1.00 8.81 C ANISOU 1093 CA SER A 141 1062 922 1363 -37 117 -97 C ATOM 1094 C SER A 141 29.413 14.076 23.193 1.00 8.16 C ANISOU 1094 C SER A 141 781 952 1367 -28 25 -104 C ATOM 1095 O SER A 141 28.797 13.020 23.409 1.00 9.19 O ANISOU 1095 O SER A 141 1240 898 1353 -55 -36 -59 O ATOM 1096 CB SER A 141 28.359 16.033 22.041 1.00 9.49 C ANISOU 1096 CB SER A 141 1136 1037 1431 68 36 -50 C ATOM 1097 OG SER A 141 27.144 15.679 22.709 1.00 9.92 O ANISOU 1097 OG SER A 141 1234 1093 1444 239 183 -14 O ATOM 1098 N ASN A 142 30.147 14.675 24.133 1.00 8.30 N ANISOU 1098 N ASN A 142 992 842 1318 -43 -22 -69 N ATOM 1099 CA ASN A 142 30.217 14.117 25.484 1.00 8.54 C ANISOU 1099 CA ASN A 142 897 1096 1253 -58 -30 -35 C ATOM 1100 C ASN A 142 28.822 14.010 26.129 1.00 7.55 C ANISOU 1100 C ASN A 142 933 863 1071 -94 -164 8 C ATOM 1101 O ASN A 142 28.515 13.019 26.804 1.00 9.03 O ANISOU 1101 O ASN A 142 1109 993 1330 -107 -158 115 O ATOM 1102 CB ASN A 142 31.214 14.896 26.356 1.00 9.56 C ANISOU 1102 CB ASN A 142 900 1096 1637 -63 -172 2 C ATOM 1103 CG ASN A 142 30.984 16.374 26.561 1.00 9.50 C ANISOU 1103 CG ASN A 142 915 1127 1569 -80 -220 -98 C ATOM 1104 OD1 ASN A 142 30.138 16.995 25.915 1.00 10.61 O ANISOU 1104 OD1 ASN A 142 1188 1114 1729 -90 -346 -85 O ATOM 1105 ND2 ASN A 142 31.758 17.002 27.456 1.00 12.10 N ANISOU 1105 ND2 ASN A 142 1286 1442 1868 -221 -334 -323 N ATOM 1106 N LEU A 143 27.965 15.025 25.905 1.00 7.87 N ANISOU 1106 N LEU A 143 879 968 1145 -4 2 2 N ATOM 1107 CA LEU A 143 26.595 15.001 26.403 1.00 8.23 C ANISOU 1107 CA LEU A 143 961 1065 1099 43 -7 -173 C ATOM 1108 C LEU A 143 25.812 13.801 25.862 1.00 8.11 C ANISOU 1108 C LEU A 143 942 1032 1109 1 -91 5 C ATOM 1109 O LEU A 143 25.183 13.060 26.644 1.00 9.28 O ANISOU 1109 O LEU A 143 1123 1153 1249 -94 -114 88 O ATOM 1110 CB LEU A 143 25.883 16.328 26.054 1.00 9.24 C ANISOU 1110 CB LEU A 143 1088 945 1480 -21 -52 -51 C ATOM 1111 CG LEU A 143 26.477 17.568 26.754 1.00 10.80 C ANISOU 1111 CG LEU A 143 1141 1006 1955 87 -43 -252 C ATOM 1112 CD1 LEU A 143 26.050 18.829 26.010 1.00 13.70 C ANISOU 1112 CD1 LEU A 143 1678 1063 2464 73 -116 -68 C ATOM 1113 CD2 LEU A 143 26.049 17.627 28.215 1.00 15.79 C ANISOU 1113 CD2 LEU A 143 2154 1732 2112 37 311 -376 C ATOM 1114 N GLN A 144 25.833 13.581 24.549 1.00 7.94 N ANISOU 1114 N GLN A 144 953 922 1140 -129 -92 -26 N ATOM 1115 CA GLN A 144 25.102 12.447 23.959 1.00 7.92 C ANISOU 1115 CA GLN A 144 1016 842 1151 -55 -235 44 C ATOM 1116 C GLN A 144 25.673 11.118 24.406 1.00 8.52 C ANISOU 1116 C GLN A 144 1016 835 1385 -129 -206 148 C ATOM 1117 O GLN A 144 24.899 10.163 24.637 1.00 9.44 O ANISOU 1117 O GLN A 144 1215 796 1577 -164 -215 126 O ATOM 1118 CB GLN A 144 25.080 12.606 22.442 1.00 8.92 C ANISOU 1118 CB GLN A 144 1235 1022 1131 54 -111 -27 C ATOM 1119 CG GLN A 144 24.469 11.432 21.692 1.00 9.65 C ANISOU 1119 CG GLN A 144 1125 1068 1474 -56 -102 -54 C ATOM 1120 CD GLN A 144 23.030 11.098 22.010 1.00 8.81 C ANISOU 1120 CD GLN A 144 1090 1016 1243 -91 -258 -13 C ATOM 1121 OE1 GLN A 144 22.212 11.966 22.356 1.00 9.62 O ANISOU 1121 OE1 GLN A 144 1143 1161 1353 -172 31 -146 O ATOM 1122 NE2 GLN A 144 22.659 9.820 21.844 1.00 11.87 N ANISOU 1122 NE2 GLN A 144 1460 1086 1965 -194 -355 -94 N ATOM 1123 N ARG A 145 26.994 10.991 24.581 1.00 9.05 N ANISOU 1123 N ARG A 145 1040 834 1563 -3 -168 92 N ATOM 1124 CA ARG A 145 27.593 9.738 25.030 1.00 10.28 C ANISOU 1124 CA ARG A 145 1173 936 1797 66 -158 142 C ATOM 1125 C ARG A 145 27.202 9.405 26.457 1.00 11.29 C ANISOU 1125 C ARG A 145 1266 1224 1798 187 -177 199 C ATOM 1126 O ARG A 145 27.310 8.228 26.847 1.00 15.15 O ANISOU 1126 O ARG A 145 1984 1402 2370 354 -50 504 O ATOM 1127 CB ARG A 145 29.116 9.736 24.847 1.00 11.44 C ANISOU 1127 CB ARG A 145 1185 1288 1873 261 -96 115 C ATOM 1128 CG AARG A 145 29.553 9.738 23.388 0.50 11.18 C ANISOU 1128 CG AARG A 145 1297 1024 1928 88 37 -92 C ATOM 1129 CD AARG A 145 31.036 9.543 23.233 0.50 13.75 C ANISOU 1129 CD AARG A 145 1337 1662 2225 279 73 -38 C ATOM 1130 NE AARG A 145 31.860 10.623 23.737 0.50 12.85 N ANISOU 1130 NE AARG A 145 1391 1652 1838 367 30 -136 N ATOM 1131 CZ AARG A 145 32.217 11.727 23.102 0.50 11.97 C ANISOU 1131 CZ AARG A 145 1032 1558 1959 493 194 -223 C ATOM 1132 NH1AARG A 145 31.823 12.023 21.878 0.50 14.30 N ANISOU 1132 NH1AARG A 145 1170 2322 1940 67 8 -233 N ATOM 1133 NH2AARG A 145 33.015 12.584 23.737 0.50 15.09 N ANISOU 1133 NH2AARG A 145 1533 1763 2436 20 105 -202 N ATOM 1134 CG BARG A 145 29.575 9.601 23.402 0.50 14.23 C ANISOU 1134 CG BARG A 145 1869 1649 1890 98 -29 -240 C ATOM 1135 CD BARG A 145 31.074 9.443 23.255 0.50 18.70 C ANISOU 1135 CD BARG A 145 1934 2650 2523 253 189 129 C ATOM 1136 NE BARG A 145 31.533 9.574 21.878 0.50 19.82 N ANISOU 1136 NE BARG A 145 2292 2881 2358 255 9 130 N ATOM 1137 CZ BARG A 145 32.733 9.228 21.419 0.50 23.36 C ANISOU 1137 CZ BARG A 145 2403 3388 3083 402 196 78 C ATOM 1138 NH1BARG A 145 33.646 8.716 22.238 0.50 25.51 N ANISOU 1138 NH1BARG A 145 2333 3685 3676 299 -25 263 N ATOM 1139 NH2BARG A 145 33.021 9.402 20.133 0.50 23.00 N ANISOU 1139 NH2BARG A 145 2454 3439 2846 911 -183 -25 N ATOM 1140 N SER A 146 26.755 10.357 27.267 1.00 10.04 N ANISOU 1140 N SER A 146 1128 1154 1532 -82 -194 210 N ATOM 1141 CA SER A 146 26.285 10.126 28.618 1.00 10.97 C ANISOU 1141 CA SER A 146 1098 1476 1596 36 -230 293 C ATOM 1142 C SER A 146 24.944 9.382 28.655 1.00 11.79 C ANISOU 1142 C SER A 146 1219 1550 1711 -163 -298 463 C ATOM 1143 O SER A 146 24.601 8.814 29.694 1.00 15.81 O ANISOU 1143 O SER A 146 1593 2452 1963 -442 -399 870 O ATOM 1144 CB SER A 146 26.226 11.396 29.475 1.00 12.18 C ANISOU 1144 CB SER A 146 1407 1794 1426 -205 -156 97 C ATOM 1145 OG SER A 146 25.090 12.210 29.162 1.00 12.77 O ANISOU 1145 OG SER A 146 1688 1574 1588 50 30 -1 O ATOM 1146 N GLY A 147 24.194 9.381 27.563 1.00 10.74 N ANISOU 1146 N GLY A 147 1047 1452 1581 -208 -174 301 N ATOM 1147 CA GLY A 147 22.945 8.646 27.431 1.00 11.12 C ANISOU 1147 CA GLY A 147 1131 1217 1875 -178 -111 282 C ATOM 1148 C GLY A 147 21.902 9.402 26.619 1.00 9.80 C ANISOU 1148 C GLY A 147 1053 1020 1652 -63 -51 -29 C ATOM 1149 O GLY A 147 21.891 10.650 26.596 1.00 10.89 O ANISOU 1149 O GLY A 147 1246 990 1902 -88 -39 -36 O ATOM 1150 N ASN A 148 20.965 8.653 26.012 1.00 9.69 N ANISOU 1150 N ASN A 148 1135 854 1693 -55 -119 -17 N ATOM 1151 CA ASN A 148 19.937 9.267 25.170 1.00 9.23 C ANISOU 1151 CA ASN A 148 983 1101 1422 -26 38 -78 C ATOM 1152 C ASN A 148 19.016 10.200 25.949 1.00 9.04 C ANISOU 1152 C ASN A 148 1214 915 1308 4 33 8 C ATOM 1153 O ASN A 148 18.434 11.112 25.340 1.00 10.39 O ANISOU 1153 O ASN A 148 1353 1193 1400 223 24 111 O ATOM 1154 CB ASN A 148 19.099 8.199 24.450 1.00 10.66 C ANISOU 1154 CB ASN A 148 1340 1080 1631 -182 -19 -163 C ATOM 1155 CG ASN A 148 19.749 7.571 23.243 1.00 11.61 C ANISOU 1155 CG ASN A 148 1460 1308 1644 -405 169 -129 C ATOM 1156 OD1 ASN A 148 20.385 8.239 22.416 1.00 15.22 O ANISOU 1156 OD1 ASN A 148 2244 1786 1752 -840 512 -306 O ATOM 1157 ND2 ASN A 148 19.576 6.258 23.046 1.00 12.61 N ANISOU 1157 ND2 ASN A 148 1748 1286 1758 -300 227 -219 N ATOM 1158 N ASP A 149 18.892 9.995 27.252 1.00 8.84 N ANISOU 1158 N ASP A 149 1118 898 1344 4 10 109 N ATOM 1159 CA ASP A 149 18.060 10.791 28.140 1.00 9.02 C ANISOU 1159 CA ASP A 149 1004 1008 1415 -66 134 126 C ATOM 1160 C ASP A 149 18.614 12.153 28.542 1.00 8.19 C ANISOU 1160 C ASP A 149 1060 1105 947 -43 59 97 C ATOM 1161 O ASP A 149 17.960 12.881 29.306 1.00 9.12 O ANISOU 1161 O ASP A 149 1178 1076 1212 -15 130 45 O ATOM 1162 CB ASP A 149 17.711 9.977 29.415 1.00 11.85 C ANISOU 1162 CB ASP A 149 1686 1166 1651 -94 426 196 C ATOM 1163 CG ASP A 149 18.935 9.678 30.267 1.00 14.97 C ANISOU 1163 CG ASP A 149 2500 1424 1763 219 18 535 C ATOM 1164 OD1 ASP A 149 20.026 9.469 29.703 1.00 19.28 O ANISOU 1164 OD1 ASP A 149 2281 2681 2364 476 -126 840 O ATOM 1165 OD2 ASP A 149 18.791 9.599 31.508 1.00 20.81 O ANISOU 1165 OD2 ASP A 149 3647 2482 1779 382 -22 525 O ATOM 1166 N TRP A 150 19.789 12.568 28.018 1.00 8.01 N ANISOU 1166 N TRP A 150 1072 820 1151 23 105 63 N ATOM 1167 CA TRP A 150 20.370 13.832 28.477 1.00 7.82 C ANISOU 1167 CA TRP A 150 965 881 1126 -47 -41 156 C ATOM 1168 C TRP A 150 19.474 15.033 28.195 1.00 6.98 C ANISOU 1168 C TRP A 150 807 825 1020 -111 -80 67 C ATOM 1169 O TRP A 150 19.419 15.980 29.006 1.00 8.36 O ANISOU 1169 O TRP A 150 1109 960 1106 70 -131 -14 O ATOM 1170 CB TRP A 150 21.748 14.052 27.870 1.00 8.97 C ANISOU 1170 CB TRP A 150 1068 1129 1210 -11 1 28 C ATOM 1171 CG TRP A 150 21.866 14.423 26.435 1.00 8.48 C ANISOU 1171 CG TRP A 150 846 1076 1301 -29 165 44 C ATOM 1172 CD1 TRP A 150 21.919 13.575 25.364 1.00 9.36 C ANISOU 1172 CD1 TRP A 150 1077 1045 1436 -7 -102 -4 C ATOM 1173 CD2 TRP A 150 22.026 15.755 25.900 1.00 8.22 C ANISOU 1173 CD2 TRP A 150 836 1023 1265 30 35 -77 C ATOM 1174 NE1 TRP A 150 22.104 14.283 24.200 1.00 9.19 N ANISOU 1174 NE1 TRP A 150 1129 1111 1252 53 -26 -284 N ATOM 1175 CE2 TRP A 150 22.187 15.620 24.511 1.00 8.22 C ANISOU 1175 CE2 TRP A 150 849 1008 1265 50 68 30 C ATOM 1176 CE3 TRP A 150 22.047 17.037 26.469 1.00 8.98 C ANISOU 1176 CE3 TRP A 150 1054 1077 1279 12 -97 -43 C ATOM 1177 CZ2 TRP A 150 22.394 16.718 23.671 1.00 9.75 C ANISOU 1177 CZ2 TRP A 150 1115 1147 1444 95 15 75 C ATOM 1178 CZ3 TRP A 150 22.255 18.116 25.628 1.00 10.61 C ANISOU 1178 CZ3 TRP A 150 1418 961 1654 -84 -22 -99 C ATOM 1179 CH2 TRP A 150 22.418 17.959 24.246 1.00 10.85 C ANISOU 1179 CH2 TRP A 150 1326 1124 1672 22 166 153 C ATOM 1180 N ILE A 151 18.774 15.041 27.060 1.00 7.06 N ANISOU 1180 N ILE A 151 838 905 941 52 -37 52 N ATOM 1181 CA ILE A 151 17.920 16.160 26.664 1.00 6.73 C ANISOU 1181 CA ILE A 151 816 822 918 -17 -47 56 C ATOM 1182 C ILE A 151 16.743 16.265 27.639 1.00 7.13 C ANISOU 1182 C ILE A 151 805 975 930 -6 -53 -6 C ATOM 1183 O ILE A 151 16.445 17.353 28.176 1.00 7.63 O ANISOU 1183 O ILE A 151 988 1000 911 53 46 72 O ATOM 1184 CB ILE A 151 17.448 16.026 25.199 1.00 7.13 C ANISOU 1184 CB ILE A 151 840 958 910 -84 32 56 C ATOM 1185 CG1 ILE A 151 18.640 15.923 24.231 1.00 8.76 C ANISOU 1185 CG1 ILE A 151 1054 1165 1107 -68 189 98 C ATOM 1186 CG2 ILE A 151 16.521 17.178 24.814 1.00 8.27 C ANISOU 1186 CG2 ILE A 151 947 1047 1149 -5 -52 113 C ATOM 1187 CD1 ILE A 151 18.248 15.734 22.782 1.00 10.73 C ANISOU 1187 CD1 ILE A 151 1261 1735 1079 138 232 66 C ATOM 1188 N GLU A 152 16.031 15.151 27.903 1.00 7.96 N ANISOU 1188 N GLU A 152 785 1112 1128 -116 -1 27 N ATOM 1189 CA GLU A 152 14.920 15.141 28.856 1.00 8.87 C ANISOU 1189 CA GLU A 152 941 1295 1135 -211 101 6 C ATOM 1190 C GLU A 152 15.377 15.634 30.223 1.00 8.24 C ANISOU 1190 C GLU A 152 1044 965 1122 -123 76 162 C ATOM 1191 O GLU A 152 14.645 16.383 30.910 1.00 9.49 O ANISOU 1191 O GLU A 152 1143 1237 1225 -40 122 57 O ATOM 1192 CB GLU A 152 14.313 13.709 28.940 1.00 12.78 C ANISOU 1192 CB GLU A 152 1467 1779 1609 -802 249 -434 C ATOM 1193 CG GLU A 152 13.499 13.392 30.173 1.00 15.23 C ANISOU 1193 CG GLU A 152 1735 2019 2032 -477 348 201 C ATOM 1194 CD GLU A 152 12.880 12.016 30.295 1.00 17.44 C ANISOU 1194 CD GLU A 152 2187 1753 2687 -319 381 -122 C ATOM 1195 OE1 GLU A 152 13.123 11.134 29.441 1.00 16.41 O ANISOU 1195 OE1 GLU A 152 2200 1688 2349 -436 96 -71 O ATOM 1196 OE2 GLU A 152 12.134 11.820 31.294 1.00 21.94 O ANISOU 1196 OE2 GLU A 152 2975 2443 2917 -521 624 439 O ATOM 1197 N VAL A 153 16.531 15.170 30.723 1.00 8.24 N ANISOU 1197 N VAL A 153 1206 909 1015 -106 -53 135 N ATOM 1198 CA VAL A 153 17.036 15.599 32.027 1.00 8.19 C ANISOU 1198 CA VAL A 153 1106 1009 996 -36 18 70 C ATOM 1199 C VAL A 153 17.248 17.120 32.071 1.00 7.46 C ANISOU 1199 C VAL A 153 888 1023 924 53 -10 88 C ATOM 1200 O VAL A 153 16.898 17.779 33.074 1.00 8.55 O ANISOU 1200 O VAL A 153 1278 1066 903 16 -5 73 O ATOM 1201 CB VAL A 153 18.287 14.810 32.430 1.00 10.29 C ANISOU 1201 CB VAL A 153 1536 1147 1228 181 -142 297 C ATOM 1202 CG1 VAL A 153 18.993 15.393 33.657 1.00 12.73 C ANISOU 1202 CG1 VAL A 153 1878 1422 1537 141 -443 222 C ATOM 1203 CG2 VAL A 153 17.940 13.339 32.666 1.00 13.53 C ANISOU 1203 CG2 VAL A 153 2492 1083 1565 168 -233 224 C ATOM 1204 N ALA A 154 17.818 17.698 31.001 1.00 7.22 N ANISOU 1204 N ALA A 154 895 944 905 -49 29 62 N ATOM 1205 CA ALA A 154 18.006 19.150 30.964 1.00 7.23 C ANISOU 1205 CA ALA A 154 831 959 956 -108 -91 50 C ATOM 1206 C ALA A 154 16.671 19.897 31.064 1.00 6.62 C ANISOU 1206 C ALA A 154 865 980 670 -100 11 6 C ATOM 1207 O ALA A 154 16.562 20.873 31.825 1.00 7.82 O ANISOU 1207 O ALA A 154 1002 1038 932 83 -3 -75 O ATOM 1208 CB ALA A 154 18.758 19.555 29.691 1.00 8.08 C ANISOU 1208 CB ALA A 154 840 1017 1213 -23 28 135 C ATOM 1209 N PHE A 155 15.638 19.464 30.324 1.00 6.65 N ANISOU 1209 N PHE A 155 762 970 796 -24 -25 55 N ATOM 1210 CA PHE A 155 14.322 20.099 30.405 1.00 6.57 C ANISOU 1210 CA PHE A 155 744 895 857 -51 6 65 C ATOM 1211 C PHE A 155 13.657 19.965 31.780 1.00 7.26 C ANISOU 1211 C PHE A 155 849 1007 904 38 26 93 C ATOM 1212 O PHE A 155 13.087 20.927 32.306 1.00 7.92 O ANISOU 1212 O PHE A 155 999 1118 893 75 69 37 O ATOM 1213 CB PHE A 155 13.379 19.605 29.290 1.00 7.30 C ANISOU 1213 CB PHE A 155 861 1059 854 4 -150 205 C ATOM 1214 CG PHE A 155 13.644 20.301 27.960 1.00 6.91 C ANISOU 1214 CG PHE A 155 872 899 855 -68 -25 115 C ATOM 1215 CD1 PHE A 155 13.061 21.528 27.698 1.00 8.42 C ANISOU 1215 CD1 PHE A 155 1217 1037 947 159 58 131 C ATOM 1216 CD2 PHE A 155 14.461 19.742 26.984 1.00 9.63 C ANISOU 1216 CD2 PHE A 155 1446 1338 876 362 1 244 C ATOM 1217 CE1 PHE A 155 13.325 22.207 26.518 1.00 9.27 C ANISOU 1217 CE1 PHE A 155 1396 1080 1047 50 70 195 C ATOM 1218 CE2 PHE A 155 14.688 20.410 25.801 1.00 10.37 C ANISOU 1218 CE2 PHE A 155 1622 1441 878 469 372 183 C ATOM 1219 CZ PHE A 155 14.138 21.644 25.557 1.00 8.98 C ANISOU 1219 CZ PHE A 155 1207 1218 988 46 -49 261 C ATOM 1220 N ARG A 156 13.709 18.761 32.398 1.00 7.50 N ANISOU 1220 N ARG A 156 978 1016 854 -31 134 108 N ATOM 1221 CA ARG A 156 13.115 18.580 33.726 1.00 8.03 C ANISOU 1221 CA ARG A 156 901 1298 850 -68 44 301 C ATOM 1222 C ARG A 156 13.803 19.480 34.762 1.00 8.42 C ANISOU 1222 C ARG A 156 987 1285 925 -7 99 221 C ATOM 1223 O ARG A 156 13.145 20.073 35.633 1.00 9.83 O ANISOU 1223 O ARG A 156 1166 1551 1016 0 98 63 O ATOM 1224 CB ARG A 156 13.151 17.106 34.169 1.00 10.22 C ANISOU 1224 CB ARG A 156 1349 1328 1208 -84 5 399 C ATOM 1225 CG ARG A 156 12.229 16.190 33.354 1.00 11.53 C ANISOU 1225 CG ARG A 156 1426 1574 1381 -217 36 270 C ATOM 1226 CD ARG A 156 12.088 14.800 33.960 1.00 15.83 C ANISOU 1226 CD ARG A 156 2216 1927 1871 -658 -92 687 C ATOM 1227 NE ARG A 156 11.298 13.867 33.158 1.00 17.95 N ANISOU 1227 NE ARG A 156 2451 2215 2156 -642 184 119 N ATOM 1228 CZ ARG A 156 9.968 13.809 33.127 1.00 20.98 C ANISOU 1228 CZ ARG A 156 2465 2955 2551 -663 307 154 C ATOM 1229 NH1 ARG A 156 9.207 14.628 33.847 1.00 22.98 N ANISOU 1229 NH1 ARG A 156 2386 3335 3010 -646 639 142 N ATOM 1230 NH2 ARG A 156 9.348 12.911 32.363 1.00 24.96 N ANISOU 1230 NH2 ARG A 156 3642 3097 2744 -973 239 -25 N ATOM 1231 N THR A 157 15.130 19.616 34.658 1.00 7.85 N ANISOU 1231 N THR A 157 972 1132 878 5 41 96 N ATOM 1232 CA THR A 157 15.901 20.462 35.557 1.00 8.45 C ANISOU 1232 CA THR A 157 1153 1213 843 9 -62 173 C ATOM 1233 C THR A 157 15.495 21.925 35.407 1.00 8.45 C ANISOU 1233 C THR A 157 1164 1205 842 26 -59 70 C ATOM 1234 O THR A 157 15.251 22.660 36.379 1.00 9.34 O ANISOU 1234 O THR A 157 1399 1309 840 143 -82 72 O ATOM 1235 CB THR A 157 17.423 20.294 35.305 1.00 9.53 C ANISOU 1235 CB THR A 157 1169 1364 1090 113 -230 148 C ATOM 1236 OG1 THR A 157 17.785 18.914 35.464 1.00 12.06 O ANISOU 1236 OG1 THR A 157 1413 1500 1669 308 -324 167 O ATOM 1237 CG2 THR A 157 18.229 21.160 36.239 1.00 10.34 C ANISOU 1237 CG2 THR A 157 1140 1607 1182 -34 -90 -11 C ATOM 1238 N ALA A 158 15.380 22.398 34.157 1.00 8.18 N ANISOU 1238 N ALA A 158 1248 1100 759 66 -57 35 N ATOM 1239 CA ALA A 158 15.035 23.783 33.872 1.00 7.70 C ANISOU 1239 CA ALA A 158 1048 1043 835 -45 58 17 C ATOM 1240 C ALA A 158 13.641 24.155 34.360 1.00 7.83 C ANISOU 1240 C ALA A 158 1130 1014 831 16 160 63 C ATOM 1241 O ALA A 158 13.446 25.269 34.875 1.00 9.30 O ANISOU 1241 O ALA A 158 1395 1146 993 107 57 3 O ATOM 1242 CB ALA A 158 15.233 24.058 32.386 1.00 8.72 C ANISOU 1242 CB ALA A 158 1051 1421 841 -82 24 150 C ATOM 1243 N ARG A 159 12.659 23.264 34.183 1.00 7.81 N ANISOU 1243 N ARG A 159 1102 1023 843 34 50 151 N ATOM 1244 CA ARG A 159 11.286 23.553 34.630 1.00 8.21 C ANISOU 1244 CA ARG A 159 1090 1109 920 146 52 170 C ATOM 1245 C ARG A 159 11.230 23.837 36.125 1.00 8.97 C ANISOU 1245 C ARG A 159 1069 1402 937 156 65 94 C ATOM 1246 O ARG A 159 10.537 24.743 36.579 1.00 10.94 O ANISOU 1246 O ARG A 159 1474 1669 1012 390 100 12 O ATOM 1247 CB ARG A 159 10.342 22.387 34.249 1.00 9.11 C ANISOU 1247 CB ARG A 159 1168 1252 1040 -11 70 240 C ATOM 1248 CG ARG A 159 8.953 22.458 34.864 1.00 9.85 C ANISOU 1248 CG ARG A 159 1082 1462 1197 -209 51 311 C ATOM 1249 CD ARG A 159 8.049 23.569 34.330 1.00 10.23 C ANISOU 1249 CD ARG A 159 1009 1785 1093 33 128 170 C ATOM 1250 NE ARG A 159 7.281 23.158 33.165 1.00 11.13 N ANISOU 1250 NE ARG A 159 1217 1822 1188 -211 -42 378 N ATOM 1251 CZ ARG A 159 7.235 23.736 31.973 1.00 10.03 C ANISOU 1251 CZ ARG A 159 1045 1739 1027 -80 71 143 C ATOM 1252 NH1 ARG A 159 7.967 24.803 31.680 1.00 10.89 N ANISOU 1252 NH1 ARG A 159 1348 1792 998 -223 91 189 N ATOM 1253 NH2 ARG A 159 6.448 23.231 31.027 1.00 11.97 N ANISOU 1253 NH2 ARG A 159 1477 1724 1347 -246 -306 233 N ATOM 1254 N ALA A 160 11.957 23.021 36.904 1.00 9.18 N ANISOU 1254 N ALA A 160 1123 1581 783 154 103 204 N ATOM 1255 CA ALA A 160 11.963 23.182 38.356 1.00 10.69 C ANISOU 1255 CA ALA A 160 1423 1803 835 -8 0 322 C ATOM 1256 C ALA A 160 12.717 24.424 38.795 1.00 10.42 C ANISOU 1256 C ALA A 160 1372 1689 899 159 91 39 C ATOM 1257 O ALA A 160 12.367 25.024 39.820 1.00 14.12 O ANISOU 1257 O ALA A 160 1978 2254 1134 12 250 -263 O ATOM 1258 CB ALA A 160 12.564 21.927 38.989 1.00 12.56 C ANISOU 1258 CB ALA A 160 1829 1906 1039 -107 -198 595 C ATOM 1259 N ALA A 161 13.749 24.824 38.054 1.00 9.72 N ANISOU 1259 N ALA A 161 1464 1401 827 -22 7 89 N ATOM 1260 CA ALA A 161 14.549 25.993 38.426 1.00 10.46 C ANISOU 1260 CA ALA A 161 1637 1366 972 54 7 -50 C ATOM 1261 C ALA A 161 13.788 27.298 38.247 1.00 10.51 C ANISOU 1261 C ALA A 161 1475 1464 1055 91 -105 -141 C ATOM 1262 O ALA A 161 13.936 28.227 39.061 1.00 14.24 O ANISOU 1262 O ALA A 161 2395 1693 1320 223 -359 -387 O ATOM 1263 CB ALA A 161 15.854 25.996 37.634 1.00 11.95 C ANISOU 1263 CB ALA A 161 1612 1569 1358 73 62 62 C ATOM 1264 N ASP A 162 12.987 27.432 37.191 1.00 10.37 N ANISOU 1264 N ASP A 162 1524 1494 922 252 -80 -21 N ATOM 1265 CA ASP A 162 12.196 28.640 36.976 1.00 10.81 C ANISOU 1265 CA ASP A 162 1516 1424 1168 210 131 -29 C ATOM 1266 C ASP A 162 10.906 28.271 36.258 1.00 11.03 C ANISOU 1266 C ASP A 162 1592 1471 1127 205 78 90 C ATOM 1267 O ASP A 162 10.851 28.265 35.027 1.00 11.33 O ANISOU 1267 O ASP A 162 1531 1643 1131 117 31 -73 O ATOM 1268 CB ASP A 162 12.949 29.737 36.219 1.00 12.54 C ANISOU 1268 CB ASP A 162 1780 1597 1388 89 49 137 C ATOM 1269 CG ASP A 162 12.164 31.039 36.106 1.00 12.31 C ANISOU 1269 CG ASP A 162 1841 1652 1186 112 -17 -15 C ATOM 1270 OD1 ASP A 162 11.010 31.080 36.601 1.00 14.20 O ANISOU 1270 OD1 ASP A 162 2000 1614 1780 355 258 8 O ATOM 1271 OD2 ASP A 162 12.717 32.006 35.528 1.00 15.28 O ANISOU 1271 OD2 ASP A 162 2435 1677 1692 82 3 202 O ATOM 1272 N PRO A 163 9.839 27.976 37.003 1.00 12.07 N ANISOU 1272 N PRO A 163 1557 1784 1244 93 70 148 N ATOM 1273 CA PRO A 163 8.561 27.603 36.404 1.00 13.59 C ANISOU 1273 CA PRO A 163 1420 2130 1612 -5 199 83 C ATOM 1274 C PRO A 163 7.883 28.673 35.561 1.00 14.34 C ANISOU 1274 C PRO A 163 1510 2204 1733 232 157 -25 C ATOM 1275 O PRO A 163 6.957 28.350 34.805 1.00 18.42 O ANISOU 1275 O PRO A 163 1936 2926 2137 88 -184 -29 O ATOM 1276 CB PRO A 163 7.680 27.210 37.596 1.00 18.29 C ANISOU 1276 CB PRO A 163 1622 3034 2294 -160 559 481 C ATOM 1277 CG PRO A 163 8.616 26.973 38.724 1.00 20.60 C ANISOU 1277 CG PRO A 163 2314 3372 2139 -155 307 229 C ATOM 1278 CD PRO A 163 9.823 27.839 38.479 1.00 16.12 C ANISOU 1278 CD PRO A 163 1936 2928 1262 172 144 161 C ATOM 1279 N SER A 164 8.334 29.934 35.616 1.00 13.51 N ANISOU 1279 N SER A 164 1747 2009 1379 446 304 14 N ATOM 1280 CA SER A 164 7.745 31.008 34.840 1.00 14.44 C ANISOU 1280 CA SER A 164 1678 2210 1597 415 201 173 C ATOM 1281 C SER A 164 8.288 31.129 33.418 1.00 13.68 C ANISOU 1281 C SER A 164 1554 2120 1523 460 155 -73 C ATOM 1282 O SER A 164 7.650 31.782 32.588 1.00 18.19 O ANISOU 1282 O SER A 164 2082 2969 1859 919 84 258 O ATOM 1283 CB ASER A 164 7.915 32.356 35.552 0.50 14.59 C ANISOU 1283 CB ASER A 164 2010 2053 1481 756 281 240 C ATOM 1284 OG ASER A 164 9.246 32.830 35.505 0.50 15.49 O ANISOU 1284 OG ASER A 164 2332 1821 1732 310 -155 -16 O ATOM 1285 CB BSER A 164 7.985 32.352 35.548 0.50 19.64 C ANISOU 1285 CB BSER A 164 2837 2250 2374 350 15 -42 C ATOM 1286 OG BSER A 164 7.309 32.347 36.792 0.50 25.96 O ANISOU 1286 OG BSER A 164 3835 3487 2541 284 426 -303 O ATOM 1287 N ALA A 165 9.422 30.531 33.103 1.00 11.33 N ANISOU 1287 N ALA A 165 1405 1678 1221 272 91 -153 N ATOM 1288 CA ALA A 165 10.038 30.631 31.791 1.00 10.60 C ANISOU 1288 CA ALA A 165 1506 1305 1215 104 106 -95 C ATOM 1289 C ALA A 165 9.481 29.628 30.793 1.00 10.20 C ANISOU 1289 C ALA A 165 1434 1227 1214 107 116 -56 C ATOM 1290 O ALA A 165 9.148 28.496 31.143 1.00 13.18 O ANISOU 1290 O ALA A 165 2292 1462 1252 -267 -99 217 O ATOM 1291 CB ALA A 165 11.552 30.383 31.914 1.00 14.32 C ANISOU 1291 CB ALA A 165 1454 2102 1884 -78 -15 -393 C ATOM 1292 N LYS A 166 9.363 30.035 29.531 1.00 8.86 N ANISOU 1292 N LYS A 166 1137 1011 1220 -4 143 -64 N ATOM 1293 CA LYS A 166 9.046 29.117 28.444 1.00 8.05 C ANISOU 1293 CA LYS A 166 950 1102 1006 69 170 -38 C ATOM 1294 C LYS A 166 10.346 28.403 28.017 1.00 7.23 C ANISOU 1294 C LYS A 166 863 973 911 -16 162 19 C ATOM 1295 O LYS A 166 11.364 29.059 27.746 1.00 10.14 O ANISOU 1295 O LYS A 166 1060 969 1823 -86 307 40 O ATOM 1296 CB LYS A 166 8.412 29.828 27.252 1.00 9.99 C ANISOU 1296 CB LYS A 166 1068 1445 1281 165 32 145 C ATOM 1297 CG LYS A 166 7.002 30.319 27.496 1.00 14.67 C ANISOU 1297 CG LYS A 166 1446 2172 1958 855 -3 5 C ATOM 1298 CD LYS A 166 6.256 30.788 26.260 1.00 19.04 C ANISOU 1298 CD LYS A 166 2301 2707 2226 1100 -322 112 C ATOM 1299 CE LYS A 166 4.791 31.079 26.580 1.00 24.08 C ANISOU 1299 CE LYS A 166 2381 3461 3308 1057 -71 -401 C ATOM 1300 NZ LYS A 166 3.987 31.490 25.415 1.00 25.74 N ANISOU 1300 NZ LYS A 166 3244 3611 2926 535 -234 -441 N ATOM 1301 N LEU A 167 10.302 27.074 27.966 1.00 6.85 N ANISOU 1301 N LEU A 167 763 951 888 -45 98 6 N ATOM 1302 CA LEU A 167 11.481 26.254 27.685 1.00 6.57 C ANISOU 1302 CA LEU A 167 794 929 775 -25 72 -7 C ATOM 1303 C LEU A 167 11.508 25.764 26.251 1.00 6.08 C ANISOU 1303 C LEU A 167 747 829 735 -27 18 -5 C ATOM 1304 O LEU A 167 10.597 25.043 25.813 1.00 7.90 O ANISOU 1304 O LEU A 167 963 1150 888 -247 30 -33 O ATOM 1305 CB LEU A 167 11.507 25.043 28.642 1.00 7.50 C ANISOU 1305 CB LEU A 167 893 1051 904 61 79 62 C ATOM 1306 CG LEU A 167 11.415 25.370 30.133 1.00 8.65 C ANISOU 1306 CG LEU A 167 1124 1324 837 153 137 107 C ATOM 1307 CD1 LEU A 167 11.459 24.060 30.921 1.00 11.67 C ANISOU 1307 CD1 LEU A 167 1735 1552 1145 118 -109 320 C ATOM 1308 CD2 LEU A 167 12.482 26.344 30.596 1.00 10.13 C ANISOU 1308 CD2 LEU A 167 1266 1716 866 168 -124 -138 C ATOM 1309 N CYS A 168 12.514 26.186 25.471 1.00 6.35 N ANISOU 1309 N CYS A 168 689 1027 697 -19 27 10 N ATOM 1310 CA CYS A 168 12.623 25.847 24.065 1.00 6.36 C ANISOU 1310 CA CYS A 168 863 848 704 -53 71 44 C ATOM 1311 C CYS A 168 13.774 24.871 