HEADER HYDROLASE 19-NOV-01 1KF7 TITLE ATOMIC RESOLUTION STRUCTURE OF RNASE A AT PH 8.0 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PANCREATIC RIBONUCLEASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RNASE A; COMPND 5 EC: 3.1.27.5 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 ORGAN: PANCREAS KEYWDS RNASE A, TITRATION, PH, CRYSTAL, SOAKING, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR R.BERISIO,F.SICA,V.S.LAMZIN,K.S.WILSON,A.ZAGARI,L.MAZZARELLA REVDAT 3 24-FEB-09 1KF7 1 VERSN REVDAT 2 06-MAR-02 1KF7 1 JRNL REVDAT 1 19-DEC-01 1KF7 0 JRNL AUTH R.BERISIO,F.SICA,V.S.LAMZIN,K.S.WILSON,A.ZAGARI, JRNL AUTH 2 L.MAZZARELLA JRNL TITL ATOMIC RESOLUTION STRUCTURES OF RIBONUCLEASE A AT JRNL TITL 2 SIX PH VALUES. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 441 2002 JRNL REFN ISSN 0907-4449 JRNL PMID 11856829 JRNL DOI 10.1107/S0907444901021758 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.BERISIO,V.S.LAMZIN,F.SICA,K.S.WILSON,A.ZAGARI, REMARK 1 AUTH 2 L.MAZZARELLA REMARK 1 TITL PROTEIN TITRATION IN THE CRYSTAL STATE REMARK 1 REF J.MOL.BIOL. V. 292 845 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1999.3093 REMARK 2 REMARK 2 RESOLUTION. 1.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-96 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.106 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.106 REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 41956 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.100 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1044 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 232 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1139.84 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 901.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 23 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11299 REMARK 3 NUMBER OF RESTRAINTS : 13940 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) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-22 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KF7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-01. REMARK 100 THE RCSB ID CODE IS RCSB014890. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41972 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.03500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.17 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.03500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 7RSA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.74 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL, PH 8.0, LIQUID REMARK 280 DIFFUSION, TEMPERATURE 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 19.19000 REMARK 290 SMTRY3 2 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 39 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES REMARK 500 CYS A 72 CB - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 CYS A 72 CA - CB - SG ANGL. DEV. = -12.0 DEGREES REMARK 500 ASP A 83 CB - CG - OD1 ANGL. DEV. = 6.1 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 HIS A 48 64.40 -102.36 REMARK 500 GLN A 60 -136.91 -99.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KF2 RELATED DB: PDB REMARK 900 1KF2 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 5.2. REMARK 900 RELATED ID: 1KF3 RELATED DB: PDB REMARK 900 1KF3 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 5.9. REMARK 900 RELATED ID: 1KF4 RELATED DB: PDB REMARK 900 1KF4 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 6.3. REMARK 900 RELATED ID: 1KF5 RELATED DB: PDB REMARK 900 1KF5 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 7.1. REMARK 900 RELATED ID: 1KF8 RELATED DB: PDB REMARK 900 1KF8 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 8.8. DBREF 1KF7 A 1 124 UNP P61823 RNAS1_BOVIN 27 150 SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL FORMUL 2 HOH *230(H2 O) HELIX 1 1 THR A 3 MET A 13 1 11 HELIX 2 2 ASN A 24 ARG A 33 1 10 HELIX 3 3 SER A 50 ALA A 56 1 7 HELIX 4 4 VAL A 57 GLN A 60 5 4 SHEET 1 A 3 VAL A 43 VAL A 47 0 SHEET 2 A 3 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44 SHEET 3 A 3 TYR A 97 LYS A 104 -1 O LYS A 98 N ARG A 85 SHEET 1 B 4 LYS A 61 VAL A 63 0 SHEET 2 B 4 CYS A 72 GLN A 74 -1 O GLN A 74 N LYS A 61 SHEET 3 B 4 ILE A 106 GLU A 111 -1 O VAL A 108 N TYR A 73 SHEET 4 B 4 VAL A 116 SER A 123 -1 O VAL A 118 N ALA A 109 SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.03 SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.02 SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.00 SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.02 CISPEP 1 TYR A 92 PRO A 93 0 7.41 CISPEP 2 ASN A 113 PRO A 114 0 2.06 CRYST1 30.440 38.380 53.320 90.00 105.74 90.00 P 1 21 1 2 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 0.032852 0.000000 0.009259 0.00000 SCALE2 0.000000 0.026055 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019485 0.00000 ATOM 1 N LYS A 1 21.236 9.173 27.460 1.00 48.39 N ANISOU 1 N LYS A 1 5578 6894 5915 705 -4207 -2478 N ATOM 2 CA LYS A 1 20.731 7.939 26.946 1.00 31.56 C ANISOU 2 CA LYS A 1 2486 6785 2718 -227 -1214 -1364 C ATOM 3 C LYS A 1 20.054 8.231 25.584 1.00 24.96 C ANISOU 3 C LYS A 1 2059 5245 2178 -11 -509 -1298 C ATOM 4 O LYS A 1 19.688 9.359 25.305 1.00 28.42 O ANISOU 4 O LYS A 1 2808 4805 3184 -209 -1105 -1827 O ATOM 5 CB LYS A 1 19.604 7.460 27.875 1.00 37.43 C ATOM 6 CG LYS A 1 19.908 6.329 28.832 1.00 76.76 C ATOM 7 CD LYS A 1 18.959 6.399 30.029 1.00106.07 C ATOM 8 CE LYS A 1 17.533 6.036 29.644 1.00101.35 C ATOM 9 NZ LYS A 1 17.075 4.740 30.232 1.00139.28 N ATOM 10 N GLU A 2 19.883 7.201 24.795 1.00 19.95 N ANISOU 10 N GLU A 2 1539 4385 1656 -34 -164 -584 N ATOM 11 CA GLU A 2 19.136 7.367 23.544 1.00 17.57 C ANISOU 11 CA GLU A 2 1468 3441 1768 -2 -112 -894 C ATOM 12 C GLU A 2 17.727 7.857 23.829 1.00 18.16 C ANISOU 12 C GLU A 2 1461 3716 1724 69 -215 -1018 C ATOM 13 O GLU A 2 17.018 7.345 24.644 1.00 21.16 O ANISOU 13 O GLU A 2 1532 4328 2180 123 31 -787 O ATOM 14 CB GLU A 2 19.091 5.996 22.928 1.00 17.36 C ANISOU 14 CB GLU A 2 1711 3158 1726 154 -140 -556 C ATOM 15 CG GLU A 2 18.550 5.989 21.534 1.00 17.35 C ANISOU 15 CG GLU A 2 1991 2787 1814 -27 -374 -590 C ATOM 16 CD GLU A 2 18.501 4.628 20.888 1.00 15.97 C ANISOU 16 CD GLU A 2 1879 2571 1618 197 -95 -367 C ATOM 17 OE1 GLU A 2 18.239 3.638 21.595 1.00 20.87 O ANISOU 17 OE1 GLU A 2 3446 2851 1632 -243 184 -328 O ATOM 18 OE2 GLU A 2 18.702 4.523 19.668 1.00 16.05 O ANISOU 18 OE2 GLU A 2 1929 2459 1711 -54 28 -364 O ATOM 19 N THR A 3 17.286 8.852 23.103 1.00 18.86 N ANISOU 19 N THR A 3 1703 3383 2081 109 -561 -1263 N ATOM 20 CA THR A 3 15.926 9.356 23.251 1.00 20.76 C ANISOU 20 CA THR A 3 1938 3702 2247 417 -568 -1478 C ATOM 21 C THR A 3 14.934 8.391 22.621 1.00 17.84 C ANISOU 21 C THR A 3 1631 3363 1784 395 -502 -986 C ATOM 22 O THR A 3 15.244 7.590 21.755 1.00 17.08 O ANISOU 22 O THR A 3 1637 3124 1727 43 -269 -893 O ATOM 23 CB THR A 3 15.783 10.765 22.624 1.00 24.03 C ANISOU 23 CB THR A 3 2557 3253 3320 375 -942 -1684 C ATOM 24 OG1 THR A 3 15.901 10.615 21.213 1.00 24.03 O ANISOU 24 OG1 THR A 3 3001 2940 3191 149 -933 -970 O ATOM 25 CG2 THR A 3 16.806 11.739 23.183 1.00 31.52 C ANISOU 25 CG2 THR A 3 3507 3785 4686 -46 -1228 -2233 C ATOM 26 N ALA A 4 13.662 8.538 23.024 1.00 19.25 N ANISOU 26 N ALA A 4 1794 3761 1761 555 -350 -940 N ATOM 27 CA ALA A 4 12.598 7.712 22.444 1.00 17.96 C ANISOU 27 CA ALA A 4 1565 3671 1587 450 -250 -643 C ATOM 28 C ALA A 4 12.476 7.979 20.938 1.00 16.20 C ANISOU 28 C ALA A 4 1669 2839 1648 248 -92 -611 C ATOM 29 O ALA A 4 12.231 7.068 20.168 1.00 16.02 O ANISOU 29 O ALA A 4 1830 2613 1644 198 -133 -572 O ATOM 30 CB ALA A 4 11.261 7.953 23.152 1.00 21.15 C ANISOU 30 CB ALA A 4 1868 4337 1831 239 139 -690 C ATOM 31 N ALA A 5 12.637 9.216 20.527 1.00 16.52 N ANISOU 31 N ALA A 5 1682 2660 1936 274 -318 -770 N ATOM 32 CA ALA A 5 12.539 9.574 19.110 1.00 16.24 C ANISOU 32 CA ALA A 5 1677 2356 2136 258 -336 -453 C ATOM 33 C ALA A 5 13.662 8.899 18.338 1.00 14.82 C ANISOU 33 C ALA A 5 1595 2107 1931 -141 -196 -460 C ATOM 34 O ALA A 5 13.442 8.405 17.215 1.00 14.91 O ANISOU 34 O ALA A 5 1834 1954 1879 -112 -392 -363 O ATOM 35 CB ALA A 5 12.580 11.054 18.891 1.00 21.32 C ANISOU 35 CB ALA A 5 2684 2205 3211 350 -396 -488 C ATOM 36 N ALA A 6 14.883 8.898 18.879 1.00 14.98 N ANISOU 36 N ALA A 6 1633 2085 1972 55 -356 -670 N ATOM 37 CA ALA A 6 16.019 8.286 18.199 1.00 14.57 C ANISOU 37 CA ALA A 6 1587 1966 1982 -158 -185 -403 C ATOM 38 C ALA A 6 15.867 6.789 18.132 1.00 12.67 C ANISOU 38 C ALA A 6 1279 1993 1541 -131 -129 -346 C ATOM 39 O ALA A 6 16.221 6.157 17.130 1.00 13.21 O ANISOU 39 O ALA A 6 1544 1993 1483 -134 52 -305 O ATOM 40 CB ALA A 6 17.328 8.664 18.913 1.00 17.66 C ANISOU 40 CB ALA A 6 1565 2245 2898 -236 -393 -650 C ATOM 41 N LYS A 7 15.312 6.190 19.184 1.00 13.29 N ANISOU 41 N LYS A 7 1454 2149 1448 -105 -14 -393 N ATOM 42 CA LYS A 7 15.069 4.767 19.209 1.00 12.93 C ANISOU 42 CA LYS A 7 1411 2100 1401 20 -141 -187 C ATOM 43 C LYS A 7 14.040 4.408 18.145 1.00 11.48 C ANISOU 43 C LYS A 7 1335 1878 1151 -17 27 -177 C ATOM 44 O LYS A 7 14.193 3.384 17.469 1.00 12.30 O ANISOU 44 O LYS A 7 1594 1768 1314 36 4 -111 O ATOM 45 CB LYS A 7 14.560 4.343 20.599 1.00 14.71 C ANISOU 45 CB LYS A 7 1871 2581 1136 159 -130 -110 C ATOM 46 CG LYS A 7 14.272 2.832 20.682 1.00 20.98 C ANISOU 46 CG LYS A 7 3479 2744 1749 -343 -342 381 C ATOM 47 CD LYS A 7 13.831 2.506 22.126 1.00 31.38 C ANISOU 47 CD LYS A 7 6298 3585 2041 -830 401 616 C ATOM 48 CE LYS A 7 12.564 1.670 22.286 1.00 52.69 C ANISOU 48 CE LYS A 7 7065 8363 4592 -2641 1448 1958 C ATOM 49 NZ LYS A 7 12.215 1.279 23.685 1.00 64.76 N ANISOU 49 NZ LYS A 7 10292 10321 3993 -5378 2207 -5 N ATOM 50 N PHE A 8 13.012 5.212 17.951 1.00 11.60 N ANISOU 50 N PHE A 8 1238 1936 1233 8 -86 -254 N ATOM 51 CA PHE A 8 12.050 4.951 16.872 1.00 11.04 C ANISOU 51 CA PHE A 8 1275 1632 1289 7 -45 -269 C ATOM 52 C PHE A 8 12.753 4.930 15.515 1.00 10.44 C ANISOU 52 C PHE A 8 1219 1450 1299 -30 -53 -200 C ATOM 53 O PHE A 8 12.488 4.065 14.694 1.00 11.00 O ANISOU 53 O PHE A 8 1419 1467 1295 -134 14 -309 O ATOM 54 CB PHE A 8 10.940 6.002 16.907 1.00 12.30 C ANISOU 54 CB PHE A 8 1266 1912 1496 147 -4 -313 C ATOM 55 CG PHE A 8 9.939 5.839 15.798 1.00 11.35 C ANISOU 55 CG PHE A 8 1141 1659 1514 69 3 -229 C ATOM 56 CD1 PHE A 8 8.793 5.108 15.965 1.00 12.86 C ANISOU 56 CD1 PHE A 8 1204 1986 1695 14 10 -90 C ATOM 57 CD2 PHE A 8 10.116 6.418 14.564 1.00 13.35 C ANISOU 57 CD2 PHE A 8 1426 2174 1474 68 56 -112 C ATOM 58 CE1 PHE A 8 7.891 4.944 14.948 1.00 13.62 C ANISOU 58 CE1 PHE A 8 1436 1847 1890 -89 -244 -120 C ATOM 59 CE2 PHE A 8 9.267 6.186 13.524 1.00 14.17 C ANISOU 59 CE2 PHE A 8 1602 2344 1439 185 9 -133 C ATOM 60 CZ PHE A 8 8.140 5.460 13.727 1.00 13.71 C ANISOU 60 CZ PHE A 8 1545 1960 1705 212 -196 -293 C ATOM 61 N GLU A 9 13.626 5.903 15.264 1.00 11.03 N ANISOU 61 N GLU A 9 1339 1503 1349 -161 5 -302 N ATOM 62 CA GLU A 9 14.336 5.924 13.997 1.00 10.92 C ANISOU 62 CA GLU A 9 1401 1431 1317 -80 -45 -138 C ATOM 63 C GLU A 9 15.175 4.664 13.812 1.00 10.34 C ANISOU 63 C GLU A 9 1301 1433 1194 -112 106 -71 C ATOM 64 O GLU A 9 15.201 4.065 12.749 1.00 11.29 O ANISOU 64 O GLU A 9 1520 1615 1153 7 100 -102 O ATOM 65 CB AGLU A 9 15.253 7.141 13.870 0.54 12.01 C ANISOU 65 CB AGLU A 9 1500 1462 1600 -174 -34 73 C ATOM 66 CB BGLU A 9 15.115 7.235 13.865 0.46 13.27 C ANISOU 66 CB BGLU A 9 1848 1427 1769 -97 291 -4 C ATOM 67 CG AGLU A 9 14.475 8.421 13.828 0.54 14.25 C ANISOU 67 CG AGLU A 9 2170 1447 1797 -63 -151 402 C ATOM 68 CG BGLU A 9 15.694 7.495 12.511 0.46 14.90 C ANISOU 68 CG BGLU A 9 2010 1810 1840 -154 342 207 C ATOM 69 CD AGLU A 9 15.345 9.625 13.568 0.54 17.10 C ANISOU 69 CD AGLU A 9 2559 1447 2490 -212 -77 237 C ATOM 70 CD BGLU A 9 16.833 8.486 12.402 0.46 19.07 C ANISOU 70 CD BGLU A 9 2205 2365 2676 -532 812 -141 C ATOM 71 OE1AGLU A 9 16.438 9.435 12.946 0.54 18.80 O ANISOU 71 OE1AGLU A 9 1981 1649 3512 -429 -203 196 O ATOM 72 OE1BGLU A 9 17.149 8.772 11.235 0.46 27.83 O ANISOU 72 OE1BGLU A 9 2857 4498 3218 -1143 542 1400 O ATOM 73 OE2AGLU A 9 14.916 10.713 14.001 0.54 21.38 O ANISOU 73 OE2AGLU A 9 3341 1499 3284 -288 222 -164 O ATOM 74 OE2BGLU A 9 17.397 8.900 13.425 0.46 36.73 O ANISOU 74 OE2BGLU A 9 5438 4918 3602 -3332 -571 462 O ATOM 75 N ARG A 10 15.929 4.286 14.851 1.00 10.44 N ANISOU 75 N ARG A 10 1308 1482 1177 -56 -16 -116 N ATOM 76 CA ARG A 10 16.785 3.132 14.772 1.00 10.44 C ANISOU 76 CA ARG A 10 1212 1592 1163 -57 72 -137 C ATOM 77 C ARG A 10 15.991 1.844 14.578 1.00 9.62 C ANISOU 77 C ARG A 10 1164 1429 1062 25 14 -13 C ATOM 78 O ARG A 10 16.389 0.977 13.811 1.00 10.97 O ANISOU 78 O ARG A 10 1377 1544 1247 30 134 -35 O ATOM 79 CB ARG A 10 17.632 3.021 16.048 1.00 11.66 C ANISOU 79 CB ARG A 10 1267 1837 1329 -44 -121 -205 C ATOM 80 CG ARG A 10 18.492 1.775 16.128 1.00 12.28 C ANISOU 80 CG ARG A 10 1407 1949 1308 167 -42 -166 C ATOM 81 CD ARG A 10 19.506 1.837 17.262 1.00 14.03 C ANISOU 81 CD ARG A 10 1564 2266 1501 246 -211 -179 C ATOM 82 NE ARG A 10 18.858 1.926 18.561 1.00 14.49 N ANISOU 82 NE ARG A 10 1941 2145 1419 86 -266 -193 N ATOM 83 CZ ARG A 10 18.384 0.908 19.237 1.00 18.63 C ANISOU 83 CZ ARG A 10 3252 2345 1483 -152 83 -197 C ATOM 84 NH1 ARG A 10 18.407 -0.317 18.779 1.00 22.27 N ANISOU 84 NH1 ARG A 10 4437 2283 1743 -604 395 -303 N ATOM 85 NH2 ARG A 10 17.892 1.106 20.458 1.00 24.34 N ANISOU 85 NH2 ARG A 10 4761 2939 1547 -773 591 -380 N ATOM 86 N AGLN A 11 14.873 1.680 15.278 0.43 10.25 N ANISOU 86 N AGLN A 11 1314 1470 1111 -13 66 -87 N ATOM 87 N BGLN A 11 14.886 1.704 15.262 0.57 10.20 N ANISOU 87 N BGLN A 11 1333 1450 1091 -39 81 -80 N ATOM 88 CA AGLN A 11 14.089 0.457 15.184 0.43 9.94 C ANISOU 88 CA AGLN A 11 1406 1406 964 -29 121 170 C ATOM 89 CA BGLN A 11 14.100 0.477 15.201 0.57 10.26 C ANISOU 89 CA BGLN A 11 1276 1403 1219 20 -19 68 C ATOM 90 C AGLN A 11 13.279 0.360 13.897 0.43 10.03 C ANISOU 90 C AGLN A 11 1514 1308 988 -112 126 19 C ATOM 91 C BGLN A 11 13.259 0.362 13.941 0.57 10.18 C ANISOU 91 C BGLN A 11 1467 1308 1092 -89 109 -12 C ATOM 92 O AGLN A 11 13.027 -0.745 13.475 0.43 12.61 O ANISOU 92 O AGLN A 11 2014 1282 1497 -72 -184 -37 O ATOM 93 O BGLN A 11 13.031 -0.733 13.490 0.57 12.65 O ANISOU 93 O BGLN A 11 2018 1287 1501 -83 -205 -56 O ATOM 94 CB AGLN A 11 13.092 0.239 16.320 0.43 10.88 C ANISOU 94 CB AGLN A 11 1371 1791 972 27 118 28 C ATOM 95 CB BGLN A 11 13.276 0.407 16.467 0.57 11.79 C ANISOU 95 CB BGLN A 11 1690 1679 1111 -242 1 162 C ATOM 96 CG AGLN A 11 13.774 0.150 17.657 0.43 10.51 C ANISOU 96 CG AGLN A 11 1373 1624 998 183 107 372 C ATOM 97 CG BGLN A 11 12.572 -0.910 16.672 0.57 17.48 C ANISOU 97 CG BGLN A 11 2499 1960 2184 -596 -78 771 C ATOM 98 CD AGLN A 11 12.890 -0.193 18.814 0.43 15.06 C ANISOU 98 CD AGLN A 11 2082 2393 1245 -230 360 633 C ATOM 99 CD BGLN A 11 12.151 -1.028 18.123 0.57 22.85 C ANISOU 99 CD BGLN A 11 2774 3341 2566 -716 312 1530 C ATOM 100 OE1AGLN A 11 13.423 -0.693 19.855 0.43 27.08 O ANISOU 100 OE1AGLN A 11 3166 5815 1309 -1117 -375 1453 O ATOM 101 OE1BGLN A 11 12.943 -1.485 18.981 0.57 26.93 O ANISOU 101 OE1BGLN A 11 3095 5212 1927 -151 377 1082 O ATOM 102 NE2AGLN A 11 11.629 0.090 18.774 0.43 23.66 N ANISOU 102 NE2AGLN A 11 2292 4833 1864 597 1192 789 N ATOM 103 NE2BGLN A 11 10.945 -0.670 18.511 0.57 41.33 N ANISOU 103 NE2BGLN A 11 4478 8069 3159 2306 1313 3079 N ATOM 104 N HIS A 12 12.796 1.489 13.374 1.00 9.56 N ANISOU 104 N HIS A 12 1400 1270 963 -190 11 45 N ATOM 105 CA HIS A 12 11.730 1.446 12.404 1.00 10.17 C ANISOU 105 CA HIS A 12 1493 1377 995 -250 -46 -7 C ATOM 106 C HIS A 12 11.982 2.106 11.071 1.00 10.77 C ANISOU 106 C HIS A 12 1744 1336 1014 -295 -86 -29 C ATOM 107 O HIS A 12 11.233 1.862 10.162 1.00 16.44 O ANISOU 107 O HIS A 12 2935 2019 1294 -1128 -721 353 O ATOM 108 CB HIS A 12 10.397 1.972 12.971 1.00 10.75 C ANISOU 108 CB HIS A 12 1466 1322 1296 -70 -86 23 C ATOM 109 CG HIS A 12 9.966 1.245 14.165 1.00 10.28 C ANISOU 109 CG HIS A 12 1274 1452 1180 -69 -32 -48 C ATOM 110 ND1 HIS A 12 9.577 -0.069 14.113 1.00 11.38 N ANISOU 110 ND1 HIS A 12 1635 1430 1259 -127 319 -35 N ATOM 111 CD2 HIS A 12 9.825 1.579 15.464 1.00 11.69 C ANISOU 111 CD2 HIS A 12 1502 1699 1242 -7 -23 -189 C ATOM 112 CE1 HIS A 12 9.274 -0.459 15.380 1.00 12.74 C ANISOU 112 CE1 HIS A 12 1851 1624 1367 5 453 54 C ATOM 113 NE2 HIS A 12 9.405 0.541 16.210 1.00 12.35 N ANISOU 113 NE2 HIS A 12 1684 1815 1192 166 217 -112 N ATOM 114 N MET A 13 12.959 2.991 10.949 1.00 10.24 N ANISOU 114 N MET A 13 1510 1390 992 -152 39 7 N ATOM 115 CA MET A 13 13.097 3.737 9.694 1.00 10.35 C ANISOU 115 CA MET A 13 1468 1458 1005 -26 99 110 C ATOM 116 C MET A 13 14.147 3.135 8.797 1.00 10.33 C ANISOU 116 C MET A 13 1413 1486 1026 -32 95 174 C ATOM 117 O MET A 13 15.290 2.915 9.231 1.00 12.75 O ANISOU 117 O MET A 13 1564 2151 1129 241 72 123 O ATOM 118 CB MET A 13 13.461 5.191 9.996 1.00 11.55 C ANISOU 118 CB MET A 13 1693 1376 1321 -48 18 99 C ATOM 119 CG MET A 13 12.340 5.993 10.604 1.00 13.43 C ANISOU 119 CG MET A 13 2174 1499 1429 206 -39 -199 C ATOM 120 SD MET A 13 10.850 6.119 9.663 1.00 14.30 S ANISOU 120 SD MET A 13 1997 1982 1454 428 36 -22 S ATOM 121 CE MET A 13 11.486 6.692 8.104 1.00 17.10 C ANISOU 121 CE MET A 13 2717 2342 1438 561 170 183 C ATOM 122 N ASP A 14 13.844 2.986 7.521 1.00 10.12 N ANISOU 122 N ASP A 14 1480 1376 990 -85 169 83 N ATOM 123 CA ASP A 14 14.853 2.661 6.534 1.00 10.51 C ANISOU 123 CA ASP A 14 1611 1370 1012 -67 254 147 C ATOM 124 C ASP A 14 14.548 3.413 5.250 1.00 10.73 C ANISOU 124 C ASP A 14 1572 1492 1012 