HEADER SUGAR BINDING PROTEIN 04-JUL-05 2A6Z TITLE CRYSTAL STRUCTURE OF EMP47P CARBOHYDRATE RECOGNITION DOMAIN TITLE 2 (CRD), MONOCLINIC CRYSTAL FORM 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: EMP47P (FORM2); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 7-227; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1 KEYWDS BETA SANDWICH, CARBOHYDRATE BINDING PROTEIN, CARGO RECEPTOR, KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, SUGAR BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.SATOH,K.SATO,A.KANOH,K.YAMASHITA,R.KATO,A.NAKANO, AUTHOR 2 S.WAKATSUKI REVDAT 3 24-FEB-09 2A6Z 1 VERSN REVDAT 2 23-MAY-06 2A6Z 1 JRNL REVDAT 1 31-JAN-06 2A6Z 0 JRNL AUTH T.SATOH,K.SATO,A.KANOH,K.YAMASHITA,Y.YAMADA, JRNL AUTH 2 N.IGARASHI,R.KATO,A.NAKANO,S.WAKATSUKI JRNL TITL STRUCTURES OF THE CARBOHYDRATE RECOGNITION DOMAIN JRNL TITL 2 OF CA2+-INDEPENDENT CARGO RECEPTORS EMP46P AND JRNL TITL 3 EMP47P. JRNL REF J.BIOL.CHEM. V. 281 10410 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16439369 JRNL DOI 10.1074/JBC.M512258200 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.130 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.130 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.163 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4953 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 94223 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.123 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.154 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 4491 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 85243 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1773 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 320 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2068.50 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 10 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 18836 REMARK 3 NUMBER OF RESTRAINTS : 22535 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.016 REMARK 3 ANGLE DISTANCES (A) : 0.032 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.031 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.092 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.112 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.030 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.045 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.090 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A6Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-05. REMARK 100 THE RCSB ID CODE IS RCSB033565. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JAN-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-6A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9779 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99298 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.04 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.24900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 2A6Y REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 36.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, AMMONIUM CHLORIDE, PH 6.3, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 36.26000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.49500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.26000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.49500 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 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 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 256 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 SER A 88 CB SER A 88 OG -0.080 REMARK 500 MET A 153 CG MET A 153 SD -0.173 REMARK 500 REMARK 500 REMARK: NULL 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 MET A 70 CA - CB - CG ANGL. DEV. = 10.6 DEGREES REMARK 500 ARG A 99 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES REMARK 500 ASP A 145 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 ASP A 181 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP A 181 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = -3.0 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 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 35 -130.00 59.09 REMARK 500 GLU A 41 100.00 -58.42 REMARK 500 TYR A 155 -23.12 -140.07 REMARK 500 ASN A 182 -1.31 76.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GV9 RELATED DB: PDB REMARK 900 RELATED ID: 1R1Z RELATED DB: PDB REMARK 900 RELATED ID: 2A6V RELATED DB: PDB REMARK 900 RELATED ID: 2A6W RELATED DB: PDB REMARK 900 RELATED ID: 2A6X RELATED DB: PDB REMARK 900 RELATED ID: 2A6Y RELATED DB: PDB REMARK 900 RELATED ID: 2A70 RELATED DB: PDB REMARK 900 RELATED ID: 2A71 RELATED DB: PDB DBREF 2A6Z A 7 227 GB 854516 CAA60953 35 255 SEQADV 2A6Z GLY A 6 GB 854516 CLONING ARTIFACT SEQRES 1 A 222 GLY SER ASP ALA SER LYS LEU SER SER ASP TYR SER LEU SEQRES 2 A 222 PRO ASP LEU ILE ASN THR ARG LYS VAL PRO ASN ASN TRP SEQRES 3 A 222 GLN THR GLY GLU GLN ALA SER LEU GLU GLU GLY ARG ILE SEQRES 4 A 222 VAL LEU THR SER ASN GLN ASN SER LYS GLY SER LEU TRP SEQRES 5 A 222 LEU LYS GLN GLY PHE ASP LEU LYS ASP SER PHE THR MET SEQRES 6 A 222 GLU TRP THR PHE ARG SER VAL GLY TYR SER GLY GLN THR SEQRES 7 A 222 ASP GLY GLY ILE SER PHE TRP PHE VAL GLN ASP SER ASN SEQRES 8 A 222 ILE PRO ARG ASP LYS GLN LEU TYR ASN GLY PRO VAL ASN SEQRES 9 A 222 TYR ASP GLY LEU GLN LEU LEU VAL ASP ASN ASN GLY PRO SEQRES 10 A 222 LEU GLY PRO THR LEU ARG GLY GLN LEU ASN ASP GLY GLN SEQRES 11 A 222 LYS PRO VAL ASP LYS THR LYS ILE TYR ASP GLN SER PHE SEQRES 12 A 222 ALA SER CYS LEU MET GLY TYR GLN ASP SER SER VAL PRO SEQRES 13 A 222 SER THR ILE ARG VAL THR TYR ASP LEU GLU ASP ASP ASN SEQRES 14 A 222 LEU LEU LYS VAL GLN VAL ASP ASN LYS VAL CYS PHE GLN SEQRES 15 A 222 THR ARG LYS VAL ARG PHE PRO SER GLY SER TYR ARG ILE SEQRES 16 A 222 GLY VAL THR ALA GLN ASN GLY ALA VAL ASN ASN ASN ALA SEQRES 17 A 222 GLU SER PHE GLU ILE PHE LYS MET GLN PHE PHE ASN GLY SEQRES 18 A 222 VAL FORMUL 2 HOH *320(H2 O) HELIX 1 1 SER A 14 SER A 17 5 4 HELIX 2 2 ILE A 143 SER A 147 1 5 SHEET 1 A 7 TRP A 31 GLU A 35 0 SHEET 2 A 7 LYS A 53 LEU A 58 -1 O TRP A 57 N GLN A 32 SHEET 3 A 7 TYR A 198 GLN A 205 -1 O ALA A 204 N GLY A 54 SHEET 4 A 7 GLY A 86 GLN A 93 -1 N VAL A 92 O ARG A 199 SHEET 5 A 7 ASP A 111 ASP A 118 -1 O ASP A 111 N GLN A 93 SHEET 6 A 7 THR A 126 ASP A 133 -1 O ARG A 128 N LEU A 116 SHEET 7 A 7 ALA A 149 LEU A 152 -1 O ALA A 149 N GLY A 129 SHEET 1 B 7 SER A 38 GLU A 40 0 SHEET 2 B 7 ARG A 43 VAL A 45 -1 O VAL A 45 N SER A 38 SHEET 3 B 7 SER A 215 ASN A 225 -1 O ILE A 218 N ILE A 44 SHEET 4 B 7 PHE A 68 VAL A 77 -1 N ARG A 75 O GLU A 217 SHEET 5 B 7 SER A 162 ASP A 169 -1 O SER A 162 N PHE A 74 SHEET 6 B 7 LEU A 175 VAL A 180 -1 O LYS A 177 N THR A 167 SHEET 7 B 7 LYS A 183 THR A 188 -1 O THR A 188 N LEU A 176 SSBOND 1 CYS A 151 CYS A 185 1555 1555 2.06 CRYST1 72.520 64.990 41.540 90.00 96.68 90.00 C 1 2 1 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 0.013789 0.000000 0.001615 0.00000 SCALE2 0.000000 0.015388 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024241 0.00000 ATOM 1 N GLY A 6 21.232 -3.592 -12.215 1.00 10.46 N ANISOU 1 N GLY A 6 1537 1300 1136 110 -528 -59 N ATOM 2 CA GLY A 6 21.163 -4.550 -11.066 1.00 10.57 C ANISOU 2 CA GLY A 6 1558 1396 1063 -267 -343 87 C ATOM 3 C GLY A 6 22.447 -4.422 -10.244 1.00 8.93 C ANISOU 3 C GLY A 6 1193 1290 908 -97 -117 152 C ATOM 4 O GLY A 6 23.428 -3.846 -10.715 1.00 10.86 O ANISOU 4 O GLY A 6 1267 1673 1187 -79 -127 346 O ATOM 5 N SER A 7 22.415 -4.967 -9.066 1.00 9.67 N ANISOU 5 N SER A 7 1214 1683 777 -108 -24 51 N ATOM 6 CA SER A 7 23.627 -4.941 -8.213 1.00 10.00 C ANISOU 6 CA SER A 7 1162 1784 855 89 -78 87 C ATOM 7 C SER A 7 24.675 -5.812 -8.871 1.00 10.25 C ANISOU 7 C SER A 7 1291 1335 1267 -74 124 173 C ATOM 8 O SER A 7 24.419 -6.879 -9.473 1.00 12.24 O ANISOU 8 O SER A 7 1537 1570 1544 -105 -41 -69 O ATOM 9 CB SER A 7 23.258 -5.436 -6.823 1.00 12.18 C ANISOU 9 CB SER A 7 1315 2247 1065 542 64 416 C ATOM 10 OG SER A 7 22.257 -4.593 -6.293 1.00 10.35 O ANISOU 10 OG SER A 7 1255 1773 905 185 -51 72 O ATOM 11 N ASP A 8 25.881 -5.358 -8.770 1.00 11.61 N ANISOU 11 N ASP A 8 1265 1390 1755 -100 153 -98 N ATOM 12 CA ASP A 8 27.024 -6.044 -9.280 1.00 13.40 C ANISOU 12 CA ASP A 8 1449 2018 1626 89 92 -586 C ATOM 13 C ASP A 8 28.220 -5.717 -8.375 1.00 12.32 C ANISOU 13 C ASP A 8 1305 2036 1340 108 166 -396 C ATOM 14 O ASP A 8 28.336 -4.566 -7.924 1.00 12.97 O ANISOU 14 O ASP A 8 1344 2067 1516 73 209 -477 O ATOM 15 CB ASP A 8 27.408 -5.638 -10.695 1.00 14.37 C ANISOU 15 CB ASP A 8 1563 2421 1477 258 -104 -435 C ATOM 16 CG ASP A 8 28.478 -6.598 -11.203 1.00 17.27 C ANISOU 16 CG ASP A 8 1645 2705 2212 106 333 -867 C ATOM 17 OD1 ASP A 8 29.641 -6.156 -11.414 1.00 23.41 O ANISOU 17 OD1 ASP A 8 1531 4798 2567 -266 202 -1419 O ATOM 18 OD2 ASP A 8 28.208 -7.794 -11.445 1.00 22.51 O ANISOU 18 OD2 ASP A 8 2336 2712 3503 575 -843 -1329 O ATOM 19 N ALA A 9 29.031 -6.730 -8.167 1.00 13.59 N ANISOU 19 N ALA A 9 1437 1859 1869 -67 159 -92 N ATOM 20 CA ALA A 9 30.227 -6.439 -7.324 1.00 15.62 C ANISOU 20 CA ALA A 9 1455 2132 2350 168 -164 109 C ATOM 21 C ALA A 9 31.025 -5.256 -7.798 1.00 13.61 C ANISOU 21 C ALA A 9 1404 2062 1706 8 -195 -346 C ATOM 22 O ALA A 9 31.635 -4.569 -6.963 1.00 16.39 O ANISOU 22 O ALA A 9 1764 2557 1906 55 -289 -710 O ATOM 23 CB ALA A 9 31.026 -7.718 -7.294 1.00 18.89 C ANISOU 23 CB ALA A 9 1650 2050 3478 243 -177 -288 C ATOM 24 N SER A 10 31.034 -4.982 -9.104 1.00 15.10 N ANISOU 24 N SER A 10 1415 2709 1615 -172 210 -494 N ATOM 25 CA SER A 10 31.890 -3.893 -9.611 1.00 15.04 C ANISOU 25 CA SER A 10 1307 2885 1524 -212 339 -653 C ATOM 26 C SER A 10 31.385 -2.515 -9.172 1.00 14.46 C ANISOU 26 C SER A 10 1149 2732 1614 -257 177 -395 C ATOM 27 O SER A 10 32.100 -1.522 -9.297 1.00 17.77 O ANISOU 27 O SER A 10 1631 2977 2142 -559 639 -591 O ATOM 28 CB SER A 10 32.013 -4.074 -11.124 1.00 19.07 C ANISOU 28 CB SER A 10 1584 4047 1614 -412 656 -762 C ATOM 29 OG SER A 10 30.752 -3.722 -11.722 1.00 24.02 O ANISOU 29 OG SER A 10 2000 5621 1504 -364 143 -713 O ATOM 30 N LYS A 11 30.139 -2.446 -8.720 1.00 13.04 N ANISOU 30 N LYS A 11 1235 2664 1057 -140 190 -373 N ATOM 31 CA LYS A 11 29.538 -1.174 -8.303 1.00 12.48 C ANISOU 31 CA LYS A 11 1281 2438 1024 -132 126 -17 C ATOM 32 C LYS A 11 29.425 -1.005 -6.788 1.00 10.58 C ANISOU 32 C LYS A 11 1024 1909 1085 23 242 146 C ATOM 33 O LYS A 11 28.931 -0.021 -6.261 1.00 12.05 O ANISOU 33 O LYS A 11 1143 2120 1314 290 351 86 O ATOM 34 CB LYS A 11 28.126 -1.042 -8.940 1.00 15.63 C ANISOU 34 CB LYS A 11 1402 3489 1047 216 125 381 C ATOM 35 CG LYS A 11 28.185 -0.984 -10.484 1.00 18.17 C ANISOU 35 CG LYS A 11 1734 4207 962 -42 -53 248 C ATOM 36 CD LYS A 11 26.865 -0.656 -11.124 1.00 24.75 C ANISOU 36 CD LYS A 11 1510 6598 1295 -349 -337 -154 C ATOM 37 CE LYS A 11 25.841 -1.770 -11.093 1.00 25.69 C ANISOU 37 CE LYS A 11 1481 5458 2822 329 -332 -760 C ATOM 38 NZ LYS A 11 24.488 -1.316 -11.576 1.00 13.08 N ANISOU 38 NZ LYS A 11 1487 2207 1276 -271 -28 -187 N ATOM 39 N LEU A 12 29.914 -2.013 -6.061 1.00 10.14 N ANISOU 39 N LEU A 12 1105 1750 996 2 92 -94 N ATOM 40 CA LEU A 12 29.859 -1.993 -4.620 1.00 9.72 C ANISOU 40 CA LEU A 12 1211 1539 944 -79 134 -136 C ATOM 41 C LEU A 12 30.718 -0.881 -4.067 1.00 10.89 C ANISOU 41 C LEU A 12 800 2155 1183 -113 250 -455 C ATOM 42 O LEU A 12 31.844 -0.659 -4.542 1.00 13.83 O ANISOU 42 O LEU A 12 893 2863 1501 -416 386 -841 O ATOM 43 CB LEU A 12 30.367 -3.334 -4.113 1.00 11.41 C ANISOU 43 CB LEU A 12 1146 2008 1179 403 66 22 C ATOM 44 CG LEU A 12 30.304 -3.597 -2.598 1.00 13.45 C ANISOU 44 CG LEU A 12 1547 2320 1242 96 -83 335 C ATOM 45 CD1 LEU A 12 28.880 -3.792 -2.125 1.00 12.98 C ANISOU 45 CD1 LEU A 12 1747 1898 1287 298 337 41 C ATOM 46 CD2 LEU A 12 31.136 -4.832 -2.229 1.00 18.77 C ANISOU 46 CD2 LEU A 12 1860 3232 2039 699 390 1154 C ATOM 47 N SER A 13 30.182 -0.172 -3.078 1.00 10.18 N ANISOU 47 N SER A 13 995 1784 1090 -145 287 -312 N ATOM 48 CA SER A 13 30.911 0.854 -2.372 1.00 10.88 C ANISOU 48 CA SER A 13 1034 1897 1202 -145 246 -397 C ATOM 49 C SER A 13 31.312 0.336 -1.016 1.00 10.84 C ANISOU 49 C SER A 13 1054 1925 1139 -341 351 -377 C ATOM 50 O SER A 13 30.470 0.324 -0.091 1.00 13.22 O ANISOU 50 O SER A 13 943 2940 1140 -602 240 -432 O ATOM 51 CB SER A 13 30.043 2.112 -2.181 1.00 14.48 C ANISOU 51 CB SER A 13 1359 1925 2217 112 499 -485 C ATOM 52 OG SER A 13 30.741 2.970 -1.284 1.00 21.60 O ANISOU 52 OG SER A 13 1732 2198 4278 -192 478 -1460 O ATOM 53 N SER A 14 32.563 -0.073 -0.874 1.00 10.76 N ANISOU 53 N SER A 14 1245 1650 1193 -98 382 -246 N ATOM 54 CA SER A 14 32.999 -0.637 0.403 1.00 12.53 C ANISOU 54 CA SER A 14 1827 1632 1300 240 429 -260 C ATOM 55 C SER A 14 32.850 0.365 1.508 1.00 10.01 C ANISOU 55 C SER A 14 903 1675 1226 23 232 -258 C ATOM 56 O SER A 14 32.557 -0.051 2.642 1.00 11.07 O ANISOU 56 O SER A 14 1113 1868 1227 341 109 -106 O ATOM 57 CB SER A 14 34.464 -1.021 0.148 1.00 19.20 C ANISOU 57 CB SER A 14 2390 2926 1981 1540 381 -377 C ATOM 58 OG SER A 14 35.012 -1.352 1.381 1.00 28.14 O ANISOU 58 OG SER A 14 2895 4759 3039 1163 -182 985 O ATOM 59 N ASP A 15 33.086 1.635 1.232 1.00 9.88 N ANISOU 59 N ASP A 15 784 1645 1325 129 124 -366 N ATOM 60 CA ASP A 15 33.067 2.634 2.275 1.00 9.05 C ANISOU 60 CA ASP A 15 633 1636 1168 -69 20 -301 C ATOM 61 C ASP A 15 31.737 2.736 2.977 1.00 8.28 C ANISOU 61 C ASP A 15 712 1589 847 -133 17 -148 C ATOM 62 O ASP A 15 31.671 3.132 4.174 1.00 9.25 O ANISOU 62 O ASP A 15 609 1883 1021 -12 -68 -247 O ATOM 63 CB ASP A 15 33.391 4.036 1.693 1.00 10.56 C ANISOU 63 CB ASP A 15 1002 1663 1349 -215 461 -334 C ATOM 64 CG ASP A 15 34.851 4.093 1.233 1.00 11.02 C ANISOU 64 CG ASP A 15 1004 1752 1430 -12 390 -137 C ATOM 65 OD1 ASP A 15 35.688 3.253 1.607 1.00 13.02 O ANISOU 65 OD1 ASP A 15 866 2304 1779 -28 156 266 O ATOM 66 OD2 ASP A 15 35.093 5.024 0.477 1.00 14.72 O ANISOU 66 OD2 ASP A 15 1560 1947 2088 128 952 254 O ATOM 67 N TYR A 16 30.636 2.389 2.277 1.00 8.13 N ANISOU 67 N TYR A 16 571 1587 929 49 19 -95 N ATOM 68 CA TYR A 16 29.280 2.525 2.841 1.00 7.50 C ANISOU 68 CA TYR A 16 618 1290 943 43 24 -44 C ATOM 69 C TYR A 16 28.619 1.190 3.060 1.00 7.07 C ANISOU 69 C TYR A 16 617 1301 767 79 61 -104 C ATOM 70 O TYR A 16 27.401 1.124 3.221 1.00 8.00 O ANISOU 70 O TYR A 16 664 1258 1118 40 149 -174 O ATOM 71 CB TYR A 16 28.454 3.471 1.950 1.00 8.20 C ANISOU 71 CB TYR A 16 763 1318 1035 60 -13 6 C ATOM 72 CG TYR A 16 29.023 4.862 1.958 1.00 8.09 C ANISOU 72 CG TYR A 16 797 1308 967 45 -41 87 C ATOM 73 CD1 TYR A 16 28.921 5.702 3.031 1.00 10.30 C ANISOU 73 CD1 TYR A 16 1373 1307 1232 -165 4 -17 C ATOM 74 CD2 TYR A 16 29.785 5.327 0.895 1.00 12.14 C ANISOU 74 CD2 TYR A 16 1752 1353 1508 -76 523 92 C ATOM 75 CE1 TYR A 16 29.447 6.948 3.074 1.00 11.28 C ANISOU 75 CE1 TYR A 16 1561 1277 1447 -197 50 28 C ATOM 76 CE2 TYR A 16 30.336 6.613 0.909 1.00 14.23 C ANISOU 76 CE2 TYR A 16 1964 1253 2188 -25 1028 -41 C ATOM 77 CZ TYR A 16 30.160 7.426 1.989 1.00 10.62 C ANISOU 77 CZ TYR A 16 885 1571 1580 -228 28 -46 C ATOM 78 OH TYR A 16 30.726 8.690 2.039 1.00 13.21 O ANISOU 78 OH TYR A 16 1128 1553 2337 -449 178 28 O ATOM 79 N SER A 17 29.380 0.098 3.057 1.00 7.89 N ANISOU 79 N SER A 17 669 1324 1006 34 11 -53 N ATOM 80 CA SER A 17 28.892 -1.240 3.222 1.00 7.35 C ANISOU 80 CA SER A 17 664 1285 843 215 -7 3 C ATOM 81 C SER A 17 29.311 -1.839 4.561 1.00 7.35 C ANISOU 81 C SER A 17 693 1319 781 28 -75 -36 C ATOM 82 O SER A 17 30.260 -1.407 5.196 1.00 8.39 O ANISOU 82 O SER A 17 689 1580 919 -25 -79 -161 O ATOM 83 CB SER A 17 29.303 -2.179 2.072 1.00 8.27 C ANISOU 83 CB SER A 17 720 1600 823 236 -58 -119 C ATOM 84 OG SER A 17 28.793 -1.705 0.842 1.00 8.29 O ANISOU 84 OG SER A 17 646 1696 808 82 4 -59 O ATOM 85 N LEU A 18 28.559 -2.857 4.953 1.00 7.83 N ANISOU 85 N LEU A 18 784 1306 884 16 -155 -6 N ATOM 86 CA LEU A 18 28.764 -3.676 6.143 1.00 8.53 C ANISOU 86 CA LEU A 18 972 1302 967 10 19 70 C ATOM 87 C LEU A 18 28.926 -5.104 5.640 1.00 8.19 C ANISOU 87 C LEU A 18 695 1359 1056 149 -202 104 C ATOM 88 O LEU A 18 27.913 -5.837 5.427 1.00 9.06 O ANISOU 88 O LEU A 18 787 1397 1258 63 -182 -66 O ATOM 89 CB LEU A 18 27.562 -3.575 7.082 1.00 8.57 C ANISOU 89 CB LEU A 18 761 1537 958 86 -127 -3 C ATOM 90 CG LEU A 18 27.680 -4.357 8.370 1.00 9.67 C ANISOU 90 CG LEU A 18 1257 1605 810 28 -9 -105 C ATOM 91 CD1 LEU A 18 28.656 -3.726 9.322 1.00 14.14 C ANISOU 91 CD1 LEU A 18 2099 2057 1216 -227 -752 194 C ATOM 92 CD2 LEU A 18 26.257 -4.465 8.970 1.00 16.03 C ANISOU 92 CD2 LEU A 18 1372 3344 1374 195 292 415 C ATOM 93 N PRO A 19 30.127 -5.569 5.353 1.00 9.49 N ANISOU 93 N PRO A 19 719 1394 1493 77 -135 23 N ATOM 94 CA PRO A 19 30.325 -6.920 4.831 1.00 9.65 C ANISOU 94 CA PRO A 19 885 1441 1338 209 172 118 C ATOM 95 C PRO A 19 29.712 -7.950 5.790 1.00 9.09 C ANISOU 95 C PRO A 19 786 1324 1345 291 -87 107 C ATOM 96 O PRO A 19 29.666 -7.739 6.999 1.00 10.53 O ANISOU 96 O PRO A 19 1003 1785 1214 243 -130 272 O ATOM 97 CB PRO A 19 31.847 -7.051 4.822 1.00 12.21 C ANISOU 97 CB PRO A 19 854 1700 2084 221 78 231 C ATOM 98 CG PRO A 19 32.377 -5.652 4.673 1.00 15.00 C ANISOU 98 CG PRO A 19 991 1727 2980 170 469 147 C ATOM 99 CD PRO A 19 31.413 -4.822 5.538 1.00 11.67 C ANISOU 99 CD PRO A 19 646 1693 2094 -2 -30 126 C ATOM 100 N ASP A 20 29.277 -9.047 5.142 1.00 9.15 N ANISOU 100 N ASP A 20 745 1393 1338 207 -66 201 N ATOM 101 CA ASP A 20 28.634 -10.151 5.849 1.00 9.73 C ANISOU 101 CA ASP A 20 1072 1391 1233 236 -62 211 C ATOM 102 C ASP A 20 29.348 -10.447 7.142 1.00 10.04 C ANISOU 102 C ASP A 20 1007 1571 1238 495 -44 205 C ATOM 103 O ASP A 20 30.578 -10.676 7.163 1.00 10.69 O ANISOU 103 O ASP A 20 946 1632 1484 427 -84 275 O ATOM 104 CB ASP A 20 28.642 -11.374 4.964 1.00 10.68 C ANISOU 104 CB ASP A 20 1392 1417 1249 170 -5 162 C ATOM 105 CG ASP A 20 27.818 -12.515 5.493 1.00 13.37 C ANISOU 105 CG ASP A 20 2045 1620 1415 -234 -420 446 C ATOM 106 OD1 ASP A 20 27.594 -13.405 4.665 1.00 27.03 O ANISOU 106 OD1 ASP A 20 4940 3435 1896 -2569 161 -367 O ATOM 107 OD2 ASP A 20 27.503 -12.621 6.679 1.00 12.48 O ANISOU 107 OD2 ASP A 20 1639 1498 1605 194 23 429 O ATOM 108 N LEU A 21 28.634 -10.378 8.271 1.00 10.23 N ANISOU 108 N LEU A 21 953 1705 1229 334 -52 191 N ATOM 109 CA LEU A 21 29.209 -10.467 9.612 1.00 10.20 C ANISOU 109 CA LEU A 21 1204 1450 1221 402 -104 195 C ATOM 110 C LEU A 21 29.478 -11.900 10.043 1.00 11.28 C ANISOU 110 C LEU A 21 1227 1464 1594 245 -128 336 C ATOM 111 O LEU A 21 29.940 -12.096 11.194 1.00 12.53 O ANISOU 111 O LEU A 21 1431 1540 1790 390 -523 347 O ATOM 112 CB LEU A 21 28.275 -9.746 10.615 1.00 10.45 C ANISOU 112 CB LEU A 21 1276 1432 1262 76 21 97 C ATOM 113 CG LEU A 21 28.118 -8.232 10.398 1.00 9.77 C ANISOU 113 CG LEU A 21 1168 1387 1156 322 -216 32 C ATOM 114 CD1 LEU A 21 26.911 -7.805 11.180 1.00 12.75 C ANISOU 114 CD1 LEU A 21 1391 2094 1360 511 5 49 C ATOM 115 CD2 LEU A 21 29.411 -7.552 10.829 1.00 13.23 C ANISOU 115 CD2 LEU A 21 1453 1614 1961 -95 -402 353 C ATOM 116 N ILE A 22 29.232 -12.871 9.228 1.00 11.44 N ANISOU 116 N ILE A 22 1220 1455 1673 255 -170 290 N ATOM 117 CA ILE A 22 29.266 -14.279 9.636 1.00 14.46 C ANISOU 117 CA ILE A 22 1576 1519 2399 145 -462 396 C ATOM 118 C ILE A 22 30.497 -14.691 10.412 1.00 16.54 C ANISOU 118 C ILE A 22 1900 1604 2781 351 -679 612 C ATOM 119 O ILE A 22 30.464 -15.407 11.408 1.00 19.74 O ANISOU 119 O ILE A 22 3090 1848 2563 383 -880 569 O ATOM 120 CB ILE A 22 29.020 -15.196 8.413 1.00 15.33 C ANISOU 120 CB ILE A 22 1801 1359 2666 29 -288 207 C ATOM 121 CG1 ILE A 22 28.790 -16.653 8.867 1.00 20.42 C ANISOU 121 CG1 ILE A 22 3234 1621 2904 -262 -957 691 C ATOM 122 CG2 ILE A 22 30.083 -15.063 7.336 1.00 16.04 C ANISOU 122 CG2 ILE A 22 1585 1584 2925 39 -219 -174 C ATOM 123 CD1 ILE A 22 28.222 -17.508 7.794 1.00 21.43 C ANISOU 123 CD1 ILE A 22 2864 1532 3747 -160 240 -528 C ATOM 124 N ASN A 23 31.653 -14.183 10.023 1.00 18.18 N ANISOU 124 N ASN A 23 1567 2304 3038 393 -581 76 N ATOM 125 CA ASN A 23 32.854 -14.632 10.793 1.00 19.22 C ANISOU 125 CA ASN A 23 1938 2511 2854 955 -831 -657 C ATOM 126 C ASN A 23 33.530 -13.415 11.340 1.00 16.22 C ANISOU 126 C ASN A 23 1636 2165 2362 574 -596 234 C ATOM 127 O ASN A 23 34.735 -13.426 11.622 1.00 23.30 O ANISOU 127 O ASN A 23 1584 3010 4259 693 -914 14 O ATOM 128 CB ASN A 23 33.701 -15.466 9.830 1.00 31.12 C ANISOU 128 CB ASN A 23 3980 4710 3133 3074 -1639 -1610 C ATOM 129 CG ASN A 23 33.187 -16.884 9.649 1.00 37.92 C ANISOU 129 CG ASN A 23 4935 4617 4856 3387 -2012 -2697 C ATOM 130 OD1 ASN A 23 32.723 -17.574 10.562 1.00 38.14 O ANISOU 130 OD1 ASN A 23 3791 4851 5849 1602 -2920 -2432 O ATOM 131 ND2 ASN A 23 33.258 -17.393 8.419 1.00 52.99 N ANISOU 131 ND2 ASN A 23 7757 6449 5928 3824 -1421 -4235 N ATOM 132 N THR A 24 32.829 -12.306 11.516 1.00 14.63 N ANISOU 132 N THR A 24 1272 2294 1995 399 -288 -160 N ATOM 133 CA THR A 24 33.439 -11.062 11.948 1.00 15.01 C ANISOU 133 CA THR A 24 1670 2207 1827 269 -465 150 C ATOM 134 C THR A 24 33.497 -10.937 13.433 1.00 15.30 C ANISOU 134 C THR A 24 1521 2430 1861 526 -655 26 C ATOM 135 O THR A 24 32.528 -11.199 14.160 1.00 19.27 O ANISOU 135 O THR A 24 1912 3532 1879 198 -356 -38 O ATOM 136 CB THR A 24 32.585 -9.918 11.361 1.00 14.41 C ANISOU 136 CB THR A 24 1191 2338 1948 27 -518 393 C ATOM 137 OG1 THR A 24 32.666 -10.050 9.912 1.00 19.23 O ANISOU 137 OG1 THR A 24 1835 3549 1923 353 -458 531 O ATOM 138 CG2 THR A 24 33.084 -8.582 11.810 1.00 16.63 C ANISOU 138 CG2 THR A 24 1480 2175 2663 -159 -782 781 C ATOM 139 N ARG A 25 34.705 -10.520 13.893 1.00 18.14 N ANISOU 139 N ARG A 25 1892 2702 2300 121 -1014 493 N ATOM 140 CA ARG A 25 34.953 -10.536 15.352 1.00 21.51 C ANISOU 140 CA ARG A 25 3169 2401 2602 29 -1862 357 C ATOM 141 C ARG A 25 34.807 -9.161 15.963 1.00 17.75 C ANISOU 141 C ARG A 25 2278 2410 2058 51 -500 662 C ATOM 142 O ARG A 25 34.737 -9.082 17.201 1.00 21.72 O ANISOU 142 O ARG A 25 2978 3241 2035 767 -742 634 O ATOM 143 CB ARG A 25 36.354 -11.157 15.592 1.00 30.67 C ANISOU 143 CB ARG A 25 4745 2757 4150 1602 -2969 -99 C ATOM 144 CG ARG A 25 36.501 -12.577 15.004 1.00 34.57 C ANISOU 144 CG ARG A 25 5516 2862 4757 1357 -3608 -506 C ATOM 145 CD ARG A 25 37.820 -13.241 15.365 1.00 42.18 C ANISOU 145 CD ARG A 25 5684 3238 7106 2159 -3087 -868 C ATOM 146 NE ARG A 25 38.421 -14.063 14.317 1.00 44.00 N ANISOU 146 NE ARG A 25 6228 3392 7098 1441 -2010 -632 N ATOM 147 CZ ARG A 25 39.432 -14.909 14.450 1.00 38.09 C ANISOU 147 CZ ARG A 25 6061 2308 6103 930 -2105 -1231 C ATOM 148 NH1 ARG A 25 40.019 -15.110 15.614 1.00 51.58 N ANISOU 148 NH1 ARG A 25 7322 4483 7793 1015 -4426 -1870 N ATOM 149 NH2 ARG A 25 39.888 -15.593 13.404 1.00 47.07 N ANISOU 149 NH2 ARG A 25 6919 3524 7442 63 -363 -1971 N ATOM 150 N LYS A 26 34.846 -8.092 15.197 1.00 16.58 N ANISOU 150 N LYS A 26 1679 2377 2246 271 -1007 627 N ATOM 151 CA LYS A 26 34.729 -6.738 15.723 1.00 17.57 C ANISOU 151 CA LYS A 26 2175 2419 2080 402 -872 600 C ATOM 152 C LYS A 26 33.857 -5.947 14.732 1.00 14.93 C ANISOU 152 C LYS A 26 1795 2331 1547 438 -573 343 C ATOM 153 O LYS A 26 33.939 -6.142 13.518 1.00 15.55 O ANISOU 153 O LYS A 26 2066 2186 1658 784 -264 420 O ATOM 154 CB LYS A 26 36.085 -6.074 15.821 1.00 22.72 C ANISOU 154 CB LYS A 26 2300 2310 4021 468 -1691 192 C ATOM 155 CG LYS A 26 36.317 -4.998 16.883 1.00 34.77 C ANISOU 155 CG LYS A 26 3737 4435 5039 -698 -797 -1383 C ATOM 156 CD LYS A 26 35.229 -3.942 16.957 1.00 46.02 C ANISOU 156 CD LYS A 26 5898 5400 6186 752 125 -2815 C ATOM 157 CE LYS A 26 34.451 -3.911 18.263 1.00 51.46 C ANISOU 157 CE LYS A 26 6235 7738 5579 1452 -289 -2152 C ATOM 158 NZ LYS A 26 33.147 -4.650 18.261 1.00 40.12 N ANISOU 158 NZ LYS A 26 4556 8341 2347 2766 -1607 -394 N ATOM 159 N VAL A 27 33.036 -5.027 15.233 1.00 14.45 N ANISOU 159 N VAL A 27 1786 2204 1502 315 -484 289 N ATOM 160 CA VAL A 27 32.293 -4.192 14.300 1.00 15.09 C ANISOU 160 CA VAL A 27 2115 2479 1139 737 -375 121 C ATOM 161 C VAL A 27 33.227 -3.448 13.343 1.00 14.85 C ANISOU 161 C VAL A 27 2237 2185 1220 543 -395 114 C ATOM 162 O VAL A 27 34.195 -2.851 13.773 1.00 16.61 O ANISOU 162 O VAL A 27 2563 2131 1619 419 -627 46 O ATOM 163 CB VAL A 27 31.473 -3.146 15.087 1.00 14.31 C ANISOU 163 CB VAL A 27 2181 1921 1336 385 -263 128 C ATOM 164 CG1 VAL A 27 30.740 -2.232 14.108 1.00 16.79 C ANISOU 164 CG1 VAL A 27 1980 2379 2021 545 -413 362 C ATOM 165 CG2 VAL A 27 30.545 -3.850 16.042 1.00 16.45 C ANISOU 165 CG2 VAL A 27 1884 2445 1920 297 2 215 C ATOM 166 N PRO A 28 32.994 -3.531 12.035 1.00 14.84 N ANISOU 166 N PRO A 28 2304 2073 1260 811 -417 184 N ATOM 167 CA PRO A 28 33.824 -2.791 11.092 1.00 16.50 C ANISOU 167 CA PRO A 28 2882 2239 1148 944 -30 69 C ATOM 168 C PRO A 28 33.966 -1.324 11.424 1.00 15.12 C ANISOU 168 C PRO A 28 2255 2238 1253 836 104 242 C ATOM 169 O PRO A 28 32.996 -0.687 11.826 1.00 15.36 O ANISOU 169 O PRO A 28 2108 2210 1519 864 21 121 O ATOM 170 CB PRO A 28 33.012 -2.940 9.774 1.00 20.66 C ANISOU 170 CB PRO A 28 4101 2520 1228 1075 -515 76 C ATOM 171 CG PRO A 28 32.487 -4.341 9.954 1.00 19.77 C ANISOU 171 CG PRO A 28 3370 2705 1438 941 -620 -151 C ATOM 172 CD PRO A 28 31.991 -4.351 11.387 1.00 17.72 C ANISOU 172 CD PRO A 28 2572 2682 1478 744 -625 -233 C ATOM 173 N ASN A 29 35.179 -0.828 11.170 1.00 15.81 N ANISOU 173 N ASN A 29 1879 2597 1533 963 -277 21 N ATOM 174 CA ASN A 29 35.572 0.489 11.633 1.00 17.32 C ANISOU 174 CA ASN A 29 1689 2810 2080 897 -734 -154 C ATOM 175 C ASN A 29 34.804 1.626 10.997 1.00 11.96 C ANISOU 175 C ASN A 29 885 2248 1411 90 -278 -30 C ATOM 176 O ASN A 29 34.822 2.715 11.525 1.00 13.17 O ANISOU 176 O ASN A 29 991 2322 1690 46 -423 -176 O ATOM 177 CB ASN A 29 37.091 0.663 11.392 1.00 30.29 C ANISOU 177 CB ASN A 29 1322 4549 5638 650 -1487 314 C ATOM 178 CG ASN A 29 37.474 2.064 10.961 1.00 42.00 C ANISOU 178 CG ASN A 29 2663 5195 8102 -602 -101 430 C ATOM 179 OD1 ASN A 29 37.900 2.887 11.799 1.00 58.01 O ANISOU 179 OD1 ASN A 29 3859 5449 12734 -380 -1606 -1548 O ATOM 180 ND2 ASN A 29 37.368 2.396 9.667 1.00 55.94 N ANISOU 180 ND2 ASN A 29 4921 7084 9249 524 534 3076 N ATOM 181 N ASN A 30 34.100 1.375 9.871 1.00 10.64 N ANISOU 181 N ASN A 30 857 1931 1255 102 -140 -20 N ATOM 182 CA ASN A 30 33.308 2.425 9.254 1.00 10.04 C ANISOU 182 CA ASN A 30 754 1904 1157 85 -18 -125 C ATOM 183 C ASN A 30 31.887 2.534 9.856 1.00 8.74 C ANISOU 183 C ASN A 30 768 1561 990 13 -21 -109 C ATOM 184 O ASN A 30 31.156 3.429 9.421 1.00 9.20 O ANISOU 184 O ASN A 30 768 1590 1139 -18 -63 25 O ATOM 185 CB ASN A 30 33.245 2.218 7.737 1.00 9.74 C ANISOU 185 CB ASN A 30 743 1877 1080 -50 -52 0 C ATOM 186 CG ASN A 30 32.723 0.902 7.214 1.00 9.59 C ANISOU 186 CG ASN A 30 759 1844 1041 -97 -16 22 C ATOM 187 OD1 ASN A 30 32.944 -0.173 7.838 1.00 10.60 O ANISOU 187 OD1 ASN A 30 1007 1881 1142 215 -70 -62 O ATOM 188 ND2 ASN A 30 32.030 0.951 6.073 1.00 9.96 N ANISOU 188 ND2 ASN A 30 813 1944 1029 17 -84 -9 N ATOM 189 N TRP A 31 31.572 1.714 10.831 1.00 8.76 N ANISOU 189 N TRP A 31 733 1714 880 89 -168 -20 N ATOM 190 CA TRP A 31 30.251 1.722 11.486 1.00 8.42 C ANISOU 190 CA TRP A 31 718 1568 914 -15 -154 -40 C ATOM 191 C TRP A 31 30.389 1.961 12.965 1.00 9.41 C ANISOU 191 C TRP A 31 794 1901 880 -30 -185 -149 C ATOM 192 O TRP A 31 31.419 1.638 13.610 1.00 11.66 O ANISOU 192 O TRP A 31 877 2493 1062 61 -326 -96 O ATOM 193 CB TRP A 31 29.550 0.355 11.320 1.00 9.58 C ANISOU 193 CB TRP A 31 1174 1585 881 -134 -239 -14 C ATOM 194 CG TRP A 31 29.124 0.116 9.896 1.00 8.79 C ANISOU 194 CG TRP A 31 974 1543 822 -60 -194 -62 C ATOM 195 CD1 TRP A 31 29.914 -0.362 8.878 1.00 8.82 C ANISOU 195 CD1 TRP A 31 854 1557 940 -26 -131 -68 C ATOM 196 CD2 TRP A 31 27.832 0.347 9.308 1.00 7.85 C ANISOU 196 CD2 TRP A 31 868 1314 799 -103 -85 -62 C ATOM 197 NE1 TRP A 31 29.196 -0.443 7.696 1.00 8.51 N ANISOU 197 NE1 TRP A 31 785 1544 906 22 -77 -69 N ATOM 198 CE2 TRP A 31 27.903 -0.015 7.935 1.00 8.18 C ANISOU 198 CE2 TRP A 31 791 1494 822 -41 -111 -112 C ATOM 199 CE3 TRP A 31 26.631 0.818 9.810 1.00 8.07 C ANISOU 199 CE3 TRP A 31 914 1308 845 -94 -61 -35 C ATOM 200 CZ2 TRP A 31 26.808 0.087 7.090 1.00 8.33 C ANISOU 200 CZ2 TRP A 31 775 1448 941 72 -98 -99 C ATOM 201 CZ3 TRP A 31 25.526 0.922 8.974 1.00 8.12 C ANISOU 201 CZ3 TRP A 31 979 1287 820 99 -24 -24 C ATOM 202 CH2 TRP A 31 25.617 0.566 7.616 1.00 8.57 C ANISOU 202 CH2 TRP A 31 826 1594 837 -89 2 -136 C ATOM 203 N GLN A 32 29.297 2.496 13.567 1.00 9.47 N ANISOU 203 N GLN A 32 872 1897 829 -155 -59 -73 N ATOM 204 CA GLN A 32 29.256 2.748 15.001 1.00 11.23 C ANISOU 204 CA GLN A 32 1103 2327 836 -370 -71 -230 C ATOM 205 C GLN A 32 27.963 2.165 15.568 1.00 9.58 C ANISOU 205 C GLN A 32 867 1974 799 -95 -190 -212 C ATOM 206 O GLN A 32 26.862 2.515 15.139 1.00 10.71 O ANISOU 206 O GLN A 32 970 2252 846 -91 -222 -40 O ATOM 207 CB GLN A 32 29.330 4.272 15.242 1.00 13.16 C ANISOU 207 CB GLN A 32 1563 2396 1040 -645 147 -425 C ATOM 208 CG GLN A 32 29.283 4.625 16.767 1.00 15.67 C ANISOU 208 CG GLN A 32 2268 2760 927 -772 -14 -469 C ATOM 209 CD GLN A 32 30.498 4.082 17.445 1.00 18.32 C ANISOU 209 CD GLN A 32 1889 3861 1212 -884 -74 -642 C ATOM 210 OE1 GLN A 32 31.599 4.453 17.056 