23.738 1.00 5.94 C ANISOU 1311 C CYS A 168 780 788 691 -124 -3 188 C ATOM 1312 O CYS A 168 14.860 24.915 24.354 1.00 7.56 O ANISOU 1312 O CYS A 168 831 1120 923 -7 -112 -83 O ATOM 1313 CB CYS A 168 12.885 27.091 23.197 1.00 7.05 C ANISOU 1313 CB CYS A 168 930 865 883 -28 30 56 C ATOM 1314 SG CYS A 168 11.741 28.500 23.364 1.00 7.79 S ANISOU 1314 SG CYS A 168 963 796 1202 40 21 135 S ATOM 1315 N TYR A 169 13.529 24.019 22.728 1.00 6.30 N ANISOU 1315 N TYR A 169 747 873 774 -44 67 2 N ATOM 1316 CA TYR A 169 14.550 23.275 21.997 1.00 6.18 C ANISOU 1316 CA TYR A 169 754 883 712 -72 130 23 C ATOM 1317 C TYR A 169 14.876 24.098 20.749 1.00 6.10 C ANISOU 1317 C TYR A 169 718 812 788 37 -5 126 C ATOM 1318 O TYR A 169 13.931 24.486 20.059 1.00 9.28 O ANISOU 1318 O TYR A 169 775 1605 1143 93 4 570 O ATOM 1319 CB TYR A 169 14.030 21.848 21.622 1.00 6.89 C ANISOU 1319 CB TYR A 169 871 922 825 -196 62 -31 C ATOM 1320 CG TYR A 169 15.090 21.126 20.796 1.00 6.41 C ANISOU 1320 CG TYR A 169 838 735 862 -56 51 -3 C ATOM 1321 CD1 TYR A 169 16.213 20.581 21.420 1.00 8.49 C ANISOU 1321 CD1 TYR A 169 1088 1213 926 115 -54 16 C ATOM 1322 CD2 TYR A 169 15.016 21.079 19.414 1.00 6.89 C ANISOU 1322 CD2 TYR A 169 888 859 869 -52 21 55 C ATOM 1323 CE1 TYR A 169 17.250 20.046 20.658 1.00 8.67 C ANISOU 1323 CE1 TYR A 169 977 1302 1017 266 -129 83 C ATOM 1324 CE2 TYR A 169 16.044 20.525 18.651 1.00 6.62 C ANISOU 1324 CE2 TYR A 169 894 949 672 -50 33 61 C ATOM 1325 CZ TYR A 169 17.160 20.011 19.286 1.00 7.36 C ANISOU 1325 CZ TYR A 169 947 884 965 39 36 64 C ATOM 1326 OH TYR A 169 18.244 19.518 18.571 1.00 8.65 O ANISOU 1326 OH TYR A 169 979 1095 1214 259 13 4 O ATOM 1327 N ASN A 170 16.153 24.318 20.391 1.00 5.78 N ANISOU 1327 N ASN A 170 703 750 742 -13 15 104 N ATOM 1328 CA ASN A 170 16.554 25.176 19.262 1.00 5.79 C ANISOU 1328 CA ASN A 170 793 712 694 -30 82 29 C ATOM 1329 C ASN A 170 17.485 24.425 18.313 1.00 5.58 C ANISOU 1329 C ASN A 170 772 641 708 7 3 40 C ATOM 1330 O ASN A 170 18.411 23.747 18.785 1.00 7.50 O ANISOU 1330 O ASN A 170 959 1123 769 293 14 54 O ATOM 1331 CB ASN A 170 17.244 26.424 19.851 1.00 6.14 C ANISOU 1331 CB ASN A 170 844 770 718 6 57 35 C ATOM 1332 CG ASN A 170 17.484 27.558 18.872 1.00 6.54 C ANISOU 1332 CG ASN A 170 982 783 722 74 7 35 C ATOM 1333 OD1 ASN A 170 16.540 28.022 18.216 1.00 8.60 O ANISOU 1333 OD1 ASN A 170 1033 977 1256 29 2 403 O ATOM 1334 ND2 ASN A 170 18.733 28.003 18.742 1.00 8.37 N ANISOU 1334 ND2 ASN A 170 1037 1054 1090 -130 46 315 N ATOM 1335 N ASP A 171 17.274 24.542 17.006 1.00 6.11 N ANISOU 1335 N ASP A 171 845 841 637 125 55 7 N ATOM 1336 CA ASP A 171 18.147 23.854 16.029 1.00 6.23 C ANISOU 1336 CA ASP A 171 898 723 745 49 186 17 C ATOM 1337 C ASP A 171 18.065 24.559 14.658 1.00 5.63 C ANISOU 1337 C ASP A 171 734 643 762 60 36 -15 C ATOM 1338 O ASP A 171 17.202 25.427 14.464 1.00 6.88 O ANISOU 1338 O ASP A 171 957 749 910 160 194 100 O ATOM 1339 CB ASP A 171 17.816 22.356 15.952 1.00 6.48 C ANISOU 1339 CB ASP A 171 927 725 809 45 100 2 C ATOM 1340 CG ASP A 171 19.002 21.425 15.737 1.00 6.87 C ANISOU 1340 CG ASP A 171 1026 691 892 30 112 -5 C ATOM 1341 OD1 ASP A 171 19.997 21.862 15.104 1.00 7.39 O ANISOU 1341 OD1 ASP A 171 982 863 965 113 130 53 O ATOM 1342 OD2 ASP A 171 18.927 20.235 16.154 1.00 8.47 O ANISOU 1342 OD2 ASP A 171 1298 758 1161 144 218 41 O ATOM 1343 N TYR A 172 18.956 24.144 13.748 1.00 6.52 N ANISOU 1343 N TYR A 172 853 865 758 146 149 80 N ATOM 1344 CA TYR A 172 19.028 24.674 12.385 1.00 6.85 C ANISOU 1344 CA TYR A 172 1095 747 759 81 200 53 C ATOM 1345 C TYR A 172 18.869 23.516 11.401 1.00 6.61 C ANISOU 1345 C TYR A 172 991 731 789 23 178 64 C ATOM 1346 O TYR A 172 18.991 22.336 11.763 1.00 7.25 O ANISOU 1346 O TYR A 172 1045 873 836 11 109 23 O ATOM 1347 CB TYR A 172 20.372 25.421 12.121 1.00 7.47 C ANISOU 1347 CB TYR A 172 1135 817 887 -40 110 110 C ATOM 1348 CG TYR A 172 21.581 24.503 12.116 1.00 7.42 C ANISOU 1348 CG TYR A 172 853 974 992 -95 83 -15 C ATOM 1349 CD1 TYR A 172 22.255 24.161 13.290 1.00 8.29 C ANISOU 1349 CD1 TYR A 172 997 1109 1043 56 26 -20 C ATOM 1350 CD2 TYR A 172 22.054 23.930 10.932 1.00 8.46 C ANISOU 1350 CD2 TYR A 172 1055 1070 1091 66 153 6 C ATOM 1351 CE1 TYR A 172 23.316 23.265 13.291 1.00 9.25 C ANISOU 1351 CE1 TYR A 172 1070 1220 1225 77 117 25 C ATOM 1352 CE2 TYR A 172 23.118 23.051 10.935 1.00 9.04 C ANISOU 1352 CE2 TYR A 172 1004 1309 1122 111 152 -143 C ATOM 1353 CZ TYR A 172 23.755 22.695 12.109 1.00 8.90 C ANISOU 1353 CZ TYR A 172 975 1085 1323 118 78 -10 C ATOM 1354 OH TYR A 172 24.797 21.792 12.124 1.00 11.51 O ANISOU 1354 OH TYR A 172 1321 1418 1635 398 78 -1 O ATOM 1355 N ASN A 173 18.571 23.845 10.140 1.00 7.29 N ANISOU 1355 N ASN A 173 1093 862 814 14 113 48 N ATOM 1356 CA ASN A 173 18.337 22.826 9.107 1.00 7.55 C ANISOU 1356 CA ASN A 173 971 1043 857 74 19 -25 C ATOM 1357 C ASN A 173 17.128 21.942 9.449 1.00 7.10 C ANISOU 1357 C ASN A 173 1077 980 641 68 29 -130 C ATOM 1358 O ASN A 173 17.091 20.769 9.045 1.00 9.28 O ANISOU 1358 O ASN A 173 1331 1157 1039 -50 155 -250 O ATOM 1359 CB ASN A 173 19.560 21.985 8.744 1.00 9.56 C ANISOU 1359 CB ASN A 173 1171 1246 1214 113 124 -235 C ATOM 1360 CG ASN A 173 20.588 22.700 7.912 1.00 11.70 C ANISOU 1360 CG ASN A 173 1336 1953 1155 263 260 96 C ATOM 1361 OD1 ASN A 173 20.370 23.786 7.402 1.00 18.46 O ANISOU 1361 OD1 ASN A 173 2196 2697 2123 503 670 1100 O ATOM 1362 ND2 ASN A 173 21.750 22.072 7.769 1.00 14.61 N ANISOU 1362 ND2 ASN A 173 1375 2329 1846 325 686 38 N ATOM 1363 N VAL A 174 16.135 22.541 10.125 1.00 7.34 N ANISOU 1363 N VAL A 174 934 984 869 67 63 -143 N ATOM 1364 CA VAL A 174 14.909 21.868 10.552 1.00 7.82 C ANISOU 1364 CA VAL A 174 1050 964 958 -45 -2 47 C ATOM 1365 C VAL A 174 13.671 22.601 10.050 1.00 7.48 C ANISOU 1365 C VAL A 174 937 1079 825 -80 29 -41 C ATOM 1366 O VAL A 174 12.563 22.430 10.591 1.00 9.16 O ANISOU 1366 O VAL A 174 1020 1210 1251 -11 138 56 O ATOM 1367 CB VAL A 174 14.893 21.671 12.090 1.00 8.27 C ANISOU 1367 CB VAL A 174 1015 1133 994 19 101 57 C ATOM 1368 CG1 VAL A 174 15.891 20.610 12.539 1.00 9.41 C ANISOU 1368 CG1 VAL A 174 1264 1204 1108 76 -16 109 C ATOM 1369 CG2 VAL A 174 15.130 22.998 12.815 1.00 8.77 C ANISOU 1369 CG2 VAL A 174 1049 1185 1097 56 -64 16 C ATOM 1370 N GLU A 175 13.830 23.439 9.014 1.00 7.60 N ANISOU 1370 N GLU A 175 1011 981 896 -68 16 -95 N ATOM 1371 CA GLU A 175 12.738 24.257 8.489 1.00 7.78 C ANISOU 1371 CA GLU A 175 973 1116 866 -68 -25 -93 C ATOM 1372 C GLU A 175 11.921 23.602 7.376 1.00 8.06 C ANISOU 1372 C GLU A 175 1029 953 1079 47 -170 -102 C ATOM 1373 O GLU A 175 10.726 23.885 7.201 1.00 10.45 O ANISOU 1373 O GLU A 175 1087 1644 1238 184 -143 -371 O ATOM 1374 CB GLU A 175 13.288 25.632 8.048 1.00 8.59 C ANISOU 1374 CB GLU A 175 1220 1138 905 -88 -64 -67 C ATOM 1375 CG GLU A 175 13.959 26.433 9.166 1.00 9.44 C ANISOU 1375 CG GLU A 175 1294 1222 1069 -206 -113 -111 C ATOM 1376 CD GLU A 175 15.386 26.086 9.518 1.00 9.12 C ANISOU 1376 CD GLU A 175 1313 1052 1099 -219 -96 -13 C ATOM 1377 OE1 GLU A 175 16.088 25.411 8.725 1.00 11.45 O ANISOU 1377 OE1 GLU A 175 1241 1772 1338 -23 101 -42 O ATOM 1378 OE2 GLU A 175 15.861 26.489 10.610 1.00 12.04 O ANISOU 1378 OE2 GLU A 175 1822 1111 1640 -208 -596 -125 O ATOM 1379 N ASN A 176 12.561 22.750 6.577 1.00 8.35 N ANISOU 1379 N ASN A 176 1024 1113 1035 40 -147 -148 N ATOM 1380 CA ASN A 176 11.908 22.063 5.452 1.00 8.83 C ANISOU 1380 CA ASN A 176 1346 1220 791 -76 16 -163 C ATOM 1381 C ASN A 176 11.222 20.803 5.985 1.00 8.40 C ANISOU 1381 C ASN A 176 1127 1025 1039 14 57 -236 C ATOM 1382 O ASN A 176 11.879 19.902 6.527 1.00 9.52 O ANISOU 1382 O ASN A 176 1362 1152 1102 -67 -167 -65 O ATOM 1383 CB ASN A 176 12.941 21.772 4.374 1.00 10.12 C ANISOU 1383 CB ASN A 176 1549 1346 951 -122 171 -134 C ATOM 1384 CG ASN A 176 12.351 21.168 3.110 1.00 10.39 C ANISOU 1384 CG ASN A 176 1687 1237 1024 -17 86 -142 C ATOM 1385 OD1 ASN A 176 11.465 20.311 3.152 1.00 11.43 O ANISOU 1385 OD1 ASN A 176 1743 1541 1057 -99 85 -251 O ATOM 1386 ND2 ASN A 176 12.892 21.605 1.971 1.00 14.15 N ANISOU 1386 ND2 ASN A 176 2313 1962 1101 -265 287 -155 N ATOM 1387 N TRP A 177 9.903 20.710 5.812 1.00 9.13 N ANISOU 1387 N TRP A 177 1159 1381 928 -85 61 -77 N ATOM 1388 CA TRP A 177 9.115 19.609 6.355 1.00 9.77 C ANISOU 1388 CA TRP A 177 1278 1307 1127 -179 -33 -103 C ATOM 1389 C TRP A 177 9.589 18.236 5.908 1.00 11.14 C ANISOU 1389 C TRP A 177 1411 1325 1497 -106 57 -20 C ATOM 1390 O TRP A 177 9.420 17.233 6.634 1.00 14.42 O ANISOU 1390 O TRP A 177 1858 1487 2135 -43 358 267 O ATOM 1391 CB TRP A 177 7.626 19.813 5.969 1.00 10.87 C ANISOU 1391 CB TRP A 177 1330 1615 1186 -198 -94 -80 C ATOM 1392 CG TRP A 177 6.710 18.741 6.501 1.00 12.19 C ANISOU 1392 CG TRP A 177 1431 1838 1365 -442 29 -257 C ATOM 1393 CD1 TRP A 177 5.928 17.914 5.737 1.00 15.01 C ANISOU 1393 CD1 TRP A 177 1788 2411 1505 -812 -46 -309 C ATOM 1394 CD2 TRP A 177 6.462 18.384 7.871 1.00 12.23 C ANISOU 1394 CD2 TRP A 177 1434 1786 1429 -283 49 -155 C ATOM 1395 NE1 TRP A 177 5.229 17.069 6.567 1.00 16.79 N ANISOU 1395 NE1 TRP A 177 1923 2635 1823 -1045 -35 -233 N ATOM 1396 CE2 TRP A 177 5.532 17.320 7.874 1.00 14.77 C ANISOU 1396 CE2 TRP A 177 1755 2077 1781 -531 -75 -150 C ATOM 1397 CE3 TRP A 177 6.939 18.854 9.101 1.00 12.50 C ANISOU 1397 CE3 TRP A 177 1496 1775 1479 -265 62 -219 C ATOM 1398 CZ2 TRP A 177 5.084 16.722 9.050 1.00 16.72 C ANISOU 1398 CZ2 TRP A 177 2073 2116 2165 -635 180 6 C ATOM 1399 CZ3 TRP A 177 6.495 18.258 10.272 1.00 14.61 C ANISOU 1399 CZ3 TRP A 177 1761 2007 1782 -185 335 -106 C ATOM 1400 CH2 TRP A 177 5.576 17.200 10.238 1.00 15.81 C ANISOU 1400 CH2 TRP A 177 2049 1863 2095 -191 187 -2 C ATOM 1401 N THR A 178 10.173 18.108 4.714 1.00 11.14 N ANISOU 1401 N THR A 178 1677 1318 1239 -167 -189 -295 N ATOM 1402 CA THR A 178 10.554 16.827 4.148 1.00 12.63 C ANISOU 1402 CA THR A 178 1930 1281 1587 -129 -310 -395 C ATOM 1403 C THR A 178 11.914 16.306 4.590 1.00 12.80 C ANISOU 1403 C THR A 178 1674 1336 1853 -90 87 -383 C ATOM 1404 O THR A 178 12.254 15.148 4.297 1.00 17.74 O ANISOU 1404 O THR A 178 2479 1594 2665 353 -593 -733 O ATOM 1405 CB THR A 178 10.509 16.840 2.596 1.00 15.83 C ANISOU 1405 CB THR A 178 2739 1631 1645 -113 -303 -460 C ATOM 1406 OG1 THR A 178 11.558 17.652 2.079 1.00 18.97 O ANISOU 1406 OG1 THR A 178 3483 1927 1796 -137 489 -353 O ATOM 1407 CG2 THR A 178 9.167 17.318 2.081 1.00 18.97 C ANISOU 1407 CG2 THR A 178 3305 2080 1823 180 -889 -525 C ATOM 1408 N TRP A 179 12.744 17.087 5.246 1.00 12.15 N ANISOU 1408 N TRP A 179 1671 1615 1329 4 63 -389 N ATOM 1409 CA TRP A 179 14.083 16.667 5.644 1.00 11.37 C ANISOU 1409 CA TRP A 179 1573 1346 1403 51 226 -264 C ATOM 1410 C TRP A 179 14.083 15.690 6.815 1.00 10.25 C ANISOU 1410 C TRP A 179 1413 1249 1231 -109 106 -416 C ATOM 1411 O TRP A 179 13.279 15.799 7.762 1.00 11.36 O ANISOU 1411 O TRP A 179 1464 1619 1232 12 80 -364 O ATOM 1412 CB TRP A 179 14.988 17.879 5.924 1.00 12.50 C ANISOU 1412 CB TRP A 179 1797 1441 1510 29 -50 -333 C ATOM 1413 CG TRP A 179 15.500 18.629 4.719 1.00 17.93 C ANISOU 1413 CG TRP A 179 2554 2314 1946 -188 -203 421 C ATOM 1414 CD1 TRP A 179 14.947 18.668 3.473 1.00 17.79 C ANISOU 1414 CD1 TRP A 179 2466 2595 1699 -32 76 -43 C ATOM 1415 CD2 TRP A 179 16.691 19.432 4.605 1.00 22.64 C ANISOU 1415 CD2 TRP A 179 3285 2710 2608 -822 -195 214 C ATOM 1416 NE1 TRP A 179 15.671 19.463 2.622 1.00 19.45 N ANISOU 1416 NE1 TRP A 179 2867 2250 2271 -83 79 143 N ATOM 1417 CE2 TRP A 179 16.768 19.922 3.290 1.00 23.95 C ANISOU 1417 CE2 TRP A 179 3383 3133 2584 -540 -290 298 C ATOM 1418 CE3 TRP A 179 17.726 19.785 5.466 1.00 24.50 C ANISOU 1418 CE3 TRP A 179 3005 3119 3186 -234 -410 -74 C ATOM 1419 CZ2 TRP A 179 17.806 20.738 2.831 1.00 27.34 C ANISOU 1419 CZ2 TRP A 179 3537 3568 3282 -719 108 96 C ATOM 1420 CZ3 TRP A 179 18.769 20.590 5.035 1.00 26.89 C ANISOU 1420 CZ3 TRP A 179 3372 3892 2951 -528 -63 -66 C ATOM 1421 CH2 TRP A 179 18.798 21.065 3.714 1.00 29.14 C ANISOU 1421 CH2 TRP A 179 3653 4333 3084 -421 -38 177 C ATOM 1422 N ALA A 180 15.020 14.729 6.797 1.00 10.65 N ANISOU 1422 N ALA A 180 1548 1306 1192 5 8 -314 N ATOM 1423 CA ALA A 180 15.176 13.765 7.875 1.00 11.11 C ANISOU 1423 CA ALA A 180 1695 1138 1386 -52 74 -304 C ATOM 1424 C ALA A 180 15.437 14.428 9.232 1.00 8.77 C ANISOU 1424 C ALA A 180 1041 1013 1279 -147 136 -220 C ATOM 1425 O ALA A 180 14.940 13.949 10.264 1.00 10.95 O ANISOU 1425 O ALA A 180 1534 1162 1466 -318 354 -197 O ATOM 1426 CB ALA A 180 16.301 12.780 7.561 1.00 12.98 C ANISOU 1426 CB ALA A 180 2109 1250 1575 206 94 -387 C ATOM 1427 N LYS A 181 16.216 15.518 9.259 1.00 8.90 N ANISOU 1427 N LYS A 181 1149 1067 1165 -191 97 -211 N ATOM 1428 CA LYS A 181 16.518 16.199 10.527 1.00 8.31 C ANISOU 1428 CA LYS A 181 1167 1031 961 -65 157 -101 C ATOM 1429 C LYS A 181 15.250 16.770 11.152 1.00 7.86 C ANISOU 1429 C LYS A 181 1075 1010 903 -138 18 -157 C ATOM 1430 O LYS A 181 14.994 16.662 12.358 1.00 8.95 O ANISOU 1430 O LYS A 181 1177 1244 980 -20 63 15 O ATOM 1431 CB LYS A 181 17.594 17.271 10.303 1.00 8.26 C ANISOU 1431 CB LYS A 181 1068 1030 1042 -12 79 53 C ATOM 1432 CG LYS A 181 18.300 17.743 11.565 1.00 7.96 C ANISOU 1432 CG LYS A 181 987 972 1064 -57 100 24 C ATOM 1433 CD LYS A 181 19.286 18.870 11.281 1.00 7.53 C ANISOU 1433 CD LYS A 181 864 939 1058 66 58 44 C ATOM 1434 CE LYS A 181 20.107 19.241 12.497 1.00 7.77 C ANISOU 1434 CE LYS A 181 987 888 1077 -8 6 62 C ATOM 1435 NZ LYS A 181 21.041 20.392 12.218 1.00 7.58 N ANISOU 1435 NZ LYS A 181 966 949 965 -23 68 7 N ATOM 1436 N THR A 182 14.395 17.380 10.323 1.00 7.93 N ANISOU 1436 N THR A 182 968 1207 839 -31 95 -181 N ATOM 1437 CA THR A 182 13.117 17.935 10.762 1.00 7.68 C ANISOU 1437 CA THR A 182 1034 989 898 -108 77 -180 C ATOM 1438 C THR A 182 12.240 16.845 11.374 1.00 7.88 C ANISOU 1438 C THR A 182 887 1212 896 -114 -10 -81 C ATOM 1439 O THR A 182 11.612 17.015 12.437 1.00 9.17 O ANISOU 1439 O THR A 182 1230 1238 1018 -126 139 -59 O ATOM 1440 CB THR A 182 12.358 18.604 9.600 1.00 8.15 C ANISOU 1440 CB THR A 182 1039 1212 845 -42 98 -142 C ATOM 1441 OG1 THR A 182 13.300 19.479 8.947 1.00 8.71 O ANISOU 1441 OG1 THR A 182 1089 1287 933 -47 37 28 O ATOM 1442 CG2 THR A 182 11.144 19.387 10.044 1.00 9.48 C ANISOU 1442 CG2 THR A 182 1118 1352 1130 87 60 14 C ATOM 1443 N GLN A 183 12.150 15.690 10.686 1.00 8.72 N ANISOU 1443 N GLN A 183 1155 1167 991 -218 86 -88 N ATOM 1444 CA GLN A 183 11.336 14.572 11.166 1.00 9.50 C ANISOU 1444 CA GLN A 183 1121 1136 1352 -170 8 -19 C ATOM 1445 C GLN A 183 11.875 13.961 12.450 1.00 9.51 C ANISOU 1445 C GLN A 183 1122 1301 1189 -92 71 -61 C ATOM 1446 O GLN A 183 11.065 13.535 13.302 1.00 10.95 O ANISOU 1446 O GLN A 183 1407 1445 1308 -250 146 70 O ATOM 1447 CB GLN A 183 11.156 13.550 10.039 1.00 11.61 C ANISOU 1447 CB GLN A 183 1453 1495 1462 -326 29 -218 C ATOM 1448 CG GLN A 183 10.296 14.056 8.882 1.00 12.11 C ANISOU 1448 CG GLN A 183 1774 1490 1339 -362 -18 -231 C ATOM 1449 CD GLN A 183 8.904 14.475 9.341 1.00 13.91 C ANISOU 1449 CD GLN A 183 1623 1713 1951 -239 -81 157 C ATOM 1450 OE1 GLN A 183 8.205 13.761 10.072 1.00 18.22 O ANISOU 1450 OE1 GLN A 183 1781 2519 2622 -419 -37 710 O ATOM 1451 NE2 GLN A 183 8.460 15.656 8.918 1.00 16.54 N ANISOU 1451 NE2 GLN A 183 2103 1782 2400 21 264 265 N ATOM 1452 N ALA A 184 13.189 13.934 12.670 1.00 9.70 N ANISOU 1452 N ALA A 184 1140 1319 1225 25 69 45 N ATOM 1453 CA ALA A 184 13.768 13.467 13.931 1.00 10.10 C ANISOU 1453 CA ALA A 184 1296 1189 1353 95 0 61 C ATOM 1454 C ALA A 184 13.354 14.401 15.076 1.00 9.33 C ANISOU 1454 C ALA A 184 1095 1264 1186 -60 10 85 C ATOM 1455 O ALA A 184 12.972 13.908 16.145 1.00 10.62 O ANISOU 1455 O ALA A 184 1401 1420 1215 -80 27 214 O ATOM 1456 CB ALA A 184 15.284 13.383 13.834 1.00 12.54 C ANISOU 1456 CB ALA A 184 1365 1859 1541 217 182 31 C ATOM 1457 N MET A 185 13.376 15.710 14.848 1.00 8.90 N ANISOU 1457 N MET A 185 1071 1231 1077 -13 200 -11 N ATOM 1458 CA MET A 185 12.928 16.669 15.862 1.00 8.71 C ANISOU 1458 CA MET A 185 1073 1245 993 -60 100 -11 C ATOM 1459 C MET A 185 11.447 16.514 16.159 1.00 8.82 C ANISOU 1459 C MET A 185 1003 1261 1088 -84 37 83 C ATOM 1460 O MET A 185 11.016 16.594 17.331 1.00 9.72 O ANISOU 1460 O MET A 185 1290 1327 1077 -291 -7 93 O ATOM 1461 CB MET A 185 13.314 18.092 15.419 1.00 9.21 C ANISOU 1461 CB MET A 185 1118 1288 1094 -87 4 140 C ATOM 1462 CG MET A 185 13.054 19.169 16.467 1.00 10.05 C ANISOU 1462 CG MET A 185 1466 1350 1003 -262 -143 89 C ATOM 1463 SD MET A 185 13.632 20.809 16.004 1.00 9.51 S ANISOU 1463 SD MET A 185 1168 1163 1280 -143 -116 26 S ATOM 1464 CE MET A 185 12.392 21.288 14.834 1.00 11.37 C ANISOU 1464 CE MET A 185 1466 1657 1198 -123 -144 25 C ATOM 1465 N TYR A 186 10.614 16.330 15.125 1.00 9.23 N ANISOU 1465 N TYR A 186 1011 1437 1059 -114 51 -63 N ATOM 1466 CA TYR A 186 9.176 16.112 15.285 1.00 9.67 C ANISOU 1466 CA TYR A 186 1028 1437 1207 -131 -61 46 C ATOM 1467 C TYR A 186 8.883 14.904 16.160 1.00 10.11 C ANISOU 1467 C TYR A 186 1206 1433 1204 -386 32 -79 C ATOM 1468 O TYR A 186 8.074 14.969 17.107 1.00 11.85 O ANISOU 1468 O TYR A 186 1289 1940 1274 -296 139 62 O ATOM 1469 CB TYR A 186 8.508 15.987 13.904 1.00 10.45 C ANISOU 1469 CB TYR A 186 1085 1624 1263 -108 -74 -13 C ATOM 1470 CG TYR A 186 7.000 15.854 13.924 1.00 10.24 C ANISOU 1470 CG TYR A 186 1076 1555 1262 -213 -159 -37 C ATOM 1471 CD1 TYR A 186 6.182 16.967 14.039 1.00 10.85 C ANISOU 1471 CD1 TYR A 186 1283 1570 1270 -139 2 -25 C ATOM 1472 CD2 TYR A 186 6.413 14.602 13.834 1.00 15.12 C ANISOU 1472 CD2 TYR A 186 1379 1467 2897 -108 -315 -446 C ATOM 1473 CE1 TYR A 186 4.793 16.826 14.056 1.00 12.09 C ANISOU 1473 CE1 TYR A 186 1279 1611 1704 -143 -59 -113 C ATOM 1474 CE2 TYR A 186 5.030 14.471 13.844 1.00 15.88 C ANISOU 1474 CE2 TYR A 186 1444 1698 2893 -365 78 -597 C ATOM 1475 CZ TYR A 186 4.225 15.575 13.954 1.00 13.71 C ANISOU 1475 CZ TYR A 186 1168 1868 2172 -288 -63 -357 C ATOM 1476 OH TYR A 186 2.845 15.404 13.963 1.00 17.47 O ANISOU 1476 OH TYR A 186 1215 2247 3177 -436 -8 -403 O ATOM 1477 N ASN A 187 9.528 13.771 15.901 1.00 10.56 N ANISOU 1477 N ASN A 187 1478 1350 1182 -400 84 -35 N ATOM 1478 CA ASN A 187 9.320 12.561 16.683 1.00 11.54 C ANISOU 1478 CA ASN A 187 1623 1451 1309 -589 -44 89 C ATOM 1479 C ASN A 187 9.751 12.742 18.127 1.00 9.78 C ANISOU 1479 C ASN A 187 1249 1225 1241 -339 115 16 C ATOM 1480 O ASN A 187 9.076 12.217 19.030 1.00 10.93 O ANISOU 1480 O ASN A 187 1437 1313 1402 -385 142 206 O ATOM 1481 CB ASN A 187 9.965 11.396 15.917 1.00 16.50 C ANISOU 1481 CB ASN A 187 3244 1194 1830 -554 375 42 C ATOM 1482 CG ASN A 187 9.048 11.048 14.736 1.00 23.69 C ANISOU 1482 CG ASN A 187 3489 2289 3224 -978 -277 -643 C ATOM 1483 OD1 ASN A 187 7.840 10.826 14.889 1.00 32.78 O ANISOU 1483 OD1 ASN A 187 3421 5069 3964 -652 -59 -606 O ATOM 1484 ND2 ASN A 187 9.573 10.986 13.523 1.00 31.82 N ANISOU 1484 ND2 ASN A 187 4289 4207 3593 -1025 311 -399 N ATOM 1485 N MET A 188 10.827 13.499 18.383 1.00 9.60 N ANISOU 1485 N MET A 188 1229 1308 1111 -325 71 66 N ATOM 1486 CA MET A 188 11.264 13.763 19.752 1.00 9.40 C ANISOU 1486 CA MET A 188 1144 1317 1109 -245 2 157 C ATOM 1487 C MET A 188 10.209 14.553 20.526 1.00 8.89 C ANISOU 1487 C MET A 188 1108 1222 1048 -273 -112 89 C ATOM 1488 O MET A 188 9.855 14.233 21.672 1.00 9.93 O ANISOU 1488 O MET A 188 1172 1524 1076 -289 -12 196 O ATOM 1489 CB MET A 188 12.610 14.494 19.780 1.00 10.39 C ANISOU 1489 CB MET A 188 999 1599 1351 -278 37 32 C ATOM 1490 CG MET A 188 13.124 14.801 21.181 1.00 11.75 C ANISOU 1490 CG MET A 188 1127 1967 1371 -353 -19 147 C ATOM 1491 SD MET A 188 14.555 15.901 21.247 1.00 16.39 S ANISOU 1491 SD MET A 188 1287 3362 1579 -943 44 -200 S ATOM 1492 CE MET A 188 13.768 17.448 20.836 1.00 21.80 C ANISOU 1492 CE MET A 188 2872 2611 2802 -1210 9 -115 C ATOM 1493 N VAL A 189 9.684 15.648 19.934 1.00 9.03 N ANISOU 1493 N VAL A 189 1215 1158 1057 -233 92 165 N ATOM 1494 CA VAL A 189 8.696 16.481 20.610 1.00 9.12 C ANISOU 1494 CA VAL A 189 1228 1093 1143 -153 52 252 C ATOM 1495 C VAL A 189 7.416 15.702 20.896 1.00 8.59 C ANISOU 1495 C VAL A 189 1092 1101 1071 -120 34 195 C ATOM 1496 O VAL A 189 6.841 15.787 21.993 1.00 9.71 O ANISOU 1496 O VAL A 189 1148 1346 1196 18 95 179 O ATOM 1497 CB VAL A 189 8.426 17.801 19.853 1.00 10.34 C ANISOU 1497 CB VAL A 189 1792 972 1164 -173 -31 128 C ATOM 1498 CG1 VAL A 189 7.348 18.623 20.557 1.00 13.52 C ANISOU 1498 CG1 VAL A 189 2351 1244 1542 261 165 118 C ATOM 1499 CG2 VAL A 189 9.714 18.604 19.717 1.00 12.72 C ANISOU 1499 CG2 VAL A 189 2140 1177 1516 -481 212 104 C ATOM 1500 N ARG A 190 6.968 14.891 19.926 1.00 9.35 N ANISOU 1500 N ARG A 190 1150 1110 1293 -115 -58 56 N ATOM 1501 CA ARG A 190 5.762 14.058 20.123 1.00 10.55 C ANISOU 1501 CA ARG A 190 1166 1404 1438 -204 -59 117 C ATOM 1502 C ARG A 190 5.950 13.102 21.299 1.00 10.22 C ANISOU 1502 C ARG A 190 1267 1222 1395 -162 -86 37 C ATOM 1503 O ARG A 190 5.063 12.937 22.165 1.00 11.37 O ANISOU 1503 O ARG A 190 1300 1494 1527 -167 -43 133 O ATOM 1504 CB ARG A 190 5.433 13.296 18.839 1.00 12.24 C ANISOU 1504 CB ARG A 190 1531 1564 1556 -156 -197 37 C ATOM 1505 CG AARG A 190 4.123 12.525 18.909 0.50 17.03 C ANISOU 1505 CG AARG A 190 1879 2074 2519 -550 -89 -92 C ATOM 1506 CD AARG A 190 3.662 12.099 17.520 0.50 23.96 C ANISOU 1506 CD AARG A 190 2859 3457 2786 -782 -549 -261 C ATOM 1507 NE AARG A 190 4.609 11.216 16.869 0.50 31.13 N ANISOU 1507 NE AARG A 190 3547 4532 3747 -42 -101 -298 N ATOM 1508 CZ AARG A 190 4.641 9.893 16.909 0.50 39.41 C ANISOU 1508 CZ AARG A 190 5281 4589 5105 62 -290 42 C ATOM 1509 NH1AARG A 190 3.743 9.198 17.592 0.50 42.92 N ANISOU 1509 NH1AARG A 190 5346 5414 5547 -115 -5 110 N ATOM 1510 NH2AARG A 190 5.597 9.255 16.241 0.50 40.44 N ANISOU 1510 NH2AARG A 190 5377 5038 4951 7 -157 -70 N ATOM 1511 CG BARG A 190 4.222 12.389 18.904 0.50 15.91 C ANISOU 1511 CG BARG A 190 1809 1966 2269 -459 -327 28 C ATOM 1512 CD BARG A 190 3.933 11.800 17.523 0.50 20.91 C ANISOU 1512 CD BARG A 190 2588 2835 2521 -492 -328 -437 C ATOM 1513 NE BARG A 190 2.834 10.845 17.564 0.50 24.07 N ANISOU 1513 NE BARG A 190 2937 2688 3521 -590 -136 -258 N ATOM 1514 CZ BARG A 190 2.982 9.545 17.782 0.50 25.90 C ANISOU 1514 CZ BARG A 190 2855 2930 4054 -115 -91 160 C ATOM 1515 NH1BARG A 190 4.181 9.004 17.965 0.50 29.51 N ANISOU 1515 NH1BARG A 190 3077 3742 4395 252 -138 282 N ATOM 1516 NH2BARG A 190 1.912 8.759 17.801 0.50 29.88 N ANISOU 1516 NH2BARG A 190 3154 3641 4558 -573 29 135 N ATOM 1517 N ASP A 191 7.099 12.427 21.382 1.00 9.44 N ANISOU 1517 N ASP A 191 1269 1077 1242 -225 -18 82 N ATOM 1518 CA ASP A 191 7.427 11.521 22.485 1.00 9.81 C ANISOU 1518 CA ASP A 191 1262 1189 1276 -164 51 185 C ATOM 1519 C ASP A 191 7.454 12.244 23.835 1.00 9.21 C ANISOU 1519 C ASP A 191 1198 1040 1260 -251 81 212 C ATOM 1520 O ASP A 191 6.889 11.769 24.837 1.00 10.10 O ANISOU 1520 O ASP A 191 1222 1242 1374 -301 126 201 O ATOM 1521 CB ASP A 191 8.780 10.858 22.198 1.00 11.45 C ANISOU 1521 CB ASP A 191 1557 1239 1554 46 144 155 C ATOM 1522 CG ASP A 191 9.338 10.007 23.327 1.00 14.36 C ANISOU 1522 CG ASP A 191 1691 1597 2166 164 93 619 C ATOM 1523 OD1 ASP A 191 8.625 9.132 23.829 1.00 17.39 O ANISOU 1523 OD1 ASP A 191 2181 1613 2815 108 230 865 O ATOM 1524 OD2 ASP A 191 10.493 10.240 23.730 1.00 19.99 O ANISOU 1524 OD2 ASP A 191 2125 2760 2709 -106 -526 744 O ATOM 1525 N PHE A 192 8.089 13.432 23.855 1.00 9.03 N ANISOU 1525 N PHE A 192 1078 1080 1271 -257 -25 216 N ATOM 1526 CA PHE A 192 8.134 14.227 25.102 1.00 9.06 C ANISOU 1526 CA PHE A 192 993 1100 1350 -167 -15 195 C ATOM 1527 C PHE A 192 6.736 14.592 25.593 1.00 8.42 C ANISOU 1527 C PHE A 192 995 1093 1110 -166 -102 114 C ATOM 1528 O PHE A 192 6.449 14.475 26.799 1.00 9.62 O ANISOU 1528 O PHE A 192 1035 1487 1133 -212 -67 74 