HEADER HYDROLASE 19-NOV-01 1KF5 TITLE ATOMIC RESOLUTION STRUCTURE OF RNASE A AT PH 7.1 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 1KF5 1 VERSN REVDAT 2 06-MAR-02 1KF5 1 JRNL REVDAT 1 19-DEC-01 1KF5 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)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 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) : 42225 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)) : 37101 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1055 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 237 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1139.69 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 892.25 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 25 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11414 REMARK 3 NUMBER OF RESTRAINTS : 14207 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.015 REMARK 3 ANGLE DISTANCES (A) : 0.033 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.140 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: PLEASE NOTE: CHOH 215 IS ALTERNATIVE REMARK 3 ONLY TO THE A CONFORMER OF GLN 101. CHOH 216 IS ALTERNATIVE REMARK 3 ONLY TO THE A CONFORMER OF GLN 101. REMARK 4 REMARK 4 1KF5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-01. REMARK 100 THE RCSB ID CODE IS RCSB014888. 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 : 7.1 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 : 42236 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) : 0.04300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 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 (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.30700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.700 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 7.1, 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 - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 CYS A 72 CB - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 CYS A 72 N - CA - CB ANGL. DEV. = -11.9 DEGREES REMARK 500 CYS A 72 CA - CB - SG ANGL. DEV. = -11.8 DEGREES REMARK 500 ASN A 113 OD1 - CG - ND2 ANGL. DEV. = 21.4 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 64.19 -102.00 REMARK 500 GLN A 60 -135.02 -101.67 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: 1KF7 RELATED DB: PDB REMARK 900 1KF7 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 8.0. REMARK 900 RELATED ID: 1KF8 RELATED DB: PDB REMARK 900 1KF8 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 8.8. DBREF 1KF5 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 *229(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 2.02 SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.03 SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.01 SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.03 CISPEP 1 TYR A 92 PRO A 93 0 7.23 CISPEP 2 ASN A 113 PRO A 114 0 1.47 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 21.024 9.064 27.802 1.00 27.64 N ANISOU 1 N LYS A 1 3546 4273 2682 218 -826 -1388 N ATOM 2 CA LYS A 1 20.752 7.874 27.054 1.00 26.76 C ANISOU 2 CA LYS A 1 2844 4449 2876 710 -1249 -1660 C ATOM 3 C LYS A 1 20.027 8.196 25.726 1.00 22.66 C ANISOU 3 C LYS A 1 1860 3850 2898 836 -860 -1582 C ATOM 4 O LYS A 