1.00 25.57 O ANISOU 210 OE1 GLN A 32 2173 5668 1876 -1844 -222 -307 O ATOM 211 NE2 GLN A 32 30.269 3.215 18.428 1.00 16.54 N ANISOU 211 NE2 GLN A 32 1273 3099 1911 -189 -138 -422 N ATOM 212 N THR A 33 28.066 1.290 16.555 1.00 10.26 N ANISOU 212 N THR A 33 943 2244 711 -209 -141 -161 N ATOM 213 CA THR A 33 26.925 0.835 17.328 1.00 10.25 C ANISOU 213 CA THR A 33 938 2201 755 7 -109 -61 C ATOM 214 C THR A 33 26.566 1.856 18.382 1.00 10.43 C ANISOU 214 C THR A 33 838 2192 932 -29 -159 -183 C ATOM 215 O THR A 33 27.420 2.625 18.865 1.00 12.54 O ANISOU 215 O THR A 33 922 2914 927 -275 -139 -429 O ATOM 216 CB THR A 33 27.178 -0.519 17.996 1.00 11.09 C ANISOU 216 CB THR A 33 1247 2059 906 -51 -354 -74 C ATOM 217 OG1 THR A 33 28.430 -0.447 18.745 1.00 13.87 O ANISOU 217 OG1 THR A 33 1147 2865 1259 59 -387 211 O ATOM 218 CG2 THR A 33 27.313 -1.674 17.029 1.00 13.97 C ANISOU 218 CG2 THR A 33 1917 2225 1165 116 204 -279 C ATOM 219 N GLY A 34 25.291 1.846 18.780 1.00 10.14 N ANISOU 219 N GLY A 34 946 2034 872 -167 -62 -228 N ATOM 220 CA GLY A 34 24.826 2.733 19.833 1.00 12.03 C ANISOU 220 CA GLY A 34 998 2625 949 -201 14 -479 C ATOM 221 C GLY A 34 23.851 1.983 20.728 1.00 10.52 C ANISOU 221 C GLY A 34 1024 2227 745 59 -254 -218 C ATOM 222 O GLY A 34 23.261 0.955 20.365 1.00 10.79 O ANISOU 222 O GLY A 34 1045 2224 832 67 -92 -156 O ATOM 223 N GLU A 35 23.632 2.586 21.874 1.00 12.02 N ANISOU 223 N GLU A 35 1179 2673 716 50 -158 -295 N ATOM 224 CA GLU A 35 22.663 2.101 22.842 1.00 11.26 C ANISOU 224 CA GLU A 35 1149 2261 867 -27 -190 -349 C ATOM 225 C GLU A 35 23.132 0.692 23.178 1.00 10.97 C ANISOU 225 C GLU A 35 1000 2443 725 213 -130 -279 C ATOM 226 O GLU A 35 24.343 0.575 23.472 1.00 12.90 O ANISOU 226 O GLU A 35 1111 2914 875 183 -197 -197 O ATOM 227 CB GLU A 35 21.177 2.284 22.511 1.00 10.66 C ANISOU 227 CB GLU A 35 1137 2173 742 147 -230 -237 C ATOM 228 CG GLU A 35 20.820 3.733 22.313 1.00 11.98 C ANISOU 228 CG GLU A 35 1566 2206 781 325 -23 -357 C ATOM 229 CD GLU A 35 21.413 4.331 21.030 1.00 11.30 C ANISOU 229 CD GLU A 35 1282 2055 958 297 107 -357 C ATOM 230 OE1 GLU A 35 21.255 3.613 20.021 1.00 12.76 O ANISOU 230 OE1 GLU A 35 1226 2907 716 153 -69 -481 O ATOM 231 OE2 GLU A 35 21.952 5.438 21.103 1.00 13.43 O ANISOU 231 OE2 GLU A 35 1370 2597 1136 -106 -165 -290 O ATOM 232 N GLN A 36 22.290 -0.311 23.138 1.00 11.07 N ANISOU 232 N GLN A 36 1187 2314 706 189 -90 29 N ATOM 233 CA GLN A 36 22.673 -1.645 23.506 1.00 12.14 C ANISOU 233 CA GLN A 36 1337 2402 873 411 152 54 C ATOM 234 C GLN A 36 22.869 -2.562 22.319 1.00 11.33 C ANISOU 234 C GLN A 36 1279 2129 896 69 -12 181 C ATOM 235 O GLN A 36 22.888 -3.788 22.461 1.00 12.88 O ANISOU 235 O GLN A 36 1574 2092 1228 -113 -363 247 O ATOM 236 CB GLN A 36 21.724 -2.152 24.583 1.00 12.74 C ANISOU 236 CB GLN A 36 1437 2456 945 69 80 127 C ATOM 237 CG GLN A 36 21.852 -1.402 25.916 1.00 17.01 C ANISOU 237 CG GLN A 36 1801 3811 851 -25 -62 -152 C ATOM 238 CD GLN A 36 23.152 -1.609 26.655 1.00 18.36 C ANISOU 238 CD GLN A 36 1629 4434 914 -385 88 -280 C ATOM 239 OE1 GLN A 36 23.491 -2.743 26.993 1.00 35.61 O ANISOU 239 OE1 GLN A 36 4281 5707 3541 815 -2026 820 O ATOM 240 NE2 GLN A 36 23.833 -0.471 26.880 1.00 29.65 N ANISOU 240 NE2 GLN A 36 2947 6546 1773 -2435 741 -1359 N ATOM 241 N ALA A 37 23.085 -2.023 21.125 1.00 10.13 N ANISOU 241 N ALA A 37 1009 2141 697 59 -112 18 N ATOM 242 CA ALA A 37 23.449 -2.862 19.981 1.00 10.06 C ANISOU 242 CA ALA A 37 1088 1798 935 190 -196 -98 C ATOM 243 C ALA A 37 24.819 -3.516 20.184 1.00 10.49 C ANISOU 243 C ALA A 37 961 2004 1021 23 -200 27 C ATOM 244 O ALA A 37 25.723 -2.907 20.713 1.00 13.88 O ANISOU 244 O ALA A 37 1075 2698 1500 -9 -478 -280 O ATOM 245 CB ALA A 37 23.514 -2.010 18.723 1.00 10.73 C ANISOU 245 CB ALA A 37 1174 2124 779 178 -96 -18 C ATOM 246 N SER A 38 24.977 -4.761 19.753 1.00 11.96 N ANISOU 246 N SER A 38 1379 2194 971 548 -307 -114 N ATOM 247 CA SER A 38 26.250 -5.473 19.995 1.00 16.43 C ANISOU 247 CA SER A 38 1786 3332 1125 1185 -779 -697 C ATOM 248 C SER A 38 26.468 -6.522 18.899 1.00 12.10 C ANISOU 248 C SER A 38 1346 2210 1042 629 -489 -114 C ATOM 249 O SER A 38 25.529 -7.156 18.445 1.00 13.13 O ANISOU 249 O SER A 38 1299 2592 1099 550 -526 -173 O ATOM 250 CB SER A 38 26.153 -6.140 21.338 1.00 25.26 C ANISOU 250 CB SER A 38 4838 3740 1018 2815 -1047 -589 C ATOM 251 OG SER A 38 25.527 -7.391 21.391 1.00 39.32 O ANISOU 251 OG SER A 38 9761 3216 1964 2234 389 344 O ATOM 252 N LEU A 39 27.747 -6.679 18.542 1.00 12.81 N ANISOU 252 N LEU A 39 1426 2124 1316 344 -190 -106 N ATOM 253 CA LEU A 39 28.114 -7.798 17.671 1.00 11.91 C ANISOU 253 CA LEU A 39 1163 2106 1256 356 -227 2 C ATOM 254 C LEU A 39 28.122 -9.101 18.469 1.00 13.10 C ANISOU 254 C LEU A 39 1489 2178 1308 369 -639 73 C ATOM 255 O LEU A 39 28.750 -9.174 19.536 1.00 18.76 O ANISOU 255 O LEU A 39 2104 3127 1898 -6 -1255 510 O ATOM 256 CB LEU A 39 29.472 -7.533 17.043 1.00 15.68 C ANISOU 256 CB LEU A 39 1421 2995 1544 114 71 -251 C ATOM 257 CG LEU A 39 30.080 -8.640 16.173 1.00 15.00 C ANISOU 257 CG LEU A 39 1252 3040 1405 568 -73 112 C ATOM 258 CD1 LEU A 39 29.213 -8.860 14.939 1.00 14.58 C ANISOU 258 CD1 LEU A 39 2142 2311 1087 499 -172 339 C ATOM 259 CD2 LEU A 39 31.497 -8.276 15.785 1.00 18.77 C ANISOU 259 CD2 LEU A 39 1625 2923 2583 185 517 -266 C ATOM 260 N GLU A 40 27.402 -10.071 18.023 1.00 13.02 N ANISOU 260 N GLU A 40 1569 2068 1309 338 -383 72 N ATOM 261 CA GLU A 40 27.291 -11.391 18.576 1.00 16.63 C ANISOU 261 CA GLU A 40 2032 2176 2111 307 -131 366 C ATOM 262 C GLU A 40 27.672 -12.329 17.434 1.00 18.86 C ANISOU 262 C GLU A 40 3297 2110 1758 935 -190 530 C ATOM 263 O GLU A 40 28.167 -11.819 16.374 1.00 19.72 O ANISOU 263 O GLU A 40 2188 2867 2439 -117 226 331 O ATOM 264 CB GLU A 40 25.898 -11.651 19.162 1.00 18.54 C ANISOU 264 CB GLU A 40 2029 2482 2533 19 -96 341 C ATOM 265 CG GLU A 40 25.468 -10.612 20.198 1.00 18.12 C ANISOU 265 CG GLU A 40 1956 3086 1843 225 -245 375 C ATOM 266 CD GLU A 40 26.489 -10.510 21.335 1.00 30.89 C ANISOU 266 CD GLU A 40 4783 3760 3193 1598 -2301 -64 C ATOM 267 OE1 GLU A 40 27.364 -11.410 21.379 1.00 48.08 O ANISOU 267 OE1 GLU A 40 5158 4758 8351 2251 -4017 -318 O ATOM 268 OE2 GLU A 40 26.419 -9.548 22.141 1.00 30.51 O ANISOU 268 OE2 GLU A 40 5878 3462 2252 -189 -1648 441 O ATOM 269 N GLU A 41 27.585 -13.628 17.555 1.00 18.39 N ANISOU 269 N GLU A 41 3035 2279 1675 869 70 495 N ATOM 270 CA GLU A 41 28.044 -14.594 16.615 1.00 20.13 C ANISOU 270 CA GLU A 41 3029 2241 2379 1057 -629 66 C ATOM 271 C GLU A 41 27.383 -14.407 15.249 1.00 15.08 C ANISOU 271 C GLU A 41 1438 2179 2111 494 -124 -98 C ATOM 272 O GLU A 41 26.286 -14.823 14.910 1.00 18.15 O ANISOU 272 O GLU A 41 1479 2843 2573 -78 191 380 O ATOM 273 CB GLU A 41 27.840 -16.069 16.945 1.00 27.24 C ANISOU 273 CB GLU A 41 4778 2257 3316 1062 -474 385 C ATOM 274 CG GLU A 41 28.405 -17.006 15.886 1.00 30.30 C ANISOU 274 CG GLU A 41 4797 2047 4667 558 553 33 C ATOM 275 CD GLU A 41 29.734 -16.708 15.235 1.00 38.37 C ANISOU 275 CD GLU A 41 4835 4062 5683 260 847 -109 C ATOM 276 OE1 GLU A 41 30.312 -15.602 15.341 1.00 43.41 O ANISOU 276 OE1 GLU A 41 4603 5897 5995 -1474 -2395 1563 O ATOM 277 OE2 GLU A 41 30.241 -17.611 14.521 1.00 42.86 O ANISOU 277 OE2 GLU A 41 5278 6387 4618 3588 91 687 O ATOM 278 N GLY A 42 28.156 -13.765 14.375 1.00 16.38 N ANISOU 278 N GLY A 42 1316 2023 2884 211 -392 530 N ATOM 279 CA GLY A 42 27.699 -13.603 13.009 1.00 15.42 C ANISOU 279 CA GLY A 42 1640 1619 2600 440 128 436 C ATOM 280 C GLY A 42 26.694 -12.531 12.749 1.00 12.45 C ANISOU 280 C GLY A 42 1295 1637 1796 247 7 192 C ATOM 281 O GLY A 42 26.197 -12.470 11.602 1.00 12.72 O ANISOU 281 O GLY A 42 1803 1622 1408 335 296 2 O ATOM 282 N ARG A 43 26.370 -11.668 13.703 1.00 12.02 N ANISOU 282 N ARG A 43 1275 1722 1570 360 -446 89 N ATOM 283 CA ARG A 43 25.341 -10.667 13.416 1.00 10.64 C ANISOU 283 CA ARG A 43 1307 1403 1334 207 -574 62 C ATOM 284 C ARG A 43 25.404 -9.589 14.470 1.00 9.95 C ANISOU 284 C ARG A 43 1185 1528 1069 90 -430 100 C ATOM 285 O ARG A 43 25.877 -9.808 15.592 1.00 13.44 O ANISOU 285 O ARG A 43 1948 2067 1092 694 -670 87 O ATOM 286 CB ARG A 43 23.939 -11.329 13.451 1.00 12.56 C ANISOU 286 CB ARG A 43 1344 1801 1625 21 -615 -37 C ATOM 287 CG ARG A 43 23.609 -11.855 14.848 1.00 17.02 C ANISOU 287 CG ARG A 43 2059 2766 1644 -318 439 -682 C ATOM 288 CD ARG A 43 23.112 -13.264 14.865 1.00 17.00 C ANISOU 288 CD ARG A 43 2468 2304 1687 262 110 377 C ATOM 289 NE ARG A 43 22.594 -13.638 16.166 1.00 20.97 N ANISOU 289 NE ARG A 43 1841 4152 1973 -248 477 276 N ATOM 290 CZ ARG A 43 23.201 -14.019 17.267 1.00 31.96 C ANISOU 290 CZ ARG A 43 3691 5883 2571 -434 473 2395 C ATOM 291 NH1 ARG A 43 24.518 -14.105 17.317 1.00 40.27 N ANISOU 291 NH1 ARG A 43 4223 7919 3160 2998 -604 710 N ATOM 292 NH2 ARG A 43 22.497 -14.317 18.352 1.00 53.94 N ANISOU 292 NH2 ARG A 43 7916 9381 3199 -4014 1421 2665 N ATOM 293 N ILE A 44 24.893 -8.392 14.142 1.00 9.24 N ANISOU 293 N ILE A 44 990 1645 874 281 -261 59 N ATOM 294 CA ILE A 44 24.722 -7.330 15.127 1.00 8.78 C ANISOU 294 CA ILE A 44 986 1573 779 -2 -229 36 C ATOM 295 C ILE A 44 23.302 -7.393 15.638 1.00 8.84 C ANISOU 295 C ILE A 44 975 1564 818 70 -231 65 C ATOM 296 O ILE A 44 22.326 -7.306 14.872 1.00 10.09 O ANISOU 296 O ILE A 44 953 2174 709 49 -238 153 O ATOM 297 CB ILE A 44 25.127 -5.949 14.587 1.00 9.74 C ANISOU 297 CB ILE A 44 1072 1622 1007 74 -277 158 C ATOM 298 CG1 ILE A 44 26.644 -5.892 14.374 1.00 10.70 C ANISOU 298 CG1 ILE A 44 1112 1898 1058 11 -56 248 C ATOM 299 CG2 ILE A 44 24.602 -4.820 15.490 1.00 10.43 C ANISOU 299 CG2 ILE A 44 1423 1673 867 64 -98 45 C ATOM 300 CD1 ILE A 44 27.128 -4.663 13.615 1.00 12.43 C ANISOU 300 CD1 ILE A 44 1213 1981 1529 -23 23 390 C ATOM 301 N VAL A 45 23.183 -7.577 16.952 1.00 9.10 N ANISOU 301 N VAL A 45 955 1711 792 72 -196 94 N ATOM 302 CA VAL A 45 21.885 -7.647 17.614 1.00 9.26 C ANISOU 302 CA VAL A 45 972 1732 814 71 -218 138 C ATOM 303 C VAL A 45 21.523 -6.276 18.112 1.00 9.03 C ANISOU 303 C VAL A 45 994 1646 790 63 -209 33 C ATOM 304 O VAL A 45 22.255 -5.711 18.917 1.00 11.07 O ANISOU 304 O VAL A 45 1140 2113 953 148 -420 -160 O ATOM 305 CB VAL A 45 21.941 -8.652 18.770 1.00 10.21 C ANISOU 305 CB VAL A 45 1449 1596 835 2 -225 170 C ATOM 306 CG1 VAL A 45 20.616 -8.670 19.486 1.00 10.97 C ANISOU 306 CG1 VAL A 45 1582 1710 874 -9 -40 142 C ATOM 307 CG2 VAL A 45 22.304 -10.042 18.275 1.00 11.02 C ANISOU 307 CG2 VAL A 45 1617 1632 940 -13 -161 112 C ATOM 308 N LEU A 46 20.385 -5.746 17.634 1.00 8.44 N ANISOU 308 N LEU A 46 1077 1555 574 34 -242 168 N ATOM 309 CA LEU A 46 19.970 -4.428 18.027 1.00 8.49 C ANISOU 309 CA LEU A 46 925 1584 716 84 -32 118 C ATOM 310 C LEU A 46 19.205 -4.439 19.345 1.00 8.37 C ANISOU 310 C LEU A 46 865 1632 682 -111 -108 108 C ATOM 311 O LEU A 46 19.280 -3.482 20.103 1.00 10.31 O ANISOU 311 O LEU A 46 1307 1948 660 -181 -16 -35 O ATOM 312 CB LEU A 46 19.109 -3.790 16.918 1.00 8.52 C ANISOU 312 CB LEU A 46 922 1622 694 46 -37 206 C ATOM 313 CG LEU A 46 19.870 -3.596 15.588 1.00 8.62 C ANISOU 313 CG LEU A 46 897 1782 597 -56 -144 122 C ATOM 314 CD1 LEU A 46 18.881 -3.097 14.529 1.00 9.96 C ANISOU 314 CD1 LEU A 46 1024 2068 692 -105 -197 475 C ATOM 315 CD2 LEU A 46 21.026 -2.662 15.724 1.00 11.32 C ANISOU 315 CD2 LEU A 46 1032 2130 1141 -307 -157 186 C ATOM 316 N THR A 47 18.381 -5.496 19.530 1.00 9.08 N ANISOU 316 N THR A 47 1032 1508 909 113 100 322 N ATOM 317 CA THR A 47 17.518 -5.542 20.748 1.00 9.66 C ANISOU 317 CA THR A 47 945 1946 778 -48 -58 467 C ATOM 318 C THR A 47 17.741 -6.806 21.482 1.00 10.27 C ANISOU 318 C THR A 47 1183 1683 1037 27 -91 346 C ATOM 319 O THR A 47 17.037 -7.779 21.340 1.00 12.13 O ANISOU 319 O THR A 47 1751 1417 1440 107 -551 -15 O ATOM 320 CB THR A 47 16.034 -5.339 20.297 1.00 8.13 C ANISOU 320 CB THR A 47 921 1558 608 85 -50 3 C ATOM 321 OG1 THR A 47 15.601 -6.332 19.329 1.00 8.25 O ANISOU 321 OG1 THR A 47 956 1562 617 310 -76 36 O ATOM 322 CG2 THR A 47 15.817 -3.941 19.757 1.00 8.68 C ANISOU 322 CG2 THR A 47 1129 1550 620 111 39 28 C ATOM 323 N SER A 48 18.808 -6.782 22.339 1.00 10.86 N ANISOU 323 N SER A 48 1166 1721 1240 201 -184 224 N ATOM 324 CA SER A 48 19.299 -8.013 22.922 1.00 11.69 C ANISOU 324 CA SER A 48 1449 1815 1179 324 -94 302 C ATOM 325 C SER A 48 18.597 -8.465 24.207 1.00 11.70 C ANISOU 325 C SER A 48 1843 1691 911 448 -134 53 C ATOM 326 O SER A 48 18.919 -9.570 24.668 1.00 14.37 O ANISOU 326 O SER A 48 1993 1994 1472 299 -203 623 O ATOM 327 CB SER A 48 20.800 -7.864 23.195 1.00 15.54 C ANISOU 327 CB SER A 48 1399 2793 1712 838 -154 -168 C ATOM 328 OG SER A 48 21.098 -6.807 24.067 1.00 17.48 O ANISOU 328 OG SER A 48 1889 3271 1481 -67 -478 11 O ATOM 329 N ASN A 49 17.685 -7.718 24.811 1.00 13.26 N ANISOU 329 N ASN A 49 1775 2480 785 489 -106 -261 N ATOM 330 CA ASN A 49 16.947 -8.188 25.971 1.00 11.83 C ANISOU 330 CA ASN A 49 1755 1941 799 471 -242 -13 C ATOM 331 C ASN A 49 15.569 -7.535 26.011 1.00 11.51 C ANISOU 331 C ASN A 49 1674 1876 822 447 -213 -144 C ATOM 332 O ASN A 49 15.168 -6.815 25.099 1.00 10.04 O ANISOU 332 O ASN A 49 1411 1633 770 114 -227 -90 O ATOM 333 CB ASN A 49 17.790 -7.916 27.222 1.00 11.83 C ANISOU 333 CB ASN A 49 1729 1926 839 58 -242 30 C ATOM 334 CG ASN A 49 18.009 -6.522 27.623 1.00 11.77 C ANISOU 334 CG ASN A 49 1718 1755 997 283 -134 80 C ATOM 335 OD1 ASN A 49 17.299 -5.613 27.291 1.00 14.16 O ANISOU 335 OD1 ASN A 49 1888 1927 1563 90 -252 542 O ATOM 336 ND2 ASN A 49 18.999 -6.339 28.569 1.00 14.51 N ANISOU 336 ND2 ASN A 49 1754 1959 1799 173 -517 -213 N ATOM 337 N GLN A 50 14.782 -7.796 27.082 1.00 11.97 N ANISOU 337 N GLN A 50 1698 1936 915 247 -244 117 N ATOM 338 CA GLN A 50 13.427 -7.242 27.187 1.00 10.27 C ANISOU 338 CA GLN A 50 1456 1537 907 -163 -168 50 C ATOM 339 C GLN A 50 13.491 -5.726 27.288 1.00 9.39 C ANISOU 339 C GLN A 50 1383 1475 708 -198 68 86 C ATOM 340 O GLN A 50 14.164 -5.232 28.190 1.00 13.00 O ANISOU 340 O GLN A 50 2128 1688 1124 -526 -697 280 O ATOM 341 CB GLN A 50 12.697 -7.809 28.423 1.00 11.11 C ANISOU 341 CB GLN A 50 1806 1350 1065 -167 -162 193 C ATOM 342 CG GLN A 50 12.459 -9.308 28.222 1.00 15.28 C ANISOU 342 CG GLN A 50 2894 1215 1697 -182 -618 285 C ATOM 343 CD GLN A 50 11.913 -9.926 29.492 1.00 22.48 C ANISOU 343 CD GLN A 50 3616 2340 2587 -953 -809 1372 C ATOM 344 OE1 GLN A 50 11.914 -11.162 29.555 1.00 32.90 O ANISOU 344 OE1 GLN A 50 5454 2359 4687 -1708 -1606 1907 O ATOM 345 NE2 GLN A 50 11.487 -9.146 30.485 1.00 35.60 N ANISOU 345 NE2 GLN A 50 7055 3876 2596 -1639 1507 1332 N ATOM 346 N ASN A 51 12.748 -5.026 26.424 1.00 8.53 N ANISOU 346 N ASN A 51 1226 1443 572 -178 46 -45 N ATOM 347 CA ASN A 51 12.687 -3.581 26.385 1.00 8.03 C ANISOU 347 CA ASN A 51 1045 1384 624 -57 -1 -117 C ATOM 348 C ASN A 51 14.089 -2.965 26.221 1.00 7.56 C ANISOU 348 C ASN A 51 1033 1193 647 15 24 -86 C ATOM 349 O ASN A 51 14.588 -2.253 27.083 1.00 8.57 O ANISOU 349 O ASN A 51 1268 1335 654 -197 126 -167 O ATOM 350 CB ASN A 51 12.020 -3.007 27.636 1.00 9.14 C ANISOU 350 CB ASN A 51 1291 1559 623 42 213 -29 C ATOM 351 CG ASN A 51 11.594 -1.586 27.410 1.00 9.35 C ANISOU 351 CG ASN A 51 1361 1397 793 -115 248 -201 C ATOM 352 OD1 ASN A 51 11.725 -0.962 26.327 1.00 10.99 O ANISOU 352 OD1 ASN A 51 1749 1690 736 426 136 -31 O ATOM 353 ND2 ASN A 51 11.019 -1.017 28.423 1.00 15.17 N ANISOU 353 ND2 ASN A 51 3295 1478 990 -3 841 -357 N ATOM 354 N SER A 52 14.644 -3.265 25.065 1.00 8.60 N ANISOU 354 N SER A 52 1073 1734 462 -92 20 -54 N ATOM 355 CA SER A 52 15.992 -2.787 24.700 1.00 9.11 C ANISOU 355 CA SER A 52 969 1961 529 11 -63 -54 C ATOM 356 C SER A 52 15.938 -2.012 23.412 1.00 8.12 C ANISOU 356 C SER A 52 1035 1557 493 -44 -43 -120 C ATOM 357 O SER A 52 14.940 -2.067 22.665 1.00 8.44 O ANISOU 357 O SER A 52 877 1754 574 7 -68 -147 O ATOM 358 CB SER A 52 16.994 -3.949 24.561 1.00 9.93 C ANISOU 358 CB SER A 52 1232 1819 723 130 -82 63 C ATOM 359 OG SER A 52 16.512 -4.953 23.645 1.00 10.97 O ANISOU 359 OG SER A 52 1417 2079 673 389 -138 -133 O ATOM 360 N LYS A 53 17.018 -1.276 23.150 1.00 8.87 N ANISOU 360 N LYS A 53 955 1758 657 -80 -57 -95 N ATOM 361 CA LYS A 53 17.173 -0.399 22.011 1.00 8.47 C ANISOU 361 CA LYS A 53 945 1727 548 51 66 -44 C ATOM 362 C LYS A 53 18.599 -0.518 21.495 1.00 9.58 C ANISOU 362 C LYS A 53 968 2116 557 167 -24 -34 C ATOM 363 O LYS A 53 19.531 -0.676 22.254 1.00 10.25 O ANISOU 363 O LYS A 53 1034 2268 592 51 -101 36 O ATOM 364 CB LYS A 53 16.869 1.075 22.310 1.00 9.29 C ANISOU 364 CB LYS A 53 1117 1667 746 -20 47 -292 C ATOM 365 CG LYS A 53 15.409 1.316 22.673 1.00 10.05 C ANISOU 365 CG LYS A 53 1209 1541 1070 162 14 -260 C ATOM 366 CD LYS A 53 15.088 2.747 23.047 1.00 10.18 C ANISOU 366 CD LYS A 53 1143 1605 1119 83 -46 -397 C ATOM 367 CE LYS A 53 13.588 2.982 23.056 1.00 11.14 C ANISOU 367 CE LYS A 53 1106 1456 1670 18 301 -417 C ATOM 368 NZ LYS A 53 13.199 4.253 23.730 1.00 12.87 N ANISOU 368 NZ LYS A 53 1468 1409 2011 21 523 -391 N ATOM 369 N GLY A 54 18.734 -0.388 20.167 1.00 9.25 N ANISOU 369 N GLY A 54 967 2057 490 50 48 -49 N ATOM 370 CA GLY A 54 20.066 -0.490 19.561 1.00 9.61 C ANISOU 370 CA GLY A 54 890 2278 482 38 29 8 C ATOM 371 C GLY A 54 20.081 0.326 18.283 1.00 7.36 C ANISOU 371 C GLY A 54 779 1424 594 -21 -75 -112 C ATOM 372 O GLY A 54 19.055 0.473 17.593 1.00 8.42 O ANISOU 372 O GLY A 54 853 1786 560 -12 -30 -113 O ATOM 373 N SER A 55 21.273 0.838 17.925 1.00 8.92 N ANISOU 373 N SER A 55 858 1968 562 -91 -52 -8 N ATOM 374 CA SER A 55 21.481 1.556 16.678 1.00 7.96 C ANISOU 374 CA SER A 55 788 1643 595 18 -44 -21 C ATOM 375 C SER A 55 22.775 1.123 16.020 1.00 7.79 C ANISOU 375 C SER A 55 743 1679 538 -69 -106 -65 C ATOM 376 O SER A 55 23.719 0.669 16.673 1.00 8.49 O ANISOU 376 O SER A 55 785 1803 637 2 -153 -28 O ATOM 377 CB SER A 55 21.452 3.068 16.870 1.00 9.21 C ANISOU 377 CB SER A 55 938 1699 862 -124 -116 -217 C ATOM 378 OG SER A 55 22.514 3.458 17.714 1.00 10.38 O ANISOU 378 OG SER A 55 982 2059 903 -193 -12 -413 O ATOM 379 N LEU A 56 22.824 1.332 14.719 1.00 7.26 N ANISOU 379 N LEU A 56 704 1466 587 -70 -33 36 N ATOM 380 CA LEU A 56 23.991 0.959 13.908 1.00 7.46 C ANISOU 380 CA LEU A 56 714 1522 600 19 -43 -81 C ATOM 381 C LEU A 56 24.047 1.939 12.742 1.00 7.29 C ANISOU 381 C LEU A 56 627 1501 640 -105 -17 -143 C ATOM 382 O LEU A 56 23.142 1.873 11.876 1.00 7.38 O ANISOU 382 O LEU A 56 712 1507 583 -86 -88 -78 O ATOM 383 CB LEU A 56 23.866 -0.464 13.460 1.00 7.83 C ANISOU 383 CB LEU A 56 738 1557 682 -42 -47 -19 C ATOM 384 CG LEU A 56 24.955 -0.965 12.487 1.00 8.74 C ANISOU 384 CG LEU A 56 718 1633 970 40 -2 -242 C ATOM 385 CD1 LEU A 56 26.326 -0.964 13.147 1.00 10.16 C ANISOU 385 CD1 LEU A 56 840 1829 1191 106 -28 -191 C ATOM 386 CD2 LEU A 56 24.581 -2.335 11.954 1.00 8.64 C ANISOU 386 CD2 LEU A 56 967 1332 985 87 32 70 C ATOM 387 N TRP A 57 24.999 2.862 12.711 1.00 7.76 N ANISOU 387 N TRP A 57 689 1524 734 -151 -27 -152 N ATOM 388 CA TRP A 57 25.082 3.889 11.715 1.00 7.65 C ANISOU 388 CA TRP A 57 721 1500 687 -118 -47 -126 C ATOM 389 C TRP A 57 26.470 3.948 11.108 1.00 7.60 C ANISOU 389 C TRP A 57 728 1473 687 -170 -108 -101 C ATOM 390 O TRP A 57 27.483 3.714 11.790 1.00 8.55 O ANISOU 390 O TRP A 57 768 1656 824 -68 -111 -79 O ATOM 391 CB TRP A 57 24.823 5.246 12.307 1.00 8.68 C ANISOU 391 CB TRP A 57 931 1543 826 -133 17 -234 C ATOM 392 CG TRP A 57 23.430 5.537 12.825 1.00 8.47 C ANISOU 392 CG TRP A 57 816 1481 920 -103 -45 -214 C ATOM 393 CD1 TRP A 57 22.954 5.263 14.080 1.00 8.43 C ANISOU 393 CD1 TRP A 57 849 1445 909 -86 -25 -194 C ATOM 394 CD2 TRP A 57 22.351 6.180 12.107 1.00 7.61 C ANISOU 394 CD2 TRP A 57 865 1133 893 -204 43 -173 C ATOM 395 NE1 TRP A 57 21.629 5.687 14.185 1.00 8.77 N ANISOU 395 NE1 TRP A 57 930 1488 915 -80 152 -177 N ATOM 396 CE2 TRP A 57 21.250 6.260 13.000 1.00 7.65 C ANISOU 396 CE2 TRP A 57 888 1234 785 -122 -16 -337 C ATOM 397 CE3 TRP A 57 22.240 6.719 10.799 1.00 7.93 C ANISOU 397 CE3 TRP A 57 1005 1130 880 -207 -40 -183 C ATOM 398 CZ2 TRP A 57 20.042 6.832 12.615 1.00 7.70 C ANISOU 398 CZ2 TRP A 57 889 1049 987 -115 85 -219 C ATOM 399 CZ3 TRP A 57 21.019 7.289 10.437 1.00 8.21 C ANISOU 399 CZ3 TRP A 57 968 1222 928 -212 -56 -250 C ATOM 400 CH2 TRP A 57 19.945 7.333 11.347 1.00 8.50 C ANISOU 400 CH2 TRP A 57 967 1334 926 -292 -119 -271 C ATOM 401 N LEU A 58 26.551 4.362 9.850 1.00 7.45 N ANISOU 401 N LEU A 58 721 1389 720 -146 34 -150 N ATOM 402 CA LEU A 58 27.842 4.672 9.236 1.00 7.38 C ANISOU 402 CA LEU A 58 687 1383 735 -169 -58 -106 C ATOM 403 C LEU A 58 28.435 5.908 9.918 1.00 8.27 C ANISOU 403 C LEU A 58 695 1564 884 -163 -53 -226 C ATOM 404 O LEU A 58 27.746 6.889 10.192 1.00 8.41 O ANISOU 404 O LEU A 58 839 1460 895 -119 -58 -247 O ATOM 405 CB LEU A 58 27.680 4.884 7.722 1.00 8.12 C ANISOU 405 CB LEU A 58 899 1403 782 -107 -18 -22 C ATOM 406 CG LEU A 58 27.621 3.515 6.998 1.00 8.18 C ANISOU 406 CG LEU A 58 786 1519 804 115 -68 -275 C ATOM 407 CD1 LEU A 58 26.789 3.579 5.730 1.00 9.78 C ANISOU 407 CD1 LEU A 58 947 1894 873 303 -124 -247 C ATOM 408 CD2 LEU A 58 29.025 3.009 6.691 1.00 8.96 C ANISOU 408 CD2 LEU A 58 773 1713 918 68 -59 -208 C ATOM 409 N LYS A 59 29.778 5.833 10.155 1.00 9.05 N ANISOU 409 N LYS A 59 740 1796 902 -231 -195 -87 N ATOM 410 CA LYS A 59 30.449 6.991 10.742 1.00 9.37 C ANISOU 410 CA LYS A 59 760 1765 1035 -191 -185 -166 C ATOM 411 C LYS A 59 30.578 8.204 9.840 1.00 9.82 C ANISOU 411 C LYS A 59 817 1768 1148 -256 -155 -183 C ATOM 412 O LYS A 59 30.659 9.339 10.349 1.00 11.27 O ANISOU 412 O LYS A 59 1196 1778 1309 -431 -298 -282 O ATOM 413 CB LYS A 59 31.860 6.553 11.178 1.00 11.04 C ANISOU 413 CB LYS A 59 878 2037 1280 -266 -355 -11 C ATOM 414 CG LYS A 59 31.846 5.661 12.387 1.00 12.52 C ANISOU 414 CG LYS A 59 1257 2115 1384 -316 -535 103 C ATOM 415 CD LYS A 59 33.286 5.334 12.762 1.00 14.34 C ANISOU 415 CD LYS A 59 1334 2605 1509 -427 -665 320 C ATOM 416 CE LYS A 59 33.436 4.303 13.858 1.00 15.02 C ANISOU 416 CE LYS A 59 1340 2665 1702 -343 -821 385 C ATOM 417 NZ LYS A 59 34.928 4.035 14.033 1.00 16.49 N ANISOU 417 NZ LYS A 59 1431 2650 2184 316 -462 -101 N ATOM 418 N GLN A 60 30.622 8.010 8.528 1.00 9.25 N ANISOU 418 N GLN A 60 857 1550 1109 -280 -130 -93 N ATOM 419 CA GLN A 60 30.781 9.108 7.565 1.00 10.80 C ANISOU 419 CA GLN A 60 1109 1658 1337 -278 -251 92 C ATOM 420 C GLN A 60 29.495 9.290 6.796 1.00 9.87 C ANISOU 420 C GLN A 60 1160 1533 1057 -231 -203 -94 C ATOM 421 O GLN A 60 28.793 8.308 6.429 1.00 10.60 O ANISOU 421 O GLN A 60 917 1645 1466 -206 -152 -261 O ATOM 422 CB GLN A 60 31.953 8.807 6.660 1.00 15.61 C ANISOU 422 CB GLN A 60 1104 2882 1945 -248 225 641 C ATOM 423 CG GLN A 60 33.298 8.571 7.329 1.00 28.33 C ANISOU 423 CG GLN A 60 923 5827 4014 -335 -170 467 C ATOM 424 CD GLN A 60 33.781 9.397 8.483 1.00 37.39 C ANISOU 424 CD GLN A 60 2089 5757 6363 -1374 -2010 158 C ATOM 425 OE1 GLN A 60 34.299 8.969 9.553 1.00 43.33 O ANISOU 425 OE1 GLN A 60 3729 8312 4421 -2138 -903 412 O ATOM 426 NE2 GLN A 60 33.652 10.713 8.362 1.00 53.47 N ANISOU 426 NE2 GLN A 60 6772 5273 8272 -4011 -126 1121 N ATOM 427 N GLY A 61 29.224 10.561 6.472 1.00 10.73 N ANISOU 427 N GLY A 61 1292 1575 1208 46 -176 -177 N ATOM 428 CA GLY A 61 28.088 10.818 5.617 1.00 11.02 C ANISOU 428 CA GLY A 61 1379 1831 979 33 -145 -149 C ATOM 429 C GLY A 61 28.351 10.390 4.177 1.00 9.21 C ANISOU 429 C GLY A 61 1023 1420 1055 -53 -19 -187 C ATOM 430 O GLY A 61 29.479 10.290 3.778 1.00 9.68 O ANISOU 430 O GLY A 61 1004 1400 1273 -223 -110 -321 O ATOM 431 N PHE A 62 27.243 10.202 3.450 1.00 9.20 N ANISOU 431 N PHE A 62 1075 1403 1015 -81 60 -96 N ATOM 432 CA PHE A 62 27.215 9.879 2.039 1.00 8.63 C ANISOU 432 CA PHE A 62 920 1322 1036 -86 56 -154 C ATOM 433 C PHE A 62 26.746 11.117 1.295 1.00 8.13 C ANISOU 433 C PHE A 62 1050 1102 938 -93 102 -153 C ATOM 434 O PHE A 62 25.656 11.635 1.561 1.00 8.75 O ANISOU 434 O PHE A 62 1037 1135 1153 -129 141 -205 O ATOM 435 CB PHE A 62 26.283 8.678 1.813 1.00 9.07 C ANISOU 435 CB PHE A 62 888 1320 1238 -224 -84 105 C ATOM 436 CG PHE A 62 25.891 8.490 0.352 1.00 9.80 C ANISOU 436 CG PHE A 62 1076 1356 1293 -324 103 -178 C ATOM 437 CD1 PHE A 62 26.774 8.104 -0.625 1.00 14.21 C ANISOU 437 CD1 PHE A 62 1198 2340 1860 -528 337 -880 C ATOM 438 CD2 PHE A 62 24.576 8.777 -0.055 1.00 9.99 C ANISOU 438 CD2 PHE A 62 1180 1361 1253 -197 -126 -76 C ATOM 439 CE1 PHE A 62 26.356 7.969 -1.960 1.00 15.13 C ANISOU 439 CE1 PHE A 62 1444 2524 1780 -855 439 -1057 C ATOM 440 CE2 PHE A 62 24.131 8.604 -1.349 1.00 12.22 C ANISOU 440 CE2 PHE A 62 1635 1744 1263 -82 -106 -227 C ATOM 441 CZ PHE A 62 25.031 8.231 -2.305 1.00 12.39 C ANISOU 441 CZ PHE A 62 1756 1533 1420 -580 267 -137 C ATOM 442 N ASP A 63 27.575 11.588 0.352 1.00 8.53 N ANISOU 442 N ASP A 63 888 1365 988 -285 41 -212 N ATOM 443 CA ASP A 63 27.234 12.751 -0.424 1.00 9.62 C ANISOU 443 CA ASP A 63 1282 1395 980 -577 -52 0 C ATOM 444 C ASP A 63 26.394 12.327 -1.617 1.00 9.23 C ANISOU 444 C ASP A 63 1164 1308 1034 -356 -14 -244 C ATOM 445 O ASP A 63 26.861 11.713 -2.587 1.00 10.81 O ANISOU 445 O ASP A 63 1146 1882 1081 -193 133 -346 O ATOM 446 CB ASP A 63 28.540 13.379 -0.925 1.00 12.49 C ANISOU 446 CB ASP A 63 1174 1998 1575 -665 -73 160 C ATOM 447 CG ASP A 63 28.355 14.688 -1.633 1.00 16.80 C ANISOU 447 CG ASP A 63 2134 2168 2080 -1215 -564 624 C ATOM 448 OD1 ASP A 63 29.308 15.019 -2.338 1.00 30.14 O ANISOU 448 OD1 ASP A 63 2598 4225 4628 -1320 129 2391 O ATOM 449 OD2 ASP A 63 27.294 15.335 -1.475 1.00 28.88 O ANISOU 449 OD2 ASP A 63 2545 2846 5580 -352 -225 2277 O ATOM 450 N LEU A 64 25.079 12.668 -1.599 1.00 8.59 N ANISOU 450 N LEU A 64 1066 1193 1005 -398 71 -226 N ATOM 451 CA LEU A 64 24.154 12.206 -2.630 1.00 8.17 C ANISOU 451 CA LEU A 64 1098 1173 835 -314 22 -117 C ATOM 452 C LEU A 64 24.322 13.054 -3.894 1.00 7.98 C ANISOU 452 C LEU A 64 1047 1028 956 -355 -18 -66 C ATOM 453 O LEU A 64 23.911 14.225 -3.943 1.00 10.43 O ANISOU 453 O LEU A 64 1715 1072 1175 -480 -11 -89 O ATOM 454 CB LEU A 64 22.733 12.242 -2.108 1.00 8.88 C ANISOU 454 CB LEU A 64 1092 1286 997 -421 112 -258 C ATOM 455 CG LEU A 64 21.681 11.892 -3.190 1.00 7.69 C ANISOU 455 CG LEU A 64 1054 907 959 -253 108 -143 C ATOM 456 CD1 LEU A 64 21.815 10.447 -3.665 1.00 9.07 C ANISOU 456 CD1 LEU A 64 1348 933 1165 -197 54 -281 C ATOM 457 CD2 LEU A 64 20.274 12.159 -2.663 1.00 9.46 C ANISOU 457 CD2 LEU A 64 1029 1154 1413 -166 131 -189 C ATOM 458 N LYS A 65 24.818 12.449 -4.957 1.00 8.74 N ANISOU 458 N LYS A 65 1051 1357 914 -520 61 -117 N ATOM 459 CA LYS A 65 25.004 13.096 -6.252 1.00 9.60 C ANISOU 459 CA LYS A 65 1329 1400 918 -762 104 -74 C ATOM 460 C LYS A 65 24.452 12.277 -7.417 1.00 7.95 C ANISOU 460 C LYS A 65 1024 1078 918 -444 171 -43 C ATOM 461 O LYS A 65 24.257 12.841 -8.506 1.00 8.92 O ANISOU 461 O LYS A 65 1386 1097 908 -428 19 -31 O ATOM 462 CB LYS A 65 26.492 13.365 -6.513 1.00 11.79 C ANISOU 462 CB LYS A 65 1292 2041 1145 -909 132 9 C ATOM 463 CG LYS A 65 27.141 14.288 -5.468 1.00 16.33 C ANISOU 463 CG LYS A 65 1687 2799 1718 -1436 191 -464 C ATOM 464 CD LYS A 65 26.644 15.715 -5.643 1.00 22.50 C ANISOU 464 CD LYS A 65 3024 2680 2844 -1124 540 -1212 C ATOM 465 CE LYS A 65 27.398 16.646 -4.729 1.00 26.32 C ANISOU 465 CE LYS A 65 3060 3217 3724 60 -671 -1844 C ATOM 466 NZ LYS A 65 26.587 17.823 -4.365 1.00 21.80 N ANISOU 466 NZ LYS A 65 2929 2125 3228 -753 646 -878 N ATOM 467 N ASP A 66 24.250 10.977 -7.213 1.00 8.61 N ANISOU 467 N ASP A 66 1132 1089 1050 -452 211 -33 N ATOM 468 CA ASP A 66 23.923 10.069 -8.302 1.00 9.01 C ANISOU 468 CA ASP A 66 1274 1112 1039 -462 287 -145 C ATOM 469 C ASP A 66 23.161 8.856 -7.712 1.00 7.07 C ANISOU 469 C ASP A 66 936 875 874 -191 209 -63 C ATOM 470 O ASP A 66 23.064 8.720 -6.495 1.00 7.55 O ANISOU 470 O ASP A 66 971 1139 757 -379 63 -37 O ATOM 471 CB ASP A 66 25.212 9.570 -8.989 1.00 16.88 C ANISOU 471 CB ASP A 66 1780 2191 2442 -942 1335 -901 C ATOM 472 CG ASP A 66 26.008 10.601 -9.762 1.00 19.52 C ANISOU 472 CG ASP A 66 2178 2582 2657 -1212 1254 -646 C ATOM 473 OD1 ASP A 66 27.052 11.121 -9.303 1.00 24.50 O ANISOU 473 OD1 ASP A 66 1958 3055 4295 -1289 1371 -1254 O ATOM 474 OD2 ASP A 66 25.503 10.903 -10.858 1.00 24.60 O ANISOU 474 OD2 ASP A 66 3441 3537 2369 -763 1394 -455 O ATOM 475 N SER A 67 22.669 8.035 -8.612 1.00 6.88 N ANISOU 475 N SER A 67 728 1048 839 -180 63 -109 N ATOM 476 CA SER A 67 21.844 6.884 -8.226 1.00 6.51 C ANISOU 476 CA SER A 67 784 978 710 -289 93 -19 C ATOM 477 C SER A 67 22.583 5.965 -7.281 1.00 7.00 C ANISOU 477 C SER A 67 737 938 986 -211 66 -74 C ATOM 478 O SER A 67 23.818 5.828 -7.303 1.00 7.98 O ANISOU 478 O SER A 67 647 1217 1167 -145 78 -92 O ATOM 479 CB SER A 67 21.473 6.130 -9.500 1.00 7.09 C ANISOU 479 CB SER A 67 852 990 851 -131 145 -240 C ATOM 480 OG SER A 67 20.791 7.017 -10.363 1.00 7.47 O ANISOU 480 OG SER A 67 897 1198 743 -135 161 -98 O ATOM 481 N PHE A 68 21.787 5.227 -6.456 1.00 6.74 N ANISOU 481 N PHE A 68 793 983 783 -130 94 12 N ATOM 482 CA PHE A 68 22.412 4.308 -5.504 1.00 6.54 C ANISOU 482 CA PHE A 68 647 1074 764 -147 -5 2 C ATOM 483 C PHE A 68 21.406 3.216 -5.143 1.00 6.34 C ANISOU 483 C PHE A 68 