27 223 74 C ATOM 125 O ASP A 14 13.986 2.883 4.306 1.00 12.99 O ANISOU 125 O ASP A 14 1943 1918 1075 -191 72 51 O ATOM 126 CB ASP A 14 15.012 1.178 6.261 1.00 12.83 C ANISOU 126 CB ASP A 14 2131 1381 1362 -14 460 80 C ATOM 127 CG ASP A 14 16.182 0.914 5.335 1.00 13.57 C ANISOU 127 CG ASP A 14 2316 1464 1378 230 469 72 C ATOM 128 OD1 ASP A 14 16.958 1.860 5.039 1.00 15.13 O ANISOU 128 OD1 ASP A 14 2082 1875 1792 64 588 165 O ATOM 129 OD2 ASP A 14 16.288 -0.236 4.858 1.00 16.54 O ANISOU 129 OD2 ASP A 14 2852 1648 1785 217 815 -57 O ATOM 130 N SER A 15 14.967 4.679 5.217 1.00 12.00 N ANISOU 130 N SER A 15 1913 1505 1142 -105 86 239 N ATOM 131 CA SER A 15 14.779 5.558 4.083 1.00 13.48 C ANISOU 131 CA SER A 15 1982 1804 1336 95 231 458 C ATOM 132 C SER A 15 15.763 5.261 2.971 1.00 13.10 C ANISOU 132 C SER A 15 1909 1857 1212 -77 193 359 C ATOM 133 O SER A 15 15.644 5.879 1.904 1.00 17.28 O ANISOU 133 O SER A 15 3124 1980 1464 270 513 546 O ATOM 134 CB ASER A 15 14.969 7.013 4.527 0.65 18.18 C ANISOU 134 CB ASER A 15 3285 1513 2108 797 579 493 C ATOM 135 CB BSER A 15 14.906 7.044 4.434 0.35 15.42 C ANISOU 135 CB BSER A 15 2320 1650 1887 46 1143 644 C ATOM 136 OG ASER A 15 14.167 7.333 5.652 0.65 15.49 O ANISOU 136 OG ASER A 15 2282 1696 1907 39 237 211 O ATOM 137 OG BSER A 15 16.235 7.278 4.861 0.35 22.10 O ANISOU 137 OG BSER A 15 3084 1973 3338 -481 48 256 O ATOM 138 N SER A 16 16.685 4.354 3.148 1.00 14.16 N ANISOU 138 N SER A 16 1893 2046 1441 60 428 453 N ATOM 139 CA SER A 16 17.740 4.054 2.193 1.00 14.84 C ANISOU 139 CA SER A 16 1917 2167 1556 -119 433 363 C ATOM 140 C SER A 16 17.357 3.039 1.147 1.00 14.27 C ANISOU 140 C SER A 16 1939 2022 1462 107 433 439 C ATOM 141 O SER A 16 18.063 2.889 0.173 1.00 17.04 O ANISOU 141 O SER A 16 2249 2544 1681 165 620 291 O ATOM 142 CB ASER A 16 18.985 3.485 2.907 0.71 17.23 C ANISOU 142 CB ASER A 16 1737 2758 2053 26 356 127 C ATOM 143 CB BSER A 16 19.064 3.727 2.881 0.28 19.56 C ANISOU 143 CB BSER A 16 1605 3827 2000 -188 446 99 C ATOM 144 OG ASER A 16 18.873 2.098 3.213 0.71 18.98 O ANISOU 144 OG ASER A 16 2130 2963 2117 582 574 719 O ATOM 145 OG BSER A 16 19.473 4.813 3.708 0.28 22.80 O ANISOU 145 OG BSER A 16 1815 3863 2984 -422 0 15 O ATOM 146 N THR A 17 16.200 2.412 1.311 1.00 14.79 N ANISOU 146 N THR A 17 2111 1698 1812 22 576 207 N ATOM 147 CA THR A 17 15.706 1.450 0.341 1.00 15.51 C ANISOU 147 CA THR A 17 2281 1761 1852 142 469 123 C ATOM 148 C THR A 17 14.222 1.697 0.167 1.00 14.29 C ANISOU 148 C THR A 17 2291 1701 1437 96 429 247 C ATOM 149 O THR A 17 13.536 2.171 1.055 1.00 15.50 O ANISOU 149 O THR A 17 2110 2268 1510 64 331 -12 O ATOM 150 CB ATHR A 17 15.918 0.004 0.862 0.47 15.74 C ANISOU 150 CB ATHR A 17 2164 1741 2077 173 328 27 C ATOM 151 CB BTHR A 17 16.002 -0.028 0.616 0.53 18.11 C ANISOU 151 CB BTHR A 17 2781 1795 2307 423 247 -75 C ATOM 152 OG1ATHR A 17 15.207 -0.172 2.099 0.47 15.88 O ANISOU 152 OG1ATHR A 17 1590 2084 2358 -66 205 596 O ATOM 153 OG1BTHR A 17 15.692 -0.825 -0.550 0.53 17.56 O ANISOU 153 OG1BTHR A 17 2795 1642 2234 291 498 17 O ATOM 154 CG2ATHR A 17 17.399 -0.256 1.123 0.47 17.18 C ANISOU 154 CG2ATHR A 17 2070 1961 2496 415 624 -154 C ATOM 155 CG2BTHR A 17 15.159 -0.534 1.777 0.53 28.42 C ANISOU 155 CG2BTHR A 17 6142 2287 2368 769 1214 831 C ATOM 156 N SER A 18 13.671 1.336 -0.977 1.00 14.84 N ANISOU 156 N SER A 18 2431 1649 1557 13 501 137 N ATOM 157 CA SER A 18 12.277 1.528 -1.261 1.00 14.99 C ANISOU 157 CA SER A 18 2526 1747 1421 51 166 188 C ATOM 158 C SER A 18 11.397 0.371 -0.819 1.00 13.12 C ANISOU 158 C SER A 18 2275 1619 1092 146 108 54 C ATOM 159 O SER A 18 10.174 0.566 -0.665 1.00 14.47 O ANISOU 159 O SER A 18 2259 1827 1410 249 132 122 O ATOM 160 CB ASER A 18 12.020 1.955 -2.693 0.58 22.85 C ANISOU 160 CB ASER A 18 3840 2950 1892 -616 -255 1065 C ATOM 161 CB BSER A 18 12.072 1.702 -2.775 0.17 21.49 C ANISOU 161 CB BSER A 18 4450 1980 1733 -418 -419 904 C ATOM 162 CB CSER A 18 12.084 1.664 -2.780 0.24 16.73 C ANISOU 162 CB CSER A 18 3124 1748 1485 453 362 460 C ATOM 163 OG ASER A 18 12.864 3.065 -3.032 0.58 26.95 O ANISOU 163 OG ASER A 18 5067 2941 2231 -1039 -147 1121 O ATOM 164 OG BSER A 18 12.431 0.525 -3.487 0.17 20.03 O ANISOU 164 OG BSER A 18 3376 3376 857 -312 620 445 O ATOM 165 OG CSER A 18 10.694 1.703 -3.058 0.24 30.87 O ANISOU 165 OG CSER A 18 3781 4368 3581 -1224 -1620 1448 O ATOM 166 N ALA A 19 11.946 -0.804 -0.628 1.00 14.24 N ANISOU 166 N ALA A 19 2190 1633 1589 160 265 72 N ATOM 167 CA ALA A 19 11.321 -2.045 -0.237 1.00 13.56 C ANISOU 167 CA ALA A 19 2072 1618 1463 97 108 55 C ATOM 168 C ALA A 19 12.418 -3.043 0.082 1.00 13.30 C ANISOU 168 C ALA A 19 2092 1595 1367 196 232 -41 C ATOM 169 O ALA A 19 13.569 -2.873 -0.276 1.00 16.81 O ANISOU 169 O ALA A 19 2217 1798 2370 126 558 276 O ATOM 170 CB ALA A 19 10.416 -2.596 -1.341 1.00 17.18 C ANISOU 170 CB ALA A 19 2508 2222 1799 48 -344 49 C ATOM 171 N ALA A 20 12.064 -4.088 0.783 1.00 13.19 N ANISOU 171 N ALA A 20 2119 1496 1395 163 208 -23 N ATOM 172 CA ALA A 20 13.014 -5.165 1.058 1.00 13.54 C ANISOU 172 CA ALA A 20 2150 1503 1490 166 204 -86 C ATOM 173 C ALA A 20 13.407 -5.820 -0.258 1.00 15.28 C ANISOU 173 C ALA A 20 2550 1600 1656 326 561 10 C ATOM 174 O ALA A 20 12.574 -6.167 -1.049 1.00 20.73 O ANISOU 174 O ALA A 20 3409 2802 1665 255 318 -601 O ATOM 175 CB ALA A 20 12.401 -6.192 1.973 1.00 14.51 C ANISOU 175 CB ALA A 20 2479 1671 1363 262 261 112 C ATOM 176 N SER A 21 14.675 -6.103 -0.446 1.00 18.65 N ANISOU 176 N SER A 21 2905 1976 2206 647 1081 381 N ATOM 177 CA SER A 21 15.126 -6.605 -1.761 1.00 21.81 C ANISOU 177 CA SER A 21 3799 2210 2276 1207 1417 490 C ATOM 178 C SER A 21 15.439 -8.077 -1.758 1.00 16.90 C ANISOU 178 C SER A 21 2842 1998 1583 634 549 268 C ATOM 179 O SER A 21 15.734 -8.626 -2.820 1.00 19.81 O ANISOU 179 O SER A 21 3422 2506 1599 887 1012 296 O ATOM 180 CB SER A 21 16.377 -5.866 -2.272 1.00 30.77 C ANISOU 180 CB SER A 21 5656 1956 4080 712 3250 535 C ATOM 181 OG SER A 21 17.319 -6.001 -1.173 1.00 40.71 O ANISOU 181 OG SER A 21 3907 2977 8582 -313 1487 1551 O ATOM 182 N SER A 22 15.423 -8.772 -0.624 1.00 15.03 N ANISOU 182 N SER A 22 2616 1641 1455 288 613 -15 N ATOM 183 CA SER A 22 15.696 -10.191 -0.586 1.00 14.10 C ANISOU 183 CA SER A 22 2616 1594 1146 268 456 -98 C ATOM 184 C SER A 22 15.122 -10.747 0.696 1.00 13.07 C ANISOU 184 C SER A 22 2388 1456 1123 104 307 -226 C ATOM 185 O SER A 22 14.770 -10.030 1.638 1.00 13.37 O ANISOU 185 O SER A 22 2305 1544 1231 68 355 -261 O ATOM 186 CB SER A 22 17.175 -10.491 -0.665 1.00 16.11 C ANISOU 186 CB SER A 22 2653 1818 1650 373 614 -98 C ATOM 187 OG SER A 22 17.895 -10.173 0.490 1.00 20.82 O ANISOU 187 OG SER A 22 2815 3199 1898 200 257 -129 O ATOM 188 N SER A 23 15.084 -12.076 0.732 1.00 14.39 N ANISOU 188 N SER A 23 2817 1487 1164 12 276 -271 N ATOM 189 CA SER A 23 14.632 -12.808 1.932 1.00 14.53 C ANISOU 189 CA SER A 23 2717 1657 1148 -204 232 -158 C ATOM 190 C SER A 23 15.472 -12.573 3.136 1.00 14.06 C ANISOU 190 C SER A 23 2663 1417 1263 -116 203 -162 C ATOM 191 O SER A 23 15.028 -12.821 4.239 1.00 17.41 O ANISOU 191 O SER A 23 3172 2307 1136 -574 195 -79 O ATOM 192 CB SER A 23 14.593 -14.313 1.599 1.00 19.61 C ANISOU 192 CB SER A 23 4143 1645 1662 -812 -40 -162 C ATOM 193 OG SER A 23 15.869 -14.808 1.334 1.00 27.14 O ANISOU 193 OG SER A 23 5632 1791 2888 462 1030 -436 O ATOM 194 N AASN A 24 16.730 -12.186 2.992 0.62 15.35 N ANISOU 194 N AASN A 24 2523 2056 1253 119 243 -416 N ATOM 195 N BASN A 24 16.630 -12.076 3.045 0.38 11.86 N ANISOU 195 N BASN A 24 2634 725 1149 274 111 19 N ATOM 196 CA AASN A 24 17.632 -11.843 4.059 0.62 13.41 C ANISOU 196 CA AASN A 24 2298 1529 1267 447 111 -92 C ATOM 197 CA BASN A 24 17.633 -11.796 4.013 0.38 13.09 C ANISOU 197 CA BASN A 24 2497 1239 1238 -9 310 -121 C ATOM 198 C AASN A 24 17.544 -10.440 4.648 0.62 13.38 C ANISOU 198 C AASN A 24 2434 1327 1325 61 63 121 C ATOM 199 C BASN A 24 17.569 -10.411 4.649 0.38 11.17 C ANISOU 199 C BASN A 24 1675 1480 1089 227 471 -276 C ATOM 200 O AASN A 24 18.282 -10.142 5.610 0.62 14.02 O ANISOU 200 O AASN A 24 2190 1710 1426 281 108 -178 O ATOM 201 O BASN A 24 18.290 -10.141 5.619 0.38 13.22 O ANISOU 201 O BASN A 24 2116 1593 1315 281 150 -314 O ATOM 202 CB AASN A 24 19.085 -12.090 3.695 0.62 19.79 C ANISOU 202 CB AASN A 24 2326 2985 2208 553 367 -231 C ATOM 203 CB BASN A 24 19.078 -12.032 3.587 0.38 14.88 C ANISOU 203 CB BASN A 24 2584 1156 1916 390 394 -736 C ATOM 204 CG AASN A 24 19.530 -13.504 4.024 0.62 26.26 C ANISOU 204 CG AASN A 24 2531 3933 3513 1664 923 469 C ATOM 205 CG BASN A 24 19.902 -12.558 4.771 0.38 21.42 C ANISOU 205 CG BASN A 24 2896 2417 2826 382 -214 -267 C ATOM 206 OD1AASN A 24 19.893 -14.206 3.138 0.62 37.05 O ANISOU 206 OD1AASN A 24 6768 2869 4440 1232 1642 1 O ATOM 207 OD1BASN A 24 19.308 -13.365 5.524 0.38 36.08 O ANISOU 207 OD1BASN A 24 2992 5955 4763 1959 1385 2857 O ATOM 208 ND2AASN A 24 19.488 -13.783 5.305 0.62 37.69 N ANISOU 208 ND2AASN A 24 6046 4106 4170 2246 2388 1494 N ATOM 209 ND2BASN A 24 21.144 -12.113 4.856 0.38 50.55 N ANISOU 209 ND2BASN A 24 2908 12847 3452 -1825 -319 1352 N ATOM 210 N TYR A 25 16.708 -9.570 4.120 1.00 12.01 N ANISOU 210 N TYR A 25 2031 1378 1155 140 268 -101 N ATOM 211 CA TYR A 25 16.589 -8.193 4.597 1.00 11.24 C ANISOU 211 CA TYR A 25 1802 1310 1160 28 220 -126 C ATOM 212 C TYR A 25 16.420 -8.140 6.103 1.00 10.91 C ANISOU 212 C TYR A 25 1829 1193 1124 -32 159 -24 C ATOM 213 O TYR A 25 17.144 -7.426 6.798 1.00 11.68 O ANISOU 213 O TYR A 25 1784 1449 1205 -103 166 -114 O ATOM 214 CB TYR A 25 15.499 -7.459 3.853 1.00 12.46 C ANISOU 214 CB TYR A 25 2210 1347 1176 38 20 -35 C ATOM 215 CG TYR A 25 15.296 -6.029 4.354 1.00 12.10 C ANISOU 215 CG TYR A 25 1952 1366 1278 48 20 -26 C ATOM 216 CD1 TYR A 25 15.983 -4.977 3.825 1.00 13.01 C ANISOU 216 CD1 TYR A 25 2244 1384 1313 53 343 83 C ATOM 217 CD2 TYR A 25 14.387 -5.723 5.372 1.00 12.46 C ANISOU 217 CD2 TYR A 25 1782 1387 1565 80 254 70 C ATOM 218 CE1 TYR A 25 15.806 -3.682 4.270 1.00 13.71 C ANISOU 218 CE1 TYR A 25 2562 1411 1237 -62 290 31 C ATOM 219 CE2 TYR A 25 14.233 -4.475 5.851 1.00 13.09 C ANISOU 219 CE2 TYR A 25 1803 1484 1685 134 302 30 C ATOM 220 CZ TYR A 25 14.959 -3.422 5.312 1.00 12.68 C ANISOU 220 CZ TYR A 25 2175 1348 1296 33 113 -45 C ATOM 221 OH TYR A 25 14.780 -2.180 5.820 1.00 14.20 O ANISOU 221 OH TYR A 25 2339 1379 1676 191 147 -94 O ATOM 222 N CYS A 26 15.405 -8.824 6.640 1.00 10.83 N ANISOU 222 N CYS A 26 1747 1308 1062 -84 90 -82 N ATOM 223 CA CYS A 26 15.158 -8.728 8.071 1.00 10.65 C ANISOU 223 CA CYS A 26 1654 1283 1110 -46 168 -80 C ATOM 224 C CYS A 26 16.345 -9.259 8.883 1.00 10.64 C ANISOU 224 C CYS A 26 1637 1374 1031 -120 157 -109 C ATOM 225 O CYS A 26 16.720 -8.680 9.881 1.00 11.98 O ANISOU 225 O CYS A 26 1719 1620 1211 -38 60 -178 O ATOM 226 CB CYS A 26 13.870 -9.462 8.448 1.00 11.47 C ANISOU 226 CB CYS A 26 1629 1528 1203 -75 80 24 C ATOM 227 SG CYS A 26 12.362 -8.618 7.895 1.00 11.46 S ANISOU 227 SG CYS A 26 1686 1496 1170 -20 71 -55 S ATOM 228 N ASN A 27 16.897 -10.408 8.479 1.00 11.42 N ANISOU 228 N ASN A 27 1734 1463 1145 67 61 -96 N ATOM 229 CA ASN A 27 18.032 -10.939 9.222 1.00 12.24 C ANISOU 229 CA ASN A 27 1879 1496 1278 93 37 9 C ATOM 230 C ASN A 27 19.156 -9.905 9.353 1.00 12.90 C ANISOU 230 C ASN A 27 1770 1772 1360 25 70 -39 C ATOM 231 O ASN A 27 19.754 -9.737 10.395 1.00 15.05 O ANISOU 231 O ASN A 27 1950 2248 1519 -137 -112 52 O ATOM 232 CB ASN A 27 18.581 -12.207 8.566 1.00 13.48 C ANISOU 232 CB ASN A 27 1893 1600 1628 195 165 49 C ATOM 233 CG ASN A 27 17.630 -13.381 8.755 1.00 14.45 C ANISOU 233 CG ASN A 27 2140 1501 1850 72 336 -7 C ATOM 234 OD1 ASN A 27 16.864 -13.413 9.656 1.00 16.03 O ANISOU 234 OD1 ASN A 27 2516 1770 1804 -107 418 115 O ATOM 235 ND2 ASN A 27 17.735 -14.395 7.885 1.00 21.17 N ANISOU 235 ND2 ASN A 27 3674 1505 2864 -69 1022 -467 N ATOM 236 N GLN A 28 19.445 -9.239 8.236 1.00 12.33 N ANISOU 236 N GLN A 28 1713 1609 1361 53 184 -85 N ATOM 237 CA GLN A 28 20.530 -8.254 8.231 1.00 13.27 C ANISOU 237 CA GLN A 28 1622 1803 1619 20 317 -109 C ATOM 238 C GLN A 28 20.181 -7.005 9.035 1.00 11.79 C ANISOU 238 C GLN A 28 1526 1668 1287 -17 130 30 C ATOM 239 O GLN A 28 21.015 -6.527 9.784 1.00 14.11 O ANISOU 239 O GLN A 28 1581 1991 1787 -42 -33 -234 O ATOM 240 CB AGLN A 28 20.824 -7.871 6.805 0.62 15.33 C ANISOU 240 CB AGLN A 28 1914 2153 1760 -90 674 -115 C ATOM 241 CB BGLN A 28 20.910 -7.873 6.796 0.38 18.17 C ANISOU 241 CB BGLN A 28 3037 1955 1914 -179 1135 -191 C ATOM 242 CG AGLN A 28 21.454 -8.993 6.026 0.62 20.86 C ANISOU 242 CG AGLN A 28 2902 2519 2503 -561 1034 -993 C ATOM 243 CG BGLN A 28 22.002 -6.800 6.805 0.38 23.44 C ANISOU 243 CG BGLN A 28 3442 3972 1492 -1385 914 -243 C ATOM 244 CD AGLN A 28 21.673 -8.704 4.573 0.62 40.64 C ANISOU 244 CD AGLN A 28 9196 3805 2442 1067 1973 -862 C ATOM 245 CD BGLN A 28 23.333 -7.465 6.494 0.38 43.05 C ANISOU 245 CD BGLN A 28 3106 8389 4863 -1054 1352 -2174 C ATOM 246 OE1AGLN A 28 22.372 -9.458 3.875 0.62 61.58 O ANISOU 246 OE1AGLN A 28 13561 6713 3122 3985 3288 -525 O ATOM 247 OE1BGLN A 28 23.406 -8.697 6.426 0.38 59.56 O ANISOU 247 OE1BGLN A 28 3896 8832 9903 1175 2551 -3339 O ATOM 248 NE2AGLN A 28 21.053 -7.689 3.986 0.62 55.52 N ANISOU 248 NE2AGLN A 28 13640 4421 3036 2549 2771 254 N ATOM 249 NE2BGLN A 28 24.381 -6.662 6.358 0.38 57.53 N ANISOU 249 NE2BGLN A 28 3875 12930 5052 -3018 1929 -681 N ATOM 250 N MET A 29 18.973 -6.495 8.857 1.00 11.14 N ANISOU 250 N MET A 29 1473 1428 1330 -130 64 -84 N ATOM 251 CA MET A 29 18.580 -5.248 9.491 1.00 11.41 C ANISOU 251 CA MET A 29 1582 1452 1302 -114 63 -69 C ATOM 252 C MET A 29 18.356 -5.374 10.984 1.00 10.89 C ANISOU 252 C MET A 29 1504 1268 1365 -30 74 7 C ATOM 253 O MET A 29 18.687 -4.494 11.750 1.00 12.40 O ANISOU 253 O MET A 29 1840 1407 1464 -184 -16 -135 O ATOM 254 CB MET A 29 17.356 -4.669 8.813 1.00 12.50 C ANISOU 254 CB MET A 29 1775 1490 1485 11 -87 -29 C ATOM 255 CG MET A 29 17.596 -4.198 7.442 1.00 16.32 C ANISOU 255 CG MET A 29 2905 1833 1465 25 -122 29 C ATOM 256 SD MET A 29 18.670 -2.775 7.332 1.00 22.53 S ANISOU 256 SD MET A 29 3887 2395 2278 -702 -37 811 S ATOM 257 CE MET A 29 17.672 -1.545 8.177 1.00 33.09 C ANISOU 257 CE MET A 29 8524 2012 2037 -769 786 -460 C ATOM 258 N MET A 30 17.767 -6.499 11.405 1.00 10.87 N ANISOU 258 N MET A 30 1594 1343 1192 -92 104 -23 N ATOM 259 CA MET A 30 17.537 -6.690 12.815 1.00 11.26 C ANISOU 259 CA MET A 30 1765 1357 1157 -16 15 -3 C ATOM 260 C MET A 30 18.861 -6.711 13.545 1.00 11.77 C ANISOU 260 C MET A 30 1765 1436 1270 -33 -9 47 C ATOM 261 O MET A 30 19.006 -6.210 14.661 1.00 14.59 O ANISOU 261 O MET A 30 2033 2077 1435 -34 -187 -263 O ATOM 262 CB MET A 30 16.729 -7.961 13.064 1.00 11.38 C ANISOU 262 CB MET A 30 1670 1367 1287 14 93 45 C ATOM 263 CG MET A 30 15.305 -7.940 12.550 1.00 11.81 C ANISOU 263 CG MET A 30 1707 1501 1280 0 103 -28 C ATOM 264 SD MET A 30 14.239 -6.708 13.331 1.00 13.11 S ANISOU 264 SD MET A 30 1808 1691 1484 177 252 118 S ATOM 265 CE MET A 30 13.927 -7.511 14.908 1.00 15.39 C ANISOU 265 CE MET A 30 2399 2082 1364 325 557 166 C ATOM 266 N LYS A 31 19.867 -7.336 12.953 1.00 12.41 N ANISOU 266 N LYS A 31 1670 1600 1446 -5 -78 93 N ATOM 267 CA LYS A 31 21.205 -7.397 13.536 1.00 14.03 C ANISOU 267 CA LYS A 31 1898 1652 1779 164 -286 141 C ATOM 268 C LYS A 31 21.895 -6.049 13.511 1.00 13.64 C ANISOU 268 C LYS A 31 1607 1793 1781 65 -171 97 C ATOM 269 O LYS A 31 22.409 -5.565 14.517 1.00 15.23 O ANISOU 269 O LYS A 31 1849 2194 1745 -56 -295 -6 O ATOM 270 CB LYS A 31 22.040 -8.431 12.821 0.84 15.29 C ANISOU 270 CB LYS A 31 1711 1968 2131 240 -320 -73 C ATOM 271 CG LYS A 31 23.417 -8.623 13.422 1.00 21.95 C ATOM 272 CD LYS A 31 24.131 -9.695 12.665 1.00 34.45 C ATOM 273 CE LYS A 31 24.132 -11.036 13.396 1.00 88.69 C ATOM 274 NZ LYS A 31 24.739 -12.102 12.528 1.00115.66 N ATOM 275 N SER A 32 21.870 -5.388 12.347 1.00 13.54 N ANISOU 275 N SER A 32 1669 1855 1621 -112 23 13 N ATOM 276 CA SER A 32 22.620 -4.117 12.194 1.00 14.86 C ANISOU 276 CA SER A 32 1584 2099 1961 -235 165 78 C ATOM 277 C SER A 32 22.074 -2.972 13.024 1.00 14.20 C ANISOU 277 C SER A 32 1682 1817 1896 -268 -88 143 C ATOM 278 O SER A 32 22.811 -2.092 13.431 1.00 17.98 O ANISOU 278 O SER A 32 1992 2240 2601 -675 36 -199 O ATOM 279 CB ASER A 32 22.583 -3.709 10.711 0.38 20.04 C ANISOU 279 CB ASER A 32 3286 2280 2048 -323 695 232 C ATOM 280 CB BSER A 32 22.833 -3.795 10.736 0.40 16.63 C ANISOU 280 CB BSER A 32 1638 2693 1988 -723 267 56 C ATOM 281 CB CSER A 32 22.577 -3.713 10.711 0.23 19.81 C ANISOU 281 CB CSER A 32 3366 2091 2071 -2 688 281 C ATOM 282 OG ASER A 32 23.455 -4.553 9.971 0.38 22.83 O ANISOU 282 OG ASER A 32 3151 3213 2309 -349 1068 14 O ATOM 283 OG BSER A 32 21.623 -3.337 10.194 0.40 16.69 O ANISOU 283 OG BSER A 32 1892 2674 1776 -659 168 326 O ATOM 284 OG CSER A 32 23.492 -2.655 10.487 0.23 32.78 O ANISOU 284 OG CSER A 32 8242 2245 1967 -2261 296 55 O ATOM 285 N ARG A 33 20.759 -2.976 13.281 1.00 12.74 N ANISOU 285 N ARG A 33 1625 1717 1498 -220 -126 54 N ATOM 286 CA ARG A 33 20.133 -1.946 14.093 1.00 12.78 C ANISOU 286 CA ARG A 33 1883 1577 1394 -178 -191 73 C ATOM 287 C ARG A 33 20.184 -2.301 15.594 1.00 13.50 C ANISOU 287 C ARG A 33 2219 1536 1374 -144 -254 20 C ATOM 288 O ARG A 33 19.578 -1.590 16.397 1.00 16.63 O ANISOU 288 O ARG A 33 3112 1689 1515 113 -280 -218 O ATOM 289 CB ARG A 33 18.700 -1.703 13.647 1.00 12.54 C ANISOU 289 CB ARG A 33 1841 1430 1496 -153 -80 92 C ATOM 290 CG ARG A 33 18.626 -1.151 12.215 1.00 12.40 C ANISOU 290 CG ARG A 33 1582 1665 