O ATOM 1529 CB PHE A 192 8.984 15.483 24.870 1.00 9.42 C ANISOU 1529 CB PHE A 192 955 1206 1419 -246 -112 252 C ATOM 1530 CG PHE A 192 10.489 15.319 24.903 1.00 9.28 C ANISOU 1530 CG PHE A 192 991 1147 1386 -186 -149 179 C ATOM 1531 CD1 PHE A 192 11.122 14.086 24.971 1.00 11.48 C ANISOU 1531 CD1 PHE A 192 1075 1403 1882 47 -129 310 C ATOM 1532 CD2 PHE A 192 11.292 16.454 24.855 1.00 11.79 C ANISOU 1532 CD2 PHE A 192 1091 1298 2092 -308 -290 277 C ATOM 1533 CE1 PHE A 192 12.499 13.997 25.000 1.00 11.83 C ANISOU 1533 CE1 PHE A 192 1081 1403 2012 46 -72 220 C ATOM 1534 CE2 PHE A 192 12.666 16.364 24.891 1.00 14.07 C ANISOU 1534 CE2 PHE A 192 1119 1650 2575 -464 -202 255 C ATOM 1535 CZ PHE A 192 13.280 15.128 24.967 1.00 11.81 C ANISOU 1535 CZ PHE A 192 931 1887 1668 -256 -47 131 C ATOM 1536 N LYS A 193 5.839 15.009 24.710 1.00 8.75 N ANISOU 1536 N LYS A 193 852 1252 1222 -126 -69 116 N ATOM 1537 CA LYS A 193 4.470 15.335 25.135 1.00 9.17 C ANISOU 1537 CA LYS A 193 898 1251 1334 -85 -9 87 C ATOM 1538 C LYS A 193 3.743 14.118 25.715 1.00 9.93 C ANISOU 1538 C LYS A 193 820 1340 1613 -174 95 85 C ATOM 1539 O LYS A 193 3.024 14.208 26.739 1.00 11.75 O ANISOU 1539 O LYS A 193 1040 1713 1712 -153 233 116 O ATOM 1540 CB LYS A 193 3.681 15.934 23.961 1.00 10.31 C ANISOU 1540 CB LYS A 193 882 1644 1390 30 56 224 C ATOM 1541 CG LYS A 193 4.136 17.336 23.567 1.00 12.23 C ANISOU 1541 CG LYS A 193 1429 1555 1662 175 1 305 C ATOM 1542 CD LYS A 193 3.771 18.362 24.636 1.00 14.44 C ANISOU 1542 CD LYS A 193 1683 1758 2044 -154 168 -6 C ATOM 1543 CE LYS A 193 4.312 19.730 24.309 1.00 15.90 C ANISOU 1543 CE LYS A 193 2055 1922 2064 -411 257 -13 C ATOM 1544 NZ LYS A 193 4.115 20.722 25.391 1.00 14.93 N ANISOU 1544 NZ LYS A 193 1312 2031 2328 -666 371 -207 N ATOM 1545 N GLN A 194 3.881 12.952 25.084 1.00 9.67 N ANISOU 1545 N GLN A 194 1018 1307 1350 -349 72 155 N ATOM 1546 CA GLN A 194 3.215 11.749 25.578 1.00 10.23 C ANISOU 1546 CA GLN A 194 965 1423 1498 -321 141 281 C ATOM 1547 C GLN A 194 3.685 11.400 26.982 1.00 11.12 C ANISOU 1547 C GLN A 194 1239 1521 1467 -347 -4 227 C ATOM 1548 O GLN A 194 2.844 11.005 27.831 1.00 11.77 O ANISOU 1548 O GLN A 194 1338 1718 1415 -500 19 233 O ATOM 1549 CB GLN A 194 3.484 10.559 24.654 1.00 12.27 C ANISOU 1549 CB GLN A 194 1349 1437 1874 -371 -12 58 C ATOM 1550 CG GLN A 194 2.781 10.620 23.308 1.00 13.70 C ANISOU 1550 CG GLN A 194 1393 1683 2129 -253 -268 100 C ATOM 1551 CD GLN A 194 3.119 9.491 22.373 1.00 20.05 C ANISOU 1551 CD GLN A 194 2727 2178 2712 -203 -272 -485 C ATOM 1552 OE1 GLN A 194 4.188 8.888 22.425 1.00 25.90 O ANISOU 1552 OE1 GLN A 194 3410 2948 3482 586 -495 -1114 O ATOM 1553 NE2 GLN A 194 2.192 9.174 21.470 1.00 27.19 N ANISOU 1553 NE2 GLN A 194 2991 3542 3798 -363 -658 -1242 N ATOM 1554 N ARG A 195 4.989 11.501 27.252 1.00 11.03 N ANISOU 1554 N ARG A 195 1213 1466 1511 -295 20 386 N ATOM 1555 CA ARG A 195 5.595 11.089 28.504 1.00 12.16 C ANISOU 1555 CA ARG A 195 1498 1591 1533 -161 -8 469 C ATOM 1556 C ARG A 195 5.676 12.173 29.566 1.00 12.12 C ANISOU 1556 C ARG A 195 1234 1850 1523 -187 75 354 C ATOM 1557 O ARG A 195 6.212 11.920 30.659 1.00 17.26 O ANISOU 1557 O ARG A 195 2457 2364 1735 87 -384 390 O ATOM 1558 CB ARG A 195 6.998 10.480 28.255 1.00 12.22 C ANISOU 1558 CB ARG A 195 1513 1381 1748 -251 107 373 C ATOM 1559 CG ARG A 195 6.953 9.202 27.430 1.00 12.55 C ANISOU 1559 CG ARG A 195 1503 1387 1881 -295 -97 316 C ATOM 1560 CD ARG A 195 8.299 8.470 27.394 1.00 14.53 C ANISOU 1560 CD ARG A 195 1567 1780 2175 -188 72 294 C ATOM 1561 NE ARG A 195 9.344 9.225 26.705 1.00 14.41 N ANISOU 1561 NE ARG A 195 1460 1996 2017 -269 -155 419 N ATOM 1562 CZ ARG A 195 10.403 9.799 27.276 1.00 14.27 C ANISOU 1562 CZ ARG A 195 1915 1516 1991 -312 -264 219 C ATOM 1563 NH1 ARG A 195 10.648 9.733 28.572 1.00 17.03 N ANISOU 1563 NH1 ARG A 195 2188 2276 2006 -593 -455 244 N ATOM 1564 NH2 ARG A 195 11.231 10.471 26.495 1.00 15.56 N ANISOU 1564 NH2 ARG A 195 1849 1856 2209 -548 -252 203 N ATOM 1565 N GLY A 196 5.167 13.380 29.323 1.00 11.73 N ANISOU 1565 N GLY A 196 1193 1696 1568 -347 187 278 N ATOM 1566 CA GLY A 196 5.192 14.426 30.323 1.00 13.03 C ANISOU 1566 CA GLY A 196 1394 1916 1641 -352 76 102 C ATOM 1567 C GLY A 196 6.515 15.140 30.519 1.00 12.21 C ANISOU 1567 C GLY A 196 1315 1988 1334 -325 101 167 C ATOM 1568 O GLY A 196 6.735 15.749 31.577 1.00 15.51 O ANISOU 1568 O GLY A 196 1597 2789 1506 -431 258 -259 O ATOM 1569 N VAL A 197 7.415 15.107 29.544 1.00 10.07 N ANISOU 1569 N VAL A 197 1124 1531 1170 -382 -23 62 N ATOM 1570 CA VAL A 197 8.677 15.865 29.618 1.00 9.57 C ANISOU 1570 CA VAL A 197 984 1415 1237 -243 -136 63 C ATOM 1571 C VAL A 197 8.350 17.330 29.324 1.00 9.12 C ANISOU 1571 C VAL A 197 1010 1450 1005 -136 -47 111 C ATOM 1572 O VAL A 197 7.728 17.600 28.288 1.00 11.39 O ANISOU 1572 O VAL A 197 1354 1717 1257 -364 -320 322 O ATOM 1573 CB VAL A 197 9.704 15.337 28.607 1.00 10.50 C ANISOU 1573 CB VAL A 197 1149 1616 1225 -226 -65 -114 C ATOM 1574 CG1 VAL A 197 10.995 16.156 28.649 1.00 11.80 C ANISOU 1574 CG1 VAL A 197 1143 1631 1710 -217 115 -91 C ATOM 1575 CG2 VAL A 197 10.019 13.871 28.852 1.00 13.14 C ANISOU 1575 CG2 VAL A 197 1549 1636 1806 -121 -243 -177 C ATOM 1576 N PRO A 198 8.705 18.280 30.190 1.00 9.48 N ANISOU 1576 N PRO A 198 1159 1362 1083 -84 -114 127 N ATOM 1577 CA PRO A 198 8.321 19.676 29.985 1.00 9.76 C ANISOU 1577 CA PRO A 198 1097 1387 1223 -129 -23 228 C ATOM 1578 C PRO A 198 9.046 20.304 28.804 1.00 11.51 C ANISOU 1578 C PRO A 198 1190 1730 1454 -304 -83 485 C ATOM 1579 O PRO A 198 10.260 20.222 28.707 1.00 18.67 O ANISOU 1579 O PRO A 198 1229 3464 2400 -243 -107 1456 O ATOM 1580 CB PRO A 198 8.671 20.370 31.304 1.00 12.03 C ANISOU 1580 CB PRO A 198 1847 1503 1222 -285 15 203 C ATOM 1581 CG PRO A 198 9.586 19.462 32.015 1.00 14.42 C ANISOU 1581 CG PRO A 198 2428 1724 1325 85 -507 -204 C ATOM 1582 CD PRO A 198 9.412 18.073 31.480 1.00 10.70 C ANISOU 1582 CD PRO A 198 1391 1437 1237 135 -239 113 C ATOM 1583 N ILE A 199 8.339 20.751 27.808 1.00 9.69 N ANISOU 1583 N ILE A 199 1162 1316 1206 -454 -36 342 N ATOM 1584 CA ILE A 199 8.859 21.464 26.635 1.00 8.00 C ANISOU 1584 CA ILE A 199 881 1072 1085 -242 -101 269 C ATOM 1585 C ILE A 199 7.735 22.382 26.167 1.00 8.14 C ANISOU 1585 C ILE A 199 864 1155 1074 -137 -90 153 C ATOM 1586 O ILE A 199 6.621 21.914 25.882 1.00 11.37 O ANISOU 1586 O ILE A 199 977 1405 1939 -333 -232 264 O ATOM 1587 CB ILE A 199 9.429 20.567 25.519 1.00 8.98 C ANISOU 1587 CB ILE A 199 1048 1252 1113 -21 -141 211 C ATOM 1588 CG1 ILE A 199 9.939 21.420 24.346 1.00 10.17 C ANISOU 1588 CG1 ILE A 199 1184 1470 1212 -108 57 183 C ATOM 1589 CG2 ILE A 199 8.425 19.512 25.069 1.00 11.31 C ANISOU 1589 CG2 ILE A 199 1525 1192 1581 -252 68 33 C ATOM 1590 CD1 ILE A 199 10.774 20.663 23.337 1.00 12.59 C ANISOU 1590 CD1 ILE A 199 1291 1841 1652 -272 407 3 C ATOM 1591 N ASP A 200 8.009 23.686 26.105 1.00 7.37 N ANISOU 1591 N ASP A 200 871 1088 839 -125 -11 111 N ATOM 1592 CA ASP A 200 6.977 24.657 25.771 1.00 7.55 C ANISOU 1592 CA ASP A 200 885 1290 695 -108 -21 171 C ATOM 1593 C ASP A 200 7.075 25.246 24.395 1.00 7.00 C ANISOU 1593 C ASP A 200 895 1073 690 -13 97 139 C ATOM 1594 O ASP A 200 6.097 25.807 23.871 1.00 9.17 O ANISOU 1594 O ASP A 200 917 1637 932 57 8 249 O ATOM 1595 CB ASP A 200 7.065 25.848 26.761 1.00 7.95 C ANISOU 1595 CB ASP A 200 990 1162 868 -94 6 156 C ATOM 1596 CG ASP A 200 7.021 25.414 28.208 1.00 7.99 C ANISOU 1596 CG ASP A 200 984 1294 757 -194 89 89 C ATOM 1597 OD1 ASP A 200 6.065 24.690 28.584 1.00 12.45 O ANISOU 1597 OD1 ASP A 200 1202 2475 1052 -739 80 261 O ATOM 1598 OD2 ASP A 200 7.933 25.790 28.979 1.00 9.15 O ANISOU 1598 OD2 ASP A 200 1037 1638 803 -288 52 113 O ATOM 1599 N CYS A 201 8.242 25.157 23.731 1.00 7.53 N ANISOU 1599 N CYS A 201 872 1243 745 49 90 221 N ATOM 1600 CA CYS A 201 8.508 25.861 22.493 1.00 6.81 C ANISOU 1600 CA CYS A 201 834 1100 655 -105 43 23 C ATOM 1601 C CYS A 201 9.586 25.145 21.676 1.00 6.35 C ANISOU 1601 C CYS A 201 762 858 793 -98 -4 194 C ATOM 1602 O CYS A 201 10.473 24.494 22.229 1.00 7.40 O ANISOU 1602 O CYS A 201 896 1119 798 -6 -74 159 O ATOM 1603 CB CYS A 201 8.881 27.327 22.774 1.00 10.29 C ANISOU 1603 CB CYS A 201 1147 1400 1363 -379 377 -244 C ATOM 1604 SG ACYS A 201 9.918 27.815 24.081 0.50 7.44 S ANISOU 1604 SG ACYS A 201 884 1043 901 153 227 118 S ATOM 1605 SG BCYS A 201 10.306 28.156 22.040 0.50 7.76 S ANISOU 1605 SG BCYS A 201 911 984 1051 -34 -25 330 S ATOM 1606 N VAL A 202 9.499 25.362 20.357 1.00 6.66 N ANISOU 1606 N VAL A 202 735 1105 690 40 40 125 N ATOM 1607 CA VAL A 202 10.544 24.955 19.429 1.00 6.62 C ANISOU 1607 CA VAL A 202 757 964 794 -13 99 84 C ATOM 1608 C VAL A 202 11.049 26.197 18.688 1.00 6.65 C ANISOU 1608 C VAL A 202 728 983 817 55 74 115 C ATOM 1609 O VAL A 202 10.247 26.966 18.144 1.00 7.92 O ANISOU 1609 O VAL A 202 772 1144 1094 182 132 233 O ATOM 1610 CB VAL A 202 10.077 23.852 18.464 1.00 9.31 C ANISOU 1610 CB VAL A 202 1336 990 1213 -25 -20 -96 C ATOM 1611 CG1 VAL A 202 11.096 23.542 17.389 1.00 13.54 C ANISOU 1611 CG1 VAL A 202 1737 1916 1491 137 131 -545 C ATOM 1612 CG2 VAL A 202 9.762 22.560 19.228 1.00 12.92 C ANISOU 1612 CG2 VAL A 202 2049 1157 1703 -532 -128 25 C ATOM 1613 N GLY A 203 12.369 26.360 18.677 1.00 6.69 N ANISOU 1613 N GLY A 203 731 1034 776 -6 125 217 N ATOM 1614 CA GLY A 203 13.042 27.423 17.959 1.00 6.36 C ANISOU 1614 CA GLY A 203 728 907 781 19 108 167 C ATOM 1615 C GLY A 203 13.652 26.911 16.641 1.00 6.28 C ANISOU 1615 C GLY A 203 699 860 828 112 67 116 C ATOM 1616 O GLY A 203 14.415 25.949 16.633 1.00 8.51 O ANISOU 1616 O GLY A 203 1129 1151 954 339 72 167 O ATOM 1617 N PHE A 204 13.271 27.615 15.565 1.00 6.22 N ANISOU 1617 N PHE A 204 867 819 677 92 49 41 N ATOM 1618 CA PHE A 204 13.783 27.361 14.211 1.00 6.24 C ANISOU 1618 CA PHE A 204 818 860 692 66 65 16 C ATOM 1619 C PHE A 204 14.820 28.443 13.918 1.00 6.16 C ANISOU 1619 C PHE A 204 857 710 773 63 75 120 C ATOM 1620 O PHE A 204 14.456 29.616 13.752 1.00 6.83 O ANISOU 1620 O PHE A 204 919 777 901 70 100 100 O ATOM 1621 CB PHE A 204 12.625 27.408 13.187 1.00 7.11 C ANISOU 1621 CB PHE A 204 925 950 827 -50 -144 142 C ATOM 1622 CG PHE A 204 11.601 26.316 13.422 1.00 6.75 C ANISOU 1622 CG PHE A 204 855 912 799 17 -62 -21 C ATOM 1623 CD1 PHE A 204 10.547 26.475 14.307 1.00 7.80 C ANISOU 1623 CD1 PHE A 204 871 981 1113 -72 59 -155 C ATOM 1624 CD2 PHE A 204 11.708 25.085 12.763 1.00 7.93 C ANISOU 1624 CD2 PHE A 204 1011 991 1013 -67 -101 -136 C ATOM 1625 CE1 PHE A 204 9.629 25.470 14.528 1.00 9.75 C ANISOU 1625 CE1 PHE A 204 779 1447 1479 -254 159 -159 C ATOM 1626 CE2 PHE A 204 10.797 24.081 12.997 1.00 8.98 C ANISOU 1626 CE2 PHE A 204 1197 1077 1137 -209 -50 -72 C ATOM 1627 CZ PHE A 204 9.761 24.250 13.884 1.00 9.21 C ANISOU 1627 CZ PHE A 204 995 1277 1227 -350 -81 22 C ATOM 1628 N GLN A 205 16.104 28.076 13.901 1.00 6.21 N ANISOU 1628 N GLN A 205 809 598 952 11 42 35 N ATOM 1629 CA GLN A 205 17.141 29.112 13.717 1.00 5.87 C ANISOU 1629 CA GLN A 205 934 578 718 16 2 -64 C ATOM 1630 C GLN A 205 16.937 29.912 12.429 1.00 5.59 C ANISOU 1630 C GLN A 205 721 650 753 -50 95 10 C ATOM 1631 O GLN A 205 17.154 31.119 12.423 1.00 6.99 O ANISOU 1631 O GLN A 205 1117 732 806 -79 23 71 O ATOM 1632 CB GLN A 205 18.543 28.506 13.786 1.00 6.34 C ANISOU 1632 CB GLN A 205 846 755 809 76 34 -38 C ATOM 1633 CG GLN A 205 19.014 28.108 15.195 1.00 6.56 C ANISOU 1633 CG GLN A 205 852 805 837 28 -54 -14 C ATOM 1634 CD GLN A 205 20.431 27.588 15.216 1.00 6.67 C ANISOU 1634 CD GLN A 205 816 765 955 2 23 18 C ATOM 1635 OE1 GLN A 205 21.246 27.874 14.342 1.00 8.26 O ANISOU 1635 OE1 GLN A 205 843 1180 1117 49 68 187 O ATOM 1636 NE2 GLN A 205 20.758 26.764 16.209 1.00 8.13 N ANISOU 1636 NE2 GLN A 205 951 1001 1137 181 -46 157 N ATOM 1637 N SER A 206 16.549 29.239 11.347 1.00 6.18 N ANISOU 1637 N SER A 206 892 741 715 -26 -18 -10 N ATOM 1638 CA SER A 206 16.232 29.934 10.092 1.00 6.47 C ANISOU 1638 CA SER A 206 974 678 806 -44 -25 9 C ATOM 1639 C SER A 206 17.439 30.657 9.482 1.00 6.80 C ANISOU 1639 C SER A 206 1092 819 672 30 140 -16 C ATOM 1640 O SER A 206 17.322 31.795 8.988 1.00 7.96 O ANISOU 1640 O SER A 206 1190 900 936 7 251 64 O ATOM 1641 CB SER A 206 15.015 30.861 10.257 1.00 7.61 C ANISOU 1641 CB SER A 206 912 1052 928 7 2 180 C ATOM 1642 OG SER A 206 13.893 30.147 10.794 1.00 9.04 O ANISOU 1642 OG SER A 206 880 1233 1322 -71 71 171 O ATOM 1643 N HIS A 207 18.589 29.970 9.440 1.00 7.18 N ANISOU 1643 N HIS A 207 946 956 826 -17 168 40 N ATOM 1644 CA HIS A 207 19.753 30.435 8.665 1.00 7.49 C ANISOU 1644 CA HIS A 207 1106 1023 717 -24 229 -40 C ATOM 1645 C HIS A 207 19.567 29.938 7.228 1.00 8.70 C ANISOU 1645 C HIS A 207 1476 927 901 -55 163 -157 C ATOM 1646 O HIS A 207 19.955 28.817 6.885 1.00 14.43 O ANISOU 1646 O HIS A 207 2871 1300 1310 728 -197 -309 O ATOM 1647 CB HIS A 207 21.051 29.868 9.260 1.00 8.43 C ANISOU 1647 CB HIS A 207 1055 1102 1048 -73 237 -22 C ATOM 1648 CG HIS A 207 21.372 30.408 10.621 1.00 7.95 C ANISOU 1648 CG HIS A 207 900 1170 949 -2 248 -9 C ATOM 1649 ND1 HIS A 207 21.622 31.745 10.846 1.00 8.11 N ANISOU 1649 ND1 HIS A 207 1002 1107 971 53 95 -81 N ATOM 1650 CD2 HIS A 207 21.481 29.780 11.832 1.00 8.72 C ANISOU 1650 CD2 HIS A 207 1084 1169 1062 107 228 106 C ATOM 1651 CE1 HIS A 207 21.853 31.925 12.135 1.00 8.73 C ANISOU 1651 CE1 HIS A 207 1147 1185 986 114 149 -87 C ATOM 1652 NE2 HIS A 207 21.777 30.761 12.766 1.00 8.98 N ANISOU 1652 NE2 HIS A 207 1101 1435 875 75 97 135 N ATOM 1653 N PHE A 208 18.938 30.740 6.381 1.00 8.21 N ANISOU 1653 N PHE A 208 1265 1046 808 26 140 -165 N ATOM 1654 CA PHE A 208 18.659 30.357 4.991 1.00 8.83 C ANISOU 1654 CA PHE A 208 1533 978 842 -139 234 -160 C ATOM 1655 C PHE A 208 19.781 30.808 4.066 1.00 9.15 C ANISOU 1655 C PHE A 208 1296 1202 978 -89 227 -253 C ATOM 1656 O PHE A 208 20.243 31.961 4.107 1.00 11.31 O ANISOU 1656 O PHE A 208 1870 1305 1123 -259 461 -229 O ATOM 1657 CB PHE A 208 17.304 30.938 4.546 1.00 9.79 C ANISOU 1657 CB PHE A 208 1638 1224 859 -44 181 -12 C ATOM 1658 CG PHE A 208 16.093 30.421 5.277 1.00 8.93 C ANISOU 1658 CG PHE A 208 1327 1269 797 -12 -10 32 C ATOM 1659 CD1 PHE A 208 15.725 29.081 5.184 1.00 10.83 C ANISOU 1659 CD1 PHE A 208 1610 1479 1025 -288 150 -138 C ATOM 1660 CD2 PHE A 208 15.257 31.260 5.996 1.00 10.41 C ANISOU 1660 CD2 PHE A 208 1521 1239 1195 81 53 11 C ATOM 1661 CE1 PHE A 208 14.601 28.619 5.831 1.00 11.61 C ANISOU 1661 CE1 PHE A 208 1694 1483 1234 -306 134 6 C ATOM 1662 CE2 PHE A 208 14.131 30.795 6.654 1.00 11.22 C ANISOU 1662 CE2 PHE A 208 1464 1712 1086 103 -15 89 C ATOM 1663 CZ PHE A 208 13.787 29.460 6.563 1.00 11.57 C ANISOU 1663 CZ PHE A 208 1443 1884 1070 -193 63 36 C ATOM 1664 N ASN A 209 20.253 29.876 3.231 1.00 10.37 N ANISOU 1664 N ASN A 209 1705 1181 1053 -78 364 -259 N ATOM 1665 CA ASN A 209 21.363 30.160 2.305 1.00 10.54 C ANISOU 1665 CA ASN A 209 1512 1434 1059 -247 299 -449 C ATOM 1666 C ASN A 209 21.300 29.133 1.183 1.00 10.49 C ANISOU 1666 C ASN A 209 1449 1467 1071 -30 213 -374 C ATOM 1667 O ASN A 209 20.377 28.315 1.130 1.00 11.87 O ANISOU 1667 O ASN A 209 1532 1774 1204 -161 319 -485 O ATOM 1668 CB ASN A 209 22.690 30.179 3.055 1.00 14.00 C ANISOU 1668 CB ASN A 209 1850 2157 1315 -317 -47 -442 C ATOM 1669 CG ASN A 209 23.027 28.886 3.754 1.00 16.05 C ANISOU 1669 CG ASN A 209 1944 2305 1851 -181 -267 -235 C ATOM 1670 OD1 ASN A 209 22.774 27.781 3.291 1.00 17.76 O ANISOU 1670 OD1 ASN A 209 2288 2089 2371 211 -323 -315 O ATOM 1671 ND2 ASN A 209 23.631 28.986 4.942 1.00 26.26 N ANISOU 1671 ND2 ASN A 209 3919 3564 2495 -223 -1402 14 N ATOM 1672 N SER A 210 22.250 29.164 0.234 1.00 12.72 N ANISOU 1672 N SER A 210 1573 2109 1149 -130 404 -587 N ATOM 1673 CA SER A 210 22.182 28.281 -0.927 1.00 14.34 C ANISOU 1673 CA SER A 210 2104 2123 1223 -125 413 -637 C ATOM 1674 C SER A 210 22.132 26.812 -0.561 1.00 13.69 C ANISOU 1674 C SER A 210 1550 2167 1486 38 529 -541 C ATOM 1675 O SER A 210 21.405 26.056 -1.227 1.00 17.06 O ANISOU 1675 O SER A 210 2239 2587 1655 -364 518 -774 O ATOM 1676 CB SER A 210 23.337 28.563 -1.895 1.00 17.48 C ANISOU 1676 CB SER A 210 2483 2544 1615 -236 677 -257 C ATOM 1677 OG ASER A 210 24.571 28.289 -1.268 0.50 18.79 O ANISOU 1677 OG ASER A 210 1973 2888 2277 -258 895 -562 O ATOM 1678 OG BSER A 210 23.314 29.884 -2.393 0.50 22.78 O ANISOU 1678 OG BSER A 210 3816 2732 2107 41 966 14 O ATOM 1679 N GLY A 211 22.877 26.382 0.447 1.00 14.16 N ANISOU 1679 N GLY A 211 1413 2247 1718 119 563 -346 N ATOM 1680 CA GLY A 211 22.863 24.992 0.861 1.00 17.26 C ANISOU 1680 CA GLY A 211 1825 2294 2439 313 459 -180 C ATOM 1681 C GLY A 211 21.641 24.600 1.670 1.00 17.31 C ANISOU 1681 C GLY A 211 1811 2069 2697 309 574 -282 C ATOM 1682 O GLY A 211 21.340 23.409 1.761 1.00 22.26 O ANISOU 1682 O GLY A 211 2553 2022 3884 469 1043 -185 O ATOM 1683 N SER A 212 20.905 25.530 2.273 1.00 12.57 N ANISOU 1683 N SER A 212 1415 1765 1595 152 227 -38 N ATOM 1684 CA SER A 212 19.720 25.253 3.082 1.00 11.81 C ANISOU 1684 CA SER A 212 1318 1692 1476 79 84 2 C ATOM 1685 C SER A 212 18.687 26.324 2.762 1.00 10.11 C ANISOU 1685 C SER A 212 1354 1294 1194 -13 1 -287 C ATOM 1686 O SER A 212 18.450 27.273 3.509 1.00 12.43 O ANISOU 1686 O SER A 212 1760 1641 1324 -46 181 -516 O ATOM 1687 CB SER A 212 20.082 25.286 4.565 1.00 17.31 C ANISOU 1687 CB SER A 212 2036 3062 1479 311 29 381 C ATOM 1688 OG ASER A 212 19.034 24.678 5.319 0.50 20.43 O ANISOU 1688 OG ASER A 212 2123 3699 1941 -236 -114 514 O ATOM 1689 OG BSER A 212 21.109 24.367 4.870 0.50 20.65 O ANISOU 1689 OG BSER A 212 2388 3159 2300 442 55 845 O ATOM 1690 N PRO A 213 18.043 26.217 1.591 1.00 9.88 N ANISOU 1690 N PRO A 213 1140 1452 1163 42 87 -385 N ATOM 1691 CA PRO A 213 17.177 27.279 1.112 1.00 10.38 C ANISOU 1691 CA PRO A 213 1149 1641 1155 10 48 -112 C ATOM 1692 C PRO A 213 15.781 27.300 1.707 1.00 9.46 C ANISOU 1692 C PRO A 213 1142 1378 1073 15 48 -199 C ATOM 1693 O PRO A 213 15.242 26.262 2.099 1.00 11.67 O ANISOU 1693 O PRO A 213 1349 1457 1628 13 202 -91 O ATOM 1694 CB PRO A 213 17.103 27.026 -0.411 1.00 13.72 C ANISOU 1694 CB PRO A 213 1830 2234 1151 173 273 -60 C ATOM 1695 CG PRO A 213 17.298 25.559 -0.519 1.00 14.00 C ANISOU 1695 CG PRO A 213 1785 2213 1322 -115 -92 -535 C ATOM 1696 CD PRO A 213 18.257 25.163 0.567 1.00 12.49 C ANISOU 1696 CD PRO A 213 1573 1670 1505 151 -38 -700 C ATOM 1697 N TYR A 214 15.156 28.478 1.703 1.00 8.58 N ANISOU 1697 N TYR A 214 935 1296 1030 -106 66 -169 N ATOM 1698 CA TYR A 214 13.749 28.599 2.107 1.00 8.55 C ANISOU 1698 CA TYR A 214 942 1443 865 -45 26 -188 C ATOM 1699 C TYR A 214 12.891 27.776 1.135 1.00 8.80 C ANISOU 1699 C TYR A 214 1074 1504 767 -61 -49 -113 C ATOM 1700 O TYR A 214 13.132 27.746 -0.078 1.00 10.39 O ANISOU 1700 O TYR A 214 1325 1715 908 -377 117 -281 O ATOM 1701 CB TYR A 214 13.354 30.097 2.028 1.00 9.91 C ANISOU 1701 CB TYR A 214 1146 1359 1261 -63 183 -239 C ATOM 1702 CG TYR A 214 11.872 30.330 2.234 1.00 8.96 C ANISOU 1702 CG TYR A 214 1095 1302 1007 -59 100 -209 C ATOM 1703 CD1 TYR A 214 11.276 30.315 3.499 1.00 9.40 C ANISOU 1703 CD1 TYR A 214 1230 1372 970 13 11 -211 C ATOM 1704 CD2 TYR A 214 11.022 30.482 1.139 1.00 9.57 C ANISOU 1704 CD2 TYR A 214 1171 1490 974 -9 123 -81 C ATOM 1705 CE1 TYR A 214 9.910 30.480 3.661 1.00 9.99 C ANISOU 1705 CE1 TYR A 214 1215 1491 1089 88 -77 -166 C ATOM 1706 CE2 TYR A 214 9.664 30.628 1.324 1.00 9.72 C ANISOU 1706 CE2 TYR A 214 1153 1661 878 112 -37 -26 C ATOM 1707 CZ TYR A 214 9.081 30.621 2.579 1.00 9.09 C ANISOU 1707 CZ TYR A 214 942 1458 1056 -32 56 -76 C ATOM 1708 OH TYR A 214 7.709 30.767 2.677 1.00 11.10 O ANISOU 1708 OH TYR A 214 1029 1921 1265 61 25 -47 O ATOM 1709 N ASN A 215 11.860 27.142 1.682 1.00 8.32 N ANISOU 1709 N ASN A 215 1135 1224 802 -80 -32 -239 N ATOM 1710 CA ASN A 215 10.833 26.425 0.935 1.00 8.28 C ANISOU 1710 CA ASN A 215 1074 1350 722 -60 12 -267 C ATOM 1711 C ASN A 215 9.457 26.888 1.420 1.00 8.11 C ANISOU 1711 C ASN A 215 1196 1145 741 24 47 -141 C ATOM 1712 O ASN A 215 9.298 27.125 2.633 1.00 9.04 O ANISOU 1712 O ASN A 215 1234 1427 774 -165 69 -178 O ATOM 1713 CB ASN A 215 11.012 24.916 1.152 1.00 10.14 C ANISOU 1713 CB ASN A 215 1342 1350 1161 -180 -13 -187 C ATOM 1714 CG ASN A 215 10.188 24.020 0.237 1.00 9.62 C ANISOU 1714 CG ASN A 215 1271 1284 1100 -12 2 -246 C ATOM 1715 OD1 ASN A 215 8.957 24.018 0.257 1.00 10.20 O ANISOU 1715 OD1 ASN A 215 1262 1458 1154 -141 2 -306 O ATOM 1716 ND2 ASN A 215 10.860 23.230 -0.603 1.00 12.24 N ANISOU 1716 ND2 ASN A 215 1561 1670 1421 0 236 -439 N ATOM 1717 N SER A 216 8.467 26.991 0.511 1.00 8.56 N ANISOU 1717 N SER A 216 1066 1307 880 110 12 -37 N ATOM 1718 CA SER A 216 7.114 27.366 0.934 1.00 9.40 C ANISOU 1718 CA SER A 216 1182 1247 1142 218 81 -88 C ATOM 1719 C SER A 216 6.546 26.432 1.998 1.00 9.60 C ANISOU 1719 C SER A 216 1220 1439 988 -32 -19 -208 C ATOM 1720 O SER A 216 5.654 26.837 2.775 1.00 11.09 O ANISOU 1720 O SER A 216 1317 1703 1194 68 110 -154 O ATOM 1721 CB SER A 216 6.148 27.377 -0.265 1.00 11.68 C ANISOU 1721 CB SER A 216 1007 2149 1280 359 132 458 C ATOM 1722 OG ASER A 216 6.021 26.106 -0.823 0.50 19.06 O ANISOU 1722 OG ASER A 216 2425 2844 1972 -114 -110 -291 O ATOM 1723 OG BSER A 216 6.585 28.269 -1.256 0.50 10.45 O ANISOU 1723 OG BSER A 216 1287 1683 1001 322 117 150 O ATOM 1724 N ASN A 217 7.025 25.192 2.114 1.00 8.63 N ANISOU 1724 N ASN A 217 1046 1426 806 -186 -89 -85 N ATOM 1725 CA ASN A 217 6.542 24.239 3.108 1.00 9.00 C ANISOU 1725 CA ASN A 217 1249 1286 884 -237 -39 -102 C ATOM 1726 C ASN A 217 7.010 24.583 4.522 1.00 9.04 C ANISOU 1726 C ASN A 217 1118 1377 939 -256 -18 -97 C ATOM 1727 O ASN A 217 6.550 23.933 5.478 1.00 10.58 O ANISOU 1727 O ASN A 217 1570 1466 985 -385 200 -110 O ATOM 1728 CB ASN A 217 6.870 22.789 2.732 1.00 10.21 C ANISOU 1728 CB ASN A 217 1509 1337 1032 -264 -131 -205 C ATOM 1729 CG ASN A 217 8.300 22.360 2.929 1.00 10.24 C ANISOU 1729 CG ASN A 217 1597 1228 1066 -163 -107 -135 C ATOM 1730 OD1 ASN A 217 9.065 22.963 3.683 1.00 11.72 O ANISOU 1730 OD1 ASN A 217 1461 1558 1433 -78 -287 -288 O ATOM 1731 ND2 ASN A 217 8.687 21.261 2.290 1.00 12.88 N ANISOU 1731 ND2 ASN A 217 1811 1496 1586 177 -236 -384 N ATOM 1732 N PHE A 218 7.762 25.672 4.733 1.00 8.76 N ANISOU 1732 N PHE A 218 1220 1420 688 -259 8 -155 N ATOM 1733 CA PHE A 218 8.061 26.149 6.083 1.00 8.43 C ANISOU 1733 CA PHE A 218 1233 1287 683 -134 29 -211 C ATOM 1734 C PHE A 218 6.780 26.413 6.872 1.00 8.45 C ANISOU 1734 C PHE A 218 1201 1263 744 -131 -8 -149 C ATOM 1735 O PHE A 218 6.687 26.142 8.073 1.00 8.86 O ANISOU 1735 O PHE A 218 1184 1439 743 -15 -11 -18 O ATOM 1736 CB PHE A 218 8.911 27.425 6.044 1.00 9.45 C ANISOU 1736 CB PHE A 218 1258 1390 940 -204 35 -138 C ATOM 1737 CG PHE A 218 9.428 27.954 7.356 1.00 10.01 C ANISOU 1737 CG PHE A 218 1267 1513 1022 -341 162 -336 C ATOM 1738 CD1 PHE A 218 9.932 27.124 8.339 1.00 11.66 C ANISOU 1738 CD1 PHE A 218 1382 1745 1302 201 -155 -558 C ATOM 1739 CD2 PHE A 218 9.429 29.316 7.597 1.00 14.00 C ANISOU 1739 CD2 PHE A 218 2674 1492 1154 -529 109 -208 C ATOM 1740 CE1 PHE A 218 10.438 27.624 9.529 1.00 12.54 C ANISOU 1740 CE1 PHE A 218 1345 2097 1322 80 -240 -431 C ATOM 1741 CE2 PHE A 218 9.933 29.835 8.782 1.00 16.16 C ANISOU 1741 CE2 PHE A 218 3063 1833 1244 -709 5 -318 C ATOM 1742 CZ PHE A 218 10.444 28.978 9.745 1.00 14.66 C ANISOU 1742 CZ PHE A 218 2129 2114 1328 -515 -98 -488 C ATOM 1743 N ARG A 219 5.718 26.928 6.225 1.00 9.42 N ANISOU 1743 N ARG A 219 1177 1617 786 -106 52 100 N ATOM 1744 CA ARG A 219 4.462 27.180 6.912 1.00 9.81 C ANISOU 1744 CA ARG A 219 1104 1597 1027 -65 89 112 C ATOM 1745 C ARG A 219 3.851 25.875 7.422 1.00 9.22 C ANISOU 1745 C ARG A 219 1047 1482 975 -43 -93 63 C ATOM 1746 O ARG A 219 3.265 25.822 8.522 1.00 11.46 O ANISOU 1746 O ARG A 219 1361 