583 1137 690 -54 10 65 C ATOM 484 O PHE A 68 20.228 3.314 -5.360 1.00 6.92 O ANISOU 484 O PHE A 68 650 1184 795 -28 90 125 O ATOM 485 CB PHE A 68 22.870 5.068 -4.222 1.00 8.65 C ANISOU 485 CB PHE A 68 1084 1211 991 -23 -111 -283 C ATOM 486 CG PHE A 68 21.753 5.586 -3.361 1.00 8.71 C ANISOU 486 CG PHE A 68 1129 1223 957 -71 -110 -248 C ATOM 487 CD1 PHE A 68 21.255 4.810 -2.306 1.00 14.00 C ANISOU 487 CD1 PHE A 68 2698 1623 1000 537 563 75 C ATOM 488 CD2 PHE A 68 21.198 6.816 -3.599 1.00 8.21 C ANISOU 488 CD2 PHE A 68 907 1146 1066 -111 -202 -330 C ATOM 489 CE1 PHE A 68 20.223 5.266 -1.549 1.00 15.93 C ANISOU 489 CE1 PHE A 68 3048 1899 1104 719 846 250 C ATOM 490 CE2 PHE A 68 20.131 7.294 -2.826 1.00 8.64 C ANISOU 490 CE2 PHE A 68 1114 1170 999 -187 -174 -389 C ATOM 491 CZ PHE A 68 19.626 6.506 -1.810 1.00 10.83 C ANISOU 491 CZ PHE A 68 1661 1342 1112 -99 136 -310 C ATOM 492 N THR A 69 21.997 2.187 -4.491 1.00 6.99 N ANISOU 492 N THR A 69 697 1129 830 -120 28 167 N ATOM 493 CA THR A 69 21.257 1.059 -3.964 1.00 8.05 C ANISOU 493 CA THR A 69 803 1291 966 -179 -49 261 C ATOM 494 C THR A 69 21.756 0.804 -2.533 1.00 7.06 C ANISOU 494 C THR A 69 651 1099 932 40 -48 178 C ATOM 495 O THR A 69 22.983 0.828 -2.275 1.00 8.21 O ANISOU 495 O THR A 69 647 1445 1028 -195 -21 230 O ATOM 496 CB THR A 69 21.547 -0.197 -4.756 1.00 8.21 C ANISOU 496 CB THR A 69 901 1246 972 -176 -239 194 C ATOM 497 OG1 THR A 69 21.175 0.010 -6.118 1.00 8.96 O ANISOU 497 OG1 THR A 69 1127 1215 1061 -218 -167 139 O ATOM 498 CG2 THR A 69 20.786 -1.408 -4.261 1.00 9.80 C ANISOU 498 CG2 THR A 69 1203 1334 1186 -250 -152 269 C ATOM 499 N MET A 70 20.834 0.514 -1.617 1.00 8.14 N ANISOU 499 N MET A 70 721 1334 1040 -196 -68 387 N ATOM 500 CA MET A 70 21.138 0.026 -0.287 1.00 8.23 C ANISOU 500 CA MET A 70 870 1339 916 -193 -194 252 C ATOM 501 C MET A 70 20.423 -1.306 -0.094 1.00 7.08 C ANISOU 501 C MET A 70 629 1331 729 -48 -114 286 C ATOM 502 O MET A 70 19.185 -1.350 -0.229 1.00 8.60 O ANISOU 502 O MET A 70 600 1624 1042 -29 -161 333 O ATOM 503 CB MET A 70 20.669 0.993 0.753 1.00 12.83 C ANISOU 503 CB MET A 70 1635 1707 1534 -542 -41 -426 C ATOM 504 CG AMET A 70 21.133 2.418 0.841 0.53 8.27 C ANISOU 504 CG AMET A 70 863 1497 783 -256 -246 -94 C ATOM 505 CG BMET A 70 21.083 0.790 2.173 0.47 16.16 C ANISOU 505 CG BMET A 70 1703 3065 1371 284 281 -601 C ATOM 506 SD AMET A 70 20.411 3.674 1.938 0.53 9.36 S ANISOU 506 SD AMET A 70 1352 1319 886 -278 -102 -92 S ATOM 507 SD BMET A 70 20.670 2.491 2.692 0.47 17.16 S ANISOU 507 SD BMET A 70 2890 2306 1322 -856 -229 -552 S ATOM 508 CE AMET A 70 18.706 3.634 1.374 0.53 11.43 C ANISOU 508 CE AMET A 70 1160 1501 1684 -132 79 -483 C ATOM 509 CE BMET A 70 21.366 3.344 1.294 0.47 19.71 C ANISOU 509 CE BMET A 70 1618 3580 2291 -1387 91 -222 C ATOM 510 N GLU A 71 21.145 -2.372 0.265 1.00 7.13 N ANISOU 510 N GLU A 71 690 1291 729 -3 2 219 N ATOM 511 CA GLU A 71 20.546 -3.675 0.538 1.00 7.02 C ANISOU 511 CA GLU A 71 714 1268 685 81 -21 197 C ATOM 512 C GLU A 71 20.827 -4.043 1.968 1.00 6.52 C ANISOU 512 C GLU A 71 638 1194 646 35 -18 154 C ATOM 513 O GLU A 71 22.002 -4.229 2.361 1.00 7.87 O ANISOU 513 O GLU A 71 518 1759 714 41 -14 229 O ATOM 514 CB GLU A 71 21.110 -4.741 -0.391 1.00 7.88 C ANISOU 514 CB GLU A 71 911 1375 710 207 63 146 C ATOM 515 CG GLU A 71 20.814 -4.524 -1.846 1.00 9.96 C ANISOU 515 CG GLU A 71 1064 1964 755 333 -61 71 C ATOM 516 CD GLU A 71 21.353 -5.488 -2.825 1.00 9.17 C ANISOU 516 CD GLU A 71 1169 1532 782 85 -6 136 C ATOM 517 OE1 GLU A 71 22.080 -6.429 -2.412 1.00 13.55 O ANISOU 517 OE1 GLU A 71 2321 2041 785 838 -34 42 O ATOM 518 OE2 GLU A 71 21.060 -5.352 -4.027 1.00 11.68 O ANISOU 518 OE2 GLU A 71 1686 2010 742 103 -27 223 O ATOM 519 N TRP A 72 19.778 -4.203 2.758 1.00 6.36 N ANISOU 519 N TRP A 72 642 1223 552 100 -6 140 N ATOM 520 CA TRP A 72 19.892 -4.620 4.186 1.00 6.13 C ANISOU 520 CA TRP A 72 705 1106 519 156 -24 85 C ATOM 521 C TRP A 72 19.437 -6.043 4.316 1.00 5.72 C ANISOU 521 C TRP A 72 570 1136 469 204 -35 54 C ATOM 522 O TRP A 72 18.332 -6.392 3.882 1.00 6.69 O ANISOU 522 O TRP A 72 789 982 771 148 -157 141 O ATOM 523 CB TRP A 72 18.989 -3.715 5.028 1.00 6.92 C ANISOU 523 CB TRP A 72 797 1176 655 27 -4 -51 C ATOM 524 CG TRP A 72 19.444 -2.338 5.273 1.00 6.83 C ANISOU 524 CG TRP A 72 733 1081 781 69 34 -22 C ATOM 525 CD1 TRP A 72 19.056 -1.198 4.650 1.00 8.16 C ANISOU 525 CD1 TRP A 72 964 1190 946 94 -60 -74 C ATOM 526 CD2 TRP A 72 20.410 -1.914 6.279 1.00 7.00 C ANISOU 526 CD2 TRP A 72 671 1247 740 2 151 -80 C ATOM 527 NE1 TRP A 72 19.712 -0.099 5.182 1.00 8.57 N ANISOU 527 NE1 TRP A 72 1149 1208 898 -86 11 -16 N ATOM 528 CE2 TRP A 72 20.525 -0.525 6.187 1.00 8.23 C ANISOU 528 CE2 TRP A 72 1017 1270 840 -104 0 -165 C ATOM 529 CE3 TRP A 72 21.141 -2.640 7.248 1.00 8.03 C ANISOU 529 CE3 TRP A 72 794 1643 614 94 65 -112 C ATOM 530 CZ2 TRP A 72 21.379 0.213 7.038 1.00 8.43 C ANISOU 530 CZ2 TRP A 72 855 1555 793 -198 162 -313 C ATOM 531 CZ3 TRP A 72 21.983 -1.872 8.070 1.00 9.11 C ANISOU 531 CZ3 TRP A 72 795 1822 845 -59 82 -147 C ATOM 532 CH2 TRP A 72 22.083 -0.498 7.943 1.00 9.37 C ANISOU 532 CH2 TRP A 72 886 1797 878 -230 61 -257 C ATOM 533 N THR A 73 20.250 -6.854 4.997 1.00 6.54 N ANISOU 533 N THR A 73 798 1156 531 260 49 142 N ATOM 534 CA THR A 73 19.897 -8.237 5.284 1.00 6.79 C ANISOU 534 CA THR A 73 819 1206 556 258 45 110 C ATOM 535 C THR A 73 19.691 -8.337 6.828 1.00 6.46 C ANISOU 535 C THR A 73 729 1194 533 221 -23 149 C ATOM 536 O THR A 73 20.642 -8.109 7.583 1.00 7.32 O ANISOU 536 O THR A 73 632 1520 630 202 -114 158 O ATOM 537 CB THR A 73 21.016 -9.187 4.828 1.00 7.22 C ANISOU 537 CB THR A 73 774 1246 725 296 102 71 C ATOM 538 OG1 THR A 73 21.245 -9.029 3.436 1.00 8.64 O ANISOU 538 OG1 THR A 73 1100 1406 779 320 239 83 O ATOM 539 CG2 THR A 73 20.607 -10.629 5.068 1.00 9.37 C ANISOU 539 CG2 THR A 73 1253 1254 1051 329 251 198 C ATOM 540 N PHE A 74 18.461 -8.654 7.222 1.00 6.62 N ANISOU 540 N PHE A 74 768 1129 617 206 54 134 N ATOM 541 CA PHE A 74 18.101 -8.572 8.657 1.00 6.78 C ANISOU 541 CA PHE A 74 936 1204 437 115 34 23 C ATOM 542 C PHE A 74 17.146 -9.688 8.997 1.00 6.26 C ANISOU 542 C PHE A 74 769 1062 548 329 30 39 C ATOM 543 O PHE A 74 16.518 -10.292 8.119 1.00 6.38 O ANISOU 543 O PHE A 74 900 930 595 260 16 25 O ATOM 544 CB PHE A 74 17.524 -7.212 9.038 1.00 7.63 C ANISOU 544 CB PHE A 74 983 1200 714 143 -73 -99 C ATOM 545 CG PHE A 74 16.027 -7.121 8.737 1.00 7.35 C ANISOU 545 CG PHE A 74 1004 1084 705 217 -65 -147 C ATOM 546 CD1 PHE A 74 15.092 -7.237 9.771 1.00 8.18 C ANISOU 546 CD1 PHE A 74 1038 1182 889 318 64 -190 C ATOM 547 CD2 PHE A 74 15.553 -6.960 7.434 1.00 7.58 C ANISOU 547 CD2 PHE A 74 1152 850 879 123 -211 -44 C ATOM 548 CE1 PHE A 74 13.744 -7.216 9.518 1.00 8.73 C ANISOU 548 CE1 PHE A 74 1009 1190 1117 444 -4 -176 C ATOM 549 CE2 PHE A 74 14.202 -6.926 7.190 1.00 8.58 C ANISOU 549 CE2 PHE A 74 1098 1106 1057 355 -185 -22 C ATOM 550 CZ PHE A 74 13.279 -7.043 8.217 1.00 9.59 C ANISOU 550 CZ PHE A 74 1281 1380 982 655 -35 -135 C ATOM 551 N ARG A 75 16.949 -9.914 10.287 1.00 6.57 N ANISOU 551 N ARG A 75 682 1204 609 237 25 108 N ATOM 552 CA ARG A 75 15.903 -10.833 10.706 1.00 6.49 C ANISOU 552 CA ARG A 75 785 1065 617 238 37 37 C ATOM 553 C ARG A 75 15.370 -10.371 12.071 1.00 6.20 C ANISOU 553 C ARG A 75 811 913 631 273 22 131 C ATOM 554 O ARG A 75 15.956 -9.552 12.756 1.00 6.77 O ANISOU 554 O ARG A 75 755 1247 570 109 10 -21 O ATOM 555 CB ARG A 75 16.369 -12.299 10.785 1.00 7.42 C ANISOU 555 CB ARG A 75 976 1185 658 468 -64 50 C ATOM 556 CG ARG A 75 17.397 -12.550 11.909 1.00 8.72 C ANISOU 556 CG ARG A 75 1048 1391 875 525 -225 108 C ATOM 557 CD ARG A 75 17.821 -14.011 11.857 1.00 8.97 C ANISOU 557 CD ARG A 75 1152 1437 821 694 -58 180 C ATOM 558 NE ARG A 75 18.712 -14.237 13.026 1.00 10.13 N ANISOU 558 NE ARG A 75 1332 1707 811 716 -153 227 N ATOM 559 CZ ARG A 75 19.231 -15.399 13.303 1.00 11.60 C ANISOU 559 CZ ARG A 75 1941 1732 735 833 -151 301 C ATOM 560 NH1 ARG A 75 18.996 -16.440 12.535 1.00 11.17 N ANISOU 560 NH1 ARG A 75 1446 1635 1162 820 -256 255 N ATOM 561 NH2 ARG A 75 20.002 -15.504 14.386 1.00 13.01 N ANISOU 561 NH2 ARG A 75 1608 1936 1399 556 -576 317 N ATOM 562 N SER A 76 14.206 -10.967 12.383 1.00 5.87 N ANISOU 562 N SER A 76 790 922 520 209 24 97 N ATOM 563 CA SER A 76 13.631 -10.887 13.729 1.00 6.43 C ANISOU 563 CA SER A 76 915 987 542 329 87 130 C ATOM 564 C SER A 76 13.410 -12.307 14.214 1.00 6.57 C ANISOU 564 C SER A 76 941 982 574 351 115 93 C ATOM 565 O SER A 76 12.742 -13.112 13.537 1.00 6.97 O ANISOU 565 O SER A 76 943 1013 692 308 23 196 O ATOM 566 CB SER A 76 12.265 -10.160 13.690 1.00 6.91 C ANISOU 566 CB SER A 76 856 1007 764 278 205 228 C ATOM 567 OG SER A 76 11.680 -10.346 14.975 1.00 7.91 O ANISOU 567 OG SER A 76 1114 1197 694 402 241 212 O ATOM 568 N VAL A 77 13.971 -12.587 15.407 1.00 6.99 N ANISOU 568 N VAL A 77 949 1016 690 361 -26 217 N ATOM 569 CA VAL A 77 13.796 -13.915 16.007 1.00 7.68 C ANISOU 569 CA VAL A 77 1132 1076 711 346 125 239 C ATOM 570 C VAL A 77 13.350 -13.745 17.466 1.00 7.41 C ANISOU 570 C VAL A 77 1106 1041 667 329 -13 257 C ATOM 571 O VAL A 77 13.584 -12.719 18.098 1.00 8.08 O ANISOU 571 O VAL A 77 1185 1177 707 179 96 147 O ATOM 572 CB VAL A 77 15.079 -14.797 15.932 1.00 8.02 C ANISOU 572 CB VAL A 77 1294 1121 630 463 -7 178 C ATOM 573 CG1 VAL A 77 15.341 -15.163 14.471 1.00 9.91 C ANISOU 573 CG1 VAL A 77 1632 1455 679 703 92 59 C ATOM 574 CG2 VAL A 77 16.265 -14.079 16.540 1.00 9.70 C ANISOU 574 CG2 VAL A 77 1143 1338 1206 549 -160 -107 C ATOM 575 N GLY A 78 12.732 -14.819 17.973 1.00 7.86 N ANISOU 575 N GLY A 78 1101 1089 797 289 116 272 N ATOM 576 CA GLY A 78 12.489 -14.935 19.411 1.00 9.63 C ANISOU 576 CA GLY A 78 1255 1541 862 326 199 525 C ATOM 577 C GLY A 78 11.124 -14.529 19.886 1.00 8.91 C ANISOU 577 C GLY A 78 1194 1334 856 181 111 343 C ATOM 578 O GLY A 78 10.856 -14.739 21.094 1.00 10.77 O ANISOU 578 O GLY A 78 1502 1717 875 437 271 537 O ATOM 579 N TYR A 79 10.254 -13.999 19.016 1.00 8.53 N ANISOU 579 N TYR A 79 1169 1109 961 286 112 313 N ATOM 580 CA TYR A 79 8.949 -13.585 19.488 1.00 8.54 C ANISOU 580 CA TYR A 79 1164 1205 876 111 175 241 C ATOM 581 C TYR A 79 7.959 -13.498 18.299 1.00 8.03 C ANISOU 581 C TYR A 79 1071 1062 919 133 191 134 C ATOM 582 O TYR A 79 8.269 -12.991 17.243 1.00 9.47 O ANISOU 582 O TYR A 79 1064 1655 878 79 96 224 O ATOM 583 CB TYR A 79 8.990 -12.190 20.129 1.00 8.91 C ANISOU 583 CB TYR A 79 1193 1245 946 195 189 135 C ATOM 584 CG TYR A 79 7.671 -11.802 20.730 1.00 9.30 C ANISOU 584 CG TYR A 79 1334 1149 1051 130 268 50 C ATOM 585 CD1 TYR A 79 7.235 -12.416 21.903 1.00 12.89 C ANISOU 585 CD1 TYR A 79 2014 1331 1555 -107 766 270 C ATOM 586 CD2 TYR A 79 6.837 -10.863 20.136 1.00 9.95 C ANISOU 586 CD2 TYR A 79 1179 1557 1045 287 28 -126 C ATOM 587 CE1 TYR A 79 6.039 -12.100 22.476 1.00 15.72 C ANISOU 587 CE1 TYR A 79 2500 1603 1869 -363 1292 -284 C ATOM 588 CE2 TYR A 79 5.613 -10.559 20.737 1.00 13.04 C ANISOU 588 CE2 TYR A 79 1098 2301 1557 280 -100 -670 C ATOM 589 CZ TYR A 79 5.217 -11.171 21.893 1.00 14.60 C ANISOU 589 CZ TYR A 79 1304 2120 2124 -438 764 -947 C ATOM 590 OH TYR A 79 4.012 -10.836 22.450 1.00 22.57 O ANISOU 590 OH TYR A 79 1467 3454 3653 -677 1275 -1941 O ATOM 591 N SER A 80 6.759 -14.000 18.548 1.00 9.33 N ANISOU 591 N SER A 80 1086 1115 1346 80 147 100 N ATOM 592 CA SER A 80 5.654 -13.820 17.586 1.00 9.17 C ANISOU 592 CA SER A 80 1152 1018 1313 114 152 105 C ATOM 593 C SER A 80 4.484 -13.208 18.351 1.00 9.02 C ANISOU 593 C SER A 80 1145 1071 1210 59 322 273 C ATOM 594 O SER A 80 4.065 -13.734 19.364 1.00 11.23 O ANISOU 594 O SER A 80 1458 1304 1503 295 472 557 O ATOM 595 CB SER A 80 5.174 -15.195 17.112 1.00 14.30 C ANISOU 595 CB SER A 80 1382 1780 2272 28 92 -893 C ATOM 596 OG SER A 80 4.054 -15.082 16.270 1.00 19.65 O ANISOU 596 OG SER A 80 2102 2288 3075 134 -558 -1214 O ATOM 597 N GLY A 81 3.992 -12.100 17.831 1.00 8.49 N ANISOU 597 N GLY A 81 1194 974 1060 66 194 200 N ATOM 598 CA GLY A 81 2.843 -11.406 18.422 1.00 9.43 C ANISOU 598 CA GLY A 81 1244 1151 1189 110 197 105 C ATOM 599 C GLY A 81 2.980 -9.897 18.148 1.00 9.57 C ANISOU 599 C GLY A 81 1104 1120 1413 90 -303 -239 C ATOM 600 O GLY A 81 3.993 -9.325 17.874 1.00 10.29 O ANISOU 600 O GLY A 81 1813 1242 856 -236 -71 162 O ATOM 601 N GLN A 82 1.864 -9.222 18.111 1.00 11.82 N ANISOU 601 N GLN A 82 1580 1315 1594 233 7 -21 N ATOM 602 CA GLN A 82 1.889 -7.768 17.930 1.00 9.61 C ANISOU 602 CA GLN A 82 1037 1268 1347 10 -65 116 C ATOM 603 C GLN A 82 2.579 -7.069 19.054 1.00 9.89 C ANISOU 603 C GLN A 82 1281 1361 1116 -124 114 301 C ATOM 604 O GLN A 82 2.375 -7.350 20.231 1.00 11.47 O ANISOU 604 O GLN A 82 1786 1516 1055 25 129 250 O ATOM 605 CB GLN A 82 0.439 -7.284 17.776 1.00 11.44 C ANISOU 605 CB GLN A 82 1102 1712 1531 87 183 219 C ATOM 606 CG GLN A 82 0.523 -5.763 17.389 1.00 14.87 C ANISOU 606 CG GLN A 82 3194 1535 922 1112 -70 104 C ATOM 607 CD GLN A 82 -0.988 -5.454 17.095 1.00 18.09 C ANISOU 607 CD GLN A 82 3140 1753 1981 -60 -1378 666 C ATOM 608 OE1 GLN A 82 -1.401 -4.375 16.822 1.00 40.13 O ANISOU 608 OE1 GLN A 82 1511 2952 10784 -622 -956 3888 O ATOM 609 NE2 GLN A 82 -1.736 -6.582 17.112 1.00 29.69 N ANISOU 609 NE2 GLN A 82 4375 2363 4543 -942 471 346 N ATOM 610 N THR A 83 3.440 -6.123 18.785 1.00 10.95 N ANISOU 610 N THR A 83 1169 1052 1941 -114 -389 162 N ATOM 611 CA THR A 83 4.137 -5.360 19.838 1.00 8.59 C ANISOU 611 CA THR A 83 976 1199 1090 70 258 -156 C ATOM 612 C THR A 83 4.205 -3.963 19.316 1.00 7.26 C ANISOU 612 C THR A 83 643 1194 920 59 143 -142 C ATOM 613 O THR A 83 3.911 -3.708 18.132 1.00 8.08 O ANISOU 613 O THR A 83 790 1303 976 163 14 -193 O ATOM 614 CB THR A 83 5.583 -5.847 20.064 1.00 8.97 C ANISOU 614 CB THR A 83 1076 1377 957 116 -11 261 C ATOM 615 OG1 THR A 83 6.411 -5.332 19.081 1.00 13.90 O ANISOU 615 OG1 THR A 83 1092 1351 2838 124 686 551 O ATOM 616 CG2 THR A 83 5.605 -7.325 20.307 1.00 12.48 C ANISOU 616 CG2 THR A 83 1625 1496 1620 90 -204 583 C ATOM 617 N ASP A 84 4.635 -3.005 20.152 1.00 7.51 N ANISOU 617 N ASP A 84 919 1194 743 38 195 -132 N ATOM 618 CA ASP A 84 4.906 -1.658 19.731 1.00 8.17 C ANISOU 618 CA ASP A 84 1058 1163 884 10 115 -132 C ATOM 619 C ASP A 84 6.389 -1.432 19.381 1.00 7.76 C ANISOU 619 C ASP A 84 1151 1253 544 -169 154 -33 C ATOM 620 O ASP A 84 6.819 -0.305 19.199 1.00 9.32 O ANISOU 620 O ASP A 84 1606 1148 789 -211 279 -129 O ATOM 621 CB ASP A 84 4.356 -0.641 20.742 1.00 10.18 C ANISOU 621 CB ASP A 84 1340 1180 1348 -42 408 -268 C ATOM 622 CG ASP A 84 5.045 -0.733 22.100 1.00 12.57 C ANISOU 622 CG ASP A 84 1963 1805 1008 -357 541 -566 C ATOM 623 OD1 ASP A 84 6.121 -1.251 22.241 1.00 13.11 O ANISOU 623 OD1 ASP A 84 2390 1800 790 -130 62 -169 O ATOM 624 OD2 ASP A 84 4.415 -0.264 23.102 1.00 22.23 O ANISOU 624 OD2 ASP A 84 3487 3326 1632 84 1002 -1238 O ATOM 625 N GLY A 85 7.123 -2.539 19.251 1.00 7.30 N ANISOU 625 N GLY A 85 858 1319 598 -105 102 -15 N ATOM 626 CA GLY A 85 8.503 -2.483 18.776 1.00 8.60 C ANISOU 626 CA GLY A 85 913 1856 498 -207 168 23 C ATOM 627 C GLY A 85 8.534 -2.259 17.239 1.00 6.76 C ANISOU 627 C GLY A 85 836 1179 552 -197 18 45 C ATOM 628 O GLY A 85 7.526 -2.126 16.577 1.00 6.75 O ANISOU 628 O GLY A 85 778 1227 560 42 47 -8 O ATOM 629 N GLY A 86 9.762 -2.266 16.722 1.00 6.34 N ANISOU 629 N GLY A 86 793 1159 457 81 42 -14 N ATOM 630 CA GLY A 86 9.942 -2.189 15.270 1.00 6.97 C ANISOU 630 CA GLY A 86 816 1321 513 108 88 22 C ATOM 631 C GLY A 86 11.376 -1.894 14.944 1.00 6.10 C ANISOU 631 C GLY A 86 773 1079 464 -28 -13 -19 C ATOM 632 O GLY A 86 12.197 -1.593 15.841 1.00 7.34 O ANISOU 632 O GLY A 86 846 1475 469 67 20 -136 O ATOM 633 N ILE A 87 11.658 -2.002 13.663 1.00 6.16 N ANISOU 633 N ILE A 87 715 1109 517 9 33 -22 N ATOM 634 CA ILE A 87 13.027 -1.758 13.132 1.00 5.67 C ANISOU 634 CA ILE A 87 679 998 478 -111 57 1 C ATOM 635 C ILE A 87 12.886 -0.729 12.009 1.00 5.78 C ANISOU 635 C ILE A 87 710 1013 473 22 46 -50 C ATOM 636 O ILE A 87 11.994 -0.845 11.165 1.00 6.11 O ANISOU 636 O ILE A 87 695 1108 519 6 -115 -46 O ATOM 637 CB ILE A 87 13.734 -3.061 12.693 1.00 6.64 C ANISOU 637 CB ILE A 87 730 1139 655 108 -89 -112 C ATOM 638 CG1 ILE A 87 15.158 -2.781 12.173 1.00 6.40 C ANISOU 638 CG1 ILE A 87 764 1129 541 101 -72 -6 C ATOM 639 CG2 ILE A 87 12.933 -3.879 11.672 1.00 6.42 C ANISOU 639 CG2 ILE A 87 849 972 617 36 -120 -41 C ATOM 640 CD1 ILE A 87 16.009 -4.004 11.977 1.00 7.84 C ANISOU 640 CD1 ILE A 87 884 1302 793 331 38 104 C ATOM 641 N SER A 88 13.751 0.265 12.068 1.00 5.85 N ANISOU 641 N SER A 88 657 1017 550 -66 -4 -56 N ATOM 642 CA SER A 88 13.728 1.372 11.093 1.00 5.84 C ANISOU 642 CA SER A 88 765 882 573 42 88 -88 C ATOM 643 C SER A 88 15.069 1.484 10.393 1.00 5.36 C ANISOU 643 C SER A 88 668 781 589 21 -20 -79 C ATOM 644 O SER A 88 16.150 1.432 10.998 1.00 6.91 O ANISOU 644 O SER A 88 673 1333 618 -35 -45 7 O ATOM 645 CB SER A 88 13.489 2.674 11.826 1.00 7.25 C ANISOU 645 CB SER A 88 734 1109 913 13 34 -407 C ATOM 646 OG ASER A 88 12.130 2.836 12.202 0.61 5.74 O ANISOU 646 OG ASER A 88 624 942 614 111 55 -212 O ATOM 647 OG BSER A 88 13.167 3.808 11.194 0.39 10.14 O ANISOU 647 OG BSER A 88 1414 944 1496 -112 203 -130 O ATOM 648 N PHE A 89 14.983 1.676 9.073 1.00 5.64 N ANISOU 648 N PHE A 89 668 948 528 -44 18 -114 N ATOM 649 CA PHE A 89 16.133 1.872 8.188 1.00 5.40 C ANISOU 649 CA PHE A 89 485 967 600 -42 10 -34 C ATOM 650 C PHE A 89 16.082 3.301 7.681 1.00 5.95 C ANISOU 650 C PHE A 89 616 894 748 -46 -35 -84 C ATOM 651 O PHE A 89 15.039 3.744 7.219 1.00 7.42 O ANISOU 651 O PHE A 89 655 1025 1141 -93 -193 234 O ATOM 652 CB PHE A 89 16.107 0.877 7.014 1.00 6.17 C ANISOU 652 CB PHE A 89 772 987 586 -31 14 -115 C ATOM 653 CG PHE A 89 16.010 -0.557 7.459 1.00 6.00 C ANISOU 653 CG PHE A 89 753 1050 478 41 -89 -91 C ATOM 654 CD1 PHE A 89 17.144 -1.324 7.637 1.00 6.83 C ANISOU 654 CD1 PHE A 89 945 1198 452 226 -71 -132 C ATOM 655 CD2 PHE A 89 14.765 -1.166 7.684 1.00 6.67 C ANISOU 655 CD2 PHE A 89 901 956 676 -60 -70 -167 C ATOM 656 CE1 PHE A 89 17.072 -2.638 8.044 1.00 8.13 C ANISOU 656 CE1 PHE A 89 1279 1171 638 275 -139 -176 C ATOM 657 CE2 PHE A 89 14.675 -2.460 8.137 1.00 7.77 C ANISOU 657 CE2 PHE A 89 1236 994 725 -105 25 -187 C ATOM 658 CZ PHE A 89 15.851 -3.205 8.297 1.00 8.41 C ANISOU 658 CZ PHE A 89 1534 1038 623 129 -146 -162 C ATOM 659 N TRP A 90 17.204 4.010 7.802 1.00 5.86 N ANISOU 659 N TRP A 90 628 968 629 -112 108 26 N ATOM 660 CA TRP A 90 17.199 5.454 7.637 1.00 6.43 C ANISOU 660 CA TRP A 90 882 888 673 -155 76 -74 C ATOM 661 C TRP A 90 18.084 5.917 6.472 1.00 5.91 C ANISOU 661 C TRP A 90 649 974 623 -181 66 -68 C ATOM 662 O TRP A 90 19.159 5.339 6.250 1.00 7.04 O ANISOU 662 O TRP A 90 714 1068 892 -104 62 -80 O ATOM 663 CB TRP A 90 17.741 6.120 8.904 1.00 7.12 C ANISOU 663 CB TRP A 90 899 1148 658 -243 46 -206 C ATOM 664 CG TRP A 90 16.975 5.771 10.149 1.00 6.65 C ANISOU 664 CG TRP A 90 744 1076 707 -108 -89 -122 C ATOM 665 CD1 TRP A 90 17.254 4.736 11.009 1.00 7.38 C ANISOU 665 CD1 TRP A 90 788 1239 779 -115 67 -23 C ATOM 666 CD2 TRP A 90 15.819 6.450 10.671 1.00 6.60 C ANISOU 666 CD2 TRP A 90 822 934 752 -233 29 -220 C ATOM 667 NE1 TRP A 90 16.330 4.729 12.059 1.00 7.13 N ANISOU 667 NE1 TRP A 90 827 1172 712 -94 9 -174 N ATOM 668 CE2 TRP A 90 15.468 5.771 11.867 1.00 6.86 C ANISOU 668 CE2 TRP A 90 796 1132 679 -126 -31 -219 C ATOM 669 CE3 TRP A 90 15.071 7.568 10.262 1.00 7.48 C ANISOU 669 CE3 TRP A 90 888 875 1081 -74 54 -183 C ATOM 670 CZ2 TRP A 90 14.373 6.173 12.669 1.00 7.49 C ANISOU 670 CZ2 TRP A 90 941 1156 751 -172 104 -314 C ATOM 671 CZ3 TRP A 90 14.012 7.956 11.060 1.00 8.59 C ANISOU 671 CZ3 TRP A 90 1099 1019 1147 -115 86 -228 C ATOM 672 CH2 TRP A 90 13.664 7.268 12.245 1.00 8.36 C ANISOU 672 CH2 TRP A 90 960 1104 1114 -153 113 -257 C ATOM 673 N PHE A 91 17.653 6.970 5.832 1.00 6.32 N ANISOU 673 N PHE A 91 789 933 680 -134 -9 -63 N ATOM 674 CA PHE A 91 18.436 7.696 4.833 1.00 6.36 C ANISOU 674 CA PHE A 91 878 815 723 -141 117 -82 C ATOM 675 C PHE A 91 18.081 9.185 5.027 1.00 6.31 C ANISOU 675 C PHE A 91 777 884 737 -55 44 -68 C ATOM 676 O PHE A 91 17.075 9.632 4.514 1.00 6.83 O ANISOU 676 O PHE A 91 799 934 863 -81 43 -137 O ATOM 677 CB PHE A 91 18.097 7.161 3.435 1.00 6.99 C ANISOU 677 CB PHE A 91 873 1037 748 -301 49 -135 C ATOM 678 CG PHE A 91 18.834 7.903 2.313 1.00 6.93 C ANISOU 678 CG PHE A 91 997 944 691 -296 11 -161 C ATOM 679 CD1 PHE A 91 20.190 7.623 2.119 1.00 8.62 C ANISOU 679 CD1 PHE A 91 925 1634 717 -279 90 -183 C ATOM 680 CD2 PHE A 91 18.205 8.834 1.484 1.00 8.48 C ANISOU 680 CD2 PHE A 91 1491 903 828 -77 -1 -90 C ATOM 681 CE1 PHE A 91 20.918 8.259 1.108 1.00 9.94 C ANISOU 681 CE1 PHE A 91 1209 1726 842 -650 84 -264 C ATOM 682 CE2 PHE A 91 18.909 9.442 0.488 1.00 10.20 C ANISOU 682 CE2 PHE A 91 2057 1068 751 -123 165 -94 C ATOM 683 CZ PHE A 91 20.267 9.144 0.286 1.00 10.70 C ANISOU 683 CZ PHE A 91 1850 1378 836 -592 111 -277 C ATOM 684 N VAL A 92 18.887 9.869 5.839 1.00 7.13 N ANISOU 684 N VAL A 92 883 901 924 -156 123 -263 N ATOM 685 CA VAL A 92 18.444 11.169 6.363 1.00 6.99 C ANISOU 685 CA VAL A 92 794 842 1020 -172 50 -126 C ATOM 686 C VAL A 92 19.601 12.209 6.349 1.00 7.08 C ANISOU 686 C VAL A 92 792 906 992 -172 80 -243 C ATOM 687 O VAL A 92 20.749 11.859 6.633 1.00 8.68 O ANISOU 687 O VAL A 92 824 1118 1356 -220 10 -183 O ATOM 688 CB VAL A 92 17.867 11.073 7.802 1.00 7.35 C ANISOU 688 CB VAL A 92 899 908 986 -147 90 -197 C ATOM 689 CG1 VAL A 92 16.652 10.114 7.829 1.00 8.53 C ANISOU 689 CG1 VAL A 92 977 1026 1240 -203 299 -327 C ATOM 690 CG2 VAL A 92 18.881 10.597 8.819 1.00 9.62 C ANISOU 690 CG2 VAL A 92 1153 1609 892 -316 16 5 C ATOM 691 N GLN A 93 19.258 13.440 6.056 1.00 7.89 N ANISOU 691 N GLN A 93 1035 856 1108 -317 105 -174 N ATOM 692 CA GLN A 93 20.313 14.481 5.990 1.00 9.65 C ANISOU 692 CA GLN A 93 1189 908 1571 -435 -53 -277 C ATOM 693 C GLN A 93 20.662 14.954 7.381 1.00 9.50 C ANISOU 693 C GLN A 93 1150 1090 1369 -421 36 -217 C ATOM 694 O GLN A 93 19.804 15.372 8.141 1.00 11.60 O ANISOU 694 O GLN A 93 1261 1287 1860 -275 26 -652 O ATOM 695 CB GLN A 93 19.801 15.678 5.206 1.00 12.08 C ANISOU 695 CB GLN A 93 1757 1299 1534 -695 -26 345 C ATOM 696 CG GLN A 93 19.484 15.521 3.782 1.00 15.22 C ANISOU 696 CG GLN A 93 2164 2080 1539 -72 -51 -228 C ATOM 697 CD GLN A 93 18.845 16.816 3.255 1.00 18.91 C ANISOU 697 CD GLN A 93 3239 2278 1669 -138 -250 476 C ATOM 698 OE1 GLN A 93 19.464 17.884 3.318 1.00 31.30 O ANISOU 698 OE1 GLN A 93 7053 2168 2671 -1163 1460 -235 O ATOM 699 NE2 GLN A 93 17.611 16.675 2.775 1.00 30.44 N ANISOU 699 NE2 GLN A 93 3250 6322 1996 1372 -818 149 N ATOM 700 N ASP A 94 21.953 14.913 7.716 1.00 10.08 N ANISOU 700 N ASP A 94 1183 1137 1509 -431 -108 -334 N ATOM 701 CA ASP A 94 22.449 15.463 8.984 1.00 10.38 C ANISOU 701 CA ASP A 94 1371 1337 1235 -352 -191 -111 C ATOM 702 C ASP A 94 23.979 15.601 8.820 1.00 10.92 C ANISOU 702 C ASP A 94 1367 1399 1383 -519 -240 -134 C ATOM 703 O ASP A 94 24.566 14.953 7.964 1.00 13.00 O ANISOU 703 O ASP A 94 1275 1872 1793 -612 -101 -446 O ATOM 704 CB ASP A 94 22.081 14.573 10.139 1.00 11.12 C ANISOU 704 CB ASP A 94 1643 1240 1340 -493 74 -406 C ATOM 705 CG ASP A 94 21.983 15.241 11.490 1.00 12.23 C ANISOU 705 CG ASP A 94 2031 1437 1177 -389 -64 -347 C ATOM 706 OD1 ASP A 94 22.698 16.246 11.664 1.00 17.91 O ANISOU 706 OD1 ASP A 94 2693 2262 1852 -1188 565 -1080 O ATOM 707 OD2 ASP A 94 21.194 14.799 12.324 1.00 12.99 O ANISOU 707 OD2 ASP A 94 1850 1842 1243 -466 -41 -352 O ATOM 708 N SER A 95 24.565 16.407 9.647 1.00 13.17 N ANISOU 708 N SER A 95 1693 1672 1637 -757 -300 -258 N ATOM 709 CA SER A 95 26.028 16.611 9.614 1.00 14.33 C ANISOU 709 CA SER A 95 1807 1974 1662 -996 -408 -165 C ATOM 710 C SER A 95 26.749 15.633 10.524 1.00 13.02 C ANISOU 710 C SER A 95 1574 1856 1517 -898 -135 -216 C ATOM 711 O SER A 95 27.997 15.655 10.603 1.00 17.38 O ANISOU 711 O SER A 95 1564 2910 2129 -859 -44 374 O ATOM 712 CB SER A 95 26.325 18.075 9.985 1.00 18.83 C ANISOU 712 CB SER A 95 1767 1817 3570 -713 -507 -455 C ATOM 713 OG SER A 95 25.831 18.273 11.309 1.00 25.67 O ANISOU 713 OG SER A 95 2940 2873 3943 -417 -338 -1793 O ATOM 714 N ASN A 96 26.029 14.829 11.280 1.00 12.29 N ANISOU 714 N ASN A 96 1462 1820 1389 -682 -100 -250 N ATOM 715 CA ASN A 96 26.605 13.819 12.144 1.00 11.97 C ANISOU 715 CA ASN A 96 1476 1986 1086 -718 -248 -279 C ATOM 716 C ASN A 96 25.636 12.660 12.208 1.00 10.33 C ANISOU 716 C ASN A 96 1190 1598 1137 -350 9 -452 C ATOM 717 O ASN A 96 24.483 12.788 11.727 1.00 10.55 O ANISOU 717 O ASN A 96 1249 1671 1091 -483 -112 -382 O ATOM 718 CB ASN A 96 26.827 14.376 13.577 1.00 13.49 C ANISOU 718 CB ASN A 96 1946 1865 1313 -552 -169 -630 C ATOM 719 CG ASN A 96 25.791 15.406 13.900 1.00 15.51 C ANISOU 719 CG ASN A 96 2138 1978 1779 -301 -69 -306 C ATOM 720 OD1 ASN A 96 26.077 16.614 13.802 1.00 25.60 O ANISOU 720 OD1 ASN A 96 3646 1885 4194 -410 1590 -647 O ATOM 721 ND2 ASN A 96 24.587 14.964 14.275 1.00 17.16 N ANISOU 721 ND2 ASN A 96 2005 2288 2225 -409 -118 -801 N ATOM 722 N ILE A 97 25.995 11.573 12.848 1.00 10.31 N ANISOU 722 N ILE A 97 1204 1709 1006 -267 50 -462 N ATOM 723 CA ILE A 97 24.985 10.568 13.166 1.00 10.36 C ANISOU 723 CA ILE A 97 1204 1733 999 -148 130 -272 C ATOM 724 C ILE A 97 23.856 11.251 13.922 1.00 9.40 C ANISOU 724 C ILE A 97 1190 1424 956 -262 3 -360 C ATOM 725 O ILE A 97 24.149 12.030 14.849 1.00 10.82 O ANISOU 725 O ILE A 97 1253 1714 1143 -467 143 -572 O ATOM 726 CB ILE A 97 25.612 9.428 13.992 1.00 11.11 C ANISOU 726 CB ILE A 97 1336 1635 1252 -186 -53 -341 C ATOM 727 CG1 ILE A 97 26.653 8.626 13.191 1.00 11.16 C ANISOU 727 CG1 ILE A 97 1228 1820 1191 -66 -58 -275 C ATOM 728 CG2 ILE A 97 24.550 8.506 14.597 1.00 11.88 C ANISOU 728 CG2 ILE A 97 1640 1792 1081 -399 100 -319 C ATOM 729 CD1 ILE A 97 27.432 7.597 13.978 1.00 14.06 C ANISOU 729 CD1 ILE A 97 1455 2365 1522 208 26 3 C ATOM 730 N PRO A 98 22.607 11.044 13.547 1.00 9.41 N ANISOU 730 N PRO A 98 1208 1290 1078 -263 -6 -404 N ATOM 731 CA PRO A 98 21.552 11.835 14.183 1.00 10.16 C ANISOU 731 CA PRO A 98 1137 1521 1202 -322 164 -360 C ATOM 732 C PRO A 98 21.530 11.657 15.682 1.00 9.57 C ANISOU 732 C PRO A 98 999 1372 1266 -252 86 -467 C ATOM 733 O PRO A 98 21.650 10.531 16.200 1.00 9.99 O ANISOU 733 O PRO A 98 1162 1509 1125 -291 -64 -408 O ATOM 734 CB PRO A 98 20.282 11.278 13.501 1.00 10.54 C ANISOU 734 CB PRO A 98 1167 1553 1285 -163 -135 -355 C ATOM 735 CG PRO A 98 20.790 10.885 12.143 1.00 10.83 C ANISOU 735 CG PRO A 98 1216 1551 1348 -318 -144 -440 C ATOM 736 CD PRO A 98 22.116 10.194 12.429 1.00 9.65 C ANISOU 736 CD PRO A 98 1287 1436 943 -325 -87 -305 C ATOM 737 N ARG A 99 21.327 12.781 16.392 1.00 11.76 N ANISOU 737 N ARG A 99 1258 1647 1565 -434 176 -859 N ATOM 738 CA ARG A 99 21.321 12.692 17.840 1.00 13.82 C ANISOU 738 CA ARG A 99 1452 2277 1521 -543 45 -1091 C ATOM 739 C ARG A 99 20.021 12.161 18.437 1.00 12.15 C ANISOU 739 C ARG A 99 1384 2067 1164 -251 -39 -815 C ATOM 740 O ARG A 99 19.994 11.524 19.506 1.00 14.41 O ANISOU 740 O ARG A 99 1608 2709 1158 -242 -42 -701 O ATOM 741 CB ARG A 99 21.593 14.136 18.366 1.00 16.39 C ANISOU 741 CB ARG A 99 1706 2438 2085 -673 360 -1514 C ATOM 742 CG ARG A 99 23.025 14.653 18.034 1.00 16.18 C ANISOU 742 CG ARG A 99 1647 2211 2292 -537 28 -1117 C ATOM 743 CD ARG A 99 23.161 16.104 18.552 1.00 22.51 C ANISOU 743 CD ARG A 99 2617 1974 3961 -690 -616 -1048 C ATOM 744 NE ARG A 99 24.375 16.704 18.018 1.00 27.52 N ANISOU 744 NE ARG A 99 3535 2307 4616 -1211 -172 -758 N ATOM 745 CZ ARG A 99 24.612 17.346 16.889 1.00 34.77 C ANISOU 745 CZ ARG A 99 5223 3318 4669 -2162 -2 -700 C ATOM 746 NH1 ARG A 99 25.850 17.783 16.644 1.00 40.23 N ANISOU 746 NH1 ARG A 99 5971 4182 5131 -2536 2326 -2803 N ATOM 747 NH2 ARG A 99 23.688 17.599 15.967 1.00 47.86 N ANISOU 747 NH2 ARG A 99 7425 5664 5094 -1017 -770 532 N ATOM 748 N ASP A 100 18.909 12.483 17.808 1.00 11.27 N ANISOU 748 N ASP A 100 1295 1543 1443 -244 90 -749 N ATOM 749 CA ASP A 100 17.586 12.212 18.395 1.00 9.55 C ANISOU 749 CA ASP A 100 1367 1285 977 -168 12 -312 C ATOM 750 C ASP A 100 17.268 10.710 18.329 1.00 9.40 C ANISOU 750 C ASP A 100 1340 1268 964 -112 60 -319 C ATOM 751 O ASP A 100 17.545 10.075 17.316 1.00 9.88 O ANISOU 751 O ASP A 100 1352 1440 961 -342 137 -414 O ATOM 752 CB ASP A 100 16.511 13.049 17.729 1.00 9.95 C ANISOU 752 CB ASP A 100 1372 1295 1114 -48 13 -362 C ATOM 753 CG ASP A 100 15.158 12.879 18.409 1.00 9.95 C ANISOU 753 CG ASP A 100 1328 1289 1162 -87 -93 -603 C ATOM 754 OD1 ASP A 100 14.900 13.678 19.328 1.00 15.57 O ANISOU 754 OD1 ASP A 100 1581 2114 2222 -394 477 -1351 O ATOM 755 OD2 ASP A 100 14.412 11.959 18.071 1.00 9.33 O ANISOU 755 OD2 ASP A 100 1334 1257 953 -100 -92 -264 O ATOM 756 N LYS A 101 16.679 10.194 19.398 1.00 9.19 N ANISOU 756 N LYS A 101 1218 1408 864 -188 -123 -225 N ATOM 757 CA LYS A 101 16.395 8.786 19.589 1.00 9.36 C ANISOU 757 CA LYS A 101 1301 1343 913 10 13 -48 C ATOM 758 C LYS A 101 14.911 8.514 19.793 1.00 8.40 C ANISOU 758 C LYS A 101 1318 1297 578 -76 -33 -275 C ATOM 759 O LYS A 101 