1465 25 -71 67 C ATOM 291 CD ARG A 33 19.242 0.238 12.116 1.00 12.16 C ANISOU 291 CD ARG A 33 1392 1679 1548 6 37 290 C ATOM 292 NE ARG A 33 19.110 0.800 10.767 1.00 13.00 N ANISOU 292 NE ARG A 33 1557 1949 1434 184 197 270 N ATOM 293 CZ ARG A 33 18.030 1.437 10.333 1.00 11.66 C ANISOU 293 CZ ARG A 33 1497 1729 1204 94 161 93 C ATOM 294 NH1 ARG A 33 16.994 1.649 11.135 1.00 12.49 N ANISOU 294 NH1 ARG A 33 1573 1864 1308 278 238 202 N ATOM 295 NH2 ARG A 33 18.001 1.888 9.101 1.00 14.17 N ANISOU 295 NH2 ARG A 33 1877 2244 1262 313 324 337 N ATOM 296 N ASN A 34 20.874 -3.357 15.957 1.00 13.42 N ANISOU 296 N ASN A 34 2137 1497 1465 -203 -281 131 N ATOM 297 CA ASN A 34 21.089 -3.713 17.363 1.00 15.03 C ANISOU 297 CA ASN A 34 2387 1862 1463 -465 -459 177 C ATOM 298 C ASN A 34 19.820 -4.166 18.017 1.00 15.03 C ANISOU 298 C ASN A 34 2331 2065 1316 -193 -257 40 C ATOM 299 O ASN A 34 19.699 -4.035 19.237 1.00 21.16 O ANISOU 299 O ASN A 34 2920 3647 1474 -483 -162 -379 O ATOM 300 CB AASN A 34 21.905 -2.692 18.147 0.54 19.53 C ANISOU 300 CB AASN A 34 2413 2922 2086 -510 -788 -359 C ATOM 301 CB BASN A 34 21.741 -2.539 18.106 0.46 18.27 C ANISOU 301 CB BASN A 34 3298 1827 1818 -559 -874 239 C ATOM 302 CG AASN A 34 23.286 -2.459 17.583 0.54 20.23 C ANISOU 302 CG AASN A 34 2312 2720 2653 -494 -724 -342 C ATOM 303 CG BASN A 34 22.720 -2.987 19.179 0.46 15.45 C ANISOU 303 CG BASN A 34 2119 2229 1523 -1164 -305 549 C ATOM 304 OD1AASN A 34 23.743 -1.289 17.613 0.54 25.69 O ANISOU 304 OD1AASN A 34 3200 2965 3596 -917 -566 265 O ATOM 305 OD1BASN A 34 23.205 -4.091 19.103 0.46 18.11 O ANISOU 305 OD1BASN A 34 2590 2314 1978 -854 -927 670 O ATOM 306 ND2AASN A 34 24.039 -3.492 17.216 0.54 29.75 N ANISOU 306 ND2AASN A 34 2606 3630 5067 26 -606 -1079 N ATOM 307 ND2BASN A 34 22.900 -2.073 20.117 0.46 20.22 N ANISOU 307 ND2BASN A 34 3055 2872 1756 -1095 -517 140 N ATOM 308 N LEU A 35 18.907 -4.760 17.274 1.00 13.24 N ANISOU 308 N LEU A 35 1922 1820 1290 -32 -171 56 N ATOM 309 CA LEU A 35 17.620 -5.213 17.822 1.00 15.57 C ANISOU 309 CA LEU A 35 1922 2524 1469 31 -116 258 C ATOM 310 C LEU A 35 17.666 -6.640 18.328 1.00 17.30 C ANISOU 310 C LEU A 35 1689 2964 1921 -302 -188 930 C ATOM 311 O LEU A 35 16.722 -7.183 18.844 1.00 26.02 O ANISOU 311 O LEU A 35 1890 4322 3676 -113 419 2088 O ATOM 312 CB LEU A 35 16.492 -5.063 16.801 1.00 14.52 C ANISOU 312 CB LEU A 35 1824 2049 1646 75 -131 51 C ATOM 313 CG LEU A 35 16.389 -3.630 16.268 1.00 17.92 C ANISOU 313 CG LEU A 35 2863 1942 2003 484 -679 -213 C ATOM 314 CD1 LEU A 35 15.374 -3.529 15.177 1.00 20.83 C ANISOU 314 CD1 LEU A 35 3355 2039 2521 721 -1177 -315 C ATOM 315 CD2 LEU A 35 16.150 -2.619 17.320 1.00 23.54 C ANISOU 315 CD2 LEU A 35 3736 2480 2729 688 -970 -838 C ATOM 316 N THR A 36 18.794 -7.298 18.137 1.00 14.93 N ANISOU 316 N THR A 36 1866 2158 1647 -392 -163 638 N ATOM 317 CA THR A 36 18.988 -8.668 18.599 1.00 17.83 C ANISOU 317 CA THR A 36 2403 2187 2184 -809 -677 1056 C ATOM 318 C THR A 36 20.103 -8.801 19.607 1.00 18.45 C ANISOU 318 C THR A 36 2207 2683 2119 -817 -589 1120 C ATOM 319 O THR A 36 20.555 -9.906 19.905 1.00 21.48 O ANISOU 319 O THR A 36 2823 2948 2391 -268 -714 1127 O ATOM 320 CB THR A 36 19.227 -9.591 17.404 1.00 19.89 C ANISOU 320 CB THR A 36 3222 1649 2686 -766 -1150 809 C ATOM 321 OG1 THR A 36 20.443 -9.253 16.781 1.00 22.20 O ANISOU 321 OG1 THR A 36 3682 2219 2534 -350 -464 262 O ATOM 322 CG2 THR A 36 18.107 -9.589 16.405 1.00 24.58 C ANISOU 322 CG2 THR A 36 4167 1888 3282 -367 -1921 500 C ATOM 323 N LYS A 37 20.533 -7.674 20.182 1.00 20.89 N ANISOU 323 N LYS A 37 2605 2889 2444 -1084 -990 1186 N ATOM 324 CA LYS A 37 21.727 -7.745 21.044 1.00 23.98 C ANISOU 324 CA LYS A 37 3070 3459 2583 -1492 -1284 1465 C ATOM 325 C LYS A 37 21.491 -8.548 22.285 1.00 19.45 C ANISOU 325 C LYS A 37 2433 2450 2507 -577 -749 1025 C ATOM 326 O LYS A 37 22.369 -9.367 22.692 1.00 21.86 O ANISOU 326 O LYS A 37 2798 2819 2690 -102 -739 777 O ATOM 327 CB LYS A 37 22.156 -6.290 21.379 1.00 33.38 C ANISOU 327 CB LYS A 37 4884 3789 4010 -2755 -2424 2074 C ATOM 328 CG LYS A 37 23.286 -6.203 22.365 1.00 38.11 C ANISOU 328 CG LYS A 37 5301 4034 5146 -2736 -3149 2204 C ATOM 329 CD LYS A 37 23.555 -4.756 22.791 1.00 49.75 C ANISOU 329 CD LYS A 37 9048 5055 4800 -4415 -3219 1565 C ATOM 330 CE LYS A 37 24.577 -4.541 23.907 1.00 74.94 C ANISOU 330 CE LYS A 37 12137 9570 6767 -4692 -5609 -37 C ATOM 331 NZ LYS A 37 23.988 -4.291 25.256 1.00 93.52 N ANISOU 331 NZ LYS A 37 15897 13547 6088 -4681 -5774 -615 N ATOM 332 N ASP A 38 20.390 -8.293 22.976 1.00 18.09 N ANISOU 332 N ASP A 38 2653 1744 2477 -644 -714 264 N ATOM 333 CA ASP A 38 20.136 -8.942 24.275 1.00 16.62 C ANISOU 333 CA ASP A 38 2427 1840 2049 -261 -636 -79 C ATOM 334 C ASP A 38 19.196 -10.131 24.206 1.00 13.19 C ANISOU 334 C ASP A 38 2016 1656 1339 0 -260 -50 C ATOM 335 O ASP A 38 19.228 -11.017 25.055 1.00 15.06 O ANISOU 335 O ASP A 38 2198 2055 1469 43 -389 226 O ATOM 336 CB ASP A 38 19.570 -7.907 25.252 1.00 24.45 C ANISOU 336 CB ASP A 38 3986 2350 2953 -93 -634 -963 C ATOM 337 CG ASP A 38 20.538 -6.791 25.603 1.00 37.14 C ANISOU 337 CG ASP A 38 4985 2892 6233 -238 -1910 -1969 C ATOM 338 OD1 ASP A 38 20.108 -5.630 25.577 1.00 45.20 O ANISOU 338 OD1 ASP A 38 6009 2620 8545 -471 -505 -1717 O ATOM 339 OD2 ASP A 38 21.716 -7.115 25.822 1.00 47.48 O ANISOU 339 OD2 ASP A 38 4845 4508 8688 -520 -2480 -2320 O ATOM 340 N ARG A 39 18.359 -10.168 23.201 1.00 13.34 N ANISOU 340 N ARG A 39 2129 1364 1578 -202 -421 307 N ATOM 341 CA ARG A 39 17.364 -11.184 22.944 1.00 12.72 C ANISOU 341 CA ARG A 39 2096 1384 1351 -200 -212 224 C ATOM 342 C ARG A 39 16.911 -11.000 21.505 1.00 12.19 C ANISOU 342 C ARG A 39 1907 1381 1343 -22 -181 181 C ATOM 343 O ARG A 39 17.070 -9.933 20.930 1.00 15.18 O ANISOU 343 O ARG A 39 2655 1569 1541 -365 -454 435 O ATOM 344 CB ARG A 39 16.207 -11.126 23.932 1.00 14.61 C ANISOU 344 CB ARG A 39 2297 1916 1339 -160 -153 268 C ATOM 345 CG ARG A 39 15.417 -9.825 23.945 1.00 20.05 C ANISOU 345 CG ARG A 39 2718 2310 2589 360 269 264 C ATOM 346 CD ARG A 39 14.306 -9.731 24.936 1.00 34.65 C ANISOU 346 CD ARG A 39 5248 4656 3263 2031 1857 911 C ATOM 347 NE ARG A 39 13.532 -8.553 24.713 1.00 51.99 N ANISOU 347 NE ARG A 39 5375 5671 8708 3286 1268 -321 N ATOM 348 CZ ARG A 39 12.380 -8.442 24.064 1.00 60.29 C ANISOU 348 CZ ARG A 39 4963 6430 11513 2801 941 1488 C ATOM 349 NH1 ARG A 39 11.791 -9.474 23.470 1.00 61.67 N ANISOU 349 NH1 ARG A 39 9268 11153 3010 3952 -168 -2072 N ATOM 350 NH2 ARG A 39 11.872 -7.219 24.024 1.00 86.76 N ANISOU 350 NH2 ARG A 39 9016 8084 15864 5367 -18 2986 N ATOM 351 N CYS A 40 16.273 -12.036 20.962 1.00 12.33 N ANISOU 351 N CYS A 40 1907 1399 1378 -14 -137 145 N ATOM 352 CA CYS A 40 15.656 -11.893 19.652 1.00 13.18 C ANISOU 352 CA CYS A 40 1848 1784 1378 -10 -211 10 C ATOM 353 C CYS A 40 14.325 -11.165 19.804 1.00 14.49 C ANISOU 353 C CYS A 40 1985 2227 1295 284 -184 89 C ATOM 354 O CYS A 40 13.365 -11.667 20.368 1.00 19.64 O ANISOU 354 O CYS A 40 2174 2454 2834 272 264 437 O ATOM 355 CB CYS A 40 15.364 -13.239 19.007 1.00 14.62 C ANISOU 355 CB CYS A 40 1991 1914 1650 -40 -218 -151 C ATOM 356 SG CYS A 40 16.816 -14.318 18.820 1.00 13.90 S ANISOU 356 SG CYS A 40 2147 1667 1466 -67 -127 -9 S ATOM 357 N LYS A 41 14.214 -9.958 19.250 1.00 15.82 N ANISOU 357 N LYS A 41 2291 2317 1401 421 15 147 N ATOM 358 CA LYS A 41 12.944 -9.238 19.256 1.00 16.17 C ANISOU 358 CA LYS A 41 2405 2607 1134 727 140 100 C ATOM 359 C LYS A 41 12.013 -10.027 18.362 1.00 16.04 C ANISOU 359 C LYS A 41 2237 2720 1136 841 113 84 C ATOM 360 O LYS A 41 12.394 -10.346 17.229 1.00 17.57 O ANISOU 360 O LYS A 41 2401 3140 1136 829 216 -29 O ATOM 361 CB ALYS A 41 13.108 -7.779 18.779 0.46 20.62 C ANISOU 361 CB ALYS A 41 3042 2482 2312 816 307 67 C ATOM 362 CB BLYS A 41 13.199 -7.810 18.709 0.54 18.10 C ANISOU 362 CB BLYS A 41 2756 2594 1528 783 312 150 C ATOM 363 CG ALYS A 41 11.907 -6.884 19.005 0.46 26.51 C ANISOU 363 CG ALYS A 41 2718 2658 4698 846 -255 74 C ATOM 364 CG BLYS A 41 12.019 -6.874 18.691 0.54 15.78 C ANISOU 364 CG BLYS A 41 1879 1961 2156 -40 61 -118 C ATOM 365 CD ALYS A 41 11.975 -5.497 18.384 0.46 24.54 C ANISOU 365 CD ALYS A 41 3057 2423 3843 747 -111 -361 C ATOM 366 CD BLYS A 41 12.323 -5.437 18.357 0.54 19.82 C ANISOU 366 CD BLYS A 41 3450 1943 2137 58 957 -19 C ATOM 367 CE ALYS A 41 10.757 -4.669 18.777 0.46 33.53 C ANISOU 367 CE ALYS A 41 3630 3547 5564 1822 470 843 C ATOM 368 CE BLYS A 41 11.140 -4.517 18.504 0.54 20.77 C ANISOU 368 CE BLYS A 41 3955 2153 1785 554 304 -269 C ATOM 369 NZ ALYS A 41 10.481 -3.535 17.852 0.46 33.22 N ANISOU 369 NZ ALYS A 41 4890 5997 1734 3504 424 315 N ATOM 370 NZ BLYS A 41 10.056 -4.610 17.503 0.54 26.10 N ANISOU 370 NZ BLYS A 41 4053 2657 3205 -34 -397 -644 N ATOM 371 N PRO A 42 10.788 -10.363 18.763 1.00 15.39 N ANISOU 371 N PRO A 42 2511 2250 1086 596 264 166 N ATOM 372 CA PRO A 42 9.985 -11.317 17.997 1.00 16.20 C ANISOU 372 CA PRO A 42 2902 1876 1376 547 187 210 C ATOM 373 C PRO A 42 9.414 -10.796 16.680 1.00 13.46 C ANISOU 373 C PRO A 42 2214 1606 1294 243 339 143 C ATOM 374 O PRO A 42 9.212 -11.569 15.756 1.00 16.39 O ANISOU 374 O PRO A 42 3029 1716 1482 190 136 -20 O ATOM 375 CB PRO A 42 8.838 -11.737 18.930 1.00 20.55 C ANISOU 375 CB PRO A 42 3742 2553 1512 -329 189 712 C ATOM 376 CG PRO A 42 8.845 -10.689 19.986 1.00 28.65 C ANISOU 376 CG PRO A 42 3988 4925 1972 -1442 1328 -721 C ATOM 377 CD PRO A 42 10.236 -10.174 20.119 1.00 19.17 C ANISOU 377 CD PRO A 42 3166 2918 1199 137 561 0 C ATOM 378 N VAL A 43 9.073 -9.551 16.642 1.00 12.23 N ANISOU 378 N VAL A 43 1956 1520 1171 -17 274 191 N ATOM 379 CA VAL A 43 8.449 -8.898 15.496 1.00 12.22 C ANISOU 379 CA VAL A 43 1742 1552 1349 -123 179 292 C ATOM 380 C VAL A 43 9.001 -7.506 15.391 1.00 11.74 C ANISOU 380 C VAL A 43 1745 1515 1200 -42 78 190 C ATOM 381 O VAL A 43 9.306 -6.869 16.392 1.00 15.19 O ANISOU 381 O VAL A 43 2795 1780 1196 -441 -81 196 O ATOM 382 CB AVAL A 43 6.912 -8.853 15.584 0.59 15.85 C ANISOU 382 CB AVAL A 43 1768 1766 2488 -148 14 498 C ATOM 383 CB BVAL A 43 6.910 -8.800 15.726 0.41 16.76 C ANISOU 383 CB BVAL A 43 1709 2448 2211 -245 88 722 C ATOM 384 CG1AVAL A 43 6.251 -10.202 15.705 0.59 20.03 C ANISOU 384 CG1AVAL A 43 2039 2155 3418 -602 245 502 C ATOM 385 CG1BVAL A 43 6.590 -7.832 16.843 0.41 29.00 C ANISOU 385 CG1BVAL A 43 3379 5776 1864 1711 966 269 C ATOM 386 CG2AVAL A 43 6.434 -7.997 16.725 0.59 21.26 C ANISOU 386 CG2AVAL A 43 1537 2809 3732 30 557 -346 C ATOM 387 CG2BVAL A 43 6.206 -8.339 14.454 0.41 22.04 C ANISOU 387 CG2BVAL A 43 1605 4384 2384 -587 -395 755 C ATOM 388 N ASN A 44 9.067 -6.981 14.188 1.00 11.19 N ANISOU 388 N ASN A 44 1670 1391 1190 -117 128 96 N ATOM 389 CA ASN A 44 9.413 -5.592 13.968 1.00 10.51 C ANISOU 389 CA ASN A 44 1569 1285 1140 -11 177 15 C ATOM 390 C ASN A 44 8.907 -5.173 12.597 1.00 11.40 C ANISOU 390 C ASN A 44 1878 1394 1058 -74 206 25 C ATOM 391 O ASN A 44 8.760 -6.009 11.722 1.00 16.17 O ANISOU 391 O ASN A 44 3584 1409 1151 234 -58 -129 O ATOM 392 CB ASN A 44 10.919 -5.386 14.082 1.00 11.99 C ANISOU 392 CB ASN A 44 1538 1447 1570 -119 178 38 C ATOM 393 CG ASN A 44 11.309 -3.944 14.204 1.00 11.89 C ANISOU 393 CG ASN A 44 1723 1489 1307 -114 194 -125 C ATOM 394 OD1 ASN A 44 10.748 -3.248 15.021 1.00 19.42 O ANISOU 394 OD1 ASN A 44 2983 1785 2610 -372 1245 -519 O ATOM 395 ND2 ASN A 44 12.185 -3.453 13.400 1.00 13.38 N ANISOU 395 ND2 ASN A 44 1727 1614 1742 -372 321 -140 N ATOM 396 N THR A 45 8.729 -3.883 12.412 1.00 10.40 N ANISOU 396 N THR A 45 1606 1355 992 -85 97 21 N ATOM 397 CA THR A 45 8.358 -3.302 11.115 1.00 10.15 C ANISOU 397 CA THR A 45 1444 1423 990 -99 85 29 C ATOM 398 C THR A 45 9.347 -2.188 10.768 1.00 9.85 C ANISOU 398 C THR A 45 1499 1261 983 -24 -17 23 C ATOM 399 O THR A 45 9.649 -1.335 11.611 1.00 12.09 O ANISOU 399 O THR A 45 2058 1456 1080 -245 129 -136 O ATOM 400 CB THR A 45 6.932 -2.718 11.178 1.00 11.91 C ANISOU 400 CB THR A 45 1483 1694 1350 -55 16 23 C ATOM 401 OG1 THR A 45 6.043 -3.750 11.588 1.00 15.79 O ANISOU 401 OG1 THR A 45 1472 2415 2111 -306 207 233 O ATOM 402 CG2 THR A 45 6.520 -2.138 9.857 1.00 14.57 C ANISOU 402 CG2 THR A 45 1677 2319 1541 195 -162 140 C ATOM 403 N PHE A 46 9.784 -2.183 9.527 1.00 9.71 N ANISOU 403 N PHE A 46 1464 1216 1010 -100 77 -7 N ATOM 404 CA PHE A 46 10.585 -1.104 8.961 1.00 10.24 C ANISOU 404 CA PHE A 46 1502 1370 1017 -67 -32 105 C ATOM 405 C PHE A 46 9.758 -0.339 7.949 1.00 10.25 C ANISOU 405 C PHE A 46 1605 1346 944 -42 32 86 C ATOM 406 O PHE A 46 8.952 -0.928 7.224 1.00 12.09 O ANISOU 406 O PHE A 46 1969 1316 1309 -69 -451 -41 O ATOM 407 CB PHE A 46 11.845 -1.659 8.281 1.00 11.27 C ANISOU 407 CB PHE A 46 1520 1561 1201 -8 161 154 C ATOM 408 CG PHE A 46 12.849 -2.221 9.269 1.00 10.55 C ANISOU 408 CG PHE A 46 1369 1566 1073 -81 157 -4 C ATOM 409 CD1 PHE A 46 13.711 -1.385 9.964 1.00 12.76 C ANISOU 409 CD1 PHE A 46 1511 1681 1657 -129 24 -52 C ATOM 410 CD2 PHE A 46 12.920 -3.582 9.501 1.00 11.51 C ANISOU 410 CD2 PHE A 46 1606 1555 1212 20 55 18 C ATOM 411 CE1 PHE A 46 14.616 -1.922 10.869 1.00 14.43 C ANISOU 411 CE1 PHE A 46 1488 2335 1659 -8 -132 -190 C ATOM 412 CE2 PHE A 46 13.830 -4.097 10.389 1.00 13.93 C ANISOU 412 CE2 PHE A 46 1735 1981 1576 351 70 15 C ATOM 413 CZ PHE A 46 14.676 -3.283 11.050 1.00 14.17 C ANISOU 413 CZ PHE A 46 1599 2455 1329 330 -62 63 C ATOM 414 N VAL A 47 9.957 0.976 7.897 1.00 10.51 N ANISOU 414 N VAL A 47 1591 1292 1111 -161 -94 117 N ATOM 415 CA VAL A 47 9.208 1.885 7.047 1.00 9.94 C ANISOU 415 CA VAL A 47 1557 1293 929 -72 21 37 C ATOM 416 C VAL A 47 10.164 2.483 6.037 1.00 10.02 C ANISOU 416 C VAL A 47 1488 1263 1056 -44 15 3 C ATOM 417 O VAL A 47 11.171 3.097 6.393 1.00 11.47 O ANISOU 417 O VAL A 47 1539 1647 1172 -197 -21 9 O ATOM 418 CB VAL A 47 8.519 2.973 7.856 1.00 11.36 C ANISOU 418 CB VAL A 47 1713 1474 1131 25 169 -59 C ATOM 419 CG1 VAL A 47 7.703 3.838 6.946 1.00 14.08 C ANISOU 419 CG1 VAL A 47 2016 1684 1651 354 203 8 C ATOM 420 CG2 VAL A 47 7.683 2.377 8.997 1.00 15.06 C ANISOU 420 CG2 VAL A 47 2053 2251 1419 -161 452 -57 C ATOM 421 N HIS A 48 9.829 2.330 4.755 1.00 10.27 N ANISOU 421 N HIS A 48 1479 1425 996 -64 -23 53 N ATOM 422 CA HIS A 48 10.689 2.757 3.644 1.00 10.85 C ANISOU 422 CA HIS A 48 1623 1468 1032 -112 72 52 C ATOM 423 C HIS A 48 10.172 4.055 3.069 1.00 11.66 C ANISOU 423 C HIS A 48 1941 1451 1037 -169 195 20 C ATOM 424 O HIS A 48 9.723 4.139 1.935 1.00 15.37 O ANISOU 424 O HIS A 48 3001 1741 1099 188 -144 46 O ATOM 425 CB HIS A 48 10.672 1.653 2.565 1.00 11.41 C ANISOU 425 CB HIS A 48 1770 1493 1071 65 132 18 C ATOM 426 CG HIS A 48 11.110 0.344 3.068 1.00 11.41 C ANISOU 426 CG HIS A 48 1591 1495 1250 63 175 103 C ATOM 427 ND1 HIS A 48 12.386 0.039 3.349 1.00 20.23 N ANISOU 427 ND1 HIS A 48 1766 2067 3855 -192 -311 1361 N ATOM 428 CD2 HIS A 48 10.450 -0.787 3.337 1.00 12.28 C ANISOU 428 CD2 HIS A 48 1785 1460 1422 -3 285 -67 C ATOM 429 CE1 HIS A 48 12.438 -1.213 3.758 1.00 20.90 C ANISOU 429 CE1 HIS A 48 2012 2079 3850 -53 -415 1325 C ATOM 430 NE2 HIS A 48 11.283 -1.764 3.822 1.00 13.61 N ANISOU 430 NE2 HIS A 48 2017 1553 1601 40 200 223 N ATOM 431 N GLU A 49 10.200 5.095 3.858 1.00 12.63 N ANISOU 431 N GLU A 49 2329 1328 1140 -135 95 63 N ATOM 432 CA GLU A 49 9.739 6.427 3.528 1.00 12.23 C ANISOU 432 CA GLU A 49 2077 1416 1154 -26 144 53 C ATOM 433 C GLU A 49 10.716 7.425 4.123 1.00 12.38 C ANISOU 433 C GLU A 49 2046 1419 1241 -30 240 30 C ATOM 434 O GLU A 49 11.535 7.097 4.971 1.00 14.01 O ANISOU 434 O GLU A 49 2270 1561 1491 -122 -101 77 O ATOM 435 CB GLU A 49 8.352 6.642 4.074 1.00 13.62 C ANISOU 435 CB GLU A 49 2144 1547 1484 -126 260 -29 C ATOM 436 CG GLU A 49 7.282 5.653 3.574 1.00 14.60 C ANISOU 436 CG GLU A 49 2117 1756 1673 -97 102 38 C ATOM 437 CD GLU A 49 6.901 5.772 2.110 1.00 15.64 C ANISOU 437 CD GLU A 49 2377 1780 1786 -222 -190 136 C ATOM 438 OE1 GLU A 49 7.227 6.791 1.468 1.00 21.01 O ANISOU 438 OE1 GLU A 49 3585 2017 2382 -532 -974 684 O ATOM 439 OE2 GLU A 49 6.230 4.835 1.639 1.00 17.09 O ANISOU 439 OE2 GLU A 49 2350 2037 2105 -311 -461 198 O ATOM 440 N SER A 50 10.611 8.689 3.667 1.00 12.66 N ANISOU 440 N SER A 50 2035 1407 1369 -37 157 43 N ATOM 441 CA SER A 50 11.406 9.735 4.283 1.00 12.91 C ANISOU 441 CA SER A 50 1840 1445 1622 -240 367 -55 C ATOM 442 C SER A 50 10.992 9.899 5.757 1.00 12.67 C ANISOU 442 C SER A 50 1796 1419 1597 -270 317 3 C ATOM 443 O SER A 50 9.827 9.742 6.150 1.00 13.52 O ANISOU 443 O SER A 50 1824 1657 1656 -276 326 -149 O ATOM 444 CB SER A 50 11.212 11.034 3.593 1.00 15.55 C ANISOU 444 CB SER A 50 2593 1639 1675 -211 674 139 C ATOM 445 OG SER A 50 9.980 11.603 3.844 1.00 19.57 O ANISOU 445 OG SER A 50 3014 2112 2310 455 624 481 O ATOM 446 N LEU A 51 11.947 10.325 6.546 1.00 13.34 N ANISOU 446 N LEU A 51 1714 1775 1579 -112 388 -66 N ATOM 447 CA LEU A 51 11.682 10.616 7.948 1.00 13.68 C ANISOU 447 CA LEU A 51 1841 1799 1557 -130 332 -29 C ATOM 448 C LEU A 51 10.641 11.706 8.069 1.00 13.11 C ANISOU 448 C LEU A 51 1949 1552 1482 -221 275 -210 C ATOM 449 O LEU A 51 9.746 11.612 8.917 1.00 13.91 O ANISOU 449 O LEU A 51 1945 1940 1399 -171 329 -36 O ATOM 450 CB LEU A 51 12.971 11.009 8.677 1.00 16.67 C ANISOU 450 CB LEU A 51 2127 2277 1930 -191 89 -190 C ATOM 451 CG LEU A 51 12.814 11.273 10.133 1.00 16.81 C ANISOU 451 CG LEU A 51 2560 1913 1914 -25 -95 -282 C ATOM 452 CD1 LEU A 51 12.294 10.054 10.886 1.00 21.13 C ANISOU 452 CD1 LEU A 51 4117 2027 1886 -17 189 -55 C ATOM 453 CD2 LEU A 51 14.152 11.691 10.742 1.00 24.92 C ANISOU 453 CD2 LEU A 51 3052 3456 2959 -234 -732 -813 C ATOM 454 N ALA A 52 10.704 12.738 7.230 1.00 13.82 N ANISOU 454 N ALA A 52 2017 1476 1758 -272 488 -57 N ATOM 455 CA ALA A 52 9.733 13.835 7.322 1.00 15.30 C ANISOU 455 CA ALA A 52 2350 1411 2051 -232 521 -5 C ATOM 456 C ALA A 52 8.327 13.344 7.092 1.00 14.07 C ANISOU 456 C ALA A 52 2230 1356 1760 37 433 108 C ATOM 457 O ALA A 52 7.378 13.808 7.747 1.00 15.75 O ANISOU 457 O ALA A 52 2354 1613 2019 32 568 -122 O ATOM 458 CB ALA A 52 10.094 14.915 6.319 1.00 19.75 C ANISOU 458 CB ALA A 52 2811 1599 3094 -181 841 478 C ATOM 459 N ASP A 53 8.139 12.407 6.155 1.00 13.68 N ANISOU 459 N ASP A 53 2084 1548 1566 24 412 86 N ATOM 460 CA ASP A 53 6.809 11.900 5.892 1.00 13.94 C ANISOU 460 CA ASP A 53 2140 1685 1470 43 262 185 C ATOM 461 C ASP A 53 6.246 11.074 7.047 1.00 12.84 C ANISOU 461 C ASP A 53 1773 1716 1390 127 214 103 C ATOM 462 O ASP A 53 5.034 11.096 7.285 1.00 14.92 O ANISOU 462 O ASP A 53 1800 2001 1867 148 83 467 O ATOM 463 CB ASP A 53 6.728 11.093 4.596 1.00 14.61 C ANISOU 463 CB ASP A 53 2095 2021 1434 96 171 184 C ATOM 464 CG ASP A 53 6.804 11.908 3.335 1.00 18.11 C ANISOU 464 CG ASP A 53 2892 2471 1519 680 254 386 C ATOM 465 OD1 ASP A 53 6.594 13.103 3.366 1.00 23.39 O ANISOU 465 OD1 ASP A 53 4506 2414 1965 785 497 679 O ATOM 466 OD2 ASP A 53 7.078 11.331 2.293 1.00 24.42 O ANISOU 466 OD2 ASP A 53 4696 3004 1578 1136 589 384 O ATOM 467 N VAL A 54 7.101 10.366 7.759 1.00 11.79 N ANISOU 467 N VAL A 54 1693 1451 1337 67 252 99 N ATOM 468 CA VAL A 54 6.665 9.623 8.912 1.00 11.35 C ANISOU 468 CA VAL A 54 1614 1429 1270 -131 125 0 C ATOM 469 C VAL A 54 6.411 10.545 10.082 1.00 11.90 C ANISOU 469 C VAL A 54 1706 1413 1403 -64 288 -1 C ATOM 470 O VAL A 54 5.420 10.407 10.795 1.00 12.67 O ANISOU 470 O VAL A 54 1740 1567 1506 -104 325 -2 O ATOM 471 CB VAL A 54 7.663 8.479 9.245 1.00 11.85 C ANISOU 471 CB VAL A 54 1643 1486 1374 60 22 -44 C ATOM 472 CG1 VAL A 54 7.277 7.758 10.507 1.00 14.67 C ANISOU 472 CG1 VAL A 54 2182 1835 1557 196 68 295 C ATOM 473 CG2 VAL A 54 7.723 7.523 8.071 1.00 14.42 C ANISOU 473 CG2 VAL A 54 2135 1569 1775 17 27 -281 C ATOM 474 N GLN A 55 7.282 11.538 10.326 1.00 12.20 N ANISOU 474 N GLN A 55 1823 1417 1395 -137 357 0 N ATOM 475 CA GLN A 55 7.030 12.515 11.366 1.00 13.11 C ANISOU 475 CA GLN A 55 2033 1605 1342 -127 213 -168 C ATOM 476 C GLN A 55 5.728 13.249 11.153 1.00 13.11 C ANISOU 476 C GLN A 55 1952 1504 1525 -164 326 -137 C ATOM 477 O GLN A 55 5.050 13.593 12.147 1.00 15.23 O ANISOU 477 O GLN A 55 2034 1924 1827 -95 435 -301 O ATOM 478 CB GLN A 55 8.197 13.499 11.454 1.00 15.88 C ANISOU 478 CB GLN A 55 1987 2060 1988 -341 385 -539 C ATOM 479 CG GLN A 55 9.507 12.929 11.971 1.00 17.00 C ANISOU 479 CG GLN A 55 2122 2458 1880 -211 254 -415 C ATOM 480 CD GLN A 55 10.714 13.894 11.791 1.00 17.05 C ANISOU 480 CD GLN A 55 2079 1909 2490 -183 127 -656 C ATOM 481 OE1 GLN A 55 10.678 14.771 10.905 1.00 23.45 O ANISOU 481 OE1 GLN A 55 2681 3005 3222 -682 -162 269 O ATOM 482 NE2 GLN A 55 11.726 13.666 12.529 1.00 19.18 N ANISOU 482 NE2 GLN A 55 2512 2176 2600 -518 -26 -410 N ATOM 483 N ALA A 56 5.358 13.507 9.927 1.00 13.59 N ANISOU 483 N ALA A 56 1870 1606 1686 -17 344 47 N ATOM 484 CA ALA A 56 4.133 14.219 9.594 1.00 14.13 C ANISOU 484 CA ALA A 56 2031 1466 1870 126 420 12 C ATOM 485 C ALA A 56 2.883 13.478 10.049 1.00 13.07 C ANISOU 485 C ALA A 56 1871 1524 1571 115 211 123 C ATOM 486 O ALA A 56 1.826 14.095 10.210 1.00 14.87 O ANISOU 486 O ALA A 56 1920 1677 2052 256 213 189 O ATOM 487 CB ALA A 56 4.011 14.515 8.134 1.00 17.20 C ANISOU 487 CB ALA A 56 2362 2107 2068 131 441 708 C ATOM 488 N VAL A 57 2.983 12.166 10.277 1.00 12.80 N ANISOU 488 N VAL A 57 1723 1519 1620 75 249 0 N ATOM 489 CA VAL A 57 1.836 11.393 10.709 1.00 12.67 C ANISOU 489 CA VAL A 57 1658 1609 1546 34 94 45 C ATOM 490 C VAL A 57 1.275 11.918 12.031 1.00 11.95 C ANISOU 490 C VAL A 57 1467 1535 1540 172 55 55 C ATOM 491 O VAL A 57 0.096 11.792 12.292 1.00 13.28 O ANISOU 491 O VAL A 57 1562 1661 1824 63 123 115 O ATOM 492 CB VAL A 57 2.139 9.890 10.700 1.00 12.83 C ANISOU 492 CB VAL A 57 1715 1558 1603 -43 122 -62 C ATOM 493 CG1 VAL A 57 0.968 9.075 11.258 1.00 14.27 C ANISOU 493 CG1 VAL A 57 1873 1528 2021 -126 167 -6 C ATOM 494 CG2 VAL A 57 2.480 9.438 9.279 1.00 14.45 C ANISOU 494 CG2 VAL A 57 2041 1770 1679 46 154 -200 C ATOM 495 N CYS A 58 2.118 12.503 12.866 1.00 12.47 N ANISOU 495 N CYS A 58 1526 1668 1544 70 230 -35 N ATOM 496 CA CYS A 58 1.690 13.071 14.133 1.00 13.30 C ANISOU 496 CA CYS A 58 1862 1563 1630 106 219 -41 C ATOM 497 C CYS A 58 0.717 14.229 14.015 1.00 14.59 C ANISOU 497 C CYS A 58 1946 1675 1922 206 238 -231 C ATOM 498 O CYS A 58 0.170 14.621 15.022 1.00 17.91 O ANISOU 498 O CYS A 58 2478 2152 2175 567 553 -97 O ATOM 499 CB CYS A 58 2.895 13.499 14.983 1.00 14.17 C ANISOU 499 CB CYS A 58 2067 1609 1706 -102 152 -89 C ATOM 500 SG CYS A 58 4.012 12.156 15.434 1.00 14.82 S ANISOU 500 SG CYS A 58 1773 2130 1727 67 110 -144 S ATOM 501 N SER A 59 0.515 14.729 12.802 1.00 15.29 N ANISOU 501 N SER A 59 2125 1551 2134 309 177 -10 N ATOM 502 CA SER A 59 -0.416 15.771 12.491 1.00 17.85 C ANISOU 502 CA SER A 59 2713 1682 2389 532 -72 -153 C ATOM 503 C SER A 59 -1.611 15.247 11.686 1.00 17.16 C ANISOU 503 C SER A 59 2413 1958 2152 643 24 86 C ATOM 504 O SER A 59 -2.389 16.058 11.169 1.00 21.89 O ANISOU 504 O SER A 59 2936 2200 3183 809 -348 324 O ATOM 505 CB ASER A 59 0.268 16.969 11.827 0.46 22.36 C ANISOU 505 CB ASER A 59 3902 1177 3415 209 -510 -160 C ATOM 506 CB BSER A 59 0.231 16.938 11.748 0.54 23.35 C ANISOU 506 CB BSER A 59 2812 2076 3984 365 -747 876 C ATOM 507 OG ASER A 59 0.761 16.641 10.534 0.46 25.11 O ANISOU 507 OG ASER A 59 3579 1891 4072 541 860 779 O ATOM 508 OG BSER A 59 1.208 17.547 12.545 0.54 28.67 O ANISOU 508 OG BSER A 59 4348 2456 4090 -684 -485 10 O ATOM 509 N GLN A 60 -1.759 13.938 11.527 1.00 15.94 N ANISOU 509 N GLN A 60 2010 1994 2052 464 -19 106 N ATOM 510 CA GLN A 60 -2.781 13.295 10.706 1.00 16.21 C ANISOU 510 CA GLN A 60 1919 2270 1971 418 0 291 C ATOM 511 C GLN A 60 -3.937 12.796 11.515 1.00 17.37 C ANISOU 511 C GLN A 60 1933 2198 2470 536 256 290 C ATOM 512 O GLN A 60 -4.373 13.480 12.444 1.00 20.71 O ANISOU 512 O GLN A 60 2427 2514 2927 416 682 -47 O ATOM 513 CB GLN A 60 -2.137 12.350 9.704 1.00 15.54 C ANISOU 513 CB GLN A 60 1806 2113 1984 308 0 210 C ATOM 514 CG GLN A 60 -1.195 13.135 8.809 1.00 17.38 C ANISOU 514 CG GLN A 60 2310 2010 2284 342 287 275 C ATOM 515 CD GLN A 60 -0.436 12.325 7.792 1.00 15.87 C ANISOU 515 CD GLN A 60 2087 2131 1814 257 37 279 C ATOM 516 OE1 GLN A 60 -0.687 11.152 7.509 1.00 18.56 O ANISOU 516 OE1 GLN A 60 2640 2190 2224 119 340 93 O ATOM 517 NE2 GLN A 60 0.601 12.941 7.232 1.00 21.53 N ANISOU 517 NE2 GLN A 60 2819 2761 2600 -238 744 41 N ATOM 518 N LYS A 61 -4.470 11.600 11.280 1.00 16.45 N ANISOU 518 N LYS A 61 1960 2381 1909 399 94 318 N ATOM 519 CA LYS A 61 -5.730 11.204 11.883 1.00 17.88 C ANISOU 519 CA LYS A 61 1941 2538 2315 433 61 546 C ATOM 520 C LYS A 61 -5.490 10.660 13.275 1.00 15.95 C ANISOU 520 C LYS A 61 1595 2298 2165 375 254 320 C ATOM 521 O LYS A 61 -4.891 9.603 13.469 1.00 17.58 O ANISOU 521 O LYS A 61 1945 2630 2105 790 107 249 O ATOM 522 CB ALYS A 61 -6.450 10.169 11.028 0.45 20.33 C ATOM 523 CB BLYS A 61 -6.342 10.091 11.013 0.55 19.69 C ATOM 524 CG ALYS A 61 -7.682 9.583 11.717 0.45 31.94 C ATOM 525 CG BLYS A 61 -7.748 9.787 11.574 0.55 20.51 C ATOM 526 CD ALYS A 61 -8.871 10.524 11.780 0.45 25.14 C ATOM 527 CD BLYS A 61 -8.544 9.018 10.535 0.55 29.83 C ATOM 528 CE ALYS A 61 -10.141 9.786 12.201 0.45 27.30 C ATOM 529 CE BLYS A 61 -9.950 8.659 10.980 0.55 33.76 C ATOM 530 NZ ALYS A 61 -11.266 10.683 12.615 0.45 25.94 N ATOM 531 NZ BLYS A 61 -10.583 9.703 11.819 0.55 51.39 N ATOM 532 N ASN A 62 -6.019 11.319 14.304 1.00 16.45 N ANISOU 532 N ASN A 62 1846 2106 2299 424 217 306 N ATOM 533 CA ASN A 62 -5.888 10.840 15.672 1.00 15.13 C ANISOU 533 CA ASN A 62 1606 1988 2155 331 66 94 C ATOM 534 C ASN A 62 -6.811 9.642 15.881 1.00 15.60 C ANISOU 534 C ASN A 62 1544 2236 2145 214 1 189 C ATOM 535 O ASN A 62 -7.997 9.731 15.549 1.00 19.70 O ANISOU 535 O ASN A 62 1571 2758 3157 219 60 543 O ATOM 536 CB ASN A 62 -6.254 12.009 16.608 1.00 18.43 C ANISOU 536 CB ASN A 62 2175 2290 2537 490 314 -168 C ATOM 537 CG ASN A 62 -6.035 11.815 18.079 1.00 20.26 C ANISOU 537 CG ASN A 62 2261 3030 2408 690 463 -178 C ATOM 538 OD1 ASN A 62 -6.804 12.350 18.866 1.00 32.11 O ANISOU 538 OD1 ASN A 62 3776 5687 2735 2494 374 -566 O ATOM 539 ND2 ASN A 62 -5.100 11.023 18.561 1.00 18.03 N ANISOU 539 ND2 ASN A 62 2173 2414 2265 394 368 -299 N ATOM 540 N VAL A 63 -6.271 8.557 16.416 1.00 14.65 N ANISOU 540 N VAL A 63 1512 2064 1990 31 85 114 N ATOM 541 CA VAL A 63 -6.978 7.338 16.680 1.00 14.90 C ANISOU 541 CA VAL A 63 1469 2201 1991 -80 -26 103 C ATOM 542 C VAL A 63 -6.477 6.752 17.999 1.00 13.95 C ANISOU 542 C VAL A 63 1253 2181 1866 141 202 69 C ATOM 543 O VAL A 63 -5.401 7.087 18.504 1.00 16.77 O ANISOU 543 O VAL A 63 1437 2674 2260 -198 -85 357 O ATOM 544 CB VAL A 63 -6.744 6.289 15.575 1.00 16.38 C ANISOU 544 CB VAL A 63 1898 2333 1992 -226 -104 -1 C ATOM 545 CG1 VAL A 63 -7.335 6.775 14.258 1.00 20.91 C ANISOU 545 CG1 VAL A 63 2633 3296 2015 -338 -324 150 C ATOM 546 CG2 VAL A 63 -5.302 5.893 15.429 1.00 17.61 C ANISOU 546 CG2 VAL A 63 2113 2378 2199 76 328 20 C ATOM 547 N ALA A 64 -7.252 5.860 18.591 1.00 14.40 N ANISOU 547 N ALA A 64 1307 2284 1882 -50 -68 71 N ATOM 548 CA ALA A 64 -6.801 5.124 19.764 1.00 13.73 C ANISOU 548 CA ALA A 64 1408 2371 1436 29 98 -56 C ATOM 549 C ALA A 64 -5.705 4.133 19.376 1.00 12.49 C ANISOU 549 C ALA A 64 1484 1862 1401 -177 -48 -111 C ATOM 550 O ALA A 64 -5.805 3.421 18.374 1.00 16.21 O ANISOU 550 O ALA A 64 1839 2680 1641 43 -233 -524 O ATOM 551 CB ALA A 64 -7.958 4.451 20.417 1.00 17.55 C ANISOU 551 CB ALA A 64 1656 2748 2264 90 348 418 C ATOM 552 N CYS A 65 -4.701 4.040 20.195 1.00 12.50 N ANISOU 552 N CYS A 65 1449 1918 1383 -63 -13 -165 N ATOM 553 CA CYS A 65 -3.726 2.986 20.097 1.00 12.27 C ANISOU 553 CA CYS A 65 1456 1838 1366 -134 101 -32 C ATOM 554 C CYS A 65 -4.342 1.654 20.462 1.00 12.55 C ANISOU 554 C CYS A 65 1536 1959 1272 -175 122 61 C ATOM 555 O CYS A 65 -5.396 1.598 21.096 1.00 14.49 O ANISOU 555 O CYS A 65 1596 2224 1685 -384 240 -108 O ATOM 556 CB ACYS A 65 -2.556 3.250 21.083 0.87 12.91 C ANISOU 556 CB ACYS A 65 1479 1966 1462 -124 -24 135 C ATOM 557 CB BCYS A 65 -2.421 3.132 20.878 0.14 11.36 C ANISOU 557 CB BCYS A 65 1579 1738 999 -92 32 316 C ATOM 558 SG ACYS A 65 -1.802 4.907 20.972 0.87 13.04 S ANISOU 558 SG ACYS A 65 1641 1902 1411 -214 -10 -66 S ATOM 559 SG BCYS A 65 -1.068 3.920 19.938 0.14 11.70 S ANISOU 559 SG BCYS A 65 1475 1487 1485 -122 133 132 S ATOM 560 N LYS A 66 -3.664 0.550 20.157 1.00 13.44 N ANISOU 560 N LYS A 66 1763 1820 1522 -289 73 -109 N ATOM 561 CA LYS A 66 -4.185 -0.761 20.477 1.00 15.71 C ANISOU 561 CA LYS A 66 2301 1919 1747 -531 -27 -147 C ATOM 562 C LYS A 66 -4.442 -0.953 21.954 1.00 15.51 C ANISOU 562 C LYS A 66 2304 1861 1727 -591 3 -123 C ATOM 563 O LYS A 66 -5.380 -1.659 22.303 1.00 20.05 O ANISOU 563 O LYS A 66 2947 2612 2061 -1307 36 58 O ATOM 564 CB LYS A 66 -3.180 -1.843 20.014 1.00 20.83 C ANISOU 564 CB LYS A 66 3807 1923 2184 -147 413 -404 C ATOM 565 CG LYS A 66 -3.078 -2.112 18.549 1.00 31.38 C ATOM 566 CD LYS A 66 -1.800 -2.947 18.305 1.00 69.00 C ATOM 567 CE LYS A 66 -2.076 -4.431 18.192 1.00104.77 C ATOM 568 NZ LYS A 66 -1.950 -4.961 16.801 1.00109.37 N ATOM 569 N ASN A 67 -3.655 -0.331 22.818 1.00 15.01 N ANISOU 569 N ASN A 67 2241 1858 1604 -500 26 -71 N ATOM 570 CA ASN A 67 -3.805 -0.445 24.250 1.00 17.28 C ANISOU 570 CA ASN A 67 3072 1983 1509 -245 -100 96 C ATOM 571 C ASN A 67 -4.737 0.600 24.846 1.00 17.26 C ANISOU 571 C ASN A 67 2582 2349 1627 -522 362 27 C ATOM 572 O ASN A 67 -4.878 0.703 26.063 1.00 21.68 O ANISOU 572 O ASN A 67 3328 3203 1708 -293 447 -8 O ATOM 573 CB ASN A 67 -2.411 -0.346 24.947 1.00 19.28 C ANISOU 573 CB ASN A 67 3118 2479 1727 23 -324 92 C ATOM 574 CG ASN A 67 -1.898 1.091 24.963 1.00 21.09 C ANISOU 574 CG ASN A 67 3036 2577 2398 -361 -415 259 C ATOM 575 OD1 ASN A 67 -2.271 2.074 24.316 1.00 20.52 O ANISOU 575 OD1 ASN A 67 2574 2906 2318 -25 -7 514 O ATOM 576 ND2 ASN A 67 -0.887 1.325 25.864 1.00 34.12 N ANISOU 576 ND2 ASN A 67 5660 2726 4576 -488 -2820 424 N ATOM 577 N GLY A 68 -5.378 1.409 24.047 1.00 16.14 N ANISOU 577 N GLY A 68 2274 2047 1810 -471 236 -293 N ATOM 578 CA GLY A 68 -6.352 2.376 24.490 1.00 18.02 C ANISOU 578 CA GLY A 68 2161 2518 2168 -484 574 -368 C ATOM 579 C GLY A 68 -5.848 3.786 24.668 1.00 16.59 C ANISOU 579 C GLY A 68 1920 2511 1871 -290 320 -789 C ATOM 580 O GLY A 68 -6.679 4.705 24.806 1.00 18.19 O ANISOU 580 O GLY A 68 1840 2730 2344 -218 249 -874 O ATOM 581 N GLN A 69 -4.552 4.042 24.634 1.00 15.61 N ANISOU 581 N GLN A 69 1870 2281 1780 -241 88 -499 N ATOM 582 CA GLN A 69 -4.051 5.427 24.710 1.00 15.19 C ANISOU 582 CA GLN A 69 1949 2151 1673 -152 84 -530 C ATOM 583 C GLN A 69 -4.544 6.189 23.498 1.00 13.83 C ANISOU 583 C GLN A 69 1488 2303 1465 -214 174 -569 C ATOM 584 O GLN A 69 -4.820 5.665 22.450 1.00 17.10 O ANISOU 584 O GLN A 69 2114 2815 1570 5 -101 -760 O ATOM 585 CB GLN A 69 -2.484 5.439 24.642 1.00 16.49 C ANISOU 585 CB GLN A 69 1880 2199 2189 -250 -272 -418 C ATOM 586 CG GLN A 69 -1.782 4.884 25.793 1.00 18.27 C ANISOU 586 CG GLN A 69 2617 2304 2020 -141 -335 -514 C ATOM 587 CD GLN A 69 -0.286 4.869 25.630 1.00 21.14 C ANISOU 587 CD GLN A 69 2321 2360 3349 -98 -682 -517 C ATOM 588 OE1 GLN A 69 0.299 4.079 26.343 1.00 23.84 O ANISOU 588 OE1 GLN A 69 3123 3134 2801 322 -278 -168 O ATOM 589 NE2 GLN A 69 0.385 5.678 24.791 1.00 22.10 N ANISOU 589 NE2 GLN A 69 2216 2695 3486 192 -434 -108 N ATOM 590 N THR A 70 -4.604 7.504 23.677 1.00 13.74 N ANISOU 590 N THR A 70 1472 2450 1298 -127 57 -426 N ATOM 591 CA THR A 70 -5.169 8.341 22.648 1.00 14.58 C ANISOU 591 CA THR A 70 1452 2645 1442 -66 56 -269 C ATOM 592 C THR A 70 -4.201 9.276 21.960 1.00 14.40 C ANISOU 592 C THR A 70 1533 2336 1603 70 165 -304 C ATOM 593 O THR A 70 -4.624 10.166 21.216 1.00 18.88 O ANISOU 593 O THR A 70 1832 2816 2527 313 381 336 O ATOM 594 CB THR A 70 -6.411 9.061 23.129 1.00 19.11 C ANISOU 594 CB THR A 70 1595 3892 1776 476 166 155 C ATOM 595 OG1 THR A 70 -6.074 9.722 24.329 1.00 26.23 O ANISOU 595 OG1 THR A 70 3353 4723 1891 2291 -244 -648 O ATOM 596 CG2 THR A 70 -7.545 8.056 23.407 1.00 32.19 C ANISOU 596 CG2 THR A 70 1471 6065 4694 17 748 1422 C ATOM 597 N ASN A 71 -2.901 9.016 22.104 1.00 14.12 N ANISOU 597 N ASN A 71 1509 2216 1638 -38 286 -204 N ATOM 598 CA ASN A 71 -1.877 9.749 21.376 1.00 14.59 C ANISOU 598 CA ASN A 71 1559 2122 1863 -26 352 -305 C ATOM 599 C ASN A 71 -1.357 9.038 20.142 1.00 13.20 C ANISOU 599 C ASN A 71 1476 1849 1689 -157 305 -67 C ATOM 600 O ASN A 71 -0.188 9.155 19.815 1.00 14.49 O ANISOU 600 O ASN A 71 1451 2102 1953 -173 394 -200 O ATOM 601 CB ASN A 71 -0.727 10.136 22.288 1.00 15.62 C ANISOU 601 CB ASN A 71 1738 2356 1840 -206 306 -263 C ATOM 602 CG ASN A 71 0.050 8.975 22.841 1.00 15.60 C ANISOU 602 CG ASN A 71 1784 2691 1451 -316 130 -92 C ATOM 603 OD1 ASN A 71 -0.555 7.965 23.218 1.00 17.74 O ANISOU 603 OD1 ASN A 71 1767 2849 2124 -320 12 471 O ATOM 604 ND2 ASN A 71 1.370 9.091 22.937 1.00 17.81 N ANISOU 604 ND2 ASN A 71 1671 2931 2164 -303 92 -73 N ATOM 605 N CYS A 72 -2.206 8.207 19.514 1.00 13.41 N ANISOU 605 N CYS A 72 1335 2184 1578 -67 314 -147 N ATOM 606 CA CYS A 72 -1.858 7.568 18.273 1.00 12.08 C ANISOU 606 CA CYS A 72 1242 1843 1506 106 135 -3 C ATOM 607 C CYS A 72 -2.463 8.274 17.069 1.00 11.94 C ANISOU 607 C CYS A 72 1213 1776 1549 -42 124 -19 C ATOM 608 O CYS A 72 -3.480 9.004 17.158 1.00 13.42 O ANISOU 608 O CYS A 72 1345 1984 1771 139 175 24 O ATOM 609 CB ACYS A 72 -2.247 6.076 18.208 0.87 13.23 C ANISOU 609 CB ACYS A 72 1525 1905 1596 -8 126 50 C ATOM 610 CB BCYS A 72 -2.245 6.132 18.563 0.14 10.93 C ANISOU 610 CB BCYS A 72 595 1968 1589 -11 8 125 C ATOM 611 SG ACYS A 72 -1.095 4.982 19.083 0.87 12.91 S ANISOU 611 SG ACYS A 72 1385 1829 1690 30 247 -52 S ATOM 612 SG BCYS A 72 -1.491 5.858 20.239 0.14 11.59 S ANISOU 612 SG BCYS A 72 1475 1581 1347 -52 25 -3 S ATOM 613 N TYR A 73 -1.797 8.091 15.946 1.00 11.94 N ANISOU 613 N TYR A 73 1405 1641 1490 168 154 26 N ATOM 614 CA TYR A 73 -2.127 8.767 14.697 1.00 12.23 C ANISOU 614 CA TYR A 73 1443 1667 1539 246 103 44 C ATOM 615 C TYR A 73 -1.956 7.776 13.560 1.00 12.60 C ANISOU 615 C TYR A 73 1477 1762 1549 134 23 18 C ATOM 616 O TYR A 73 -0.947 7.065 13.495 1.00 13.45 O ANISOU 616 O TYR A 73 1657 1771 1681 312 41 -111 O ATOM 617 CB TYR A 73 -1.238 9.995 14.451 1.00 13.96 C ANISOU 617 CB TYR A 73 1894 1675 1735 100 303 31 C ATOM 618 CG TYR A 73 -1.481 11.043 15.520 1.00 13.60 C ANISOU 618 CG TYR A 73 1677 1676 1815 0 374 -16 C ATOM 619 CD1 TYR A 73 -0.800 10.999 16.710 1.00 15.36 C ANISOU 619 CD1 TYR A 73 1943 1994 1900 -234 263 -45 C ATOM 620 CD2 TYR A 73 -2.413 12.037 15.294 1.00 17.42 C ANISOU 620 CD2 TYR A 73 2184 1841 2592 306 223 -128 C ATOM 621 CE1 TYR A 73 -1.054 11.884 17.718 1.00 19.12 C ANISOU 621 CE1 TYR A 73 2578 2542 2143 -664 339 -559 C ATOM 622 CE2 TYR A 73 -2.652 12.942 16.301 1.00 20.63 C ANISOU 622 CE2 TYR A 73 2084 1992 3761 56 345 -785 C ATOM 623 CZ TYR A 73 -1.991 12.864 17.487 1.00 20.69 C ANISOU 623 CZ TYR A 73 2377 2431 3055 -476 796 -1049 C ATOM 624 OH TYR A 73 -2.435 13.900 18.321 1.00 31.26 O ANISOU 624 OH TYR A 73 3965 3549 4365 -601 1880 -2079 O ATOM 625 N GLN A 74 -2.918 7.786 12.664 1.00 13.67 N ANISOU 625 N GLN A 74 