1897 1098 -82 41 174 O ATOM 1747 CB ARG A 219 3.496 27.934 5.997 1.00 11.30 C ANISOU 1747 CB ARG A 219 1365 1647 1280 27 -71 167 C ATOM 1748 CG ARG A 219 2.296 28.506 6.748 1.00 13.58 C ANISOU 1748 CG ARG A 219 1429 2118 1612 136 145 310 C ATOM 1749 CD ARG A 219 1.335 29.277 5.862 1.00 15.47 C ANISOU 1749 CD ARG A 219 1490 2070 2317 174 -124 332 C ATOM 1750 NE ARG A 219 1.968 30.470 5.325 1.00 13.73 N ANISOU 1750 NE ARG A 219 1453 2056 1709 79 -133 81 N ATOM 1751 CZ ARG A 219 1.316 31.455 4.719 1.00 15.03 C ANISOU 1751 CZ ARG A 219 1575 2222 1914 234 -337 -36 C ATOM 1752 NH1 ARG A 219 -0.013 31.417 4.612 1.00 18.23 N ANISOU 1752 NH1 ARG A 219 1527 3009 2391 451 -210 96 N ATOM 1753 NH2 ARG A 219 1.999 32.489 4.245 1.00 18.11 N ANISOU 1753 NH2 ARG A 219 2369 2288 2223 237 -253 440 N ATOM 1754 N THR A 220 3.950 24.799 6.627 1.00 9.77 N ANISOU 1754 N THR A 220 1325 1584 804 -285 -145 37 N ATOM 1755 CA THR A 220 3.506 23.468 7.048 1.00 10.18 C ANISOU 1755 CA THR A 220 1137 1559 1173 -236 -192 30 C ATOM 1756 C THR A 220 4.306 22.983 8.261 1.00 9.20 C ANISOU 1756 C THR A 220 997 1557 942 -262 -39 -111 C ATOM 1757 O THR A 220 3.705 22.419 9.208 1.00 10.08 O ANISOU 1757 O THR A 220 1214 1607 1010 -365 20 -24 O ATOM 1758 CB THR A 220 3.635 22.462 5.880 1.00 12.77 C ANISOU 1758 CB THR A 220 1651 1809 1391 -480 -338 -240 C ATOM 1759 OG1 THR A 220 2.839 22.943 4.780 1.00 19.49 O ANISOU 1759 OG1 THR A 220 2841 2837 1726 -312 -1042 -249 O ATOM 1760 CG2 THR A 220 3.175 21.071 6.264 1.00 16.10 C ANISOU 1760 CG2 THR A 220 2398 1815 1902 -580 -144 -250 C ATOM 1761 N THR A 221 5.625 23.151 8.249 1.00 8.97 N ANISOU 1761 N THR A 221 977 1498 935 -172 40 -150 N ATOM 1762 CA THR A 221 6.447 22.788 9.406 1.00 8.37 C ANISOU 1762 CA THR A 221 954 1290 938 -32 108 -49 C ATOM 1763 C THR A 221 5.968 23.492 10.672 1.00 8.11 C ANISOU 1763 C THR A 221 959 1206 915 -98 125 0 C ATOM 1764 O THR A 221 5.744 22.859 11.728 1.00 9.11 O ANISOU 1764 O THR A 221 1085 1337 1039 -54 187 108 O ATOM 1765 CB THR A 221 7.932 23.117 9.144 1.00 8.49 C ANISOU 1765 CB THR A 221 1041 1258 924 -110 152 -35 C ATOM 1766 OG1 THR A 221 8.319 22.387 7.977 1.00 11.30 O ANISOU 1766 OG1 THR A 221 1318 1715 1259 -96 262 -400 O ATOM 1767 CG2 THR A 221 8.818 22.747 10.316 1.00 10.48 C ANISOU 1767 CG2 THR A 221 1017 1758 1208 94 119 64 C ATOM 1768 N LEU A 222 5.802 24.818 10.610 1.00 8.24 N ANISOU 1768 N LEU A 222 1069 1183 878 -41 74 66 N ATOM 1769 CA LEU A 222 5.370 25.584 11.780 1.00 7.97 C ANISOU 1769 CA LEU A 222 1007 1258 764 91 -60 85 C ATOM 1770 C LEU A 222 4.004 25.118 12.282 1.00 8.26 C ANISOU 1770 C LEU A 222 1129 1209 801 40 58 -78 C ATOM 1771 O LEU A 222 3.818 24.925 13.497 1.00 9.90 O ANISOU 1771 O LEU A 222 1260 1586 915 -152 148 19 O ATOM 1772 CB LEU A 222 5.329 27.084 11.465 1.00 8.43 C ANISOU 1772 CB LEU A 222 1086 1246 871 85 -84 -10 C ATOM 1773 CG LEU A 222 6.658 27.779 11.128 1.00 9.64 C ANISOU 1773 CG LEU A 222 1324 1267 1074 -95 15 -34 C ATOM 1774 CD1 LEU A 222 6.428 29.242 10.741 1.00 14.18 C ANISOU 1774 CD1 LEU A 222 2118 1297 1974 -287 -271 225 C ATOM 1775 CD2 LEU A 222 7.670 27.696 12.256 1.00 12.22 C ANISOU 1775 CD2 LEU A 222 1296 2028 1321 -284 -85 192 C ATOM 1776 N GLN A 223 3.024 24.935 11.384 1.00 8.60 N ANISOU 1776 N GLN A 223 886 1558 823 -17 148 98 N ATOM 1777 CA GLN A 223 1.691 24.481 11.790 1.00 9.49 C ANISOU 1777 CA GLN A 223 940 1540 1125 46 229 214 C ATOM 1778 C GLN A 223 1.706 23.087 12.421 1.00 9.20 C ANISOU 1778 C GLN A 223 887 1443 1167 -269 -55 99 C ATOM 1779 O GLN A 223 0.991 22.832 13.404 1.00 10.78 O ANISOU 1779 O GLN A 223 1190 1713 1193 -113 107 155 O ATOM 1780 CB GLN A 223 0.769 24.457 10.561 1.00 12.45 C ANISOU 1780 CB GLN A 223 847 2383 1499 -80 68 351 C ATOM 1781 CG GLN A 223 0.386 25.686 9.818 1.00 19.26 C ANISOU 1781 CG GLN A 223 2369 2354 2595 40 115 605 C ATOM 1782 CD GLN A 223 -0.284 25.579 8.472 1.00 29.91 C ANISOU 1782 CD GLN A 223 4059 4186 3120 -132 -658 -112 C ATOM 1783 OE1 GLN A 223 -1.002 26.508 8.074 1.00 39.81 O ANISOU 1783 OE1 GLN A 223 4763 4870 5493 563 -546 457 O ATOM 1784 NE2 GLN A 223 -0.113 24.515 7.695 1.00 30.80 N ANISOU 1784 NE2 GLN A 223 3883 4462 3357 587 -582 -206 N ATOM 1785 N ASN A 224 2.479 22.159 11.842 1.00 10.01 N ANISOU 1785 N ASN A 224 1138 1473 1193 -187 -42 -24 N ATOM 1786 CA ASN A 224 2.498 20.789 12.351 1.00 10.87 C ANISOU 1786 CA ASN A 224 1251 1497 1381 -189 -14 84 C ATOM 1787 C ASN A 224 3.162 20.696 13.721 1.00 9.33 C ANISOU 1787 C ASN A 224 1126 1126 1294 -172 69 -55 C ATOM 1788 O ASN A 224 2.694 19.922 14.579 1.00 11.11 O ANISOU 1788 O ASN A 224 1245 1588 1390 -432 -57 132 O ATOM 1789 CB ASN A 224 3.170 19.844 11.351 1.00 12.62 C ANISOU 1789 CB ASN A 224 1829 1427 1539 -170 -68 -121 C ATOM 1790 CG AASN A 224 2.299 19.606 10.130 0.50 11.67 C ANISOU 1790 CG AASN A 224 1608 1396 1429 -480 78 141 C ATOM 1791 OD1AASN A 224 1.127 19.989 10.095 0.50 13.30 O ANISOU 1791 OD1AASN A 224 1502 2420 1131 -514 -251 -256 O ATOM 1792 ND2AASN A 224 2.828 18.970 9.095 0.50 13.20 N ANISOU 1792 ND2AASN A 224 2075 1681 1261 5 -455 -182 N ATOM 1793 CG BASN A 224 2.205 19.299 10.321 0.50 19.50 C ANISOU 1793 CG BASN A 224 2308 2776 2325 -563 -509 -348 C ATOM 1794 OD1BASN A 224 1.542 18.289 10.570 0.50 26.80 O ANISOU 1794 OD1BASN A 224 3409 2932 3840 -901 -48 -126 O ATOM 1795 ND2BASN A 224 2.113 19.942 9.172 0.50 25.62 N ANISOU 1795 ND2BASN A 224 3528 3622 2586 -452 -447 118 N ATOM 1796 N PHE A 225 4.206 21.493 13.993 1.00 8.54 N ANISOU 1796 N PHE A 225 870 1231 1145 -69 81 -2 N ATOM 1797 CA PHE A 225 4.773 21.529 15.342 1.00 8.44 C ANISOU 1797 CA PHE A 225 887 1187 1134 -146 34 87 C ATOM 1798 C PHE A 225 3.816 22.184 16.332 1.00 8.21 C ANISOU 1798 C PHE A 225 780 1293 1046 -202 18 152 C ATOM 1799 O PHE A 225 3.619 21.677 17.450 1.00 9.78 O ANISOU 1799 O PHE A 225 1192 1471 1051 -243 39 194 O ATOM 1800 CB PHE A 225 6.153 22.212 15.360 1.00 8.75 C ANISOU 1800 CB PHE A 225 976 1281 1069 -211 -156 -36 C ATOM 1801 CG PHE A 225 7.278 21.268 14.985 1.00 8.80 C ANISOU 1801 CG PHE A 225 970 1153 1221 -238 -57 22 C ATOM 1802 CD1 PHE A 225 7.669 21.072 13.675 1.00 9.25 C ANISOU 1802 CD1 PHE A 225 1003 1253 1260 -65 -22 85 C ATOM 1803 CD2 PHE A 225 7.965 20.582 15.990 1.00 9.83 C ANISOU 1803 CD2 PHE A 225 1177 1308 1250 -92 -88 9 C ATOM 1804 CE1 PHE A 225 8.707 20.205 13.367 1.00 10.99 C ANISOU 1804 CE1 PHE A 225 1196 1365 1614 -7 55 -33 C ATOM 1805 CE2 PHE A 225 9.006 19.733 15.669 1.00 12.36 C ANISOU 1805 CE2 PHE A 225 1286 1638 1774 148 -212 -1 C ATOM 1806 CZ PHE A 225 9.382 19.533 14.360 1.00 10.77 C ANISOU 1806 CZ PHE A 225 925 1263 1906 2 8 9 C ATOM 1807 N ALA A 226 3.162 23.294 15.941 1.00 8.85 N ANISOU 1807 N ALA A 226 1135 1267 959 -49 187 73 N ATOM 1808 CA ALA A 226 2.201 23.944 16.838 1.00 9.47 C ANISOU 1808 CA ALA A 226 1275 1325 998 -97 235 0 C ATOM 1809 C ALA A 226 1.088 22.992 17.262 1.00 9.95 C ANISOU 1809 C ALA A 226 1289 1420 1072 -87 152 259 C ATOM 1810 O ALA A 226 0.622 23.026 18.422 1.00 11.42 O ANISOU 1810 O ALA A 226 1567 1577 1194 47 433 132 O ATOM 1811 CB ALA A 226 1.646 25.189 16.162 1.00 11.92 C ANISOU 1811 CB ALA A 226 1698 1280 1551 228 508 22 C ATOM 1812 N ALA A 227 0.628 22.111 16.354 1.00 9.88 N ANISOU 1812 N ALA A 227 1026 1464 1265 -84 156 153 N ATOM 1813 CA ALA A 227 -0.424 21.146 16.657 1.00 10.95 C ANISOU 1813 CA ALA A 227 1116 1528 1516 -146 -6 186 C ATOM 1814 C ALA A 227 -0.044 20.115 17.702 1.00 10.64 C ANISOU 1814 C ALA A 227 986 1523 1535 -342 -42 226 C ATOM 1815 O ALA A 227 -0.937 19.513 18.319 1.00 14.15 O ANISOU 1815 O ALA A 227 1273 2134 1968 -516 46 614 O ATOM 1816 CB ALA A 227 -0.890 20.452 15.369 1.00 13.69 C ANISOU 1816 CB ALA A 227 1141 2503 1557 -328 -279 142 C ATOM 1817 N LEU A 228 1.241 19.924 18.011 1.00 9.97 N ANISOU 1817 N LEU A 228 1051 1293 1445 -213 -46 188 N ATOM 1818 CA LEU A 228 1.701 19.038 19.068 1.00 10.60 C ANISOU 1818 CA LEU A 228 1300 1163 1566 -137 80 280 C ATOM 1819 C LEU A 228 1.534 19.662 20.461 1.00 10.48 C ANISOU 1819 C LEU A 228 958 1584 1440 -93 11 337 C ATOM 1820 O LEU A 228 1.662 18.940 21.474 1.00 13.63 O ANISOU 1820 O LEU A 228 1796 1788 1596 186 262 474 O ATOM 1821 CB LEU A 228 3.180 18.645 18.913 1.00 11.90 C ANISOU 1821 CB LEU A 228 1340 1533 1650 -37 43 41 C ATOM 1822 CG LEU A 228 3.580 17.856 17.665 1.00 13.27 C ANISOU 1822 CG LEU A 228 1506 2013 1524 153 76 80 C ATOM 1823 CD1 LEU A 228 5.089 17.641 17.633 1.00 15.04 C ANISOU 1823 CD1 LEU A 228 1622 2528 1564 631 72 46 C ATOM 1824 CD2 LEU A 228 2.854 16.522 17.579 1.00 17.70 C ANISOU 1824 CD2 LEU A 228 2445 2104 2176 -90 -57 -146 C ATOM 1825 N GLY A 229 1.240 20.950 20.540 1.00 10.41 N ANISOU 1825 N GLY A 229 1168 1524 1264 -263 36 258 N ATOM 1826 CA GLY A 229 1.086 21.633 21.811 1.00 11.22 C ANISOU 1826 CA GLY A 229 1338 1482 1445 -324 81 140 C ATOM 1827 C GLY A 229 2.292 22.443 22.246 1.00 9.59 C ANISOU 1827 C GLY A 229 1280 1296 1069 -238 181 111 C ATOM 1828 O GLY A 229 2.556 22.597 23.446 1.00 13.16 O ANISOU 1828 O GLY A 229 1830 2032 1137 -681 284 87 O ATOM 1829 N VAL A 230 3.073 22.968 21.303 1.00 9.96 N ANISOU 1829 N VAL A 230 1233 1431 1121 -523 43 122 N ATOM 1830 CA VAL A 230 4.186 23.864 21.601 1.00 8.66 C ANISOU 1830 CA VAL A 230 1092 1128 1069 -299 89 73 C ATOM 1831 C VAL A 230 3.985 25.178 20.835 1.00 8.11 C ANISOU 1831 C VAL A 230 976 1231 874 -187 67 119 C ATOM 1832 O VAL A 230 3.386 25.204 19.760 1.00 10.66 O ANISOU 1832 O VAL A 230 1363 1559 1128 -412 -218 220 O ATOM 1833 CB VAL A 230 5.561 23.282 21.207 1.00 9.83 C ANISOU 1833 CB VAL A 230 1240 1258 1238 -98 75 161 C ATOM 1834 CG1 VAL A 230 5.928 22.107 22.128 1.00 13.02 C ANISOU 1834 CG1 VAL A 230 1693 1461 1795 8 -357 373 C ATOM 1835 CG2 VAL A 230 5.674 22.875 19.743 1.00 11.49 C ANISOU 1835 CG2 VAL A 230 1306 1815 1247 -113 20 29 C ATOM 1836 N ASP A 231 4.521 26.260 21.399 1.00 7.24 N ANISOU 1836 N ASP A 231 855 1082 814 -118 67 130 N ATOM 1837 CA ASP A 231 4.712 27.515 20.666 1.00 7.47 C ANISOU 1837 CA ASP A 231 796 1233 811 -91 -13 261 C ATOM 1838 C ASP A 231 5.910 27.356 19.718 1.00 6.66 C ANISOU 1838 C ASP A 231 668 1008 857 -82 -58 202 C ATOM 1839 O ASP A 231 6.802 26.517 19.971 1.00 8.84 O ANISOU 1839 O ASP A 231 813 1427 1119 77 91 437 O ATOM 1840 CB ASP A 231 4.928 28.675 21.627 1.00 8.98 C ANISOU 1840 CB ASP A 231 1014 1375 1023 -112 32 76 C ATOM 1841 CG ASP A 231 3.751 28.968 22.559 1.00 10.90 C ANISOU 1841 CG ASP A 231 1400 1455 1284 -92 328 173 C ATOM 1842 OD1 ASP A 231 2.611 28.767 22.114 1.00 13.50 O ANISOU 1842 OD1 ASP A 231 1178 2153 1798 31 433 -28 O ATOM 1843 OD2 ASP A 231 3.994 29.388 23.698 1.00 16.38 O ANISOU 1843 OD2 ASP A 231 2384 2488 1352 -32 499 -277 O ATOM 1844 N VAL A 232 5.948 28.165 18.666 1.00 6.86 N ANISOU 1844 N VAL A 232 708 990 910 -30 75 169 N ATOM 1845 CA VAL A 232 7.065 28.158 17.718 1.00 6.51 C ANISOU 1845 CA VAL A 232 636 959 877 -42 37 164 C ATOM 1846 C VAL A 232 7.639 29.555 17.637 1.00 6.58 C ANISOU 1846 C VAL A 232 699 906 895 55 104 81 C ATOM 1847 O VAL A 232 6.933 30.563 17.746 1.00 8.38 O ANISOU 1847 O VAL A 232 887 911 1385 102 156 95 O ATOM 1848 CB VAL A 232 6.651 27.565 16.353 1.00 7.99 C ANISOU 1848 CB VAL A 232 957 1059 1018 -74 26 68 C ATOM 1849 CG1 VAL A 232 6.232 26.105 16.480 1.00 9.99 C ANISOU 1849 CG1 VAL A 232 1342 1137 1319 -240 -35 -33 C ATOM 1850 CG2 VAL A 232 5.602 28.379 15.622 1.00 9.69 C ANISOU 1850 CG2 VAL A 232 1280 1445 958 160 -64 13 C ATOM 1851 N ALA A 233 8.955 29.660 17.396 1.00 7.37 N ANISOU 1851 N ALA A 233 668 919 1212 -32 202 108 N ATOM 1852 CA ALA A 233 9.639 30.935 17.283 1.00 8.56 C ANISOU 1852 CA ALA A 233 961 923 1366 -65 418 49 C ATOM 1853 C ALA A 233 10.713 30.847 16.218 1.00 6.85 C ANISOU 1853 C ALA A 233 766 822 1014 -1 156 96 C ATOM 1854 O ALA A 233 11.347 29.783 16.055 1.00 8.56 O ANISOU 1854 O ALA A 233 1049 847 1357 68 357 129 O ATOM 1855 CB ALA A 233 10.264 31.369 18.607 1.00 12.29 C ANISOU 1855 CB ALA A 233 1562 1616 1492 -537 688 -511 C ATOM 1856 N ILE A 234 10.980 31.919 15.498 1.00 6.47 N ANISOU 1856 N ILE A 234 741 753 963 53 188 59 N ATOM 1857 CA ILE A 234 12.066 32.051 14.539 1.00 5.73 C ANISOU 1857 CA ILE A 234 689 735 752 32 113 -45 C ATOM 1858 C ILE A 234 13.206 32.746 15.289 1.00 5.67 C ANISOU 1858 C ILE A 234 759 608 787 -20 69 35 C ATOM 1859 O ILE A 234 13.001 33.896 15.720 1.00 6.76 O ANISOU 1859 O ILE A 234 826 706 1036 47 -26 -84 O ATOM 1860 CB ILE A 234 11.604 32.779 13.267 1.00 7.42 C ANISOU 1860 CB ILE A 234 1011 939 871 37 -43 43 C ATOM 1861 CG1 ILE A 234 10.624 31.923 12.474 1.00 12.01 C ANISOU 1861 CG1 ILE A 234 1577 1533 1452 14 -640 -27 C ATOM 1862 CG2 ILE A 234 12.803 33.156 12.394 1.00 9.97 C ANISOU 1862 CG2 ILE A 234 1391 1491 904 147 239 204 C ATOM 1863 CD1AILE A 234 9.715 32.633 11.517 0.50 10.39 C ANISOU 1863 CD1AILE A 234 1249 1486 1212 74 -515 -191 C ATOM 1864 CD1BILE A 234 9.202 31.882 12.943 0.50 22.09 C ANISOU 1864 CD1BILE A 234 1855 3332 3205 -192 -29 -85 C ATOM 1865 N THR A 235 14.334 32.061 15.559 1.00 5.76 N ANISOU 1865 N THR A 235 696 764 729 46 33 42 N ATOM 1866 CA THR A 235 15.277 32.530 16.562 1.00 5.78 C ANISOU 1866 CA THR A 235 674 701 821 2 -1 27 C ATOM 1867 C THR A 235 16.537 33.195 16.070 1.00 5.34 C ANISOU 1867 C THR A 235 571 735 724 50 15 28 C ATOM 1868 O THR A 235 17.144 33.967 16.846 1.00 6.30 O ANISOU 1868 O THR A 235 792 828 775 -68 19 -18 O ATOM 1869 CB THR A 235 15.628 31.355 17.523 1.00 6.15 C ANISOU 1869 CB THR A 235 916 730 691 -58 57 48 C ATOM 1870 OG1 THR A 235 16.154 30.302 16.705 1.00 7.16 O ANISOU 1870 OG1 THR A 235 1129 795 797 165 62 94 O ATOM 1871 CG2 THR A 235 14.420 30.907 18.314 1.00 7.81 C ANISOU 1871 CG2 THR A 235 1077 1010 882 -216 82 112 C ATOM 1872 N GLU A 236 17.039 32.904 14.864 1.00 5.69 N ANISOU 1872 N GLU A 236 707 768 685 -30 79 61 N ATOM 1873 CA GLU A 236 18.349 33.424 14.407 1.00 5.46 C ANISOU 1873 CA GLU A 236 816 640 618 -42 155 29 C ATOM 1874 C GLU A 236 18.320 33.755 12.926 1.00 5.57 C ANISOU 1874 C GLU A 236 824 624 669 -14 57 38 C ATOM 1875 O GLU A 236 19.252 33.444 12.169 1.00 6.82 O ANISOU 1875 O GLU A 236 834 996 760 0 105 -1 O ATOM 1876 CB GLU A 236 19.485 32.420 14.731 1.00 6.42 C ANISOU 1876 CB GLU A 236 929 688 821 -41 -11 102 C ATOM 1877 CG GLU A 236 19.555 31.921 16.171 1.00 6.27 C ANISOU 1877 CG GLU A 236 963 577 841 50 25 45 C ATOM 1878 CD GLU A 236 20.702 30.997 16.484 1.00 7.17 C ANISOU 1878 CD GLU A 236 1108 856 759 128 -124 -31 C ATOM 1879 OE1 GLU A 236 21.652 30.843 15.671 1.00 9.13 O ANISOU 1879 OE1 GLU A 236 1119 1335 1014 344 -39 61 O ATOM 1880 OE2 GLU A 236 20.643 30.384 17.598 1.00 8.46 O ANISOU 1880 OE2 GLU A 236 1163 1065 987 139 -83 176 O ATOM 1881 N LEU A 237 17.227 34.375 12.455 1.00 6.18 N ANISOU 1881 N LEU A 237 914 761 673 94 27 53 N ATOM 1882 CA LEU A 237 17.008 34.576 11.035 1.00 6.36 C ANISOU 1882 CA LEU A 237 1002 764 650 50 68 109 C ATOM 1883 C LEU A 237 18.086 35.420 10.364 1.00 6.07 C ANISOU 1883 C LEU A 237 891 757 657 61 98 8 C ATOM 1884 O LEU A 237 18.424 36.538 10.799 1.00 6.91 O ANISOU 1884 O LEU A 237 1037 816 771 -85 159 -25 O ATOM 1885 CB LEU A 237 15.628 35.246 10.810 1.00 6.57 C ANISOU 1885 CB LEU A 237 876 871 750 -15 78 16 C ATOM 1886 CG LEU A 237 15.194 35.585 9.375 1.00 7.46 C ANISOU 1886 CG LEU A 237 957 984 893 24 -114 31 C ATOM 1887 CD1 LEU A 237 15.060 34.328 8.523 1.00 8.70 C ANISOU 1887 CD1 LEU A 237 1213 1101 991 91 -179 -63 C ATOM 1888 CD2 LEU A 237 13.884 36.368 9.389 1.00 7.86 C ANISOU 1888 CD2 LEU A 237 929 1025 1033 11 -20 148 C ATOM 1889 N ASP A 238 18.585 34.910 9.241 1.00 6.55 N ANISOU 1889 N ASP A 238 923 805 762 -6 183 -29 N ATOM 1890 CA ASP A 238 19.435 35.654 8.299 1.00 6.98 C ANISOU 1890 CA ASP A 238 1066 945 643 -44 139 -4 C ATOM 1891 C ASP A 238 19.269 34.946 6.954 1.00 7.23 C ANISOU 1891 C ASP A 238 1175 785 788 16 136 17 C ATOM 1892 O ASP A 238 18.960 33.750 6.892 1.00 8.42 O ANISOU 1892 O ASP A 238 1364 911 925 -50 321 23 O ATOM 1893 CB ASP A 238 20.865 35.861 8.781 1.00 7.87 C ANISOU 1893 CB ASP A 238 1155 870 966 -191 47 55 C ATOM 1894 CG ASP A 238 21.636 34.667 9.304 1.00 7.65 C ANISOU 1894 CG ASP A 238 948 1046 914 -56 163 46 C ATOM 1895 OD1 ASP A 238 21.373 33.519 8.845 1.00 8.86 O ANISOU 1895 OD1 ASP A 238 1220 1006 1142 -36 103 -87 O ATOM 1896 OD2 ASP A 238 22.511 34.855 10.185 1.00 9.95 O ANISOU 1896 OD2 ASP A 238 1136 1114 1531 1 -209 -86 O ATOM 1897 N ILE A 239 19.374 35.711 5.847 1.00 7.50 N ANISOU 1897 N ILE A 239 1264 911 675 -123 165 -64 N ATOM 1898 CA ILE A 239 19.110 35.134 4.526 1.00 7.65 C ANISOU 1898 CA ILE A 239 1363 846 697 -216 230 7 C ATOM 1899 C ILE A 239 20.178 35.647 3.560 1.00 8.43 C ANISOU 1899 C ILE A 239 1257 1097 851 -182 286 -92 C ATOM 1900 O ILE A 239 20.324 36.858 3.343 1.00 9.78 O ANISOU 1900 O ILE A 239 1694 1158 862 -237 385 -62 O ATOM 1901 CB ILE A 239 17.708 35.495 3.961 1.00 8.65 C ANISOU 1901 CB ILE A 239 1428 1114 744 -250 66 100 C ATOM 1902 CG1 ILE A 239 16.588 35.210 4.979 1.00 9.62 C ANISOU 1902 CG1 ILE A 239 1301 1309 1045 -216 147 144 C ATOM 1903 CG2 ILE A 239 17.470 34.727 2.651 1.00 10.92 C ANISOU 1903 CG2 ILE A 239 1613 1720 814 -228 -1 -142 C ATOM 1904 CD1 ILE A 239 15.182 35.620 4.580 1.00 11.92 C ANISOU 1904 CD1 ILE A 239 1397 1555 1578 -195 -45 336 C ATOM 1905 N GLN A 240 20.960 34.738 2.962 1.00 10.27 N ANISOU 1905 N GLN A 240 1491 1307 1105 -159 516 -126 N ATOM 1906 CA GLN A 240 22.040 35.097 2.044 1.00 10.82 C ANISOU 1906 CA GLN A 240 1505 1471 1136 -189 520 -187 C ATOM 1907 C GLN A 240 21.563 36.082 0.984 1.00 11.24 C ANISOU 1907 C GLN A 240 1622 1594 1054 -234 430 -217 C ATOM 1908 O GLN A 240 20.591 35.785 0.275 1.00 12.08 O ANISOU 1908 O GLN A 240 1780 1811 998 -361 370 -103 O ATOM 1909 CB GLN A 240 22.569 33.818 1.378 1.00 12.66 C ANISOU 1909 CB GLN A 240 1725 1632 1454 -93 761 -201 C ATOM 1910 CG GLN A 240 23.710 34.058 0.397 1.00 15.00 C ANISOU 1910 CG GLN A 240 1927 2112 1661 -343 886 -336 C ATOM 1911 CD GLN A 240 24.349 32.787 -0.105 1.00 19.67 C ANISOU 1911 CD GLN A 240 2653 2438 2382 -6 1113 -551 C ATOM 1912 OE1 GLN A 240 23.910 31.670 0.142 1.00 21.28 O ANISOU 1912 OE1 GLN A 240 2822 2476 2787 -176 1428 -754 O ATOM 1913 NE2 GLN A 240 25.446 32.932 -0.850 1.00 27.29 N ANISOU 1913 NE2 GLN A 240 3010 3794 3565 271 1800 -277 N ATOM 1914 N GLY A 241 22.215 37.231 0.823 1.00 11.44 N ANISOU 1914 N GLY A 241 1480 1651 1214 -253 491 56 N ATOM 1915 CA GLY A 241 21.837 38.257 -0.139 1.00 13.29 C ANISOU 1915 CA GLY A 241 1825 1783 1440 -157 523 193 C ATOM 1916 C GLY A 241 20.690 39.156 0.264 1.00 12.43 C ANISOU 1916 C GLY A 241 1692 1548 1482 -352 426 136 C ATOM 1917 O GLY A 241 20.374 40.118 -0.453 1.00 15.20 O ANISOU 1917 O GLY A 241 2317 1942 1517 -65 540 349 O ATOM 1918 N ALA A 242 20.011 38.892 1.377 1.00 10.99 N ANISOU 1918 N ALA A 242 1492 1450 1233 -314 338 -10 N ATOM 1919 CA ALA A 242 18.857 39.626 1.874 1.00 11.04 C ANISOU 1919 CA ALA A 242 1528 1545 1122 -212 199 83 C ATOM 1920 C ALA A 242 17.794 39.950 0.832 1.00 10.52 C ANISOU 1920 C ALA A 242 1386 1415 1197 -280 214 130 C ATOM 1921 O ALA A 242 17.378 41.107 0.656 1.00 12.74 O ANISOU 1921 O ALA A 242 1946 1533 1360 -146 -40 150 O ATOM 1922 CB ALA A 242 19.282 40.886 2.636 1.00 12.42 C ANISOU 1922 CB ALA A 242 1687 1719 1312 -174 26 -88 C ATOM 1923 N PRO A 243 17.279 38.946 0.117 1.00 11.43 N ANISOU 1923 N PRO A 243 1652 1551 1141 -295 46 123 N ATOM 1924 CA PRO A 243 16.229 39.185 -0.867 1.00 12.07 C ANISOU 1924 CA PRO A 243 1724 1693 1169 -307 57 175 C ATOM 1925 C PRO A 243 14.945 39.638 -0.195 1.00 11.60 C ANISOU 1925 C PRO A 243 1681 1592 1135 -348 2 119 C ATOM 1926 O PRO A 243 14.471 39.005 0.769 1.00 13.11 O ANISOU 1926 O PRO A 243 1704 2131 1145 -259 32 358 O ATOM 1927 CB PRO A 243 16.057 37.851 -1.581 1.00 15.18 C ANISOU 1927 CB PRO A 243 2064 2177 1527 -429 17 -315 C ATOM 1928 CG PRO A 243 16.666 36.822 -0.702 1.00 17.75 C ANISOU 1928 CG PRO A 243 2662 1926 2156 -492 -249 -204 C ATOM 1929 CD PRO A 243 17.608 37.511 0.241 1.00 15.24 C ANISOU 1929 CD PRO A 243 2398 1473 1920 -343 -49 -188 C ATOM 1930 N ALA A 244 14.313 40.693 -0.718 1.00 12.27 N ANISOU 1930 N ALA A 244 1826 1679 1157 -215 96 142 N ATOM 1931 CA ALA A 244 13.077 41.215 -0.148 1.00 12.31 C ANISOU 1931 CA ALA A 244 1823 1597 1256 -204 68 185 C ATOM 1932 C ALA A 244 11.958 40.181 -0.167 1.00 11.81 C ANISOU 1932 C ALA A 244 1579 1742 1165 -144 -81 204 C ATOM 1933 O ALA A 244 11.191 40.055 0.806 1.00 13.48 O ANISOU 1933 O ALA A 244 1796 1861 1465 -229 174 287 O ATOM 1934 CB ALA A 244 12.672 42.501 -0.866 1.00 15.28 C ANISOU 1934 CB ALA A 244 2342 1577 1885 -2 301 292 C ATOM 1935 N SER A 245 11.807 39.453 -1.278 1.00 13.07 N ANISOU 1935 N SER A 245 2133 1766 1068 -325 18 280 N ATOM 1936 CA SER A 245 10.723 38.476 -1.382 1.00 14.81 C ANISOU 1936 CA SER A 245 2450 1937 1239 -571 -340 322 C ATOM 1937 C SER A 245 10.790 37.385 -0.318 1.00 11.75 C ANISOU 1937 C SER A 245 1946 1562 956 -368 12 20 C ATOM 1938 O SER A 245 9.773 37.081 0.310 1.00 13.74 O ANISOU 1938 O SER A 245 1911 2024 1286 -383 -10 123 O ATOM 1939 CB SER A 245 10.692 37.860 -2.791 1.00 19.59 C ANISOU 1939 CB SER A 245 3493 2610 1341 -614 -528 105 C ATOM 1940 OG SER A 245 11.906 37.155 -3.002 1.00 25.16 O ANISOU 1940 OG SER A 245 4291 3389 1880 -22 102 -302 O ATOM 1941 N THR A 246 11.972 36.817 -0.079 1.00 12.19 N ANISOU 1941 N THR A 246 1814 1641 1177 -496 -45 -6 N ATOM 1942 CA THR A 246 12.109 35.745 0.911 1.00 11.09 C ANISOU 1942 CA THR A 246 1553 1459 1202 -452 77 -83 C ATOM 1943 C THR A 246 11.865 36.273 2.326 1.00 9.80 C ANISOU 1943 C THR A 246 1314 1438 969 -267 -114 160 C ATOM 1944 O THR A 246 11.209 35.622 3.147 1.00 10.51 O ANISOU 1944 O THR A 246 1414 1372 1206 -206 120 139 O ATOM 1945 CB THR A 246 13.460 35.028 0.797 1.00 12.37 C ANISOU 1945 CB THR A 246 1686 1703 1311 -300 394 -223 C ATOM 1946 OG1 THR A 246 13.700 34.769 -0.599 1.00 16.64 O ANISOU 1946 OG1 THR A 246 2767 2151 1403 -301 655 -270 O ATOM 1947 CG2 THR A 246 13.465 33.742 1.587 1.00 13.95 C ANISOU 1947 CG2 THR A 246 1915 1589 1795 -139 121 -191 C ATOM 1948 N TYR A 247 12.393 37.465 2.642 1.00 9.87 N ANISOU 1948 N TYR A 247 1227 1390 1133 -189 49 -10 N ATOM 1949 CA TYR A 247 12.168 38.078 3.960 1.00 9.25 C ANISOU 1949 CA TYR A 247 1253 1196 1067 -128 -35 104 C ATOM 1950 C TYR A 247 10.673 38.280 4.203 1.00 9.30 C ANISOU 1950 C TYR A 247 1212 1336 986 -100 -86 38 C ATOM 1951 O TYR A 247 10.173 38.015 5.327 1.00 10.30 O ANISOU 1951 O TYR A 247 1284 1565 1066 -56 26 35 O ATOM 1952 CB TYR A 247 12.986 39.378 4.134 1.00 8.83 C ANISOU 1952 CB TYR A 247 1343 1114 898 -145 -28 160 C ATOM 1953 CG TYR A 247 14.256 39.241 4.961 1.00 8.50 C ANISOU 1953 CG TYR A 247 1229 1163 838 -168 83 87 C ATOM 1954 CD1 TYR A 247 14.194 39.002 6.324 1.00 8.70 C ANISOU 1954 CD1 TYR A 247 1242 1213 851 -94 15 112 C ATOM 1955 CD2 TYR A 247 15.520 39.345 4.384 1.00 8.69 C ANISOU 1955 CD2 TYR A 247 1201 1189 910 -168 121 188 C ATOM 1956 CE1 TYR A 247 15.332 38.887 7.095 1.00 8.27 C ANISOU 1956 CE1 TYR A 247 1186 1250 705 -127 73 98 C ATOM 1957 CE2 TYR A 247 16.674 39.233 5.160 1.00 9.12 C ANISOU 1957 CE2 TYR A 247 1197 1334 934 -116 131 107 C ATOM 1958 CZ TYR A 247 16.580 38.995 6.507 1.00 8.28 C ANISOU 1958 CZ TYR A 247 1076 1213 859 -153 77 103 C ATOM 1959 OH TYR A 247 17.690 38.886 7.324 1.00 9.71 O ANISOU 1959 OH TYR A 247 1190 1562 937 -27 -7 132 O ATOM 1960 N ALA A 248 9.911 38.756 3.208 1.00 9.63 N ANISOU 1960 N ALA A 248 1092 1478 1089 -37 1 207 N ATOM 1961 CA ALA A 248 8.471 38.924 3.362 1.00 9.92 C ANISOU 1961 CA ALA A 248 1182 1382 1203 -46 41 183 C ATOM 1962 C ALA A 248 7.762 37.568 3.539 1.00 9.73 C ANISOU 1962 C ALA A 248 1205 1388 1105 -21 -105 312 C ATOM 1963 O ALA A 248 6.832 37.443 4.336 1.00 10.97 O ANISOU 1963 O ALA A 248 1296 1705 1166 -166 -57 295 O ATOM 1964 CB ALA A 248 7.876 39.675 2.170 1.00 13.72 C ANISOU 1964 CB ALA A 248 1460 1799 1955 65 -239 668 C ATOM 1965 N ASN A 249 8.189 36.557 2.764 