14.593 7.415 20.263 1.00 9.26 O ANISOU 759 O LYS A 101 1351 1440 729 -80 52 -124 O ATOM 760 CB LYS A 101 17.210 8.222 20.726 1.00 11.27 C ANISOU 760 CB LYS A 101 1377 1978 927 -12 -153 -35 C ATOM 761 CG LYS A 101 18.714 8.487 20.670 1.00 11.62 C ANISOU 761 CG LYS A 101 1329 2247 841 -101 -50 -380 C ATOM 762 CD LYS A 101 19.381 7.573 19.634 1.00 11.21 C ANISOU 762 CD LYS A 101 1447 1745 1069 -186 -125 -479 C ATOM 763 CE LYS A 101 20.833 7.998 19.444 1.00 13.59 C ANISOU 763 CE LYS A 101 1388 2279 1498 -83 143 -878 C ATOM 764 NZ LYS A 101 21.679 6.913 18.836 1.00 12.79 N ANISOU 764 NZ LYS A 101 1498 2115 1248 190 -245 -581 N ATOM 765 N GLN A 102 14.024 9.429 19.521 1.00 9.09 N ANISOU 765 N GLN A 102 1224 1414 818 8 47 -443 N ATOM 766 CA GLN A 102 12.654 9.286 19.931 1.00 10.02 C ANISOU 766 CA GLN A 102 1285 1646 876 35 218 -478 C ATOM 767 C GLN A 102 11.749 8.502 19.020 1.00 9.53 C ANISOU 767 C GLN A 102 1214 1589 820 -62 98 -340 C ATOM 768 O GLN A 102 10.573 8.256 19.391 1.00 12.93 O ANISOU 768 O GLN A 102 1300 2361 1253 -156 313 -825 O ATOM 769 CB GLN A 102 12.030 10.682 20.116 1.00 9.99 C ANISOU 769 CB GLN A 102 1486 1405 906 81 80 -226 C ATOM 770 CG GLN A 102 12.683 11.519 21.200 1.00 12.17 C ANISOU 770 CG GLN A 102 1963 1695 966 72 232 -529 C ATOM 771 CD GLN A 102 11.995 12.850 21.371 1.00 15.27 C ANISOU 771 CD GLN A 102 3026 1500 1276 92 1076 -362 C ATOM 772 OE1 GLN A 102 10.916 12.907 22.003 1.00 19.66 O ANISOU 772 OE1 GLN A 102 3277 1682 2512 408 1645 -117 O ATOM 773 NE2 GLN A 102 12.523 13.908 20.736 1.00 13.54 N ANISOU 773 NE2 GLN A 102 2199 1739 1208 -290 142 -206 N ATOM 774 N LEU A 103 12.215 8.066 17.848 1.00 8.13 N ANISOU 774 N LEU A 103 1118 1239 732 5 86 -254 N ATOM 775 CA LEU A 103 11.362 7.342 16.891 1.00 7.92 C ANISOU 775 CA LEU A 103 947 1247 815 87 11 -178 C ATOM 776 C LEU A 103 12.048 6.024 16.549 1.00 7.53 C ANISOU 776 C LEU A 103 892 1231 737 0 32 -217 C ATOM 777 O LEU A 103 13.008 5.990 15.788 1.00 7.76 O ANISOU 777 O LEU A 103 893 1356 699 -136 78 -211 O ATOM 778 CB LEU A 103 11.182 8.226 15.645 1.00 8.24 C ANISOU 778 CB LEU A 103 1169 1160 802 -37 9 -210 C ATOM 779 CG LEU A 103 10.342 7.588 14.504 1.00 8.40 C ANISOU 779 CG LEU A 103 929 1330 933 1 -70 -264 C ATOM 780 CD1 LEU A 103 8.962 7.181 15.019 1.00 9.25 C ANISOU 780 CD1 LEU A 103 1027 1229 1259 -21 -27 -320 C ATOM 781 CD2 LEU A 103 10.274 8.578 13.365 1.00 9.09 C ANISOU 781 CD2 LEU A 103 1324 1229 900 217 -90 -238 C ATOM 782 N TYR A 104 11.592 4.931 17.209 1.00 7.34 N ANISOU 782 N TYR A 104 966 1209 615 10 59 -193 N ATOM 783 CA TYR A 104 12.246 3.626 17.049 1.00 7.74 C ANISOU 783 CA TYR A 104 1010 1237 692 24 -62 -261 C ATOM 784 C TYR A 104 13.743 3.755 17.255 1.00 7.34 C ANISOU 784 C TYR A 104 1005 1292 491 84 18 -96 C ATOM 785 O TYR A 104 14.583 3.108 16.575 1.00 8.18 O ANISOU 785 O TYR A 104 986 1538 585 23 40 -215 O ATOM 786 CB TYR A 104 11.948 2.937 15.645 1.00 7.97 C ANISOU 786 CB TYR A 104 965 1533 529 -89 14 -221 C ATOM 787 CG TYR A 104 10.452 2.711 15.534 1.00 6.96 C ANISOU 787 CG TYR A 104 1013 1079 551 -29 87 -191 C ATOM 788 CD1 TYR A 104 9.878 1.561 16.051 1.00 7.44 C ANISOU 788 CD1 TYR A 104 950 1105 771 25 25 -178 C ATOM 789 CD2 TYR A 104 9.603 3.671 15.008 1.00 7.62 C ANISOU 789 CD2 TYR A 104 971 1122 803 -9 -22 -187 C ATOM 790 CE1 TYR A 104 8.518 1.346 15.995 1.00 7.20 C ANISOU 790 CE1 TYR A 104 1047 1051 639 -63 -73 -166 C ATOM 791 CE2 TYR A 104 8.235 3.475 14.961 1.00 7.74 C ANISOU 791 CE2 TYR A 104 920 1162 860 -66 25 -241 C ATOM 792 CZ TYR A 104 7.706 2.299 15.475 1.00 7.30 C ANISOU 792 CZ TYR A 104 828 1170 777 65 -8 -200 C ATOM 793 OH TYR A 104 6.323 2.151 15.404 1.00 8.49 O ANISOU 793 OH TYR A 104 913 1178 1134 -23 71 -167 O ATOM 794 N ASN A 105 14.144 4.508 18.285 1.00 8.01 N ANISOU 794 N ASN A 105 1019 1236 788 -81 19 -214 N ATOM 795 CA ASN A 105 15.558 4.722 18.638 1.00 8.16 C ANISOU 795 CA ASN A 105 1070 1404 627 -93 -81 -52 C ATOM 796 C ASN A 105 16.365 5.411 17.549 1.00 7.45 C ANISOU 796 C ASN A 105 994 1166 670 -15 47 -236 C ATOM 797 O ASN A 105 17.579 5.303 17.543 1.00 8.41 O ANISOU 797 O ASN A 105 966 1569 662 -21 43 -248 O ATOM 798 CB ASN A 105 16.187 3.397 19.097 1.00 8.06 C ANISOU 798 CB ASN A 105 1050 1333 682 -100 32 -167 C ATOM 799 CG ASN A 105 17.555 3.653 19.775 1.00 8.86 C ANISOU 799 CG ASN A 105 1056 1583 728 153 -101 -238 C ATOM 800 OD1 ASN A 105 17.645 4.543 20.654 1.00 9.56 O ANISOU 800 OD1 ASN A 105 1279 1739 615 98 -62 -309 O ATOM 801 ND2 ASN A 105 18.553 2.900 19.397 1.00 9.20 N ANISOU 801 ND2 ASN A 105 1112 1636 747 224 -37 -139 N ATOM 802 N GLY A 106 15.674 6.170 16.713 1.00 8.61 N ANISOU 802 N GLY A 106 1105 1365 802 -146 -59 44 N ATOM 803 CA GLY A 106 16.224 7.047 15.721 1.00 7.74 C ANISOU 803 CA GLY A 106 946 1189 805 -131 1 -53 C ATOM 804 C GLY A 106 15.504 8.396 15.739 1.00 7.39 C ANISOU 804 C GLY A 106 1013 1045 750 -213 -26 -271 C ATOM 805 O GLY A 106 14.736 8.670 16.661 1.00 8.86 O ANISOU 805 O GLY A 106 1166 1427 774 -104 96 -270 O ATOM 806 N PRO A 107 15.816 9.261 14.785 1.00 7.46 N ANISOU 806 N PRO A 107 932 1069 833 -192 40 -179 N ATOM 807 CA PRO A 107 15.397 10.664 14.901 1.00 7.75 C ANISOU 807 CA PRO A 107 1087 1038 819 -64 -9 -210 C ATOM 808 C PRO A 107 13.952 10.910 14.522 1.00 8.41 C ANISOU 808 C PRO A 107 1025 1195 974 -139 -22 -399 C ATOM 809 O PRO A 107 13.528 10.630 13.423 1.00 9.42 O ANISOU 809 O PRO A 107 1070 1532 977 41 -72 -520 O ATOM 810 CB PRO A 107 16.363 11.384 13.948 1.00 9.14 C ANISOU 810 CB PRO A 107 1207 1263 1001 -320 114 -230 C ATOM 811 CG PRO A 107 16.671 10.302 12.908 1.00 8.15 C ANISOU 811 CG PRO A 107 1233 1014 848 -186 78 -107 C ATOM 812 CD PRO A 107 16.774 9.042 13.696 1.00 7.42 C ANISOU 812 CD PRO A 107 850 1233 737 -84 9 -170 C ATOM 813 N VAL A 108 13.191 11.548 15.437 1.00 8.36 N ANISOU 813 N VAL A 108 1147 1039 991 -12 52 -363 N ATOM 814 CA VAL A 108 11.777 11.862 15.175 1.00 8.48 C ANISOU 814 CA VAL A 108 1084 1260 880 38 14 -367 C ATOM 815 C VAL A 108 11.561 13.073 14.317 1.00 9.06 C ANISOU 815 C VAL A 108 1290 1103 1050 170 74 -430 C ATOM 816 O VAL A 108 10.505 13.236 13.701 1.00 10.16 O ANISOU 816 O VAL A 108 1354 1212 1295 186 44 -191 O ATOM 817 CB VAL A 108 11.033 11.990 16.546 1.00 9.71 C ANISOU 817 CB VAL A 108 1269 1361 1060 32 182 -470 C ATOM 818 CG1 VAL A 108 11.381 13.283 17.273 1.00 10.89 C ANISOU 818 CG1 VAL A 108 1614 1377 1146 -166 139 -537 C ATOM 819 CG2 VAL A 108 9.511 11.896 16.385 1.00 10.60 C ANISOU 819 CG2 VAL A 108 1166 1584 1279 -129 207 -413 C ATOM 820 N ASN A 109 12.563 13.937 14.206 1.00 9.85 N ANISOU 820 N ASN A 109 1692 1108 942 -15 -107 -299 N ATOM 821 CA ASN A 109 12.550 15.141 13.398 1.00 11.65 C ANISOU 821 CA ASN A 109 2374 929 1124 115 339 -330 C ATOM 822 C ASN A 109 13.521 15.010 12.256 1.00 10.15 C ANISOU 822 C ASN A 109 1594 1024 1241 36 97 -285 C ATOM 823 O ASN A 109 14.251 15.947 11.969 1.00 12.72 O ANISOU 823 O ASN A 109 2080 1209 1545 -221 231 -446 O ATOM 824 CB ASN A 109 13.082 16.235 14.358 1.00 17.38 C ANISOU 824 CB ASN A 109 3546 1487 1572 -683 748 -706 C ATOM 825 CG ASN A 109 14.527 15.880 14.840 1.00 28.10 C ANISOU 825 CG ASN A 109 4563 2121 3994 -571 -1429 -1800 C ATOM 826 OD1 ASN A 109 15.025 14.717 15.003 1.00 19.95 O ANISOU 826 OD1 ASN A 109 2995 2235 2353 -711 24 -1364 O ATOM 827 ND2 ASN A 109 15.352 16.925 15.077 1.00 45.28 N ANISOU 827 ND2 ASN A 109 5463 2381 9360 -1550 -3122 445 N ATOM 828 N TYR A 110 13.527 13.837 11.619 1.00 10.51 N ANISOU 828 N TYR A 110 1604 1278 1111 -169 237 -531 N ATOM 829 CA TYR A 110 14.493 13.592 10.502 1.00 9.62 C ANISOU 829 CA TYR A 110 1428 1113 1113 -134 203 -257 C ATOM 830 C TYR A 110 14.120 14.378 9.265 1.00 8.80 C ANISOU 830 C TYR A 110 1251 962 1129 -9 79 -357 C ATOM 831 O TYR A 110 12.974 14.784 9.087 1.00 9.84 O ANISOU 831 O TYR A 110 1272 1093 1373 -101 14 -380 O ATOM 832 CB TYR A 110 14.517 12.080 10.242 1.00 8.67 C ANISOU 832 CB TYR A 110 1201 1000 1092 -13 -1 -305 C ATOM 833 CG TYR A 110 13.238 11.542 9.701 1.00 7.87 C ANISOU 833 CG TYR A 110 1144 891 956 79 51 -108 C ATOM 834 CD1 TYR A 110 13.006 11.344 8.327 1.00 7.63 C ANISOU 834 CD1 TYR A 110 1074 853 973 27 80 -210 C ATOM 835 CD2 TYR A 110 12.197 11.179 10.590 1.00 8.19 C ANISOU 835 CD2 TYR A 110 1128 1034 952 40 68 -177 C ATOM 836 CE1 TYR A 110 11.819 10.841 7.837 1.00 7.43 C ANISOU 836 CE1 TYR A 110 1098 786 939 84 44 -87 C ATOM 837 CE2 TYR A 110 10.989 10.680 10.112 1.00 7.97 C ANISOU 837 CE2 TYR A 110 1125 963 939 67 35 -283 C ATOM 838 CZ TYR A 110 10.817 10.514 8.764 1.00 7.98 C ANISOU 838 CZ TYR A 110 1082 946 1002 -29 118 -263 C ATOM 839 OH TYR A 110 9.623 10.013 8.251 1.00 8.35 O ANISOU 839 OH TYR A 110 1161 1061 952 -154 28 -189 O ATOM 840 N ASP A 111 15.125 14.518 8.381 1.00 9.07 N ANISOU 840 N ASP A 111 1283 1038 1125 -366 39 -240 N ATOM 841 CA ASP A 111 14.968 15.114 7.059 1.00 8.68 C ANISOU 841 CA ASP A 111 1254 774 1270 -236 -45 -134 C ATOM 842 C ASP A 111 15.372 14.099 6.021 1.00 7.86 C ANISOU 842 C ASP A 111 1030 826 1129 -212 -71 -26 C ATOM 843 O ASP A 111 16.586 13.925 5.776 1.00 9.08 O ANISOU 843 O ASP A 111 1001 1095 1354 -174 -80 -198 O ATOM 844 CB ASP A 111 15.901 16.346 6.997 1.00 11.14 C ANISOU 844 CB ASP A 111 1667 1032 1532 -600 -4 -249 C ATOM 845 CG ASP A 111 15.805 17.071 5.673 1.00 15.07 C ANISOU 845 CG ASP A 111 2469 1264 1994 -833 -150 181 C ATOM 846 OD1 ASP A 111 14.939 16.688 4.842 1.00 16.05 O ANISOU 846 OD1 ASP A 111 2285 1899 1914 -876 -318 745 O ATOM 847 OD2 ASP A 111 16.635 17.991 5.486 1.00 19.38 O ANISOU 847 OD2 ASP A 111 3383 1649 2331 -1366 -67 301 O ATOM 848 N GLY A 112 14.451 13.347 5.475 1.00 7.83 N ANISOU 848 N GLY A 112 1037 823 1116 -207 12 -141 N ATOM 849 CA GLY A 112 14.759 12.296 4.563 1.00 7.56 C ANISOU 849 CA GLY A 112 935 978 958 -249 115 -132 C ATOM 850 C GLY A 112 13.703 11.179 4.655 1.00 6.87 C ANISOU 850 C GLY A 112 922 846 844 -163 138 -151 C ATOM 851 O GLY A 112 12.501 11.449 4.748 1.00 7.51 O ANISOU 851 O GLY A 112 840 904 1110 -149 127 -152 O ATOM 852 N LEU A 113 14.184 9.939 4.592 1.00 6.73 N ANISOU 852 N LEU A 113 851 860 847 -150 112 -175 N ATOM 853 CA LEU A 113 13.391 8.737 4.479 1.00 6.41 C ANISOU 853 CA LEU A 113 830 903 703 -244 50 -119 C ATOM 854 C LEU A 113 13.581 7.816 5.675 1.00 6.16 C ANISOU 854 C LEU A 113 675 853 814 -142 138 -190 C ATOM 855 O LEU A 113 14.729 7.509 6.091 1.00 7.04 O ANISOU 855 O LEU A 113 736 1061 880 -88 57 -69 O ATOM 856 CB LEU A 113 13.845 7.971 3.212 1.00 6.49 C ANISOU 856 CB LEU A 113 823 756 887 -113 150 -158 C ATOM 857 CG LEU A 113 13.191 6.600 2.954 1.00 6.59 C ANISOU 857 CG LEU A 113 698 882 923 -104 128 -201 C ATOM 858 CD1 LEU A 113 11.695 6.775 2.636 1.00 7.53 C ANISOU 858 CD1 LEU A 113 794 886 1180 -127 -58 -249 C ATOM 859 CD2 LEU A 113 13.944 5.898 1.837 1.00 7.65 C ANISOU 859 CD2 LEU A 113 1031 1138 738 -52 149 -267 C ATOM 860 N GLN A 114 12.455 7.330 6.211 1.00 5.99 N ANISOU 860 N GLN A 114 837 681 759 -202 102 -196 N ATOM 861 CA GLN A 114 12.431 6.255 7.169 1.00 5.87 C ANISOU 861 CA GLN A 114 735 850 647 -95 40 -192 C ATOM 862 C GLN A 114 11.690 5.066 6.530 1.00 5.65 C ANISOU 862 C GLN A 114 679 766 700 -34 19 -87 C ATOM 863 O GLN A 114 10.580 5.233 6.019 1.00 6.60 O ANISOU 863 O GLN A 114 706 773 1031 6 -44 -112 O ATOM 864 CB GLN A 114 11.666 6.701 8.431 1.00 6.46 C ANISOU 864 CB GLN A 114 837 865 754 -42 134 -213 C ATOM 865 CG GLN A 114 11.540 5.615 9.491 1.00 7.48 C ANISOU 865 CG GLN A 114 984 1016 841 49 279 -142 C ATOM 866 CD GLN A 114 10.392 5.838 10.473 1.00 6.28 C ANISOU 866 CD GLN A 114 819 916 651 -44 20 -228 C ATOM 867 OE1 GLN A 114 9.504 6.642 10.266 1.00 7.70 O ANISOU 867 OE1 GLN A 114 912 1167 848 155 173 -129 O ATOM 868 NE2 GLN A 114 10.426 5.126 11.571 1.00 7.68 N ANISOU 868 NE2 GLN A 114 1083 1073 761 108 142 -108 N ATOM 869 N LEU A 115 12.289 3.885 6.615 1.00 5.35 N ANISOU 869 N LEU A 115 622 764 646 -15 33 -29 N ATOM 870 CA LEU A 115 11.571 2.634 6.243 1.00 5.26 C ANISOU 870 CA LEU A 115 668 737 593 -125 17 -93 C ATOM 871 C LEU A 115 11.336 1.884 7.546 1.00 5.47 C ANISOU 871 C LEU A 115 608 825 645 48 -3 -107 C ATOM 872 O LEU A 115 12.302 1.519 8.225 1.00 7.11 O ANISOU 872 O LEU A 115 649 1311 741 -7 -11 149 O ATOM 873 CB LEU A 115 12.393 1.772 5.287 1.00 6.07 C ANISOU 873 CB LEU A 115 702 949 653 64 45 -115 C ATOM 874 CG LEU A 115 12.732 2.436 3.970 1.00 6.17 C ANISOU 874 CG LEU A 115 639 1073 635 10 -6 -148 C ATOM 875 CD1 LEU A 115 13.610 1.526 3.115 1.00 9.53 C ANISOU 875 CD1 LEU A 115 1110 1852 661 584 102 -134 C ATOM 876 CD2 LEU A 115 11.489 2.804 3.173 1.00 6.65 C ANISOU 876 CD2 LEU A 115 719 1174 635 28 -3 46 C ATOM 877 N LEU A 116 10.066 1.670 7.862 1.00 5.41 N ANISOU 877 N LEU A 116 632 807 617 -94 32 -84 N ATOM 878 CA LEU A 116 9.688 1.048 9.133 1.00 5.64 C ANISOU 878 CA LEU A 116 615 927 599 -48 -13 -81 C ATOM 879 C LEU A 116 9.138 -0.353 8.881 1.00 5.07 C ANISOU 879 C LEU A 116 581 784 560 32 35 -66 C ATOM 880 O LEU A 116 8.177 -0.500 8.096 1.00 5.52 O ANISOU 880 O LEU A 116 596 914 586 -31 -16 -7 O ATOM 881 CB LEU A 116 8.608 1.881 9.831 1.00 6.56 C ANISOU 881 CB LEU A 116 867 912 714 4 161 -174 C ATOM 882 CG LEU A 116 8.028 1.259 11.116 1.00 6.47 C ANISOU 882 CG LEU A 116 765 979 714 69 160 -95 C ATOM 883 CD1 LEU A 116 9.083 1.118 12.205 1.00 6.99 C ANISOU 883 CD1 LEU A 116 925 992 740 -7 26 -185 C ATOM 884 CD2 LEU A 116 6.877 2.144 11.608 1.00 8.28 C ANISOU 884 CD2 LEU A 116 825 1243 1080 132 193 -321 C ATOM 885 N VAL A 117 9.701 -1.353 9.542 1.00 5.31 N ANISOU 885 N VAL A 117 565 891 560 -23 58 -58 N ATOM 886 CA VAL A 117 9.138 -2.688 9.579 1.00 5.38 C ANISOU 886 CA VAL A 117 664 766 613 122 42 13 C ATOM 887 C VAL A 117 8.578 -2.892 10.984 1.00 5.08 C ANISOU 887 C VAL A 117 564 887 479 147 -5 -73 C ATOM 888 O VAL A 117 9.282 -2.807 11.989 1.00 5.83 O ANISOU 888 O VAL A 117 601 1081 534 27 40 -49 O ATOM 889 CB VAL A 117 10.181 -3.760 9.205 1.00 6.21 C ANISOU 889 CB VAL A 117 742 960 657 262 152 -24 C ATOM 890 CG1 VAL A 117 9.606 -5.143 9.415 1.00 6.81 C ANISOU 890 CG1 VAL A 117 873 934 782 233 96 56 C ATOM 891 CG2 VAL A 117 10.671 -3.550 7.779 1.00 6.74 C ANISOU 891 CG2 VAL A 117 764 1135 661 49 177 -39 C ATOM 892 N ASP A 118 7.262 -3.133 11.044 1.00 5.46 N ANISOU 892 N ASP A 118 614 914 545 68 43 -30 N ATOM 893 CA ASP A 118 6.592 -3.314 12.345 1.00 5.55 C ANISOU 893 CA ASP A 118 738 894 475 47 91 -42 C ATOM 894 C ASP A 118 5.275 -3.989 12.104 1.00 5.38 C ANISOU 894 C ASP A 118 693 833 519 206 104 -38 C ATOM 895 O ASP A 118 4.863 -4.290 10.965 1.00 5.47 O ANISOU 895 O ASP A 118 639 823 616 1 44 28 O ATOM 896 CB ASP A 118 6.472 -2.019 13.154 1.00 6.06 C ANISOU 896 CB ASP A 118 724 921 659 96 108 -39 C ATOM 897 CG ASP A 118 5.165 -1.279 12.890 1.00 5.72 C ANISOU 897 CG ASP A 118 706 851 617 -8 70 -84 C ATOM 898 OD1 ASP A 118 4.837 -1.050 11.704 1.00 6.39 O ANISOU 898 OD1 ASP A 118 719 1055 653 107 59 -88 O ATOM 899 OD2 ASP A 118 4.450 -0.986 13.889 1.00 6.65 O ANISOU 899 OD2 ASP A 118 764 1088 673 132 90 -147 O ATOM 900 N ASN A 119 4.542 -4.259 13.212 1.00 5.57 N ANISOU 900 N ASN A 119 631 840 644 109 57 36 N ATOM 901 CA ASN A 119 3.287 -4.986 13.078 1.00 6.06 C ANISOU 901 CA ASN A 119 726 927 648 86 156 -20 C ATOM 902 C ASN A 119 2.166 -4.343 13.907 1.00 5.99 C ANISOU 902 C ASN A 119 661 1006 608 74 121 25 C ATOM 903 O ASN A 119 1.128 -4.989 14.094 1.00 7.00 O ANISOU 903 O ASN A 119 713 1002 944 108 204 67 O ATOM 904 CB ASN A 119 3.442 -6.461 13.390 1.00 6.68 C ANISOU 904 CB ASN A 119 963 896 679 114 124 46 C ATOM 905 CG ASN A 119 3.655 -6.781 14.854 1.00 7.33 C ANISOU 905 CG ASN A 119 1111 1004 670 157 104 55 C ATOM 906 OD1 ASN A 119 3.548 -5.916 15.704 1.00 6.62 O ANISOU 906 OD1 ASN A 119 882 973 661 47 87 66 O ATOM 907 ND2 ASN A 119 3.996 -8.040 15.104 1.00 11.37 N ANISOU 907 ND2 ASN A 119 2388 1057 876 453 -16 145 N ATOM 908 N ASN A 120 2.375 -3.141 14.431 1.00 5.90 N ANISOU 908 N ASN A 120 685 940 618 226 99 57 N ATOM 909 CA ASN A 120 1.397 -2.513 15.329 1.00 6.78 C ANISOU 909 CA ASN A 120 875 1119 582 246 119 32 C ATOM 910 C ASN A 120 0.340 -1.681 14.619 1.00 6.06 C ANISOU 910 C ASN A 120 552 989 761 106 139 -59 C ATOM 911 O ASN A 120 -0.515 -1.125 15.318 1.00 7.53 O ANISOU 911 O ASN A 120 845 1126 890 215 133 -126 O ATOM 912 CB ASN A 120 2.144 -1.655 16.365 1.00 7.54 C ANISOU 912 CB ASN A 120 761 1477 626 206 86 -120 C ATOM 913 CG ASN A 120 1.362 -1.552 17.684 1.00 8.56 C ANISOU 913 CG ASN A 120 1032 1486 736 296 238 -59 C ATOM 914 OD1 ASN A 120 0.674 -2.485 18.102 1.00 9.45 O ANISOU 914 OD1 ASN A 120 1184 1734 674 147 240 64 O ATOM 915 ND2 ASN A 120 1.518 -0.423 18.316 1.00 11.91 N ANISOU 915 ND2 ASN A 120 1481 1903 1143 52 406 -565 N ATOM 916 N GLY A 121 0.405 -1.572 13.295 1.00 6.26 N ANISOU 916 N GLY A 121 685 953 742 197 -28 -30 N ATOM 917 CA GLY A 121 -0.547 -0.786 12.560 1.00 6.43 C ANISOU 917 CA GLY A 121 777 785 879 156 -91 -98 C ATOM 918 C GLY A 121 -1.744 -1.630 12.104 1.00 5.81 C ANISOU 918 C GLY A 121 620 799 790 177 75 26 C ATOM 919 O GLY A 121 -1.844 -2.819 12.365 1.00 6.72 O ANISOU 919 O GLY A 121 749 904 899 33 40 186 O ATOM 920 N PRO A 122 -2.657 -0.974 11.408 1.00 6.27 N ANISOU 920 N PRO A 122 724 849 809 110 -18 32 N ATOM 921 CA PRO A 122 -3.985 -1.573 11.104 1.00 6.80 C ANISOU 921 CA PRO A 122 652 907 1026 188 0 -88 C ATOM 922 C PRO A 122 -3.934 -2.657 10.072 1.00 6.13 C ANISOU 922 C PRO A 122 695 870 765 57 44 45 C ATOM 923 O PRO A 122 -4.952 -3.347 9.899 1.00 7.71 O ANISOU 923 O PRO A 122 785 1182 964 -110 60 -88 O ATOM 924 CB PRO A 122 -4.828 -0.386 10.649 1.00 9.45 C ANISOU 924 CB PRO A 122 882 993 1715 247 -320 -119 C ATOM 925 CG PRO A 122 -3.880 0.654 10.240 1.00 13.40 C ANISOU 925 CG PRO A 122 1043 1278 2770 110 -610 715 C ATOM 926 CD PRO A 122 -2.592 0.458 11.020 1.00 8.42 C ANISOU 926 CD PRO A 122 961 807 1432 235 -225 62 C ATOM 927 N LEU A 123 -2.812 -2.843 9.385 1.00 6.00 N ANISOU 927 N LEU A 123 661 881 738 141 -9 -14 N ATOM 928 CA LEU A 123 -2.695 -3.846 8.301 1.00 6.58 C ANISOU 928 CA LEU A 123 815 784 900 60 46 -101 C ATOM 929 C LEU A 123 -1.874 -5.045 8.777 1.00 6.74 C ANISOU 929 C LEU A 123 664 903 995 54 81 1 C ATOM 930 O LEU A 123 -1.662 -5.953 7.974 1.00 8.35 O ANISOU 930 O LEU A 123 1156 919 1098 201 194 -106 O ATOM 931 CB LEU A 123 -2.044 -3.281 7.042 1.00 7.39 C ANISOU 931 CB LEU A 123 705 1232 872 80 16 52 C ATOM 932 CG LEU A 123 -2.667 -1.965 6.523 1.00 10.61 C ANISOU 932 CG LEU A 123 1178 1696 1159 265 139 516 C ATOM 933 CD1 LEU A 123 -1.934 -1.584 5.267 1.00 12.48 C ANISOU 933 CD1 LEU A 123 2223 1487 1033 -290 360 -43 C ATOM 934 CD2 LEU A 123 -4.171 -2.041 6.395 1.00 11.57 C ANISOU 934 CD2 LEU A 123 1184 1500 1711 235 -315 366 C ATOM 935 N GLY A 124 -1.419 -5.045 10.051 1.00 6.76 N ANISOU 935 N GLY A 124 589 976 1005 126 140 92 N ATOM 936 CA GLY A 124 -0.526 -6.114 10.496 1.00 7.91 C ANISOU 936 CA GLY A 124 610 985 1411 221 124 245 C ATOM 937 C GLY A 124 0.897 -5.883 10.004 1.00 5.75 C ANISOU 937 C GLY A 124 654 714 818 -15 152 75 C ATOM 938 O GLY A 124 1.279 -4.728 9.737 1.00 6.11 O ANISOU 938 O GLY A 124 718 705 898 163 77 53 O ATOM 939 N PRO A 125 1.721 -6.938 9.914 1.00 5.56 N ANISOU 939 N PRO A 125 607 784 719 84 23 142 N ATOM 940 CA PRO A 125 3.156 -6.774 9.552 1.00 5.66 C ANISOU 940 CA PRO A 125 664 825 661 153 99 26 C ATOM 941 C PRO A 125 3.307 -6.106 8.199 1.00 5.03 C ANISOU 941 C PRO A 125 577 705 631 115 38 -16 C ATOM 942 O PRO A 125 2.799 -6.595 7.160 1.00 5.32 O ANISOU 942 O PRO A 125 645 749 628 41 -13 27 O ATOM 943 CB PRO A 125 3.662 -8.202 9.573 1.00 6.47 C ANISOU 943 CB PRO A 125 864 775 819 226 42 81 C ATOM 944 CG PRO A 125 2.724 -8.951 10.468 1.00 8.35 C ANISOU 944 CG PRO A 125 818 964 1391 206 206 265 C ATOM 945 CD PRO A 125 1.365 -8.324 10.222 1.00 7.19 C ANISOU 945 CD PRO A 125 871 778 1084 94 94 255 C ATOM 946 N THR A 126 4.071 -5.006 8.197 1.00 5.24 N ANISOU 946 N THR A 126 576 757 658 56 50 18 N ATOM 947 CA THR A 126 4.263 -4.196 7.014 1.00 5.18 C ANISOU 947 CA THR A 126 621 793 555 69 4 40 C ATOM 948 C THR A 126 5.703 -3.678 6.941 1.00 4.93 C ANISOU 948 C THR A 126 632 628 612 49 -28 -57 C ATOM 949 O THR A 126 6.408 -3.582 7.966 1.00 5.50 O ANISOU 949 O THR A 126 604 909 578 35 -36 41 O ATOM 950 CB THR A 126 3.347 -2.961 6.985 1.00 5.20 C ANISOU 950 CB THR A 126 676 700 599 5 -73 -65 C ATOM 951 OG1 THR A 126 3.360 -2.273 8.250 1.00 5.64 O ANISOU 951 OG1 THR A 126 679 737 729 74 37 -69 O ATOM 952 CG2 THR A 126 1.896 -3.330 6.717 1.00 6.38 C ANISOU 952 CG2 THR A 126 591 907 927 71 -114 26 C ATOM 953 N LEU A 127 6.074 -3.283 5.722 1.00 5.10 N ANISOU 953 N LEU A 127 636 698 604 36 24 25 N ATOM 954 CA LEU A 127 7.187 -2.361 5.458 1.00 4.85 C ANISOU 954 CA LEU A 127 547 710 584 28 11 22 C ATOM 955 C LEU A 127 6.557 -1.099 4.941 1.00 4.99 C ANISOU 955 C LEU A 127 521 729 645 59 -59 -47 C ATOM 956 O LEU A 127 5.825 -1.105 3.946 1.00 5.91 O ANISOU 956 O LEU A 127 706 770 770 31 -236 -42 O ATOM 957 CB LEU A 127 8.182 -2.992 4.459 1.00 4.83 C ANISOU 957 CB LEU A 127 632 641 565 57 -9 30 C ATOM 958 CG ALEU A 127 9.482 -2.148 4.317 0.67 4.93 C ANISOU 958 CG ALEU A 127 597 717 560 60 14 105 C ATOM 959 CG BLEU A 127 9.354 -2.182 3.916 0.33 7.90 C ANISOU 959 CG BLEU A 127 829 1652 520 -347 216 -283 C ATOM 960 CD1ALEU A 127 10.563 -3.076 3.760 0.67 7.60 C ANISOU 960 CD1ALEU A 127 778 1091 1019 377 226 125 C ATOM 961 CD1BLEU A 127 10.175 -1.532 5.003 0.33 7.77 C ANISOU 961 CD1BLEU A 127 1088 1089 777 -212 -390 143 C ATOM 962 CD2ALEU A 127 9.355 -0.939 3.387 0.67 4.69 C ANISOU 962 CD2ALEU A 127 661 550 570 41 -9 57 C ATOM 963 CD2BLEU A 127 10.266 -3.089 3.090 0.33 8.16 C ANISOU 963 CD2BLEU A 127 968 926 1206 -208 420 -14 C ATOM 964 N ARG A 128 6.860 0.021 5.591 1.00 5.12 N ANISOU 964 N ARG A 128 653 659 635 67 -39 -69 N ATOM 965 CA ARG A 128 6.266 1.301 5.259 1.00 5.51 C ANISOU 965 CA ARG A 128 603 662 828 52 28 -6 C ATOM 966 C ARG A 128 7.359 2.332 5.000 1.00 5.05 C ANISOU 966 C ARG A 128 605 609 704 -13 43 -172 C ATOM 967 O ARG A 128 8.392 2.378 5.693 1.00 6.46 O ANISOU 967 O ARG A 128 681 959 815 -80 -87 -9 O ATOM 968 CB ARG A 128 5.419 1.812 6.434 1.00 6.50 C ANISOU 968 CB ARG A 128 656 622 1191 -15 238 -95 C ATOM 969 CG ARG A 128 4.127 1.016 6.609 1.00 7.64 C ANISOU 969 CG ARG A 128 759 1034 1111 -78 224 -47 C ATOM 970 CD ARG A 128 3.504 1.235 8.003 1.00 7.03 C ANISOU 970 CD ARG A 128 809 779 1081 -19 252 -139 C ATOM 971 NE ARG A 128 2.206 0.462 8.063 1.00 6.71 N ANISOU 971 NE ARG A 128 667 866 1015 126 170 -29 N ATOM 972 CZ ARG A 128 1.035 0.910 7.674 1.00 7.28 C ANISOU 972 CZ ARG A 128 771 983 1013 38 114 151 C ATOM 973 NH1 ARG A 128 0.883 2.149 7.170 1.00 7.72 N ANISOU 973 NH1 ARG A 128 917 810 1207 117 154 12 N ATOM 974 NH2 ARG A 128 -0.033 0.100 7.793 1.00 7.84 N ANISOU 974 NH2 ARG A 128 735 1002 1242 -22 115 39 N ATOM 975 N GLY A 129 7.082 3.211 4.050 1.00 5.57 N ANISOU 975 N GLY A 129 618 658 841 -5 51 -42 N ATOM 976 CA GLY A 129 7.946 4.402 3.818 1.00 6.33 C ANISOU 976 CA GLY A 129 664 703 1040 -9 233 -33 C ATOM 977 C GLY A 129 7.293 5.625 4.443 1.00 5.67 C ANISOU 977 C GLY A 129 705 672 778 4 -21 23 C ATOM 978 O GLY A 129 6.094 5.878 4.302 1.00 6.42 O ANISOU 978 O GLY A 129 571 858 1008 52 24 -107 O ATOM 979 N GLN A 130 8.143 6.390 5.114 1.00 6.06 N ANISOU 979 N GLN A 130 674 748 880 27 121 -111 N ATOM 980 CA GLN A 130 7.754 7.622 5.761 1.00 6.22 C ANISOU 980 CA GLN A 130 652 753 959 -83 106 -198 C ATOM 981 C GLN A 130 8.743 8.748 5.332 1.00 6.53 C ANISOU 981 C GLN A 130 841 879 763 -13 136 -76 C ATOM 982 O GLN A 130 9.951 8.451 5.195 1.00 6.86 O ANISOU 982 O GLN A 130 678 898 1029 -70 138 -128 O ATOM 983 CB GLN A 130 7.785 7.545 7.298 1.00 6.95 C ANISOU 983 CB GLN A 130 730 961 950 -59 240 -134 C ATOM 984 CG GLN A 130 7.183 6.264 7.879 1.00 7.50 C ANISOU 984 CG GLN A 130 748 1029 1073 -45 231 40 C ATOM 985 CD GLN A 130 5.699 6.051 7.806 1.00 6.71 C ANISOU 985 CD GLN A 130 709 925 915 26 134 -40 C ATOM 986 OE1 GLN A 130 5.254 4.944 7.510 1.00 7.68 O ANISOU 986 OE1 GLN A 130 900 868 1149 -63 180 -157 O ATOM 987 NE2 GLN A 130 4.902 7.088 8.120 1.00 7.63 N ANISOU 987 NE2 GLN A 130 854 864 1179 33 287 -39 N ATOM 988 N LEU A 131 8.242 9.950 5.171 1.00 6.50 N ANISOU 988 N LEU A 131 859 745 864 -37 128 -61 N ATOM 989 CA LEU A 131 9.102 11.100 4.802 1.00 7.24 C ANISOU 989 CA LEU A 131 846 831 1073 -82 135 -137 C ATOM 990 C LEU A 131 8.880 12.213 5.809 1.00 7.41 C ANISOU 990 C LEU A 131 943 657 1214 15 184 -39 C ATOM 991 O LEU A 131 7.791 12.416 6.315 1.00 9.04 O ANISOU 991 O LEU A 131 1082 862 1491 135 342 -164 O ATOM 992 CB LEU A 131 8.698 11.657 3.441 1.00 8.20 C ANISOU 992 CB LEU A 131 1083 865 1166 -69 155 79 C ATOM 993 CG LEU A 131 8.956 10.697 2.284 1.00 10.49 C ANISOU 993 CG LEU A 131 1563 1335 1089 -99 143 -74 C ATOM 994 CD1 LEU A 131 8.077 11.060 1.110 1.00 13.79 C ANISOU 994 CD1 LEU A 131 1932 2094 1213 332 -59 -71 C ATOM 995 CD2 LEU A 131 10.469 10.626 1.975 1.00 10.93 C ANISOU 995 CD2 LEU A 131 1703 1327 1123 370 170 -231 C ATOM 996 N ASN A 132 9.956 12.964 6.049 1.00 8.29 N ANISOU 996 N ASN A 132 1174 823 1153 -85 124 -253 N ATOM 997 CA ASN A 132 9.847 14.205 6.835 1.00 9.12 C ANISOU 997 CA ASN A 132 1356 905 1203 -85 33 -301 C ATOM 998 C ASN A 132 10.939 15.136 6.350 1.00 8.91 C ANISOU 998 C ASN A 132 1339 828 1219 3 -39 -183 C ATOM 999 O ASN A 132 11.966 14.703 5.811 1.00 8.80 O ANISOU 999 O ASN A 132 1293 767 1283 -75 -24 -193 O ATOM 1000 CB ASN A 132 9.993 13.882 8.314 1.00 9.11 C ANISOU 1000 CB ASN A 132 1394 953 1114 66 209 -283 C ATOM 1001 CG ASN A 132 9.573 15.067 9.207 1.00 9.96 C ANISOU 1001 CG ASN A 132 1564 974 1245 142 115 -314 C ATOM 1002 OD1 ASN A 132 8.505 15.655 8.999 1.00 12.69 O ANISOU 1002 OD1 ASN A 132 1655 1535 1633 442 229 -535 O ATOM 1003 ND2 ASN A 132 10.411 15.346 10.181 1.00 10.85 N ANISOU 1003 ND2 ASN A 132 1583 1181 1356 -161 177 -552 N ATOM 1004 N ASP A 133 10.740 16.439 6.562 1.00 10.48 N ANISOU 1004 N ASP A 133 1912 772 1296 59 56 -79 N ATOM 1005 CA ASP A 133 11.653 17.447 6.029 1.00 11.12 C ANISOU 1005 CA ASP A 133 1690 1017 1519 -66 65 -86 C ATOM 1006 C ASP A 133 12.490 18.126 7.103 1.00 11.70 C ANISOU 1006 C ASP A 133 2270 761 1414 -71 34 -99 C ATOM 1007 O ASP A 133 13.103 19.176 6.848 1.00 14.15 O ANISOU 1007 O ASP A 133 2426 1076 1873 -410 -136 -95 O ATOM 1008 CB ASP A 133 10.888 18.514 5.207 1.00 13.13 C ANISOU 1008 CB ASP A 133 2544 1072 1374 -26 -66 71 C ATOM 1009 CG ASP A 133 9.914 19.321 6.013 1.00 14.08 C ANISOU 1009 CG ASP A 133 2328 1158 1863 288 -485 -217 C ATOM 1010 OD1 ASP A 133 9.938 19.194 7.281 1.00 14.29 O ANISOU 1010 OD1 ASP A 133 2341 1210 1879 398 89 -221 O ATOM 1011 OD2 ASP A 133 9.169 20.142 5.439 1.00 21.10 O ANISOU 1011 OD2 ASP A 133 3491 1938 2587 953 -567 206 O ATOM 1012 N GLY A 134 12.477 17.600 8.312 1.00 11.65 N ANISOU 1012 N GLY A 134 2119 1054 1252 89 104 -247 N ATOM 1013 CA GLY A 134 13.329 18.134 9.395 1.00 12.84 C ANISOU 1013 CA GLY A 134 1887 1604 1389 -11 131 -453 C ATOM 1014 C GLY A 134 12.783 19.342 10.082 1.00 14.18 C ANISOU 1014 C GLY A 134 2732 1230 1425 159 -257 -335 C ATOM 1015 O GLY A 134 13.419 19.821 11.039 1.00 18.04 O ANISOU 1015 O GLY A 134 2864 2064 1927 -83 -201 -909 O ATOM 1016 N GLN A 135 11.633 19.847 9.686 1.00 13.24 N ANISOU 1016 N GLN A 135 2719 881 1431 216 138 -223 N ATOM 1017 CA GLN A 135 11.125 21.079 10.336 1.00 15.43 C ANISOU 1017 CA GLN A 135 3034 1029 1800 241 37 -567 C ATOM 1018 C GLN A 135 10.418 20.747 11.632 1.00 16.83 C ANISOU 1018 C GLN A 135 2642 1637 2116 165 366 -747 C ATOM 1019 O GLN A 135 10.461 21.518 12.623 1.00 20.66 O ANISOU 1019 O GLN A 135 3115 2254 2478 -387 795 -1190 O ATOM 1020 CB GLN A 135 10.244 21.816 9.354 1.00 20.59 C ANISOU 1020 CB GLN A 135 4130 1347 2348 1003 -457 -717 C ATOM 1021 CG GLN A 135 10.976 22.403 8.145 1.00 23.21 C ANISOU 1021 CG GLN A 135 5549 1349 1921 125 -928 -539 C ATOM 1022 CD GLN A 135 9.984 23.129 7.249 1.00 30.84 C ANISOU 1022 CD GLN A 135 6389 2311 3020 692 -1209 93 C ATOM 1023 OE1 GLN A 135 8.825 23.323 7.625 1.00 34.87 O ANISOU 1023 OE1 GLN A 135 6148 2350 4751 1028 -1887 -2004 O ATOM 1024 NE2 GLN A 135 10.421 23.540 6.074 1.00 47.10 N ANISOU 1024 NE2 GLN A 135 10809 4038 3048 2004 -580 1157 N ATOM 1025 N LYS A 136 9.706 19.657 11.710 1.00 18.44 N ANISOU 1025 N LYS A 136 2727 1803 2476 -16 761 -899 N ATOM 1026 CA LYS A 136 8.966 19.329 12.945 1.00 18.04 C ANISOU 1026 CA LYS A 136 2691 1869 2293 179 688 -870 C ATOM 1027 C LYS A 136 9.128 17.848 13.215 1.00 16.86 C ANISOU 1027 C LYS A 136 2511 1837 2057 80 656 -960 C ATOM 1028 O LYS A 136 9.231 17.021 12.331 1.00 18.37 O ANISOU 1028 O LYS A 136 3163 1965 1851 507 77 -964 O ATOM 1029 CB LYS A 136 7.484 19.653 12.716 1.00 21.97 C ANISOU 1029 CB LYS A 136 2732 2564 3052 467 884 -511 C ATOM 1030 CG LYS A 136 7.099 21.140 12.798 1.00 28.15 C ANISOU 1030 CG LYS A 136 3080 2234 5382 340 -305 1781 C ATOM 1031 CD LYS A 136 5.612 21.349 12.531 1.00 38.58 C ANISOU 1031 CD LYS A 136 3194 3355 8107 795 -708 839 C ATOM 1032 CE LYS A 136 5.276 22.719 11.933 1.00 42.02 C ANISOU 1032 CE LYS A 136 2998 3854 9115 1075 -1533 1224 C ATOM 1033 NZ LYS A 136 4.282 22.651 10.823 1.00 44.45 N ANISOU 1033 NZ LYS A 136 2159 5254 9477 -757 -1333 2624 N ATOM 1034 N PRO A 137 8.997 17.410 14.447 1.00 