1542 2088 1565 326 50 -55 N ATOM 626 CA GLN A 74 -2.910 6.969 11.476 1.00 13.31 C ANISOU 626 CA GLN A 74 1539 2036 1484 303 -38 32 C ATOM 627 C GLN A 74 -2.581 7.818 10.264 1.00 13.45 C ANISOU 627 C GLN A 74 1632 1868 1611 196 -60 129 C ATOM 628 O GLN A 74 -3.104 8.911 10.051 1.00 15.75 O ANISOU 628 O GLN A 74 2083 2017 1886 467 -82 161 O ATOM 629 CB GLN A 74 -4.287 6.342 11.284 1.00 14.77 C ANISOU 629 CB GLN A 74 1635 2271 1705 23 102 114 C ATOM 630 CG GLN A 74 -4.372 5.409 10.097 1.00 18.89 C ANISOU 630 CG GLN A 74 2061 2670 2446 -33 -259 -418 C ATOM 631 CD GLN A 74 -5.627 4.608 10.043 1.00 28.85 C ANISOU 631 CD GLN A 74 1901 4927 4132 -693 -226 -1466 C ATOM 632 OE1 GLN A 74 -6.256 4.210 10.995 1.00 41.60 O ANISOU 632 OE1 GLN A 74 2987 6883 5936 -2062 1572 -2056 O ATOM 633 NE2 GLN A 74 -5.980 4.194 8.842 1.00 46.69 N ANISOU 633 NE2 GLN A 74 3045 9482 5213 -1116 -1309 -2799 N ATOM 634 N SER A 75 -1.700 7.265 9.409 1.00 13.17 N ANISOU 634 N SER A 75 1631 1834 1537 120 -62 95 N ATOM 635 CA SER A 75 -1.337 7.986 8.202 1.00 13.67 C ANISOU 635 CA SER A 75 1824 1828 1542 96 -77 73 C ATOM 636 C SER A 75 -2.515 8.049 7.229 1.00 14.83 C ANISOU 636 C SER A 75 1932 2103 1599 194 -112 192 C ATOM 637 O SER A 75 -3.268 7.094 7.053 1.00 16.52 O ANISOU 637 O SER A 75 2058 2373 1848 -24 -433 170 O ATOM 638 CB SER A 75 -0.142 7.308 7.541 1.00 13.74 C ANISOU 638 CB SER A 75 1713 1851 1658 0 12 49 C ATOM 639 OG SER A 75 -0.421 6.011 7.132 1.00 14.36 O ANISOU 639 OG SER A 75 1931 1974 1552 82 -98 67 O ATOM 640 N TYR A 76 -2.643 9.166 6.561 1.00 15.96 N ANISOU 640 N TYR A 76 2066 2224 1774 465 -72 307 N ATOM 641 CA TYR A 76 -3.702 9.301 5.532 1.00 17.38 C ANISOU 641 CA TYR A 76 2280 2421 1901 517 -230 283 C ATOM 642 C TYR A 76 -3.365 8.460 4.308 1.00 19.30 C ANISOU 642 C TYR A 76 2447 2829 2059 489 -480 -32 C ATOM 643 O TYR A 76 -4.293 7.969 3.672 1.00 25.72 O ANISOU 643 O TYR A 76 2879 4462 2432 144 -717 -468 O ATOM 644 CB TYR A 76 -3.839 10.770 5.101 1.00 22.44 C ANISOU 644 CB TYR A 76 3675 2718 2135 1306 -100 573 C ATOM 645 CG TYR A 76 -4.332 11.739 6.127 1.00 24.28 C ANISOU 645 CG TYR A 76 3545 3009 2672 1750 -467 229 C ATOM 646 CD1 TYR A 76 -5.441 11.451 6.898 1.00 30.68 C ANISOU 646 CD1 TYR A 76 5099 3831 2728 1931 716 455 C ATOM 647 CD2 TYR A 76 -3.768 12.995 6.279 1.00 29.47 C ANISOU 647 CD2 TYR A 76 3997 3057 4143 1793 -1012 -303 C ATOM 648 CE1 TYR A 76 -5.926 12.352 7.825 1.00 32.86 C ANISOU 648 CE1 TYR A 76 6009 3759 2716 2360 652 518 C ATOM 649 CE2 TYR A 76 -4.241 13.924 7.198 1.00 31.25 C ANISOU 649 CE2 TYR A 76 4441 3404 4030 2116 -1273 -471 C ATOM 650 CZ TYR A 76 -5.329 13.584 7.965 1.00 33.83 C ANISOU 650 CZ TYR A 76 4196 4469 4191 2536 -1137 -505 C ATOM 651 OH TYR A 76 -5.869 14.458 8.883 1.00 37.33 O ANISOU 651 OH TYR A 76 4586 4770 4827 2489 -984 -988 O ATOM 652 N SER A 77 -2.110 8.220 4.012 1.00 18.76 N ANISOU 652 N SER A 77 2671 2537 1919 680 -306 -1 N ATOM 653 CA SER A 77 -1.679 7.446 2.851 1.00 20.77 C ANISOU 653 CA SER A 77 3309 2841 1740 836 -224 156 C ATOM 654 C SER A 77 -1.045 6.133 3.294 1.00 16.48 C ANISOU 654 C SER A 77 2179 2690 1393 537 -70 111 C ATOM 655 O SER A 77 -0.606 5.981 4.423 1.00 17.32 O ANISOU 655 O SER A 77 2502 2571 1509 484 -357 -65 O ATOM 656 CB ASER A 77 -0.713 8.248 1.994 0.28 29.31 C ANISOU 656 CB ASER A 77 6054 2803 2277 483 1103 339 C ATOM 657 CB BSER A 77 -0.757 8.216 1.924 0.31 25.89 C ANISOU 657 CB BSER A 77 5379 2222 2234 461 769 -91 C ATOM 658 CB CSER A 77 -0.578 8.226 2.122 0.41 28.52 C ANISOU 658 CB CSER A 77 5677 3255 1906 399 918 684 C ATOM 659 OG ASER A 77 0.034 7.461 1.087 0.28 24.37 O ANISOU 659 OG ASER A 77 4867 2774 1620 519 454 595 O ATOM 660 OG BSER A 77 0.445 8.632 2.551 0.31 41.20 O ANISOU 660 OG BSER A 77 5139 4120 6396 -1069 973 -821 O ATOM 661 OG CSER A 77 -1.194 9.420 1.580 0.41 44.39 O ANISOU 661 OG CSER A 77 11712 2663 2492 1909 1693 631 O ATOM 662 N THR A 78 -1.042 5.177 2.410 1.00 17.29 N ANISOU 662 N THR A 78 1944 3114 1512 711 -435 -160 N ATOM 663 CA THR A 78 -0.306 3.955 2.633 1.00 16.64 C ANISOU 663 CA THR A 78 1747 2635 1942 287 -408 -154 C ATOM 664 C THR A 78 1.190 4.228 2.436 1.00 14.89 C ANISOU 664 C THR A 78 1790 2174 1695 249 -308 8 C ATOM 665 O THR A 78 1.607 5.174 1.759 1.00 18.19 O ANISOU 665 O THR A 78 2264 2540 2107 337 -193 538 O ATOM 666 CB THR A 78 -0.739 2.754 1.762 1.00 19.29 C ANISOU 666 CB THR A 78 2222 3048 2060 -122 -484 -363 C ATOM 667 OG1 THR A 78 -0.513 3.118 0.408 1.00 23.42 O ANISOU 667 OG1 THR A 78 3282 3554 2062 -46 -247 -392 O ATOM 668 CG2 THR A 78 -2.211 2.407 1.914 1.00 22.71 C ANISOU 668 CG2 THR A 78 2366 3516 2747 -343 -565 -339 C ATOM 669 N MET A 79 1.987 3.407 3.103 1.00 13.93 N ANISOU 669 N MET A 79 1646 1924 1722 149 -164 24 N ATOM 670 CA MET A 79 3.445 3.513 3.053 1.00 12.85 C ANISOU 670 CA MET A 79 1585 1707 1591 60 -184 58 C ATOM 671 C MET A 79 4.032 2.146 2.757 1.00 12.38 C ANISOU 671 C MET A 79 1619 1672 1412 10 -135 114 C ATOM 672 O MET A 79 3.464 1.103 3.090 1.00 13.88 O ANISOU 672 O MET A 79 1834 1716 1726 3 32 -13 O ATOM 673 CB MET A 79 3.962 4.001 4.426 1.00 14.25 C ANISOU 673 CB MET A 79 1849 1999 1565 66 -41 -118 C ATOM 674 CG MET A 79 3.545 5.510 4.606 1.00 17.07 C ANISOU 674 CG MET A 79 2079 2199 2209 301 -271 -533 C ATOM 675 SD MET A 79 4.314 6.141 6.087 1.00 17.68 S ANISOU 675 SD MET A 79 2653 2307 1758 -92 -101 -231 S ATOM 676 CE MET A 79 3.754 7.818 5.989 1.00 23.15 C ANISOU 676 CE MET A 79 4101 2210 2487 231 66 -788 C ATOM 677 N SER A 80 5.225 2.144 2.174 1.00 12.53 N ANISOU 677 N SER A 80 1745 1647 1370 80 -124 101 N ATOM 678 CA SER A 80 5.982 0.924 1.954 1.00 12.24 C ANISOU 678 CA SER A 80 1795 1619 1236 52 -145 -10 C ATOM 679 C SER A 80 6.591 0.457 3.252 1.00 11.29 C ANISOU 679 C SER A 80 1574 1502 1216 -30 -116 18 C ATOM 680 O SER A 80 7.373 1.226 3.845 1.00 12.64 O ANISOU 680 O SER A 80 1677 1657 1470 -87 -223 18 O ATOM 681 CB SER A 80 7.058 1.199 0.928 1.00 13.74 C ANISOU 681 CB SER A 80 2134 1840 1245 60 58 70 C ATOM 682 OG SER A 80 7.852 0.028 0.780 1.00 16.07 O ANISOU 682 OG SER A 80 2338 2188 1580 280 253 74 O ATOM 683 N ILE A 81 6.293 -0.736 3.683 1.00 11.25 N ANISOU 683 N ILE A 81 1585 1511 1176 53 -178 -86 N ATOM 684 CA ILE A 81 6.806 -1.296 4.917 1.00 11.08 C ANISOU 684 CA ILE A 81 1616 1485 1110 73 -67 18 C ATOM 685 C ILE A 81 7.305 -2.709 4.698 1.00 11.04 C ANISOU 685 C ILE A 81 1586 1480 1128 41 -114 -103 C ATOM 686 O ILE A 81 6.928 -3.411 3.741 1.00 12.75 O ANISOU 686 O ILE A 81 1963 1642 1239 85 -283 -198 O ATOM 687 CB ILE A 81 5.736 -1.265 6.038 1.00 12.21 C ANISOU 687 CB ILE A 81 1683 1746 1210 136 -9 -53 C ATOM 688 CG1 ILE A 81 4.574 -2.169 5.763 1.00 14.37 C ANISOU 688 CG1 ILE A 81 1736 2050 1675 -60 73 -10 C ATOM 689 CG2 ILE A 81 5.311 0.153 6.326 1.00 14.57 C ANISOU 689 CG2 ILE A 81 2014 1956 1567 395 23 -253 C ATOM 690 CD1 ILE A 81 3.621 -2.345 6.979 1.00 19.94 C ANISOU 690 CD1 ILE A 81 1994 3554 2029 -542 182 238 C ATOM 691 N THR A 82 8.152 -3.154 5.609 1.00 11.16 N ANISOU 691 N THR A 82 1808 1276 1155 33 -202 -135 N ATOM 692 CA THR A 82 8.604 -4.515 5.707 1.00 10.51 C ANISOU 692 CA THR A 82 1656 1241 1097 -77 -124 -104 C ATOM 693 C THR A 82 8.280 -5.045 7.072 1.00 10.82 C ANISOU 693 C THR A 82 1678 1352 1081 -31 -26 -121 C ATOM 694 O THR A 82 8.664 -4.428 8.075 1.00 12.22 O ANISOU 694 O THR A 82 2050 1496 1098 -226 -33 -81 O ATOM 695 CB THR A 82 10.111 -4.658 5.437 1.00 11.27 C ANISOU 695 CB THR A 82 1679 1358 1245 -71 82 -43 C ATOM 696 OG1 THR A 82 10.393 -4.234 4.108 1.00 12.82 O ANISOU 696 OG1 THR A 82 2090 1502 1280 55 226 -44 O ATOM 697 CG2 THR A 82 10.583 -6.065 5.617 1.00 13.50 C ANISOU 697 CG2 THR A 82 1939 1417 1772 131 220 45 C ATOM 698 N ASP A 83 7.609 -6.172 7.149 1.00 11.27 N ANISOU 698 N ASP A 83 1722 1355 1203 -64 -62 -50 N ATOM 699 CA ASP A 83 7.354 -6.894 8.382 1.00 11.79 C ANISOU 699 CA ASP A 83 1653 1485 1343 -74 75 -60 C ATOM 700 C ASP A 83 8.396 -7.971 8.564 1.00 11.18 C ANISOU 700 C ASP A 83 1831 1257 1161 -121 29 -38 C ATOM 701 O ASP A 83 8.718 -8.707 7.624 1.00 13.43 O ANISOU 701 O ASP A 83 2212 1568 1325 96 -81 -272 O ATOM 702 CB AASP A 83 5.960 -7.512 8.188 0.52 16.29 C ANISOU 702 CB AASP A 83 1531 2520 2137 -261 436 -85 C ATOM 703 CB BASP A 83 5.945 -7.452 8.488 0.48 15.53 C ANISOU 703 CB BASP A 83 1716 2226 1959 -280 -35 421 C ATOM 704 CG AASP A 83 5.460 -8.336 9.347 0.52 19.13 C ANISOU 704 CG AASP A 83 2069 2837 2362 -641 558 41 C ATOM 705 CG BASP A 83 4.868 -6.416 8.748 0.48 18.99 C ANISOU 705 CG BASP A 83 1545 2444 3228 -486 428 -213 C ATOM 706 OD1AASP A 83 5.731 -9.545 9.383 0.52 23.67 O ANISOU 706 OD1AASP A 83 3452 2667 2873 -865 1211 71 O ATOM 707 OD1BASP A 83 5.025 -5.402 9.442 0.48 21.30 O ANISOU 707 OD1BASP A 83 2178 2425 3489 -152 -451 -215 O ATOM 708 OD2AASP A 83 4.894 -7.752 10.264 0.52 25.22 O ANISOU 708 OD2AASP A 83 4276 2726 2580 -1143 1509 -182 O ATOM 709 OD2BASP A 83 3.757 -6.710 8.245 0.48 25.27 O ANISOU 709 OD2BASP A 83 1578 3466 4557 -26 -37 -1341 O ATOM 710 N CYS A 84 8.921 -8.043 9.757 1.00 11.35 N ANISOU 710 N CYS A 84 1833 1374 1105 -29 68 -78 N ATOM 711 CA CYS A 84 9.892 -9.042 10.136 1.00 11.84 C ANISOU 711 CA CYS A 84 2035 1323 1141 59 138 28 C ATOM 712 C CYS A 84 9.301 -9.855 11.306 1.00 12.32 C ANISOU 712 C CYS A 84 2102 1399 1179 113 180 17 C ATOM 713 O CYS A 84 8.921 -9.282 12.312 1.00 15.53 O ANISOU 713 O CYS A 84 3110 1504 1285 42 590 30 O ATOM 714 CB CYS A 84 11.181 -8.385 10.625 1.00 12.05 C ANISOU 714 CB CYS A 84 1890 1569 1122 134 70 -91 C ATOM 715 SG CYS A 84 11.998 -7.328 9.416 1.00 12.25 S ANISOU 715 SG CYS A 84 1924 1307 1422 -47 67 -89 S ATOM 716 N ARG A 85 9.307 -11.164 11.173 1.00 12.96 N ANISOU 716 N ARG A 85 2270 1322 1333 -13 241 105 N ATOM 717 CA ARG A 85 8.707 -12.034 12.236 1.00 14.92 C ANISOU 717 CA ARG A 85 2556 1493 1619 45 326 228 C ATOM 718 C ARG A 85 9.676 -13.205 12.438 1.00 13.06 C ANISOU 718 C ARG A 85 2261 1294 1406 -216 358 189 C ATOM 719 O ARG A 85 10.191 -13.803 11.480 1.00 14.19 O ANISOU 719 O ARG A 85 2399 1627 1368 21 237 40 O ATOM 720 CB AARG A 85 7.323 -12.481 11.852 0.52 21.97 C ATOM 721 CB BARG A 85 7.440 -12.658 11.553 0.48 17.45 C ATOM 722 CG AARG A 85 6.349 -12.839 12.935 0.52 48.08 C ATOM 723 CG BARG A 85 6.483 -13.405 12.456 0.48 35.11 C ATOM 724 CD AARG A 85 5.052 -12.066 12.749 0.52 65.76 C ATOM 725 CD BARG A 85 5.167 -13.321 11.650 0.48 25.73 C ATOM 726 NE AARG A 85 4.674 -11.802 11.361 0.52 59.73 N ATOM 727 NE BARG A 85 4.871 -11.901 11.380 0.48 30.64 N ATOM 728 CZ AARG A 85 3.814 -10.850 11.010 0.52 61.83 C ATOM 729 CZ BARG A 85 4.445 -11.094 12.350 0.48 62.26 C ATOM 730 NH1AARG A 85 3.227 -10.077 11.923 0.52 50.15 N ATOM 731 NH1BARG A 85 4.259 -11.559 13.581 0.48 79.11 N ATOM 732 NH2AARG A 85 3.532 -10.672 9.722 0.52 62.61 N ATOM 733 NH2BARG A 85 4.173 -9.822 12.117 0.48 57.93 N ATOM 734 N GLU A 86 9.932 -13.536 13.678 1.00 13.63 N ANISOU 734 N GLU A 86 2315 1426 1440 -97 365 159 N ATOM 735 CA GLU A 86 10.842 -14.609 14.010 1.00 13.77 C ANISOU 735 CA GLU A 86 2291 1453 1488 -213 152 171 C ATOM 736 C GLU A 86 10.366 -15.921 13.407 1.00 14.49 C ANISOU 736 C GLU A 86 2165 1331 2011 -195 -54 367 C ATOM 737 O GLU A 86 9.198 -16.261 13.495 1.00 18.57 O ANISOU 737 O GLU A 86 2348 1585 3122 -441 98 181 O ATOM 738 CB GLU A 86 10.926 -14.689 15.529 1.00 17.42 C ANISOU 738 CB GLU A 86 2751 2406 1463 -145 152 407 C ATOM 739 CG GLU A 86 12.181 -15.188 16.038 1.00 23.66 C ANISOU 739 CG GLU A 86 2915 4536 1539 358 20 89 C ATOM 740 CD GLU A 86 12.305 -15.211 17.524 1.00 17.74 C ANISOU 740 CD GLU A 86 2515 2790 1437 -451 133 188 C ATOM 741 OE1 GLU A 86 11.344 -14.924 18.288 1.00 20.34 O ANISOU 741 OE1 GLU A 86 2993 3035 1702 -130 408 232 O ATOM 742 OE2 GLU A 86 13.410 -15.575 17.898 1.00 17.35 O ANISOU 742 OE2 GLU A 86 2730 2294 1569 -447 -117 -89 O ATOM 743 N THR A 87 11.291 -16.717 12.874 1.00 15.42 N ANISOU 743 N THR A 87 2309 1245 2305 -189 -129 112 N ATOM 744 CA THR A 87 10.956 -18.039 12.383 1.00 16.55 C ANISOU 744 CA THR A 87 2615 1288 2386 -284 -223 145 C ATOM 745 C THR A 87 11.182 -19.082 13.433 1.00 13.83 C ANISOU 745 C THR A 87 2004 1206 2044 -176 311 -12 C ATOM 746 O THR A 87 11.811 -18.871 14.464 1.00 15.48 O ANISOU 746 O THR A 87 2736 1291 1854 -297 190 -72 O ATOM 747 CB THR A 87 11.813 -18.405 11.172 1.00 18.20 C ANISOU 747 CB THR A 87 3424 1649 1840 -579 -107 37 C ATOM 748 OG1 THR A 87 13.164 -18.648 11.629 1.00 19.57 O ANISOU 748 OG1 THR A 87 3092 2151 2194 -357 404 -71 O ATOM 749 CG2 THR A 87 11.803 -17.321 10.131 1.00 24.23 C ANISOU 749 CG2 THR A 87 5236 1750 2218 -258 -17 257 C ATOM 750 N GLY A 88 10.753 -20.307 13.075 1.00 15.45 N ANISOU 750 N GLY A 88 2410 1268 2192 -323 122 -66 N ATOM 751 CA GLY A 88 10.855 -21.398 14.009 1.00 16.52 C ANISOU 751 CA GLY A 88 2505 1288 2483 -433 294 56 C ATOM 752 C GLY A 88 12.212 -21.824 14.298 1.00 15.91 C ANISOU 752 C GLY A 88 2503 1390 2151 -627 -22 291 C ATOM 753 O GLY A 88 12.431 -22.511 15.270 1.00 23.33 O ANISOU 753 O GLY A 88 3639 2576 2648 -837 -371 1058 O ATOM 754 N SER A 89 13.180 -21.543 13.464 1.00 15.18 N ANISOU 754 N SER A 89 2391 1276 2101 -280 20 -146 N ATOM 755 CA SER A 89 14.574 -21.874 13.647 1.00 16.98 C ANISOU 755 CA SER A 89 2447 1577 2427 -119 -94 -340 C ATOM 756 C SER A 89 15.373 -20.818 14.368 1.00 18.06 C ANISOU 756 C SER A 89 2454 1545 2862 -116 -276 -336 C ATOM 757 O SER A 89 16.567 -20.993 14.615 1.00 22.85 O ANISOU 757 O SER A 89 2475 2286 3922 49 -487 -892 O ATOM 758 CB ASER A 89 15.221 -22.226 12.337 0.65 18.40 C ANISOU 758 CB ASER A 89 2456 1681 2852 -221 218 -430 C ATOM 759 CB BSER A 89 15.170 -22.124 12.262 0.35 27.39 C ANISOU 759 CB BSER A 89 3353 3853 3200 743 426 -1504 C ATOM 760 OG ASER A 89 14.596 -23.388 11.844 0.65 21.27 O ANISOU 760 OG ASER A 89 2507 2099 3478 -89 235 -1299 O ATOM 761 OG BSER A 89 15.077 -21.082 11.311 0.35 40.13 O ANISOU 761 OG BSER A 89 5706 7043 2499 -216 1247 41 O ATOM 762 N SER A 90 14.763 -19.694 14.716 1.00 14.59 N ANISOU 762 N SER A 90 2487 1356 1702 -282 -141 -11 N ATOM 763 CA SER A 90 15.483 -18.650 15.424 1.00 14.70 C ANISOU 763 CA SER A 90 2556 1604 1424 -357 -45 -68 C ATOM 764 C SER A 90 15.880 -19.113 16.796 1.00 16.74 C ANISOU 764 C SER A 90 2919 1771 1670 -661 -250 145 C ATOM 765 O SER A 90 14.998 -19.572 17.540 1.00 20.41 O ANISOU 765 O SER A 90 3156 2770 1828 -893 -260 630 O ATOM 766 CB SER A 90 14.501 -17.481 15.537 1.00 15.28 C ANISOU 766 CB SER A 90 2608 1376 1821 -451 72 -130 C ATOM 767 OG SER A 90 15.132 -16.399 16.157 1.00 15.33 O ANISOU 767 OG SER A 90 2531 1561 1734 -572 31 -17 O ATOM 768 N LYS A 91 17.117 -18.890 17.182 1.00 16.82 N ANISOU 768 N LYS A 91 2838 1767 1787 -436 -319 188 N ATOM 769 CA LYS A 91 17.606 -19.267 18.501 1.00 18.50 C ANISOU 769 CA LYS A 91 3541 1805 1682 -368 -549 69 C ATOM 770 C LYS A 91 18.763 -18.362 18.862 1.00 17.23 C ANISOU 770 C LYS A 91 2989 1885 1673 -102 -333 18 C ATOM 771 O LYS A 91 19.815 -18.372 18.182 1.00 19.22 O ANISOU 771 O LYS A 91 3229 2260 1813 -68 19 -184 O ATOM 772 CB LYS A 91 18.046 -20.733 18.552 1.00 24.01 C ANISOU 772 CB LYS A 91 4333 1822 2967 -295 -1154 217 C ATOM 773 CG LYS A 91 18.477 -21.192 19.915 1.00 27.78 C ANISOU 773 CG LYS A 91 4561 2602 3391 -135 -1266 774 C ATOM 774 CD LYS A 91 19.147 -22.560 19.934 1.00 46.24 C ANISOU 774 CD LYS A 91 9864 2635 5070 1177 -2064 1096 C ATOM 775 CE LYS A 91 20.102 -22.668 21.115 1.00 83.41 C ANISOU 775 CE LYS A 91 15924 5120 10648 3234 -7627 2273 C ATOM 776 NZ LYS A 91 21.403 -23.305 20.724 1.00118.54 N ANISOU 776 NZ LYS A 91 14082 11356 19602 4662 -6391 7974 N ATOM 777 N TYR A 92 18.571 -17.516 19.862 1.00 16.04 N ANISOU 777 N TYR A 92 2224 1966 1904 -43 -280 -69 N ATOM 778 CA TYR A 92 19.561 -16.553 20.283 1.00 15.34 C ANISOU 778 CA TYR A 92 1958 2175 1697 21 -259 -150 C ATOM 779 C TYR A 92 20.941 -17.210 20.451 1.00 15.80 C ANISOU 779 C TYR A 92 2089 2268 1647 283 -163 -80 C ATOM 780 O TYR A 92 21.002 -18.266 21.081 1.00 19.70 O ANISOU 780 O TYR A 92 2935 2378 2173 420 -314 92 O ATOM 781 CB TYR A 92 19.092 -15.909 21.581 1.00 14.77 C ANISOU 781 CB TYR A 92 1837 2074 1702 -12 -12 -31 C ATOM 782 CG TYR A 92 20.001 -14.829 22.056 1.00 14.60 C ANISOU 782 CG TYR A 92 2053 1947 1546 25 -117 -14 C ATOM 783 CD1 TYR A 92 19.883 -13.544 21.590 1.00 14.69 C ANISOU 783 CD1 TYR A 92 1954 1983 1646 113 -219 -71 C ATOM 784 CD2 TYR A 92 21.013 -15.074 22.970 1.00 15.87 C ANISOU 784 CD2 TYR A 92 2332 2135 1564 83 -314 11 C ATOM 785 CE1 TYR A 92 20.747 -12.522 21.977 1.00 16.50 C ANISOU 785 CE1 TYR A 92 2295 1978 1996 -141 -121 -159 C ATOM 786 CE2 TYR A 92 21.874 -14.124 23.355 1.00 18.41 C ANISOU 786 CE2 TYR A 92 2682 2456 1858 52 -509 -390 C ATOM 787 CZ TYR A 92 21.752 -12.837 22.906 1.00 16.27 C ANISOU 787 CZ TYR A 92 2002 2323 1858 -161 -69 -376 C ATOM 788 OH TYR A 92 22.642 -11.912 23.383 1.00 21.80 O ANISOU 788 OH TYR A 92 2700 2887 2695 -551 -459 -477 O ATOM 789 N PRO A 93 22.021 -16.615 19.962 1.00 17.70 N ANISOU 789 N PRO A 93 1935 2627 2165 115 -255 -231 N ATOM 790 CA PRO A 93 22.127 -15.293 19.377 1.00 17.65 C ANISOU 790 CA PRO A 93 1882 2637 2188 -33 23 -225 C ATOM 791 C PRO A 93 21.922 -15.265 17.876 1.00 18.30 C ANISOU 791 C PRO A 93 2108 2769 2077 -9 133 -224 C ATOM 792 O PRO A 93 22.075 -14.204 17.250 1.00 21.64 O ANISOU 792 O PRO A 93 2854 2997 2370 -277 175 1 O ATOM 793 CB PRO A 93 23.592 -14.887 19.694 1.00 21.30 C ANISOU 793 CB PRO A 93 1874 3764 2455 -403 88 -124 C ATOM 794 CG PRO A 93 24.313 -16.212 19.590 1.00 27.58 C ANISOU 794 CG PRO A 93 1928 4553 3998 352 45 172 C ATOM 795 CD PRO A 93 23.371 -17.221 20.218 1.00 21.15 C ANISOU 795 CD PRO A 93 2049 3557 2431 644 -258 -139 