1.00 9.93 N ANISOU 1965 N ASN A 249 1334 1407 1032 -136 -98 226 N ATOM 1966 CA ASN A 249 7.541 35.238 2.881 1.00 10.14 C ANISOU 1966 CA ASN A 249 1364 1449 1041 -188 -137 212 C ATOM 1967 C ASN A 249 7.691 34.644 4.274 1.00 8.66 C ANISOU 1967 C ASN A 249 1088 1310 890 -125 -123 99 C ATOM 1968 O ASN A 249 6.724 34.093 4.829 1.00 9.93 O ANISOU 1968 O ASN A 249 1225 1570 977 -240 -42 194 O ATOM 1969 CB ASN A 249 8.118 34.267 1.852 1.00 12.57 C ANISOU 1969 CB ASN A 249 1931 1697 1147 -360 -83 -106 C ATOM 1970 CG ASN A 249 7.737 34.501 0.397 1.00 16.63 C ANISOU 1970 CG ASN A 249 2773 2290 1255 -394 -274 -118 C ATOM 1971 OD1 ASN A 249 8.393 33.982 -0.523 1.00 21.47 O ANISOU 1971 OD1 ASN A 249 3470 3153 1536 -507 187 -339 O ATOM 1972 ND2 ASN A 249 6.705 35.270 0.170 1.00 20.16 N ANISOU 1972 ND2 ASN A 249 3221 3132 1309 -46 -986 86 N ATOM 1973 N VAL A 250 8.880 34.734 4.882 1.00 9.37 N ANISOU 1973 N VAL A 250 1122 1397 1039 -243 -158 113 N ATOM 1974 CA VAL A 250 9.121 34.196 6.221 1.00 9.06 C ANISOU 1974 CA VAL A 250 1105 1302 1036 -97 -113 66 C ATOM 1975 C VAL A 250 8.259 34.931 7.241 1.00 8.54 C ANISOU 1975 C VAL A 250 895 1256 1093 -102 -130 183 C ATOM 1976 O VAL A 250 7.647 34.319 8.139 1.00 9.79 O ANISOU 1976 O VAL A 250 1197 1424 1101 -144 -35 175 O ATOM 1977 CB VAL A 250 10.625 34.292 6.576 1.00 9.94 C ANISOU 1977 CB VAL A 250 1136 1368 1273 -117 -142 -6 C ATOM 1978 CG1 VAL A 250 10.861 34.004 8.049 1.00 11.81 C ANISOU 1978 CG1 VAL A 250 1217 1903 1368 128 -164 164 C ATOM 1979 CG2 VAL A 250 11.484 33.379 5.711 1.00 11.67 C ANISOU 1979 CG2 VAL A 250 1512 1392 1531 119 -218 -49 C ATOM 1980 N THR A 251 8.160 36.268 7.105 1.00 8.31 N ANISOU 1980 N THR A 251 1032 1212 913 -17 -54 184 N ATOM 1981 CA THR A 251 7.343 37.071 8.016 1.00 8.90 C ANISOU 1981 CA THR A 251 1081 1371 928 -67 -139 8 C ATOM 1982 C THR A 251 5.878 36.641 7.936 1.00 8.35 C ANISOU 1982 C THR A 251 965 1281 927 8 -20 134 C ATOM 1983 O THR A 251 5.189 36.430 8.965 1.00 9.77 O ANISOU 1983 O THR A 251 1191 1459 1064 -147 151 70 O ATOM 1984 CB THR A 251 7.532 38.568 7.699 1.00 10.30 C ANISOU 1984 CB THR A 251 1414 1343 1158 -25 -83 -21 C ATOM 1985 OG1 THR A 251 8.932 38.910 7.816 1.00 12.11 O ANISOU 1985 OG1 THR A 251 1467 1368 1768 -394 80 -36 O ATOM 1986 CG2 THR A 251 6.744 39.438 8.661 1.00 11.57 C ANISOU 1986 CG2 THR A 251 1588 1454 1353 -12 94 10 C ATOM 1987 N ASN A 252 5.338 36.511 6.719 1.00 9.60 N ANISOU 1987 N ASN A 252 1100 1556 992 -158 -182 256 N ATOM 1988 CA ASN A 252 3.962 36.067 6.519 1.00 9.64 C ANISOU 1988 CA ASN A 252 1087 1358 1219 -11 -152 92 C ATOM 1989 C ASN A 252 3.700 34.652 7.034 1.00 8.92 C ANISOU 1989 C ASN A 252 1016 1459 913 94 -15 204 C ATOM 1990 O ASN A 252 2.598 34.375 7.540 1.00 10.52 O ANISOU 1990 O ASN A 252 974 1714 1309 96 24 204 O ATOM 1991 CB ASN A 252 3.542 36.214 5.054 1.00 11.43 C ANISOU 1991 CB ASN A 252 1253 1776 1315 -119 -352 275 C ATOM 1992 CG ASN A 252 3.286 37.672 4.693 1.00 14.62 C ANISOU 1992 CG ASN A 252 1648 1926 1983 7 -495 452 C ATOM 1993 OD1 ASN A 252 2.730 38.412 5.505 1.00 21.63 O ANISOU 1993 OD1 ASN A 252 3362 2338 2519 809 -326 295 O ATOM 1994 ND2 ASN A 252 3.657 38.094 3.496 1.00 19.61 N ANISOU 1994 ND2 ASN A 252 2463 2727 2260 170 -336 924 N ATOM 1995 N ASP A 253 4.680 33.745 6.948 1.00 8.68 N ANISOU 1995 N ASP A 253 902 1327 1070 -74 -15 73 N ATOM 1996 CA ASP A 253 4.529 32.396 7.491 1.00 8.89 C ANISOU 1996 CA ASP A 253 988 1377 1014 -54 -80 55 C ATOM 1997 C ASP A 253 4.301 32.436 8.993 1.00 9.06 C ANISOU 1997 C ASP A 253 1096 1360 988 -112 -1 49 C ATOM 1998 O ASP A 253 3.451 31.713 9.510 1.00 10.51 O ANISOU 1998 O ASP A 253 1286 1577 1129 -277 46 73 O ATOM 1999 CB ASP A 253 5.695 31.494 7.117 1.00 9.44 C ANISOU 1999 CB ASP A 253 1145 1335 1107 -23 -47 51 C ATOM 2000 CG ASP A 253 5.820 31.101 5.674 1.00 9.65 C ANISOU 2000 CG ASP A 253 1129 1324 1215 -18 92 -21 C ATOM 2001 OD1 ASP A 253 4.779 31.124 4.952 1.00 11.58 O ANISOU 2001 OD1 ASP A 253 1308 1904 1187 70 -37 -242 O ATOM 2002 OD2 ASP A 253 6.929 30.765 5.207 1.00 12.52 O ANISOU 2002 OD2 ASP A 253 1430 2076 1250 332 249 101 O ATOM 2003 N CYS A 254 5.065 33.241 9.738 1.00 8.68 N ANISOU 2003 N CYS A 254 922 1445 932 -163 -4 108 N ATOM 2004 CA CYS A 254 4.832 33.392 11.176 1.00 8.16 C ANISOU 2004 CA CYS A 254 874 1298 929 -40 30 81 C ATOM 2005 C CYS A 254 3.469 34.010 11.500 1.00 7.92 C ANISOU 2005 C CYS A 254 780 1355 876 -112 -66 113 C ATOM 2006 O CYS A 254 2.731 33.539 12.387 1.00 9.27 O ANISOU 2006 O CYS A 254 878 1612 1032 -35 19 272 O ATOM 2007 CB CYS A 254 5.961 34.216 11.805 1.00 8.90 C ANISOU 2007 CB CYS A 254 1046 1368 969 -142 -10 93 C ATOM 2008 SG CYS A 254 5.849 34.491 13.601 1.00 8.09 S ANISOU 2008 SG CYS A 254 958 1217 900 -194 -10 53 S ATOM 2009 N LEU A 255 3.071 35.066 10.765 1.00 9.29 N ANISOU 2009 N LEU A 255 1047 1377 1106 81 88 205 N ATOM 2010 CA LEU A 255 1.772 35.710 10.999 1.00 10.09 C ANISOU 2010 CA LEU A 255 1107 1380 1346 138 -44 -6 C ATOM 2011 C LEU A 255 0.588 34.790 10.738 1.00 9.53 C ANISOU 2011 C LEU A 255 1091 1406 1124 74 103 80 C ATOM 2012 O LEU A 255 -0.481 34.997 11.341 1.00 13.07 O ANISOU 2012 O LEU A 255 1180 1852 1934 129 372 8 O ATOM 2013 CB LEU A 255 1.636 36.991 10.173 1.00 11.76 C ANISOU 2013 CB LEU A 255 1480 1400 1586 280 42 54 C ATOM 2014 CG LEU A 255 2.563 38.150 10.483 1.00 15.23 C ANISOU 2014 CG LEU A 255 1872 1612 2302 46 -37 9 C ATOM 2015 CD1 LEU A 255 2.423 39.269 9.450 1.00 19.61 C ANISOU 2015 CD1 LEU A 255 2856 1672 2923 -129 -317 332 C ATOM 2016 CD2 LEU A 255 2.301 38.719 11.867 1.00 21.41 C ANISOU 2016 CD2 LEU A 255 3224 2366 2544 -311 428 -356 C ATOM 2017 N ALA A 256 0.741 33.778 9.899 1.00 9.22 N ANISOU 2017 N ALA A 256 904 1493 1106 68 -169 38 N ATOM 2018 CA ALA A 256 -0.313 32.833 9.555 1.00 10.58 C ANISOU 2018 CA ALA A 256 1021 1800 1197 -59 -297 22 C ATOM 2019 C ALA A 256 -0.487 31.714 10.569 1.00 10.06 C ANISOU 2019 C ALA A 256 1041 1424 1359 2 -146 -101 C ATOM 2020 O ALA A 256 -1.466 30.959 10.447 1.00 13.41 O ANISOU 2020 O ALA A 256 1276 2113 1707 -384 -480 377 O ATOM 2021 CB ALA A 256 -0.011 32.224 8.184 1.00 13.85 C ANISOU 2021 CB ALA A 256 1728 2235 1300 -493 -318 -266 C ATOM 2022 N VAL A 257 0.420 31.580 11.541 1.00 9.02 N ANISOU 2022 N VAL A 257 980 1353 1093 -77 30 88 N ATOM 2023 CA VAL A 257 0.389 30.467 12.507 1.00 8.46 C ANISOU 2023 CA VAL A 257 892 1038 1285 -34 69 -27 C ATOM 2024 C VAL A 257 0.077 31.058 13.874 1.00 7.50 C ANISOU 2024 C VAL A 257 832 888 1131 46 -77 111 C ATOM 2025 O VAL A 257 0.846 31.887 14.415 1.00 8.39 O ANISOU 2025 O VAL A 257 929 1126 1132 12 -98 -40 O ATOM 2026 CB VAL A 257 1.710 29.676 12.444 1.00 9.38 C ANISOU 2026 CB VAL A 257 1015 1170 1378 157 -26 -195 C ATOM 2027 CG1 VAL A 257 1.769 28.626 13.548 1.00 11.91 C ANISOU 2027 CG1 VAL A 257 1392 1567 1567 384 176 65 C ATOM 2028 CG2 VAL A 257 1.905 29.054 11.066 1.00 11.94 C ANISOU 2028 CG2 VAL A 257 1458 1613 1466 221 230 -260 C ATOM 2029 N SER A 258 -1.030 30.646 14.501 1.00 8.22 N ANISOU 2029 N SER A 258 833 1052 1239 -15 -15 -46 N ATOM 2030 CA SER A 258 -1.512 31.258 15.734 1.00 8.98 C ANISOU 2030 CA SER A 258 779 1228 1405 247 89 -137 C ATOM 2031 C SER A 258 -0.520 31.205 16.888 1.00 8.88 C ANISOU 2031 C SER A 258 815 1241 1318 133 92 -51 C ATOM 2032 O SER A 258 -0.495 32.131 17.697 1.00 11.49 O ANISOU 2032 O SER A 258 1324 1488 1554 321 -121 -213 O ATOM 2033 CB SER A 258 -2.850 30.666 16.170 1.00 11.41 C ANISOU 2033 CB SER A 258 847 1904 1585 130 260 -233 C ATOM 2034 OG ASER A 258 -2.792 29.305 16.431 0.70 14.05 O ANISOU 2034 OG ASER A 258 1351 1902 2086 -299 221 -22 O ATOM 2035 OG BSER A 258 -3.868 30.884 15.224 0.30 14.30 O ANISOU 2035 OG BSER A 258 796 2445 2194 353 23 -167 O ATOM 2036 N ARG A 259 0.301 30.144 16.964 1.00 8.07 N ANISOU 2036 N ARG A 259 734 1166 1166 92 15 -8 N ATOM 2037 CA ARG A 259 1.282 29.964 18.021 1.00 8.23 C ANISOU 2037 CA ARG A 259 779 1295 1052 20 72 29 C ATOM 2038 C ARG A 259 2.705 30.398 17.657 1.00 7.03 C ANISOU 2038 C ARG A 259 788 931 953 90 67 95 C ATOM 2039 O ARG A 259 3.654 30.092 18.409 1.00 8.56 O ANISOU 2039 O ARG A 259 791 1479 981 26 0 231 O ATOM 2040 CB ARG A 259 1.257 28.517 18.542 1.00 10.62 C ANISOU 2040 CB ARG A 259 1032 1508 1494 -176 57 353 C ATOM 2041 CG ARG A 259 -0.093 28.093 19.099 1.00 13.45 C ANISOU 2041 CG ARG A 259 1102 2079 1930 -423 -57 619 C ATOM 2042 CD ARG A 259 -0.062 26.778 19.853 1.00 15.85 C ANISOU 2042 CD ARG A 259 2041 2086 1897 -798 -110 603 C ATOM 2043 NE ARG A 259 0.631 26.925 21.123 1.00 14.83 N ANISOU 2043 NE ARG A 259 1600 2358 1679 -407 218 365 N ATOM 2044 CZ ARG A 259 0.417 26.183 22.198 1.00 15.74 C ANISOU 2044 CZ ARG A 259 2045 2376 1558 -381 367 292 C ATOM 2045 NH1 ARG A 259 -0.499 25.207 22.189 1.00 18.35 N ANISOU 2045 NH1 ARG A 259 2505 2484 1983 -596 448 222 N ATOM 2046 NH2 ARG A 259 1.125 26.424 23.292 1.00 19.50 N ANISOU 2046 NH2 ARG A 259 2509 3129 1772 -719 42 461 N ATOM 2047 N CYS A 260 2.889 31.149 16.567 1.00 7.07 N ANISOU 2047 N CYS A 260 774 998 915 -10 -84 131 N ATOM 2048 CA CYS A 260 4.194 31.729 16.250 1.00 7.50 C ANISOU 2048 CA CYS A 260 824 1023 1004 29 -27 91 C ATOM 2049 C CYS A 260 4.374 32.999 17.085 1.00 6.89 C ANISOU 2049 C CYS A 260 730 890 1000 82 -17 114 C ATOM 2050 O CYS A 260 3.639 33.991 16.910 1.00 9.49 O ANISOU 2050 O CYS A 260 1026 1038 1540 223 -253 -113 O ATOM 2051 CB CYS A 260 4.365 32.021 14.758 1.00 8.12 C ANISOU 2051 CB CYS A 260 767 1293 1025 -11 39 194 C ATOM 2052 SG CYS A 260 6.069 32.623 14.416 1.00 7.97 S ANISOU 2052 SG CYS A 260 722 1404 904 -11 -13 200 S ATOM 2053 N LEU A 261 5.310 32.994 18.024 1.00 6.41 N ANISOU 2053 N LEU A 261 693 901 841 44 54 -18 N ATOM 2054 CA LEU A 261 5.491 34.076 18.986 1.00 7.07 C ANISOU 2054 CA LEU A 261 742 1018 925 -74 167 -105 C ATOM 2055 C LEU A 261 6.126 35.333 18.423 1.00 6.75 C ANISOU 2055 C LEU A 261 578 884 1101 -28 143 -101 C ATOM 2056 O LEU A 261 5.873 36.441 18.921 1.00 8.24 O ANISOU 2056 O LEU A 261 1014 913 1204 43 166 -104 O ATOM 2057 CB LEU A 261 6.323 33.580 20.196 1.00 8.71 C ANISOU 2057 CB LEU A 261 1210 1132 967 -92 3 -47 C ATOM 2058 CG LEU A 261 5.772 32.365 20.953 1.00 10.31 C ANISOU 2058 CG LEU A 261 1493 1365 1059 -345 -71 125 C ATOM 2059 CD1 LEU A 261 6.738 31.958 22.048 1.00 13.57 C ANISOU 2059 CD1 LEU A 261 2128 1728 1300 -512 -435 396 C ATOM 2060 CD2 LEU A 261 4.375 32.635 21.500 1.00 14.97 C ANISOU 2060 CD2 LEU A 261 1950 2042 1697 -299 608 274 C ATOM 2061 N GLY A 262 7.016 35.170 17.442 1.00 7.10 N ANISOU 2061 N GLY A 262 710 894 1094 -65 216 4 N ATOM 2062 CA GLY A 262 7.793 36.286 16.937 1.00 7.56 C ANISOU 2062 CA GLY A 262 849 916 1107 -19 176 65 C ATOM 2063 C GLY A 262 9.031 35.816 16.189 1.00 6.43 C ANISOU 2063 C GLY A 262 777 816 848 -72 47 6 C ATOM 2064 O GLY A 262 9.262 34.607 16.012 1.00 7.77 O ANISOU 2064 O GLY A 262 900 872 1179 -8 211 80 O ATOM 2065 N ILE A 263 9.802 36.811 15.754 1.00 6.53 N ANISOU 2065 N ILE A 263 738 732 1011 -60 154 -74 N ATOM 2066 CA ILE A 263 10.983 36.654 14.901 1.00 6.00 C ANISOU 2066 CA ILE A 263 709 798 772 -18 102 -93 C ATOM 2067 C ILE A 263 12.155 37.412 15.518 1.00 6.10 C ANISOU 2067 C ILE A 263 790 687 840 6 9 -22 C ATOM 2068 O ILE A 263 11.981 38.590 15.852 1.00 8.50 O ANISOU 2068 O ILE A 263 837 823 1571 76 -67 -231 O ATOM 2069 CB ILE A 263 10.689 37.222 13.477 1.00 7.65 C ANISOU 2069 CB ILE A 263 924 1049 935 22 -11 5 C ATOM 2070 CG1 ILE A 263 9.557 36.457 12.804 1.00 11.18 C ANISOU 2070 CG1 ILE A 263 1543 1577 1126 -208 -454 64 C ATOM 2071 CG2 ILE A 263 11.944 37.217 12.612 1.00 9.94 C ANISOU 2071 CG2 ILE A 263 1350 1427 1001 123 252 130 C ATOM 2072 CD1 ILE A 263 9.003 37.053 11.546 1.00 16.30 C ANISOU 2072 CD1 ILE A 263 2364 2215 1615 -663 -979 453 C ATOM 2073 N THR A 264 13.315 36.766 15.604 1.00 6.38 N ANISOU 2073 N THR A 264 649 694 1080 -1 57 -57 N ATOM 2074 CA THR A 264 14.592 37.435 15.921 1.00 6.02 C ANISOU 2074 CA THR A 264 600 815 871 -25 73 33 C ATOM 2075 C THR A 264 15.494 37.338 14.690 1.00 5.99 C ANISOU 2075 C THR A 264 641 734 902 39 30 -85 C ATOM 2076 O THR A 264 15.670 36.221 14.166 1.00 7.69 O ANISOU 2076 O THR A 264 1133 814 975 -54 297 -108 O ATOM 2077 CB THR A 264 15.284 36.737 17.106 1.00 6.28 C ANISOU 2077 CB THR A 264 675 793 916 14 41 -76 C ATOM 2078 OG1 THR A 264 14.444 36.926 18.269 1.00 7.21 O ANISOU 2078 OG1 THR A 264 899 1043 798 -84 92 12 O ATOM 2079 CG2 THR A 264 16.685 37.272 17.355 1.00 7.43 C ANISOU 2079 CG2 THR A 264 717 961 1147 44 -38 102 C ATOM 2080 N VAL A 265 16.062 38.448 14.220 1.00 6.40 N ANISOU 2080 N VAL A 265 826 804 802 -42 149 -32 N ATOM 2081 CA VAL A 265 17.091 38.476 13.188 1.00 7.10 C ANISOU 2081 CA VAL A 265 920 941 837 -112 156 -44 C ATOM 2082 C VAL A 265 18.463 38.444 13.871 1.00 7.10 C ANISOU 2082 C VAL A 265 950 979 766 -167 255 -116 C ATOM 2083 O VAL A 265 18.668 39.034 14.938 1.00 8.38 O ANISOU 2083 O VAL A 265 942 1296 948 -76 168 -288 O ATOM 2084 CB VAL A 265 16.970 39.648 12.216 1.00 8.69 C ANISOU 2084 CB VAL A 265 1211 1173 918 -80 138 109 C ATOM 2085 CG1 VAL A 265 15.781 39.448 11.290 1.00 12.17 C ANISOU 2085 CG1 VAL A 265 1686 1658 1281 -70 -321 262 C ATOM 2086 CG2 VAL A 265 17.004 41.009 12.878 1.00 9.87 C ANISOU 2086 CG2 VAL A 265 1279 1086 1383 -159 76 108 C ATOM 2087 N TRP A 266 19.446 37.758 13.250 1.00 6.73 N ANISOU 2087 N TRP A 266 868 938 750 -81 132 -123 N ATOM 2088 CA TRP A 266 20.726 37.485 13.932 1.00 6.84 C ANISOU 2088 CA TRP A 266 955 780 864 -105 44 0 C ATOM 2089 C TRP A 266 21.765 38.593 13.721 1.00 7.13 C ANISOU 2089 C TRP A 266 855 786 1068 -64 196 -89 C ATOM 2090 O TRP A 266 22.856 38.388 13.162 1.00 8.73 O ANISOU 2090 O TRP A 266 987 1013 1316 -92 271 -109 O ATOM 2091 CB TRP A 266 21.229 36.079 13.553 1.00 7.85 C ANISOU 2091 CB TRP A 266 912 861 1211 -129 138 -60 C ATOM 2092 CG TRP A 266 22.120 35.466 14.585 1.00 8.60 C ANISOU 2092 CG TRP A 266 1110 791 1368 -63 102 96 C ATOM 2093 CD1 TRP A 266 23.407 35.057 14.396 1.00 10.37 C ANISOU 2093 CD1 TRP A 266 1175 1188 1578 10 123 64 C ATOM 2094 CD2 TRP A 266 21.811 35.163 15.953 1.00 8.35 C ANISOU 2094 CD2 TRP A 266 1114 737 1322 -126 104 34 C ATOM 2095 NE1 TRP A 266 23.904 34.522 15.546 1.00 11.89 N ANISOU 2095 NE1 TRP A 266 1075 1616 1829 566 162 256 N ATOM 2096 CE2 TRP A 266 22.960 34.580 16.538 1.00 10.32 C ANISOU 2096 CE2 TRP A 266 1245 1230 1446 77 101 227 C ATOM 2097 CE3 TRP A 266 20.693 35.342 16.768 1.00 8.64 C ANISOU 2097 CE3 TRP A 266 1217 962 1104 -219 71 -160 C ATOM 2098 CZ2 TRP A 266 22.999 34.184 17.881 1.00 12.40 C ANISOU 2098 CZ2 TRP A 266 1597 1513 1601 216 34 414 C ATOM 2099 CZ3 TRP A 266 20.711 34.953 18.093 1.00 10.33 C ANISOU 2099 CZ3 TRP A 266 1522 1196 1209 -355 155 42 C ATOM 2100 CH2 TRP A 266 21.869 34.376 18.632 1.00 12.75 C ANISOU 2100 CH2 TRP A 266 1923 1570 1351 25 150 303 C ATOM 2101 N GLY A 267 21.439 39.781 14.218 1.00 7.30 N ANISOU 2101 N GLY A 267 858 771 1145 -136 167 -125 N ATOM 2102 CA GLY A 267 22.282 40.960 14.152 1.00 7.80 C ANISOU 2102 CA GLY A 267 910 802 1250 -180 -86 5 C ATOM 2103 C GLY A 267 21.558 42.190 13.627 1.00 7.50 C ANISOU 2103 C GLY A 267 875 880 1093 -71 115 -89 C ATOM 2104 O GLY A 267 20.421 42.125 13.160 1.00 9.82 O ANISOU 2104 O GLY A 267 1087 961 1685 -159 -260 145 O ATOM 2105 N VAL A 268 22.263 43.321 13.667 1.00 7.67 N ANISOU 2105 N VAL A 268 800 728 1386 -38 62 -20 N ATOM 2106 CA VAL A 268 21.707 44.627 13.271 1.00 8.49 C ANISOU 2106 CA VAL A 268 890 869 1468 -30 142 65 C ATOM 2107 C VAL A 268 22.137 44.997 11.848 1.00 8.10 C ANISOU 2107 C VAL A 268 869 812 1399 -63 36 86 C ATOM 2108 O VAL A 268 21.327 44.901 10.902 1.00 10.46 O ANISOU 2108 O VAL A 268 1082 1402 1489 -309 -162 362 O ATOM 2109 CB VAL A 268 22.031 45.700 14.332 1.00 9.40 C ANISOU 2109 CB VAL A 268 1123 912 1535 -47 250 -83 C ATOM 2110 CG1 VAL A 268 21.394 47.041 13.957 1.00 12.30 C ANISOU 2110 CG1 VAL A 268 1764 946 1965 165 444 -52 C ATOM 2111 CG2 VAL A 268 21.536 45.278 15.721 1.00 11.36 C ANISOU 2111 CG2 VAL A 268 1455 1256 1604 -222 476 -143 C ATOM 2112 N ARG A 269 23.364 45.447 11.632 1.00 8.27 N ANISOU 2112 N ARG A 269 856 905 1381 -26 139 33 N ATOM 2113 CA ARG A 269 23.895 45.776 10.315 1.00 7.99 C ANISOU 2113 CA ARG A 269 857 915 1262 6 6 84 C ATOM 2114 C ARG A 269 24.557 44.555 9.694 1.00 7.45 C ANISOU 2114 C ARG A 269 813 862 1154 -182 79 119 C ATOM 2115 O ARG A 269 25.072 43.687 10.409 1.00 8.04 O ANISOU 2115 O ARG A 269 930 928 1197 -50 89 102 O ATOM 2116 CB ARG A 269 24.915 46.919 10.416 1.00 8.70 C ANISOU 2116 CB ARG A 269 1021 1137 1146 -183 101 -16 C ATOM 2117 CG ARG A 269 24.426 48.198 11.077 1.00 10.55 C ANISOU 2117 CG ARG A 269 1375 1044 1587 73 -86 -16 C ATOM 2118 CD ARG A 269 25.554 49.113 11.533 1.00 12.08 C ANISOU 2118 CD ARG A 269 1693 1072 1826 21 -345 -88 C ATOM 2119 NE ARG A 269 26.307 48.504 12.630 1.00 10.95 N ANISOU 2119 NE ARG A 269 1516 1074 1572 -85 -157 -65 N ATOM 2120 CZ ARG A 269 27.192 49.130 13.389 1.00 11.24 C ANISOU 2120 CZ ARG A 269 1625 1139 1508 -148 -89 -180 C ATOM 2121 NH1 ARG A 269 27.479 50.432 13.219 1.00 13.50 N ANISOU 2121 NH1 ARG A 269 2259 1164 1707 -212 -377 -17 N ATOM 2122 NH2 ARG A 269 27.820 48.435 14.348 1.00 11.32 N ANISOU 2122 NH2 ARG A 269 1406 1188 1706 -251 -58 -36 N ATOM 2123 N ASP A 270 24.712 44.553 8.354 1.00 8.23 N ANISOU 2123 N ASP A 270 988 999 1139 19 54 150 N ATOM 2124 CA ASP A 270 25.447 43.474 7.687 1.00 8.21 C ANISOU 2124 CA ASP A 270 959 1046 1116 -125 178 59 C ATOM 2125 C ASP A 270 26.837 43.284 8.302 1.00 8.90 C ANISOU 2125 C ASP A 270 1038 1175 1167 -34 219 26 C ATOM 2126 O ASP A 270 27.280 42.136 8.474 1.00 10.40 O ANISOU 2126 O ASP A 270 1370 1229 1354 199 290 -14 O ATOM 2127 CB ASP A 270 25.563 43.723 6.180 1.00 9.75 C ANISOU 2127 CB ASP A 270 1298 1245 1161 -196 79 114 C ATOM 2128 CG ASP A 270 24.292 43.441 5.395 1.00 10.05 C ANISOU 2128 CG ASP A 270 1296 1424 1100 -180 130 39 C ATOM 2129 OD1 ASP A 270 23.432 42.664 5.889 1.00 11.53 O ANISOU 2129 OD1 ASP A 270 1451 1434 1498 -432 -5 86 O ATOM 2130 OD2 ASP A 270 24.175 43.983 4.268 1.00 14.04 O ANISOU 2130 OD2 ASP A 270 1742 2284 1307 -529 -78 418 O ATOM 2131 N SER A 271 27.538 44.370 8.650 1.00 9.10 N ANISOU 2131 N SER A 271 867 1234 1356 -72 6 261 N ATOM 2132 CA SER A 271 28.873 44.294 9.228 1.00 10.63 C ANISOU 2132 CA SER A 271 885 1646 1509 -180 -16 384 C ATOM 2133 C SER A 271 28.927 43.720 10.623 1.00 9.75 C ANISOU 2133 C SER A 271 904 1345 1458 -5 -46 313 C ATOM 2134 O SER A 271 30.025 43.376 11.091 1.00 12.61 O ANISOU 2134 O SER A 271 889 1966 1937 -39 -25 612 O ATOM 2135 CB SER A 271 29.540 45.686 9.162 1.00 14.28 C ANISOU 2135 CB SER A 271 1131 2095 2201 -581 -407 920 C ATOM 2136 OG SER A 271 28.701 46.640 9.784 1.00 17.83 O ANISOU 2136 OG SER A 271 1931 1571 3272 -598 -767 215 O ATOM 2137 N ASP A 272 27.780 43.555 11.314 1.00 8.55 N ANISOU 2137 N ASP A 272 983 1101 1166 -42 33 144 N ATOM 2138 CA ASP A 272 27.702 42.942 12.627 1.00 7.69 C ANISOU 2138 CA ASP A 272 899 896 1127 32 -54 10 C ATOM 2139 C ASP A 272 27.495 41.436 12.551 1.00 8.21 C ANISOU 2139 C ASP A 272 1020 934 1164 18 22 -13 C ATOM 2140 O ASP A 272 27.536 40.734 13.589 1.00 10.60 O ANISOU 2140 O ASP A 272 1737 980 1308 158 39 150 O ATOM 2141 CB ASP A 272 26.562 43.566 13.440 1.00 9.47 C ANISOU 2141 CB ASP A 272 1088 1036 1474 51 109 -128 C ATOM 2142 CG ASP A 272 26.673 45.059 13.658 1.00 8.43 C ANISOU 2142 CG ASP A 272 925 1022 1255 30 21 -49 C ATOM 2143 OD1 ASP A 272 27.764 45.509 14.087 1.00 9.49 O ANISOU 2143 OD1 ASP A 272 1097 1107 1402 -22 -71 -83 O ATOM 2144 OD2 ASP A 272 25.655 45.766 13.406 1.00 8.94 O ANISOU 2144 OD2 ASP A 272 1086 1069 1243 70 -69 36 O ATOM 2145 N SER A 273 27.239 40.900 11.357 1.00 9.16 N ANISOU 2145 N SER A 273 1368 852 1261 -163 117 -45 N ATOM 2146 CA SER A 273 26.919 39.505 11.176 1.00 9.28 C ANISOU 2146 CA SER A 273 1294 935 1297 -198 91 -41 C ATOM 2147 C SER A 273 28.105 38.580 11.280 1.00 10.59 C ANISOU 2147 C SER A 273 1309 1066 1650 -200 -101 -198 C ATOM 2148 O SER A 273 29.165 38.864 10.718 1.00 11.91 O ANISOU 2148 O SER A 273 1198 1359 1970 32 46 -174 O ATOM 2149 CB SER A 273 26.250 39.285 9.818 1.00 9.20 C ANISOU 2149 CB SER A 273 1038 1087 1373 -218 129 -143 C ATOM 2150 OG SER A 273 25.980 37.945 9.523 1.00 10.30 O ANISOU 2150 OG SER A 273 1211 1209 1492 -181 12 -248 O ATOM 2151 N TRP A 274 27.835 37.368 11.811 1.00 11.59 N ANISOU 2151 N TRP A 274 1523 1146 1734 -47 -182 41 N ATOM 2152 CA TRP A 274 28.765 36.263 11.827 1.00 13.27 C ANISOU 2152 CA TRP A 274 1449 1606 1989 160 -24 202 C ATOM 2153 C TRP A 274 29.094 35.807 10.401 1.00 13.98 C ANISOU 2153 C TRP A 274 1570 1444 2297 306 149 -102 C ATOM 2154 O TRP A 274 30.073 35.087 10.194 1.00 18.17 O ANISOU 2154 O TRP A 274 1998 2004 2902 652 339 -374 O ATOM 2155 CB TRP A 274 28.258 35.078 12.655 1.00 13.53 C ANISOU 2155 CB TRP A 274 1495 1515 2131 -97 -34 100 C ATOM 2156 CG TRP A 274 27.076 34.305 12.141 1.00 13.37 C ANISOU 2156 CG TRP A 274 1630 1352 2098 64 -339 42 C ATOM 2157 CD1 TRP A 274 25.929 34.771 11.566 1.00 12.24 C ANISOU 2157 CD1 TRP A 274 1453 1422 1777 -74 -117 35 C ATOM 2158 CD2 TRP A 274 26.931 32.874 12.177 1.00 16.08 C ANISOU 2158 CD2 TRP A 274 1802 1416 2893 -67 -282 -53 C ATOM 2159 NE1 TRP A 274 25.072 33.734 11.227 1.00 12.77 N ANISOU 2159 NE1 TRP A 274 1329 1534 1990 8 17 -181 N ATOM 2160 CE2 TRP A 274 25.677 32.548 11.611 1.00 15.40 C ANISOU 2160 CE2 TRP A 274 1497 1463 2893 -44 50 -17 C ATOM 2161 CE3 TRP A 274 27.741 31.828 12.649 1.00 23.99 C ANISOU 2161 CE3 TRP A 274 2335 2372 4409 546 -443 427 C ATOM 2162 CZ2 TRP A 274 25.214 31.235 11.505 1.00 19.72 C ANISOU 2162 CZ2 TRP A 274 2083 1651 3758 -333 28 -88 C ATOM 2163 CZ3 TRP A 274 27.288 30.528 12.533 1.00 29.47 C ANISOU 2163 CZ3 TRP A 274 3204 2822 5173 -148 -349 138 C ATOM 2164 CH2 TRP A 274 26.036 30.244 11.962 1.00 27.21 C ANISOU 2164 CH2 TRP A 274 3219 2324 4797 135 -455 390 C ATOM 2165 N ARG A 275 28.264 36.159 9.417 1.00 12.62 N ANISOU 2165 N ARG A 275 1378 1386 2032 40 208 -279 N ATOM 2166 CA ARG A 275 28.440 35.885 8.003 1.00 14.73 C ANISOU 2166 CA ARG A 275 1811 1774 2010 32 273 -266 C ATOM 2167 C ARG A 275 28.298 37.142 7.141 1.00 12.61 C ANISOU 2167 C ARG A 275 1234 1671 1887 -40 447 -412 C ATOM 2168 O ARG A 275 27.576 37.257 6.133 1.00 13.69 O ANISOU 2168 O ARG A 275 1368 1863 1970 -218 419 -355 O ATOM 2169 CB ARG A 275 27.520 34.761 7.569 1.00 19.72 C ANISOU 2169 CB ARG A 275 3248 2146 2098 -523 97 -499 C ATOM 2170 CG AARG A 275 27.684 33.443 8.297 0.50 25.52 C ANISOU 2170 CG AARG A 275 4298 2677 2720 88 712 93 C ATOM 2171 CD AARG A 275 26.686 32.383 7.897 0.50 33.62 C ANISOU 2171 CD AARG A 275 4054 4418 4303 -388 119 -336 C ATOM 2172 NE AARG A 275 27.029 31.091 8.500 0.50 37.43 N ANISOU 2172 NE AARG A 275 5222 4852 4148 109 281 -63 N ATOM 2173 CZ AARG A 275 26.246 30.021 8.396 0.50 40.91 C ANISOU 2173 CZ AARG A 275 5425 5180 4938 -138 268 -294 C ATOM 2174 NH1AARG A 275 25.100 30.088 7.734 0.50 34.51 N ANISOU 2174 NH1AARG A 275 5059 3968 4087 -545 746 -650 N ATOM 2175 NH2AARG A 275 26.619 28.885 8.968 0.50 42.40 N ANISOU 2175 NH2AARG A 275 5589 5086 5434 -188 228 -234 N ATOM 2176 CG BARG A 275 27.949 33.376 8.052 0.50 24.97 C ANISOU 2176 CG BARG A 275 4029 2342 3118 -294 51 -150 C ATOM 2177 CD BARG A 275 26.979 32.235 7.799 0.50 26.30 C ANISOU 2177 CD BARG A 275 2855 3335 3803 -283 -104 -286 C ATOM 2178 NE BARG A 275 25.617 32.713 8.061 0.50 29.30 N ANISOU 2178 NE BARG A 275 3106 4262 3765 378 -256 34 N ATOM 2179 CZ BARG A 275 24.912 33.325 7.111 0.50 27.40 C ANISOU 2179 CZ BARG A 275 3177 3954 3281 236 163 191 C ATOM 2180 NH1BARG A 275 25.471 33.498 5.931 0.50 34.14 N ANISOU 2180 NH1BARG A 275 4336 5163 3472 -31 642 58 N ATOM 2181 NH2BARG A 275 23.729 33.795 7.406 0.50 32.18 N ANISOU 2181 NH2BARG A 275 3268 4601 4356 334 393 -147 N ATOM 2182 N SER A 276 29.053 38.189 7.542 1.00 13.19 N ANISOU 2182 N SER A 276 1330 1528 2153 -79 216 -199 N ATOM 2183 CA SER A 276 29.022 