16.09 N ANISOU 1034 N PRO A 137 2377 1754 1981 64 247 -1073 N ATOM 1035 CA PRO A 137 8.865 15.961 14.680 1.00 14.40 C ANISOU 1035 CA PRO A 137 1758 1741 1973 12 51 -894 C ATOM 1036 C PRO A 137 7.583 15.448 14.021 1.00 13.78 C ANISOU 1036 C PRO A 137 1786 1614 1834 443 -235 -926 C ATOM 1037 O PRO A 137 6.535 16.064 13.960 1.00 15.99 O ANISOU 1037 O PRO A 137 1949 1644 2484 619 -111 -897 O ATOM 1038 CB PRO A 137 8.787 15.916 16.216 1.00 15.63 C ANISOU 1038 CB PRO A 137 1998 2066 1874 -91 -163 -1032 C ATOM 1039 CG PRO A 137 8.069 17.211 16.516 1.00 24.66 C ANISOU 1039 CG PRO A 137 5456 1701 2212 325 1138 -676 C ATOM 1040 CD PRO A 137 8.880 18.191 15.688 1.00 20.42 C ANISOU 1040 CD PRO A 137 3655 1966 2139 -180 707 -1314 C ATOM 1041 N VAL A 138 7.704 14.200 13.497 1.00 11.64 N ANISOU 1041 N VAL A 138 1432 1427 1564 285 24 -659 N ATOM 1042 CA VAL A 138 6.482 13.534 13.028 1.00 12.08 C ANISOU 1042 CA VAL A 138 1328 1596 1664 262 49 -691 C ATOM 1043 C VAL A 138 5.575 13.204 14.232 1.00 13.16 C ANISOU 1043 C VAL A 138 1348 2021 1631 328 200 -946 C ATOM 1044 O VAL A 138 5.996 13.039 15.379 1.00 16.33 O ANISOU 1044 O VAL A 138 1608 3020 1578 295 118 -1112 O ATOM 1045 CB VAL A 138 6.826 12.308 12.219 1.00 11.27 C ANISOU 1045 CB VAL A 138 1885 1370 1026 83 215 -359 C ATOM 1046 CG1 VAL A 138 7.750 12.616 11.033 1.00 11.80 C ANISOU 1046 CG1 VAL A 138 1424 1563 1497 -168 292 -569 C ATOM 1047 CG2 VAL A 138 7.496 11.247 13.087 1.00 12.75 C ANISOU 1047 CG2 VAL A 138 1994 1549 1301 448 65 -571 C ATOM 1048 N ASP A 139 4.296 13.090 13.928 1.00 14.98 N ANISOU 1048 N ASP A 139 1359 2402 1931 288 170 -947 N ATOM 1049 CA ASP A 139 3.284 12.714 14.921 1.00 15.02 C ANISOU 1049 CA ASP A 139 1316 2546 1844 32 93 -1044 C ATOM 1050 C ASP A 139 3.236 11.197 14.958 1.00 14.47 C ANISOU 1050 C ASP A 139 1420 2571 1506 414 184 -779 C ATOM 1051 O ASP A 139 2.729 10.561 14.022 1.00 13.42 O ANISOU 1051 O ASP A 139 1479 2094 1525 141 403 -675 O ATOM 1052 CB ASP A 139 1.953 13.311 14.545 1.00 17.74 C ANISOU 1052 CB ASP A 139 1459 2543 2739 357 426 -532 C ATOM 1053 CG ASP A 139 0.883 13.070 15.606 1.00 19.91 C ANISOU 1053 CG ASP A 139 1854 2888 2823 602 886 -878 C ATOM 1054 OD1 ASP A 139 1.044 12.108 16.398 1.00 19.81 O ANISOU 1054 OD1 ASP A 139 2012 3104 2411 440 970 -892 O ATOM 1055 OD2 ASP A 139 -0.068 13.838 15.593 1.00 21.74 O ANISOU 1055 OD2 ASP A 139 1484 3315 3461 517 332 -1213 O ATOM 1056 N LYS A 140 3.750 10.564 15.995 1.00 18.04 N ANISOU 1056 N LYS A 140 1881 3304 1669 792 103 -574 N ATOM 1057 CA LYS A 140 3.793 9.122 16.034 1.00 18.86 C ANISOU 1057 CA LYS A 140 2214 3301 1651 857 17 -250 C ATOM 1058 C LYS A 140 2.411 8.517 16.033 1.00 19.13 C ANISOU 1058 C LYS A 140 2420 3195 1652 713 596 -39 C ATOM 1059 O LYS A 140 2.285 7.366 15.589 1.00 25.90 O ANISOU 1059 O LYS A 140 2708 2325 4810 507 1587 370 O ATOM 1060 CB LYS A 140 4.620 8.636 17.244 1.00 24.19 C ANISOU 1060 CB LYS A 140 3785 3792 1616 1311 -606 -580 C ATOM 1061 CG LYS A 140 6.090 8.990 17.083 1.00 27.24 C ANISOU 1061 CG LYS A 140 3155 4784 2411 2232 -1012 -1230 C ATOM 1062 CD LYS A 140 6.914 8.289 18.157 1.00 39.12 C ANISOU 1062 CD LYS A 140 4605 7210 3049 1681 -1750 215 C ATOM 1063 CE LYS A 140 7.582 9.253 19.106 1.00 35.92 C ANISOU 1063 CE LYS A 140 3952 8294 1402 947 -714 432 C ATOM 1064 NZ LYS A 140 8.136 8.483 20.287 1.00 23.03 N ANISOU 1064 NZ LYS A 140 1824 5408 1519 347 450 302 N ATOM 1065 N THR A 141 1.415 9.280 16.513 1.00 19.03 N ANISOU 1065 N THR A 141 2387 3389 1456 558 630 -256 N ATOM 1066 CA THR A 141 0.087 8.728 16.588 1.00 21.30 C ANISOU 1066 CA THR A 141 2431 3356 2308 518 891 250 C ATOM 1067 C THR A 141 -0.553 8.656 15.196 1.00 17.29 C ANISOU 1067 C THR A 141 2211 1777 2580 -130 704 224 C ATOM 1068 O THR A 141 -1.605 8.041 15.108 1.00 25.04 O ANISOU 1068 O THR A 141 2119 3647 3749 -641 706 724 O ATOM 1069 CB THR A 141 -0.853 9.532 17.510 1.00 25.76 C ANISOU 1069 CB THR A 141 2953 3957 2878 9 1765 -169 C ATOM 1070 OG1 THR A 141 -1.085 10.829 16.946 1.00 24.64 O ANISOU 1070 OG1 THR A 141 3037 3323 2999 134 1930 -870 O ATOM 1071 CG2 THR A 141 -0.215 9.732 18.872 1.00 33.79 C ANISOU 1071 CG2 THR A 141 3837 6428 2574 554 1838 -472 C ATOM 1072 N LYS A 142 0.027 9.220 14.154 1.00 14.48 N ANISOU 1072 N LYS A 142 1773 1598 2132 184 943 -409 N ATOM 1073 CA LYS A 142 -0.503 9.204 12.807 1.00 12.86 C ANISOU 1073 CA LYS A 142 1304 1251 2332 64 740 -438 C ATOM 1074 C LYS A 142 0.390 8.448 11.805 1.00 10.88 C ANISOU 1074 C LYS A 142 932 1120 2080 87 412 -443 C ATOM 1075 O LYS A 142 0.176 8.547 10.598 1.00 10.83 O ANISOU 1075 O LYS A 142 1049 940 2125 171 385 -269 O ATOM 1076 CB LYS A 142 -0.746 10.631 12.312 1.00 14.45 C ANISOU 1076 CB LYS A 142 1530 1344 2616 490 509 -604 C ATOM 1077 CG LYS A 142 -1.737 11.370 13.249 1.00 19.08 C ANISOU 1077 CG LYS A 142 2102 2419 2729 1186 286 -995 C ATOM 1078 CD LYS A 142 -1.969 12.779 12.696 1.00 22.53 C ANISOU 1078 CD LYS A 142 2942 2206 3413 1479 -110 -1281 C ATOM 1079 CE LYS A 142 -2.944 13.655 13.444 1.00 23.33 C ANISOU 1079 CE LYS A 142 3321 2347 3197 1518 775 -236 C ATOM 1080 NZ LYS A 142 -4.149 12.993 13.950 1.00 28.12 N ANISOU 1080 NZ LYS A 142 2446 4084 4156 237 -163 -1890 N ATOM 1081 N ILE A 143 1.408 7.738 12.334 1.00 10.53 N ANISOU 1081 N ILE A 143 1062 1083 1855 23 344 -303 N ATOM 1082 CA ILE A 143 2.417 7.199 11.406 1.00 9.76 C ANISOU 1082 CA ILE A 143 917 1010 1783 75 273 -347 C ATOM 1083 C ILE A 143 1.806 6.292 10.343 1.00 8.18 C ANISOU 1083 C ILE A 143 756 831 1521 199 247 -5 C ATOM 1084 O ILE A 143 2.235 6.375 9.192 1.00 8.57 O ANISOU 1084 O ILE A 143 755 1041 1462 102 229 -26 O ATOM 1085 CB ILE A 143 3.497 6.497 12.244 1.00 10.16 C ANISOU 1085 CB ILE A 143 1073 1342 1446 48 226 -229 C ATOM 1086 CG1 ILE A 143 4.759 6.222 11.415 1.00 14.45 C ANISOU 1086 CG1 ILE A 143 1138 2687 1667 690 250 39 C ATOM 1087 CG2 ILE A 143 3.016 5.256 13.011 1.00 14.72 C ANISOU 1087 CG2 ILE A 143 2024 1316 2253 246 646 36 C ATOM 1088 CD1 ILE A 143 5.969 5.949 12.319 1.00 13.75 C ANISOU 1088 CD1 ILE A 143 1177 2084 1965 225 -53 -404 C ATOM 1089 N TYR A 144 0.826 5.457 10.708 1.00 8.28 N ANISOU 1089 N TYR A 144 805 742 1600 123 186 -38 N ATOM 1090 CA TYR A 144 0.324 4.517 9.700 1.00 8.25 C ANISOU 1090 CA TYR A 144 1034 713 1388 83 218 -77 C ATOM 1091 C TYR A 144 -0.477 5.225 8.603 1.00 8.90 C ANISOU 1091 C TYR A 144 1111 878 1393 185 277 -39 C ATOM 1092 O TYR A 144 -0.388 4.880 7.418 1.00 11.27 O ANISOU 1092 O TYR A 144 1967 962 1353 389 173 -44 O ATOM 1093 CB TYR A 144 -0.506 3.384 10.366 1.00 7.81 C ANISOU 1093 CB TYR A 144 761 869 1337 46 222 -29 C ATOM 1094 CG TYR A 144 0.360 2.700 11.427 1.00 7.86 C ANISOU 1094 CG TYR A 144 853 795 1339 91 148 -108 C ATOM 1095 CD1 TYR A 144 1.524 1.996 11.070 1.00 7.00 C ANISOU 1095 CD1 TYR A 144 814 744 1103 58 214 -111 C ATOM 1096 CD2 TYR A 144 0.055 2.800 12.795 1.00 8.86 C ANISOU 1096 CD2 TYR A 144 1025 991 1350 220 306 -48 C ATOM 1097 CE1 TYR A 144 2.321 1.388 12.020 1.00 7.15 C ANISOU 1097 CE1 TYR A 144 758 1001 957 66 128 -140 C ATOM 1098 CE2 TYR A 144 0.863 2.208 13.732 1.00 8.77 C ANISOU 1098 CE2 TYR A 144 1155 958 1219 232 291 -195 C ATOM 1099 CZ TYR A 144 1.995 1.514 13.344 1.00 7.56 C ANISOU 1099 CZ TYR A 144 928 970 974 117 184 -228 C ATOM 1100 OH TYR A 144 2.770 0.941 14.325 1.00 8.03 O ANISOU 1100 OH TYR A 144 1011 1110 932 142 183 -137 O ATOM 1101 N ASP A 145 -1.222 6.245 9.004 1.00 8.50 N ANISOU 1101 N ASP A 145 738 957 1535 52 333 -35 N ATOM 1102 CA ASP A 145 -1.962 7.019 7.978 1.00 8.88 C ANISOU 1102 CA ASP A 145 684 1025 1664 117 328 -25 C ATOM 1103 C ASP A 145 -1.024 7.854 7.135 1.00 10.22 C ANISOU 1103 C ASP A 145 757 963 2165 174 91 434 C ATOM 1104 O ASP A 145 -1.368 8.184 5.962 1.00 12.70 O ANISOU 1104 O ASP A 145 1028 1859 1938 -229 39 407 O ATOM 1105 CB ASP A 145 -2.965 7.903 8.664 1.00 9.88 C ANISOU 1105 CB ASP A 145 724 1299 1730 186 -66 -596 C ATOM 1106 CG AASP A 145 -4.302 7.916 8.038 0.51 6.33 C ANISOU 1106 CG AASP A 145 753 660 990 44 102 2 C ATOM 1107 CG BASP A 145 -4.330 7.397 8.885 0.49 6.95 C ANISOU 1107 CG BASP A 145 802 970 871 189 115 -121 C ATOM 1108 OD1AASP A 145 -5.293 8.369 8.609 0.51 6.95 O ANISOU 1108 OD1AASP A 145 766 1110 764 335 -105 -152 O ATOM 1109 OD1BASP A 145 -4.473 6.178 8.745 0.49 8.38 O ANISOU 1109 OD1BASP A 145 921 973 1290 166 98 -259 O ATOM 1110 OD2AASP A 145 -4.255 7.586 6.834 0.51 6.81 O ANISOU 1110 OD2AASP A 145 810 886 892 97 123 -5 O ATOM 1111 OD2BASP A 145 -5.166 8.231 9.288 0.49 6.67 O ANISOU 1111 OD2BASP A 145 671 1053 811 154 -83 -368 O ATOM 1112 N GLN A 146 0.146 8.196 7.676 1.00 7.96 N ANISOU 1112 N GLN A 146 667 709 1649 73 226 -71 N ATOM 1113 CA GLN A 146 1.084 9.104 6.995 1.00 8.84 C ANISOU 1113 CA GLN A 146 1060 774 1523 -49 264 20 C ATOM 1114 C GLN A 146 2.106 8.358 6.152 1.00 8.25 C ANISOU 1114 C GLN A 146 630 912 1593 134 138 112 C ATOM 1115 O GLN A 146 2.839 9.025 5.423 1.00 10.09 O ANISOU 1115 O GLN A 146 912 912 2008 89 295 277 O ATOM 1116 CB GLN A 146 1.782 10.037 8.017 1.00 11.55 C ANISOU 1116 CB GLN A 146 1426 891 2072 -347 286 -196 C ATOM 1117 CG GLN A 146 0.701 10.963 8.621 1.00 14.91 C ANISOU 1117 CG GLN A 146 2284 935 2445 -240 592 -494 C ATOM 1118 CD AGLN A 146 1.030 12.182 9.377 0.63 14.42 C ANISOU 1118 CD AGLN A 146 1711 825 2943 94 58 -366 C ATOM 1119 CD BGLN A 146 0.566 12.119 7.645 0.37 13.83 C ANISOU 1119 CD BGLN A 146 2135 637 2481 -159 859 -585 C ATOM 1120 OE1AGLN A 146 2.130 12.129 9.901 0.63 18.09 O ANISOU 1120 OE1AGLN A 146 1593 790 4492 52 -262 -497 O ATOM 1121 OE1BGLN A 146 1.505 12.842 7.329 0.37 19.31 O ANISOU 1121 OE1BGLN A 146 2537 1761 3041 -886 324 42 O ATOM 1122 NE2AGLN A 146 0.127 13.172 9.437 0.63 15.98 N ANISOU 1122 NE2AGLN A 146 1789 1079 3204 310 -147 -520 N ATOM 1123 NE2BGLN A 146 -0.680 12.171 7.223 0.37 18.29 N ANISOU 1123 NE2BGLN A 146 2929 1473 2547 -1356 -409 150 N ATOM 1124 N SER A 147 2.134 7.015 6.149 1.00 7.90 N ANISOU 1124 N SER A 147 769 794 1440 198 181 95 N ATOM 1125 CA SER A 147 3.048 6.308 5.213 1.00 7.64 C ANISOU 1125 CA SER A 147 689 928 1285 106 162 122 C ATOM 1126 C SER A 147 2.770 6.782 3.805 1.00 8.78 C ANISOU 1126 C SER A 147 816 1120 1399 288 190 298 C ATOM 1127 O SER A 147 1.600 6.840 3.391 1.00 9.68 O ANISOU 1127 O SER A 147 846 1441 1391 208 44 299 O ATOM 1128 CB SER A 147 2.776 4.814 5.291 1.00 7.83 C ANISOU 1128 CB SER A 147 1022 838 1115 195 219 76 C ATOM 1129 OG SER A 147 2.811 4.335 6.618 1.00 7.21 O ANISOU 1129 OG SER A 147 788 830 1122 108 216 53 O ATOM 1130 N PHE A 148 3.832 7.081 3.044 1.00 7.86 N ANISOU 1130 N PHE A 148 867 780 1340 128 165 204 N ATOM 1131 CA PHE A 148 3.586 7.444 1.642 1.00 7.66 C ANISOU 1131 CA PHE A 148 917 677 1318 111 107 206 C ATOM 1132 C PHE A 148 3.431 6.207 0.791 1.00 8.06 C ANISOU 1132 C PHE A 148 1004 784 1273 116 281 202 C ATOM 1133 O PHE A 148 2.891 6.334 -0.311 1.00 8.71 O ANISOU 1133 O PHE A 148 1125 809 1374 146 17 97 O ATOM 1134 CB PHE A 148 4.656 8.406 1.073 1.00 8.26 C ANISOU 1134 CB PHE A 148 1023 816 1300 87 197 144 C ATOM 1135 CG PHE A 148 6.057 7.801 0.915 1.00 7.69 C ANISOU 1135 CG PHE A 148 1104 717 1102 -6 170 211 C ATOM 1136 CD1 PHE A 148 6.371 7.145 -0.279 1.00 8.83 C ANISOU 1136 CD1 PHE A 148 1268 956 1130 110 247 167 C ATOM 1137 CD2 PHE A 148 7.005 7.882 1.931 1.00 8.59 C ANISOU 1137 CD2 PHE A 148 886 1095 1281 -135 45 214 C ATOM 1138 CE1 PHE A 148 7.623 6.560 -0.448 1.00 9.08 C ANISOU 1138 CE1 PHE A 148 1099 1113 1237 58 115 46 C ATOM 1139 CE2 PHE A 148 8.278 7.297 1.739 1.00 8.94 C ANISOU 1139 CE2 PHE A 148 949 1364 1083 -178 330 217 C ATOM 1140 CZ PHE A 148 8.576 6.651 0.559 1.00 8.52 C ANISOU 1140 CZ PHE A 148 1123 1009 1104 -136 169 259 C ATOM 1141 N ALA A 149 3.902 5.062 1.270 1.00 7.64 N ANISOU 1141 N ALA A 149 759 666 1477 149 279 177 N ATOM 1142 CA ALA A 149 3.836 3.817 0.519 1.00 7.93 C ANISOU 1142 CA ALA A 149 870 688 1458 76 210 108 C ATOM 1143 C ALA A 149 4.033 2.690 1.527 1.00 7.05 C ANISOU 1143 C ALA A 149 459 740 1482 36 -63 66 C ATOM 1144 O ALA A 149 4.619 2.903 2.580 1.00 7.69 O ANISOU 1144 O ALA A 149 620 799 1504 -32 -22 28 O ATOM 1145 CB ALA A 149 4.887 3.775 -0.578 1.00 10.23 C ANISOU 1145 CB ALA A 149 1427 832 1630 239 420 103 C ATOM 1146 N SER A 150 3.568 1.501 1.157 1.00 8.32 N ANISOU 1146 N SER A 150 759 751 1651 -28 -297 283 N ATOM 1147 CA SER A 150 3.722 0.361 2.049 1.00 7.89 C ANISOU 1147 CA SER A 150 871 781 1345 -4 -404 239 C ATOM 1148 C SER A 150 3.462 -0.920 1.321 1.00 8.21 C ANISOU 1148 C SER A 150 917 788 1414 -118 -557 173 C ATOM 1149 O SER A 150 2.862 -0.936 0.227 1.00 9.72 O ANISOU 1149 O SER A 150 1291 825 1579 -294 -909 421 O ATOM 1150 CB SER A 150 2.768 0.499 3.248 1.00 9.14 C ANISOU 1150 CB SER A 150 776 1117 1578 -151 -221 197 C ATOM 1151 OG SER A 150 1.395 0.426 2.754 1.00 10.89 O ANISOU 1151 OG SER A 150 848 1307 1984 -158 -297 363 O ATOM 1152 N CYS A 151 3.884 -2.024 1.941 1.00 6.59 N ANISOU 1152 N CYS A 151 855 699 949 -67 -358 78 N ATOM 1153 CA CYS A 151 3.457 -3.349 1.538 1.00 5.64 C ANISOU 1153 CA CYS A 151 678 662 802 -198 -209 57 C ATOM 1154 C CYS A 151 3.310 -4.204 2.778 1.00 5.09 C ANISOU 1154 C CYS A 151 569 710 655 44 -102 -38 C ATOM 1155 O CYS A 151 3.921 -3.943 3.823 1.00 6.14 O ANISOU 1155 O CYS A 151 786 902 647 -115 -175 -9 O ATOM 1156 CB CYS A 151 4.416 -3.995 0.525 1.00 6.56 C ANISOU 1156 CB CYS A 151 788 905 801 -70 -103 90 C ATOM 1157 SG CYS A 151 6.059 -4.364 1.186 1.00 7.00 S ANISOU 1157 SG CYS A 151 827 981 852 -62 -65 185 S ATOM 1158 N LEU A 152 2.527 -5.283 2.641 1.00 4.74 N ANISOU 1158 N LEU A 152 565 634 604 -11 -97 30 N ATOM 1159 CA LEU A 152 2.556 -6.330 3.663 1.00 4.98 C ANISOU 1159 CA LEU A 152 560 722 611 -12 -50 46 C ATOM 1160 C LEU A 152 3.910 -7.005 3.625 1.00 5.27 C ANISOU 1160 C LEU A 152 675 724 604 85 -40 24 C ATOM 1161 O LEU A 152 4.479 -7.245 2.552 1.00 6.17 O ANISOU 1161 O LEU A 152 762 961 620 262 27 44 O ATOM 1162 CB LEU A 152 1.441 -7.354 3.392 1.00 5.31 C ANISOU 1162 CB LEU A 152 661 691 667 5 -101 6 C ATOM 1163 CG LEU A 152 0.029 -6.758 3.326 1.00 6.05 C ANISOU 1163 CG LEU A 152 586 998 715 -41 -18 -65 C ATOM 1164 CD1 LEU A 152 -0.971 -7.885 3.047 1.00 8.32 C ANISOU 1164 CD1 LEU A 152 820 1259 1083 -293 -24 -119 C ATOM 1165 CD2 LEU A 152 -0.335 -6.010 4.596 1.00 8.72 C ANISOU 1165 CD2 LEU A 152 781 1474 1059 133 31 -350 C ATOM 1166 N MET A 153 4.435 -7.321 4.814 1.00 5.41 N ANISOU 1166 N MET A 153 648 759 649 135 -90 13 N ATOM 1167 CA MET A 153 5.713 -7.999 4.918 1.00 6.14 C ANISOU 1167 CA MET A 153 628 986 718 249 -89 77 C ATOM 1168 C MET A 153 5.766 -8.771 6.228 1.00 6.77 C ANISOU 1168 C MET A 153 793 1115 663 363 12 53 C ATOM 1169 O MET A 153 5.863 -8.185 7.303 1.00 7.30 O ANISOU 1169 O MET A 153 890 1214 667 280 17 45 O ATOM 1170 CB MET A 153 6.877 -6.996 4.881 1.00 6.77 C ANISOU 1170 CB MET A 153 594 1184 796 162 -15 22 C ATOM 1171 CG MET A 153 8.165 -7.823 4.849 1.00 8.60 C ANISOU 1171 CG MET A 153 650 1277 1339 162 -76 -260 C ATOM 1172 SD AMET A 153 9.604 -6.730 5.218 0.61 5.83 S ANISOU 1172 SD AMET A 153 469 876 870 103 -88 81 S ATOM 1173 SD BMET A 153 9.100 -7.631 6.175 0.39 15.92 S ANISOU 1173 SD BMET A 153 1460 2866 1723 921 -654 -651 S ATOM 1174 CE AMET A 153 10.867 -7.979 5.399 0.61 9.38 C ANISOU 1174 CE AMET A 153 773 1943 848 876 -217 -351 C ATOM 1175 CE BMET A 153 10.756 -8.058 5.604 0.39 13.63 C ANISOU 1175 CE BMET A 153 861 1776 2542 275 -478 1231 C ATOM 1176 N GLY A 154 5.719 -10.111 6.129 1.00 7.82 N ANISOU 1176 N GLY A 154 1020 1051 901 327 -132 186 N ATOM 1177 CA GLY A 154 5.896 -10.900 7.352 1.00 8.39 C ANISOU 1177 CA GLY A 154 1086 1171 929 82 -172 223 C ATOM 1178 C GLY A 154 7.410 -10.942 7.702 1.00 7.62 C ANISOU 1178 C GLY A 154 1036 1002 859 334 -23 146 C ATOM 1179 O GLY A 154 8.279 -11.104 6.841 1.00 10.12 O ANISOU 1179 O GLY A 154 1140 1888 817 362 17 151 O ATOM 1180 N TYR A 155 7.718 -10.769 8.964 1.00 7.63 N ANISOU 1180 N TYR A 155 989 1064 846 392 -98 35 N ATOM 1181 CA TYR A 155 9.122 -10.721 9.412 1.00 7.72 C ANISOU 1181 CA TYR A 155 915 1221 797 387 27 -62 C ATOM 1182 C TYR A 155 9.364 -11.441 10.724 1.00 7.50 C ANISOU 1182 C TYR A 155 1024 1021 802 496 27 -55 C ATOM 1183 O TYR A 155 10.510 -11.753 11.041 1.00 8.33 O ANISOU 1183 O TYR A 155 985 1232 949 471 -15 -25 O ATOM 1184 CB TYR A 155 9.677 -9.263 9.467 1.00 7.91 C ANISOU 1184 CB TYR A 155 932 1179 893 273 125 86 C ATOM 1185 CG TYR A 155 8.920 -8.486 10.506 1.00 7.11 C ANISOU 1185 CG TYR A 155 836 1067 798 216 -6 97 C ATOM 1186 CD1 TYR A 155 9.410 -8.371 11.828 1.00 7.09 C ANISOU 1186 CD1 TYR A 155 810 1012 872 187 -32 185 C ATOM 1187 CD2 TYR A 155 7.693 -7.854 10.212 1.00 6.84 C ANISOU 1187 CD2 TYR A 155 792 926 881 160 -42 96 C ATOM 1188 CE1 TYR A 155 8.738 -7.686 12.798 1.00 6.52 C ANISOU 1188 CE1 TYR A 155 693 979 805 112 -68 196 C ATOM 1189 CE2 TYR A 155 7.021 -7.177 11.227 1.00 7.20 C ANISOU 1189 CE2 TYR A 155 755 1051 930 188 -114 69 C ATOM 1190 CZ TYR A 155 7.526 -7.069 12.510 1.00 6.62 C ANISOU 1190 CZ TYR A 155 766 973 777 193 26 234 C ATOM 1191 OH TYR A 155 6.791 -6.416 13.437 1.00 7.12 O ANISOU 1191 OH TYR A 155 754 1106 846 140 15 81 O ATOM 1192 N GLN A 156 8.359 -11.637 11.585 1.00 7.86 N ANISOU 1192 N GLN A 156 973 1014 999 202 48 111 N ATOM 1193 CA GLN A 156 8.673 -12.133 12.925 1.00 7.57 C ANISOU 1193 CA GLN A 156 939 1045 891 271 -21 17 C ATOM 1194 C GLN A 156 8.973 -13.602 12.900 1.00 7.82 C ANISOU 1194 C GLN A 156 1027 1048 894 149 35 82 C ATOM 1195 O GLN A 156 8.441 -14.352 12.079 1.00 8.68 O ANISOU 1195 O GLN A 156 1282 998 1018 122 -39 51 O ATOM 1196 CB GLN A 156 7.478 -11.981 13.926 1.00 8.62 C ANISOU 1196 CB GLN A 156 1193 1156 924 188 145 -9 C ATOM 1197 CG GLN A 156 7.284 -10.519 14.325 1.00 8.69 C ANISOU 1197 CG GLN A 156 1174 1156 973 144 260 14 C ATOM 1198 CD GLN A 156 6.320 -10.462 15.483 1.00 8.37 C ANISOU 1198 CD GLN A 156 1177 1102 899 -82 161 -3 C ATOM 1199 OE1 GLN A 156 5.300 -11.126 15.480 1.00 8.31 O ANISOU 1199 OE1 GLN A 156 1146 1118 892 -131 182 -1 O ATOM 1200 NE2 GLN A 156 6.637 -9.661 16.485 1.00 8.74 N ANISOU 1200 NE2 GLN A 156 1189 1234 900 45 57 -106 N ATOM 1201 N ASP A 157 9.804 -14.002 13.858 1.00 8.01 N ANISOU 1201 N ASP A 157 1054 1201 787 320 130 165 N ATOM 1202 CA ASP A 157 9.945 -15.412 14.203 1.00 9.45 C ANISOU 1202 CA ASP A 157 1382 1184 1024 278 258 297 C ATOM 1203 C ASP A 157 10.397 -16.241 13.007 1.00 9.03 C ANISOU 1203 C ASP A 157 1336 993 1102 249 158 261 C ATOM 1204 O ASP A 157 9.927 -17.361 12.771 1.00 11.01 O ANISOU 1204 O ASP A 157 1557 1028 1598 257 145 232 O ATOM 1205 CB ASP A 157 8.610 -15.914 14.808 1.00 11.24 C ANISOU 1205 CB ASP A 157 1271 1699 1299 135 258 461 C ATOM 1206 CG ASP A 157 8.697 -17.258 15.472 1.00 14.88 C ANISOU 1206 CG ASP A 157 1567 1977 2108 -63 83 964 C ATOM 1207 OD1 ASP A 157 7.662 -17.980 15.447 1.00 21.84 O ANISOU 1207 OD1 ASP A 157 1819 2623 3856 -401 -26 1813 O ATOM 1208 OD2 ASP A 157 9.759 -17.635 16.024 1.00 20.68 O ANISOU 1208 OD2 ASP A 157 1806 3141 2910 -10 -190 2005 O ATOM 1209 N SER A 158 11.368 -15.718 12.272 1.00 9.33 N ANISOU 1209 N SER A 158 1452 951 1142 376 395 173 N ATOM 1210 CA SER A 158 12.052 -16.530 11.240 1.00 9.06 C ANISOU 1210 CA SER A 158 1367 1050 1023 356 91 -41 C ATOM 1211 C SER A 158 13.534 -16.263 11.324 1.00 7.22 C ANISOU 1211 C SER A 158 1286 827 632 431 157 141 C ATOM 1212 O SER A 158 13.995 -15.130 11.283 1.00 7.91 O ANISOU 1212 O SER A 158 1297 911 796 539 137 147 O ATOM 1213 CB SER A 158 11.566 -16.220 9.828 1.00 9.31 C ANISOU 1213 CB SER A 158 1357 1045 1134 332 -23 43 C ATOM 1214 OG SER A 158 12.324 -16.967 8.886 1.00 10.76 O ANISOU 1214 OG SER A 158 1933 1119 1036 402 98 -7 O ATOM 1215 N SER A 159 14.298 -17.377 11.385 1.00 8.33 N ANISOU 1215 N SER A 159 1397 859 910 439 176 196 N ATOM 1216 CA SER A 159 15.742 -17.297 11.418 1.00 8.38 C ANISOU 1216 CA SER A 159 1350 1016 817 583 137 234 C ATOM 1217 C SER A 159 16.361 -17.057 10.063 1.00 8.27 C ANISOU 1217 C SER A 159 1176 1150 816 584 97 240 C ATOM 1218 O SER A 159 17.563 -16.807 10.003 1.00 8.59 O ANISOU 1218 O SER A 159 1287 1088 889 560 74 198 O ATOM 1219 CB SER A 159 16.263 -18.663 11.992 1.00 10.75 C ANISOU 1219 CB SER A 159 1937 1273 875 934 202 402 C ATOM 1220 OG SER A 159 15.965 -18.713 13.380 1.00 12.57 O ANISOU 1220 OG SER A 159 2561 1336 878 911 404 397 O ATOM 1221 N VAL A 160 15.560 -17.111 8.983 1.00 7.88 N ANISOU 1221 N VAL A 160 1223 1016 753 498 183 188 N ATOM 1222 CA VAL A 160 16.041 -16.891 7.628 1.00 7.24 C ANISOU 1222 CA VAL A 160 1098 876 775 426 161 74 C ATOM 1223 C VAL A 160 15.913 -15.414 7.328 1.00 7.00 C ANISOU 1223 C VAL A 160 1001 793 865 387 59 99 C ATOM 1224 O VAL A 160 14.783 -14.858 7.438 1.00 8.10 O ANISOU 1224 O VAL A 160 1069 949 1060 529 149 174 O ATOM 1225 CB VAL A 160 15.186 -17.682 6.654 1.00 7.29 C ANISOU 1225 CB VAL A 160 1163 730 878 273 226 115 C ATOM 1226 CG1 VAL A 160 15.636 -17.434 5.190 1.00 7.81 C ANISOU 1226 CG1 VAL A 160 1251 870 848 294 181 174 C ATOM 1227 CG2 VAL A 160 15.164 -19.188 6.901 1.00 9.32 C ANISOU 1227 CG2 VAL A 160 1614 773 1153 327 462 279 C ATOM 1228 N PRO A 161 16.986 -14.697 7.067 1.00 7.03 N ANISOU 1228 N PRO A 161 1039 871 761 428 98 133 N ATOM 1229 CA PRO A 161 16.908 -13.243 7.004 1.00 6.95 C ANISOU 1229 CA PRO A 161 1010 816 815 267 -14 123 C ATOM 1230 C PRO A 161 16.259 -12.747 5.729 1.00 6.55 C ANISOU 1230 C PRO A 161 1018 808 663 352 97 -8 C ATOM 1231 O PRO A 161 16.342 -13.397 4.675 1.00 9.70 O ANISOU 1231 O PRO A 161 1761 1166 760 770 -186 -119 O ATOM 1232 CB PRO A 161 18.395 -12.835 7.036 1.00 7.74 C ANISOU 1232 CB PRO A 161 956 1050 935 339 13 76 C ATOM 1233 CG PRO A 161 19.084 -13.942 6.274 1.00 8.68 C ANISOU 1233 CG PRO A 161 1076 1030 1194 481 130 222 C ATOM 1234 CD PRO A 161 18.372 -15.190 6.804 1.00 8.31 C ANISOU 1234 CD PRO A 161 980 1055 1121 479 163 257 C ATOM 1235 N SER A 162 15.584 -11.619 5.832 1.00 6.25 N ANISOU 1235 N SER A 162 892 819 663 293 -48 98 N ATOM 1236 CA SER A 162 14.988 -10.915 4.689 1.00 6.35 C ANISOU 1236 CA SER A 162 830 824 759 264 -87 132 C ATOM 1237 C SER A 162 15.981 -9.950 4.120 1.00 6.19 C ANISOU 1237 C SER A 162 890 786 677 327 47 38 C ATOM 1238 O SER A 162 16.850 -9.442 4.835 1.00 7.13 O ANISOU 1238 O SER A 162 952 1124 633 89 -3 100 O ATOM 1239 CB SER A 162 13.755 -10.161 5.164 1.00 6.98 C ANISOU 1239 CB SER A 162 845 869 938 269 -12 149 C ATOM 1240 OG SER A 162 12.737 -10.971 5.695 1.00 7.92 O ANISOU 1240 OG SER A 162 865 1118 1028 207 -14 323 O ATOM 1241 N THR A 163 15.759 -9.629 2.814 1.00 6.69 N ANISOU 1241 N THR A 163 948 858 735 263 -42 120 N ATOM 1242 CA THR A 163 16.607 -8.643 2.171 1.00 6.58 C ANISOU 1242 CA THR A 163 906 788 806 269 32 183 C ATOM 1243 C THR A 163 15.743 -7.481 1.667 1.00 6.02 C ANISOU 1243 C THR A 163 755 792 741 174 -144 121 C ATOM 1244 O THR A 163 14.874 -7.669 0.824 1.00 6.68 O ANISOU 1244 O THR A 163 898 804 835 136 -238 41 O ATOM 1245 CB THR A 163 17.357 -9.231 0.948 1.00 8.41 C ANISOU 1245 CB THR A 163 1383 796 1017 396 312 210 C ATOM 1246 OG1 THR A 163 17.986 -10.458 1.358 1.00 9.33 O ANISOU 1246 OG1 THR A 163 1238 1077 1230 559 -5 47 O ATOM 1247 CG2 THR A 163 18.433 -8.251 0.474 1.00 10.29 C ANISOU 1247 CG2 THR A 163 1194 1513 1203 282 403 353 C ATOM 1248 N ILE A 164 16.016 -6.301 2.223 1.00 5.55 N ANISOU 1248 N ILE A 164 780 796 535 149 -46 54 N ATOM 1249 CA ILE A 164 15.341 -5.073 1.770 1.00 5.28 C ANISOU 1249 CA ILE A 164 726 741 539 112 -42 34 C ATOM 1250 C ILE A 164 16.291 -4.374 0.818 1.00 5.24 C ANISOU 1250 C ILE A 164 582 875 534 154 -41 13 C ATOM 1251 O ILE A 164 17.401 -4.021 1.208 1.00 6.60 O ANISOU 1251 O ILE A 164 620 1276 610 14 -60 97 O ATOM 1252 CB ILE A 164 14.977 -4.148 2.955 1.00 5.82 C ANISOU 1252 CB ILE A 164 788 842 582 59 20 -30 C ATOM 1253 CG1 ILE A 164 13.975 -4.841 3.888 1.00 7.90 C ANISOU 1253 CG1 ILE A 164 1080 1169 751 43 279 -46 C ATOM 1254 CG2 ILE A 164 14.470 -2.817 2.444 1.00 7.23 C ANISOU 1254 CG2 ILE A 164 970 870 908 191 66 -81 C ATOM 1255 CD1 ILE A 164 13.728 -4.074 5.167 1.00 9.85 C ANISOU 1255 CD1 ILE A 164 1643 1313 787 213 284 -32 C ATOM 1256 N ARG A 165 15.839 -4.170 -0.440 1.00 5.24 N ANISOU 1256 N ARG A 165 583 817 591 58 7 40 N ATOM 1257 CA ARG A 165 16.695 -3.527 -1.444 1.00 5.55 C ANISOU 1257 CA ARG A 165 738 844 526 102 14 56 C ATOM 1258 C ARG A 165 16.044 -2.216 -1.832 1.00 5.16 C ANISOU 1258 C ARG A 165 641 783 536 -3 29 -40 C ATOM 1259 O ARG A 165 14.929 -2.173 -2.386 1.00 5.58 O ANISOU 1259 O ARG A 165 643 761 715 -12 -109 35 O ATOM 1260 CB ARG A 165 16.802 -4.478 -2.657 1.00 5.75 C ANISOU 1260 CB ARG A 165 702 931 553 94 53 -65 C ATOM 1261 CG ARG A 165 17.617 -3.859 -3.814 1.00 7.42 C ANISOU 1261 CG ARG A 165 942 1174 703 105 214 -50 C ATOM 1262 CD ARG A 165 17.869 -4.986 -4.870 1.00 8.40 C ANISOU 1262 CD ARG A 165 1131 1404 656 -95 227 -131 C ATOM 1263 NE ARG A 165 18.909 -4.518 -5.809 1.00 8.11 N ANISOU 1263 NE ARG A 165 1090 1220 773 -29 211 -108 N ATOM 1264 CZ ARG A 165 18.685 -3.867 -6.938 1.00 7.76 C ANISOU 1264 CZ ARG A 165 1041 1246 662 -137 196 -256 C ATOM 1265 NH1 ARG A 165 17.418 -3.642 -7.351 1.00 8.34 N ANISOU 1265 NH1 ARG A 165 1095 1138 936 -136 71 -93 N ATOM 1266 NH2 ARG A 165 19.724 -3.467 -7.647 1.00 9.19 N ANISOU 1266 NH2 ARG A 165 1125 1557 811 -378 244 -150 N ATOM 1267 N VAL A 166 16.746 -1.135 -1.525 1.00 5.19 N ANISOU 1267 N VAL A 166 586 836 552 9 -15 -14 N ATOM 1268 CA VAL A 166 16.278 0.224 -1.777 1.00 5.56 C ANISOU 1268 CA VAL A 166 715 720 678 -60 39 8 C ATOM 1269 C VAL A 166 17.082 0.778 -2.928 1.00 5.75 C ANISOU 1269 C VAL A 166 647 812 725 17 -19 -33 C ATOM 1270 O VAL A 166 18.322 0.784 -2.890 1.00 7.04 O ANISOU 1270 O VAL A 166 584 1203 889 -137 -61 212 O ATOM 1271 CB VAL A 166 16.505 1.132 -0.541 1.00 6.67 C ANISOU 1271 CB VAL A 166 750 948 835 -19 -6 -173 C ATOM 1272 CG1 VAL A 166 15.847 2.493 -0.770 1.00 8.18 C ANISOU 1272 CG1 VAL A 166 1254 891 964 38 -180 -309 C ATOM 1273 CG2 VAL A 166 16.013 0.444 0.706 1.00 7.37 C ANISOU 1273 CG2 VAL A 166 972 1116 715 -18 18 -239 C ATOM 1274 N THR A 167 16.397 1.251 -3.981 1.00 5.69 N ANISOU 1274 N THR A 167 620 806 736 -52 -17 13 N ATOM 1275 CA THR A 167 17.079 1.841 -5.111 1.00 5.85 C ANISOU 1275 CA THR A 167 655 863 704 -45 14 -21 C ATOM 1276 C THR A 167 16.516 3.220 -5.364 1.00 5.41 C ANISOU 1276 C THR A 167 601 810 645 -124 19 -1 C ATOM 1277 O THR A 167 15.333 3.483 -5.219 1.00 5.99 O ANISOU 1277 O THR A 167 546 826 903 -115 17 114 O ATOM 1278 CB THR A 167 16.935 0.978 -6.393 1.00 6.41 C ANISOU 1278 CB THR A 167 685 931 818 -8 -32 -64 C ATOM 1279 OG1 THR A 167 15.562 0.670 -6.637 1.00 6.56 O ANISOU 1279 OG1 THR A 167 738 960 794 -118 -65 -13 O ATOM 1280 CG2 THR A 167 17.737 -0.320 -6.280 1.00 7.20 C ANISOU 1280 CG2 THR A 167 858 873 1006 63 29 -84 C ATOM 1281 N TYR A 168 17.429 4.137 -5.767 1.00 5.75 N ANISOU 1281 N TYR A 168 586 879 718 -170 45 -7 N ATOM 1282 CA TYR A 168 17.044 5.488 -6.119 1.00 5.64 C ANISOU 1282 CA TYR A 168 757 752 635 -113 140 -89 C ATOM 1283 C TYR A 168 17.736 5.815 -7.461 1.00 5.52 C ANISOU 1283 C TYR A 168 693 670 736 -158 13 -108 C ATOM 1284 O TYR A 168 18.973 5.854 -7.520 1.00 6.47 O ANISOU 1284 O TYR A 168 614 1045 800 -197 80 -70 O ATOM 1285 CB TYR A 168 17.452 6.491 -5.029 1.00 6.32 C ANISOU 1285 CB TYR A 168 811 938 651 -203 -5 -71 C ATOM 1286 CG TYR A 168 16.959 7.890 -5.325 1.00 6.13 C ANISOU 1286 CG TYR A 168 801 808 719 -279 36 -144 C ATOM 1287 CD1 TYR A 168 15.596 8.182 -5.441 1.00 7.37 C ANISOU 1287 CD1 TYR A 168 802 892 1106 -174 298 -141 C ATOM 1288 CD2 TYR A 168 17.851 8.948 -5.491 1.00 6.63 C ANISOU 1288 CD2 TYR A 168 948 877 694 -303 67 -110 C ATOM 1289 CE1 TYR A 168 15.118 9.450 -5.714 1.00 7.39 C ANISOU 1289 CE1 TYR A 168 967 729 1113 -258 228 -161 C ATOM 1290 CE2 TYR A 168 17.376 10.221 -5.749 1.00 6.85 C ANISOU 1290 CE2 TYR A 168 907 841 854 -278 211 -206 C ATOM 1291 CZ TYR A 168 16.040 10.488 -5.883 1.00 6.86 C ANISOU 1291 CZ TYR A 168 902 837 866 -233 228 -115 C ATOM 1292 OH TYR A 168 15.540 11.744 -6.104 1.00 8.31 O ANISOU 1292 OH TYR A 168 1030 784 1343 -215 200 -88 O ATOM 1293 N ASP A 169 16.916 5.943 -8.490 1.00 6.03 N ANISOU 1293 N ASP A 169 773 875 642 -119 35 -70 N ATOM 1294 CA ASP A 169 17.404 5.950 -9.857 1.00 6.64 C ANISOU 1294 CA ASP A 169 863 963 697 -175 117 -92 C ATOM 1295 C ASP A 169 17.152 7.286 -10.533 1.00 6.32 C ANISOU 1295 C ASP A 169 839 930 633 -184 99 -96 C ATOM 1296 O ASP A 169 16.048 7.578 -11.038 1.00 7.03 O ANISOU 1296 O ASP A 169 879 990 804 -190 42 -30 O ATOM 1297 CB ASP A 169 16.726 4.813 -10.667 1.00 7.86 C ANISOU 1297 CB ASP A 169 1045 1081 861 -246 -20 -262 C ATOM 1298 CG ASP A 169 17.410 4.592 -12.021 1.00 8.69 C ANISOU 1298 CG ASP A 169 1385 1041 876 -125 -32 -279 C ATOM 1299 OD1 ASP A 169 18.311 5.387 -12.373 1.00 11.56 O ANISOU 1299 OD1 ASP A 169 1867 1598 928 -380 500 -294 O ATOM 1300 OD2 ASP A 169 17.024 3.625 -12.683 1.00 10.92 O ANISOU 1300 OD2 ASP A 169 1727 1311 1111 -65 -246 -469 O ATOM 1301 N LEU A 170 18.199 8.127 -10.563 1.00 6.62 N ANISOU 1301 N LEU A 170 929 890 698 -241 80 -79 N ATOM 1302 CA LEU A 170 18.112 9.408 -11.234 1.00 7.64 C ANISOU 1302 CA LEU A 170 1196 903 804 -356 91 -35 C ATOM 1303 C LEU A 170 18.030 9.256 -12.741 1.00 8.61 C ANISOU 1303 C LEU A 170 1331 1147 792 -450 -64 14 C ATOM 1304 O LEU A 170 17.644 10.228 -13.379 1.00 11.48 O ANISOU 1304 O LEU A 170 2038 1339 984 -492 -267 162 O ATOM 1305 CB LEU A 170 19.377 10.266 -10.941 1.00 7.42 C ANISOU 1305 CB LEU A 170 1007 977 834 -282 71 -215 C ATOM 1306 CG LEU A 170 19.475 10.946 -9.576 1.00 8.32 C ANISOU 1306 CG LEU A 170 1022 1232 909 -202 32 -224 C ATOM 1307 CD1 LEU A 170 18.251 11.855 -9.280 1.00 10.90 C ANISOU 1307 CD1 LEU A 170 1523 1277 1340 61 357 -313 C ATOM 1308 CD2 LEU A 170 19.698 9.962 -8.474 1.00 9.02 C ANISOU 1308 CD2 LEU A 170 1326 1221 880 -307 28 -178 C ATOM 1309 N GLU A 171 18.366 8.074 -13.249 1.00 8.81 N ANISOU 1309 N GLU A 171 1233 1379 737 -501 145 -181 N ATOM 1310 CA GLU A 171 18.309 7.820 -14.694 1.00 11.39 C ANISOU 1310 CA GLU A 171 1421 2110 796 -826 299 -400 C ATOM 1311 C GLU A 171 16.964 7.165 -15.062 1.00 13.54 C ANISOU 1311 C GLU A 171 1617 2745 785 -1126 229 -347 C ATOM 1312 O GLU A 171 16.814 6.737 -16.227 1.00 18.32 O ANISOU 1312 O GLU A 171 1911 4247 804 -1577 247 -622 O ATOM 1313 CB GLU A 171 19.459 6.883 -15.095 1.00 11.82 C ANISOU 1313 CB GLU A 171 1673 1945 875 -853 463 -472 C ATOM 1314 CG GLU A 171 20.811 7.549 -15.082 1.00 10.74 C ANISOU 1314 CG GLU A 171 1399 1800 884 -421 162 -175 C ATOM 1315 CD GLU A 171 21.351 7.787 -13.674 1.00 10.01 C ANISOU 1315 CD GLU A 171 1384 1557 863 -386 288 -173 C ATOM 1316 OE1 GLU A 171 21.453 6.779 -12.909 1.00 11.32 O ANISOU 1316 OE1 GLU A 171 1844 1615 844 -559 305 -27 O ATOM 1317 OE2 GLU A 171 21.739 8.940 -13.351 1.00 12.00 O ANISOU 1317 OE2 GLU A 171 2009 1581 969 -646 86 -64 O ATOM 1318 N ASP A 172 15.994 7.145 -14.130 1.00 9.17 N ANISOU 1318 N ASP A 172 1124 1509 850 -547 79 -73 N ATOM 1319 CA ASP A 172 14.621 6.706 -14.429 1.00 10.28 C ANISOU 1319 CA ASP A 172 1203 1806 898 -455 -66 -208 C ATOM 1320 C ASP A 172 13.647 7.689 -13.781 1.00 9.70 C ANISOU 1320 C ASP A 172 1126 1537 1024 -564 -16 -33 C ATOM 1321 O ASP A 172 12.685 7.289 -13.135 1.00 9.87 O ANISOU 1321 O ASP A 172 1208 1573 970 -499 19 67 O ATOM 1322 CB ASP A 172 14.469 5.241 -13.951 1.00 12.39 C ANISOU 1322 CB ASP A 172 1280 1646 1781 -631 42 -420 C ATOM 1323 CG ASP A 172 13.241 4.538 -14.530 1.00 15.48 C ANISOU 1323 CG ASP A 172 1885 2580 1419 -1171 -147 -633 C ATOM 1324 OD1 ASP A 172 12.506 5.124 -15.359 1.00 18.35 O ANISOU 1324 OD1 ASP A 172 1859 3289 1823 -725 -401 -846 O ATOM 1325 OD2 ASP A 172 13.025 3.365 -14.133 1.00 20.28 O ANISOU 1325 OD2 ASP A 172 2491 2770 2445 -1695 -86 -425 O ATOM 1326 N ASP A 173 13.927 8.991 -13.951 1.00 9.87 N ANISOU 1326 N ASP A 173 1417 1521 813 -512 -28 107 N ATOM 1327 CA ASP A 173 13.039 10.077 -13.461 1.00 10.12 C ANISOU 1327 CA ASP A 173 1281 1477 1087 -437 20 351 C ATOM 1328 C ASP A 173 12.800 9.973 -11.965 1.00 8.29 C ANISOU 1328 C ASP A 173 1103 961 1087 -349 0 267 C ATOM 1329 O ASP A 173 11.685 10.133 -11.456 1.00 8.87 O ANISOU 1329 O ASP A 173 1085 1090 1195 -299 34 298 O ATOM 1330 CB ASP A 173 11.723 10.066 -14.286 1.00 13.55 C ANISOU 1330 CB ASP A 173 1682 2116 1351 -216 -326 851 C ATOM 1331 CG AASP A 173 12.036 10.472 -15.707 0.50 15.07 C ANISOU 1331 CG AASP A 173 2033 2332 1360 -842 -352 747 C ATOM 1332 CG BASP A 173 10.865 11.291 -14.065 0.50 16.17 C ANISOU 1332 CG BASP A 173 1560 1909 2675 -299 -97 1188 C ATOM 1333 OD1AASP A 173 12.547 11.593 -15.935 0.50 18.19 O ANISOU 1333 OD1AASP A 173 2519 2685 1707 -1250 -456 1041 O ATOM 1334 OD1BASP A 173 11.424 12.371 -13.767 0.50 18.55 O ANISOU 1334 OD1BASP A 173 2951 2235 1862 -726 726 367 O ATOM 1335 OD2AASP A 173 11.839 9.697 -16.659 0.50 27.20 O ANISOU 1335 OD2AASP A 173 5967 2879 1490 -1841 392 375 O ATOM 1336 OD2BASP A 173 9.632 11.179 -14.214 0.50 24.79 O ANISOU 1336 OD2BASP A 173 1547 3024 4848 -91 -341 1919 O ATOM 1337 N ASN A 174 13.897 9.773 -11.194 1.00 7.43 N ANISOU 1337 N ASN A 174 964 865 994 -366 98 84 N ATOM 1338 CA ASN A 174 13.906 9.822 -9.758 1.00 7.45 C ANISOU 1338 CA ASN A 174 970 939 922 -349 163 -18 C ATOM 1339 C ASN A 174 13.031 8.685 -9.174 1.00 6.34 C ANISOU 1339 C ASN A 174 777 843 789 -377 -11 -4 C ATOM 1340 O ASN A 174 12.250 8.940 -8.266 1.00 8.05 O ANISOU 1340 O ASN A 174 1061 977 1021 -368 190 -100 O ATOM 1341 CB ASN A 174 13.415 11.177 -9.187 1.00 9.85 C ANISOU 1341 CB ASN A 174 1569 995 1178 -475 234 -105 C ATOM 1342 CG ASN A 174 13.989 12.313 -9.968 1.00 9.41 C ANISOU 1342 CG ASN A 174 1243 939 1392 -303 154 -21 C ATOM 1343 OD1 ASN A 174 15.235 12.471 -10.040 1.00 10.74 O ANISOU 1343 OD1 ASN A 174 1373 1330 1378 -461 197 -6 O ATOM 1344 ND2 ASN A 174 13.098 13.137 -10.492 1.00 13.12 N ANISOU 1344 ND2 ASN A 174 1881 1244 1860 13 -64 86 N ATOM 1345 N LEU A 175 13.189 7.477 -9.707 1.00 6.24 N ANISOU 1345 N LEU A 175 725 737 907 -235 62 60 N ATOM 1346 CA LEU A 175 12.396 6.354 -9.178 1.00 6.03 C ANISOU 1346 CA LEU A 175 843 712 735 -237 36 43 C ATOM 1347 C LEU A 175 13.020 5.869 -7.860 1.00 5.51 C ANISOU 1347 C LEU A 175 616 739 739 -220 40 -42 C ATOM 1348 O LEU A 175 14.182 5.420 -7.817 1.00 6.17 O ANISOU 1348 O LEU A 175 691 901 751 -140 89 5 O ATOM 1349 CB LEU A 175 12.408 5.213 -10.203 1.00 7.03 C ANISOU 1349 CB LEU A 175 980 933 759 -435 108 -169 C ATOM 1350 CG LEU A 175 11.512 4.008 -9.790 1.00 7.25 C ANISOU 1350 CG LEU A 175 1095 717 943 -350 -55 58 C ATOM 1351 CD1 LEU A 175 10.056 4.428 -9.756 1.00 7.56 C ANISOU 1351 CD1 LEU A 175 1037 1024 814 -447 -60 23 C ATOM 1352 CD2 LEU A 175 11.727 2.863 -10.751 1.00 11.32 C ANISOU 1352 CD2 LEU A 175 1712 984 1606 -451 141 -483 C ATOM 1353 N LEU A 176 12.220 5.907 -6.808 1.00 5.51 N ANISOU 1353 N LEU A 176 730 675 687 -120 -15 0 N ATOM 1354 CA LEU A 176 12.555 5.318 -5.485 1.00 5.31 C ANISOU 1354 CA LEU A 176 651 664 701 -162 1 -38 C ATOM 1355 C LEU A 176 11.773 4.008 -5.406 1.00 5.04 C ANISOU 1355 C LEU A 176 591 669 657 -80 12 24 C ATOM 1356 O LEU A 176 10.544 4.041 -5.516 1.00 5.93 O ANISOU 1356 O LEU A 176 590 686 976 -140 -22 131 O ATOM 1357 CB LEU A 176 12.143 6.267 -4.383 1.00 5.98 C ANISOU 1357 CB LEU A 176 742 782 746 -71 8 -113 C ATOM 1358 CG LEU A 176 12.275 5.729 -2.973 1.00 6.03 C ANISOU 1358 CG LEU A 176 711 766 816 -30 27 -30 C ATOM 1359 CD1 LEU A 176 13.759 5.426 -2.622 1.00 7.16 C ANISOU 1359 CD1 LEU A 176 831 1007 882 24 -141 -144 C ATOM 1360 CD2 LEU A 176 11.706 6.735 -1.968 1.00 8.18 C ANISOU 1360 CD2 LEU A 176 954 1345 808 131 119 -176 C ATOM 1361 N LYS A 177 12.475 2.910 -5.214 1.00 5.01 N ANISOU 1361 N LYS A 177 592 665 645 -131 -43 27 N ATOM 1362 CA LYS A 177 11.835 1.605 -5.176 1.00 5.14 C ANISOU 1362 CA LYS A 177 634 663 658 -155 -39 14 C ATOM 1363 C LYS A 177 12.390 0.836 -3.985 1.00 4.82 C ANISOU 1363 C LYS A 177 601 607 624 -37 -6 -6 C ATOM 1364 O LYS A 177 13.576 0.921 -3.660 1.00 5.34 O ANISOU 1364 O LYS A 177 552 723 755 -104 -53 40 O ATOM 1365 CB LYS A 177 12.087 0.850 -6.483 1.00 6.08 C ANISOU 1365 CB LYS A 177 806 769 737 -186 -68 -44 C ATOM 1366 CG LYS A 177 11.470 -0.544 -6.538 1.00 6.66 C ANISOU 1366 CG LYS A 177 748 712 1071 -163 -72 -171 C ATOM 1367 CD LYS A 177 11.431 -1.081 -7.933 1.00 11.57 C ANISOU 1367 CD LYS A 177 1775 1278 1343 -441 233 -712 C ATOM 1368 CE LYS A 177 12.765 -1.434 -8.419 1.00 12.99 C ANISOU 1368 CE LYS A 177 1554 2279 1103 -408 78 -469 C ATOM 1369 NZ LYS A 177 12.550 -2.009 -9.780 1.00 14.49 N ANISOU 1369 NZ LYS A 177 2191 2133 1180 -648 669 -697 N ATOM 1370 N VAL A 178 11.488 0.083 -3.353 1.00 4.81 N ANISOU 1370 N VAL A 178 559 607 663 -38 8 -30 N ATOM 1371 CA VAL A 178 11.868 -0.857 -2.322 1.00 4.70 C ANISOU 1371 CA VAL A 178 602 600 582 11 8 13 C ATOM 1372 C VAL A 178 11.379 -2.255 -2.754 1.00 4.82 C ANISOU 1372 C VAL A 178 592 684 556 -17 -66 13 C ATOM 1373 O VAL A 178 10.215 -2.406 -3.103 1.00 5.55 O ANISOU 1373 O VAL A 178 566 676 867 -83 -116 45 O ATOM 1374 CB VAL A 178 11.278 -0.468 -0.961 1.00 5.78 C ANISOU 1374 CB VAL A 178 604 958 633 1 -19 -101 C ATOM 1375 CG1 VAL A 178 11.557 -1.540 0.083 1.00 8.15 C ANISOU 1375 CG1 VAL A 178 1082 1411 603 -48 57 183 C ATOM 1376 CG2 VAL A 178 11.829 0.891 -0.537 1.00 6.81 C ANISOU 1376 CG2 VAL A 178 753 1086 748 21 -78 -366 C ATOM 1377 N GLN A 179 12.300 -3.211 -2.702 1.00 5.09 N ANISOU 1377 N GLN A 179 599 649 685 -3 -95 50 N ATOM 1378 CA GLN A 179 12.005 -4.631 -2.915 1.00 5.39 C ANISOU 1378 CA GLN A 179 723 561 766 -33 -92 0 C ATOM 1379 C GLN A 179 12.260 -5.378 -1.619 1.00 5.09 C ANISOU 1379 C GLN A 179 582 668 682 34 -100 -20 C ATOM 1380 O GLN A 179 13.131 -5.000 -0.830 1.00 6.10 O ANISOU 1380 O GLN A 179 664 820 834 -25 -151 85 O ATOM 1381 CB GLN A 179 12.915 -5.192 -4.006 1.00 6.24 C ANISOU 1381 CB GLN A 179 824 854 692 30 -40 -27 C ATOM 1382 CG GLN A 179 12.630 -4.575 -5.399 1.00 6.47 C ANISOU 1382 CG GLN A 179 872 828 759 -47 97 30 C ATOM 1383 CD GLN A 179 13.843 -4.789 -6.307 1.00 7.56 C ANISOU 1383 CD GLN A 179 944 1099 831 -77 80 -198 C ATOM 1384 OE1 GLN A 179 14.827 -4.084 -6.159 1.00 8.13 O ANISOU 1384 OE1 GLN A 179 1023 1113 955 -145 175 -141 O ATOM 1385 NE2 GLN A 179 13.803 -5.753 -7.169 1.00 16.61 N ANISOU 1385 NE2 GLN A 179 1189 2626 2495 -396 532 -1822 N ATOM 1386 N VAL A 180 11.488 -6.449 -1.411 1.00 5.26 N ANISOU 1386 N VAL A 180 651 650 698 84 -62 51 N ATOM 1387 CA VAL A 180 11.700 -7.369 -0.310 1.00 5.80 C ANISOU 1387 CA VAL A 180 885 655 663 101 -16 111 C ATOM 1388 C VAL A 180 11.899 -8.739 -0.938 1.00 5.72 C ANISOU 1388 C VAL A 180 877 618 678 44 -91 87 C ATOM 1389 O VAL A 180 11.036 -9.245 -1.674 1.00 6.59 O ANISOU 1389 O VAL A 180 1021 627 857 5 -85 50 O ATOM 1390 CB VAL A 180 10.467 -7.388 0.635 1.00 6.56 C ANISOU 1390 CB VAL A 180 832 858 803 80 21 28 C ATOM 1391 CG1 VAL A 180 10.631 -8.488 1.683 1.00 8.51 C ANISOU 1391 CG1 VAL A 180 1131 1005 1099 124 235 356 C ATOM 1392 CG2 VAL A 180 10.248 -6.016 1.262 1.00 7.85 C ANISOU 1392 CG2 VAL A 180 1303 935 744 157 -14 -96 C ATOM 1393 N ASP A 181 13.082 -9.311 -0.678 1.00 6.80 N ANISOU 1393 N ASP A 181 971 776 836 185 21 39 N ATOM 1394 CA ASP A 181 13.415 -10.631 -1.248 1.00 7.79 C ANISOU 1394 CA ASP A 181 1233 759 970 277 -144 -55 C ATOM 1395 C ASP A 181 13.203 -10.610 -2.768 1.00 8.18 C ANISOU 1395 C ASP A 181 1309 795 1006 187 -51 -200 C ATOM 1396 O ASP A 181 12.747 -11.608 -3.347 1.00 9.81 O ANISOU 1396 O ASP A 181 1673 881 1174 114 -240 -253 O ATOM 1397 CB ASP A 181 12.595 -11.734 -0.605 1.00 8.84 C ANISOU 1397 CB ASP A 181 1379 871 1108 143 -245 59 C ATOM 1398 CG ASP A 181 12.672 -11.730 0.922 1.00 7.93 C ANISOU 1398 CG ASP A 181 1177 752 1083 200 -135 -73 C ATOM 1399 OD1 ASP A 181 13.518 -11.190 1.576 1.00 9.07 O ANISOU 1399 OD1 ASP A 181 1333 897 1215 152 -367 113 O ATOM 1400 OD2 ASP A 181 11.682 -12.419 1.433 1.00 9.84 O ANISOU 1400 OD2 ASP A 181 1231 1254 1252 124 58 -50 O ATOM 1401 N ASN A 182 13.604 -9.509 -3.398 1.00 8.06 N ANISOU 1401 N ASN A 182 1262 955 847 234 -47 -95 N ATOM 1402 CA ASN A 182 13.560 -9.316 -4.834 1.00 10.03 C ANISOU 1402 CA ASN A 182 1410 1658 746 117 74 -198 C ATOM 1403 C ASN A 182 12.167 -9.013 -5.349 1.00 12.97 C ANISOU 1403 C ASN A 182 1432 2742 755 -275 -182 -27 C ATOM 1404 O ASN A 182 11.997 -8.813 -6.533 1.00 30.27 O ANISOU 1404 O ASN A 182 1809 8683 1010 524 -96 1156 O ATOM 1405 CB ASN A 182 14.192 -10.473 -5.605 1.00 14.55 C ANISOU 1405 CB ASN A 182 2612 1717 1198 39 392 -535 C ATOM 1406 CG ASN A 182 15.659 -10.558 -5.214 1.00 22.92 C ANISOU 1406 CG ASN A 182 2194 2384 4132 698 856 -111 C ATOM 1407 OD1 ASN A 182 16.308 -9.515 -5.105 1.00 21.77 O ANISOU 1407 OD1 ASN A 182 2148 3071 3054 242 123 -218 O ATOM 1408 ND2 ASN A 182 16.129 -11.773 -5.019 1.00 39.82 N ANISOU 1408 ND2 ASN A 182 4012 2836 8280 1668 77 -185 N ATOM 1409 N LYS A 183 11.131 -8.965 -4.559 1.00 8.46 N ANISOU 1409 N LYS A 183 1363 992 860 159 -209 -121 N ATOM 1410 CA LYS A 183 9.780 -8.668 -5.049 1.00 9.27 C ANISOU 1410 CA LYS A 183 1457 848 1216 1 -322 10 C ATOM 1411 C LYS A 183 9.470 -7.214 -4.728 1.00 7.07 C ANISOU 1411 C LYS A 183 1054 822 810 -94 -200 59 C ATOM 1412 O LYS A 183 9.721 -6.744 -3.610 1.00 7.62 O ANISOU 1412 O LYS A 183 1022 912 960 6 -356 22 O ATOM 1413 CB LYS A 183 8.751 -9.550 -4.359 1.00 11.60 C ANISOU 1413 CB LYS A 183 1568 1003 1837 -299 -535 327 C ATOM 1414 CG LYS A 183 8.968 -11.025 -4.759 1.00 23.13 C ANISOU 1414 CG LYS A 183 3059 808 4920 -100 -163 291 C ATOM 1415 CD LYS A 183 7.745 -11.867 -4.398 1.00 38.30 C ANISOU 1415 CD LYS A 183 3989 2552 8013 -2282 -2246 1081 C ATOM 1416 CE LYS A 183 6.574 -11.499 -5.309 1.00 49.32 C ANISOU 1416 CE LYS A 183 4592 4671 9476 -1160 -3407 -583 C ATOM 1417 NZ LYS A 183 6.419 -12.448 -6.456 1.00 66.16 N ANISOU 1417 NZ LYS A 183 7189 7387 10563 3435 -5502 -2561 N ATOM 1418 N VAL A 184 8.955 -6.455 -5.670 1.00 8.30 N ANISOU 1418 N VAL A 184 1374 859 921 -89 -305 77 N ATOM 1419 CA VAL A 184 8.630 -5.064 -5.387 1.00 6.79 C ANISOU 1419 CA VAL A 184 1039 839 703 -101 -97 138 C ATOM 1420 C VAL A 184 7.653 -4.941 -4.247 1.00 6.56 C ANISOU 1420 C VAL A 184 916 906 673 -312 -201 182 C ATOM 1421 O VAL A 184 6.627 -5.583 -4.219 1.00 9.35 O ANISOU 1421 O VAL A 184 1151 1511 890 -705 -141 64 O ATOM 1422 CB VAL A 184 8.137 -4.337 -6.670 1.00 7.80 C ANISOU 1422 CB VAL A 184 1200 991 773 31 -186 102 C ATOM 1423 CG1AVAL A 184 6.949 -4.993 -7.288 0.55 7.25 C ANISOU 1423 CG1AVAL A 184 916 1019 820 53 -111 78 C ATOM 1424 CG1BVAL A 184 8.015 -2.857 -6.354 0.45 7.81 C ANISOU 1424 CG1BVAL A 184 1637 842 488 -235 -64 306 C ATOM 1425 CG2AVAL A 184 7.828 -2.888 -6.356 0.55 9.99 C ANISOU 1425 CG2AVAL A 184 1484 873 1439 89 -669 106 C ATOM 1426 CG2BVAL A 184 9.076 -4.536 -7.783 0.45 10.21 C ANISOU 1426 CG2BVAL A 184 1925 1163 793 -423 254 7 C ATOM 1427 N CYS A 185 7.976 -4.017 -3.307 1.00 5.76 N ANISOU 1427 N CYS A 185 740 723 724 -175 -166 133 N ATOM 1428 CA CYS A 185 7.136 -3.612 -2.199 1.00 5.82 C ANISOU 1428 CA CYS A 185 732 740 739 -161 -141 200 C ATOM 1429 C CYS A 185 6.377 -2.333 -2.564 1.00 5.48 C ANISOU 1429 C CYS A 185 690 859 532 -203 -30 139 C ATOM 1430 O CYS A 185 5.154 -2.296 -2.538 1.00 6.53 O ANISOU 1430 O CYS A 185 672 928 881 -197 -89 285 O ATOM 1431 CB CYS A 185 8.011 -3.434 -0.961 1.00 6.85 C ANISOU 1431 CB CYS A 185 836 1075 691 -167 -180 166 C ATOM 1432 SG CYS A 185 7.182 -2.776 0.516 1.00 7.17 S ANISOU 1432 SG CYS A 185 848 1046 831 -152 -182 96 S ATOM 1433 N PHE A 186 7.157 -1.312 -2.983 1.00 5.07 N ANISOU 1433 N PHE A 186 668 728 530 -109 -49 96 N ATOM 1434 CA PHE A 186 6.531 -0.093 -3.468 1.00 5.06 C ANISOU 1434 CA PHE A 186 577 700 645 -88 31 43 C ATOM 1435 C PHE A 186 7.531 0.615 -4.391 1.00 4.67 C ANISOU 1435 C PHE A 186 563 723 488 -135 -52 -11 C ATOM 1436 O PHE A 186 8.717 0.383 -4.340 1.00 5.01 O ANISOU 1436 O PHE A 186 491 787 628 -70 -66 -36 O ATOM 1437 CB PHE A 186 6.048 0.816 -2.330 1.00 6.13 C ANISOU 1437 CB PHE A 186 635 1014 681 -16 -5 -82 C ATOM 1438 CG PHE A 186 7.139 1.435 -1.432 1.00 6.47 C ANISOU 1438 CG PHE A 186 732 1066 660 196 -107 -165 C ATOM 1439 CD1 PHE A 186 7.938 2.493 -1.862 1.00 7.26 C ANISOU 1439 CD1 PHE A 186 593 1161 1003 -3 -40 -339 C ATOM 1440 CD2 PHE A 186 7.297 0.974 -0.132 1.00 8.35 C ANISOU 1440 CD2 PHE A 186 1256 1186 731 476 -233 -196 C ATOM 1441 CE1 PHE A 186 8.866 3.101 -1.049 1.00 8.65 C ANISOU 1441 CE1 PHE A 186 830 1307 1151 51 -191 -351 C ATOM 1442 CE2 PHE A 186 8.265 1.598 0.734 1.00 8.64 C ANISOU 1442 CE2 PHE A 186 1248 1211 824 579 -351 -342 C ATOM 1443 CZ PHE A 186 8.995 2.671 0.234 1.00 9.69 C ANISOU 1443 CZ PHE A 186 1090 1450 1141 418 -270 -353 C ATOM 1444 N GLN A 187 6.990 1.550 -5.171 1.00 4.90 N ANISOU 1444 N GLN A 187 574 613 674 -111 1 6 N ATOM 1445 CA GLN A 187 7.858 2.470 -5.924 1.00 5.27 C ANISOU 1445 CA GLN A 187 667 635 699 -100 66 60 C ATOM 1446 C GLN A 187 7.135 3.781 -6.132 1.00 5.02 C ANISOU 1446 C GLN A 187 627 670 612 -118 13 105 C ATOM 1447 O GLN A 187 5.897 3.845 -6.145 1.00 6.01 O ANISOU 1447 O GLN A 187 564 754 965 -70 -67 182 O ATOM 1448 CB GLN A 187 8.306 1.879 -7.267 1.00 5.38 C ANISOU 1448 CB GLN A 187 708 713 623 -195 -15 -34 C ATOM 1449 CG GLN A 187 7.193 1.722 -8.287 1.00 6.74 C ANISOU 1449 CG GLN A 187 587 1271 703 -176 -17 11 C ATOM 1450 CD GLN A 187 7.713 1.193 -9.606 1.00 7.26 C ANISOU 1450 CD GLN A 187 849 1076 835 -222 -69 -225 C ATOM 1451 OE1 GLN A 187 8.340 0.153 -9.637 1.00 9.59 O ANISOU 1451 OE1 GLN A 187 1085 1430 1127 88 -91 -381 O ATOM 1452 NE2 GLN A 187 7.418 1.941 -10.671 1.00 7.99 N ANISOU 1452 NE2 GLN A 187 997 1286 754 -484 17 -68 N ATOM 1453 N THR A 188 7.917 4.838 -6.354 1.00 5.46 N ANISOU 1453 N THR A 188 619 635 820 -60 61 151 N ATOM 1454 CA THR A 188 7.332 6.174 -6.586 1.00 6.16 C ANISOU 1454 CA THR A 188 723 583 1033 -54 170 187 C ATOM 1455 C THR A 188 8.362 7.050 -7.271 1.00 5.90 C ANISOU 1455 C THR A 188 694 728 820 -108 -24 126 C ATOM 1456 O THR A 188 9.571 6.848 -7.140 1.00 6.24 O ANISOU 1456 O THR A 188 724 731 917 -109 -15 125 O ATOM 1457 CB THR A 188 6.912 6.806 -5.244 1.00 7.29 C ANISOU 1457 CB THR A 188 861 834 1074 127 174 160 C ATOM 1458 OG1 THR A 188 6.231 8.071 -5.512 1.00 9.26 O ANISOU 1458 OG1 THR A 188 1143 819 1555 257 495 339 O ATOM 1459 CG2 THR A 188 8.090 7.122 -4.317 1.00 8.19 C ANISOU 1459 CG2 THR A 188 987 1042 1083 4 140 -44 C ATOM 1460 N ARG A 189 7.865 8.078 -7.965 1.00 6.91 N ANISOU 1460 N ARG A 189 747 752 1125 -121 13 285 N ATOM 1461 CA ARG A 189 8.681 9.140 -8.528 1.00 7.36 C ANISOU 1461 CA ARG A 189 1052 777 969 -210 37 228 C ATOM 1462 C ARG A 189 8.325 10.478 -7.859 1.00 7.81 C ANISOU 1462 C ARG A 189 911 802 1255 -63 -38 280 C ATOM 1463 O ARG A 189 8.761 11.544 -8.307 1.00 9.80 O ANISOU 1463 O ARG A 189 1343 781 1599 -116 -53 332 O ATOM 1464 CB ARG A 189 8.504 9.247 -10.052 1.00 8.00 C ANISOU 1464 CB ARG A 189 1035 952 1052 -126 -132 397 C ATOM 1465 CG ARG A 189 9.170 8.052 -10.739 1.00 7.89 C ANISOU 1465 CG ARG A 189 958 1137 904 -193 7 291 C ATOM 1466 CD ARG A 189 9.112 8.145 -12.253 1.00 9.29 C ANISOU 1466 CD ARG A 189 1201 1403 928 -488 -133 230 C ATOM 1467 NE ARG A 189 9.775 7.050 -12.938 1.00 9.41 N ANISOU 1467 NE ARG A 189 985 1799 792 -228 -96 190 N ATOM 1468 CZ ARG A 189 9.170 5.910 -13.267 1.00 10.31 C ANISOU 1468 CZ ARG A 189 1163 1693 1063 -170 -161 -23 C ATOM 1469 NH1 ARG A 189 7.922 5.722 -12.911 1.00 10.77 N ANISOU 1469 NH1 ARG A 189 1208 1685 1200 -296 -79 -71 N ATOM 1470 NH2 ARG A 189 9.829 4.937 -13.902 1.00 14.25 N ANISOU 1470 NH2 ARG A 189 1701 2466 1249 175 39 -456 N ATOM 1471 N LYS A 190 7.606 10.451 -6.734 1.00 8.30 N ANISOU 1471 N LYS A 190 1155 717 1281 116 59 30 N ATOM 1472 CA LYS A 190 7.193 11.703 -6.098 1.00 10.09 C ANISOU 1472 CA LYS A 190 1198 783 1851 103 7 -79 C ATOM 1473 C LYS A 190 8.246 12.267 -5.153 1.00 10.48 C ANISOU 1473 C LYS A 190 1374 706 1903 -28 -35 -68 C ATOM 1474 O LYS A 190 8.060 13.382 -4.671 1.00 12.75 O ANISOU 1474 O LYS A 190 1685 837 2323 88 -4 -312 O ATOM 1475 CB LYS A 190 5.874 11.536 -5.339 1.00 12.43 C ANISOU 1475 CB LYS A 190 1161 1219 2342 118 267 -645 C ATOM 1476 CG LYS A 190 4.698 11.254 -6.248 1.00 18.00 C ANISOU 1476 CG LYS A 190 1151 2322 3366 441 -320 -745 C ATOM 1477 CD LYS A 190 3.461 10.825 -5.486 1.00 23.61 C ANISOU 1477 CD LYS A 190 1439 4453 3078 -381 -120 -1705 C ATOM 1478 CE LYS A 190 2.543 11.854 -4.894 1.00 35.16 C ANISOU 1478 CE LYS A 190 3438 6642 3280 1260 1310 -1199 C ATOM 1479 NZ LYS A 190 1.485 11.036 -4.205 1.00 48.05 N ANISOU 1479 NZ LYS A 190 3704 8221 6330 -251 2527 -2636 N ATOM 1480 N VAL A 191 9.314 11.532 -4.879 1.00 8.09 N ANISOU 1480 N VAL A 191 914 923 1237 -130 303 -6 N ATOM 1481 CA VAL A 191 10.348 11.963 -3.952 1.00 9.61 C ANISOU 1481 CA VAL A 191 1192 1285 1176 -284 269 -186 C ATOM 1482 C VAL A 191 11.614 12.291 -4.718 1.00 9.32 C ANISOU 1482 C VAL A 191 1012 994 1536 -310 236 -442 C ATOM 1483 O VAL A 191 12.229 11.414 -5.346 1.00 11.08 O ANISOU 1483 O VAL A 191 1114 913 2182 -310 514 -446 O ATOM 1484 CB VAL A 191 10.647 10.845 -2.940 1.00 10.07 C ANISOU 1484 CB VAL A 191 1155 1403 1267 -38 144 -188 C ATOM 1485 CG1 VAL A 191 11.651 11.277 -1.890 1.00 13.74 C ANISOU 1485 CG1 VAL A 191 1986 2040 1196 -184 -54 -351 C ATOM 1486 CG2 VAL A 191 9.341 10.428 -2.244 1.00 13.78 C ANISOU 1486 CG2 VAL A 191 1802 1987 1445 -202 481 370 C ATOM 1487 N ARG A 192 11.980 13.576 -4.716 1.00 9.42 N ANISOU 1487 N ARG A 192 1141 968 1468 -249 247 -430 N ATOM 1488 CA ARG A 192 13.228 14.026 -5.357 1.00 8.69 C ANISOU 1488 CA ARG A 192 987 954 1359 -286 1 -233 C ATOM 1489 C ARG A 192 14.108 14.485 -4.232 1.00 8.08 C ANISOU 1489 C ARG A 192 1198 767 1106 -173 124 -145 C ATOM 1490 O ARG A 192 13.982 15.624 -3.743 1.00 10.70 O ANISOU 1490 O ARG A 192 1728 888 1449 -27 -280 -361 O ATOM 1491 CB ARG A 192 13.018 15.146 -6.380 1.00 10.11 C ANISOU 1491 CB ARG A 192 1552 806 1485 -287 -351 -183 C ATOM 1492 CG ARG A 192 12.021 14.678 -7.473 1.00 11.13 C ANISOU 1492 CG ARG A 192 1504 1364 1363 -327 -252 -245 C ATOM 1493 CD ARG A 192 11.945 15.624 -8.646 1.00 11.36 C ANISOU 1493 CD ARG A 192 1543 1364 1410 -95 -186 -183 C ATOM 1494 NE ARG A 192 11.346 16.924 -8.263 1.00 11.48 N ANISOU 1494 NE ARG A 192 1197 1370 1797 -186 -250 -183 N ATOM 1495 CZ ARG A 192 11.043 17.872 -9.124 1.00 11.22 C ANISOU 1495 CZ ARG A 192 1322 1380 1560 -204 -93 -146 C ATOM 1496 NH1 ARG A 192 11.346 17.674 -10.398 1.00 13.91 N ANISOU 1496 NH1 ARG A 192 1806 1903 1576 -286 -64 -419 N ATOM 1497 NH2 ARG A 192 10.505 19.020 -8.790 1.00 11.97 N ANISOU 1497 NH2 ARG A 192 1292 1442 1812 -174 -24 -231 N ATOM 1498 N PHE A 193 14.991 13.633 -3.748 1.00 7.51 N ANISOU 1498 N PHE A 193 997 788 1069 -368 212 -72 N ATOM 1499 CA PHE A 193 15.862 13.970 -2.647 1.00 7.88 C ANISOU 1499 CA PHE A 193 1197 835 963 -387 131 -12 C ATOM 1500 C PHE A 193 16.824 15.088 -3.037 1.00 7.61 C ANISOU 1500 C PHE A 193 1151 768 973 -332 161 -173 C ATOM 1501 O PHE A 193 17.440 15.039 -4.115 1.00 9.10 O ANISOU 1501 O PHE A 193 1330 989 1140 -547 365 -273 O ATOM 1502 CB PHE A 193 16.742 12.799 -2.229 1.00 8.45 C ANISOU 1502 CB PHE A 193 1069 932 1210 -361 140 -43 C ATOM 1503 CG PHE A 193 15.968 11.641 -1.580 1.00 7.85 C ANISOU 1503 CG PHE A 193 1084 942 958 -328 92 28 C ATOM 1504 CD1 PHE A 193 15.427 11.776 -0.311 1.00 8.92 C ANISOU 1504 CD1 PHE A 193 1509 981 898 -368 165 -59 C ATOM 1505 CD2 PHE A 193 15.850 10.425 -2.235 1.00 9.52 C ANISOU 1505 CD2 PHE A 193 1596 972 1047 -434 133 -87 C ATOM 1506 CE1 PHE A 193 14.775 10.702 0.288 1.00 9.74 C ANISOU 1506 CE1 PHE A 193 1552 1149 999 -394 218 -20 C ATOM 1507 CE2 PHE A 193 15.170 9.358 -1.646 1.00 11.26 C ANISOU 1507 CE2 PHE A 193 2225 982 1071 -630 122 -93 C ATOM 1508 CZ PHE A 193 14.632 9.491 -0.379 1.00 11.37 C ANISOU 1508 CZ PHE A 193 2049 1135 1137 -667 209 44 C ATOM 1509 N PRO A 194 17.021 16.091 -2.198 1.00 7.63 N ANISOU 1509 N PRO A 194 1057 798 1044 -321 224 -129 N ATOM 1510 CA PRO A 194 18.024 17.125 -2.510 1.00 8.09 C ANISOU 1510 CA PRO A 194 1141 785 1147 -351 72 -107 C ATOM 1511 C PRO A 194 19.410 16.642 -2.117 1.00 7.25 C ANISOU 1511 C PRO A 194 1232 654 870 -325 65 -48 C ATOM 1512 O PRO A 194 19.638 15.714 -1.338 1.00 8.80 O ANISOU 1512 O PRO A 194 1298 958 1089 -306 97 49 O ATOM 1513 CB PRO A 194 17.600 18.301 -1.619 1.00 10.11 C ANISOU 1513 CB PRO A 194 1353 877 1610 -242 11 -285 C ATOM 1514 CG PRO A 194 17.024 17.579 -0.404 1.00 12.00 C ANISOU 1514 CG PRO A 194 1777 1408 1375 -435 333 -542 C ATOM 1515 CD PRO A 194 16.305 16.373 -0.937 1.00 9.39 C ANISOU 1515 CD PRO A 194 1539 1069 961 -270 282 -292 C ATOM 1516 N SER A 195 20.415 17.318 -2.680 1.00 7.74 N ANISOU 1516 N SER A 195 1173 801 965 -263 55 -54 N ATOM 1517 CA SER A 195 21.790 16.954 -2.449 1.00 8.31 C ANISOU 1517 CA SER A 195 1261 1031 867 -252 140 6 C ATOM 1518 C SER A 195 22.225 17.321 -1.031 1.00 7.88 C ANISOU 1518 C SER A 195 1048 861 1084 -214 4 -70 C ATOM 1519 O SER A 195 21.653 18.188 -0.385 1.00 12.20 O ANISOU 1519 O SER A 195 1591 1435 1611 265 -468 -734 O ATOM 1520 CB SER A 195 22.692 17.639 -3.504 1.00 12.36 C ANISOU 1520 CB SER A 195 1244 2053 1400 -102 323 516 C ATOM 1521 OG SER A 195 23.945 16.998 -3.500 1.00 12.89 O ANISOU 1521 OG SER A 195 1398 1566 1936 -321 393 -108 O ATOM 1522 N GLY A 196 23.230 16.665 -0.576 1.00 9.06 N ANISOU 1522 N GLY A 196 1217 1119 1106 -54 -49 -145 N ATOM 1523 CA GLY A 196 23.802 16.927 0.739 1.00 9.90 C ANISOU 1523 CA GLY A 196 1541 1123 1096 -57 -196 -62 C ATOM 1524 C GLY A 196 24.327 15.637 1.317 1.00 7.79 C ANISOU 1524 C GLY A 196 994 1057 910 -196 -24 -224 C ATOM 1525 O GLY A 196 24.421 14.597 0.672 1.00 8.90 O ANISOU 1525 O GLY A 196 1295 1021 1064 -217 69 -207 O ATOM 1526 N SER A 197 24.721 15.727 2.590 1.00 7.97 N ANISOU 1526 N SER A 197 1095 1012 923 -149 18 -63 N ATOM 1527 CA SER A 197 25.298 14.617 3.257 1.00 8.06 C ANISOU 1527 CA SER A 197 1013 1003 1048 -346 -181 -122 C ATOM 1528 C SER A 197 24.251 13.812 4.024 1.00 7.76 C ANISOU 1528 C SER A 197 962 973 1015 -154 -90 -54 C ATOM 1529 O SER A 197 23.604 14.370 4.933 1.00 9.39 O ANISOU 1529 O SER A 197 1472 1025 1072 -336 95 -198 O ATOM 1530 CB SER A 197 26.368 15.134 4.279 1.00 9.76 C ANISOU 1530 CB SER A 197 1107 1207 1394 -300 -399 -54 C ATOM 1531 OG ASER A 197 27.095 14.029 4.772 0.64 8.45 O ANISOU 1531 OG ASER A 197 1033 1114 1062 -435 -256 37 O ATOM 1532 OG BSER A 197 25.789 16.013 5.222 0.36 15.99 O ANISOU 1532 OG BSER A 197 3193 1672 1212 -487 -115 -448 O ATOM 1533 N TYR A 198 24.101 12.546 3.630 1.00 7.30 N ANISOU 1533 N TYR A 198 887 960 924 -187 -124 -79 N ATOM 1534 CA TYR A 198 23.108 11.688 4.232 1.00 7.44 C ANISOU 1534 CA TYR A 198 1017 1018 794 -238 -84 -76 C ATOM 1535 C TYR A 198 23.695 10.650 5.148 1.00 7.33 C ANISOU 1535 C TYR A 198 882 1022 880 -215 8 -215 C ATOM 1536 O TYR A 198 24.774 10.079 4.899 1.00 8.72 O ANISOU 1536 O TYR A 198 1000 1208 1105 59 110 -26 O ATOM 1537 CB TYR A 198 22.278 10.952 3.138 1.00 7.74 C ANISOU 1537 CB TYR A 198 1067 929 943 -190 -125 -195 C ATOM 1538 CG TYR A 198 21.328 11.862 2.433 1.00 6.94 C ANISOU 1538 CG TYR A 198 1006 901 729 -242 -56 -180 C ATOM 1539 CD1 TYR A 198 21.695 12.781 1.448 1.00 7.58 C ANISOU 1539 CD1 TYR A 198 1049 1018 814 -277 31 -88 C ATOM 1540 CD2 TYR A 198 19.955 11.781 2.762 1.00 7.30 C ANISOU 1540 CD2 TYR A 198 973 986 814 -251 2 -104 C ATOM 1541 CE1 TYR A 198 20.753 13.588 0.858 1.00 7.65 C ANISOU 1541 CE1 TYR A 198 1021 1005 879 -110 146 -43 C ATOM 1542 CE2 TYR A 198 19.030 12.574 2.158 1.00 7.77 C ANISOU 1542 CE2 TYR A 198 1017 1046 889 -240 -28 25 C ATOM 1543 CZ TYR A 198 19.382 13.481 1.178 1.00 7.35 C ANISOU 1543 CZ TYR A 198 1039 782 974 -265 147 -26 C ATOM 1544 OH TYR A 198 18.466 14.285 0.587 1.00 9.66 O ANISOU 1544 OH TYR A 198 1039 1371 1259 -84 -65 238 O ATOM 1545 N ARG A 199 22.956 10.421 6.217 1.00 7.30 N ANISOU 1545 N ARG A 199 865 1046 862 -171 -85 -30 N ATOM 1546 CA ARG A 199 23.282 9.429 7.217 1.00 7.20 C ANISOU 1546 CA ARG A 199 911 1073 750 -198 -56 -144 C ATOM 1547 C ARG A 199 22.455 8.169 6.952 1.00 6.81 C ANISOU 1547 C ARG A 199 776 1065 746 -198 -14 -155 C ATOM 1548 O ARG A 199 21.275 8.253 6.663 1.00 7.57 O ANISOU 1548 O ARG A 199 791 999 1088 -77 -154 -178 O ATOM 1549 CB ARG A 199 23.014 9.963 8.634 1.00 7.61 C ANISOU 1549 CB ARG A 199 970 1074 846 -228 74 -210 C ATOM 1550 CG ARG A 199 23.565 11.340 8.901 1.00 8.44 C ANISOU 1550 CG ARG A 199 958 1324 925 -397 -79 -283 C ATOM 1551 CD ARG A 199 25.019 11.549 8.507 1.00 9.01 C ANISOU 1551 CD ARG A 199 936 1273 1216 -229 -32 -104 C ATOM 1552 NE ARG A 199 25.919 10.594 9.145 1.00 8.79 N ANISOU 1552 NE ARG A 199 1019 1330 989 -261 -73 -204 N ATOM 1553 CZ ARG A 199 27.156 10.905 9.511 1.00 9.04 C ANISOU 1553 CZ ARG A 199 944 1559 932 -340 -41 -155 C ATOM 1554 NH1 ARG A 199 27.695 12.093 9.344 1.00 9.79 N ANISOU 1554 NH1 ARG A 199 1018 1624 1077 -363 -83 -169 N ATOM 1555 NH2 ARG A 199 27.884 9.945 10.079 1.00 9.99 N ANISOU 1555 NH2 ARG A 199 1060 1541 1194 -50 -135 -442 N ATOM 1556 N ILE A 200 23.122 7.009 7.049 1.00 6.88 N ANISOU 1556 N ILE A 200 789 1047 779 -139 -149 -118 N ATOM 1557 CA ILE A 200 22.580 5.702 6.702 1.00 6.61 C ANISOU 1557 CA ILE A 200 792 1048 673 -240 -37 -44 C ATOM 1558 C ILE A 200 22.771 4.820 7.903 1.00 6.83 C ANISOU 1558 C ILE A 200 720 1141 733 -147 -4 -81 C ATOM 1559 O ILE A 200 23.892 4.718 8.451 1.00 7.04 O ANISOU 1559 O ILE A 200 679 1173 821 -81 -46 -31 O ATOM 1560 CB ILE A 200 23.338 5.140 5.466 1.00 7.72 C ANISOU 1560 CB ILE A 200 1048 1151 733 -61 -37 -105 C ATOM 1561 CG1 ILE A 200 23.043 5.993 4.233 1.00 9.96 C ANISOU 1561 CG1 ILE A 200 1658 1435 690 -182 144 27 C ATOM 1562 CG2 ILE A 200 23.018 3.668 5.265 1.00 8.39 C ANISOU 1562 CG2 ILE A 200 1110 1154 926 -173 43 -142 C ATOM 1563 CD1 ILE A 200 24.060 5.782 3.124 1.00 13.25 C ANISOU 1563 CD1 ILE A 200 2253 1640 1139 -337 748 64 C ATOM 1564 N GLY A 201 21.681 4.181 8.347 1.00 6.60 N ANISOU 1564 N GLY A 201 797 1079 630 -124 -6 -45 N ATOM 1565 CA GLY A 201 21.783 3.334 9.523 1.00 6.95 C ANISOU 1565 CA GLY A 201 672 1059 911 -85 8 63 C ATOM 1566 C GLY A 201 20.464 2.638 9.773 1.00 5.83 C ANISOU 1566 C GLY A 201 649 1030 537 -34 -10 -158 C ATOM 1567 O GLY A 201 19.504 2.758 9.019 1.00 6.50 O ANISOU 1567 O GLY A 201 628 1186 655 -49 -59 -33 O ATOM 1568 N VAL A 202 20.459 1.896 10.846 1.00 6.50 N ANISOU 1568 N VAL A 202 626 1196 647 -35 8 -83 N ATOM 1569 CA VAL A 202 19.322 1.069 11.257 1.00 6.31 C ANISOU 1569 CA VAL A 202 728 1170 501 -62 5 -83 C ATOM 1570 C VAL A 202 19.202 1.143 12.775 