C ATOM 796 N ASN A 94 21.586 -16.404 17.293 1.00 17.37 N ANISOU 796 N ASN A 94 2076 2652 1871 419 79 -127 N ATOM 797 CA ASN A 94 21.305 -16.545 15.871 1.00 19.36 C ANISOU 797 CA ASN A 94 2335 3100 1923 523 -121 -286 C ATOM 798 C ASN A 94 19.847 -16.369 15.574 1.00 16.32 C ANISOU 798 C ASN A 94 2218 2350 1633 166 129 -358 C ATOM 799 O ASN A 94 19.115 -17.295 15.239 1.00 18.50 O ANISOU 799 O ASN A 94 2750 2166 2114 65 -102 -400 O ATOM 800 CB ASN A 94 21.849 -17.862 15.299 1.00 25.07 C ANISOU 800 CB ASN A 94 2822 3975 2730 1080 -2 -1068 C ATOM 801 CG ASN A 94 23.353 -17.989 15.561 1.00 30.46 C ANISOU 801 CG ASN A 94 2808 4805 3960 1370 75 -953 C ATOM 802 OD1 ASN A 94 23.774 -18.942 16.206 1.00 45.77 O ANISOU 802 OD1 ASN A 94 3615 5993 7782 1937 -451 767 O ATOM 803 ND2 ASN A 94 24.101 -16.989 15.138 1.00 38.64 N ANISOU 803 ND2 ASN A 94 2658 6914 5109 1006 802 345 N ATOM 804 N CYS A 95 19.416 -15.120 15.767 1.00 15.84 N ANISOU 804 N CYS A 95 1969 2208 1843 18 -110 -341 N ATOM 805 CA CYS A 95 18.064 -14.732 15.539 1.00 13.99 C ANISOU 805 CA CYS A 95 1973 1838 1505 -215 20 -86 C ATOM 806 C CYS A 95 17.714 -14.768 14.066 1.00 14.80 C ANISOU 806 C CYS A 95 2153 2071 1399 -276 0 172 C ATOM 807 O CYS A 95 18.529 -14.332 13.236 1.00 20.35 O ANISOU 807 O CYS A 95 2679 3436 1617 -1043 234 33 O ATOM 808 CB CYS A 95 17.737 -13.402 16.116 1.00 14.01 C ANISOU 808 CB CYS A 95 2111 1598 1613 -106 -61 129 C ATOM 809 SG CYS A 95 18.166 -13.176 17.842 1.00 14.30 S ANISOU 809 SG CYS A 95 2057 1728 1650 -154 -89 -98 S ATOM 810 N ALA A 96 16.598 -15.285 13.614 1.00 13.30 N ANISOU 810 N ALA A 96 2131 1567 1357 -117 19 54 N ATOM 811 CA ALA A 96 16.219 -15.512 12.280 1.00 13.73 C ANISOU 811 CA ALA A 96 2316 1678 1222 59 55 -64 C ATOM 812 C ALA A 96 14.766 -15.071 12.051 1.00 12.17 C ANISOU 812 C ALA A 96 2147 1224 1254 -269 46 10 C ATOM 813 O ALA A 96 13.894 -15.297 12.876 1.00 13.75 O ANISOU 813 O ALA A 96 2298 1558 1366 -242 169 228 O ATOM 814 CB ALA A 96 16.374 -16.996 11.917 1.00 18.17 C ANISOU 814 CB ALA A 96 3171 1859 1872 448 -150 -366 C ATOM 815 N TYR A 97 14.570 -14.443 10.910 1.00 12.30 N ANISOU 815 N TYR A 97 2151 1335 1188 -52 183 56 N ATOM 816 CA TYR A 97 13.328 -13.755 10.579 1.00 12.36 C ANISOU 816 CA TYR A 97 2157 1280 1259 -133 138 -70 C ATOM 817 C TYR A 97 12.866 -14.044 9.187 1.00 12.43 C ANISOU 817 C TYR A 97 2286 1317 1122 -232 85 127 C ATOM 818 O TYR A 97 13.666 -14.187 8.252 1.00 14.75 O ANISOU 818 O TYR A 97 2412 1997 1196 -184 127 -106 O ATOM 819 CB TYR A 97 13.543 -12.203 10.675 1.00 12.61 C ANISOU 819 CB TYR A 97 2372 1217 1204 -53 111 3 C ATOM 820 CG TYR A 97 13.877 -11.779 12.082 1.00 11.76 C ANISOU 820 CG TYR A 97 2109 1211 1149 -88 94 -1 C ATOM 821 CD1 TYR A 97 12.833 -11.506 12.967 1.00 12.31 C ANISOU 821 CD1 TYR A 97 2030 1292 1355 -149 66 -42 C ATOM 822 CD2 TYR A 97 15.160 -11.734 12.560 1.00 12.47 C ANISOU 822 CD2 TYR A 97 2112 1334 1293 -80 168 39 C ATOM 823 CE1 TYR A 97 13.104 -11.197 14.296 1.00 12.47 C ANISOU 823 CE1 TYR A 97 1983 1526 1229 13 88 -124 C ATOM 824 CE2 TYR A 97 15.438 -11.442 13.890 1.00 12.42 C ANISOU 824 CE2 TYR A 97 1998 1390 1331 30 110 -35 C ATOM 825 CZ TYR A 97 14.415 -11.182 14.751 1.00 11.77 C ANISOU 825 CZ TYR A 97 1991 1268 1213 -44 136 -13 C ATOM 826 OH TYR A 97 14.710 -10.890 16.054 1.00 14.73 O ANISOU 826 OH TYR A 97 2246 2147 1203 124 -82 -113 O ATOM 827 N LYS A 98 11.565 -14.054 9.019 1.00 12.75 N ANISOU 827 N LYS A 98 2295 1245 1303 -122 65 -56 N ATOM 828 CA LYS A 98 10.859 -14.034 7.737 1.00 13.02 C ANISOU 828 CA LYS A 98 2354 1322 1270 -67 -27 -39 C ATOM 829 C LYS A 98 10.588 -12.572 7.370 1.00 12.54 C ANISOU 829 C LYS A 98 2243 1316 1206 -135 39 -158 C ATOM 830 O LYS A 98 10.087 -11.793 8.185 1.00 14.23 O ANISOU 830 O LYS A 98 2591 1399 1418 73 192 -130 O ATOM 831 CB LYS A 98 9.550 -14.798 7.808 1.00 16.88 C ANISOU 831 CB LYS A 98 2799 1610 2004 -509 -350 -2 C ATOM 832 CG LYS A 98 8.759 -14.778 6.543 1.00 21.44 C ANISOU 832 CG LYS A 98 3100 2470 2577 -493 -833 296 C ATOM 833 CD LYS A 98 7.404 -15.436 6.586 1.00 49.87 C ANISOU 833 CD LYS A 98 5441 7550 5958 -4205 -2746 1734 C ATOM 834 CE LYS A 98 7.200 -16.347 5.398 1.00 65.99 C ANISOU 834 CE LYS A 98 7691 8638 8746 -4231 -4554 -196 C ATOM 835 NZ LYS A 98 6.017 -17.225 5.591 1.00 70.22 N ANISOU 835 NZ LYS A 98 5814 11196 9669 -3613 2029 -7201 N ATOM 836 N THR A 99 10.887 -12.222 6.130 1.00 12.17 N ANISOU 836 N THR A 99 2130 1213 1282 -98 52 -150 N ATOM 837 CA THR A 99 10.696 -10.915 5.566 1.00 11.48 C ANISOU 837 CA THR A 99 2038 1221 1104 -18 6 -217 C ATOM 838 C THR A 99 9.421 -10.899 4.729 1.00 12.58 C ANISOU 838 C THR A 99 2147 1414 1219 -76 -145 -227 C ATOM 839 O THR A 99 9.332 -11.697 3.793 1.00 15.23 O ANISOU 839 O THR A 99 2413 1819 1555 14 -369 -492 O ATOM 840 CB THR A 99 11.913 -10.553 4.678 1.00 12.37 C ANISOU 840 CB THR A 99 2146 1421 1133 -8 77 -88 C ATOM 841 OG1 THR A 99 13.095 -10.509 5.447 1.00 13.13 O ANISOU 841 OG1 THR A 99 2017 1551 1422 18 -21 -53 O ATOM 842 CG2 THR A 99 11.776 -9.229 3.975 1.00 13.95 C ANISOU 842 CG2 THR A 99 2307 1592 1400 -22 43 121 C ATOM 843 N THR A 100 8.532 -9.969 4.965 1.00 13.04 N ANISOU 843 N THR A 100 2034 1495 1426 -81 -267 -187 N ATOM 844 CA THR A 100 7.298 -9.812 4.198 1.00 14.73 C ANISOU 844 CA THR A 100 2219 1694 1685 27 -440 -249 C ATOM 845 C THR A 100 7.160 -8.382 3.787 1.00 14.26 C ANISOU 845 C THR A 100 2034 1700 1686 -4 -508 -221 C ATOM 846 O THR A 100 7.238 -7.489 4.612 1.00 16.22 O ANISOU 846 O THR A 100 2926 1656 1581 -92 -396 -259 O ATOM 847 CB THR A 100 6.044 -10.255 5.007 1.00 19.62 C ANISOU 847 CB THR A 100 2027 2236 3190 -404 -420 279 C ATOM 848 OG1 THR A 100 6.258 -11.616 5.389 1.00 20.77 O ANISOU 848 OG1 THR A 100 2708 2161 3023 -459 -366 70 O ATOM 849 CG2 THR A 100 4.850 -10.173 4.090 1.00 28.31 C ANISOU 849 CG2 THR A 100 2473 3858 4423 -899 -1042 1282 C ATOM 850 N GLN A 101 6.931 -8.098 2.515 1.00 17.29 N ANISOU 850 N GLN A 101 3186 1668 1714 224 -812 -310 N ATOM 851 CA GLN A 101 6.733 -6.769 2.002 1.00 16.32 C ANISOU 851 CA GLN A 101 2746 1756 1700 214 -654 -173 C ATOM 852 C GLN A 101 5.250 -6.432 2.107 1.00 16.10 C ANISOU 852 C GLN A 101 2617 1793 1706 -60 -594 -200 C ATOM 853 O GLN A 101 4.394 -7.263 1.840 1.00 20.62 O ANISOU 853 O GLN A 101 2864 2029 2944 -147 -794 -552 O ATOM 854 CB GLN A 101 7.136 -6.732 0.522 1.00 19.70 C ANISOU 854 CB GLN A 101 3196 2561 1727 511 -396 -131 C ATOM 855 CG GLN A 101 8.546 -7.109 0.134 1.00 23.90 C ANISOU 855 CG GLN A 101 3435 3250 2394 704 -66 -422 C ATOM 856 CD GLN A 101 8.693 -7.205 -1.369 1.00 31.82 C ANISOU 856 CD GLN A 101 3735 6047 2309 248 69 -730 C ATOM 857 OE1 GLN A 101 7.778 -7.513 -2.125 1.00 47.03 O ANISOU 857 OE1 GLN A 101 4597 10505 2766 -1369 26 -1491 O ATOM 858 NE2 GLN A 101 9.886 -6.885 -1.844 1.00 43.38 N ANISOU 858 NE2 GLN A 101 5016 9009 2457 -1977 415 -914 N ATOM 859 N ALA A 102 4.949 -5.161 2.369 1.00 15.89 N ANISOU 859 N ALA A 102 2417 1876 1746 30 -520 -269 N ATOM 860 CA ALA A 102 3.563 -4.723 2.407 1.00 16.61 C ANISOU 860 CA ALA A 102 2345 2004 1964 -99 -319 -273 C ATOM 861 C ALA A 102 3.453 -3.236 2.059 1.00 14.53 C ANISOU 861 C ALA A 102 1956 2031 1535 -30 -413 -332 C ATOM 862 O ALA A 102 4.435 -2.512 2.126 1.00 15.22 O ANISOU 862 O ALA A 102 2012 2005 1767 -4 -521 -210 O ATOM 863 CB ALA A 102 2.886 -5.058 3.698 1.00 20.25 C ANISOU 863 CB ALA A 102 3002 2177 2516 -275 196 -14 C ATOM 864 N ASN A 103 2.245 -2.761 1.787 1.00 16.07 N ANISOU 864 N ASN A 103 1915 2079 2112 -38 -343 -492 N ATOM 865 CA ASN A 103 1.944 -1.365 1.571 1.00 15.51 C ANISOU 865 CA ASN A 103 2016 2188 1690 95 -297 -295 C ATOM 866 C ASN A 103 0.691 -1.100 2.364 1.00 15.57 C ANISOU 866 C ASN A 103 1735 2312 1869 6 -438 -516 C ATOM 867 O ASN A 103 -0.369 -1.553 2.022 1.00 19.94 O ANISOU 867 O ASN A 103 1982 3199 2396 -264 -350 -966 O ATOM 868 CB AASN A 103 1.742 -1.034 0.101 0.32 17.91 C ANISOU 868 CB AASN A 103 2578 2575 1651 267 -384 -506 C ATOM 869 CB BASN A 103 1.818 -1.149 0.079 0.68 21.67 C ANISOU 869 CB BASN A 103 2656 3771 1805 93 -173 166 C ATOM 870 CG AASN A 103 3.004 -1.098 -0.718 0.32 17.68 C ANISOU 870 CG AASN A 103 2361 3021 1334 311 -627 -93 C ATOM 871 CG BASN A 103 1.682 0.323 -0.240 0.68 33.72 C ANISOU 871 CG BASN A 103 6045 4051 2716 -682 -2339 969 C ATOM 872 OD1AASN A 103 3.262 -2.103 -1.393 0.32 30.12 O ANISOU 872 OD1AASN A 103 3632 4944 2868 585 242 -1769 O ATOM 873 OD1BASN A 103 2.669 1.012 -0.248 0.68 62.19 O ANISOU 873 OD1BASN A 103 9654 6365 7610 -4144 -5857 3857 O ATOM 874 ND2AASN A 103 3.801 -0.053 -0.672 0.32 25.49 N ANISOU 874 ND2AASN A 103 3727 4678 1279 -1350 -852 534 N ATOM 875 ND2BASN A 103 0.430 0.673 -0.497 0.68 50.71 N ANISOU 875 ND2BASN A 103 6001 6380 6889 2751 2618 3810 N ATOM 876 N LYS A 104 0.825 -0.386 3.500 1.00 14.45 N ANISOU 876 N LYS A 104 1704 2119 1668 -64 -217 -306 N ATOM 877 CA LYS A 104 -0.239 -0.284 4.478 1.00 14.66 C ANISOU 877 CA LYS A 104 1694 2101 1773 -189 -164 -249 C ATOM 878 C LYS A 104 -0.185 1.113 5.104 1.00 13.84 C ANISOU 878 C LYS A 104 1518 2104 1637 -78 -197 -204 C ATOM 879 O LYS A 104 0.823 1.787 5.073 1.00 14.60 O ANISOU 879 O LYS A 104 1702 2131 1716 -237 -10 -154 O ATOM 880 CB ALYS A 104 -0.203 -1.358 5.536 0.58 17.28 C ATOM 881 CB BLYS A 104 0.056 -1.293 5.614 0.42 16.76 C ATOM 882 CG ALYS A 104 -0.698 -2.706 4.970 0.58 20.54 C ATOM 883 CG BLYS A 104 0.128 -2.745 5.163 0.42 16.55 C ATOM 884 CD ALYS A 104 -0.642 -3.720 6.123 0.58 43.32 C ATOM 885 CD BLYS A 104 -0.967 -3.608 5.765 0.42 36.89 C ATOM 886 CE ALYS A 104 -1.904 -4.565 6.203 0.58 50.19 C ATOM 887 CE BLYS A 104 -1.146 -4.972 5.112 0.42 24.49 C ATOM 888 NZ ALYS A 104 -1.615 -6.007 6.422 0.58 70.06 N ATOM 889 NZ BLYS A 104 -2.459 -5.045 4.362 0.42 49.65 N ATOM 890 N HIS A 105 -1.305 1.504 5.688 1.00 14.54 N ANISOU 890 N HIS A 105 1506 2159 1859 -183 -165 -290 N ATOM 891 CA HIS A 105 -1.290 2.674 6.581 1.00 14.32 C ANISOU 891 CA HIS A 105 1711 2060 1670 -5 -147 -163 C ATOM 892 C HIS A 105 -0.543 2.318 7.854 1.00 13.43 C ANISOU 892 C HIS A 105 1623 1840 1639 -267 -50 -8 C ATOM 893 O HIS A 105 -0.601 1.163 8.274 1.00 16.71 O ANISOU 893 O HIS A 105 2270 1924 2155 -503 -371 227 O ATOM 894 CB HIS A 105 -2.701 3.102 6.957 1.00 17.14 C ANISOU 894 CB HIS A 105 1757 2546 2209 243 -136 -173 C ATOM 895 CG HIS A 105 -3.587 3.442 5.802 1.00 17.65 C ANISOU 895 CG HIS A 105 1643 2839 2222 131 -150 -200 C ATOM 896 ND1 HIS A 105 -3.724 4.709 5.292 1.00 21.04 N ANISOU 896 ND1 HIS A 105 1957 3123 2913 177 -504 268 N ATOM 897 CD2 HIS A 105 -4.356 2.627 5.048 1.00 25.06 C ANISOU 897 CD2 HIS A 105 2469 3480 3571 -251 -1238 -132 C ATOM 898 CE1 HIS A 105 -4.539 4.693 4.257 1.00 25.69 C ANISOU 898 CE1 HIS A 105 2254 3972 3537 326 -1036 405 C ATOM 899 NE2 HIS A 105 -4.956 3.449 4.088 1.00 26.37 N ANISOU 899 NE2 HIS A 105 2372 4282 3366 -4 -1098 15 N ATOM 900 N ILE A 106 0.154 3.215 8.459 1.00 12.96 N ANISOU 900 N ILE A 106 1786 1666 1473 -70 -88 -10 N ATOM 901 CA ILE A 106 0.828 3.058 9.690 1.00 12.51 C ANISOU 901 CA ILE A 106 1715 1685 1354 96 -38 -105 C ATOM 902 C ILE A 106 0.110 3.831 10.819 1.00 12.03 C ANISOU 902 C ILE A 106 1638 1512 1421 12 -16 -9 C ATOM 903 O ILE A 106 -0.484 4.873 10.575 1.00 13.81 O ANISOU 903 O ILE A 106 1852 1835 1561 276 47 118 O ATOM 904 CB ILE A 106 2.325 3.388 9.647 1.00 13.61 C ANISOU 904 CB ILE A 106 1724 2018 1429 171 24 -33 C ATOM 905 CG1 ILE A 106 2.611 4.881 9.470 1.00 15.18 C ANISOU 905 CG1 ILE A 106 1755 2156 1855 -127 50 80 C ATOM 906 CG2 ILE A 106 2.989 2.529 8.582 1.00 17.11 C ANISOU 906 CG2 ILE A 106 2013 2715 1773 485 154 -351 C ATOM 907 CD1 ILE A 106 4.058 5.242 9.698 1.00 17.14 C ANISOU 907 CD1 ILE A 106 1628 2865 2018 -249 46 122 C ATOM 908 N ILE A 107 0.239 3.312 12.023 1.00 11.60 N ANISOU 908 N ILE A 107 1488 1532 1386 30 -23 -51 N ATOM 909 CA ILE A 107 -0.268 3.946 13.224 1.00 11.67 C ANISOU 909 CA ILE A 107 1434 1599 1401 90 5 -156 C ATOM 910 C ILE A 107 0.902 4.071 14.184 1.00 11.20 C ANISOU 910 C ILE A 107 1344 1521 1391 87 53 -72 C ATOM 911 O ILE A 107 1.522 3.063 14.518 1.00 12.46 O ANISOU 911 O ILE A 107 1539 1535 1661 129 -60 -56 O ATOM 912 CB ILE A 107 -1.432 3.181 13.879 1.00 12.97 C ANISOU 912 CB ILE A 107 1464 1913 1550 -74 44 -15 C ATOM 913 CG1 ILE A 107 -2.625 3.055 12.867 1.00 16.08 C ANISOU 913 CG1 ILE A 107 1662 2549 1899 -351 -146 -202 C ATOM 914 CG2 ILE A 107 -1.880 3.898 15.150 1.00 14.32 C ANISOU 914 CG2 ILE A 107 1497 2208 1737 -2 199 -199 C ATOM 915 CD1 ILE A 107 -3.728 2.179 13.358 1.00 22.78 C ANISOU 915 CD1 ILE A 107 1961 3528 3165 -891 -238 1 C ATOM 916 N VAL A 108 1.179 5.302 14.617 1.00 11.50 N ANISOU 916 N VAL A 108 1354 1537 1479 88 -21 -142 N ATOM 917 CA VAL A 108 2.297 5.593 15.496 1.00 11.23 C ANISOU 917 CA VAL A 108 1230 1628 1411 53 -53 -102 C ATOM 918 C VAL A 108 1.766 6.376 16.702 1.00 11.15 C ANISOU 918 C VAL A 108 1211 1633 1394 -23 7 -75 C ATOM 919 O VAL A 108 0.750 7.046 16.615 1.00 14.20 O ANISOU 919 O VAL A 108 1503 2309 1584 424 -90 -304 O ATOM 920 CB VAL A 108 3.415 6.394 14.814 1.00 12.76 C ANISOU 920 CB VAL A 108 1395 1942 1511 -122 87 -201 C ATOM 921 CG1 VAL A 108 4.064 5.603 13.691 1.00 15.30 C ANISOU 921 CG1 VAL A 108 1696 2463 1653 104 282 -208 C ATOM 922 CG2 VAL A 108 2.921 7.718 14.284 1.00 16.61 C ANISOU 922 CG2 VAL A 108 2264 1850 2196 -114 186 163 C ATOM 923 N ALA A 109 2.479 6.270 17.812 1.00 11.43 N ANISOU 923 N ALA A 109 1280 1597 1467 27 -23 -172 N ATOM 924 CA ALA A 109 2.217 7.110 18.980 1.00 11.36 C ANISOU 924 CA ALA A 109 1284 1651 1383 -122 112 -183 C ATOM 925 C ALA A 109 3.242 8.254 18.967 1.00 11.47 C ANISOU 925 C ALA A 109 1339 1619 1400 -47 167 -177 C ATOM 926 O ALA A 109 4.411 8.010 18.659 1.00 12.81 O ANISOU 926 O ALA A 109 1217 1766 1885 -78 200 -211 O ATOM 927 CB ALA A 109 2.287 6.359 20.273 1.00 14.37 C ANISOU 927 CB ALA A 109 1916 2001 1543 -273 145 -34 C ATOM 928 N CYS A 110 2.783 9.447 19.288 1.00 12.29 N ANISOU 928 N CYS A 110 1383 1644 1642 -90 316 -321 N ATOM 929 CA CYS A 110 3.627 10.663 19.249 1.00 12.36 C ANISOU 929 CA CYS A 110 1602 1636 1458 -233 351 -179 C ATOM 930 C CYS A 110 3.699 11.284 20.623 1.00 13.59 C ANISOU 930 C CYS A 110 1777 1823 1565 -288 411 -323 C ATOM 931 O CYS A 110 2.772 11.236 21.406 1.00 15.41 O ANISOU 931 O CYS A 110 1964 2130 1759 -280 701 -302 O ATOM 932 CB CYS A 110 3.028 11.651 18.258 1.00 14.73 C ANISOU 932 CB CYS A 110 2223 1622 1751 16 108 -284 C ATOM 933 SG CYS A 110 2.926 10.939 16.595 1.00 14.63 S ANISOU 933 SG CYS A 110 2208 1725 1624 -6 -3 -140 S ATOM 934 N GLU A 111 4.865 11.913 20.898 1.00 14.00 N ANISOU 934 N GLU A 111 1812 1949 1559 -395 345 -408 N ATOM 935 CA GLU A 111 5.119 12.582 22.151 1.00 15.13 C ANISOU 935 CA GLU A 111 1995 2288 1465 -470 366 -401 C ATOM 936 C GLU A 111 6.110 13.726 21.869 1.00 15.48 C ANISOU 936 C GLU A 111 1915 2317 1649 -449 249 -550 C ATOM 937 O GLU A 111 6.897 13.631 20.962 1.00 17.24 O ANISOU 937 O GLU A 111 2314 2468 1769 -777 451 -451 O ATOM 938 CB GLU A 111 5.766 11.626 23.173 1.00 19.39 C ANISOU 938 CB GLU A 111 3142 2816 1410 -222 201 -240 C ATOM 939 CG GLU A 111 4.940 10.485 23.692 1.00 24.45 C ANISOU 939 CG GLU A 111 4207 3029 2053 -190 882 194 C ATOM 940 CD GLU A 111 5.544 9.672 24.826 1.00 29.24 C ANISOU 940 CD GLU A 111 5147 4088 1875 -1038 -101 535 C ATOM 941 OE1 GLU A 111 6.566 10.088 25.395 1.00 53.46 O ANISOU 941 OE1 GLU A 111 8000 8124 4187 -3036 -2596 862 O ATOM 942 OE2 GLU A 111 4.993 8.565 25.103 1.00 41.62 O ANISOU 942 OE2 GLU A 111 7204 4480 4131 -1412 -299 1857 O ATOM 943 N GLY A 112 6.139 14.692 22.756 1.00 19.65 N ANISOU 943 N GLY A 112 2918 2484 2064 -817 486 -795 N ATOM 944 CA GLY A 112 7.171 15.673 22.806 1.00 21.42 C ANISOU 944 CA GLY A 112 3237 2767 2134 -1077 145 -772 C ATOM 945 C GLY A 112 6.931 16.984 22.142 1.00 20.02 C ANISOU 945 C GLY A 112 3028 2659 1919 -1014 634 -871 C ATOM 946 O GLY A 112 5.857 17.209 21.612 1.00 21.43 O ANISOU 946 O GLY A 112 2897 2604 2643 -608 744 -820 O ATOM 947 N ASN A 113 7.953 17.839 22.248 1.00 23.23 N ANISOU 947 N ASN A 113 3523 2887 2416 -1414 688 -973 N ATOM 948 CA ASN A 113 7.967 19.087 21.522 1.00 26.67 C ANISOU 948 CA ASN A 113 4355 2580 3199 -1246 1610 -1059 C ATOM 949 C ASN A 113 9.374 19.236 20.952 1.00 30.34 C ANISOU 949 C ASN A 113 4439 4283 2807 -2515 1366 -1469 C ATOM 950 O ASN A 113 10.295 19.459 21.780 1.00 36.12 O ANISOU 950 O ASN A 113 5031 5357 3335 -2933 919 -1690 O ATOM 951 CB ASN A 113 7.500 20.267 22.362 1.00 35.81 C ANISOU 951 CB ASN A 113 7114 2973 3521 -1101 2016 -1607 C ATOM 952 CG ASN A 113 7.822 21.500 21.530 1.00 47.14 C ANISOU 952 CG ASN A 113 9689 2488 5735 -1592 906 -904 C ATOM 953 OD1 ASN A 113 8.606 22.302 22.078 1.00 62.21 O ANISOU 953 OD1 ASN A 113 8598 4569 10473 -2795 -1295 900 O ATOM 954 ND2 ASN A 113 7.342 21.616 20.322 1.00 41.71 N ANISOU 954 ND2 ASN A 113 7116 3328 5403 123 2199 -155 N ATOM 955 N PRO A 114 9.626 19.077 19.671 1.00 25.86 N ANISOU 955 N PRO A 114 3876 3099 2852 -1693 1225 -1060 N ATOM 956 CA PRO A 114 8.636 18.789 18.631 1.00 22.78 C ANISOU 956 CA PRO A 114 3721 2321 2613 -1097 1132 -651 C ATOM 957 C PRO A 114 7.900 17.449 18.770 1.00 18.33 C ANISOU 957 C PRO A 114 2787 2076 2102 -562 595 -280 C ATOM 958 O PRO A 114 8.422 16.573 19.433 1.00 18.50 O ANISOU 958 O PRO A 114 2547 2337 2145 -561 216 -369 O ATOM 959 CB PRO A 114 9.442 18.733 17.324 1.00 25.50 C ANISOU 959 CB PRO A 114 3936 3005 2750 -1558 1369 -664 C ATOM 960 CG PRO A 114 10.850 18.890 17.727 1.00 34.44 C ANISOU 960 CG PRO A 114 3775 6508 2803 -774 1191 -449 C ATOM 961 CD PRO A 114 11.026 19.196 19.156 1.00 29.35 C ANISOU 961 CD PRO A 114 3980 4100 3073 -2152 1314 -831 C ATOM 962 N