39.495 6.911 1.00 12.91 C ANISOU 2183 CA SER A 276 1277 1790 1838 -182 230 -54 C ATOM 2184 C SER A 276 29.274 39.474 5.421 1.00 14.29 C ANISOU 2184 C SER A 276 1483 2047 1901 -203 301 -187 C ATOM 2185 O SER A 276 28.682 40.266 4.673 1.00 15.32 O ANISOU 2185 O SER A 276 1558 2348 1916 -316 331 102 O ATOM 2186 CB SER A 276 29.962 40.460 7.645 1.00 14.46 C ANISOU 2186 CB SER A 276 1333 1880 2280 -277 231 -189 C ATOM 2187 OG SER A 276 31.335 40.119 7.519 1.00 17.01 O ANISOU 2187 OG SER A 276 1439 2226 2798 -298 473 -554 O ATOM 2188 N GLU A 277 30.073 38.529 4.915 1.00 15.77 N ANISOU 2188 N GLU A 277 1419 2577 1997 -223 736 -434 N ATOM 2189 CA GLU A 277 30.343 38.432 3.491 1.00 17.36 C ANISOU 2189 CA GLU A 277 1746 2879 1971 -109 677 -480 C ATOM 2190 C GLU A 277 29.122 38.077 2.655 1.00 17.92 C ANISOU 2190 C GLU A 277 1648 2905 2255 -90 605 -274 C ATOM 2191 O GLU A 277 29.075 38.332 1.441 1.00 22.49 O ANISOU 2191 O GLU A 277 2218 3991 2335 -211 761 -55 O ATOM 2192 CB GLU A 277 31.493 37.463 3.197 1.00 21.25 C ANISOU 2192 CB GLU A 277 2079 3217 2777 245 868 -361 C ATOM 2193 CG GLU A 277 31.206 36.013 3.473 1.00 25.37 C ANISOU 2193 CG GLU A 277 2776 3096 3766 393 406 -304 C ATOM 2194 CD GLU A 277 31.129 35.531 4.895 1.00 32.95 C ANISOU 2194 CD GLU A 277 4420 4301 3797 142 119 -48 C ATOM 2195 OE1 GLU A 277 31.407 36.259 5.874 1.00 28.40 O ANISOU 2195 OE1 GLU A 277 3579 3599 3613 728 757 -56 O ATOM 2196 OE2 GLU A 277 30.764 34.337 5.055 1.00 39.89 O ANISOU 2196 OE2 GLU A 277 5232 4233 5691 68 118 -131 O ATOM 2197 N GLN A 278 28.085 37.535 3.289 1.00 14.82 N ANISOU 2197 N GLN A 278 1428 2059 2144 -35 431 -456 N ATOM 2198 CA GLN A 278 26.839 37.172 2.618 1.00 14.64 C ANISOU 2198 CA GLN A 278 1579 2050 1932 2 408 -644 C ATOM 2199 C GLN A 278 25.754 38.235 2.726 1.00 13.60 C ANISOU 2199 C GLN A 278 1553 1952 1662 -35 502 -286 C ATOM 2200 O GLN A 278 24.590 38.017 2.318 1.00 14.16 O ANISOU 2200 O GLN A 278 1625 1981 1773 73 359 -324 O ATOM 2201 CB GLN A 278 26.364 35.817 3.191 1.00 16.76 C ANISOU 2201 CB GLN A 278 1874 1935 2557 -81 213 -583 C ATOM 2202 CG GLN A 278 27.326 34.673 2.877 1.00 21.80 C ANISOU 2202 CG GLN A 278 2165 2452 3665 296 213 -816 C ATOM 2203 CD GLN A 278 26.930 33.340 3.451 1.00 30.62 C ANISOU 2203 CD GLN A 278 3866 3079 4687 -215 119 -92 C ATOM 2204 OE1 GLN A 278 25.749 33.012 3.574 1.00 31.33 O ANISOU 2204 OE1 GLN A 278 3979 3089 4836 -351 176 295 O ATOM 2205 NE2 GLN A 278 27.898 32.513 3.852 1.00 38.92 N ANISOU 2205 NE2 GLN A 278 4935 4240 5612 795 49 225 N ATOM 2206 N THR A 279 26.083 39.427 3.223 1.00 13.07 N ANISOU 2206 N THR A 279 1356 1889 1719 -217 826 -161 N ATOM 2207 CA THR A 279 25.195 40.582 3.409 1.00 12.80 C ANISOU 2207 CA THR A 279 1396 1807 1661 -201 709 -29 C ATOM 2208 C THR A 279 23.747 40.199 3.712 1.00 10.37 C ANISOU 2208 C THR A 279 1306 1276 1357 -115 439 89 C ATOM 2209 O THR A 279 22.817 40.492 2.931 1.00 12.16 O ANISOU 2209 O THR A 279 1634 1656 1332 -49 352 220 O ATOM 2210 CB THR A 279 25.285 41.522 2.189 1.00 16.69 C ANISOU 2210 CB THR A 279 1954 2397 1990 -287 843 395 C ATOM 2211 OG1 THR A 279 24.733 40.910 1.008 1.00 19.12 O ANISOU 2211 OG1 THR A 279 2758 2856 1652 -196 732 531 O ATOM 2212 CG2 THR A 279 26.726 41.935 1.879 1.00 20.79 C ANISOU 2212 CG2 THR A 279 2007 2907 2985 -382 975 752 C ATOM 2213 N PRO A 280 23.482 39.563 4.858 1.00 9.09 N ANISOU 2213 N PRO A 280 1064 1214 1175 -130 347 -30 N ATOM 2214 CA PRO A 280 22.235 38.831 5.050 1.00 8.36 C ANISOU 2214 CA PRO A 280 1025 1155 998 -140 244 -33 C ATOM 2215 C PRO A 280 21.181 39.447 5.941 1.00 7.71 C ANISOU 2215 C PRO A 280 804 1085 1039 -15 129 -90 C ATOM 2216 O PRO A 280 20.172 38.779 6.242 1.00 8.81 O ANISOU 2216 O PRO A 280 1003 1095 1250 -72 313 -83 O ATOM 2217 CB PRO A 280 22.780 37.512 5.642 1.00 9.92 C ANISOU 2217 CB PRO A 280 1146 1219 1405 47 380 -20 C ATOM 2218 CG PRO A 280 23.896 37.942 6.541 1.00 11.55 C ANISOU 2218 CG PRO A 280 1509 1486 1395 32 74 122 C ATOM 2219 CD PRO A 280 24.487 39.162 5.876 1.00 10.19 C ANISOU 2219 CD PRO A 280 1013 1492 1368 -46 193 -153 C ATOM 2220 N LEU A 281 21.388 40.706 6.354 1.00 8.19 N ANISOU 2220 N LEU A 281 1060 968 1083 10 323 22 N ATOM 2221 CA LEU A 281 20.554 41.399 7.343 1.00 7.39 C ANISOU 2221 CA LEU A 281 763 1036 1009 -109 143 -25 C ATOM 2222 C LEU A 281 19.793 42.580 6.747 1.00 7.91 C ANISOU 2222 C LEU A 281 991 1126 888 -18 67 -40 C ATOM 2223 O LEU A 281 19.770 42.797 5.526 1.00 9.78 O ANISOU 2223 O LEU A 281 1380 1373 964 123 23 20 O ATOM 2224 CB LEU A 281 21.421 41.757 8.566 1.00 7.62 C ANISOU 2224 CB LEU A 281 1018 872 1007 -132 89 47 C ATOM 2225 CG LEU A 281 21.945 40.566 9.378 1.00 7.82 C ANISOU 2225 CG LEU A 281 1034 932 1004 79 91 27 C ATOM 2226 CD1 LEU A 281 22.902 41.036 10.453 1.00 10.15 C ANISOU 2226 CD1 LEU A 281 1177 1273 1407 77 -211 -6 C ATOM 2227 CD2 LEU A 281 20.812 39.753 9.997 1.00 10.59 C ANISOU 2227 CD2 LEU A 281 1491 1250 1283 -267 -72 327 C ATOM 2228 N LEU A 282 19.087 43.342 7.599 1.00 7.55 N ANISOU 2228 N LEU A 282 986 992 891 53 73 77 N ATOM 2229 CA LEU A 282 18.124 44.349 7.159 1.00 7.73 C ANISOU 2229 CA LEU A 282 924 994 1018 -8 -4 80 C ATOM 2230 C LEU A 282 18.664 45.772 7.038 1.00 7.90 C ANISOU 2230 C LEU A 282 1024 1044 933 22 -9 282 C ATOM 2231 O LEU A 282 17.974 46.629 6.462 1.00 10.14 O ANISOU 2231 O LEU A 282 1171 1084 1599 -62 -224 480 O ATOM 2232 CB LEU A 282 16.903 44.355 8.112 1.00 8.17 C ANISOU 2232 CB LEU A 282 893 1033 1178 -20 28 41 C ATOM 2233 CG LEU A 282 16.104 43.044 8.194 1.00 10.02 C ANISOU 2233 CG LEU A 282 1040 1139 1629 -85 147 286 C ATOM 2234 CD1 LEU A 282 14.955 43.171 9.197 1.00 13.89 C ANISOU 2234 CD1 LEU A 282 1415 1717 2144 -56 592 454 C ATOM 2235 CD2 LEU A 282 15.570 42.621 6.829 1.00 12.19 C ANISOU 2235 CD2 LEU A 282 1348 1337 1945 -335 78 -121 C ATOM 2236 N PHE A 283 19.838 46.056 7.615 1.00 8.42 N ANISOU 2236 N PHE A 283 978 989 1233 -24 -51 239 N ATOM 2237 CA PHE A 283 20.459 47.368 7.589 1.00 9.01 C ANISOU 2237 CA PHE A 283 1131 977 1315 -63 214 160 C ATOM 2238 C PHE A 283 21.841 47.289 6.931 1.00 8.83 C ANISOU 2238 C PHE A 283 958 1130 1269 -91 -41 223 C ATOM 2239 O PHE A 283 22.605 46.341 7.134 1.00 9.68 O ANISOU 2239 O PHE A 283 1107 1127 1445 14 100 226 O ATOM 2240 CB PHE A 283 20.619 47.982 9.002 1.00 9.70 C ANISOU 2240 CB PHE A 283 1132 1147 1406 -71 -29 142 C ATOM 2241 CG PHE A 283 19.307 48.235 9.698 1.00 9.05 C ANISOU 2241 CG PHE A 283 1115 1148 1177 14 -57 34 C ATOM 2242 CD1 PHE A 283 18.690 47.270 10.464 1.00 11.05 C ANISOU 2242 CD1 PHE A 283 1221 1517 1461 9 85 270 C ATOM 2243 CD2 PHE A 283 18.643 49.445 9.553 1.00 11.81 C ANISOU 2243 CD2 PHE A 283 1595 1295 1598 241 -60 115 C ATOM 2244 CE1 PHE A 283 17.465 47.492 11.086 1.00 14.10 C ANISOU 2244 CE1 PHE A 283 1483 2077 1796 -280 420 -32 C ATOM 2245 CE2 PHE A 283 17.428 49.701 10.169 1.00 14.09 C ANISOU 2245 CE2 PHE A 283 1694 1929 1731 519 -177 -462 C ATOM 2246 CZ PHE A 283 16.846 48.711 10.931 1.00 14.60 C ANISOU 2246 CZ PHE A 283 1152 2633 1760 220 15 -488 C ATOM 2247 N ASN A 284 22.144 48.322 6.129 1.00 9.98 N ANISOU 2247 N ASN A 284 1180 1118 1494 -86 250 234 N ATOM 2248 CA ASN A 284 23.440 48.498 5.509 1.00 10.40 C ANISOU 2248 CA ASN A 284 1280 1335 1336 -219 223 249 C ATOM 2249 C ASN A 284 24.484 48.841 6.577 1.00 10.74 C ANISOU 2249 C ASN A 284 1202 1291 1587 -154 137 254 C ATOM 2250 O ASN A 284 24.177 49.220 7.727 1.00 12.20 O ANISOU 2250 O ASN A 284 1410 1449 1775 -333 294 127 O ATOM 2251 CB ASN A 284 23.383 49.612 4.452 1.00 13.58 C ANISOU 2251 CB ASN A 284 1486 1909 1765 -232 129 728 C ATOM 2252 CG ASN A 284 22.636 49.218 3.208 1.00 14.10 C ANISOU 2252 CG ASN A 284 1754 1846 1758 -199 262 361 C ATOM 2253 OD1 ASN A 284 22.956 48.179 2.604 1.00 16.71 O ANISOU 2253 OD1 ASN A 284 2486 2158 1705 121 169 142 O ATOM 2254 ND2 ASN A 284 21.657 50.021 2.807 1.00 16.92 N ANISOU 2254 ND2 ASN A 284 2305 2179 1945 62 -110 451 N ATOM 2255 N ASN A 285 25.760 48.849 6.133 1.00 12.14 N ANISOU 2255 N ASN A 285 1221 1858 1534 -226 145 267 N ATOM 2256 CA ASN A 285 26.852 49.137 7.055 1.00 12.34 C ANISOU 2256 CA ASN A 285 1416 1720 1552 -255 1 286 C ATOM 2257 C ASN A 285 26.846 50.548 7.635 1.00 13.16 C ANISOU 2257 C ASN A 285 1280 1837 1883 -191 91 106 C ATOM 2258 O ASN A 285 27.381 50.764 8.725 1.00 15.64 O ANISOU 2258 O ASN A 285 1851 2027 2065 -134 -213 -76 O ATOM 2259 CB ASN A 285 28.203 48.875 6.356 1.00 14.79 C ANISOU 2259 CB ASN A 285 1462 2084 2073 -264 143 114 C ATOM 2260 CG ASN A 285 28.406 47.431 5.935 1.00 16.86 C ANISOU 2260 CG ASN A 285 1703 2188 2514 142 -503 32 C ATOM 2261 OD1 ASN A 285 27.726 46.515 6.400 1.00 21.53 O ANISOU 2261 OD1 ASN A 285 2861 2131 3187 -164 -1040 654 O ATOM 2262 ND2 ASN A 285 29.356 47.185 5.039 1.00 23.68 N ANISOU 2262 ND2 ASN A 285 2346 3211 3439 566 -11 -668 N ATOM 2263 N ASP A 286 26.218 51.498 6.965 1.00 13.86 N ANISOU 2263 N ASP A 286 1302 1743 2222 -158 20 173 N ATOM 2264 CA ASP A 286 26.092 52.875 7.428 1.00 16.06 C ANISOU 2264 CA ASP A 286 1799 1749 2552 -130 -105 128 C ATOM 2265 C ASP A 286 24.829 53.100 8.251 1.00 15.36 C ANISOU 2265 C ASP A 286 1660 1549 2628 -341 -133 18 C ATOM 2266 O ASP A 286 24.510 54.236 8.616 1.00 19.76 O ANISOU 2266 O ASP A 286 2128 1755 3625 -213 51 -341 O ATOM 2267 CB ASP A 286 26.156 53.861 6.254 1.00 19.04 C ANISOU 2267 CB ASP A 286 2157 1973 3104 -557 298 509 C ATOM 2268 CG ASP A 286 25.034 53.750 5.250 1.00 19.09 C ANISOU 2268 CG ASP A 286 2670 1830 2753 -299 151 490 C ATOM 2269 OD1 ASP A 286 24.140 52.880 5.413 1.00 17.30 O ANISOU 2269 OD1 ASP A 286 1937 2161 2475 -157 88 350 O ATOM 2270 OD2 ASP A 286 25.016 54.532 4.265 1.00 25.59 O ANISOU 2270 OD2 ASP A 286 3352 2702 3670 -420 -337 1373 O ATOM 2271 N GLY A 287 24.040 52.064 8.542 1.00 13.50 N ANISOU 2271 N GLY A 287 1373 1635 2121 -225 23 0 N ATOM 2272 CA GLY A 287 22.820 52.188 9.308 1.00 13.85 C ANISOU 2272 CA GLY A 287 1574 1791 1897 -68 52 -204 C ATOM 2273 C GLY A 287 21.561 52.455 8.483 1.00 12.33 C ANISOU 2273 C GLY A 287 1524 1352 1809 -84 99 -208 C ATOM 2274 O GLY A 287 20.481 52.503 9.085 1.00 16.12 O ANISOU 2274 O GLY A 287 1575 2164 2385 98 299 -244 O ATOM 2275 N SER A 288 21.689 52.639 7.185 1.00 12.97 N ANISOU 2275 N SER A 288 1469 1589 1871 -168 -21 33 N ATOM 2276 CA SER A 288 20.515 52.879 6.341 1.00 13.04 C ANISOU 2276 CA SER A 288 1568 1327 2061 -131 -107 202 C ATOM 2277 C SER A 288 19.710 51.596 6.120 1.00 12.11 C ANISOU 2277 C SER A 288 1443 1274 1882 -75 58 230 C ATOM 2278 O SER A 288 20.236 50.483 6.187 1.00 13.30 O ANISOU 2278 O SER A 288 1670 1316 2067 21 -79 208 O ATOM 2279 CB SER A 288 20.929 53.521 5.012 1.00 15.84 C ANISOU 2279 CB SER A 288 1994 1787 2236 -30 -103 518 C ATOM 2280 OG SER A 288 21.770 52.708 4.218 1.00 16.89 O ANISOU 2280 OG SER A 288 2487 1773 2158 -179 300 591 O ATOM 2281 N LYS A 289 18.431 51.756 5.805 1.00 12.70 N ANISOU 2281 N LYS A 289 1538 1136 2149 -101 -181 316 N ATOM 2282 CA LYS A 289 17.517 50.644 5.576 1.00 11.90 C ANISOU 2282 CA LYS A 289 1544 1249 1727 -116 -173 200 C ATOM 2283 C LYS A 289 17.671 50.020 4.197 1.00 13.26 C ANISOU 2283 C LYS A 289 1998 1384 1658 119 89 341 C ATOM 2284 O LYS A 289 17.740 50.764 3.210 1.00 16.79 O ANISOU 2284 O LYS A 289 2967 1520 1894 -134 -36 555 O ATOM 2285 CB LYS A 289 16.070 51.133 5.773 1.00 12.23 C ANISOU 2285 CB LYS A 289 1539 1303 1805 -59 -253 152 C ATOM 2286 CG LYS A 289 15.746 51.528 7.214 1.00 12.99 C ANISOU 2286 CG LYS A 289 1872 1321 1743 3 -338 148 C ATOM 2287 CD LYS A 289 14.510 52.420 7.302 1.00 14.67 C ANISOU 2287 CD LYS A 289 2012 1471 2092 104 -154 167 C ATOM 2288 CE LYS A 289 14.186 52.738 8.758 1.00 14.93 C ANISOU 2288 CE LYS A 289 1901 1652 2120 34 73 318 C ATOM 2289 NZ LYS A 289 13.047 53.688 8.900 1.00 18.39 N ANISOU 2289 NZ LYS A 289 2453 1940 2595 435 338 348 N ATOM 2290 N LYS A 290 17.699 48.702 4.110 1.00 12.08 N ANISOU 2290 N LYS A 290 1775 1376 1440 82 155 199 N ATOM 2291 CA LYS A 290 17.747 47.974 2.850 1.00 12.19 C ANISOU 2291 CA LYS A 290 1877 1345 1410 -115 82 231 C ATOM 2292 C LYS A 290 16.336 47.743 2.321 1.00 12.35 C ANISOU 2292 C LYS A 290 1948 1397 1347 -39 -31 236 C ATOM 2293 O LYS A 290 15.313 47.879 3.044 1.00 12.99 O ANISOU 2293 O LYS A 290 1913 1565 1458 -54 -11 251 O ATOM 2294 CB LYS A 290 18.516 46.640 3.026 1.00 13.43 C ANISOU 2294 CB LYS A 290 2426 1324 1352 -1 209 158 C ATOM 2295 CG ALYS A 290 19.959 46.813 3.446 0.50 14.54 C ANISOU 2295 CG ALYS A 290 2301 1591 1633 109 274 431 C ATOM 2296 CD ALYS A 290 20.740 45.612 3.927 0.50 12.62 C ANISOU 2296 CD ALYS A 290 1718 1617 1460 -221 10 401 C ATOM 2297 CE ALYS A 290 21.092 44.638 2.832 0.50 12.44 C ANISOU 2297 CE ALYS A 290 1779 1102 1847 -78 11 445 C ATOM 2298 NZ ALYS A 290 21.730 43.403 3.381 0.50 8.18 N ANISOU 2298 NZ ALYS A 290 1129 1197 781 27 -23 17 N ATOM 2299 CG BLYS A 290 19.977 46.852 3.378 0.50 18.47 C ANISOU 2299 CG BLYS A 290 2426 2333 2261 23 55 219 C ATOM 2300 CD BLYS A 290 20.731 45.630 3.859 0.50 18.46 C ANISOU 2300 CD BLYS A 290 2657 2109 2249 -151 156 309 C ATOM 2301 CE BLYS A 290 20.656 44.482 2.880 0.50 16.93 C ANISOU 2301 CE BLYS A 290 2845 2130 1456 -294 83 623 C ATOM 2302 NZ BLYS A 290 21.546 43.356 3.289 0.50 15.19 N ANISOU 2302 NZ BLYS A 290 2165 2157 1448 -268 119 105 N ATOM 2303 N ALA A 291 16.222 47.288 1.067 1.00 14.00 N ANISOU 2303 N ALA A 291 2160 1825 1334 -280 139 172 N ATOM 2304 CA ALA A 291 14.920 46.951 0.487 1.00 14.82 C ANISOU 2304 CA ALA A 291 2327 2116 1187 -198 -141 399 C ATOM 2305 C ALA A 291 14.198 45.903 1.331 1.00 13.16 C ANISOU 2305 C ALA A 291 1778 1993 1230 -118 7 119 C ATOM 2306 O ALA A 291 12.964 45.958 1.476 1.00 14.78 O ANISOU 2306 O ALA A 291 1808 2409 1399 58 -148 132 O ATOM 2307 CB ALA A 291 15.067 46.472 -0.957 1.00 18.06 C ANISOU 2307 CB ALA A 291 2811 2802 1247 -430 -87 278 C ATOM 2308 N ALA A 292 14.924 44.933 1.895 1.00 12.53 N ANISOU 2308 N ALA A 292 1860 1687 1212 -208 116 124 N ATOM 2309 CA ALA A 292 14.302 43.902 2.721 1.00 12.21 C ANISOU 2309 CA ALA A 292 1656 1744 1237 -338 208 -11 C ATOM 2310 C ALA A 292 13.654 44.472 3.977 1.00 10.62 C ANISOU 2310 C ALA A 292 1291 1570 1172 -106 100 92 C ATOM 2311 O ALA A 292 12.649 43.911 4.445 1.00 12.32 O ANISOU 2311 O ALA A 292 1574 1616 1490 -275 367 35 O ATOM 2312 CB ALA A 292 15.317 42.811 3.051 1.00 15.09 C ANISOU 2312 CB ALA A 292 2264 1541 1928 -55 587 101 C ATOM 2313 N TYR A 293 14.186 45.563 4.553 1.00 10.75 N ANISOU 2313 N TYR A 293 1401 1429 1256 -108 186 121 N ATOM 2314 CA TYR A 293 13.545 46.192 5.724 1.00 10.31 C ANISOU 2314 CA TYR A 293 1318 1180 1419 -136 317 223 C ATOM 2315 C TYR A 293 12.115 46.592 5.375 1.00 10.38 C ANISOU 2315 C TYR A 293 1412 1314 1219 -303 -130 116 C ATOM 2316 O TYR A 293 11.171 46.319 6.134 1.00 11.52 O ANISOU 2316 O TYR A 293 1344 1516 1516 -75 30 147 O ATOM 2317 CB TYR A 293 14.363 47.418 6.190 1.00 10.36 C ANISOU 2317 CB TYR A 293 1371 1254 1310 -108 79 157 C ATOM 2318 CG TYR A 293 13.686 48.173 7.321 1.00 10.08 C ANISOU 2318 CG TYR A 293 1184 1452 1194 -9 112 297 C ATOM 2319 CD1 TYR A 293 12.683 49.102 7.085 1.00 11.06 C ANISOU 2319 CD1 TYR A 293 1604 1342 1257 134 -179 219 C ATOM 2320 CD2 TYR A 293 14.024 47.936 8.647 1.00 10.20 C ANISOU 2320 CD2 TYR A 293 1392 1306 1179 31 -18 167 C ATOM 2321 CE1 TYR A 293 12.010 49.749 8.092 1.00 11.71 C ANISOU 2321 CE1 TYR A 293 1487 1453 1510 230 -177 61 C ATOM 2322 CE2 TYR A 293 13.391 48.596 9.695 1.00 9.89 C ANISOU 2322 CE2 TYR A 293 1083 1315 1360 71 56 188 C ATOM 2323 CZ TYR A 293 12.378 49.501 9.413 1.00 10.43 C ANISOU 2323 CZ TYR A 293 1118 1411 1435 199 -26 22 C ATOM 2324 OH TYR A 293 11.710 50.142 10.441 1.00 13.00 O ANISOU 2324 OH TYR A 293 1368 1883 1689 439 54 -113 O ATOM 2325 N THR A 294 11.937 47.296 4.254 1.00 12.31 N ANISOU 2325 N THR A 294 1557 1637 1484 -147 -84 401 N ATOM 2326 CA THR A 294 10.624 47.770 3.810 1.00 13.20 C ANISOU 2326 CA THR A 294 1767 1568 1682 52 -148 344 C ATOM 2327 C THR A 294 9.644 46.628 3.556 1.00 12.91 C ANISOU 2327 C THR A 294 1661 1832 1412 10 -89 315 C ATOM 2328 O THR A 294 8.477 46.688 3.959 1.00 14.01 O ANISOU 2328 O THR A 294 1566 2105 1652 67 -97 357 O ATOM 2329 CB THR A 294 10.772 48.678 2.559 1.00 18.48 C ANISOU 2329 CB THR A 294 2948 1879 2194 -131 -496 821 C ATOM 2330 OG1 THR A 294 11.618 49.783 2.921 1.00 23.71 O ANISOU 2330 OG1 THR A 294 3459 1976 3572 -507 -486 952 O ATOM 2331 CG2 THR A 294 9.423 49.181 2.092 1.00 23.24 C ANISOU 2331 CG2 THR A 294 3160 2624 3047 246 -513 1158 C ATOM 2332 N ALA A 295 10.127 45.531 2.964 1.00 12.08 N ANISOU 2332 N ALA A 295 1626 1621 1342 -243 -167 247 N ATOM 2333 CA ALA A 295 9.284 44.362 2.728 1.00 12.67 C ANISOU 2333 CA ALA A 295 1670 1798 1348 -348 -173 190 C ATOM 2334 C ALA A 295 8.789 43.742 4.037 1.00 11.84 C ANISOU 2334 C ALA A 295 1628 1516 1355 -235 -109 77 C ATOM 2335 O ALA A 295 7.626 43.324 4.132 1.00 13.31 O ANISOU 2335 O ALA A 295 1710 1956 1392 -400 -147 227 O ATOM 2336 CB ALA A 295 10.015 43.329 1.880 1.00 16.21 C ANISOU 2336 CB ALA A 295 2410 2241 1509 -547 208 -243 C ATOM 2337 N VAL A 296 9.658 43.652 5.052 1.00 11.41 N ANISOU 2337 N VAL A 296 1509 1544 1280 -240 3 136 N ATOM 2338 CA VAL A 296 9.253 43.113 6.363 1.00 9.76 C ANISOU 2338 CA VAL A 296 1341 1127 1239 -174 -74 47 C ATOM 2339 C VAL A 296 8.254 44.039 7.055 1.00 10.18 C ANISOU 2339 C VAL A 296 1392 1281 1197 -16 50 217 C ATOM 2340 O VAL A 296 7.213 43.585 7.576 1.00 10.90 O ANISOU 2340 O VAL A 296 1370 1476 1296 -30 22 302 O ATOM 2341 CB VAL A 296 10.483 42.841 7.232 1.00 10.60 C ANISOU 2341 CB VAL A 296 1372 1303 1351 45 -87 35 C ATOM 2342 CG1 VAL A 296 10.081 42.443 8.656 1.00 11.17 C ANISOU 2342 CG1 VAL A 296 1539 1329 1377 -65 -134 99 C ATOM 2343 CG2 VAL A 296 11.351 41.729 6.645 1.00 11.93 C ANISOU 2343 CG2 VAL A 296 1621 1348 1565 11 157 19 C ATOM 2344 N LEU A 297 8.533 45.350 7.089 1.00 10.79 N ANISOU 2344 N LEU A 297 1309 1322 1468 2 -14 111 N ATOM 2345 CA LEU A 297 7.642 46.304 7.744 1.00 11.19 C ANISOU 2345 CA LEU A 297 1366 1180 1706 82 -167 176 C ATOM 2346 C LEU A 297 6.263 46.290 7.100 1.00 11.60 C ANISOU 2346 C LEU A 297 1424 1451 1534 68 -165 265 C ATOM 2347 O LEU A 297 5.246 46.269 7.813 1.00 13.04 O ANISOU 2347 O LEU A 297 1373 1693 1889 67 -63 115 O ATOM 2348 CB LEU A 297 8.216 47.720 7.721 1.00 11.99 C ANISOU 2348 CB LEU A 297 1425 1241 1891 35 -34 176 C ATOM 2349 CG LEU A 297 7.462 48.784 8.531 1.00 12.93 C ANISOU 2349 CG LEU A 297 1370 1615 1927 211 -11 108 C ATOM 2350 CD1 LEU A 297 7.491 48.471 10.024 1.00 17.92 C ANISOU 2350 CD1 LEU A 297 2602 2313 1896 339 246 90 C ATOM 2351 CD2 LEU A 297 8.008 50.186 8.283 1.00 18.14 C ANISOU 2351 CD2 LEU A 297 2469 1651 2773 -7 255 95 C ATOM 2352 N ASP A 298 6.204 46.270 5.770 1.00 12.82 N ANISOU 2352 N ASP A 298 1493 1837 1539 97 -354 398 N ATOM 2353 CA ASP A 298 4.939 46.220 5.046 1.00 14.25 C ANISOU 2353 CA ASP A 298 1624 2024 1765 27 -499 316 C ATOM 2354 C ASP A 298 4.147 44.954 5.361 1.00 14.93 C ANISOU 2354 C ASP A 298 1642 2139 1891 -3 -165 262 C ATOM 2355 O ASP A 298 2.925 45.009 5.568 1.00 16.83 O ANISOU 2355 O ASP A 298 1601 2368 2424 -7 -258 451 O ATOM 2356 CB ASP A 298 5.147 46.342 3.538 1.00 16.89 C ANISOU 2356 CB ASP A 298 2138 2447 1834 -117 -490 649 C ATOM 2357 CG ASP A 298 5.492 47.733 3.043 1.00 20.51 C ANISOU 2357 CG ASP A 298 2644 2314 2833 79 -77 656 C ATOM 2358 OD1 ASP A 298 5.404 48.717 3.808 1.00 23.93 O ANISOU 2358 OD1 ASP A 298 3505 2224 3362 563 48 605 O ATOM 2359 OD2 ASP A 298 5.849 47.835 1.840 1.00 26.36 O ANISOU 2359 OD2 ASP A 298 3507 3621 2888 69 24 987 O ATOM 2360 N ALA A 299 4.819 43.803 5.478 1.00 13.15 N ANISOU 2360 N ALA A 299 1498 1961 1536 -182 -346 211 N ATOM 2361 CA ALA A 299 4.155 42.550 5.825 1.00 13.52 C ANISOU 2361 CA ALA A 299 1555 1873 1710 -155 -291 97 C ATOM 2362 C ALA A 299 3.585 42.619 7.243 1.00 12.97 C ANISOU 2362 C ALA A 299 1379 1794 1755 -225 -285 54 C ATOM 2363 O ALA A 299 2.445 42.213 7.488 1.00 15.25 O ANISOU 2363 O ALA A 299 1523 2255 2015 -373 -197 60 O ATOM 2364 CB ALA A 299 5.114 41.380 5.665 1.00 13.75 C ANISOU 2364 CB ALA A 299 1799 1712 1713 -197 -97 137 C ATOM 2365 N LEU A 300 4.382 43.143 8.194 1.00 12.06 N ANISOU 2365 N LEU A 300 1251 1684 1648 -74 -278 67 N ATOM 2366 CA LEU A 300 3.885 43.290 9.564 1.00 12.61 C ANISOU 2366 CA LEU A 300 1242 1687 1862 -88 -67 -21 C ATOM 2367 C LEU A 300 2.678 44.222 9.666 1.00 13.55 C ANISOU 2367 C LEU A 300 1281 1976 1893 57 69 53 C ATOM 2368 O LEU A 300 1.774 43.983 10.483 1.00 17.43 O ANISOU 2368 O LEU A 300 1471 2872 2280 46 280 234 O ATOM 2369 CB LEU A 300 5.007 43.799 10.480 1.00 11.80 C ANISOU 2369 CB LEU A 300 1257 1616 1610 -75 -18 44 C ATOM 2370 CG LEU A 300 6.176 42.833 10.727 1.00 11.00 C ANISOU 2370 CG LEU A 300 1582 1388 1209 58 84 -54 C ATOM 2371 CD1 LEU A 300 7.311 43.583 11.409 1.00 12.11 C ANISOU 2371 CD1 LEU A 300 1410 1533 1658 185 -79 -77 C ATOM 2372 CD2 LEU A 300 5.757 41.605 11.531 1.00 13.02 C ANISOU 2372 CD2 LEU A 300 1835 1538 1575 -44 224 68 C ATOM 2373 N ASN A 301 2.635 45.285 8.859 1.00 14.90 N ANISOU 2373 N ASN A 301 1529 1973 2160 151 73 145 N ATOM 2374 CA ASN A 301 1.535 46.232 8.836 1.00 16.00 C ANISOU 2374 CA ASN A 301 1431 2127 2520 164 -68 -55 C ATOM 2375 C ASN A 301 0.331 45.772 8.024 1.00 20.49 C ANISOU 2375 C ASN A 301 1607 2822 3358 0 -417 -54 C ATOM 2376 O ASN A 301 -0.723 46.424 8.082 1.00 26.76 O ANISOU 2376 O ASN A 301 1676 3481 5012 247 -556 -168 O ATOM 2377 CB ASN A 301 2.017 47.602 8.328 1.00 15.91 C ANISOU 2377 CB ASN A 301 1441 2036 2568 298 -230 12 C ATOM 2378 CG ASN A 301 2.747 48.422 9.371 1.00 15.55 C ANISOU 2378 CG ASN A 301 1508 1959 2441 217 -193 149 C ATOM 2379 OD1 ASN A 301 2.448 48.402 10.567 1.00 17.47 O ANISOU 2379 OD1 ASN A 301 1906 2232 2498 11 -161 15 O ATOM 2380 ND2 ASN A 301 3.730 49.202 8.930 1.00 17.37 N ANISOU 2380 ND2 ASN A 301 1690 1999 2910 145 167 -97 N ATOM 2381 N GLY A 302 0.407 44.678 7.292 1.00 21.88 N ANISOU 2381 N GLY A 302 1556 2981 3776 -56 -272 -305 N ATOM 2382 CA GLY A 302 -0.680 44.152 6.488 1.00 29.07 C ANISOU 2382 CA GLY A 302 2366 4347 4331 -568 -847 -291 C ATOM 2383 C GLY A 302 -0.708 44.746 5.087 1.00 40.73 C ANISOU 2383 C GLY A 302 5262 5633 4579 -238 -176 249 C ATOM 2384 O GLY A 302 0.331 45.216 4.579 1.00 44.09 O ANISOU 2384 O GLY A 302 4814 6522 5415 -177 -148 123 O ATOM 2385 OXT GLY A 302 -1.806 44.735 4.479 1.00 48.56 O ANISOU 2385 OXT GLY A 302 5229 6887 6336 -159 -599 9 O TER 2386 GLY A 302 HETATM 2387 O HOH A2001 5.042 52.924 8.006 1.00 56.81 O ANISOU 2387 O HOH A2001 7337 7125 7124 73 -60 406 O HETATM 2388 O HOH A2002 4.994 53.914 14.765 1.00 41.55 O ANISOU 2388 O HOH A2002 5613 5932 4244 186 329 -1354 O HETATM 2389 O HOH A2003 10.211 56.432 9.851 1.00 40.35 O ANISOU 2389 O HOH A2003 5483 4284 5565 -346 -136 -60 O HETATM 2390 O HOH A2004 9.382 48.620 20.509 1.00 37.53 O ANISOU 2390 O HOH A2004 5021 4463 4777 147 -187 971 O HETATM 2391 O HOH A2005 9.622 53.724 8.981 1.00 32.75 O ANISOU 2391 O HOH A2005 4805 4213 3426 -916 316 928 O HETATM 2392 O HOH A2006 4.488 49.068 20.721 1.00 40.82 O ANISOU 2392 O HOH A2006 4920 5785 4803 159 -101 467 O HETATM 2393 O HOH A2007 10.098 49.226 17.890 1.00 23.56 O ANISOU 2393 O HOH A2007 2569 2758 3624 -788 361 -451 O HETATM 2394 O HOH A2008 7.253 53.095 16.393 1.00 29.47 O ANISOU 2394 O HOH A2008 3640 3156 4399 481 836 -246 O HETATM 2395 O HOH A2009 -0.156 37.051 25.805 1.00 59.70 O ANISOU 2395 O HOH A2009 7772 7313 7600 -40 -182 34 O HETATM 2396 O HOH A2010 2.397 48.737 18.590 1.00 26.10 O ANISOU 2396 O HOH A2010 3849 2960 3106 910 1578 -249 O HETATM 2397 O HOH A2011 1.962 42.998 21.923 1.00 24.92 O ANISOU 2397 O HOH A2011 2344 4337 2789 -328 197 -436 O HETATM 2398 O HOH A2012 -2.840 46.865 12.667 1.00 50.40 O ANISOU 2398 O HOH A2012 5776 7024 6349 6 -39 128 O HETATM 2399 O HOH A2013 30.170 52.823 11.927 1.00 58.17 O ANISOU 2399 O HOH A2013 6575 7613 7913 -34 -132 -143 O HETATM 2400 O HOH A2014 31.822 53.879 16.502 1.00 56.64 O ANISOU 