1.00 6.15 C ANISOU 1570 C VAL A 202 626 1196 513 35 -56 -77 C ATOM 1571 O VAL A 202 20.200 1.177 13.493 1.00 7.14 O ANISOU 1571 O VAL A 202 724 1454 534 28 -68 -91 O ATOM 1572 CB VAL A 202 19.431 -0.376 10.741 1.00 6.54 C ANISOU 1572 CB VAL A 202 664 1168 655 35 -145 -50 C ATOM 1573 CG1 VAL A 202 20.717 -1.048 11.270 1.00 7.21 C ANISOU 1573 CG1 VAL A 202 670 1406 663 107 -32 37 C ATOM 1574 CG2 VAL A 202 18.207 -1.201 11.075 1.00 6.83 C ANISOU 1574 CG2 VAL A 202 723 1193 679 -22 -59 -107 C ATOM 1575 N THR A 203 17.952 1.213 13.250 1.00 6.73 N ANISOU 1575 N THR A 203 757 1310 492 15 -28 -59 N ATOM 1576 CA THR A 203 17.694 1.342 14.676 1.00 6.69 C ANISOU 1576 CA THR A 203 794 1176 572 -81 123 -71 C ATOM 1577 C THR A 203 16.515 0.429 14.988 1.00 6.30 C ANISOU 1577 C THR A 203 838 1011 543 -21 -32 -58 C ATOM 1578 O THR A 203 15.654 0.140 14.145 1.00 6.77 O ANISOU 1578 O THR A 203 782 1353 435 -74 -59 -95 O ATOM 1579 CB THR A 203 17.375 2.795 15.068 1.00 7.14 C ANISOU 1579 CB THR A 203 834 1222 656 -92 -68 -185 C ATOM 1580 OG1 THR A 203 16.171 3.230 14.452 1.00 6.88 O ANISOU 1580 OG1 THR A 203 887 1124 603 8 57 -84 O ATOM 1581 CG2 THR A 203 18.487 3.737 14.653 1.00 7.88 C ANISOU 1581 CG2 THR A 203 928 1216 850 -184 -96 -65 C ATOM 1582 N ALA A 204 16.423 -0.004 16.249 1.00 6.93 N ANISOU 1582 N ALA A 204 855 1288 489 -75 -15 -16 N ATOM 1583 CA ALA A 204 15.274 -0.874 16.608 1.00 7.10 C ANISOU 1583 CA ALA A 204 812 1336 548 -50 98 -137 C ATOM 1584 C ALA A 204 15.030 -0.757 18.104 1.00 6.85 C ANISOU 1584 C ALA A 204 859 1253 492 -47 -41 10 C ATOM 1585 O ALA A 204 15.895 -0.402 18.895 1.00 8.00 O ANISOU 1585 O ALA A 204 912 1595 530 -99 -57 -95 O ATOM 1586 CB ALA A 204 15.471 -2.326 16.220 1.00 6.90 C ANISOU 1586 CB ALA A 204 832 1242 547 64 -43 42 C ATOM 1587 N GLN A 205 13.779 -1.119 18.452 1.00 7.37 N ANISOU 1587 N GLN A 205 793 1510 496 -77 54 -87 N ATOM 1588 CA GLN A 205 13.356 -1.240 19.831 1.00 7.19 C ANISOU 1588 CA GLN A 205 931 1311 490 -38 28 -74 C ATOM 1589 C GLN A 205 12.374 -2.418 19.892 1.00 7.18 C ANISOU 1589 C GLN A 205 836 1337 557 51 53 -22 C ATOM 1590 O GLN A 205 11.633 -2.643 18.916 1.00 7.44 O ANISOU 1590 O GLN A 205 1015 1265 546 -80 -140 32 O ATOM 1591 CB GLN A 205 12.696 0.039 20.349 1.00 9.09 C ANISOU 1591 CB GLN A 205 1293 1388 771 1 198 -203 C ATOM 1592 CG GLN A 205 11.313 0.271 19.691 1.00 11.39 C ANISOU 1592 CG GLN A 205 1468 1750 1109 429 76 -199 C ATOM 1593 CD GLN A 205 10.680 1.598 19.963 1.00 15.15 C ANISOU 1593 CD GLN A 205 2112 1867 1778 688 -133 -152 C ATOM 1594 OE1 GLN A 205 11.457 2.555 20.219 1.00 16.89 O ANISOU 1594 OE1 GLN A 205 3353 1693 1371 407 -272 -379 O ATOM 1595 NE2 GLN A 205 9.337 1.620 19.902 1.00 22.67 N ANISOU 1595 NE2 GLN A 205 2194 2915 3505 1286 -178 -1034 N ATOM 1596 N ASN A 206 12.300 -3.112 21.018 1.00 7.59 N ANISOU 1596 N ASN A 206 968 1404 513 18 48 4 N ATOM 1597 CA ASN A 206 11.278 -4.119 21.170 1.00 7.37 C ANISOU 1597 CA ASN A 206 1150 1133 517 9 -9 -51 C ATOM 1598 C ASN A 206 10.169 -3.762 22.165 1.00 7.68 C ANISOU 1598 C ASN A 206 974 1277 667 45 -28 65 C ATOM 1599 O ASN A 206 9.144 -4.455 22.185 1.00 8.37 O ANISOU 1599 O ASN A 206 1030 1450 700 -146 -34 -3 O ATOM 1600 CB ASN A 206 11.851 -5.530 21.411 1.00 8.18 C ANISOU 1600 CB ASN A 206 1251 1351 507 178 -96 -50 C ATOM 1601 CG ASN A 206 12.749 -5.621 22.603 1.00 7.45 C ANISOU 1601 CG ASN A 206 878 1275 677 -3 -52 -23 C ATOM 1602 OD1 ASN A 206 12.809 -4.707 23.441 1.00 8.08 O ANISOU 1602 OD1 ASN A 206 1162 1342 566 39 -101 -39 O ATOM 1603 ND2 ASN A 206 13.462 -6.743 22.721 1.00 8.27 N ANISOU 1603 ND2 ASN A 206 1205 1382 554 74 -11 -45 N ATOM 1604 N GLY A 207 10.361 -2.704 22.923 1.00 7.70 N ANISOU 1604 N GLY A 207 985 1272 670 40 112 -108 N ATOM 1605 CA GLY A 207 9.306 -2.229 23.873 1.00 9.68 C ANISOU 1605 CA GLY A 207 1183 1735 761 85 191 -150 C ATOM 1606 C GLY A 207 9.036 -3.250 24.936 1.00 9.33 C ANISOU 1606 C GLY A 207 1090 1746 708 -67 26 -194 C ATOM 1607 O GLY A 207 9.838 -4.128 25.223 1.00 10.37 O ANISOU 1607 O GLY A 207 1154 1970 818 -20 110 187 O ATOM 1608 N ALA A 208 7.892 -3.063 25.582 1.00 9.91 N ANISOU 1608 N ALA A 208 1199 1922 645 -45 107 -245 N ATOM 1609 CA ALA A 208 7.554 -3.791 26.803 1.00 11.09 C ANISOU 1609 CA ALA A 208 1531 2064 618 -220 182 -229 C ATOM 1610 C ALA A 208 6.295 -4.659 26.645 1.00 10.75 C ANISOU 1610 C ALA A 208 1409 2023 652 -80 138 -98 C ATOM 1611 O ALA A 208 5.903 -5.292 27.621 1.00 13.63 O ANISOU 1611 O ALA A 208 1578 2976 625 -413 259 7 O ATOM 1612 CB ALA A 208 7.331 -2.831 27.954 1.00 16.25 C ANISOU 1612 CB ALA A 208 2213 3097 863 -743 489 -788 C ATOM 1613 N VAL A 209 5.683 -4.723 25.460 1.00 10.67 N ANISOU 1613 N VAL A 209 1289 2060 704 -106 173 -189 N ATOM 1614 CA VAL A 209 4.474 -5.535 25.333 1.00 10.80 C ANISOU 1614 CA VAL A 209 1458 2041 604 -260 174 17 C ATOM 1615 C VAL A 209 4.790 -7.010 25.631 1.00 11.51 C ANISOU 1615 C VAL A 209 1471 2112 788 -132 321 105 C ATOM 1616 O VAL A 209 5.706 -7.577 25.035 1.00 11.34 O ANISOU 1616 O VAL A 209 1450 2090 768 -155 368 131 O ATOM 1617 CB VAL A 209 3.859 -5.364 23.954 1.00 12.34 C ANISOU 1617 CB VAL A 209 1791 2080 819 -514 -103 139 C ATOM 1618 CG1 VAL A 209 2.685 -6.314 23.789 1.00 14.04 C ANISOU 1618 CG1 VAL A 209 1874 2470 989 -676 -186 72 C ATOM 1619 CG2 VAL A 209 3.330 -3.927 23.810 1.00 12.52 C ANISOU 1619 CG2 VAL A 209 1528 2253 977 -347 -18 255 C ATOM 1620 N ASN A 210 3.980 -7.590 26.520 1.00 12.54 N ANISOU 1620 N ASN A 210 1602 2123 1041 -308 498 104 N ATOM 1621 CA ASN A 210 4.116 -8.965 26.932 1.00 13.21 C ANISOU 1621 CA ASN A 210 1495 1988 1534 -387 726 -6 C ATOM 1622 C ASN A 210 5.515 -9.304 27.407 1.00 13.26 C ANISOU 1622 C ASN A 210 1748 2326 962 -255 584 424 C ATOM 1623 O ASN A 210 5.858 -10.477 27.336 1.00 16.64 O ANISOU 1623 O ASN A 210 2021 2434 1869 -155 705 923 O ATOM 1624 CB ASN A 210 3.678 -9.860 25.780 1.00 16.78 C ANISOU 1624 CB ASN A 210 2575 2244 1555 -1138 315 232 C ATOM 1625 CG ASN A 210 2.209 -9.897 25.504 1.00 24.05 C ANISOU 1625 CG ASN A 210 2347 3913 2876 -1679 1012 -1365 C ATOM 1626 OD1 ASN A 210 1.441 -9.741 26.482 1.00 46.97 O ANISOU 1626 OD1 ASN A 210 4270 8610 4965 -1906 3491 -506 O ATOM 1627 ND2 ASN A 210 1.811 -10.099 24.246 1.00 26.97 N ANISOU 1627 ND2 ASN A 210 3383 2970 3896 78 -1087 -1137 N ATOM 1628 N ASN A 211 6.310 -8.381 27.893 1.00 14.09 N ANISOU 1628 N ASN A 211 1582 2943 826 -219 410 270 N ATOM 1629 CA ASN A 211 7.710 -8.659 28.266 1.00 16.04 C ANISOU 1629 CA ASN A 211 1775 3622 699 78 167 397 C ATOM 1630 C ASN A 211 8.418 -9.416 27.161 1.00 14.41 C ANISOU 1630 C ASN A 211 1545 3063 867 -16 322 619 C ATOM 1631 O ASN A 211 9.255 -10.302 27.348 1.00 16.92 O ANISOU 1631 O ASN A 211 2163 3166 1099 287 308 931 O ATOM 1632 CB ASN A 211 7.758 -9.433 29.601 1.00 19.79 C ANISOU 1632 CB ASN A 211 2021 4610 887 313 386 728 C ATOM 1633 CG ASN A 211 7.642 -8.521 30.817 1.00 30.23 C ANISOU 1633 CG ASN A 211 4113 6619 755 -1019 -47 -139 C ATOM 1634 OD1 ASN A 211 7.781 -7.287 30.815 1.00 43.08 O ANISOU 1634 OD1 ASN A 211 6257 6451 3660 -500 3468 -1669 O ATOM 1635 ND2 ASN A 211 7.330 -9.243 31.864 1.00 40.23 N ANISOU 1635 ND2 ASN A 211 4661 9869 755 -3640 204 108 N ATOM 1636 N ASN A 212 8.072 -9.069 25.888 1.00 11.50 N ANISOU 1636 N ASN A 212 1360 2202 805 -198 296 390 N ATOM 1637 CA ASN A 212 8.693 -9.760 24.764 1.00 11.32 C ANISOU 1637 CA ASN A 212 1442 2133 726 -23 232 534 C ATOM 1638 C ASN A 212 10.194 -9.473 24.724 1.00 10.59 C ANISOU 1638 C ASN A 212 1384 1891 750 18 136 368 C ATOM 1639 O ASN A 212 10.697 -8.455 25.174 1.00 11.69 O ANISOU 1639 O ASN A 212 1530 2167 746 -50 248 178 O ATOM 1640 CB ASN A 212 8.056 -9.326 23.391 1.00 10.27 C ANISOU 1640 CB ASN A 212 1505 1526 870 -89 15 341 C ATOM 1641 CG ASN A 212 8.587 -7.982 22.919 1.00 8.99 C ANISOU 1641 CG ASN A 212 1367 1387 661 44 272 170 C ATOM 1642 OD1 ASN A 212 9.561 -7.977 22.149 1.00 9.51 O ANISOU 1642 OD1 ASN A 212 1314 1499 800 164 368 160 O ATOM 1643 ND2 ASN A 212 7.991 -6.870 23.312 1.00 9.35 N ANISOU 1643 ND2 ASN A 212 1346 1503 706 105 387 56 N ATOM 1644 N ALA A 213 10.901 -10.415 24.086 1.00 11.03 N ANISOU 1644 N ALA A 213 1461 2088 642 156 133 354 N ATOM 1645 CA ALA A 213 12.320 -10.292 23.821 1.00 12.95 C ANISOU 1645 CA ALA A 213 1467 2809 646 485 213 574 C ATOM 1646 C ALA A 213 12.613 -10.397 22.328 1.00 9.24 C ANISOU 1646 C ALA A 213 1225 1607 680 269 7 248 C ATOM 1647 O ALA A 213 13.557 -11.079 21.904 1.00 11.31 O ANISOU 1647 O ALA A 213 1531 1971 796 652 120 417 O ATOM 1648 CB ALA A 213 13.144 -11.357 24.591 1.00 16.09 C ANISOU 1648 CB ALA A 213 2003 3272 837 794 150 878 C ATOM 1649 N GLU A 214 11.754 -9.790 21.498 1.00 8.49 N ANISOU 1649 N GLU A 214 1206 1404 616 141 29 179 N ATOM 1650 CA GLU A 214 12.027 -9.847 20.063 1.00 7.46 C ANISOU 1650 CA GLU A 214 938 1307 591 96 -2 207 C ATOM 1651 C GLU A 214 13.416 -9.309 19.788 1.00 6.83 C ANISOU 1651 C GLU A 214 948 1010 638 158 39 157 C ATOM 1652 O GLU A 214 13.807 -8.241 20.272 1.00 7.97 O ANISOU 1652 O GLU A 214 1169 1189 672 84 7 6 O ATOM 1653 CB GLU A 214 10.962 -8.962 19.345 1.00 6.97 C ANISOU 1653 CB GLU A 214 959 1038 652 110 -13 74 C ATOM 1654 CG GLU A 214 11.048 -9.134 17.809 1.00 7.53 C ANISOU 1654 CG GLU A 214 980 1258 624 244 19 98 C ATOM 1655 CD GLU A 214 9.823 -8.623 17.043 1.00 7.35 C ANISOU 1655 CD GLU A 214 939 1143 712 218 41 44 C ATOM 1656 OE1 GLU A 214 8.944 -7.946 17.664 1.00 7.90 O ANISOU 1656 OE1 GLU A 214 850 1280 872 221 62 -110 O ATOM 1657 OE2 GLU A 214 9.766 -8.856 15.818 1.00 7.18 O ANISOU 1657 OE2 GLU A 214 896 1083 748 270 -18 18 O ATOM 1658 N SER A 215 14.133 -10.092 18.944 1.00 7.28 N ANISOU 1658 N SER A 215 983 1268 514 278 17 82 N ATOM 1659 CA SER A 215 15.548 -9.773 18.670 1.00 7.47 C ANISOU 1659 CA SER A 215 983 1297 558 347 89 125 C ATOM 1660 C SER A 215 15.709 -9.386 17.211 1.00 6.96 C ANISOU 1660 C SER A 215 933 1208 505 285 79 68 C ATOM 1661 O SER A 215 15.645 -10.277 16.339 1.00 7.46 O ANISOU 1661 O SER A 215 941 1296 597 298 -8 105 O ATOM 1662 CB SER A 215 16.397 -11.005 19.038 1.00 8.36 C ANISOU 1662 CB SER A 215 1096 1342 741 392 -95 246 C ATOM 1663 OG SER A 215 17.769 -10.653 18.917 1.00 9.20 O ANISOU 1663 OG SER A 215 1090 1593 814 473 -75 55 O ATOM 1664 N PHE A 216 15.889 -8.102 16.967 1.00 7.28 N ANISOU 1664 N PHE A 216 989 1265 512 277 -33 184 N ATOM 1665 CA PHE A 216 16.129 -7.570 15.615 1.00 7.28 C ANISOU 1665 CA PHE A 216 850 1286 629 35 90 188 C ATOM 1666 C PHE A 216 17.632 -7.618 15.360 1.00 7.79 C ANISOU 1666 C PHE A 216 825 1562 572 158 -117 33 C ATOM 1667 O PHE A 216 18.401 -7.111 16.189 1.00 8.49 O ANISOU 1667 O PHE A 216 851 1749 625 96 -124 45 O ATOM 1668 CB PHE A 216 15.610 -6.131 15.519 1.00 7.45 C ANISOU 1668 CB PHE A 216 754 1228 848 32 -58 214 C ATOM 1669 CG PHE A 216 14.108 -6.035 15.520 1.00 7.23 C ANISOU 1669 CG PHE A 216 766 1171 810 -10 -106 167 C ATOM 1670 CD1 PHE A 216 13.392 -6.380 14.379 1.00 7.77 C ANISOU 1670 CD1 PHE A 216 824 1266 862 34 -172 262 C ATOM 1671 CD2 PHE A 216 13.442 -5.628 16.662 1.00 7.71 C ANISOU 1671 CD2 PHE A 216 899 1099 933 18 40 158 C ATOM 1672 CE1 PHE A 216 12.002 -6.270 14.356 1.00 8.05 C ANISOU 1672 CE1 PHE A 216 865 1071 1124 -53 -261 182 C ATOM 1673 CE2 PHE A 216 12.049 -5.483 16.606 1.00 8.64 C ANISOU 1673 CE2 PHE A 216 938 1151 1193 118 91 92 C ATOM 1674 CZ PHE A 216 11.342 -5.814 15.471 1.00 8.46 C ANISOU 1674 CZ PHE A 216 908 1055 1252 109 -51 268 C ATOM 1675 N GLU A 217 18.025 -8.232 14.257 1.00 8.05 N ANISOU 1675 N GLU A 217 732 1717 609 180 -56 7 N ATOM 1676 CA GLU A 217 19.427 -8.607 14.015 1.00 7.89 C ANISOU 1676 CA GLU A 217 707 1612 677 73 -85 117 C ATOM 1677 C GLU A 217 19.825 -8.265 12.578 1.00 7.36 C ANISOU 1677 C GLU A 217 707 1464 625 124 -83 36 C ATOM 1678 O GLU A 217 19.016 -8.460 11.650 1.00 8.97 O ANISOU 1678 O GLU A 217 759 2030 619 44 -71 7 O ATOM 1679 CB GLU A 217 19.628 -10.084 14.243 1.00 8.82 C ANISOU 1679 CB GLU A 217 896 1653 801 102 -79 216 C ATOM 1680 CG GLU A 217 19.112 -10.507 15.620 1.00 9.11 C ANISOU 1680 CG GLU A 217 1208 1480 775 -41 51 25 C ATOM 1681 CD GLU A 217 19.388 -11.903 16.038 1.00 10.03 C ANISOU 1681 CD GLU A 217 1147 1714 952 237 -55 216 C ATOM 1682 OE1 GLU A 217 19.850 -12.712 15.169 1.00 9.66 O ANISOU 1682 OE1 GLU A 217 1145 1404 1119 295 -49 258 O ATOM 1683 OE2 GLU A 217 19.155 -12.183 17.243 1.00 12.18 O ANISOU 1683 OE2 GLU A 217 1771 1930 927 504 -68 300 O ATOM 1684 N ILE A 218 21.045 -7.772 12.423 1.00 7.11 N ANISOU 1684 N ILE A 218 704 1321 677 184 -92 109 N ATOM 1685 CA ILE A 218 21.625 -7.378 11.132 1.00 6.89 C ANISOU 1685 CA ILE A 218 764 1333 522 241 -79 50 C ATOM 1686 C ILE A 218 22.710 -8.344 10.726 1.00 7.57 C ANISOU 1686 C ILE A 218 705 1576 596 243 -12 167 C ATOM 1687 O ILE A 218 23.642 -8.635 11.506 1.00 8.88 O ANISOU 1687 O ILE A 218 849 1682 843 371 -209 27 O ATOM 1688 CB ILE A 218 22.168 -5.959 11.181 1.00 7.67 C ANISOU 1688 CB ILE A 218 641 1432 841 162 -26 222 C ATOM 1689 CG1 ILE A 218 21.175 -4.954 11.749 1.00 8.78 C ANISOU 1689 CG1 ILE A 218 1015 1400 923 289 -160 -85 C ATOM 1690 CG2 ILE A 218 22.744 -5.548 9.831 1.00 9.16 C ANISOU 1690 CG2 ILE A 218 875 1629 976 186 79 339 C ATOM 1691 CD1 ILE A 218 19.920 -4.823 10.855 1.00 9.38 C ANISOU 1691 CD1 ILE A 218 678 1240 1645 162 -195 -89 C ATOM 1692 N PHE A 219 22.620 -8.924 9.528 1.00 7.32 N ANISOU 1692 N PHE A 219 772 1341 670 309 -66 67 N ATOM 1693 CA PHE A 219 23.665 -9.808 9.006 1.00 7.36 C ANISOU 1693 CA PHE A 219 814 1256 725 295 -40 100 C ATOM 1694 C PHE A 219 24.652 -9.078 8.077 1.00 8.04 C ANISOU 1694 C PHE A 219 755 1448 851 248 -100 220 C ATOM 1695 O PHE A 219 25.828 -9.477 7.996 1.00 9.03 O ANISOU 1695 O PHE A 219 800 1652 981 362 -62 117 O ATOM 1696 CB PHE A 219 23.024 -10.937 8.231 1.00 8.50 C ANISOU 1696 CB PHE A 219 1128 1197 904 303 218 56 C ATOM 1697 CG PHE A 219 22.379 -12.055 8.974 1.00 8.35 C ANISOU 1697 CG PHE A 219 826 1345 1001 241 -110 172 C ATOM 1698 CD1 PHE A 219 22.116 -13.276 8.332 1.00 9.52 C ANISOU 1698 CD1 PHE A 219 1004 1299 1314 221 -97 127 C ATOM 1699 CD2 PHE A 219 22.039 -11.969 10.324 1.00 10.61 C ANISOU 1699 CD2 PHE A 219 1452 1624 954 -35 -66 275 C ATOM 1700 CE1 PHE A 219 21.544 -14.354 8.972 1.00 10.58 C ANISOU 1700 CE1 PHE A 219 1099 1362 1559 299 69 126 C ATOM 1701 CE2 PHE A 219 21.471 -13.064 10.979 1.00 10.82 C ANISOU 1701 CE2 PHE A 219 1360 1542 1210 47 -62 294 C ATOM 1702 CZ PHE A 219 21.249 -14.239 10.335 1.00 11.00 C ANISOU 1702 CZ PHE A 219 1311 1395 1472 299 2 288 C ATOM 1703 N LYS A 220 24.172 -8.115 7.284 1.00 7.67 N ANISOU 1703 N LYS A 220 908 1298 710 252 -9 81 N ATOM 1704 CA LYS A 220 24.953 -7.582 6.159 1.00 7.68 C ANISOU 1704 CA LYS A 220 830 1436 651 286 49 108 C ATOM 1705 C LYS A 220 24.261 -6.342 5.675 1.00 7.03 C ANISOU 1705 C LYS A 220 667 1384 620 209 -42 90 C ATOM 1706 O LYS A 220 22.992 -6.267 5.737 1.00 7.59 O ANISOU 1706 O LYS A 220 721 1493 668 237 -1 44 O ATOM 1707 CB LYS A 220 24.975 -8.636 5.033 1.00 9.57 C ANISOU 1707 CB LYS A 220 1277 1324 1036 262 311 7 C ATOM 1708 CG LYS A 220 25.811 -8.307 3.807 1.00 10.01 C ANISOU 1708 CG LYS A 220 1235 1800 768 449 207 28 C ATOM 1709 CD LYS A 220 25.904 -9.455 2.853 1.00 12.76 C ANISOU 1709 CD LYS A 220 1628 2262 960 655 -51 -297 C ATOM 1710 CE LYS A 220 24.641 -9.841 2.143 1.00 19.73 C ANISOU 1710 CE LYS A 220 1870 3268 2357 933 -501 -1484 C ATOM 1711 NZ LYS A 220 24.976 -10.788 1.047 1.00 27.03 N ANISOU 1711 NZ LYS A 220 2293 4595 3381 1020 -578 -2662 N ATOM 1712 N MET A 221 25.013 -5.414 5.111 1.00 7.32 N ANISOU 1712 N MET A 221 760 1368 652 289 14 73 N ATOM 1713 CA MET A 221 24.425 -4.312 4.359 1.00 7.24 C ANISOU 1713 CA MET A 221 661 1349 741 206 -2 59 C ATOM 1714 C MET A 221 25.380 -4.031 3.208 1.00 7.61 C ANISOU 1714 C MET A 221 610 1501 779 236 -28 69 C ATOM 1715 O MET A 221 26.585 -3.970 3.398 1.00 7.92 O ANISOU 1715 O MET A 221 597 1513 902 87 17 41 O ATOM 1716 CB MET A 221 24.228 -3.069 5.250 1.00 7.92 C ANISOU 1716 CB MET A 221 731 1271 1007 78 5 -91 C ATOM 1717 CG AMET A 221 23.574 -1.843 4.599 0.54 7.71 C ANISOU 1717 CG AMET A 221 641 1346 944 87 166 15 C ATOM 1718 CG BMET A 221 23.479 -1.994 4.411 0.46 10.88 C ANISOU 1718 CG BMET A 221 964 1485 1685 385 315 294 C ATOM 1719 SD AMET A 221 24.971 -0.860 3.973 0.54 6.59 S ANISOU 1719 SD AMET A 221 558 1375 573 13 -29 -73 S ATOM 1720 SD BMET A 221 24.293 -1.015 3.106 0.46 11.02 S ANISOU 1720 SD BMET A 221 1616 1539 1033 147 269 -83 S ATOM 1721 CE AMET A 221 24.084 0.469 3.148 0.54 9.74 C ANISOU 1721 CE AMET A 221 990 1085 1627 515 439 49 C ATOM 1722 CE BMET A 221 24.260 0.568 3.976 0.46 10.88 C ANISOU 1722 CE BMET A 221 1472 1572 1090 -82 100 -207 C ATOM 1723 N GLN A 222 24.833 -3.862 2.013 1.00 7.41 N ANISOU 1723 N GLN A 222 586 1415 813 75 32 211 N ATOM 1724 CA GLN A 222 25.645 -3.541 0.877 1.00 8.65 C ANISOU 1724 CA GLN A 222 682 1706 899 86 134 262 C ATOM 1725 C GLN A 222 25.121 -2.273 0.234 1.00 8.69 C ANISOU 1725 C GLN A 222 647 1790 864 -8 -4 387 C ATOM 1726 O GLN A 222 23.912 -2.107 0.014 1.00 11.22 O ANISOU 1726 O GLN A 222 587 2126 1549 5 -82 903 O ATOM 1727 CB GLN A 222 25.689 -4.681 -0.137 1.00 10.91 C ANISOU 1727 CB GLN A 222 1343 1944 860 400 393 233 C ATOM 1728 CG GLN A 222 26.505 -5.790 0.554 1.00 12.77 C ANISOU 1728 CG GLN A 222 1814 1975 1064 600 114 182 C ATOM 1729 CD GLN A 222 26.849 -6.882 -0.438 1.00 15.34 C ANISOU 1729 CD GLN A 222 1459 2037 2333 343 355 -413 C ATOM 1730 OE1 GLN A 222 28.039 -7.150 -0.679 1.00 18.65 O ANISOU 1730 OE1 GLN A 222 1541 3844 1700 721 301 -525 O ATOM 1731 NE2 GLN A 222 25.819 -7.501 -1.009 1.00 14.20 N ANISOU 1731 NE2 GLN A 222 1649 2437 1308 350 160 -75 N ATOM 1732 N PHE A 223 26.033 -1.368 -0.083 1.00 7.89 N ANISOU 1732 N PHE A 223 574 1604 821 42 -7 110 N ATOM 1733 CA PHE A 223 25.743 -0.123 -0.764 1.00 7.52 C ANISOU 1733 CA PHE A 223 597 1485 776 -26 -14 34 C ATOM 1734 C PHE A 223 26.373 -0.173 -2.138 1.00 7.29 C ANISOU 1734 C PHE A 223 720 1278 773 97 -3 -36 C ATOM 1735 O PHE A 223 27.563 -0.536 -2.228 1.00 8.24 O ANISOU 1735 O PHE A 223 688 1617 827 89 90 115 O ATOM 1736 CB PHE A 223 26.324 1.040 0.080 1.00 8.94 C ANISOU 1736 CB PHE A 223 859 1603 936 116 -102 -238 C ATOM 1737 CG PHE A 223 25.806 2.388 -0.380 1.00 10.45 C ANISOU 1737 CG PHE A 223 1151 1636 1186 143 -457 -359 C ATOM 1738 CD1 PHE A 223 24.728 2.968 0.273 1.00 14.75 C ANISOU 1738 CD1 PHE A 223 2149 2235 1222 1063 -458 -573 C ATOM 1739 CD2 PHE A 223 26.349 3.063 -1.440 1.00 13.15 C ANISOU 1739 CD2 PHE A 223 1217 1465 2314 -325 -488 300 C ATOM 1740 CE1 PHE A 223 24.216 4.195 -0.116 1.00 16.84 C ANISOU 1740 CE1 PHE A 223 2702 2322 1375 1205 -833 -698 C ATOM 1741 CE2 PHE A 223 25.861 4.325 -1.824 1.00 15.30 C ANISOU 1741 CE2 PHE A 223 1941 1262 2610 -187 -778 -58 C ATOM 1742 CZ PHE A 223 24.781 4.878 -1.155 1.00 15.84 C ANISOU 1742 CZ PHE A 223 2592 1375 2054 87 -1077 -823 C ATOM 1743 N PHE A 224 25.630 0.189 -3.160 1.00 7.86 N ANISOU 1743 N PHE A 224 711 1565 709 1 2 -22 N ATOM 1744 CA PHE A 224 26.151 0.254 -4.537 1.00 7.72 C ANISOU 1744 CA PHE A 224 732 1516 685 78 37 2 C ATOM 1745 C PHE A 224 25.917 1.621 -5.111 1.00 8.63 C ANISOU 1745 C PHE A 224 692 1606 983 -14 50 180 C ATOM 1746 O PHE A 224 24.885 2.265 -4.891 1.00 8.79 O ANISOU 1746 O PHE A 224 743 1610 988 93 40 111 O ATOM 1747 CB PHE A 224 25.474 -0.788 -5.457 1.00 8.44 C ANISOU 1747 CB PHE A 224 976 1502 729 -26 -32 90 C ATOM 1748 CG PHE A 224 25.524 -2.209 -4.945 1.00 8.81 C ANISOU 1748 CG PHE A 224 1012 1546 789 -30 -177 104 C ATOM 1749 CD1 PHE A 224 26.447 -3.106 -5.456 1.00 10.02 C ANISOU 1749 CD1 PHE A 224 1100 1761 946 184 -145 67 C ATOM 1750 CD2 PHE A 224 24.649 -2.667 -3.972 1.00 9.62 C ANISOU 1750 CD2 PHE A 224 944 1768 944 -89 -100 339 C ATOM 1751 CE1 PHE A 224 26.540 -4.429 -5.011 1.00 10.67 C ANISOU 1751 CE1 PHE A 224 1412 1551 1090 15 -202 -150 C ATOM 1752 CE2 PHE A 224 24.745 -3.970 -3.514 1.00 9.82 C ANISOU 1752 CE2 PHE A 224 1148 1594 989 -214 -196 89 C ATOM 1753 CZ PHE A 224 25.670 -4.900 -4.001 1.00 10.96 C ANISOU 1753 CZ PHE A 224 1268 1668 1228 -78 -250 46 C ATOM 1754 N ASN A 225 26.857 2.043 -5.951 1.00 9.81 N ANISOU 1754 N ASN A 225 903 1737 1088 23 172 295 N ATOM 1755 CA ASN A 225 26.512 3.078 -6.906 1.00 10.18 C ANISOU 1755 CA ASN A 225 1023 1648 1197 -63 202 267 C ATOM 1756 C ASN A 225 25.595 2.490 -7.978 1.00 10.81 C ANISOU 1756 C ASN A 225 1680 1760 668 194 181 -47 C ATOM 1757 O ASN A 225 25.744 1.327 -8.418 1.00 13.47 O ANISOU 1757 O ASN A 225 2022 1836 1262 341 -106 -146 O ATOM 1758 CB ASN A 225 27.837 3.639 -7.387 1.00 14.69 C ANISOU 1758 CB ASN A 225 1488 1991 2101 -212 685 451 C ATOM 1759 CG ASN A 225 28.536 4.364 -6.249 1.00 15.29 C ANISOU 1759 CG ASN A 225 1074 1721 3016 -408 265 427 C ATOM 1760 OD1 ASN A 225 28.001 5.235 -5.536 1.00 20.44 O ANISOU 1760 OD1 ASN A 225 1684 2646 3436 -533 270 -545 O ATOM 1761 ND2 ASN A 225 29.793 4.062 -5.926 1.00 23.80 N ANISOU 1761 ND2 ASN A 225 1327 2946 4768 -198 -214 837 N ATOM 1762 N GLY A 226 24.657 3.195 -8.485 1.00 9.97 N ANISOU 1762 N GLY A 226 1107 1442 1240 -216 178 -146 N ATOM 1763 CA GLY A 226 23.730 2.737 -9.522 1.00 10.06 C ANISOU 1763 CA GLY A 226 1383 1467 971 -269 223 -238 C ATOM 1764 C GLY A 226 22.654 1.870 -8.911 1.00 9.27 C ANISOU 1764 C GLY A 226 1138 1490 894 -207 251 -238 C ATOM 1765 O GLY A 226 22.535 1.748 -7.670 1.00 9.70 O ANISOU 1765 O GLY A 226 1370 1475 841 -353 209 -192 O ATOM 1766 N VAL A 227 21.865 1.282 -9.811 1.00 9.35 N ANISOU 1766 N VAL A 227 1366 1403 783 -211 114 -131 N ATOM 1767 CA VAL A 227 20.737 0.383 -9.461 1.00 8.76 C ANISOU 1767 CA VAL A 227 1197 1272 860 -144 70 -80 C ATOM 1768 C VAL A 227 20.757 -0.896 -10.304 1.00 9.20 C ANISOU 1768 C VAL A 227 1148 1453 895 -94 115 -248 C ATOM 1769 O VAL A 227 19.943 -1.790 -9.995 1.00 9.95 O ANISOU 1769 O VAL A 227 1460 1276 1043 -240 4 -176 O ATOM 1770 CB VAL A 227 19.378 1.106 -9.620 1.00 10.21 C ANISOU 1770 CB VAL A 227 1381 1397 1103 111 55 -238 C ATOM 1771 CG1 VAL A 227 19.398 2.414 -8.808 1.00 11.46 C ANISOU 1771 CG1 VAL A 227 1510 1225 1620 -193 532 -242 C ATOM 1772 CG2 VAL A 227 19.014 1.335 -11.073 1.00 13.09 C ANISOU 1772 CG2 VAL A 227 1784 1915 1276 488 -112 94 C ATOM 1773 OXT VAL A 227 21.568 -0.928 -11.232 1.00 10.29 O ANISOU 1773 OXT VAL A 227 1326 1647 937 -96 44 -288 O TER 1774 VAL A 227 HETATM 1775 O HOH A 228 12.968 -12.685 10.396 1.00 6.82 O ANISOU 1775 O HOH A 228 961 858 773 311 -39 -21 O HETATM 1776 O HOH A 229 5.542 -0.879 9.090 1.00 5.89 O ANISOU 1776 O HOH A 229 661 881 695 5 4 -1 O HETATM 1777 O HOH A 230 -1.636 -4.617 14.328 1.00 21.82 O ANISOU 1777 O HOH A 230 2053 3270 2969 297 9 1691 O HETATM 1778 O HOH A 231 12.525 -1.017 23.677 1.00 8.67 O ANISOU 1778 O HOH A 231 1079 1575 643 -3 -13 -126 O HETATM 1779 O HOH A 232 5.743 -4.102 15.870 1.00 6.58 O ANISOU 1779 O HOH A 232 829 1113 557 51 49 20 O HETATM 1780 O HOH A 233 2.354 -2.173 11.166 1.00 6.44 O ANISOU 1780 O HOH A 233 766 874 808 138 104 23 O HETATM 1781 O HOH A 234 14.629 -1.487 -5.216 1.00 6.59 O ANISOU 1781 O HOH A 234 865 903 738 -55 19 12 O HETATM 1782 O HOH A 235 8.147 9.061 10.300 1.00 8.72 O ANISOU 1782 O HOH A 235 1146 1115 1052 43 208 -284 O HETATM 1783 O HOH A 236 7.422 -7.061 -1.412 1.00 12.46 O ANISOU 1783 O HOH A 236 1209 2362 1165 75 -127 357 O HETATM 1784 O HOH A 237 -2.297 1.800 7.255 1.00 9.61 O ANISOU 1784 O HOH A 237 818 942 1892 369 -722 -377 O HETATM 1785 O HOH A 238 10.675 9.206 -5.797 1.00 7.79 O ANISOU 1785 O HOH A 238 1053 855 1051 -119 83 -5 O HETATM 1786 O HOH A 239 7.833 -6.080 15.861 1.00 8.72 O ANISOU 1786 O HOH A 239 972 1462 880 285 -76 -143 O HETATM 1787 O HOH A 240 5.554 -10.996 10.935 1.00 8.63 O ANISOU 1787 O HOH A 240 1097 1290 890 454 28 166 O HETATM 1788 O HOH A 241 26.156 7.709 5.964 1.00 9.39 O ANISOU 1788 O HOH A 241 1012 1302 1256 -8 45 -154 O HETATM 1789 O HOH A 242 20.059 6.194 16.579 1.00 8.84 O ANISOU 1789 O HOH A 242 906 1624 829 -121 36 -332 O HETATM 1790 O HOH A 243 22.674 -6.984 2.397 1.00 9.06 O ANISOU 1790 O HOH A 243 995 1571 876 248 104 193 O HETATM 1791 O HOH A 244 6.452 -3.786 22.749 1.00 9.72 O ANISOU 1791 O HOH A 244 1352 1635 707 -131 -34 -88 O HETATM 1792 O HOH A 245 10.772 -12.645 16.167 1.00 8.56 O ANISOU 1792 O HOH A 245 1210 1096 947 318 112 98 O HETATM 1793 O HOH A 246 5.542 9.558 9.656 1.00 8.79 O ANISOU 1793 O HOH A 246 996 1015 1328 46 155 -353 O HETATM 1794 O HOH A 247 14.731 2.693 -8.350 1.00 8.60 O ANISOU 1794 O HOH A 247 1241 1131 895 14 85 -60 O HETATM 1795 O HOH A 248 4.027 -10.347 13.151 1.00 9.87 O ANISOU 1795 O HOH A 248 1294 1470 988 356 117 70 O HETATM 1796 O HOH A 249 19.572 8.756 16.005 1.00 9.65 O ANISOU 1796 O HOH A 249 1218 1418 1032 -72 119 -406 O HETATM 1797 O HOH A 250 8.955 -6.128 19.633 1.00 8.86 O ANISOU 1797 O HOH A 250 738 1675 954 178 -33 -214 O HETATM 1798 O HOH A 251 15.052 -7.389 -2.160 1.00 8.86 O ANISOU 1798 O HOH A 251 1273 1149 944 -49 14 -42 O HETATM 1799 O HOH A 252 3.169 -7.621 0.088 1.00 8.49 O ANISOU 1799 O HOH A 252 1134 1160 931 100 -28 -24 O HETATM 1800 O HOH A 253 20.660 -10.815 1.506 1.00 11.36 O ANISOU 1800 O HOH A 253 1489 1415 1411 317 131 110 O HETATM 1801 O HOH A 254 3.496 10.384 11.312 1.00 10.27 O ANISOU 1801 O HOH A 254 1039 1448 1415 -35 248 -394 O HETATM 1802 O HOH A 255 19.977 -17.678 8.766 1.00 9.75 O ANISOU 1802 O HOH A 255 1404 1084 1215 559 151 82 O HETATM 1803 O HOH A 256 0.000 0.360 0.000 0.50 21.71 O ANISOU 1803 O HOH A 256 1199 4963 2087 0 318 0 O HETATM 1804 O HOH A 257 17.229 13.675 -6.483 1.00 9.01 O ANISOU 1804 O HOH A 257 1264 829 1331 -488 384 -290 O HETATM 1805 O HOH A 258 20.061 20.325 -0.303 1.00 13.48 O ANISOU 1805 O HOH A 258 1468 1193 2461 -268 -259 -281 O HETATM 1806 O HOH A 259 11.092 -12.275 3.937 1.00 11.03 O ANISOU 1806 O HOH A 259 1249 1669 1274 40 229 44 O HETATM 1807 O HOH A 260 27.064 14.124 7.463 1.00 13.69 O ANISOU 1807 O HOH A 260 1732 2215 1256 -932 -105 52 O HETATM 1808 O HOH A 261 23.104 12.591 -11.049 1.00 13.62 O ANISOU 1808 O HOH A 261 2826 727 1623 -341 -98 -176 O HETATM 1809 O HOH A 262 38.408 2.607 1.270 1.00 13.44 O ANISOU 1809 O HOH A 262 1191 2435 1481 326 122 58 O HETATM 1810 O HOH A 263 7.018 -7.809 1.372 1.00 10.31 O ANISOU 1810 O HOH A 263 1067 1686 1162 336 181 167 O HETATM 1811 O HOH A 264 3.890 3.902 -8.126 1.00 10.00 O ANISOU 1811 O HOH A 264 960 1803 1038 135 -130 -28 O HETATM 1812 O HOH A 265 -1.871 6.064 12.258 1.00 12.26 O ANISOU 1812 O HOH A 265 1287 1295 2078 -7 197 -372 O HETATM 1813 O HOH A 266 25.826 7.184 -5.763 1.00 13.53 O ANISOU 1813 O HOH A 266 1165 1822 2153 -151 -411 -196 O HETATM 1814 O HOH A 267 17.176 -1.990 -9.845 1.00 16.50 O ANISOU 1814 O HOH A 267 1895 3252 1124 -1271 -522 777 O HETATM 1815 O HOH A 268 5.564 4.237 -10.477 1.00 11.95 O ANISOU 1815 O HOH A 268 1994 1401 1145 126 -6 46 O HETATM 1816 O HOH A 269 9.743 -6.401 26.729 1.00 12.10 O ANISOU 1816 O HOH A 269 1598 2188 812 -130 200 130 O HETATM 1817 O HOH A 270 26.174 9.830 -5.101 1.00 14.33 O ANISOU 1817 O HOH A 270 1887 1626 1932 -3 -252 5 O HETATM 1818 O HOH A 271 14.859 6.337 22.778 1.00 10.38 O ANISOU 1818 O HOH A 271 1615 1485 846 60 134 -145 O HETATM 1819 O HOH A 272 17.498 5.470 23.208 1.00 10.77 O ANISOU 1819 O HOH A 272 1572 1816 703 -122 80 -200 O HETATM 1820 O HOH A 273 25.648 7.779 8.724 1.00 10.94 O ANISOU 1820 O HOH A 273 930 1485 1741 -73 -389 -311 O HETATM 1821 O HOH A 274 0.217 -7.659 13.759 1.00 15.70 O ANISOU 1821 O HOH A 274 1541 1676 2749 -79 360 -130 O HETATM 1822 O HOH A 275 17.754 14.098 9.482 1.00 12.01 O ANISOU 1822 O HOH A 275 1337 1882 1344 -245 -142 -214 O HETATM 1823 O HOH A 276 13.053 -12.770 7.688 1.00 11.34 O ANISOU 1823 O HOH A 276 1925 1397 986 996 428 327 O HETATM 1824 O HOH A 277 30.342 -6.269 1.246 1.00 15.28 O ANISOU 1824 O HOH A 277 1553 3023 1231 -153 34 677 O HETATM 1825 O HOH A 278 18.526 -0.814 25.669 1.00 12.82 O ANISOU 1825 O HOH A 278 1212 2832 827 -504 -53 -238 O HETATM 1826 O HOH A 279 23.160 -7.580 -0.283 1.00 12.21 O ANISOU 1826 O HOH A 279 1700 1902 1038 543 31 233 O HETATM 1827 O HOH A 280 12.713 -16.293 22.501 1.00 16.44 O ANISOU 1827 O HOH A 280 1896 2789 1563 363 195 824 O HETATM 1828 O HOH A 281 34.286 -0.183 -3.121 1.00 25.99 O ANISOU 1828 O HOH A 281 1939 6038 1899 -419 896 -932 O HETATM 1829 O HOH A 282 12.484 5.360 20.543 1.00 13.54 O ANISOU 1829 O HOH A 282 1740 2393 1013 76 230 -331 O HETATM 1830 O HOH A 283 26.147 19.041 -7.228 1.00 13.01 O ANISOU 1830 O HOH A 283 2054 1520 1370 -650 77 74 O HETATM 1831 O HOH A 284 -5.971 6.932 11.160 1.00 13.61 O ANISOU 1831 O HOH A 284 1153 1713 2306 598 -47 -46 O HETATM 1832 O HOH A 285 16.629 12.860 -12.450 1.00 14.14 O ANISOU 1832 O HOH A 285 1815 2016 1543 -777 94 -173 O HETATM 1833 O HOH A 286 8.517 18.330 9.406 1.00 20.19 O ANISOU 1833 O HOH A 286 3299 2368 2002 512 207 -779 O HETATM 1834 O HOH A 287 2.245 1.568 -1.427 1.00 18.13 O ANISOU 1834 O HOH A 287 1659 2257 2972 -592 -1439 1513 O HETATM 1835 O HOH A 288 23.052 9.339 -11.192 1.00 14.99 O ANISOU 1835 O HOH A 288 2016 2662 1017 -1044 59 112 O HETATM 1836 O HOH A 289 1.966 -3.158 -1.694 1.00 14.93 O ANISOU 1836 O HOH A 289 1190 3342 1142 448 -223 24 O HETATM 1837 O HOH A 290 1.400 -8.953 6.743 1.00 9.46 O ANISOU 1837 O HOH A 290 1268 1206 1122 -101 -50 44 