TYR A 115 6.672 17.415 18.322 1.00 17.71 N ANISOU 962 N TYR A 115 2696 1600 2432 -125 551 -347 N ATOM 963 CA TYR A 115 5.812 16.248 18.560 1.00 16.11 C ANISOU 963 CA TYR A 115 2283 1708 2129 -3 616 -320 C ATOM 964 C TYR A 115 6.097 15.229 17.455 1.00 14.79 C ANISOU 964 C TYR A 115 2299 1443 1879 -24 419 -99 C ATOM 965 O TYR A 115 5.836 15.464 16.297 1.00 18.14 O ANISOU 965 O TYR A 115 3062 1920 1909 331 241 -145 O ATOM 966 CB TYR A 115 4.406 16.758 18.461 1.00 19.17 C ANISOU 966 CB TYR A 115 2428 2065 2789 212 646 -328 C ATOM 967 CG TYR A 115 3.297 15.845 18.965 1.00 17.69 C ANISOU 967 CG TYR A 115 2247 2138 2335 143 576 -634 C ATOM 968 CD1 TYR A 115 3.274 15.420 20.278 1.00 18.12 C ANISOU 968 CD1 TYR A 115 2191 2392 2302 -73 380 -575 C ATOM 969 CD2 TYR A 115 2.242 15.527 18.140 1.00 18.12 C ANISOU 969 CD2 TYR A 115 2638 2038 2207 144 358 -526 C ATOM 970 CE1 TYR A 115 2.232 14.633 20.731 1.00 19.09 C ANISOU 970 CE1 TYR A 115 2331 2477 2446 -170 387 -411 C ATOM 971 CE2 TYR A 115 1.160 14.760 18.586 1.00 18.72 C ANISOU 971 CE2 TYR A 115 2336 2185 2591 165 279 -589 C ATOM 972 CZ TYR A 115 1.181 14.344 19.901 1.00 18.32 C ANISOU 972 CZ TYR A 115 2148 2328 2484 -60 534 -555 C ATOM 973 OH TYR A 115 0.192 13.593 20.484 1.00 21.66 O ANISOU 973 OH TYR A 115 2402 2908 2920 -468 656 -717 O ATOM 974 N VAL A 116 6.714 14.122 17.835 1.00 13.18 N ANISOU 974 N VAL A 116 1918 1560 1531 -201 332 -236 N ATOM 975 CA VAL A 116 7.301 13.176 16.911 1.00 12.63 C ANISOU 975 CA VAL A 116 1807 1458 1534 -15 362 -21 C ATOM 976 C VAL A 116 6.921 11.751 17.269 1.00 11.74 C ANISOU 976 C VAL A 116 1663 1461 1337 -198 223 -128 C ATOM 977 O VAL A 116 6.551 11.436 18.421 1.00 12.21 O ANISOU 977 O VAL A 116 1647 1645 1348 -202 318 -200 O ATOM 978 CB VAL A 116 8.840 13.311 16.852 1.00 14.45 C ANISOU 978 CB VAL A 116 1785 1497 2210 -212 420 26 C ATOM 979 CG1 VAL A 116 9.219 14.644 16.216 1.00 18.86 C ANISOU 979 CG1 VAL A 116 2488 1862 2814 -344 762 460 C ATOM 980 CG2 VAL A 116 9.449 13.107 18.198 1.00 16.65 C ANISOU 980 CG2 VAL A 116 1914 1853 2560 -288 -19 102 C ATOM 981 N PRO A 117 7.065 10.807 16.338 1.00 11.98 N ANISOU 981 N PRO A 117 1728 1510 1315 -121 324 -94 N ATOM 982 CA PRO A 117 6.789 9.418 16.634 1.00 11.47 C ANISOU 982 CA PRO A 117 1465 1481 1410 -219 200 -154 C ATOM 983 C PRO A 117 7.799 8.827 17.613 1.00 11.38 C ANISOU 983 C PRO A 117 1363 1476 1485 -100 218 -260 C ATOM 984 O PRO A 117 8.996 8.987 17.469 1.00 13.66 O ANISOU 984 O PRO A 117 1296 2005 1889 -198 269 -7 O ATOM 985 CB PRO A 117 6.848 8.686 15.293 1.00 14.02 C ANISOU 985 CB PRO A 117 1986 1847 1496 52 91 -385 C ATOM 986 CG PRO A 117 6.797 9.732 14.312 1.00 18.69 C ANISOU 986 CG PRO A 117 3764 2009 1328 -43 255 -341 C ATOM 987 CD PRO A 117 7.373 10.999 14.898 1.00 14.47 C ANISOU 987 CD PRO A 117 2257 1935 1307 6 471 -46 C ATOM 988 N VAL A 118 7.249 8.082 18.575 1.00 11.84 N ANISOU 988 N VAL A 118 1238 1782 1478 -100 111 0 N ATOM 989 CA VAL A 118 8.064 7.390 19.559 1.00 12.44 C ANISOU 989 CA VAL A 118 1224 1833 1668 -10 -111 -147 C ATOM 990 C VAL A 118 7.749 5.886 19.630 1.00 12.64 C ANISOU 990 C VAL A 118 1386 1818 1597 23 -68 17 C ATOM 991 O VAL A 118 8.473 5.184 20.298 1.00 17.32 O ANISOU 991 O VAL A 118 1833 2027 2723 -32 -703 244 O ATOM 992 CB VAL A 118 7.979 8.011 20.954 1.00 14.67 C ANISOU 992 CB VAL A 118 1799 2152 1622 -122 -249 -180 C ATOM 993 CG1 VAL A 118 8.541 9.436 20.887 1.00 17.86 C ANISOU 993 CG1 VAL A 118 2505 2198 2083 -373 -324 -458 C ATOM 994 CG2 VAL A 118 6.534 7.999 21.500 1.00 17.36 C ANISOU 994 CG2 VAL A 118 2108 2774 1716 -87 261 -403 C ATOM 995 N HIS A 119 6.688 5.431 18.996 1.00 12.39 N ANISOU 995 N HIS A 119 1495 1745 1467 -52 -51 0 N ATOM 996 CA HIS A 119 6.291 4.033 19.093 1.00 12.35 C ANISOU 996 CA HIS A 119 1601 1588 1502 66 -36 12 C ATOM 997 C HIS A 119 5.555 3.699 17.828 1.00 12.07 C ANISOU 997 C HIS A 119 1449 1630 1505 37 -13 71 C ATOM 998 O HIS A 119 4.718 4.464 17.349 1.00 13.63 O ANISOU 998 O HIS A 119 1741 1718 1719 267 -188 -220 O ATOM 999 CB HIS A 119 5.429 3.851 20.309 1.00 16.69 C ANISOU 999 CB HIS A 119 2179 2494 1670 -237 319 139 C ATOM 1000 CG HIS A 119 4.549 2.673 20.340 1.00 19.92 C ANISOU 1000 CG HIS A 119 2698 2921 1950 -579 366 176 C ATOM 1001 ND1 HIS A 119 5.037 1.478 20.721 1.00 23.94 N ANISOU 1001 ND1 HIS A 119 3695 2730 2670 -573 274 295 N ATOM 1002 CD2 HIS A 119 3.252 2.513 20.000 1.00 23.62 C ANISOU 1002 CD2 HIS A 119 3064 3283 2625 -1055 -205 55 C ATOM 1003 CE1 HIS A 119 4.044 0.584 20.650 1.00 26.96 C ANISOU 1003 CE1 HIS A 119 4233 3354 2657 -1206 -64 785 C ATOM 1004 NE2 HIS A 119 2.937 1.211 20.224 1.00 24.36 N ANISOU 1004 NE2 HIS A 119 3838 3209 2208 -1093 201 -196 N ATOM 1005 N PHE A 120 5.816 2.507 17.274 1.00 12.43 N ANISOU 1005 N PHE A 120 1386 1671 1664 146 -90 -53 N ATOM 1006 CA PHE A 120 5.089 1.957 16.129 1.00 11.67 C ANISOU 1006 CA PHE A 120 1352 1585 1496 108 35 23 C ATOM 1007 C PHE A 120 3.994 1.043 16.653 1.00 11.54 C ANISOU 1007 C PHE A 120 1404 1601 1380 147 48 7 C ATOM 1008 O PHE A 120 4.290 0.030 17.272 1.00 14.47 O ANISOU 1008 O PHE A 120 1739 1732 2028 166 166 400 O ATOM 1009 CB PHE A 120 6.063 1.204 15.224 1.00 13.06 C ANISOU 1009 CB PHE A 120 1450 1827 1686 89 135 -72 C ATOM 1010 CG PHE A 120 5.418 0.806 13.907 1.00 13.57 C ANISOU 1010 CG PHE A 120 1503 2022 1629 283 182 -178 C ATOM 1011 CD1 PHE A 120 4.652 -0.334 13.777 1.00 16.44 C ANISOU 1011 CD1 PHE A 120 1784 2410 2051 -121 303 -551 C ATOM 1012 CD2 PHE A 120 5.609 1.618 12.796 1.00 17.46 C ANISOU 1012 CD2 PHE A 120 2232 2645 1758 186 143 109 C ATOM 1013 CE1 PHE A 120 4.042 -0.633 12.569 1.00 18.89 C ANISOU 1013 CE1 PHE A 120 1988 2956 2232 -111 212 -676 C ATOM 1014 CE2 PHE A 120 5.004 1.314 11.573 1.00 19.63 C ANISOU 1014 CE2 PHE A 120 2466 3311 1683 237 83 12 C ATOM 1015 CZ PHE A 120 4.163 0.228 11.503 1.00 20.08 C ANISOU 1015 CZ PHE A 120 2284 2916 2430 671 -293 -372 C ATOM 1016 N ASP A 121 2.742 1.394 16.460 1.00 11.89 N ANISOU 1016 N ASP A 121 1381 1597 1539 80 122 113 N ATOM 1017 CA ASP A 121 1.639 0.663 17.051 1.00 12.80 C ANISOU 1017 CA ASP A 121 1519 2000 1346 5 138 85 C ATOM 1018 C ASP A 121 1.140 -0.454 16.163 1.00 13.31 C ANISOU 1018 C ASP A 121 1663 1720 1672 -78 133 145 C ATOM 1019 O ASP A 121 0.852 -1.524 16.647 1.00 17.45 O ANISOU 1019 O ASP A 121 2613 2033 1983 -395 54 331 O ATOM 1020 CB ASP A 121 0.487 1.588 17.441 1.00 13.87 C ANISOU 1020 CB ASP A 121 1539 2078 1654 59 253 59 C ATOM 1021 CG ASP A 121 -0.405 1.024 18.522 1.00 15.18 C ANISOU 1021 CG ASP A 121 1733 2288 1747 -84 367 -154 C ATOM 1022 OD1 ASP A 121 0.151 0.576 19.569 1.00 19.65 O ANISOU 1022 OD1 ASP A 121 2311 3342 1814 -329 283 446 O ATOM 1023 OD2 ASP A 121 -1.592 0.993 18.346 1.00 17.10 O ANISOU 1023 OD2 ASP A 121 1704 2648 2144 -111 404 -245 O ATOM 1024 N ALA A 122 0.916 -0.193 14.881 1.00 13.25 N ANISOU 1024 N ALA A 122 1680 1719 1636 -215 101 12 N ATOM 1025 CA ALA A 122 0.236 -1.158 14.012 1.00 14.22 C ANISOU 1025 CA ALA A 122 1783 1753 1867 -318 0 -29 C ATOM 1026 C ALA A 122 0.369 -0.678 12.565 1.00 13.66 C ANISOU 1026 C ALA A 122 1714 1666 1812 -226 -98 -89 C ATOM 1027 O ALA A 122 0.605 0.487 12.287 1.00 14.43 O ANISOU 1027 O ALA A 122 2074 1552 1859 -187 86 -49 O ATOM 1028 CB ALA A 122 -1.266 -1.224 14.388 1.00 18.60 C ANISOU 1028 CB ALA A 122 1911 2877 2279 -677 98 203 C ATOM 1029 N SER A 123 0.121 -1.584 11.669 1.00 16.50 N ANISOU 1029 N SER A 123 2717 1664 1888 -533 -176 -48 N ATOM 1030 CA SER A 123 -0.157 -1.283 10.263 1.00 17.12 C ANISOU 1030 CA SER A 123 2228 2394 1882 -526 -284 -22 C ATOM 1031 C SER A 123 -1.543 -1.827 9.956 1.00 17.91 C ANISOU 1031 C SER A 123 2355 2321 2128 -855 -103 -81 C ATOM 1032 O SER A 123 -1.936 -2.879 10.475 1.00 23.33 O ANISOU 1032 O SER A 123 3105 2716 3045 -1137 -482 437 O ATOM 1033 CB ASER A 123 0.877 -1.838 9.315 0.74 19.11 C ANISOU 1033 CB ASER A 123 2350 2916 1996 -775 31 56 C ATOM 1034 CB BSER A 123 0.826 -1.976 9.321 0.26 24.70 C ANISOU 1034 CB BSER A 123 2752 4621 2010 304 352 399 C ATOM 1035 OG ASER A 123 0.997 -3.232 9.417 0.74 23.07 O ANISOU 1035 OG ASER A 123 3581 2910 2276 -176 477 -270 O ATOM 1036 OG BSER A 123 2.170 -1.749 9.679 0.26 35.97 O ANISOU 1036 OG BSER A 123 2574 8045 3050 525 271 304 O ATOM 1037 N VAL A 124 -2.274 -1.136 9.098 1.00 17.16 N ANISOU 1037 N VAL A 124 1987 2608 1925 -717 39 -135 N ATOM 1038 CA VAL A 124 -3.653 -1.515 8.757 1.00 20.47 C ANISOU 1038 CA VAL A 124 2093 3323 2363 -948 -43 -258 C ATOM 1039 C VAL A 124 -3.905 -1.291 7.284 1.00 24.07 C ANISOU 1039 C VAL A 124 2276 4355 2514 -1292 -373 21 C ATOM 1040 O VAL A 124 -4.772 -1.998 6.740 1.00 33.65 O ANISOU 1040 O VAL A 124 4256 5212 3319 -2597 -1209 182 O ATOM 1041 CB VAL A 124 -4.701 -0.788 9.622 1.00 21.92 C ANISOU 1041 CB VAL A 124 1939 3481 2910 -495 -59 80 C ATOM 1042 CG1 VAL A 124 -4.629 -1.138 11.102 1.00 26.15 C ANISOU 1042 CG1 VAL A 124 3153 4167 2615 -400 403 -392 C ATOM 1043 CG2 VAL A 124 -4.637 0.730 9.495 1.00 32.56 C ANISOU 1043 CG2 VAL A 124 2938 3469 5963 224 802 628 C ATOM 1044 OXT VAL A 124 -3.271 -0.447 6.620 1.00 21.13 O ANISOU 1044 OXT VAL A 124 1979 3488 2561 -481 -158 71 O TER 1045 VAL A 124 HETATM 1046 O HOH A 125 21.808 11.434 25.959 1.00 53.24 O ANISOU 1046 O HOH A 125 6934 6941 6355 -390 -348 -289 O HETATM 1047 O HOH A 126 24.339 -10.962 20.484 0.50 34.62 O ANISOU 1047 O HOH A 126 4743 4297 4113 85 -153 -33 O HETATM 1048 O HOH A 127 18.826 12.065 25.800 0.50 47.57 O ANISOU 1048 O HOH A 127 6277 5984 5813 -30 -696 -442 O HETATM 1049 O HOH A 128 15.422 9.375 26.900 0.50 47.77 O ANISOU 1049 O HOH A 128 5814 6305 6029 258 438 -333 O HETATM 1050 O HOH A 129 17.568 5.018 26.266 1.00 51.44 O ANISOU 1050 O HOH A 129 6198 6957 6391 -396 450 128 O HETATM 1051 O HOH A 130 16.776 3.327 24.024 1.00 50.07 O ANISOU 1051 O HOH A 130 6661 6291 6073 -474 -289 -12 O HETATM 1052 O HOH A 131 20.501 2.507 23.076 1.00 37.27 O ANISOU 1052 O HOH A 131 4492 4706 4962 -18 -70 178 O HETATM 1053 O HOH A 132 19.541 9.998 21.271 1.00 25.70 O ANISOU 1053 O HOH A 132 3301 3229 3236 -28 -8 -181 O HETATM 1054 O HOH A 133 16.425 12.808 19.685 1.00 45.14 O ANISOU 1054 O HOH A 133 5906 5287 5959 -339 -449 -193 O HETATM 1055 O HOH A 134 13.162 10.204 25.480 1.00 36.71 O ANISOU 1055 O HOH A 134 4447 5063 4439 491 532 -914 O HETATM 1056 O HOH A 135 12.217 11.625 22.267 1.00 29.28 O ANISOU 1056 O HOH A 135 3824 3655 3645 304 -188 -353 O HETATM 1057 O HOH A 136 18.703 6.671 15.785 1.00 22.10 O ANISOU 1057 O HOH A 136 2649 2982 2766 -94 63 16 O HETATM 1058 O HOH A 137 17.307 5.131 10.622 1.00 33.80 O ANISOU 1058 O HOH A 137 4183 4259 4401 -157 30 -23 O HETATM 1059 O HOH A 138 16.253 13.007 13.252 1.00 34.95 O ANISOU 1059 O HOH A 138 4568 4108 4603 -185 -242 79 O HETATM 1060 O HOH A 139 16.950 -1.845 20.894 1.00 53.56 O ANISOU 1060 O HOH A 139 7163 6894 6294 -748 203 -129 O HETATM 1061 O HOH A 140 18.527 3.823 6.436 1.00 35.92 O ANISOU 1061 O HOH A 140 4480 4703 4464 -293 184 214 O HETATM 1062 O HOH A 141 18.751 -1.216 4.295 1.00 28.80 O ANISOU 1062 O HOH A 141 3546 3770 3628 223 185 186 O HETATM 1063 O HOH A 142 16.547 5.540 7.591 1.00 25.13 O ANISOU 1063 O HOH A 142 3211 3137 3199 -198 0 -76 O HETATM 1064 O HOH A 143 15.781 8.278 8.120 1.00 53.81 O ANISOU 1064 O HOH A 143 6763 6622 7061 132 -140 -751 O HETATM 1065 O HOH A 144 13.814 -8.749 -6.817 1.00 47.22 O ANISOU 1065 O HOH A 144 5588 6178 6174 -202 194 -117 O HETATM 1066 O HOH A 145 18.433 1.845 -2.766 1.00 53.38 O ANISOU 1066 O HOH A 145 6570 6940 6772 -29 479 -347 O HETATM 1067 O HOH A 146 20.532 4.088 -0.449 0.50 37.35 O ANISOU 1067 O HOH A 146 4632 4680 4879 -341 -79 356 O HETATM 1068 O HOH A 147 22.198 2.268 4.711 0.50 44.80 O ANISOU 1068 O HOH A 147 5210 5883 5929 422 63 -83 O HETATM 1069 O HOH A 148 12.790 5.077 0.699 1.00 30.59 O ANISOU 1069 O HOH A 148 3883 3678 4060 -188 -6 -23 O HETATM 1070 O HOH A 149 15.717 0.590 -3.041 1.00 33.82 O ANISOU 1070 O HOH A 149 4054 4754 4041 185 556 -474 O HETATM 1071 O HOH A 150 16.447 -3.721 0.519 1.00 30.44 O ANISOU 1071 O HOH A 150 3912 3810 3844 -14 25 1 O HETATM 1072 O HOH A 151 15.001 -2.520 -2.826 1.00 50.82 O ANISOU 1072 O HOH A 151 6644 6603 6062 -199 631 389 O HETATM 1073 O HOH A 152 15.770 -8.211 -5.489 1.00 22.83 O ANISOU 1073 O HOH A 152 2739 3215 2720 155 300 45 O HETATM 1074 O HOH A 153 17.753 -3.507 -3.993 1.00 52.28 O ANISOU 1074 O HOH A 153 6514 6912 6436 -211 752 -76 O HETATM 1075 O HOH A 154 20.457 -10.013 0.674 1.00 35.58 O ANISOU 1075 O HOH A 154 4439 4952 4129 -288 335 44 O HETATM 1076 O HOH A 155 17.953 -7.557 1.246 1.00 39.16 O ANISOU 1076 O HOH A 155 4973 5169 4736 -238 294 18 O HETATM 1077 O HOH A 156 15.187 -12.202 6.843 1.00 15.02 O ANISOU 1077 O HOH A 156 2052 1851 1803 -5 20 -43 O HETATM 1078 O HOH A 157 14.723 2.858 -5.148 0.50 42.26 O ANISOU 1078 O HOH A 157 5966 5064 5028 153 -140 -363 O HETATM 1079 O HOH A 158 21.687 -13.148 6.854 0.50 42.92 O ANISOU 1079 O HOH A 158 5110 5712 5486 281 107 276 O HETATM 1080 O HOH A 159 9.426 2.571 -5.461 0.50 49.50 O ANISOU 1080 O HOH A 159 6755 5904 6149 -98 -1066 -140 O HETATM 1081 O HOH A 160 19.106 -11.357 12.810 1.00 23.44 O ANISOU 1081 O HOH A 160 3033 3018 2857 -203 17 207 O HETATM 1082 O HOH A 161 24.274 -9.343 1.636 1.00 58.15 O ANISOU 1082 O HOH A 161 7298 7518 7278 -69 54 -211 O HETATM 1083 O HOH A 162 22.677 0.808 14.491 1.00 49.24 O ANISOU 1083 O HOH A 162 6513 5871 6324 -504 163 -146 O HETATM 1084 O HOH A 163 25.592 -2.509 14.490 1.00 40.66 O ANISOU 1084 O HOH A 163 4796 5391 5263 80 90 218 O HETATM 1085 O HOH A 164 23.962 -7.340 9.378 1.00 49.78 O ANISOU 1085 O HOH A 164 6173 6500 6241 130 172 -18 O HETATM 1086 O HOH A 165 23.647 -3.800 7.374 1.00 55.32 O ANISOU 1086 O HOH A 165 7611 6732 6678 190 269 -202 O HETATM 1087 O HOH A 166 21.480 2.592 8.662 0.50 44.19 O ANISOU 1087 O HOH A 166 5197 5934 5658 311 62 -10 O HETATM 1088 O HOH A 167 21.506 -0.157 9.530 1.00 35.58 O ANISOU 1088 O HOH A 167 4018 4971 4529 485 456 -288 O HETATM 1089 O HOH A 168 19.527 1.748 6.705 1.00 38.48 O ANISOU 1089 O HOH A 168 4637 5388 4595 -385 478 13 O HETATM 1090 O HOH A 169 19.894 -2.394 21.353 0.50 43.35 O ANISOU 1090 O HOH A 169 5573 5685 5213 10 250 89 O HETATM 1091 O HOH A 170 18.184 -4.659 21.368 1.00 48.34 O ANISOU 1091 O HOH A 170 6246 6280 5841 -712 -67 433 O HETATM 1092 O HOH A 171 15.262 -4.588 20.987 1.00 47.28 O ANISOU 1092 O HOH A 171 5813 6246 5904 167 283 390 O HETATM 1093 O HOH A 172 22.415 -11.689 18.538 1.00 33.83 O ANISOU 1093 O HOH A 172 4314 4292 4248 78 91 -364 O HETATM 1094 O HOH A 173 21.826 -6.976 17.064 1.00 22.40 O ANISOU 1094 O HOH A 173 2960 2755 2797 -125 -15 141 O HETATM 1095 O HOH A 174 20.689 -11.565 15.241 1.00 31.13 O ANISOU 1095 O HOH A 174 3853 4022 3951 -102 93 -51 O HETATM 1096 O HOH A 175 17.895 -7.053 21.943 1.00 32.74 O ANISOU 1096 O HOH A 175 4140 3894 4405 114 -109 77 O HETATM 1097 O HOH A 176 17.452 -5.078 25.029 0.50 58.66 O ANISOU 1097 O HOH A 176 7183 7436 7671 448 -313 -221 O HETATM 1098 O HOH A 177 20.279 -3.413 26.895 0.50 51.71 O ANISOU 1098 O HOH A 177 6827 6376 6443 174 -324 -72 O HETATM 1099 O HOH A 178 12.269 -12.337 23.111 1.00 57.39 O ANISOU 1099 O HOH A 178 7030 7580 7196 227 -99 50 O HETATM 1100 O HOH A 179 9.072 -9.505 23.411 1.00 57.27 O ANISOU 1100 O HOH A 179 7479 7497 6784 491 121 -99 O HETATM 1101 O HOH A 180 9.283 -7.112 22.049 1.00 55.17 O ANISOU 1101 O HOH A 180 7064 6836 7063 3 -292 -284 O HETATM 1102 O HOH A 181 15.608 -14.557 22.354 1.00 18.33 O ANISOU 1102 O HOH A 181 2445 2225 2293 -87 -46 82 O HETATM 1103 O HOH A 182 8.219 -7.061 19.537 1.00 47.71 O ANISOU 1103 O HOH A 182 6195 6054 5880 194 -347 204 O HETATM 1104 O HOH A 183 7.129 -3.248 15.589 1.00 34.22 O ANISOU 1104 O HOH A 183 4205 4080 4718 229 -42 -198 O HETATM 1105 O HOH A 184 5.737 -4.698 14.086 1.00 47.99 O ANISOU 1105 O HOH A 184 5796 6559 5878 -278 612 770 O HETATM 1106 O HOH A 185 9.330 3.316 -0.683 1.00 20.55 O ANISOU 1106 O HOH A 185 2720 2601 2489 -117 73 117 O HETATM 1107 O HOH A 186 10.497 5.797 -0.550 0.50 39.28 O ANISOU 1107 O HOH A 186 4868 5378 4679 -240 198 -126 O HETATM 1108 O HOH A 187 7.218 7.400 -1.352 1.00 61.49 O ANISOU 1108 O HOH A 187 8051 7500 7811 -521 -347 57 O HETATM 1109 O HOH A 188 4.698 4.870 -0.544 1.00 50.14 O ANISOU 1109 O HOH A 188 6946 6075 6030 -191 -522 655 O HETATM 1110 O HOH A 189 10.045 14.022 2.440 1.00 44.38 O ANISOU 1110 O HOH A 189 6092 5240 5532 -322 -68 976 O HETATM 1111 O HOH A 190 13.228 13.528 5.831 1.00 23.98 O ANISOU 1111 O HOH A 190 2930 3101 3082 -102 269 100 O HETATM 1112 O HOH A 191 7.335 16.423 8.956 1.00 32.27 O ANISOU 1112 O HOH A 191 4168 3870 4223 95 58 -181 O HETATM 1113 O HOH A 192 2.864 11.694 5.639 1.00 21.46 O ANISOU 1113 O HOH A 192 2723 2792 2637 117 29 6 O HETATM 1114 O HOH A 193 3.814 13.992 4.243 1.00 51.85 O ANISOU 1114 O HOH A 193 6816 6328 6558 104 -158 454 O HETATM 1115 O HOH A 194 6.148 14.653 1.126 0.50 49.24 O ANISOU 1115 O HOH A 194 6067 6258 6383 -242 488 493 O HETATM 1116 O HOH A 195 8.555 9.144 1.698 1.00 17.23 O ANISOU 1116 O HOH A 195 2242 2148 2156 -79 -22 111 O HETATM 1117 O HOH A 196 7.522 12.515 -0.176 0.50 49.42 O ANISOU 1117 O HOH A 196 6487 6060 6230 334 -231 666 O HETATM 1118 O HOH A 197 12.300 11.674 14.679 1.00 28.96 O ANISOU 1118 O HOH A 197 3769 3617 3615 -321 -70 196 O HETATM 1119 O HOH A 198 -1.351 16.541 16.037 1.00 38.48 O ANISOU 1119 O HOH A 198 4876 4949 4796 587 505 -325 O HETATM 1120 O HOH A 199 -4.000 18.208 13.121 0.50 42.03 O ANISOU 1120 O HOH A 199 5373 5228 5369 414 -73 135 O HETATM 1121 O HOH A 200 -1.737 17.109 8.220 0.50 53.06 O ANISOU 1121 O HOH A 200 6769 6670 6721 -108 -158 575 