2400 O HOH A2014 7232 7004 7285 -174 254 218 O HETATM 2401 O HOH A2015 -2.352 42.952 13.035 1.00 49.87 O ANISOU 2401 O HOH A2015 6568 6485 5897 348 39 49 O HETATM 2402 O HOH A2016 2.109 42.575 13.008 1.00 19.73 O ANISOU 2402 O HOH A2016 2154 2705 2639 -342 267 -393 O HETATM 2403 O HOH A2017 -0.458 36.808 19.057 1.00 20.08 O ANISOU 2403 O HOH A2017 2183 2220 3226 -182 228 45 O HETATM 2404 O HOH A2018 -2.015 39.919 12.203 1.00 38.15 O ANISOU 2404 O HOH A2018 4689 5382 4425 -426 -43 -342 O HETATM 2405 O HOH A2019 15.764 54.704 21.847 1.00 37.61 O ANISOU 2405 O HOH A2019 4848 4692 4751 251 538 802 O HETATM 2406 O HOH A2020 1.870 35.784 20.796 1.00 49.25 O ANISOU 2406 O HOH A2020 6366 5657 6689 369 -30 49 O HETATM 2407 O HOH A2021 0.781 38.782 23.203 1.00 47.65 O ANISOU 2407 O HOH A2021 6152 6094 5861 137 100 -71 O HETATM 2408 O HOH A2022 4.603 42.135 21.737 1.00 30.97 O ANISOU 2408 O HOH A2022 4378 4252 3136 680 -8 -597 O HETATM 2409 O HOH A2023 13.548 54.951 20.252 1.00 51.30 O ANISOU 2409 O HOH A2023 6924 6015 6552 64 -311 -361 O HETATM 2410 O HOH A2024 12.861 34.566 18.515 1.00 9.27 O ANISOU 2410 O HOH A2024 1242 1164 1116 -10 288 -91 O HETATM 2411 O HOH A2025 31.969 37.658 23.958 1.00 46.49 O ANISOU 2411 O HOH A2025 5547 6131 5988 -246 -407 166 O HETATM 2412 O HOH A2026 28.209 28.068 16.274 1.00 50.92 O ANISOU 2412 O HOH A2026 6197 6765 6384 20 274 266 O HETATM 2413 O HOH A2027 32.437 35.127 25.434 1.00 46.96 O ANISOU 2413 O HOH A2027 5590 6025 6226 -362 -81 89 O HETATM 2414 O HOH A2028 38.333 21.204 36.714 1.00 28.02 O ANISOU 2414 O HOH A2028 3999 3160 3487 -348 -778 532 O HETATM 2415 O HOH A2029 38.144 32.960 35.075 1.00 57.44 O ANISOU 2415 O HOH A2029 6656 7402 7768 -228 -209 -118 O HETATM 2416 O HOH A2030 31.330 47.926 24.525 1.00 35.77 O ANISOU 2416 O HOH A2030 4006 3947 5637 -749 -285 -720 O HETATM 2417 O HOH A2031 30.631 46.424 27.039 1.00 47.57 O ANISOU 2417 O HOH A2031 6364 5991 5720 -767 -249 -345 O HETATM 2418 O HOH A2032 31.255 41.267 21.948 1.00 18.54 O ANISOU 2418 O HOH A2032 2466 1694 2886 199 220 172 O HETATM 2419 O HOH A2033 34.940 45.784 21.668 1.00 33.43 O ANISOU 2419 O HOH A2033 2624 6422 3655 -430 20 463 O HETATM 2420 O HOH A2034 27.170 31.889 42.206 1.00 57.31 O ANISOU 2420 O HOH A2034 7884 7022 6868 -178 643 -246 O HETATM 2421 O HOH A2035 26.920 54.007 22.408 1.00 23.42 O ANISOU 2421 O HOH A2035 3672 2622 2605 121 401 -450 O HETATM 2422 O HOH A2036 27.895 52.830 25.444 1.00 44.67 O ANISOU 2422 O HOH A2036 6962 4967 5045 356 375 -1181 O HETATM 2423 O HOH A2037 25.668 51.231 26.177 1.00 50.17 O ANISOU 2423 O HOH A2037 6171 6295 6598 153 -125 -250 O HETATM 2424 O HOH A2038 25.151 47.658 32.940 1.00 36.86 O ANISOU 2424 O HOH A2038 4915 4616 4474 -160 -127 -524 O HETATM 2425 O HOH A2039 31.818 49.112 20.460 1.00 35.15 O ANISOU 2425 O HOH A2039 3583 4065 5709 117 -117 37 O HETATM 2426 O HOH A2040 35.101 51.904 21.535 1.00 58.82 O ANISOU 2426 O HOH A2040 6385 8134 7832 301 364 73 O HETATM 2427 O HOH A2041 30.216 48.050 16.597 1.00 26.65 O ANISOU 2427 O HOH A2041 3978 2809 3338 528 258 -489 O HETATM 2428 O HOH A2042 31.868 50.394 14.562 1.00 25.18 O ANISOU 2428 O HOH A2042 2397 1929 5240 458 608 -581 O HETATM 2429 O HOH A2043 29.191 54.091 14.080 1.00 40.06 O ANISOU 2429 O HOH A2043 5024 4845 5350 -1118 746 1071 O HETATM 2430 O HOH A2044 15.551 55.632 26.342 1.00 37.72 O ANISOU 2430 O HOH A2044 4793 5191 4346 -800 241 -262 O HETATM 2431 O HOH A2045 13.433 53.231 25.923 1.00 55.86 O ANISOU 2431 O HOH A2045 6928 6777 7519 -78 -164 -81 O HETATM 2432 O HOH A2046 4.688 16.371 2.566 1.00 59.76 O ANISOU 2432 O HOH A2046 7701 7851 7153 -98 -219 -121 O HETATM 2433 O HOH A2047 30.051 55.425 17.933 1.00 33.17 O ANISOU 2433 O HOH A2047 3028 2656 6917 -743 1422 -307 O HETATM 2434 O HOH A2048 28.108 54.863 11.484 1.00 47.28 O ANISOU 2434 O HOH A2048 5883 5727 6355 -210 335 236 O HETATM 2435 O HOH A2049 28.672 56.176 15.815 1.00 43.97 O ANISOU 2435 O HOH A2049 4519 6356 5832 -97 195 -179 O HETATM 2436 O HOH A2050 24.287 42.505 16.624 1.00 10.60 O ANISOU 2436 O HOH A2050 1546 1010 1472 -244 186 -64 O HETATM 2437 O HOH A2051 26.165 21.312 28.638 1.00 39.69 O ANISOU 2437 O HOH A2051 4800 4894 5389 146 -414 -443 O HETATM 2438 O HOH A2052 17.145 55.397 19.596 1.00 28.37 O ANISOU 2438 O HOH A2052 3290 3321 4167 543 506 -1291 O HETATM 2439 O HOH A2053 11.746 50.276 20.929 1.00 55.10 O ANISOU 2439 O HOH A2053 6108 7651 7177 22 142 136 O HETATM 2440 O HOH A2054 10.872 53.106 18.800 1.00 33.22 O ANISOU 2440 O HOH A2054 3408 4560 4652 666 862 -898 O HETATM 2441 O HOH A2055 12.052 53.180 11.479 1.00 17.84 O ANISOU 2441 O HOH A2055 1833 2492 2452 25 218 479 O HETATM 2442 O HOH A2056 17.872 12.393 36.446 1.00 56.48 O ANISOU 2442 O HOH A2056 7423 7389 6646 160 -238 514 O HETATM 2443 O HOH A2057 6.920 47.426 20.978 1.00 34.55 O ANISOU 2443 O HOH A2057 4189 4143 4796 394 39 -729 O HETATM 2444 O HOH A2058 6.612 45.748 23.092 1.00 44.27 O ANISOU 2444 O HOH A2058 4968 5696 6157 804 953 -612 O HETATM 2445 O HOH A2059 25.552 28.066 42.033 1.00 36.78 O ANISOU 2445 O HOH A2059 5489 4688 3797 -172 301 -73 O HETATM 2446 O HOH A2060 19.093 24.967 42.992 1.00 28.34 O ANISOU 2446 O HOH A2060 3984 3770 3014 431 381 -374 O HETATM 2447 O HOH A2061 18.614 16.770 40.155 1.00 34.55 O ANISOU 2447 O HOH A2061 4231 5153 3742 -308 -65 89 O HETATM 2448 O HOH A2062 16.325 30.033 43.129 1.00 48.24 O ANISOU 2448 O HOH A2062 5638 6606 6086 -125 -261 3 O HETATM 2449 O HOH A2063 10.238 34.575 40.346 1.00 52.62 O ANISOU 2449 O HOH A2063 6453 6960 6580 199 565 -64 O HETATM 2450 O HOH A2064 10.224 40.116 31.028 1.00 51.17 O ANISOU 2450 O HOH A2064 5756 6805 6882 329 418 -175 O HETATM 2451 O HOH A2065 25.674 37.582 13.930 1.00 14.58 O ANISOU 2451 O HOH A2065 1593 2048 1897 -241 48 157 O HETATM 2452 O HOH A2066 26.600 34.412 16.345 1.00 29.92 O ANISOU 2452 O HOH A2066 5247 3225 2898 504 82 -400 O HETATM 2453 O HOH A2067 26.441 40.860 16.175 1.00 19.13 O ANISOU 2453 O HOH A2067 3158 1884 2227 707 1165 347 O HETATM 2454 O HOH A2068 29.775 39.928 17.783 1.00 22.81 O ANISOU 2454 O HOH A2068 3712 2272 2681 -209 596 400 O HETATM 2455 O HOH A2069 29.376 35.122 17.216 1.00 50.02 O ANISOU 2455 O HOH A2069 6048 6879 6078 407 223 361 O HETATM 2456 O HOH A2070 29.753 38.903 22.226 1.00 28.86 O ANISOU 2456 O HOH A2070 4919 2156 3892 -89 1514 595 O HETATM 2457 O HOH A2071 27.146 12.472 12.132 1.00 51.22 O ANISOU 2457 O HOH A2071 6120 6247 7096 406 191 -196 O HETATM 2458 O HOH A2072 22.568 19.305 5.387 1.00 48.48 O ANISOU 2458 O HOH A2072 6273 6441 5706 289 389 274 O HETATM 2459 O HOH A2073 28.322 30.695 17.713 1.00 51.18 O ANISOU 2459 O HOH A2073 6607 6313 6525 74 224 -134 O HETATM 2460 O HOH A2074 26.341 33.017 18.754 1.00 25.58 O ANISOU 2460 O HOH A2074 3744 3111 2864 841 -287 -123 O HETATM 2461 O HOH A2075 23.979 10.954 1.609 1.00 54.66 O ANISOU 2461 O HOH A2075 7347 6445 6977 78 78 -395 O HETATM 2462 O HOH A2076 35.099 28.268 24.404 1.00 39.45 O ANISOU 2462 O HOH A2076 3682 5449 5859 604 346 -320 O HETATM 2463 O HOH A2077 33.960 31.119 22.877 1.00 47.31 O ANISOU 2463 O HOH A2077 6012 6607 5359 -32 257 435 O HETATM 2464 O HOH A2078 30.929 32.822 24.782 1.00 17.75 O ANISOU 2464 O HOH A2078 2190 2080 2475 325 294 447 O HETATM 2465 O HOH A2079 34.949 32.783 29.547 1.00 50.96 O ANISOU 2465 O HOH A2079 6142 6538 6682 -224 -144 94 O HETATM 2466 O HOH A2080 35.790 30.196 29.590 1.00 37.44 O ANISOU 2466 O HOH A2080 3635 6231 4360 15 -236 163 O HETATM 2467 O HOH A2081 30.250 11.477 14.400 1.00 52.23 O ANISOU 2467 O HOH A2081 6720 6840 6287 247 222 -51 O HETATM 2468 O HOH A2082 33.388 35.244 31.351 1.00 41.50 O ANISOU 2468 O HOH A2082 4902 4962 5904 -1427 -42 -586 O HETATM 2469 O HOH A2083 27.825 7.019 30.697 1.00 53.85 O ANISOU 2469 O HOH A2083 7203 6237 7020 -180 -152 -283 O HETATM 2470 O HOH A2084 30.537 6.262 26.117 1.00 51.21 O ANISOU 2470 O HOH A2084 7114 6180 6163 397 -155 -112 O HETATM 2471 O HOH A2085 24.666 4.993 32.718 1.00 56.95 O ANISOU 2471 O HOH A2085 7491 6894 7252 -218 30 41 O HETATM 2472 O HOH A2086 28.293 24.890 39.502 1.00 27.55 O ANISOU 2472 O HOH A2086 3736 4267 2463 -248 294 476 O HETATM 2473 O HOH A2087 28.876 22.731 37.002 1.00 13.40 O ANISOU 2473 O HOH A2087 1758 1483 1851 -393 -222 482 O HETATM 2474 O HOH A2088 37.578 28.455 30.910 1.00 28.21 O ANISOU 2474 O HOH A2088 3263 4359 3096 -276 572 227 O HETATM 2475 O HOH A2089 15.489 14.069 35.732 1.00 50.24 O ANISOU 2475 O HOH A2089 6299 6687 6103 -109 42 237 O HETATM 2476 O HOH A2090 37.530 24.078 36.806 1.00 19.77 O ANISOU 2476 O HOH A2090 2090 2797 2623 286 -739 -342 O HETATM 2477 O HOH A2091 40.062 25.464 33.820 1.00 39.07 O ANISOU 2477 O HOH A2091 5993 3062 5790 -1400 -1097 680 O HETATM 2478 O HOH A2092 39.470 30.911 33.580 1.00 51.71 O ANISOU 2478 O HOH A2092 6337 6532 6778 -525 21 244 O HETATM 2479 O HOH A2093 8.985 20.658 38.416 1.00 33.23 O ANISOU 2479 O HOH A2093 3295 5342 3991 -600 484 216 O HETATM 2480 O HOH A2094 7.031 18.654 34.814 1.00 57.41 O ANISOU 2480 O HOH A2094 7371 7356 7088 0 285 258 O HETATM 2481 O HOH A2095 36.913 24.882 39.864 1.00 32.51 O ANISOU 2481 O HOH A2095 3113 4903 4337 -74 -679 449 O HETATM 2482 O HOH A2096 32.894 15.119 39.532 1.00 53.40 O ANISOU 2482 O HOH A2096 6920 6730 6638 123 -562 132 O HETATM 2483 O HOH A2097 35.587 18.832 37.548 1.00 36.11 O ANISOU 2483 O HOH A2097 3787 5226 4706 708 42 -528 O HETATM 2484 O HOH A2098 36.841 31.949 37.375 1.00 57.18 O ANISOU 2484 O HOH A2098 6850 7118 7756 6 -116 -252 O HETATM 2485 O HOH A2099 34.314 33.025 37.623 1.00 50.64 O ANISOU 2485 O HOH A2099 6267 6522 6450 22 -310 153 O HETATM 2486 O HOH A2100 30.300 31.592 41.661 1.00 33.17 O ANISOU 2486 O HOH A2100 4922 5468 2213 452 -204 -676 O HETATM 2487 O HOH A2101 35.926 34.767 35.680 1.00 52.60 O ANISOU 2487 O HOH A2101 6552 6283 7149 -145 -432 -183 O HETATM 2488 O HOH A2102 28.759 36.438 31.468 1.00 16.94 O ANISOU 2488 O HOH A2102 2144 1852 2442 260 -315 -53 O HETATM 2489 O HOH A2103 29.333 37.678 38.319 1.00 29.02 O ANISOU 2489 O HOH A2103 4061 3981 2985 -21 -757 -1441 O HETATM 2490 O HOH A2104 31.490 37.877 31.994 1.00 33.26 O ANISOU 2490 O HOH A2104 3785 4213 4638 722 -573 462 O HETATM 2491 O HOH A2105 27.820 43.838 34.451 1.00 29.81 O ANISOU 2491 O HOH A2105 4066 3072 4190 23 -482 -906 O HETATM 2492 O HOH A2106 9.496 12.568 5.387 1.00 59.83 O ANISOU 2492 O HOH A2106 7762 7602 7369 210 -81 -374 O HETATM 2493 O HOH A2107 12.410 10.923 8.071 1.00 44.25 O ANISOU 2493 O HOH A2107 5368 5195 6249 -11 170 -798 O HETATM 2494 O HOH A2108 15.382 15.430 1.345 1.00 49.45 O ANISOU 2494 O HOH A2108 7034 6384 5370 300 -10 -206 O HETATM 2495 O HOH A2109 31.816 37.236 27.660 1.00 38.77 O ANISOU 2495 O HOH A2109 5285 4233 5215 240 767 50 O HETATM 2496 O HOH A2110 15.989 11.509 3.768 1.00 51.80 O ANISOU 2496 O HOH A2110 7148 6597 5936 26 -328 -266 O HETATM 2497 O HOH A2111 11.941 9.931 17.948 1.00 34.46 O ANISOU 2497 O HOH A2111 4972 2606 5516 -369 1105 373 O HETATM 2498 O HOH A2112 26.914 40.905 37.536 1.00 40.86 O ANISOU 2498 O HOH A2112 5267 6211 4045 -509 -568 -465 O HETATM 2499 O HOH A2113 20.939 40.432 36.403 1.00 31.74 O ANISOU 2499 O HOH A2113 3898 4085 4075 738 168 24 O HETATM 2500 O HOH A2114 -0.806 16.452 15.926 1.00 41.42 O ANISOU 2500 O HOH A2114 4467 5211 6058 -330 148 287 O HETATM 2501 O HOH A2115 24.564 47.733 30.225 1.00 26.62 O ANISOU 2501 O HOH A2115 3965 2097 4054 -448 -918 -366 O HETATM 2502 O HOH A2116 13.222 41.215 32.900 1.00 27.92 O ANISOU 2502 O HOH A2116 3507 2681 4421 -80 -272 -72 O HETATM 2503 O HOH A2117 15.457 43.683 36.159 1.00 38.55 O ANISOU 2503 O HOH A2117 5266 5168 4211 125 717 -350 O HETATM 2504 O HOH A2118 23.749 44.121 37.553 1.00 55.06 O ANISOU 2504 O HOH A2118 7380 7036 6506 132 -349 104 O HETATM 2505 O HOH A2119 20.460 43.220 36.757 1.00 41.96 O ANISOU 2505 O HOH A2119 6505 5609 3830 39 -229 -18 O HETATM 2506 O HOH A2120 25.726 45.483 34.393 1.00 44.66 O ANISOU 2506 O HOH A2120 5829 5548 5593 117 -262 -911 O HETATM 2507 O HOH A2121 3.954 27.788 28.202 1.00 46.45 O ANISOU 2507 O HOH A2121 5482 6353 5816 161 100 20 O HETATM 2508 O HOH A2122 23.437 52.365 25.073 1.00 19.51 O ANISOU 2508 O HOH A2122 2706 1669 3040 -507 576 -241 O HETATM 2509 O HOH A2123 24.769 26.466 11.463 1.00 38.22 O ANISOU 2509 O HOH A2123 5071 3840 5610 -1183 106 36 O HETATM 2510 O HOH A2124 11.889 47.377 30.830 1.00 39.82 O ANISOU 2510 O HOH A2124 4834 5006 5291 46 672 441 O HETATM 2511 O HOH A2125 23.034 49.906 29.972 1.00 43.73 O ANISOU 2511 O HOH A2125 5858 4765 5993 -41 -574 -140 O HETATM 2512 O HOH A2126 16.345 53.742 30.838 1.00 42.76 O ANISOU 2512 O HOH A2126 6223 4509 5516 21 111 -78 O HETATM 2513 O HOH A2127 20.550 53.073 29.491 1.00 49.46 O ANISOU 2513 O HOH A2127 6407 6021 6363 -655 -102 425 O HETATM 2514 O HOH A2128 17.486 53.856 27.661 1.00 37.14 O ANISOU 2514 O HOH A2128 6774 2477 4861 -561 1078 -492 O HETATM 2515 O HOH A2129 23.065 52.186 28.586 1.00 63.06 O ANISOU 2515 O HOH A2129 8640 7376 7943 15 -96 71 O HETATM 2516 O HOH A2130 15.620 52.555 23.407 1.00 28.97 O ANISOU 2516 O HOH A2130 3400 3990 3616 328 -555 425 O HETATM 2517 O HOH A2131 12.489 51.610 23.299 1.00 53.39 O ANISOU 2517 O HOH A2131 6896 6736 6652 334 -80 168 O HETATM 2518 O HOH A2132 5.416 19.479 2.363 1.00 46.19 O ANISOU 2518 O HOH A2132 6292 6040 5216 -226 -430 223 O HETATM 2519 O HOH A2133 9.185 45.148 28.276 1.00 52.65 O ANISOU 2519 O HOH A2133 6424 6272 7311 201 74 259 O HETATM 2520 O HOH A2134 8.846 44.948 25.491 1.00 49.12 O ANISOU 2520 O HOH A2134 6408 5676 6581 -117 210 21 O HETATM 2521 O HOH A2135 8.771 47.404 23.983 1.00 49.05 O ANISOU 2521 O HOH A2135 6525 5911 6202 351 -181 -363 O HETATM 2522 O HOH A2136 -3.569 32.481 6.581 1.00 48.41 O ANISOU 2522 O HOH A2136 4856 6791 6746 -30 -290 -349 O HETATM 2523 O HOH A2137 11.597 44.696 29.823 1.00 39.80 O ANISOU 2523 O HOH A2137 4759 6585 3779 -207 693 -381 O HETATM 2524 O HOH A2138 11.277 48.147 22.867 1.00 26.13 O ANISOU 2524 O HOH A2138 2512 3862 3555 -205 419 -1118 O HETATM 2525 O HOH A2139 6.989 37.957 24.851 1.00 44.39 O ANISOU 2525 O HOH A2139 5328 5170 6370 375 330 -402 O HETATM 2526 O HOH A2140 8.688 42.468 24.088 1.00 34.76 O ANISOU 2526 O HOH A2140 3053 5847 4305 -392 496 1149 O HETATM 2527 O HOH A2141 -3.318 22.136 12.378 1.00 54.42 O ANISOU 2527 O HOH A2141 6332 7137 7208 -100 234 11 O HETATM 2528 O HOH A2142 -1.139 26.381 12.364 1.00 38.44 O ANISOU 2528 O HOH A2142 2930 5277 6399 -172 -224 -92 O HETATM 2529 O HOH A2143 -2.197 25.215 17.231 1.00 39.11 O ANISOU 2529 O HOH A2143 3988 5461 5410 -390 204 666 O HETATM 2530 O BHOH A2144 20.671 35.426 25.729 0.50 6.19 O ANISOU 2530 O BHOH A2144 785 807 758 -216 -62 210 O HETATM 2531 O HOH A2145 24.822 33.981 24.606 1.00 9.98 O ANISOU 2531 O HOH A2145 1237 1110 1445 -227 -180 256 O HETATM 2532 O HOH A2146 24.873 30.645 19.097 1.00 19.31 O ANISOU 2532 O HOH A2146 2033 3177 2128 185 134 -354 O HETATM 2533 O HOH A2147 18.084 34.687 -3.539 1.00 55.77 O ANISOU 2533 O HOH A2147 7337 7351 6502 175 0 456 O HETATM 2534 O HOH A2148 24.949 22.537 31.023 1.00 21.85 O ANISOU 2534 O HOH A2148 3321 2279 2704 167 -1091 439 O HETATM 2535 O HOH A2149 14.067 44.008 -4.084 1.00 45.76 O ANISOU 2535 O HOH A2149 6383 6386 4619 -11 30 424 O HETATM 2536 O HOH A2150 6.475 41.522 -0.549 1.00 54.62 O ANISOU 2536 O HOH A2150 7198 7061 6497 332 -204 202 O HETATM 2537 O HOH A2151 8.787 44.782 -1.338 1.00 59.23 O ANISOU 2537 O HOH A2151 7088 7712 7705 -81 -191 127 O HETATM 2538 O HOH A2152 32.977 22.384 23.243 1.00 22.56 O ANISOU 2538 O HOH A2152 1939 3988 2644 224 -136 -611 O HETATM 2539 O HOH A2153 24.511 19.931 21.204 1.00 10.22 O ANISOU 2539 O HOH A2153 1212 1092 1578 251 -240 -23 O HETATM 2540 O HOH A2154 31.855 18.892 20.939 1.00 47.88 O ANISOU 2540 O HOH A2154 5410 6098 6684 779 -92 -159 O HETATM 2541 O HOH A2155 29.234 22.382 15.509 1.00 37.71 O ANISOU 2541 O HOH A2155 5792 5120 3418 -591 511 734 O HETATM 2542 O HOH A2156 1.721 29.095 1.939 1.00 42.37 O ANISOU 2542 O HOH A2156 5038 6091 4971 134 -354 -528 O HETATM 2543 O HOH A2157 -2.388 35.244 7.717 1.00 50.12 O ANISOU 2543 O HOH A2157 5364 7045 6637 612 38 314 O HETATM 2544 O HOH A2158 3.162 43.924 1.909 1.00 56.36 O ANISOU 2544 O HOH A2158 6565 7547 7303 27 -122 -287 O HETATM 2545 O HOH A2159 32.226 22.739 18.437 1.00 51.97 O ANISOU 2545 O HOH A2159 5663 7340 6741 25 672 -83 O HETATM 2546 O HOH A2160 30.024 28.088 18.451 1.00 37.57 O ANISOU 2546 O HOH A2160 4658 4735 4884 -181 253 -106 O HETATM 2547 O HOH A2161 33.611 24.970 20.375 1.00 34.15 O ANISOU 2547 O HOH A2161 3471 5195 4309 252 1135 354 O HETATM 2548 O HOH A2162 28.468 27.128 25.276 1.00 16.72 O ANISOU 2548 O HOH A2162 3048 1631 1673 301 -185 -257 O HETATM 2549 O HOH A2163 35.365 25.729 23.625 1.00 33.96 O ANISOU 2549 O HOH A2163 3826 4938 4141 119 160 790 O HETATM 2550 O HOH A2164 33.059 18.700 24.510 1.00 27.97 O ANISOU 2550 O HOH A2164 3049 3847 3730 -833 -4 -600 O HETATM 2551 O HOH A2165 5.477 36.041 23.549 1.00 46.46 O ANISOU 2551 O HOH A2165 6315 6007 5331 172 8 -101 O HETATM 2552 O HOH A2166 5.283 39.369 22.749 1.00 41.97 O ANISOU 2552 O HOH A2166 5659 5231 5055 249 514 -502 O HETATM 2553 O HOH A2167 38.741 25.325 31.478 1.00 20.41 O ANISOU 2553 O HOH A2167 2521 1552 3681 -167 -646 -228 O HETATM 2554 O HOH A2168 37.355 19.052 34.886 1.00 19.14 O ANISOU 2554 O HOH A2168 2596 1998 2680 130 -981 197 O HETATM 2555 O HOH A2169 38.513 18.283 23.809 1.00 27.71 O ANISOU 2555 O HOH A2169 4310 3205 3012 789 457 -367 O HETATM 2556 O HOH A2170 38.078 25.416 25.179 1.00 39.31 O ANISOU 2556 O HOH A2170 4477 4562 5895 -1373 -572 0 O HETATM 2557 O HOH A2171 34.959 19.489 22.337 1.00 41.78 O ANISOU 2557 O HOH A2171 4706 5483 5685 -475 -207 -612 O HETATM 2558 O HOH A2172 34.615 16.171 25.119 1.00 31.28 O ANISOU 2558 O HOH A2172 3978 4576 3329 436 -160 -652 O HETATM 2559 O HOH A2173 38.950 13.537 28.847 1.00 33.65 O ANISOU 2559 O HOH A2173 3757 3824 5203 202 -92 -290 O HETATM 2560 O HOH A2174 34.686 13.883 27.690 1.00 31.36 O ANISOU 2560 O HOH A2174 4248 4482 3187 185 655 -569 O HETATM 2561 O HOH A2175 34.644 12.385 34.138 1.00 23.49 O ANISOU 2561 O HOH A2175 3018 2670 3236 265 -586 695 O HETATM 2562 O HOH A2176 31.916 7.536 30.625 1.00 57.91 O ANISOU 2562 O HOH A2176 7454 7075 7476 144 144 130 O HETATM 2563 O HOH A2177 36.142 11.834 31.415 1.00 37.19 O ANISOU 2563 O HOH A2177 4152 3599 6381 -62 -120 -134 O HETATM 2564 O HOH A2178 25.055 12.059 38.152 1.00 37.13 O ANISOU 2564 O HOH A2178 4546 4563 4998 -409 462 530 O HETATM 2565 O HOH A2179 29.768 7.491 34.822 1.00 38.83 O ANISOU 2565 O HOH A2179 5954 3219 5582 935 15 679 O HETATM 2566 O HOH A2180 23.903 10.023 36.468 1.00 57.32 O ANISOU 2566 O HOH A2180 6793 7514 7471 -162 -23 -178 O HETATM 2567 O HOH A2181 19.812 44.876 -0.800 1.00 41.26 O ANISOU 2567 O HOH A2181 5060 6028 4590 -29 340 296 O HETATM 2568 O HOH A2182 24.330 44.748 0.037 1.00 54.96 O ANISOU 2568 O HOH A2182 7112 7217 6554 27 237 102 O HETATM 2569 O HOH A2183 11.871 45.525 -3.302 1.00 44.30 O ANISOU 2569 O HOH A2183 6231 6206 4395 29 -522 251 O HETATM 2570 O HOH A2184 31.688 9.890 35.795 1.00 32.41 O ANISOU 2570 O HOH A2184 3834 4031 4451 963 -665 -77 O HETATM 2571 O HOH A2185 24.706 14.935 30.644 1.00 29.59 O ANISOU 2571 O HOH A2185 4764 3282 3197 -208 -272 -135 O HETATM 2572 O HOH A2186 20.484 12.167 35.244 1.00 33.26 O ANISOU 2572 O HOH A2186 5264 3803 3572 502 -1145 434 O HETATM 2573 O HOH A2187 7.705 52.197 0.713 1.00 62.28 O ANISOU 2573 O HOH A2187 7835 7586 8242 177 -68 251 O HETATM 2574 O HOH A2188 24.201 12.990 41.447 1.00 30.73 O ANISOU 2574 O HOH A2188 4525 3530 3622 122 197 761 O HETATM 2575 O HOH A2189 21.987 14.604 41.338 1.00 36.05 O ANISOU 2575 O HOH A2189 4545 3945 5209 -913 621 695 O HETATM 2576 O HOH A2190 25.312 25.620 40.596 1.00 17.90 O ANISOU 2576 O HOH A2190 3481 1995 1324 -737 -376 407 O HETATM 2577 O HOH A2191 22.229 21.318 41.159 1.00 12.98 O ANISOU 2577 O HOH A2191 1603 1945 1385 86 -286 369 O HETATM 2578 O HOH A2192 29.364 21.370 39.354 1.00 20.17 O ANISOU 2578 O HOH A2192 1868 3144 2651 111 -539 894 O HETATM 2579 O HOH A2193 24.962 28.739 29.714 1.00 10.10 O ANISOU 2579 O HOH A2193 1471 1157 1210 -153 -341 334 O HETATM 2580 O HOH A2194 16.749 24.926 41.413 1.00 37.83 O ANISOU 2580 O HOH A2194 4413 5067 4893 1213 -768 683 O HETATM 2581 O HOH A2195 18.232 19.450 39.622 1.00 28.73 O ANISOU 2581 O HOH A2195 3167 4236 3513 -231 -442 -57 O HETATM 2582 O HOH A2196 16.234 22.377 39.012 1.00 14.37 O ANISOU 2582 O HOH A2196 1662 2508 1289 -364 -51 351 O HETATM 2583 O HOH A2197 18.161 27.047 40.548 1.00 28.68 O ANISOU 2583 O HOH A2197 3508 3527 3862 7 703 -596 O HETATM 2584 O HOH A2198 23.422 31.539 40.858 1.00 27.59 O ANISOU 2584 O HOH A2198 4522 3808 2155 -227 -791 -706 O HETATM 2585 O HOH A2199 17.077 32.967 42.580 1.00 38.42 O ANISOU 2585 O HOH A2199 4997 6111 3491 -13 837 -113 O HETATM 2586 O HOH A2200 17.917 36.114 41.386 1.00 50.62 O ANISOU 2586 O HOH A2200 7006 6311 5915 237 349 -452 O HETATM 2587 O HOH A2201 23.378 34.689 41.235 1.00 35.70 O ANISOU 2587 O HOH A2201 5737 5325 2503 339 -818 683 O HETATM 2588 O HOH A2202 12.813 27.371 41.868 1.00 41.97 O ANISOU 2588 O HOH A2202 6937 6070 2938 154 667 -477 O HETATM 2589 O HOH A2203 15.595 36.943 40.219 1.00 39.85 O ANISOU 2589 O HOH A2203 5661 4787 4692 -252 -798 -1091 O HETATM 2590 O HOH A2204 12.161 37.615 39.720 1.00 49.75 O ANISOU 2590 O HOH A2204 6725 6165 6012 448 -88 -736 O HETATM 2591 O HOH A2205 8.486 37.477 36.905 1.00 55.98 O ANISOU 2591 O HOH A2205 6635 7222 7414 254 194 133 O HETATM 2592 O HOH A2206 9.766 38.065 33.013 1.00 57.97 O ANISOU 2592 O HOH A2206 7209 7673 7145 -74 -196 162 O HETATM 2593 O HOH A2207 12.592 39.165 29.656 1.00 18.17 O ANISOU 2593 O HOH A2207 2257 3117 1529 568 535 674 O HETATM 2594 O HOH A2208 19.877 39.097 38.481 1.00 41.65 O ANISOU 2594 O HOH A2208 6006 4022 5796 -374 616 -696 O HETATM 2595 O HOH A2209 11.393 33.934 33.805 1.00 28.29 O ANISOU 2595 O HOH A2209 5339 3070 2339 -12 564 236 O HETATM 2596 O HOH A2210 7.513 33.301 30.022 1.00 27.00 O ANISOU 2596 O HOH A2210 2683 3347 4228 356 986 -90 O HETATM 2597 O HOH A2211 7.935 35.341 24.441 1.00 26.08 O ANISOU 2597 O HOH A2211 2929 3590 3390 623 1128 -460 O HETATM 2598 O HOH A2212 15.816 31.904 34.566 1.00 24.26 O ANISOU 2598 O HOH A2212 3782 2954 2481 179 730 -823 O HETATM 2599 O HOH A2213 18.828 31.673 19.599 1.00 11.22 O ANISOU 2599 O HOH A2213 1633 1299 1331 338 106 290 O HETATM 2600 O HOH A2214 27.173 24.878 15.623 1.00 35.65 O ANISOU 2600 O HOH A2214 3023 5448 5074 -654 1849 164 O HETATM 2601 O HOH A2215 25.323 27.890 16.002 1.00 42.05 O ANISOU 2601 O HOH A2215 4920 5001 6056 -900 -256 498 O HETATM 2602 O HOH A2216 23.416 15.123 20.574 1.00 9.98 O ANISOU 2602 O HOH A2216 1360 1108 1323 112 -257 -26 O HETATM 2603 O HOH A2217 19.369 14.393 12.721 1.00 38.53 O ANISOU 2603 O HOH A2217 5421 4554 4665 -171 -224 -63 O HETATM 2604 O HOH A2218 26.260 16.677 11.785 1.00 29.39 O ANISOU 2604 O HOH A2218 2336 4326 4507 -583 -34 490 O HETATM 2605 O HOH A2219 26.337 14.153 9.904 1.00 46.89 O ANISOU 2605 O HOH A2219 4762 6604 6450 425 106 -202 O HETATM 2606 O HOH A2220 18.107 16.265 6.989 1.00 16.32 O ANISOU 2606 O HOH A2220 2127 2285 1790 127 373 104 O HETATM 2607 O HOH A2221 20.851 18.347 7.492 1.00 23.39 O ANISOU 2607 O HOH A2221 3305 2691 2889 822 45 381 O HETATM 2608 O HOH A2222 19.629 14.008 10.098 1.00 17.54 O ANISOU 2608 O HOH A2222 2750 1844 2072 -100 89 47 O HETATM 2609 O HOH A2223 16.915 8.032 7.952 1.00 47.69 O ANISOU 2609 O HOH A2223 5598 6101 6421 -177 -641 138 O HETATM 2610 O HOH A2224 23.679 10.086 6.304 1.00 57.60 O ANISOU 2610 O HOH A2224 6928 7680 7280 396 313 -119 O HETATM 2611 O HOH A2225 23.716 12.375 4.743 1.00 37.15 O ANISOU 2611 O HOH A2225 4111 5119 4885 613 828 -997 O HETATM 2612 O HOH A2226 23.158 11.880 8.875 1.00 20.41 O ANISOU 2612 O HOH A2226 2916 2060 2780 -23 200 -120 O HETATM 2613 O HOH A2227 25.026 10.768 11.701 1.00 42.70 O ANISOU 2613 O HOH A2227 5968 5742 4513 652 202 13 O HETATM 2614 O HOH A2228 17.949 6.476 9.872 1.00 17.51 O ANISOU 2614 O HOH A2228 2200 1618 2836 -250 660 -289 O HETATM 2615 O HOH A2229 16.178 10.232 15.769 1.00 30.64 O ANISOU 2615 O HOH A2229 4143 2421 5076 -73 1073 458 O HETATM 2616 O HOH A2230 16.393 11.086 18.980 1.00 29.86 O ANISOU 2616 O HOH A2230 3912 3718 3716 -1625 -1537 1257 O HETATM 2617 O HOH A2231 25.843 10.940 14.813 1.00 27.98 O ANISOU 2617 O HOH A2231 3676 2063 4892 134 2483 -554 O HETATM 2618 O HOH A2232 15.439 9.921 23.697 1.00 30.91 O ANISOU 2618 O HOH A2232 3570 4587 3585 -1470 -209 341 O HETATM 2619 O HOH A2233 14.682 11.944 20.633 1.00 43.49 O ANISOU 2619 O HOH A2233 5189 5505 5829 71 -991 -263 O HETATM 2620 O HOH A2234 27.517 19.639 11.990 1.00 35.23 O ANISOU 2620 O HOH A2234 4235 4745 4405 1180 1196 758 O HETATM 2621 O HOH A2235 29.631 18.121 16.058 1.00 33.86 O ANISOU 2621 O HOH A2235 2639 4711 5516 1064 20 100 O HETATM 2622 O HOH A2236 32.437 11.504 16.158 1.00 45.92 O ANISOU 2622 O HOH A2236 5550 6513 5386 74 665 221 O HETATM 2623 O HOH A2237 30.262 15.533 16.637 1.00 57.01 O ANISOU 2623 O HOH A2237 7493 7074 7093 -7 281 297 O HETATM 2624 O HOH A2238 27.952 13.501 14.960 1.00 32.95 O ANISOU 2624 O HOH A2238 4076 6030 2413 1019 841 97 O HETATM 2625 O HOH A2239 30.653 17.297 18.985 1.00 42.98 O ANISOU 2625 O HOH A2239 5324 4183 6824 -602 505 305 O HETATM 2626 O HOH A2240 25.241 17.150 21.368 1.00 11.61 O ANISOU 2626 O HOH A2240 1239 1270 1904 121 -132 156 O HETATM 2627 O HOH A2241 29.988 11.138 28.400 1.00 15.85 O ANISOU 2627 O HOH A2241 2126 1969 1927 599 -545 -74 O HETATM 2628 O HOH A2242 31.947 16.674 22.973 1.00 24.13 O ANISOU 2628 O HOH A2242 2945 2883 3338 -1337 558 -154 O HETATM 2629 O HOH A2243 24.492 7.565 23.585 1.00 19.03 O ANISOU 2629 O HOH A2243 2920 1568 2743 -562 -284 -392 O HETATM 2630 O HOH A2244 26.554 5.956 28.470 1.00 58.64 O ANISOU 2630 O HOH A2244 8055 6961 7266 -82 187 80 O HETATM 2631 O HOH A2245 33.218 14.747 21.091 1.00 49.56 O ANISOU 2631 O HOH A2245 5381 7106 6345 140 646 77 O HETATM 2632 O HOH A2246 32.459 10.902 26.701 1.00 32.21 O ANISOU 2632 O HOH A2246 3093 5879 3265 959 -199 -96 O HETATM 2633 O HOH A2247 29.745 8.326 29.002 1.00 40.19 O ANISOU 2633 O HOH A2247 5306 4660 5303 -88 -511 279 O HETATM 2634 O HOH A2248 22.774 7.100 30.981 1.00 49.51 O ANISOU 2634 O HOH A2248 6773 5943 6095 -746 70 448 O HETATM 2635 O HOH A2249 26.085 8.652 32.125 1.00 33.26 O ANISOU 2635 O HOH A2249 4075 5347 3215 -855 -1150 725 O HETATM 2636 O HOH A2250 21.083 5.770 26.544 1.00 16.17 O ANISOU 2636 O HOH A2250 2018 1089 3036 -179 -386 -4 O HETATM 2637 O HOH A2251 16.168 12.815 26.002 1.00 11.78 O ANISOU 2637 O HOH A2251 1600 1187 1688 25 -177 -25 O HETATM 2638 O HOH A2252 16.508 9.891 33.030 1.00 39.17 O ANISOU 2638 O HOH A2252 5557 4671 4655 -312 680 -161 O HETATM 2639 O HOH A2253 14.565 12.131 33.741 1.00 40.36 O ANISOU 2639 O HOH A2253 4544 5494 5297 15 203 -63 O HETATM 2640 O HOH A2254 11.524 9.312 32.338 1.00 53.59 O ANISOU 2640 O HOH A2254 6831 6185 7346 -356 34 81 O HETATM 2641 O HOH A2255 13.926 8.615 30.582 1.00 40.64 O ANISOU 2641 O HOH A2255 5131 4432 5878 308 314 737 O HETATM 2642 O HOH A2256 14.194 11.057 27.144 1.00 22.05 O ANISOU 2642 O HOH A2256 2047 2239 4091 -682 -644 694 O HETATM 2643 O HOH A2257 14.229 18.097 38.226 1.00 38.82 O ANISOU 2643 O HOH A2257 5847 5105 3796 -372 293 -119 O HETATM 2644 O HOH A2258 9.373 17.142 35.321 1.00 32.52 O ANISOU 2644 O HOH A2258 3733 5029 3593 -720 551 -832 O HETATM 2645 O HOH A2259 6.469 12.916 33.709 1.00 41.40 O ANISOU 2645 O HOH A2259 4863 5887 4979 -465 129 464 O HETATM 2646 O HOH A2260 10.638 19.214 36.574 1.00 24.07 O ANISOU 2646 O HOH A2260 2269 3265 3612 -586 977 -14 O HETATM 2647 O HOH A2261 17.504 17.243 37.636 1.00 27.89 O ANISOU 2647 O HOH A2261 3980 3599 3018 -19 847 936 O HETATM 2648 O HOH A2262 4.912 20.695 31.312 1.00 38.10 O ANISOU 2648 O HOH A2262 3807 3950 6718 -602 601 358 O HETATM 2649 O HOH A2263 5.480 21.003 33.907 1.00 42.22 O ANISOU 2649 O HOH A2263 4581 4573 6888 -1255 687 559 O HETATM 2650 O HOH A2264 8.260 23.556 38.468 1.00 40.60 O ANISOU 2650 O HOH A2264 4695 5879 4853 376 204 55 O HETATM 2651 O HOH A2265 10.398 24.029 41.577 1.00 34.03 O ANISOU 2651 O HOH A2265 4533 5439 2959 -16 937 206 O HETATM 2652 O HOH A2266 16.154 28.857 40.685 1.00 28.20 O ANISOU 2652 O HOH A2266 3053 4142 3521 99 -519 -935 O HETATM 2653 O HOH A2267 13.921 32.985 33.365 1.00 37.81 O ANISOU 2653 O HOH A2267 5187 5247 3932 -490 732 -208 O HETATM 2654 O HOH A2268 9.716 31.931 38.921 1.00 32.51 O ANISOU 2654 O HOH A2268 3968 5245 3140 483 330 -758 O HETATM 2655 O HOH A2269 5.464 26.261 34.296 1.00 42.78 O ANISOU 2655 O HOH A2269 5426 4513 6317 -14 -335 0 O HETATM 2656 O HOH A2270 7.678 34.957 37.887 1.00 54.51 O ANISOU 2656 O HOH A2270 6906 6523 7284 -17 103 -243 O HETATM 2657 O HOH A2271 9.085 35.288 33.406 1.00 57.67 O ANISOU 2657 O HOH A2271 7598 6841 7472 -167 -18 85 O HETATM 2658 O HOH A2272 4.870 32.650 32.891 1.00 50.46 O ANISOU 2658 O HOH A2272 6069 6595 6508 508 -300 115 O HETATM 2659 O HOH A2273 6.273 28.024 31.488 1.00 41.26 O ANISOU 2659 O HOH A2273 4211 5331 6135 203 355 393 O HETATM 2660 O HOH A2274 9.770 26.557 33.068 1.00 12.41 O ANISOU 2660 O HOH A2274 2009 1385 1321 -282 -153 172 O HETATM 2661 O HOH A2275 5.221 34.079 25.276 1.00 34.83 O ANISOU 2661 O HOH A2275 4840 4113 4282 33 148 -182 O HETATM 2662 O HOH A2276 1.610 31.352 27.179 1.00 60.58 O ANISOU 2662 O HOH A2276 7054 8165 7800 369 230 -200 O HETATM 2663 O HOH A2277 22.247 20.383 14.900 1.00 8.96 O ANISOU 2663 O HOH A2277 1099 1024 1282 71 -16 -125 O HETATM 2664 O HOH A2278 27.224 23.308 12.949 1.00 50.66 O ANISOU 2664 O HOH A2278 5397 7291 6562 -576 159 -217 O HETATM 2665 O HOH A2279 24.383 23.565 6.943 1.00 47.23 O ANISOU 2665 O HOH A2279 5494 6485 5965 -521 509 402 O HETATM 2666 O HOH A2280 18.465 18.763 7.892 1.00 41.84 O ANISOU 2666 O HOH A2280 4256 4190 7452 -407 -353 -537 O HETATM 2667 O HOH A2281 18.581 26.945 9.627 1.00 12.98 O ANISOU 2667 O HOH A2281 1396 1197 2338 31 -47 302 O HETATM 2668 O HOH A2282 12.497 20.129 -0.745 1.00 29.72 O ANISOU 2668 O HOH A2282 5284 3429 2578 72 -774 -573 O HETATM 2669 O HOH A2283 15.315 21.594 6.770 1.00 23.40 O ANISOU 2669 O HOH A2283 2620 3857 2416 525 -971 -281 O HETATM 2670 O HOH A2284 3.881 14.364 6.158 1.00 53.81 O ANISOU 2670 O HOH A2284 7457 5872 7114 -664 -142 -267 O HETATM 2671 O HOH A2285 7.789 14.771 5.643 1.00 34.06 O ANISOU 2671 O HOH A2285 4550 4141 4252 -1151 102 -402 O HETATM 2672 O HOH A2286 13.181 17.063 -0.004 1.00 44.08 O ANISOU 2672 O HOH A2286 5738 6162 4848 -12 1040 -479 O HETATM 2673 O HOH A2287 12.255 12.516 5.842 1.00 40.96 O ANISOU 2673 O HOH A2287 5959 4208 5397 -311 -220 -113 O HETATM 2674 O HOH A2288 15.075 19.469 -0.447 1.00 39.10 O ANISOU 2674 O HOH A2288 5500 4678 4680 39 473 -639 O HETATM 2675 O HOH A2289 14.450 11.106 10.637 1.00 21.61 O ANISOU 2675 O HOH A2289 3199 1834 3179 -416 331 -400 O HETATM 2676 O HOH A2290 16.708 14.450 4.328 1.00 31.44 O ANISOU 2676 O HOH A2290 4206 5015 2724 1065 1238 -63 O HETATM 2677 O HOH A2291 5.394 13.185 10.266 1.00 34.20 O ANISOU 2677 O HOH A2291 3218 4413 5362 -694 68 294 O HETATM 2678 O HOH A2292 8.162 11.137 10.796 1.00 33.45 O ANISOU 2678 O HOH A2292 4479 3142 5088 -289 -188 380 O HETATM 2679 O HOH A2293 14.052 11.486 17.227 1.00 20.32 O ANISOU 2679 O HOH A2293 2378 2170 3172 94 -9 830 O HETATM 2680 O HOH A2294 2.835 14.251 10.781 1.00 42.97 O ANISOU 2680 O HOH A2294 4735 6508 5082 -420 -300 206 O HETATM 2681 O HOH A2295 1.670 13.003 15.013 1.00 43.74 O ANISOU 2681 O HOH A2295 5093 4969 6558 -556 92 288 O HETATM 2682 O HOH A2296 1.242 17.554 14.044 1.00 18.85 O ANISOU 2682 O HOH A2296 1580 2186 3395 -466 -219 -27 O HETATM 2683 O HOH A2297 10.976 8.444 12.722 1.00 50.31 O ANISOU 2683 O HOH A2297 6832 5683 6601 -88 -43 -65 O HETATM 2684 O HOH A2298 5.919 10.814 12.627 1.00 39.65 O ANISOU 2684 O HOH A2298 4772 4188 6105 -346 205 69 O HETATM 2685 O HOH A2299 7.329 9.891 18.617 1.00 25.97 O ANISOU 2685 O HOH A2299 3756 2475 3637 -883 456 -636 O HETATM 2686 O HOH A2300 12.990 10.287 12.889 1.00 44.64 O ANISOU 2686 O HOH A2300 5948 5443 5570 11 210 575 O HETATM 2687 O HOH A2301 2.112 13.626 21.726 1.00 21.33 O ANISOU 2687 O HOH A2301 2790 2558 2756 11 -258 219 O HETATM 2688 O HOH A2302 5.655 6.085 18.979 1.00 46.46 O ANISOU 2688 O HOH A2302 6634 5181 5836 -243 115 -607 O HETATM 2689 O HOH A2303 11.937 7.759 24.052 1.00 42.52 O ANISOU 2689 O HOH A2303 5794 4794 5568 903 -399 222 O HETATM 2690 O HOH A2304 12.699 11.168 22.298 1.00 33.26 O ANISOU 2690 O HOH A2304 4478 3973 4186 -1005 25 1006 O HETATM 2691 O HOH A2305 9.470 6.379 24.107 1.00 44.90 O ANISOU 2691 O HOH A2305 6281 4098 6679 919 -33 579 O HETATM 2692 O HOH A2306 6.203 7.833 24.011 1.00 26.81 O ANISOU 2692 O HOH A2306 2955 2861 4369 -390 -281 -189 O HETATM 2693 O HOH A2307 3.117 16.571 28.377 1.00 20.49 O ANISOU 2693 O HOH A2307 2145 2849 2790 496 -22 -444 O HETATM 2694 O HOH A2308 -0.704 9.670 22.110 1.00 41.47 O ANISOU 2694 O HOH A2308 3714 5999 6043 -735 88 -271 O HETATM 2695 O HOH A2309 0.697 11.748 20.258 1.00 41.12 O ANISOU 2695 O HOH A2309 5424 5150 5051 -400 -121 -569 O HETATM 2696 O HOH A2310 6.339 8.283 20.632 1.00 49.95 O ANISOU 2696 O HOH A2310 6770 5679 6530 -477 379 -123 O HETATM 2697 O HOH A2311 2.590 10.128 30.515 1.00 22.53 O ANISOU 2697 O HOH A2311 2674 3299 2588 555 1046 666 O HETATM 2698 O HOH A2312 3.834 11.892 33.082 1.00 44.05 O ANISOU 2698 O HOH A2312 5502 6811 4424 -407 240 138 O HETATM 2699 O HOH A2313 9.275 8.352 30.836 1.00 35.01 O ANISOU 2699 O HOH A2313 4864 4994 3446 -767 45 812 O HETATM 2700 O HOH A2314 6.989 9.459 32.032 1.00 46.39 O ANISOU 2700 O HOH A2314 6495 5871 5261 96 232 530 O HETATM 2701 O HOH A2315 5.453 15.484 34.104 1.00 51.48 O ANISOU 2701 O HOH A2315 6299 7147 6116 -222 352 -148 O HETATM 2702 O HOH A2316 5.077 18.151 31.913 1.00 43.07 O ANISOU 2702 O HOH A2316 5049 5541 5774 -67 234 -335 O HETATM 2703 O HOH A2317 5.122 18.427 27.874 1.00 23.91 O ANISOU 2703 O HOH A2317 2032 4138 2913 237 -658 119 O HETATM 2704 O HOH A2318 5.166 20.888 28.648 1.00 34.12 O ANISOU 2704 O HOH A2318 3007 4938 5019 20 -196 494 O HETATM 2705 O HOH A2319 4.373 26.315 30.437 1.00 40.19 O ANISOU 2705 O HOH A2319 4497 5512 5260 1002 881 -619 O HETATM 2706 O HOH A2320 3.879 23.110 27.895 1.00 21.19 O ANISOU 2706 O HOH A2320 2079 2848 3122 -616 1 -70 O HETATM 2707 O HOH A2321 3.731 26.885 25.448 1.00 25.19 O ANISOU 2707 O HOH A2321 2292 4589 2690 331 -50 659 O HETATM 2708 O HOH A2322 23.943 27.528 13.727 1.00 27.11 O ANISOU 2708 O HOH A2322 2023 3103 5174 -276 671 559 O HETATM 2709 O HOH A2323 21.551 26.575 7.738 1.00 28.14 O ANISOU 2709 O HOH A2323 4674 2760 3258 995 -1139 -575 O HETATM 2710 O HOH A2324 18.968 29.857 -1.793 1.00 44.29 O ANISOU 2710 O HOH A2324 4408 5477 6943 302 202 -86 O HETATM 2711 O HOH A2325 19.269 31.573 0.309 1.00 40.33 O ANISOU 2711 O HOH A2325 3788 6398 5137 405 -500 680 O HETATM 2712 O HOH A2326 23.802 25.386 4.440 1.00 36.70 O ANISOU 2712 O HOH A2326 3965 4965 5015 207 -661 330 O HETATM 2713 O HOH A2327 25.598 25.727 -1.898 1.00 36.82 O ANISOU 2713 O HOH A2327 4056 4763 5170 332 15 -266 O HETATM 2714 O HOH A2328 19.650 27.017 -3.225 1.00 19.19 O ANISOU 2714 O HOH A2328 2399 2573 2319 -40 119 -479 O HETATM 2715 O HOH A2329 20.247 23.412 -1.847 1.00 26.66 O ANISOU 2715 O HOH A2329 3842 3374 2912 269 658 -733 O HETATM 2716 O HOH A2330 25.647 27.100 1.876 1.00 47.01 O ANISOU 2716 O HOH A2330 5503 6144 6214 6 57 -499 O HETATM 2717 O HOH A2331 16.600 22.976 4.758 1.00 26.12 O ANISOU 2717 O HOH A2331 2847 3427 3652 103 370 -1 O HETATM 2718 O HOH A2332 16.689 25.573 6.135 1.00 25.64 O ANISOU 2718 O HOH A2332 3531 4159 2052 681 888 495 O HETATM 2719 O HOH A2333 14.320 25.177 4.433 1.00 23.84 O ANISOU 2719 O HOH A2333 4330 2628 2100 -408 558 445 O HETATM 2720 O HOH A2334 15.511 23.336 2.155 1.00 26.39 O ANISOU 2720 O HOH A2334 3697 2565 3765 -441 721 -361 O HETATM 2721 O HOH A2335 5.740 31.315 0.716 1.00 31.18 O ANISOU 2721 O HOH A2335 3712 3791 4345 -9 -1367 766 O HETATM 2722 O HOH A2336 14.140 29.680 -1.760 1.00 25.28 O ANISOU 2722 O HOH A2336 3840 3968 1796 -1395 2 150 O HETATM 2723 O HOH A2337 16.677 30.808 0.706 1.00 20.55 O ANISOU 2723 O HOH A2337 2356 2556 2895 -456 354 375 O HETATM 2724 O HOH A2338 7.013 22.600 -1.165 1.00 29.05 O ANISOU 2724 O HOH A2338 4370 4492 2175 -1887 -1241 -69 O HETATM 2725 O HOH A2339 11.920 25.943 4.508 1.00 23.50 O ANISOU 2725 O HOH A2339 3822 3411 1694 389 -635 238 O HETATM 2726 O HOH A2340 13.790 23.408 -0.539 1.00 30.09 O ANISOU 2726 O HOH A2340 2952 3230 5250 167 1249 775 O HETATM 2727 O HOH A2341 3.998 23.418 0.582 1.00 45.90 O ANISOU 2727 O HOH A2341 5673 6423 5345 1 -403 -192 O HETATM 2728 O HOH A2342 4.741 24.099 -1.703 1.00 43.89 O ANISOU 2728 O HOH A2342 6311 5052 5312 -679 244 116 O HETATM 2729 O HOH A2343 5.347 31.073 -1.874 1.00 52.64 O ANISOU 2729 O HOH A2343 6649 7037 6315 468 -205 542 O HETATM 2730 O HOH A2344 7.317 20.045 -0.138 1.00 30.19 O ANISOU 2730 O HOH A2344 4925 3850 2694 -309 -583 -560 O HETATM 2731 O HOH A2345 0.118 34.322 3.079 1.00 53.10 O ANISOU 2731 O HOH A2345 6720 6396 7059 694 -521 627 O HETATM 2732 O HOH A2346 -2.142 29.696 5.652 1.00 35.54 O ANISOU 2732 O HOH A2346 2559 5199 5747 -493 -337 42 O HETATM 2733 O HOH A2347 0.009 22.569 5.203 1.00 50.92 O ANISOU 2733 O HOH A2347 5935 6411 7002 -43 2 214 O HETATM 2734 O HOH A2348 3.376 21.597 2.391 1.00 35.92 O ANISOU 2734 O HOH A2348 4204 5649 3793 -424 154 -644 O HETATM 2735 O HOH A2349 2.966 25.474 3.148 1.00 38.12 O ANISOU 2735 O HOH A2349 3562 5561 5360 -351 314 -28 O HETATM 2736 O HOH A2350 -0.372 21.686 8.168 1.00 40.24 O ANISOU 2736 O HOH A2350 5037 5630 4621 121 -226 -167 O HETATM 2737 O HOH A2351 -1.999 28.026 10.197 1.00 48.61 O ANISOU 2737 O HOH A2351 6019 6284 6166 -427 -510 -57 O HETATM 2738 O HOH A2352 -1.598 24.066 13.683 1.00 34.38 O ANISOU 2738 O HOH A2352 2567 5498 4998 772 813 104 O HETATM 2739 O HOH A2353 1.291 17.910 6.784 1.00 36.04 O ANISOU 2739 O HOH A2353 5566 4633 3495 -932 -895 -677 O HETATM 2740 O HOH A2354 -0.796 17.999 12.209 1.00 46.80 O ANISOU 2740 O HOH A2354 5936 6228 5618 -235 -562 -154 O HETATM 2741 O HOH A2355 -1.311 20.635 11.230 1.00 48.59 O ANISOU 2741 O HOH A2355 5650 6595 6217 165 -102 -76 O HETATM 2742 O HOH A2356 -1.694 23.577 20.023 1.00 28.26 O ANISOU 2742 O HOH A2356 2797 4724 3217 49 111 -283 O HETATM 2743 O HOH A2357 -3.874 19.610 17.731 1.00 41.35 O ANISOU 2743 O HOH A2357 4191 6381 5141 -296 457 267 O HETATM 2744 O HOH A2358 1.561 16.073 20.884 1.00 25.07 O ANISOU 2744 O HOH A2358 3879 2717 2931 -249 486 370 O HETATM 2745 O HOH A2359 2.937 24.241 25.594 1.00 41.77 O ANISOU 2745 O HOH A2359 6052 5855 3964 -482 -644 -317 O HETATM 2746 O HOH A2360 0.650 30.695 22.184 1.00 33.30 O ANISOU 2746 O HOH A2360 3121 3908 5623 1324 281 -143 O HETATM 2747 O HOH A2361 17.426 34.059 19.629 1.00 8.25 O ANISOU 2747 O HOH A2361 1260 918 956 -183 91 -42 O HETATM 2748 O HOH A2362 24.290 30.420 15.895 1.00 31.85 O ANISOU 2748 O HOH A2362 2077 5423 4602 284 203 497 O HETATM 2749 O HOH A2363 22.828 28.751 18.112 1.00 12.69 O ANISOU 2749 O HOH A2363 1568 1699 1553 181 -218 250 O HETATM 2750 O HOH A2364 27.211 35.334 -0.655 1.00 50.48 O ANISOU 2750 O HOH A2364 6797 6352 6031 -501 488 -275 O HETATM 2751 O HOH A2365 19.019 33.849 -0.931 1.00 30.66 O ANISOU 2751 O HOH A2365 3717 3565 4367 -550 -140 -1198 O HETATM 2752 O HOH A2366 26.602 30.450 -2.265 1.00 49.68 O ANISOU 2752 O HOH A2366 5779 6427 6671 79 661 -81 O HETATM 2753 O HOH A2367 25.968 29.727 1.066 1.00 51.98 O ANISOU 2753 O HOH A2367 6072 6578 7099 72 32 -100 O HETATM 2754 O HOH A2368 18.704 41.688 -2.379 1.00 39.17 O ANISOU 2754 O HOH A2368 5277 5533 4071 -234 168 1523 O HETATM 2755 O HOH A2369 17.528 43.945 0.764 1.00 19.06 O ANISOU 2755 O HOH A2369 2443 1907 2891 -248 757 58 O HETATM 2756 O HOH A2370 9.080 41.909 -1.285 1.00 46.74 O ANISOU 2756 O HOH A2370 6005 5850 5902 324 -76 -180 O HETATM 2757 O HOH A2371 15.803 42.430 -2.655 1.00 31.76 O ANISOU 2757 O HOH A2371 4248 4002 3817 -125 1145 1615 O HETATM 2758 O HOH A2372 14.376 37.623 -5.189 1.00 45.35 O ANISOU 2758 O HOH A2372 6321 6375 4534 -13 250 -237 O HETATM 2759 O HOH A2373 13.262 39.834 -3.869 1.00 30.17 O ANISOU 2759 O HOH A2373 4662 4903 1898 -986 634 -15 O HETATM 2760 O HOH A2374 16.228 33.176 -0.782 1.00 28.38 O ANISOU 2760 O HOH A2374 4321 2878 3584 157 44 -110 O HETATM 2761 O HOH A2375 7.095 37.690 -1.269 1.00 44.34 O ANISOU 2761 O HOH A2375 4975 5601 6270 -199 -220 576 O HETATM 2762 O HOH A2376 4.598 33.298 2.812 1.00 22.00 O ANISOU 2762 O HOH A2376 2404 3132 2823 -624 -628 620 O HETATM 2763 O HOH A2377 6.835 34.310 -3.271 1.00 37.94 O ANISOU 2763 O HOH A2377 6364 5274 2777 705 772 360 O HETATM 2764 O HOH A2378 3.708 40.909 2.169 1.00 31.20 O ANISOU 2764 O HOH A2378 4607 3428 3821 -85 -865 667 O HETATM 2765 O HOH A2379 1.057 40.539 5.734 1.00 25.58 O ANISOU 2765 O HOH A2379 2599 3346 3773 35 -458 -408 O HETATM 2766 O HOH A2380 0.210 35.721 6.703 1.00 23.50 O ANISOU 2766 O HOH A2380 1999 3783 3147 603 -547 687 O HETATM 2767 O HOH A2381 4.276 36.200 1.428 1.00 42.32 O ANISOU 2767 O HOH A2381 5295 6225 4560 1166 -1013 -139 O HETATM 2768 O HOH A2382 -0.089 38.673 2.459 1.00 57.59 O ANISOU 2768 O HOH A2382 6904 7621 7358 -5 -180 -212 O HETATM 2769 O HOH A2383 4.430 29.449 2.703 1.00 14.81 O ANISOU 2769 O HOH A2383 1774 2340 1514 328 -140 -74 O HETATM 2770 O HOH A2384 -1.877 37.017 12.826 1.00 32.51 O ANISOU 2770 O HOH A2384 2525 4533 5295 834 -12 -1011 O HETATM 2771 O HOH A2385 -3.712 31.053 8.838 1.00 40.97 O ANISOU 2771 O HOH A2385 3460 6589 5517 -619 -861 339 O HETATM 2772 O HOH A2386 -4.177 31.445 12.496 1.00 33.86 O ANISOU 2772 O HOH A2386 4093 4420 4354 76 329 -373 O HETATM 2773 O HOH A2387 -0.938 27.489 15.735 1.00 20.14 O ANISOU 2773 O HOH A2387 2325 2296 3033 597 157 -62 O HETATM 2774 O HOH A2388 1.156 34.296 18.494 1.00 21.37 O ANISOU 2774 O HOH A2388 1993 2879 3248 -102 412 -621 O HETATM 2775 O HOH A2389 -2.793 28.711 13.051 1.00 26.66 O ANISOU 2775 O HOH A2389 2805 4034 3290 -1483 -208 -949 O HETATM 2776 O HOH A2390 0.307 25.925 25.864 1.00 47.19 O ANISOU 2776 O HOH A2390 4299 7541 6091 152 740 -382 O HETATM 2777 O HOH A2391 4.471 36.852 21.294 1.00 24.92 O ANISOU 2777 O HOH A2391 3974 3241 2254 675 1227 -29 O HETATM 2778 O HOH A2392 15.839 38.272 20.345 1.00 10.07 O ANISOU 2778 O HOH A2392 1345 1259 1220 188 -305 -203 O HETATM 2779 O HOH A2393 18.980 43.353 10.732 1.00 9.73 O ANISOU 2779 O HOH A2393 1021 1397 1280 -89 -77 117 O HETATM 2780 O HOH A2394 26.028 45.348 2.856 1.00 32.81 O ANISOU 2780 O HOH A2394 4562 4202 3702 -1557 777 898 O HETATM 2781 O HOH A2395 29.630 46.635 12.211 1.00 20.15 O ANISOU 2781 O HOH A2395 1751 2963 2941 -480 342 -103 O HETATM 2782 O HOH A2396 29.021 38.514 14.864 1.00 19.09 O ANISOU 2782 O HOH A2396 3040 2095 2117 322 -62 239 O HETATM 2783 O HOH A2397 23.664 37.281 10.686 1.00 11.26 O ANISOU 2783 O HOH A2397 1321 1564 1392 -346 236 -225 O HETATM 2784 O HOH A2398 23.855 27.343 9.101 1.00 40.01 O ANISOU 2784 O HOH A2398 4001 4901 6300 239 -290 209 O HETATM 2785 O HOH A2399 23.507 34.291 4.566 1.00 35.19 O ANISOU 2785 O HOH A2399 4960 3536 4874 -345 569 382 O HETATM 2786 O BHOH A2400 24.323 31.462 6.061 0.50 17.69 O ANISOU 2786 O BHOH A2400 1591 2504 2628 286 -248 -1023 O HETATM 2787 O HOH A2401 21.953 32.607 6.301 1.00 14.74 O ANISOU 2787 O HOH A2401 1647 2327 1627 43 274 -486 O HETATM 2788 O HOH A2402 33.033 40.181 5.119 1.00 37.65 O ANISOU 2788 O HOH A2402 4321 5947 4038 -790 681 -219 O HETATM 2789 O HOH A2403 29.996 42.454 3.316 1.00 48.77 O ANISOU 2789 O HOH A2403 6232 5416 6882 -59 -372 623 O HETATM 2790 O HOH A2404 31.811 38.022 9.222 1.00 23.37 O ANISOU 2790 O HOH A2404 2385 3110 3384 -29 -453 -229 O HETATM 2791 O HOH A2405 34.643 36.736 6.208 1.00 39.30 O ANISOU 2791 O HOH A2405 4794 5622 4516 -484 -221 -342 O HETATM 2792 O HOH A2406 30.551 40.630 0.251 1.00 56.88 O ANISOU 2792 O HOH A2406 7055 7461 7094 -201 25 232 O HETATM 2793 O HOH A2407 32.210 34.658 8.212 1.00 52.99 O ANISOU 2793 O HOH A2407 6117 7585 6433 304 261 149 O HETATM 2794 O HOH A2408 24.801 42.432 -1.424 1.00 57.86 O ANISOU 2794 O HOH A2408 7630 7481 6872 -22 -87 334 O HETATM 2795 O HOH A2409 25.872 39.013 -0.886 1.00 42.19 O ANISOU 2795 O HOH A2409 5500 6365 4165 231 940 -371 O HETATM 2796 O HOH A2410 20.111 49.575 0.194 1.00 36.11 O ANISOU 2796 O HOH A2410 4750 5426 3543 -243 -459 484 O HETATM 2797 O HOH A2411 22.213 47.141 0.093 1.00 45.47 O ANISOU 2797 O HOH A2411 6547 6144 4584 -297 308 -180 O HETATM 2798 O HOH A2412 30.935 49.467 3.908 1.00 38.90 O ANISOU 2798 O HOH A2412 4117 5197 5468 -511 145 -380 O HETATM 2799 O HOH A2413 29.366 43.877 5.611 1.00 29.64 O ANISOU 2799 O HOH A2413 3055 4035 4172 384 781 864 O HETATM 2800 O HOH A2414 26.227 48.024 3.345 1.00 27.28 O ANISOU 2800 O HOH A2414 4163 4009 2194 542 228 -40 O HETATM 2801 O HOH A2415 27.078 52.298 11.034 1.00 19.96 O ANISOU 2801 O HOH A2415 3509 1867 2208 -193 171 187 O HETATM 2802 O HOH A2416 24.845 52.572 1.964 1.00 57.68 O ANISOU 2802 O HOH A2416 7205 7506 7204 -128 143 230 O HETATM 2803 O HOH A2417 25.402 57.058 8.474 1.00 57.68 O ANISOU 2803 O HOH A2417 7121 6966 7830 -135 194 -439 O HETATM 2804 O HOH A2418 26.713 51.039 3.707 1.00 32.86 O ANISOU 2804 O HOH A2418 4256 4370 3859 -255 821 693 O HETATM 2805 O HOH A2419 23.022 55.947 3.073 1.00 42.90 O ANISOU 2805 O HOH A2419 5521 5372 5406 69 488 452 O HETATM 2806 O HOH A2420 21.365 53.405 1.047 1.00 53.26 O ANISOU 2806 O HOH A2420 6675 7130 6432 -243 -68 417 O HETATM 2807 O HOH A2421 14.530 56.155 8.490 1.00 39.04 O ANISOU 2807 O HOH A2421 6824 2694 5314 -336 767 -307 O HETATM 2808 O HOH A2422 11.009 53.108 6.766 1.00 32.28 O ANISOU 2808 O HOH A2422 3786 4054 4426 296 -657 95 O HETATM 2809 O HOH A2423 18.699 53.182 2.191 1.00 49.75 O ANISOU 2809 O HOH A2423 6806 5956 6141 -385 -302 990 O HETATM 2810 O HOH A2424 17.462 54.486 5.434 1.00 28.73 O ANISOU 2810 O HOH A2424 3218 1728 5969 378 -138 871 O HETATM 2811 O HOH A2425 21.753 42.679 0.440 1.00 23.64 O ANISOU 2811 O HOH A2425 3745 3259 1977 -492 571 -37 O HETATM 2812 O HOH A2426 11.140 46.363 -0.717 1.00 31.01 O ANISOU 2812 O HOH A2426 3866 4844 3074 140 -801 858 O HETATM 2813 O HOH A2427 18.677 47.374 -0.589 1.00 29.13 O ANISOU 2813 O HOH A2427 3513 4834 2721 -784 1038 -67 O HETATM 2814 O HOH A2428 10.177 51.362 4.875 1.00 39.74 O ANISOU 2814 O HOH A2428 5693 4365 5041 311 -133 321 O HETATM 2815 O HOH A2429 5.932 42.900 1.846 1.00 22.56 O ANISOU 2815 O HOH A2429 2976 3077 2519 2 -956 -89 O HETATM 2816 O HOH A2430 6.233 49.915 0.259 1.00 45.18 O ANISOU 2816 O HOH A2430 5933 5689 5543 344 -146 778 O HETATM 2817 O HOH A2431 6.449 45.528 0.282 1.00 42.38 O ANISOU 2817 O HOH A2431 5790 6144 4171 258 -45 502 O HETATM 2818 O HOH A2432 7.490 50.381 4.624 1.00 61.83 O ANISOU 2818 O HOH A2432 7644 8496 7355 123 17 17 O HETATM 2819 O HOH A2433 4.280 49.675 6.131 1.00 30.27 O ANISOU 2819 O HOH A2433 4690 2883 3927 165 26 399 O HETATM 2820 O HOH A2434 -1.093 44.137 10.842 1.00 50.16 O ANISOU 2820 O HOH A2434 5073 6865 7121 104 98 48 O HETATM 2821 O HOH A2435 -0.564 41.912 9.190 1.00 45.18 O ANISOU 2821 O HOH A2435 5129 5805 6235 33 144 -141 O HETATM 2822 O HOH A2436 -3.962 47.733 8.743 1.00 61.90 O ANISOU 2822 O HOH A2436 7078 7965 8476 -222 45 184 O HETATM 2823 O HOH A2437 -1.423 48.829 9.074 1.00 48.47 O ANISOU 2823 O HOH A2437 4914 6310 7193 250 35 153 O HETATM 2824 O HOH A2438 1.527 47.701 4.498 1.00 56.70 O ANISOU 2824 O HOH A2438 6829 7568 7147 110 -248 120 O CONECT 1314 1604 1605 CONECT 1604 1314 CONECT 1605 1314 CONECT 2008 2052 CONECT 2052 2008 MASTER 297 0 0 15 8 0 2 6 2823 1 5 25 END