O HETATM 1838 O HOH A 291 21.536 15.344 14.935 1.00 14.72 O ANISOU 1838 O HOH A 291 2484 1649 1459 -209 -346 -448 O HETATM 1839 O HOH A 292 22.375 -12.956 1.829 1.00 19.65 O ANISOU 1839 O HOH A 292 2555 1711 3199 673 580 513 O HETATM 1840 O HOH A 293 -1.292 -8.641 7.484 1.00 13.30 O ANISOU 1840 O HOH A 293 1560 1746 1746 87 -132 48 O HETATM 1841 O HOH A 294 8.522 -11.384 4.125 1.00 13.44 O ANISOU 1841 O HOH A 294 1748 2220 1140 527 48 -139 O HETATM 1842 O HOH A 295 21.845 6.975 23.216 1.00 19.44 O ANISOU 1842 O HOH A 295 1763 3719 1906 -78 -131 -1167 O HETATM 1843 O HOH A 296 23.343 17.053 5.542 1.00 15.73 O ANISOU 1843 O HOH A 296 2286 1418 2271 -130 277 107 O HETATM 1844 O HOH A 297 10.273 -13.166 23.424 1.00 15.85 O ANISOU 1844 O HOH A 297 2487 2118 1416 515 276 641 O HETATM 1845 O HOH A 298 3.290 13.630 11.176 1.00 20.44 O ANISOU 1845 O HOH A 298 2280 3875 1612 1041 -248 -881 O HETATM 1846 O HOH A 299 29.602 -9.133 2.234 1.00 17.47 O ANISOU 1846 O HOH A 299 2807 2089 1742 -31 -130 199 O HETATM 1847 O HOH A 300 5.321 10.130 5.135 1.00 13.95 O ANISOU 1847 O HOH A 300 768 1243 3289 -92 42 382 O HETATM 1848 O HOH A 301 33.012 -2.536 3.622 1.00 15.99 O ANISOU 1848 O HOH A 301 1929 2136 2009 714 -69 233 O HETATM 1849 O HOH A 302 3.681 -4.737 -3.234 1.00 10.41 O ANISOU 1849 O HOH A 302 1125 1393 1439 -188 -179 162 O HETATM 1850 O HOH A 303 18.565 13.971 12.204 1.00 16.22 O ANISOU 1850 O HOH A 303 1582 2948 1634 -318 -180 -108 O HETATM 1851 O HOH A 304 31.598 5.498 7.668 1.00 17.04 O ANISOU 1851 O HOH A 304 2885 1984 1606 -49 1006 -145 O HETATM 1852 O HOH A 305 15.971 14.670 2.219 1.00 14.27 O ANISOU 1852 O HOH A 305 1844 1933 1643 -274 72 62 O HETATM 1853 O HOH A 306 4.551 -4.693 30.010 1.00 16.94 O ANISOU 1853 O HOH A 306 1653 3509 1274 -51 318 374 O HETATM 1854 O HOH A 307 30.110 10.240 -0.266 1.00 15.97 O ANISOU 1854 O HOH A 307 1198 2354 2516 -142 532 -23 O HETATM 1855 O HOH A 308 4.758 -7.028 -2.034 1.00 11.97 O ANISOU 1855 O HOH A 308 1208 2114 1225 -219 -55 137 O HETATM 1856 O HOH A 309 10.309 12.514 -10.381 1.00 13.84 O ANISOU 1856 O HOH A 309 1693 1827 1737 -670 275 248 O HETATM 1857 O HOH A 310 7.380 -10.356 1.862 1.00 17.49 O ANISOU 1857 O HOH A 310 2497 2615 1532 705 -48 80 O HETATM 1858 O HOH A 311 19.215 2.736 5.286 1.00 22.30 O ANISOU 1858 O HOH A 311 1750 1153 5572 -197 1419 -621 O HETATM 1859 O HOH A 312 23.695 -2.901 -13.892 1.00 15.56 O ANISOU 1859 O HOH A 312 1823 2830 1258 320 8 32 O HETATM 1860 O HOH A 313 3.050 -0.268 -3.014 1.00 11.75 O ANISOU 1860 O HOH A 313 1127 1322 2014 -163 -257 -71 O HETATM 1861 O HOH A 314 15.124 1.926 -12.506 1.00 20.53 O ANISOU 1861 O HOH A 314 1891 1660 4248 -480 432 -772 O HETATM 1862 O HOH A 315 8.300 -14.513 9.201 1.00 15.25 O ANISOU 1862 O HOH A 315 2456 2028 1312 440 -204 -23 O HETATM 1863 O HOH A 316 5.954 -0.952 25.179 1.00 18.28 O ANISOU 1863 O HOH A 316 2064 2629 2254 1023 -364 -1204 O HETATM 1864 O HOH A 317 26.264 6.240 17.812 1.00 24.96 O ANISOU 1864 O HOH A 317 1762 3966 3757 -545 291 -2349 O HETATM 1865 O HOH A 318 9.259 5.110 18.801 1.00 16.19 O ANISOU 1865 O HOH A 318 1749 2889 1513 518 702 -76 O HETATM 1866 O HOH A 319 4.294 13.361 8.555 1.00 21.90 O ANISOU 1866 O HOH A 319 2019 2630 3670 155 76 -836 O HETATM 1867 O HOH A 320 18.551 8.870 -17.924 1.00 17.48 O ANISOU 1867 O HOH A 320 3558 1934 1148 40 -68 160 O HETATM 1868 O HOH A 321 8.385 -7.951 -8.079 1.00 23.64 O ANISOU 1868 O HOH A 321 5167 1782 2034 658 -2048 -330 O HETATM 1869 O HOH A 322 12.293 -17.065 16.225 1.00 17.13 O ANISOU 1869 O HOH A 322 2552 1405 2551 221 113 -89 O HETATM 1870 O HOH A 323 5.367 2.020 18.622 1.00 20.32 O ANISOU 1870 O HOH A 323 4072 2118 1530 967 828 41 O HETATM 1871 O HOH A 324 2.966 1.827 16.970 1.00 16.88 O ANISOU 1871 O HOH A 324 2359 2395 1658 219 513 -753 O HETATM 1872 O HOH A 325 2.221 -9.768 21.488 1.00 16.08 O ANISOU 1872 O HOH A 325 2041 2077 1991 341 417 337 O HETATM 1873 O HOH A 326 28.706 11.441 14.006 1.00 16.20 O ANISOU 1873 O HOH A 326 1360 2606 2190 -118 -197 -793 O HETATM 1874 O HOH A 327 19.976 -4.174 22.656 1.00 13.87 O ANISOU 1874 O HOH A 327 1813 2190 1267 -440 -187 16 O HETATM 1875 O HOH A 328 1.180 -3.367 20.670 1.00 13.93 O ANISOU 1875 O HOH A 328 2139 1905 1249 -524 -175 255 O HETATM 1876 O HOH A 329 6.489 4.521 18.165 1.00 21.07 O ANISOU 1876 O HOH A 329 2477 1882 3645 320 453 -236 O HETATM 1877 O HOH A 330 32.376 -10.851 5.024 1.00 20.58 O ANISOU 1877 O HOH A 330 1827 3067 2925 808 437 110 O HETATM 1878 O HOH A 331 16.382 0.034 27.192 1.00 14.44 O ANISOU 1878 O HOH A 331 2227 1883 1377 -150 428 -78 O HETATM 1879 O HOH A 332 5.666 11.299 7.590 1.00 15.02 O ANISOU 1879 O HOH A 332 1590 2111 2005 -278 77 384 O HETATM 1880 O HOH A 333 18.578 3.357 -14.830 1.00 16.34 O ANISOU 1880 O HOH A 333 3017 1525 1666 84 871 -86 O HETATM 1881 O HOH A 334 16.592 11.680 21.890 1.00 19.20 O ANISOU 1881 O HOH A 334 2562 3199 1534 -440 273 -1177 O HETATM 1882 O HOH A 335 5.015 -11.356 3.688 1.00 20.93 O ANISOU 1882 O HOH A 335 4067 1610 2274 667 -1483 -758 O HETATM 1883 O HOH A 336 1.228 8.486 -0.814 1.00 16.13 O ANISOU 1883 O HOH A 336 2126 1553 2451 308 -602 -20 O HETATM 1884 O HOH A 337 18.818 -11.308 21.351 1.00 25.21 O ANISOU 1884 O HOH A 337 3659 3657 2265 -417 -1138 1478 O HETATM 1885 O HOH A 338 10.098 15.469 -3.789 1.00 28.29 O ANISOU 1885 O HOH A 338 2979 2276 5493 16 2016 -1688 O HETATM 1886 O HOH A 339 -4.565 10.512 10.245 1.00 23.21 O ANISOU 1886 O HOH A 339 2237 2299 4285 -319 777 -1839 O HETATM 1887 O HOH A 340 10.974 -13.854 -3.291 1.00 14.68 O ANISOU 1887 O HOH A 340 2314 1264 1998 59 -778 260 O HETATM 1888 O HOH A 341 4.243 11.959 18.486 1.00 23.30 O ANISOU 1888 O HOH A 341 4122 2832 1900 385 -164 -907 O HETATM 1889 O HOH A 342 0.091 -6.050 21.033 1.00 21.70 O ANISOU 1889 O HOH A 342 2051 2733 3462 510 1475 1288 O HETATM 1890 O HOH A 343 7.825 17.004 5.918 1.00 21.74 O ANISOU 1890 O HOH A 343 2645 2099 3516 345 -597 -181 O HETATM 1891 O HOH A 344 15.847 10.286 -15.637 1.00 20.55 O ANISOU 1891 O HOH A 344 2432 3465 1912 -1358 -91 1377 O HETATM 1892 O HOH A 345 30.323 12.474 10.424 1.00 19.56 O ANISOU 1892 O HOH A 345 1570 2440 3420 -478 -799 -559 O HETATM 1893 O HOH A 346 21.186 4.246 -13.851 1.00 19.95 O ANISOU 1893 O HOH A 346 2981 2369 2230 -882 698 -723 O HETATM 1894 O HOH A 347 30.570 9.659 13.147 1.00 19.93 O ANISOU 1894 O HOH A 347 2215 3749 1607 473 -107 -1096 O HETATM 1895 O HOH A 348 0.542 8.750 -3.341 1.00 21.08 O ANISOU 1895 O HOH A 348 2821 3071 2116 -964 -95 154 O HETATM 1896 O HOH A 349 10.579 -0.603 -11.354 1.00 19.35 O ANISOU 1896 O HOH A 349 3010 2675 1668 881 474 8 O HETATM 1897 O HOH A 350 20.362 -7.531 -5.792 1.00 26.81 O ANISOU 1897 O HOH A 350 4600 1814 3774 -14 1880 -430 O HETATM 1898 O HOH A 351 16.624 15.386 20.430 1.00 21.55 O ANISOU 1898 O HOH A 351 2596 2741 2852 -771 -388 -1490 O HETATM 1899 O HOH A 352 32.543 -12.190 8.169 1.00 20.61 O ANISOU 1899 O HOH A 352 1661 2726 3446 430 -196 180 O HETATM 1900 O HOH A 353 9.325 -18.603 10.239 1.00 22.33 O ANISOU 1900 O HOH A 353 3289 2082 3113 143 -96 82 O HETATM 1901 O HOH A 354 24.826 1.333 -12.725 1.00 21.89 O ANISOU 1901 O HOH A 354 4272 2563 1480 30 -236 -264 O HETATM 1902 O HOH A 355 33.622 -2.326 6.347 1.00 18.37 O ANISOU 1902 O HOH A 355 2706 2764 1510 728 -210 -423 O HETATM 1903 O HOH A 356 25.245 16.582 20.351 1.00 30.80 O ANISOU 1903 O HOH A 356 3743 4748 3213 1495 -499 -1185 O HETATM 1904 O HOH A 357 9.628 -5.704 29.358 1.00 19.05 O ANISOU 1904 O HOH A 357 2665 3163 1409 365 114 -365 O HETATM 1905 O HOH A 358 25.874 12.104 16.938 1.00 18.44 O ANISOU 1905 O HOH A 358 2010 2952 2043 46 -466 -378 O HETATM 1906 O HOH A 359 32.914 5.343 5.239 1.00 18.19 O ANISOU 1906 O HOH A 359 1743 3750 1419 -965 244 -931 O HETATM 1907 O HOH A 360 -0.683 -10.554 18.837 1.00 22.91 O ANISOU 1907 O HOH A 360 1544 2491 4669 -157 379 295 O HETATM 1908 O HOH A 361 22.438 2.140 -12.492 1.00 19.80 O ANISOU 1908 O HOH A 361 3362 2940 1219 -863 311 -100 O HETATM 1909 O HOH A 362 8.309 24.736 5.080 1.00 30.63 O ANISOU 1909 O HOH A 362 3819 3064 4755 -1140 1858 -798 O HETATM 1910 O HOH A 363 25.137 15.556 -2.208 1.00 40.48 O ANISOU 1910 O HOH A 363 5944 4749 4688 717 992 -1786 O HETATM 1911 O HOH A 364 3.662 -5.928 -5.756 1.00 14.82 O ANISOU 1911 O HOH A 364 2053 1778 1801 82 -292 -223 O HETATM 1912 O HOH A 365 29.891 -4.914 19.752 1.00 17.99 O ANISOU 1912 O HOH A 365 2154 2646 2036 78 -549 -345 O HETATM 1913 O HOH A 366 25.566 -14.962 5.553 1.00 22.38 O ANISOU 1913 O HOH A 366 4553 1935 2015 -775 515 581 O HETATM 1914 O HOH A 367 22.482 -2.041 -7.273 1.00 14.66 O ANISOU 1914 O HOH A 367 2159 1721 1692 125 40 -127 O HETATM 1915 O HOH A 368 16.719 16.928 11.246 1.00 36.84 O ANISOU 1915 O HOH A 368 5203 4194 4601 -103 2371 -145 O HETATM 1916 O HOH A 369 5.733 -7.803 -5.648 1.00 14.65 O ANISOU 1916 O HOH A 369 1766 1318 2481 -163 -547 -226 O HETATM 1917 O HOH A 370 11.742 17.513 12.166 1.00 20.07 O ANISOU 1917 O HOH A 370 2709 2103 2812 141 445 -194 O HETATM 1918 O HOH A 371 18.280 -19.469 14.958 1.00 53.38 O ANISOU 1918 O HOH A 371 4113 8022 8148 -387 -3181 798 O HETATM 1919 O HOH A 372 8.526 1.486 -13.373 1.00 30.07 O ANISOU 1919 O HOH A 372 5363 4713 1350 1030 836 -708 O HETATM 1920 O HOH A 373 22.422 -10.259 -0.532 1.00 21.47 O ANISOU 1920 O HOH A 373 4444 1803 1912 -380 1420 -220 O HETATM 1921 O HOH A 374 22.608 2.408 26.291 1.00 23.24 O ANISOU 1921 O HOH A 374 2350 4675 1806 594 -25 -804 O HETATM 1922 O HOH A 375 16.082 -9.894 22.787 1.00 18.07 O ANISOU 1922 O HOH A 375 2298 2512 2056 -409 -814 1011 O HETATM 1923 O HOH A 376 24.344 -1.165 -8.806 1.00 19.36 O ANISOU 1923 O HOH A 376 3884 2077 1394 -349 -592 -173 O HETATM 1924 O HOH A 377 11.433 -4.541 -9.430 1.00 21.05 O ANISOU 1924 O HOH A 377 2724 2732 2541 -486 156 -1020 O HETATM 1925 O HOH A 378 20.120 -6.632 -8.647 1.00 20.78 O ANISOU 1925 O HOH A 378 2465 2048 3381 -581 1179 -357 O HETATM 1926 O HOH A 379 13.704 18.311 -4.478 1.00 18.89 O ANISOU 1926 O HOH A 379 3955 1311 1913 -330 785 -81 O HETATM 1927 O HOH A 380 3.273 -12.508 25.104 1.00 32.79 O ANISOU 1927 O HOH A 380 3136 5087 4234 322 857 2608 O HETATM 1928 O HOH A 381 -3.824 11.141 16.083 1.00 29.59 O ANISOU 1928 O HOH A 381 3194 5592 2455 -893 575 -1042 O HETATM 1929 O HOH A 382 6.400 3.737 -14.211 1.00 35.49 O ANISOU 1929 O HOH A 382 6462 3294 3730 -2425 -89 -1078 O HETATM 1930 O HOH A 383 26.278 -0.724 22.081 1.00 28.14 O ANISOU 1930 O HOH A 383 1876 4369 4446 177 144 -2203 O HETATM 1931 O HOH A 384 -7.557 -2.519 10.648 1.00 17.90 O ANISOU 1931 O HOH A 384 1400 2297 3104 315 458 -393 O HETATM 1932 O HOH A 385 0.104 2.821 3.122 1.00 21.43 O ANISOU 1932 O HOH A 385 1807 2094 4241 513 563 882 O HETATM 1933 O HOH A 386 25.670 -8.678 -3.450 1.00 24.55 O ANISOU 1933 O HOH A 386 3891 3047 2390 663 -1 87 O HETATM 1934 O HOH A 387 15.036 -13.293 22.244 1.00 27.40 O ANISOU 1934 O HOH A 387 4203 3205 3003 2014 -1008 7 O HETATM 1935 O HOH A 388 10.467 3.672 23.728 1.00 25.37 O ANISOU 1935 O HOH A 388 2139 3150 4350 194 285 -719 O HETATM 1936 O HOH A 389 30.837 0.249 16.768 1.00 20.18 O ANISOU 1936 O HOH A 389 1481 3342 2844 339 -395 527 O HETATM 1937 O HOH A 390 11.690 7.251 -16.668 1.00 25.62 O ANISOU 1937 O HOH A 390 4805 3123 1808 -1003 -522 -103 O HETATM 1938 O HOH A 391 7.520 21.722 6.521 1.00 36.16 O ANISOU 1938 O HOH A 391 4986 4705 4050 2202 -669 -511 O HETATM 1939 O HOH A 392 20.693 17.949 15.586 1.00 23.15 O ANISOU 1939 O HOH A 392 4231 2291 2274 -131 433 -1030 O HETATM 1940 O HOH A 393 13.176 -5.308 31.006 1.00 17.90 O ANISOU 1940 O HOH A 393 2340 2502 1957 -323 313 -371 O HETATM 1941 O HOH A 394 -3.592 7.472 4.445 1.00 27.50 O ANISOU 1941 O HOH A 394 2737 6241 1471 -1805 -174 412 O HETATM 1942 O HOH A 395 5.890 14.956 -4.141 1.00 24.27 O ANISOU 1942 O HOH A 395 2653 1853 4717 -410 2050 -707 O HETATM 1943 O HOH A 396 35.901 0.733 2.799 1.00 23.85 O ANISOU 1943 O HOH A 396 1660 3112 4290 422 537 -100 O HETATM 1944 O HOH A 397 33.206 0.174 15.035 1.00 24.33 O ANISOU 1944 O HOH A 397 1715 4155 3374 248 -800 976 O HETATM 1945 O HOH A 398 25.000 4.212 16.523 1.00 12.31 O ANISOU 1945 O HOH A 398 1294 2341 1042 -52 -201 -211 O HETATM 1946 O HOH A 399 25.205 4.942 22.537 1.00 26.93 O ANISOU 1946 O HOH A 399 3186 3954 3092 -1278 114 -1310 O HETATM 1947 O HOH A 400 6.575 -6.671 33.041 1.00 34.87 O ANISOU 1947 O HOH A 400 3754 6115 3381 -2358 381 -2194 O HETATM 1948 O HOH A 401 5.634 -17.813 13.760 1.00 30.83 O ANISOU 1948 O HOH A 401 3541 2870 5301 -845 -590 -134 O HETATM 1949 O HOH A 402 29.849 -14.987 3.521 1.00 27.39 O ANISOU 1949 O HOH A 402 3720 2354 4335 345 1194 1039 O HETATM 1950 O HOH A 403 1.857 -6.059 27.710 1.00 27.37 O ANISOU 1950 O HOH A 403 2648 5010 2742 287 1680 -99 O HETATM 1951 O HOH A 404 37.218 -2.465 9.658 1.00 27.41 O ANISOU 1951 O HOH A 404 2495 4411 3509 1568 512 -432 O HETATM 1952 O HOH A 405 -0.895 4.192 4.974 1.00 34.03 O ANISOU 1952 O HOH A 405 2752 6288 3888 2017 -1206 -2738 O HETATM 1953 O HOH A 406 25.006 12.590 -13.296 1.00 25.31 O ANISOU 1953 O HOH A 406 4066 2967 2585 -1403 888 -223 O HETATM 1954 O HOH A 407 10.539 24.029 12.423 1.00 18.79 O ANISOU 1954 O HOH A 407 3175 1682 2284 -433 -812 11 O HETATM 1955 O HOH A 408 19.455 -14.732 18.161 1.00 40.66 O ANISOU 1955 O HOH A 408 4062 4337 7052 -278 -2498 3705 O HETATM 1956 O HOH A 409 28.250 0.682 21.207 1.00 21.81 O ANISOU 1956 O HOH A 409 2937 3236 2114 -452 -627 391 O HETATM 1957 O HOH A 410 23.862 -6.081 24.153 1.00 33.50 O ANISOU 1957 O HOH A 410 3659 4024 5046 -192 -543 -341 O HETATM 1958 O HOH A 411 21.956 18.217 3.513 1.00 23.95 O ANISOU 1958 O HOH A 411 5363 1914 1823 -412 522 329 O HETATM 1959 O HOH A 412 22.202 -8.383 -9.313 1.00 31.49 O ANISOU 1959 O HOH A 412 4081 2764 5118 -1368 2606 -1726 O HETATM 1960 O HOH A 413 11.862 15.389 2.634 1.00 31.10 O ANISOU 1960 O HOH A 413 2809 7645 1365 -1304 33 -393 O HETATM 1961 O HOH A 414 8.251 0.465 21.829 1.00 36.95 O ANISOU 1961 O HOH A 414 3503 5241 5294 -1610 -1642 1647 O HETATM 1962 O HOH A 415 33.333 7.734 3.640 1.00 33.40 O ANISOU 1962 O HOH A 415 2040 6260 4390 -1536 -416 1209 O HETATM 1963 O HOH A 416 6.106 13.790 17.915 1.00 30.52 O ANISOU 1963 O HOH A 416 3103 5430 3064 -1540 902 -2318 O HETATM 1964 O HOH A 417 17.502 -8.293 -3.034 1.00 24.48 O ANISOU 1964 O HOH A 417 1933 4206 3162 774 702 -1044 O HETATM 1965 O HOH A 418 33.874 -20.549 9.170 1.00 30.75 O ANISOU 1965 O HOH A 418 2862 4031 4792 -1426 1364 -2595 O HETATM 1966 O HOH A 419 12.913 15.668 -12.171 1.00 23.78 O ANISOU 1966 O HOH A 419 5713 1599 1725 352 -594 -49 O HETATM 1967 O HOH A 420 30.831 12.702 7.256 1.00 20.08 O ANISOU 1967 O HOH A 420 2451 2405 2774 -553 -628 -549 O HETATM 1968 O HOH A 421 28.804 10.375 -3.735 1.00 26.97 O ANISOU 1968 O HOH A 421 2060 4150 4039 485 766 -1017 O HETATM 1969 O HOH A 422 30.861 -13.197 14.797 1.00 32.03 O ANISOU 1969 O HOH A 422 2464 4798 4909 -577 -726 2705 O HETATM 1970 O HOH A 423 14.162 16.106 17.603 1.00 30.42 O ANISOU 1970 O HOH A 423 4839 2216 4503 -583 -2080 193 O HETATM 1971 O HOH A 424 26.685 14.545 17.509 1.00 33.09 O ANISOU 1971 O HOH A 424 3342 4489 4742 -136 -1163 -1865 O HETATM 1972 O HOH A 425 29.080 13.646 3.130 1.00 24.58 O ANISOU 1972 O HOH A 425 3091 2626 3620 607 1332 -44 O HETATM 1973 O HOH A 426 25.580 6.271 -9.572 1.00 23.29 O ANISOU 1973 O HOH A 426 2900 2114 3833 501 1988 454 O HETATM 1974 O HOH A 427 14.074 -12.851 28.029 1.00 37.43 O ANISOU 1974 O HOH A 427 3963 4178 6083 -161 1715 710 O HETATM 1975 O HOH A 428 13.521 -19.076 14.365 1.00 35.69 O ANISOU 1975 O HOH A 428 4941 5496 3124 840 1555 2069 O HETATM 1976 O HOH A 429 28.710 6.034 -3.503 1.00 45.29 O ANISOU 1976 O HOH A 429 6537 4826 5845 -304 923 109 O HETATM 1977 O HOH A 430 34.789 5.778 8.830 1.00 28.25 O ANISOU 1977 O HOH A 430 2960 4914 2861 -1889 599 145 O HETATM 1978 O HOH A 431 18.077 14.112 14.943 1.00 26.53 O ANISOU 1978 O HOH A 431 2915 4080 3085 -1959 1391 -2264 O HETATM 1979 O HOH A 432 29.066 -17.024 12.538 1.00 35.97 O ANISOU 1979 O HOH A 432 4724 4396 4548 -453 -1398 -936 O HETATM 1980 O HOH A 433 26.750 -12.923 2.175 1.00 23.19 O ANISOU 1980 O HOH A 433 4422 2281 2108 407 -249 -388 O HETATM 1981 O HOH A 434 11.052 -6.555 32.132 1.00 35.18 O ANISOU 1981 O HOH A 434 4745 4858 3766 -399 1266 -2841 O HETATM 1982 O HOH A 435 3.607 3.883 -12.421 1.00 17.77 O ANISOU 1982 O HOH A 435 1161 1495 4098 -221 -316 162 O HETATM 1983 O HOH A 436 19.303 7.360 24.131 1.00 15.02 O ANISOU 1983 O HOH A 436 1963 2461 1284 -685 -64 -333 O HETATM 1984 O HOH A 437 -1.968 -9.810 9.894 1.00 22.32 O ANISOU 1984 O HOH A 437 1802 3121 3557 -693 -87 809 O HETATM 1985 O HOH A 438 13.748 14.919 0.789 1.00 16.01 O ANISOU 1985 O HOH A 438 1931 2131 2022 9 458 -205 O HETATM 1986 O HOH A 439 18.065 3.759 25.299 1.00 15.73 O ANISOU 1986 O HOH A 439 2476 2190 1313 560 166 146 O HETATM 1987 O HOH A 440 1.352 -10.143 13.463 1.00 15.51 O ANISOU 1987 O HOH A 440 1689 2098 2104 339 126 439 O HETATM 1988 O HOH A 441 4.657 -9.235 -3.714 1.00 16.23 O ANISOU 1988 O HOH A 441 2564 1864 1741 315 244 109 O HETATM 1989 O HOH A 442 24.696 1.755 -15.510 1.00 16.78 O ANISOU 1989 O HOH A 442 2298 2327 1752 238 42 184 O HETATM 1990 O HOH A 443 0.192 -11.340 20.996 1.00 25.28 O ANISOU 1990 O HOH A 443 3371 3343 2890 -571 850 485 O HETATM 1991 O HOH A 444 4.913 12.181 3.318 1.00 26.60 O ANISOU 1991 O HOH A 444 2083 3742 4284 275 458 2382 O HETATM 1992 O HOH A 445 4.129 -12.754 9.642 1.00 23.32 O ANISOU 1992 O HOH A 445 3292 2704 2864 -714 -655 -362 O HETATM 1993 O HOH A 446 2.049 -10.078 0.117 1.00 23.73 O ANISOU 1993 O HOH A 446 4759 2050 2206 -883 -619 357 O HETATM 1994 O HOH A 447 21.714 18.590 7.275 1.00 22.31 O ANISOU 1994 O HOH A 447 2566 2459 3450 288 452 -582 O HETATM 1995 O HOH A 448 28.099 10.627 16.761 1.00 30.12 O ANISOU 1995 O HOH A 448 4511 4167 2767 -253 202 -1309 O HETATM 1996 O HOH A 449 15.308 17.757 20.945 1.00 24.60 O ANISOU 1996 O HOH A 449 3429 2702 3215 -693 1538 -1394 O HETATM 1997 O HOH A 450 34.323 -6.768 7.517 1.00 24.03 O ANISOU 1997 O HOH A 450 1531 3069 4531 308 121 351 O HETATM 1998 O HOH A 451 -3.602 -4.969 13.251 1.00 32.97 O ANISOU 1998 O HOH A 451 3040 5334 4154 428 1253 2433 O HETATM 1999 O HOH A 452 18.448 9.980 24.084 1.00 27.20 O ANISOU 1999 O HOH A 452 3975 1835 4525 -475 749 -738 O HETATM 2000 O HOH A 453 35.164 -4.283 7.103 1.00 24.99 O ANISOU 2000 O HOH A 453 3051 2891 3554 470 730 -18 O HETATM 2001 O HOH A 454 25.913 18.317 5.883 1.00 21.33 O ANISOU 2001 O HOH A 454 3158 2028 2919 -420 -1052 -252 O HETATM 2002 O HOH A 455 19.878 11.022 -17.018 1.00 25.84 O ANISOU 2002 O HOH A 455 4505 2106 3206 -755 -668 122 O HETATM 2003 O HOH A 456 10.300 1.241 25.506 1.00 28.10 O ANISOU 2003 O HOH A 456 4683 3464 2531 1631 417 -492 O HETATM 2004 O HOH A 457 28.395 -10.916 0.701 1.00 33.60 O ANISOU 2004 O HOH A 457 5406 4198 3160 -1527 1292 -1609 O HETATM 2005 O HOH A 458 -2.810 -7.197 13.180 1.00 34.90 O ANISOU 2005 O HOH A 458 4473 2943 5844 -719 2207 -87 O HETATM 2006 O HOH A 459 5.735 -14.179 8.129 1.00 24.80 O ANISOU 2006 O HOH A 459 2915 3293 3214 509 -845 996 O HETATM 2007 O HOH A 460 1.938 -10.957 4.729 1.00 33.02 O ANISOU 2007 O HOH A 460 5641 2291 4615 1762 -236 -810 O HETATM 2008 O HOH A 461 24.147 8.107 18.483 1.00 24.35 O ANISOU 2008 O HOH A 461 2319 4151 2783 -579 231 -1445 O HETATM 2009 O HOH A 462 12.582 -16.820 24.848 1.00 35.76 O ANISOU 2009 O HOH A 462 3698 8393 1495 1623 -181 464 O HETATM 2010 O HOH A 463 -4.560 -5.599 17.154 1.00 24.67 O ANISOU 2010 O HOH A 463 1632 4846 2897 -132 647 295 O HETATM 2011 O HOH A 464 0.895 15.308 11.338 1.00 30.04 O ANISOU 2011 O HOH A 464 3424 2760 5231 385 572 -1279 O HETATM 2012 O HOH A 465 10.337 15.941 19.684 1.00 25.44 O ANISOU 2012 O HOH A 465 2978 3639 3050 -136 171 -1532 O HETATM 2013 O HOH A 466 31.880 -4.333 1.465 1.00 37.56 O ANISOU 2013 O HOH A 466 5731 4686 3854 2069 -1823 -1841 O HETATM 2014 O HOH A 467 -4.119 8.019 12.546 1.00 26.59 O ANISOU 2014 O HOH A 467 2557 4248 3296 1098 -702 -728 O HETATM 2015 O HOH A 468 28.158 17.244 6.638 1.00 31.71 O ANISOU 2015 O HOH A 468 3537 4423 4088 -78 -1040 -418 O HETATM 2016 O HOH A 469 12.440 16.317 -1.217 1.00 25.53 O ANISOU 2016 O HOH A 469 2498 5076 2128 910 787 1023 O HETATM 2017 O HOH A 470 8.004 -6.997 -10.541 1.00 31.46 O ANISOU 2017 O HOH A 470 5291 3483 3179 -1617 948 -643 O HETATM 2018 O HOH A 471 32.192 5.497 -2.069 1.00 46.47 O ANISOU 2018 O HOH A 471 7285 6986 3387 344 1976 1466 O HETATM 2019 O HOH A 472 -2.675 -10.231 5.210 1.00 29.99 O ANISOU 2019 O HOH A 472 2975 3308 5113 -1031 -539 1729 O HETATM 2020 O HOH A 473 3.500 3.014 20.719 1.00 23.69 O ANISOU 2020 O HOH A 473 2649 3632 2722 381 276 -763 O HETATM 2021 O HOH A 474 1.344 -9.639 29.295 1.00 35.52 O ANISOU 2021 O HOH A 474 5005 5307 3185 -77 1960 -251 O HETATM 2022 O HOH A 475 -0.081 -11.234 11.395 1.00 31.40 O ANISOU 2022 O HOH A 475 3558 3382 4989 -1013 -938 2311 O HETATM 2023 O HOH A 476 28.449 7.996 17.337 1.00 25.28 O ANISOU 2023 O HOH A 476 3044 2478 4082 -663 -497 -328 O HETATM 2024 O HOH A 477 20.655 -9.137 -11.827 1.00 27.56 O ANISOU 2024 O HOH A 477 4048 3161 3262 -87 -1836 1296 O HETATM 2025 O HOH A 478 4.000 4.115 -3.928 1.00 25.61 O ANISOU 2025 O HOH A 478 3788 2691 3253 -506 994 -649 O HETATM 2026 O HOH A 479 25.263 20.740 7.390 1.00 29.68 O ANISOU 2026 O HOH A 479 3816 2505 4956 -883 -208 -938 O HETATM 2027 O HOH A 480 5.938 16.534 11.125 1.00 38.35 O ANISOU 2027 O HOH A 480 5925 3516 5132 1294 -2346 116 O HETATM 2028 O HOH A 481 11.213 1.056 -13.820 1.00 20.45 O ANISOU 2028 O HOH A 481 3107 2574 2090 -421 -276 -277 O HETATM 2029 O HOH A 482 17.079 11.049 25.887 1.00 41.40 O ANISOU 2029 O HOH A 482 7026 2699 6006 -203 -1917 1750 O HETATM 2030 O HOH A 483 5.177 4.773 16.188 1.00 29.82 O ANISOU 2030 O HOH A 483 3221 3032 5078 319 266 330 O HETATM 2031 O HOH A 484 31.739 -10.813 2.381 1.00 36.16 O ANISOU 2031 O HOH A 484 4980 4447 4313 2378 1899 653 O HETATM 2032 O HOH A 485 14.839 -3.020 -10.790 1.00 17.31 O ANISOU 2032 O HOH A 485 2605 2411 1559 -716 -267 -79 O HETATM 2033 O HOH A 486 20.796 -11.027 25.687 1.00 20.51 O ANISOU 2033 O HOH A 486 3628 1913 2250 406 -708 375 O HETATM 2034 O HOH A 487 21.657 -7.136 26.555 1.00 29.53 O ANISOU 2034 O HOH A 487 2246 6531 2443 -1481 -174 148 O HETATM 2035 O HOH A 488 0.119 0.386 20.756 1.00 27.35 O ANISOU 2035 O HOH A 488 4413 4081 1900 1092 1182 -745 O HETATM 2036 O HOH A 489 1.203 -1.370 22.627 1.00 25.07 O ANISOU 2036 O HOH A 489 4003 2683 2841 300 1436 -338 O HETATM 2037 O HOH A 490 28.208 15.232 1.135 1.00 38.80 O ANISOU 2037 O HOH A 490 3780 5980 4984 -3170 -1552 1315 O HETATM 2038 O HOH A 491 32.372 -13.830 3.838 1.00 37.53 O ANISOU 2038 O HOH A 491 4445 3385 6429 -2134 271 384 O HETATM 2039 O HOH A 492 20.108 4.969 26.761 1.00 36.67 O ANISOU 2039 O HOH A 492 4030 5530 4374 -795 -970 -95 O HETATM 2040 O HOH A 493 0.102 -2.186 9.584 1.00 6.63 O ANISOU 2040 O HOH A 493 725 890 905 74 36 17 O HETATM 2041 O HOH A 494 5.421 -0.261 16.313 1.00 7.66 O ANISOU 2041 O HOH A 494 940 1236 737 -127 133 -197 O HETATM 2042 O HOH A 495 1.316 -5.681 0.021 1.00 9.14 O ANISOU 2042 O HOH A 495 1061 1716 697 -213 -206 -89 O HETATM 2043 O HOH A 496 3.910 1.655 -4.824 1.00 10.17 O ANISOU 2043 O HOH A 496 856 1500 1506 -415 -427 722 O HETATM 2044 O HOH A 497 32.007 -7.768 8.439 1.00 17.84 O ANISOU 2044 O HOH A 497 1409 3336 2033 442 -420 -155 O HETATM 2045 O HOH A 498 -4.910 -6.139 10.128 1.00 24.97 O ANISOU 2045 O HOH A 498 2848 2379 4259 -652 -115 351 O HETATM 2046 O HOH A 499 20.155 -8.706 -2.888 1.00 25.52 O ANISOU 2046 O HOH A 499 2952 3515 3228 220 -122 -398 O HETATM 2047 O HOH A 500 15.557 -0.125 -9.551 1.00 26.13 O ANISOU 2047 O HOH A 500 1743 5529 2654 -1106 858 -2989 O HETATM 2048 O HOH A 501 2.099 -13.716 21.435 1.00 29.94 O ANISOU 2048 O HOH A 501 4432 3350 3595 -751 1709 734 O HETATM 2049 O HOH A 502 15.276 14.131 -14.461 1.00 30.26 O ANISOU 2049 O HOH A 502 3612 3150 4737 -717 -2025 1788 O HETATM 2050 O HOH A 503 23.548 -8.030 -4.017 1.00 32.91 O ANISOU 2050 O HOH A 503 5111 3443 3952 80 2622 -977 O HETATM 2051 O HOH A 504 24.324 5.980 -11.981 1.00 29.29 O ANISOU 2051 O HOH A 504 3805 4099 3225 11 482 -831 O HETATM 2052 O HOH A 505 0.003 5.029 1.783 1.00 31.24 O ANISOU 2052 O HOH A 505 4103 2996 4772 -3 -2699 -105 O HETATM 2053 O HOH A 506 35.391 -7.853 5.301 1.00 35.77 O ANISOU 2053 O HOH A 506 2828 4583 6180 861 681 2090 O HETATM 2054 O HOH A 507 12.249 17.362 17.509 1.00 35.43 O ANISOU 2054 O HOH A 507 4946 4312 4204 1433 -604 -1192 O HETATM 2055 O HOH A 508 9.267 -13.466 -0.744 1.00 42.08 O ANISOU 2055 O HOH A 508 2493 5409 8085 849 18 1842 O HETATM 2056 O HOH A 509 31.248 -1.685 -13.036 1.00 31.49 O ANISOU 2056 O HOH A 509 2305 5394 4268 -267 -205 1188 O HETATM 2057 O HOH A 510 29.864 7.907 -2.838 1.00 38.87 O ANISOU 2057 O HOH A 510 4631 4126 6013 -66 1341 44 O HETATM 2058 O HOH A 511 27.473 5.436 19.971 1.00 27.84 O ANISOU 2058 O HOH A 511 3043 4029 3507 -199 259 -99 O HETATM 2059 O HOH A 512 19.142 19.968 2.130 1.00 40.70 O ANISOU 2059 O HOH A 512 4619 6066 4778 2035 -582 -597 O HETATM 2060 O HOH A 513 29.712 -2.572 20.008 1.00 35.39 O ANISOU 2060 O HOH A 513 4342 5701 3402 1639 -1779 -2101 O HETATM 2061 O HOH A 514 35.232 -3.619 3.711 1.00 39.50 O ANISOU 2061 O HOH A 514 4542 3957 6507 -1294 -150 1604 O HETATM 2062 O HOH A 515 1.125 -11.881 15.761 1.00 35.95 O ANISOU 2062 O HOH A 515 6352 5063 2244 -68 -1036 198 O HETATM 2063 O HOH A 516 -3.069 1.571 14.414 1.00 40.04 O ANISOU 2063 O HOH A 516 3756 7632 3826 -718 636 -466 O HETATM 2064 O HOH A 517 3.810 -1.180 26.565 1.00 35.01 O ANISOU 2064 O HOH A 517 3864 4583 4855 -320 500 -2418 O HETATM 2065 O HOH A 518 33.358 -2.007 -6.261 1.00 32.07 O ANISOU 2065 O HOH A 518 4212 4211 3760 -166 1308 -62 O HETATM 2066 O HOH A 519 35.696 -5.990 11.620 1.00 34.29 O ANISOU 2066 O HOH A 519 4027 3911 5090 1594 698 1369 O HETATM 2067 O HOH A 520 14.566 -15.074 23.888 1.00 35.04 O ANISOU 2067 O HOH A 520 4618 4579 4119 2162 -400 1279 O HETATM 2068 O HOH A 521 30.790 2.348 -8.548 1.00 38.07 O ANISOU 2068 O HOH A 521 4091 4907 5465 1460 2175 -52 O HETATM 2069 O HOH A 522 30.431 14.676 11.865 1.00 38.75 O ANISOU 2069 O HOH A 522 3967 3866 6889 -611 -757 -2554 O HETATM 2070 O HOH A 523 -1.832 14.111 17.557 1.00 39.71 O ANISOU 2070 O HOH A 523 4278 4096 6713 715 3319 -648 O HETATM 2071 O HOH A 524 35.646 6.396 15.141 1.00 38.21 O ANISOU 2071 O HOH A 524 4538 3795 6186 -769 -3132 -1353 O HETATM 2072 O HOH A 525 28.332 3.784 21.728 1.00 34.06 O ANISOU 2072 O HOH A 525 4665 5318 2956 1857 -1479 -1195 O HETATM 2073 O HOH A 526 18.500 18.702 7.664 1.00 42.78 O ANISOU 2073 O HOH A 526 5482 4421 6352 -2631 1744 1148 O HETATM 2074 O HOH A 527 -1.273 1.551 16.175 1.00 34.36 O ANISOU 2074 O HOH A 527 5701 3230 4124 523 1389 -651 O HETATM 2075 O HOH A 528 24.986 10.678 19.123 1.00 39.98 O ANISOU 2075 O HOH A 528 6352 5177 3661 1937 816 -978 O HETATM 2076 O HOH A 529 31.970 -1.225 19.253 1.00 35.82 O ANISOU 2076 O HOH A 529 5948 4353 3310 1442 -550 291 O HETATM 2077 O HOH A 530 37.018 -9.773 12.399 1.00 38.20 O ANISOU 2077 O HOH A 530 2165 6311 6040 -1382 587 -703 O HETATM 2078 O HOH A 531 36.268 -6.470 9.404 1.00 30.63 O ANISOU 2078 O HOH A 531 3028 5140 3471 612 -308 -1179 O HETATM 2079 O HOH A 532 29.459 15.688 7.717 1.00 27.80 O ANISOU 2079 O HOH A 532 2232 4496 3835 -1083 403 634 O HETATM 2080 O HOH A 533 6.116 -19.398 17.158 1.00 35.59 O ANISOU 2080 O HOH A 533 4256 4689 4579 671 1875 1155 O HETATM 2081 O HOH A 534 25.121 7.101 21.774 1.00 41.86 O ANISOU 2081 O HOH A 534 4657 4883 6367 -831 1110 -820 O HETATM 2082 O HOH A 535 19.200 -12.706 25.184 1.00 43.76 O ANISOU 2082 O HOH A 535 3254 7552 5819 -477 -2272 2131 O HETATM 2083 O HOH A 536 23.032 -10.680 24.153 1.00 36.73 O ANISOU 2083 O HOH A 536 6223 3413 4318 -686 113 220 O HETATM 2084 O HOH A 537 38.125 -8.497 6.336 1.00 38.76 O ANISOU 2084 O HOH A 537 2622 6343 5763 -1014 -428 992 O HETATM 2085 O HOH A 538 1.960 -11.493 8.111 1.00 26.79 O ANISOU 2085 O HOH A 538 4007 2204 3967 313 -1436 -430 O HETATM 2086 O HOH A 539 26.389 2.901 -11.992 1.00 34.78 O ANISOU 2086 O HOH A 539 6178 4574 2463 -223 835 188 O HETATM 2087 O HOH A 540 34.958 -7.496 2.350 1.00 42.52 O ANISOU 2087 O HOH A 540 4639 5855 5660 2771 1190 1604 O HETATM 2088 O HOH A 541 8.758 -10.725 -0.653 1.00 21.05 O ANISOU 2088 O HOH A 541 2327 2598 3072 -421 -251 -196 O HETATM 2089 O HOH A 542 37.568 -2.668 2.796 1.00 50.63 O ANISOU 2089 O HOH A 542 5722 6120 7396 -2265 1637 794 O HETATM 2090 O HOH A 543 8.443 13.652 19.896 1.00 38.32 O ANISOU 2090 O HOH A 543 2258 5644 6658 -842 -134 850 O HETATM 2091 O HOH A 544 -0.639 -11.701 4.042 1.00 33.43 O ANISOU 2091 O HOH A 544 4717 3631 4353 1732 -196 7 O HETATM 2092 O HOH A 545 34.723 -10.118 5.641 1.00 47.93 O ANISOU 2092 O HOH A 545 2809 7126 8277 -2307 529 -64 O HETATM 2093 O HOH A 546 31.124 0.316 22.344 1.00 41.35 O ANISOU 2093 O HOH A 546 7307 4624 3781 -2048 900 194 O HETATM 2094 O HOH A 547 14.302 0.739 26.061 1.00 18.62 O ANISOU 2094 O HOH A 547 2905 2537 1634 -375 207 -37 O CONECT 1157 1432 CONECT 1432 1157 MASTER 261 0 0 2 14 0 0 6 2093 1 2 18 END