O HETATM 1122 O HOH A 201 0.545 15.959 7.736 1.00 38.33 O ANISOU 1122 O HOH A 201 4733 4831 5000 0 22 90 O HETATM 1123 O HOH A 202 3.475 16.351 12.457 1.00 36.47 O ANISOU 1123 O HOH A 202 4789 4372 4697 20 90 -86 O HETATM 1124 O HOH A 203 1.129 18.331 15.572 0.50 40.83 O ANISOU 1124 O HOH A 203 5491 4931 5092 260 -253 -91 O HETATM 1125 O HOH A 204 -4.426 15.595 14.297 0.50 34.67 O ANISOU 1125 O HOH A 204 4411 4313 4450 571 210 -543 O HETATM 1126 O HOH A 205 0.229 9.863 5.025 1.00 25.04 O ANISOU 1126 O HOH A 205 3245 3148 3122 9 75 -13 O HETATM 1127 O HOH A 206 -9.850 11.612 14.613 1.00 48.06 O ANISOU 1127 O HOH A 206 5596 6295 6371 406 -105 55 O HETATM 1128 O HOH A 207 -7.748 13.656 13.692 1.00 30.71 O ANISOU 1128 O HOH A 207 3977 3763 3929 424 -72 19 O HETATM 1129 O HOH A 208 -10.467 9.046 15.895 1.00 56.02 O ANISOU 1129 O HOH A 208 6699 7526 7058 370 270 236 O HETATM 1130 O HOH A 209 -10.071 10.757 18.996 0.50 49.65 O ANISOU 1130 O HOH A 209 5696 6357 6811 -128 -193 246 O HETATM 1131 O HOH A 210 -6.217 12.793 21.898 1.00 56.63 O ANISOU 1131 O HOH A 210 7624 6813 7079 274 -286 -763 O HETATM 1132 O HOH A 211 -10.130 5.776 17.888 1.00 21.74 O ANISOU 1132 O HOH A 211 2556 2921 2783 -237 10 204 O HETATM 1133 O HOH A 212 -6.174 1.614 16.134 0.50 45.70 O ANISOU 1133 O HOH A 212 5895 5787 5683 44 101 -267 O HETATM 1134 O HOH A 213 22.447 0.777 19.794 1.00 43.86 O ANISOU 1134 O HOH A 213 5101 5091 6474 8 -480 -211 O HETATM 1135 O HOH A 214 -9.076 0.229 22.183 0.50 45.19 O ANISOU 1135 O HOH A 214 5717 5662 5790 483 -449 -74 O HETATM 1136 O HOH A 215 -0.120 -6.226 19.144 0.50 56.65 O ANISOU 1136 O HOH A 215 7313 6982 7228 -383 -95 -124 O HETATM 1137 O HOH A 216 -6.624 -0.401 28.097 0.50 41.41 O ANISOU 1137 O HOH A 216 4899 5811 5025 -283 525 353 O HETATM 1138 O HOH A 217 -0.801 -0.181 28.249 1.00 35.94 O ANISOU 1138 O HOH A 217 4844 4282 4528 44 -144 35 O HETATM 1139 O HOH A 218 -9.358 4.583 25.345 1.00 23.57 O ANISOU 1139 O HOH A 218 2785 3185 2985 -46 109 112 O HETATM 1140 O HOH A 219 -2.870 13.306 22.123 1.00 51.75 O ANISOU 1140 O HOH A 219 6954 6177 6532 98 -132 45 O HETATM 1141 O AHOH A 220 -3.799 15.865 18.211 0.50 40.98 O ANISOU 1141 O AHOH A 220 4945 5247 5377 704 351 -284 O HETATM 1142 O BHOH A 220 -5.255 15.844 16.686 0.50 38.43 O ANISOU 1142 O BHOH A 220 5044 4647 4909 403 9 -318 O HETATM 1143 O HOH A 221 -7.726 1.542 11.727 1.00 42.59 O ANISOU 1143 O HOH A 221 4734 5917 5532 -209 336 -187 O HETATM 1144 O HOH A 222 -5.265 5.774 1.817 1.00 55.57 O ANISOU 1144 O HOH A 222 6919 7166 7029 -9 -7 95 O HETATM 1145 O HOH A 223 -7.177 7.860 4.151 0.50 44.12 O ANISOU 1145 O HOH A 223 5562 5482 5718 126 -228 -202 O HETATM 1146 O HOH A 224 -4.684 16.682 9.480 1.00 49.22 O ANISOU 1146 O HOH A 224 5993 6014 6694 496 -402 -49 O HETATM 1147 O HOH A 225 -8.292 13.593 10.523 0.50 39.76 O ANISOU 1147 O HOH A 225 5073 5224 4810 -140 267 32 O HETATM 1148 O HOH A 226 2.480 10.280 3.327 1.00 48.80 O ANISOU 1148 O HOH A 226 6195 6120 6228 -311 -134 47 O HETATM 1149 O HOH A 227 1.270 6.246 -1.252 0.50 50.33 O ANISOU 1149 O HOH A 227 6565 6226 6334 112 -225 202 O HETATM 1150 O HOH A 228 -2.569 5.598 -0.039 1.00 40.34 O ANISOU 1150 O HOH A 228 5088 5046 5193 463 -277 -214 O HETATM 1151 O HOH A 229 7.142 -11.379 7.978 1.00 20.05 O ANISOU 1151 O HOH A 229 2610 2474 2534 -158 -29 29 O HETATM 1152 O HOH A 230 3.207 -4.063 10.455 1.00 33.32 O ANISOU 1152 O HOH A 230 4182 4277 4202 -118 49 55 O HETATM 1153 O HOH A 231 2.777 -8.168 6.421 1.00 59.88 O ANISOU 1153 O HOH A 231 7362 7893 7494 -128 -180 9 O HETATM 1154 O HOH A 232 7.465 -16.133 15.587 1.00 42.78 O ANISOU 1154 O HOH A 232 5055 5378 5823 -54 372 -237 O HETATM 1155 O HOH A 233 8.728 -15.496 18.223 1.00 27.76 O ANISOU 1155 O HOH A 233 3481 3547 3518 -241 149 104 O HETATM 1156 O HOH A 234 11.507 -14.139 20.741 1.00 39.21 O ANISOU 1156 O HOH A 234 5070 5239 4588 -41 154 100 O HETATM 1157 O HOH A 235 13.797 -17.410 19.569 1.00 30.29 O ANISOU 1157 O HOH A 235 3856 3925 3730 -219 44 228 O HETATM 1158 O HOH A 236 9.364 -21.185 10.592 1.00 32.49 O ANISOU 1158 O HOH A 236 4180 3967 4196 -343 -119 83 O HETATM 1159 O HOH A 237 13.297 -24.752 16.537 1.00 35.10 O ANISOU 1159 O HOH A 237 4633 4303 4400 -63 -68 263 O HETATM 1160 O HOH A 238 13.621 -21.844 17.496 1.00 47.65 O ANISOU 1160 O HOH A 238 6216 5853 6034 -814 -40 92 O HETATM 1161 O HOH A 239 17.726 -23.655 15.125 1.00 47.73 O ANISOU 1161 O HOH A 239 5920 6017 6200 445 -70 -82 O HETATM 1162 O HOH A 240 18.955 -19.712 13.898 1.00 33.62 O ANISOU 1162 O HOH A 240 4207 4165 4401 75 78 -312 O HETATM 1163 O HOH A 241 14.726 -19.290 9.403 1.00 32.81 O ANISOU 1163 O HOH A 241 4201 4242 4025 183 269 -342 O HETATM 1164 O HOH A 242 12.700 -22.294 9.877 1.00 49.24 O ANISOU 1164 O HOH A 242 6200 6383 6126 -323 -300 122 O HETATM 1165 O HOH A 243 17.648 -19.922 10.536 0.50 47.66 O ANISOU 1165 O HOH A 243 6105 5795 6208 84 -199 -139 O HETATM 1166 O HOH A 244 14.278 -23.252 8.271 0.50 57.47 O ANISOU 1166 O HOH A 244 7274 7257 7304 -74 -78 193 O HETATM 1167 O HOH A 245 22.329 -20.414 18.648 1.00 50.05 O ANISOU 1167 O HOH A 245 6125 6346 6548 123 420 -346 O HETATM 1168 O HOH A 246 18.722 12.317 20.015 1.00 43.67 O ANISOU 1168 O HOH A 246 5646 5268 5678 -11 46 -156 O HETATM 1169 O HOH A 247 16.006 -17.262 21.273 1.00 23.00 O ANISOU 1169 O HOH A 247 2856 3026 2858 -61 85 64 O HETATM 1170 O HOH A 248 19.493 -19.524 22.979 1.00 25.32 O ANISOU 1170 O HOH A 248 3308 3205 3109 -152 -37 85 O HETATM 1171 O HOH A 249 22.868 -20.576 21.098 1.00 53.10 O ANISOU 1171 O HOH A 249 6776 6435 6966 390 -142 251 O HETATM 1172 O HOH A 250 15.376 -16.375 7.858 1.00 29.96 O ANISOU 1172 O HOH A 250 3856 3714 3815 -71 124 -66 O HETATM 1173 O HOH A 251 12.344 -14.160 4.545 1.00 19.82 O ANISOU 1173 O HOH A 251 2664 2436 2433 98 106 -67 O HETATM 1174 O HOH A 252 11.184 -13.384 2.027 1.00 48.86 O ANISOU 1174 O HOH A 252 5712 6679 6174 16 280 -242 O HETATM 1175 O HOH A 253 7.214 -13.550 2.672 0.50 39.01 O ANISOU 1175 O HOH A 253 5295 4533 4994 289 -152 -789 O HETATM 1176 O HOH A 254 6.764 -10.488 0.631 1.00 35.72 O ANISOU 1176 O HOH A 254 4993 4258 4322 286 -86 -272 O HETATM 1177 O HOH A 255 3.532 -9.733 0.118 1.00 54.76 O ANISOU 1177 O HOH A 255 6890 6975 6942 5 -248 -580 O HETATM 1178 O HOH A 256 1.857 -8.236 2.206 0.50 36.29 O ANISOU 1178 O HOH A 256 4123 4675 4993 -173 165 -109 O HETATM 1179 O HOH A 257 0.268 -4.926 1.311 1.00 33.62 O ANISOU 1179 O HOH A 257 4124 4063 4586 -310 -231 -262 O HETATM 1180 O HOH A 258 2.657 3.255 -0.722 1.00 48.88 O ANISOU 1180 O HOH A 258 5810 6286 6477 279 62 -385 O HETATM 1181 O HOH A 259 2.143 2.448 -3.651 1.00 56.15 O ANISOU 1181 O HOH A 259 7265 7042 7028 -21 -15 79 O HETATM 1182 O HOH A 260 -4.814 -3.029 4.211 0.50 39.20 O ANISOU 1182 O HOH A 260 4835 4953 5104 -126 98 -182 O HETATM 1183 O HOH A 261 1.490 12.344 23.889 1.00 43.64 O ANISOU 1183 O HOH A 261 5659 5441 5481 -123 114 56 O HETATM 1184 O HOH A 262 9.723 12.971 21.799 1.00 29.31 O ANISOU 1184 O HOH A 262 3721 3683 3732 -10 -115 -103 O HETATM 1185 O HOH A 263 9.352 11.036 25.176 0.50 50.05 O ANISOU 1185 O HOH A 263 6581 6189 6248 88 -32 -128 O HETATM 1186 O HOH A 264 3.365 7.132 23.952 1.00 34.69 O ANISOU 1186 O HOH A 264 4246 4536 4398 201 -128 103 O HETATM 1187 O HOH A 265 3.756 14.704 24.738 1.00 37.18 O ANISOU 1187 O HOH A 265 4667 4995 4466 442 451 -368 O HETATM 1188 O HOH A 266 3.986 19.240 21.855 0.50 38.63 O ANISOU 1188 O HOH A 266 5268 4660 4748 851 -79 -611 O HETATM 1189 O HOH A 267 10.466 16.457 23.687 1.00 50.25 O ANISOU 1189 O HOH A 267 6297 6650 6147 -125 53 -134 O HETATM 1190 O HOH A 268 12.415 20.782 22.255 1.00 49.26 O ANISOU 1190 O HOH A 268 6019 6660 6037 -612 223 575 O HETATM 1191 O HOH A 269 10.731 15.558 20.789 1.00 32.56 O ANISOU 1191 O HOH A 269 4082 4234 4055 -178 -230 -109 O HETATM 1192 O HOH A 270 5.911 19.632 16.587 1.00 37.17 O ANISOU 1192 O HOH A 270 4747 4456 4920 -241 -21 153 O HETATM 1193 O HOH A 271 6.478 15.316 13.837 1.00 39.19 O ANISOU 1193 O HOH A 271 5017 5087 4785 -127 128 -112 O HETATM 1194 O HOH A 272 5.345 17.213 14.519 1.00 49.63 O ANISOU 1194 O HOH A 272 6531 6136 6189 -184 153 352 O HETATM 1195 O HOH A 273 -0.604 13.697 23.183 1.00 56.20 O ANISOU 1195 O HOH A 273 7486 6926 6943 -82 -316 136 O HETATM 1196 O HOH A 274 11.115 9.640 15.800 1.00 19.33 O ANISOU 1196 O HOH A 274 2396 2537 2413 -114 54 18 O HETATM 1197 O HOH A 275 10.986 4.799 21.076 1.00 28.81 O ANISOU 1197 O HOH A 275 3363 3874 3708 -109 -50 271 O HETATM 1198 O HOH A 276 7.812 6.677 24.906 0.50 45.90 O ANISOU 1198 O HOH A 276 6078 5598 5765 -112 41 123 O HETATM 1199 O HOH A 277 6.294 -1.631 18.178 1.00 39.06 O ANISOU 1199 O HOH A 277 4848 4652 5342 19 -256 411 O HETATM 1200 O HOH A 278 -0.784 0.321 22.025 1.00 22.21 O ANISOU 1200 O HOH A 278 2786 2919 2732 -66 19 59 O HETATM 1201 O HOH A 279 1.149 -2.024 19.647 1.00 44.95 O ANISOU 1201 O HOH A 279 6010 5466 5605 -292 -166 517 O HETATM 1202 O HOH A 280 -4.009 1.348 16.774 1.00 33.45 O ANISOU 1202 O HOH A 280 4230 4503 3978 134 20 -28 O HETATM 1203 O HOH A 281 1.717 -4.483 12.788 0.50 45.06 O ANISOU 1203 O HOH A 281 6140 5341 5640 219 70 -237 O HETATM 1204 O HOH A 282 -0.558 -4.604 12.661 1.00 45.78 O ANISOU 1204 O HOH A 282 6147 5415 5833 -179 70 268 O HETATM 1205 O HOH A 283 -1.965 -5.220 8.970 0.50 40.62 O ANISOU 1205 O HOH A 283 5723 4616 5094 139 -184 -84 O HETATM 1206 O HOH A 284 1.575 -6.078 7.939 1.00 54.01 O ANISOU 1206 O HOH A 284 7149 6616 6758 -282 -666 132 O HETATM 1207 O HOH A 285 -4.294 -0.698 4.130 0.50 41.07 O ANISOU 1207 O HOH A 285 5097 5326 5181 478 -184 -46 O HETATM 1208 O HOH A 286 8.050 1.078 18.500 1.00 16.54 O ANISOU 1208 O HOH A 286 2102 2194 1987 168 79 -26 O HETATM 1209 O HOH A 287 10.599 2.724 19.112 1.00 33.34 O ANISOU 1209 O HOH A 287 4259 4221 4188 7 216 -54 O HETATM 1210 O HOH A 288 0.897 2.739 22.899 1.00 43.51 O ANISOU 1210 O HOH A 288 5422 5785 5323 20 127 -288 O HETATM 1211 O HOH A 289 12.912 -23.523 19.504 1.00 50.26 O ANISOU 1211 O HOH A 289 6338 6269 6490 -74 -188 141 O HETATM 1212 O HOH A 290 20.738 11.307 23.506 1.00 58.69 O ANISOU 1212 O HOH A 290 7390 7603 7309 112 -516 -123 O HETATM 1213 O HOH A 291 -10.949 5.180 13.217 1.00 47.03 O ANISOU 1213 O HOH A 291 5574 6046 6247 -826 80 383 O HETATM 1214 O HOH A 292 10.675 9.561 26.359 1.00 44.99 O ANISOU 1214 O HOH A 292 5469 5947 5678 134 265 -350 O HETATM 1215 O HOH A 293 3.114 -4.744 15.531 0.50 57.85 O ANISOU 1215 O HOH A 293 6889 7487 7606 115 95 -308 O HETATM 1216 O HOH A 294 18.761 -3.289 1.923 1.00 40.96 O ANISOU 1216 O HOH A 294 5056 5271 5236 -76 -91 -212 O HETATM 1217 O HOH A 295 -9.591 8.574 19.489 1.00 40.34 O ANISOU 1217 O HOH A 295 5203 4926 5200 270 -53 -286 O HETATM 1218 O HOH A 296 -9.363 3.337 28.063 0.50 35.89 O ANISOU 1218 O HOH A 296 4527 4417 4692 -372 -290 502 O HETATM 1219 O HOH A 297 3.365 -4.979 -1.444 0.50 41.30 O ANISOU 1219 O HOH A 297 5317 5210 5165 -294 182 382 O HETATM 1220 O HOH A 298 4.393 9.064 2.301 1.00 62.11 O ANISOU 1220 O HOH A 298 7891 7778 7929 -558 113 108 O HETATM 1221 O HOH A 299 6.637 15.225 26.427 0.50 60.70 O ANISOU 1221 O HOH A 299 7928 7388 7747 208 -627 -353 O HETATM 1222 O HOH A 300 7.499 15.770 3.932 0.50 59.03 O ANISOU 1222 O HOH A 300 7804 7379 7247 238 -214 260 O HETATM 1223 O HOH A 301 9.313 13.322 25.180 1.00 57.05 O ANISOU 1223 O HOH A 301 7232 7218 7229 213 -66 125 O HETATM 1224 O HOH A 302 6.927 -13.583 16.368 1.00 42.75 O ANISOU 1224 O HOH A 302 5439 5373 5431 -187 325 6 O HETATM 1225 O HOH A 303 21.937 -0.535 6.435 0.50 42.49 O ANISOU 1225 O HOH A 303 5496 5009 5640 -364 -186 19 O HETATM 1226 O HOH A 304 5.794 -4.019 20.525 0.50 45.13 O ANISOU 1226 O HOH A 304 5297 5912 5937 -449 300 490 O HETATM 1227 O HOH A 305 6.674 -5.939 22.417 0.50 47.09 O ANISOU 1227 O HOH A 305 5704 6312 5877 -216 202 130 O HETATM 1228 O HOH A 306 22.948 -11.021 10.138 0.50 47.86 O ANISOU 1228 O HOH A 306 6427 5874 5883 -202 -357 188 O HETATM 1229 O HOH A 307 1.365 15.325 24.346 0.50 53.94 O ANISOU 1229 O HOH A 307 6752 7179 6565 -124 398 177 O HETATM 1230 O HOH A 308 -3.246 -4.516 13.291 0.50 42.63 O ANISOU 1230 O HOH A 308 5465 5178 5555 97 -155 296 O HETATM 1231 O HOH A 309 19.642 -2.168 -3.559 0.50 46.66 O ANISOU 1231 O HOH A 309 6238 5854 5637 271 -231 -979 O HETATM 1232 O HOH A 310 25.491 -20.230 19.095 0.50 50.49 O ANISOU 1232 O HOH A 310 6636 6220 6326 465 -206 -390 O HETATM 1233 O HOH A 311 0.508 -10.378 2.930 0.50 59.05 O ANISOU 1233 O HOH A 311 7623 7209 7605 -46 -349 73 O HETATM 1234 O HOH A 312 7.675 -16.416 10.598 1.00 46.18 O ANISOU 1234 O HOH A 312 5755 5729 6060 335 -222 -42 O HETATM 1235 O HOH A 313 20.138 -15.958 10.746 0.50 39.82 O ANISOU 1235 O HOH A 313 4937 5024 5170 -157 93 140 O HETATM 1236 O HOH A 314 14.557 5.539 24.513 0.50 50.26 O ANISOU 1236 O HOH A 314 6561 6248 6289 -200 -731 227 O HETATM 1237 O HOH A 315 0.882 18.137 20.714 0.50 48.25 O ANISOU 1237 O HOH A 315 6006 6090 6236 189 -129 151 O HETATM 1238 O HOH A 316 22.099 5.427 2.158 0.50 44.59 O ANISOU 1238 O HOH A 316 5494 5577 5872 -280 141 -13 O HETATM 1239 O HOH A 317 22.234 4.957 4.502 0.50 55.41 O ANISOU 1239 O HOH A 317 6352 7403 7298 -304 250 453 O HETATM 1240 O HOH A 318 23.782 -7.095 18.252 0.50 63.02 O ANISOU 1240 O HOH A 318 7854 8100 7992 137 185 -170 O HETATM 1241 O HOH A 319 25.855 -0.912 16.200 1.00 54.91 O ANISOU 1241 O HOH A 319 6775 7164 6926 -165 327 309 O HETATM 1242 O HOH A 320 15.564 -7.072 21.611 1.00 41.37 O ANISOU 1242 O HOH A 320 5296 5217 5204 218 -118 -359 O HETATM 1243 O HOH A 321 0.171 -3.879 16.124 0.50 41.29 O ANISOU 1243 O HOH A 321 5186 5486 5016 -441 68 344 O HETATM 1244 O HOH A 322 -6.196 9.433 1.897 1.00 48.82 O ANISOU 1244 O HOH A 322 6374 5980 6197 422 -244 -23 O HETATM 1245 O HOH A 323 21.156 -14.733 12.992 0.50 43.74 O ANISOU 1245 O HOH A 323 5285 5869 5466 370 59 118 O HETATM 1246 O HOH A 324 -3.147 -1.591 1.629 0.50 37.36 O ANISOU 1246 O HOH A 324 4413 4949 4835 -153 -96 -2 O HETATM 1247 O HOH A 325 3.568 -2.357 18.857 0.50 47.61 O ANISOU 1247 O HOH A 325 5953 6005 6131 19 -106 323 O HETATM 1248 O HOH A 326 20.220 -3.484 29.296 0.50 47.74 O ANISOU 1248 O HOH A 326 5570 6475 6094 -50 763 13 O HETATM 1249 O AHOH A 327 -0.783 15.865 22.644 0.50 58.51 O ANISOU 1249 O AHOH A 327 7619 7289 7323 -110 -65 -164 O HETATM 1250 O BHOH A 327 -1.123 17.051 20.883 0.50 52.91 O ANISOU 1250 O BHOH A 327 6514 6668 6922 19 -138 -108 O HETATM 1251 O HOH A 328 15.928 13.377 16.871 0.50 48.79 O ANISOU 1251 O HOH A 328 6094 6087 6357 45 -34 393 O HETATM 1252 O HOH A 329 -12.827 10.824 15.715 0.50 43.81 O ANISOU 1252 O HOH A 329 5522 5556 5567 -152 -93 311 O HETATM 1253 O HOH A 330 5.773 17.843 26.007 0.50 44.14 O ANISOU 1253 O HOH A 330 5347 5861 5565 -273 -42 -368 O HETATM 1254 O HOH A 331 7.380 -0.508 -2.939 0.50 44.65 O ANISOU 1254 O HOH A 331 6068 5447 5448 138 -506 -210 O HETATM 1255 O HOH A 332 8.388 -2.530 18.770 0.50 29.63 O ANISOU 1255 O HOH A 332 3529 3937 3791 583 309 -130 O HETATM 1256 O HOH A 333 -8.143 3.037 16.593 1.00 51.35 O ANISOU 1256 O HOH A 333 6560 6254 6699 -172 -277 -69 O HETATM 1257 O HOH A 334 9.688 -1.112 21.112 1.00 47.49 O ANISOU 1257 O HOH A 334 6068 6258 5718 -376 321 268 O HETATM 1258 O HOH A 335 5.058 8.214 -0.207 0.50 42.33 O ANISOU 1258 O HOH A 335 5788 5016 5277 -391 -621 104 O HETATM 1259 O HOH A 336 9.311 -4.255 1.598 1.00 15.88 O ANISOU 1259 O HOH A 336 2028 2090 1918 0 55 -27 O HETATM 1260 O HOH A 337 7.146 -2.695 0.703 1.00 18.69 O ANISOU 1260 O HOH A 337 2445 2355 2302 54 79 -81 O HETATM 1261 O HOH A 338 5.997 13.068 -2.616 0.50 47.10 O ANISOU 1261 O HOH A 338 5935 5945 6017 149 -188 -312 O HETATM 1262 O HOH A 339 1.906 10.705 0.804 0.50 49.57 O ANISOU 1262 O HOH A 339 5986 6622 6225 3 154 222 O HETATM 1263 O HOH A 340 7.250 0.690 21.794 1.00 45.84 O ANISOU 1263 O HOH A 340 5902 5723 5794 227 -123 40 O HETATM 1264 O HOH A 341 6.820 4.250 -1.150 0.50 27.51 O ANISOU 1264 O HOH A 341 3705 3371 3377 38 6 26 O HETATM 1265 O HOH A 342 -5.848 6.221 6.558 0.50 41.52 O ANISOU 1265 O HOH A 342 5274 5296 5204 -215 -105 412 O HETATM 1266 O HOH A 343 0.839 -1.111 30.921 0.50 44.77 O ANISOU 1266 O HOH A 343 5638 5809 5562 107 176 -114 O HETATM 1267 O HOH A 344 8.554 8.962 25.758 0.50 43.99 O ANISOU 1267 O HOH A 344 5728 5746 5241 77 150 -14 O HETATM 1268 O HOH A 345 5.099 20.553 20.273 0.50 44.62 O ANISOU 1268 O HOH A 345 5743 5662 5547 345 -64 -651 O HETATM 1269 O HOH A 346 26.061 -4.879 7.657 0.50 44.05 O ANISOU 1269 O HOH A 346 5726 5108 5905 -722 -307 157 O HETATM 1270 O HOH A 347 6.721 -3.613 -2.342 0.50 48.24 O ANISOU 1270 O HOH A 347 6102 6213 6015 -992 -104 478 O HETATM 1271 O HOH A 348 1.597 -6.588 17.145 1.00 79.57 O ANISOU 1271 O HOH A 348 10414 10001 9817 -395 -691 251 O HETATM 1272 O HOH A 349 18.214 1.837 -5.518 0.50 50.15 O ANISOU 1272 O HOH A 349 6403 6363 6287 -885 -503 452 O HETATM 1273 O HOH A 350 4.757 16.114 -0.039 0.50 58.59 O ANISOU 1273 O HOH A 350 7427 7555 7277 153 -403 3 O HETATM 1274 O HOH A 351 9.165 -15.301 3.713 0.50 54.06 O ANISOU 1274 O HOH A 351 6475 7196 6867 -349 202 34 O HETATM 1275 O HOH A 352 7.105 17.312 12.732 1.00 51.97 O ANISOU 1275 O HOH A 352 6808 6587 6351 35 -585 -495 O HETATM 1276 O HOH A 353 1.255 -13.178 3.536 1.00 61.38 O ANISOU 1276 O HOH A 353 7791 7735 7796 17 -108 120 O HETATM 1277 O HOH A 354 7.683 4.801 23.692 1.00 55.47 O ANISOU 1277 O HOH A 354 6734 6099 6342 -249 -108 451 O CONECT 227 715 CONECT 356 809 CONECT 500 933 CONECT 558 611 CONECT 559 612 CONECT 611 558 CONECT 612 559 CONECT 715 227 CONECT 809 356 CONECT 933 500 MASTER 228 0 0 4 7 0 0 6 1276 1 10 10 END