1 19.630 9.319 25.465 1.00 26.39 O ANISOU 4 O LYS A 1 2614 3590 3822 568 -1712 -1842 O ATOM 5 CB LYS A 1 19.782 7.062 27.959 1.00 42.17 C ATOM 6 CG LYS A 1 20.409 5.862 28.640 1.00 78.45 C ATOM 7 CD LYS A 1 19.838 5.639 30.035 1.00105.34 C ATOM 8 CE LYS A 1 18.511 4.894 29.964 1.00113.07 C ATOM 9 NZ LYS A 1 17.412 5.673 30.621 1.00124.16 N ATOM 10 N GLU A 2 19.854 7.222 24.879 1.00 16.87 N ANISOU 10 N GLU A 2 1577 3001 1832 45 -279 -589 N ATOM 11 CA GLU A 2 19.103 7.349 23.665 1.00 14.46 C ANISOU 11 CA GLU A 2 1520 2206 1768 4 -134 -498 C ATOM 12 C GLU A 2 17.690 7.841 23.942 1.00 16.04 C ANISOU 12 C GLU A 2 1663 2722 1709 262 -200 -795 C ATOM 13 O GLU A 2 16.984 7.298 24.761 1.00 19.39 O ANISOU 13 O GLU A 2 1607 3697 2065 210 -3 -553 O ATOM 14 CB GLU A 2 19.068 5.991 23.004 1.00 15.42 C ANISOU 14 CB GLU A 2 1773 2288 1797 241 -252 -541 C ATOM 15 CG GLU A 2 18.526 5.986 21.614 1.00 15.58 C ANISOU 15 CG GLU A 2 2099 2062 1757 90 -357 -388 C ATOM 16 CD GLU A 2 18.461 4.620 20.957 1.00 15.03 C ANISOU 16 CD GLU A 2 2084 2013 1614 188 -172 -371 C ATOM 17 OE1 GLU A 2 18.244 3.646 21.678 1.00 18.51 O ANISOU 17 OE1 GLU A 2 3238 2122 1674 -221 -10 -422 O ATOM 18 OE2 GLU A 2 18.663 4.515 19.752 1.00 15.51 O ANISOU 18 OE2 GLU A 2 2024 2135 1733 18 -134 -412 O ATOM 19 N THR A 3 17.237 8.833 23.205 1.00 16.70 N ANISOU 19 N THR A 3 1631 2791 1921 262 -642 -973 N ATOM 20 CA THR A 3 15.865 9.315 23.360 1.00 18.81 C ANISOU 20 CA THR A 3 1817 3150 2179 587 -780 -1229 C ATOM 21 C THR A 3 14.854 8.379 22.713 1.00 16.50 C ANISOU 21 C THR A 3 1608 2784 1876 559 -488 -824 C ATOM 22 O THR A 3 15.205 7.600 21.823 1.00 15.49 O ANISOU 22 O THR A 3 1615 2564 1706 189 -248 -812 O ATOM 23 CB THR A 3 15.696 10.742 22.848 1.00 22.74 C ANISOU 23 CB THR A 3 2930 2765 2943 672 -1147 -1557 C ATOM 24 OG1 THR A 3 15.838 10.740 21.451 1.00 23.07 O ANISOU 24 OG1 THR A 3 2893 2809 3065 176 -943 -753 O ATOM 25 CG2 THR A 3 16.709 11.707 23.397 1.00 28.41 C ANISOU 25 CG2 THR A 3 3352 3096 4348 464 -1617 -1820 C ATOM 26 N ALA A 4 13.619 8.507 23.089 1.00 17.60 N ANISOU 26 N ALA A 4 1658 3294 1735 517 -291 -886 N ATOM 27 CA ALA A 4 12.544 7.694 22.496 1.00 16.48 C ANISOU 27 CA ALA A 4 1649 3076 1538 465 -238 -585 C ATOM 28 C ALA A 4 12.451 7.974 21.018 1.00 14.88 C ANISOU 28 C ALA A 4 1656 2385 1613 522 -259 -585 C ATOM 29 O ALA A 4 12.192 7.074 20.223 1.00 14.75 O ANISOU 29 O ALA A 4 1740 2331 1535 268 -129 -552 O ATOM 30 CB ALA A 4 11.217 8.011 23.219 1.00 21.42 C ANISOU 30 CB ALA A 4 1761 4525 1852 162 102 -782 C ATOM 31 N ALA A 5 12.583 9.228 20.593 1.00 15.35 N ANISOU 31 N ALA A 5 1725 2266 1842 440 -426 -736 N ATOM 32 CA ALA A 5 12.482 9.549 19.183 1.00 14.89 C ANISOU 32 CA ALA A 5 1659 2012 1988 299 -374 -472 C ATOM 33 C ALA A 5 13.608 8.909 18.388 1.00 13.83 C ANISOU 33 C ALA A 5 1588 1761 1907 19 -350 -442 C ATOM 34 O ALA A 5 13.401 8.409 17.284 1.00 14.06 O ANISOU 34 O ALA A 5 1784 1759 1801 22 -338 -393 O ATOM 35 CB ALA A 5 12.496 11.058 19.052 1.00 20.18 C ANISOU 35 CB ALA A 5 2777 1933 2959 567 -384 -502 C ATOM 36 N ALA A 6 14.822 8.875 18.900 1.00 14.11 N ANISOU 36 N ALA A 6 1617 1732 2012 83 -418 -510 N ATOM 37 CA ALA A 6 15.982 8.304 18.273 1.00 13.82 C ANISOU 37 CA ALA A 6 1501 1607 2140 -133 -175 -275 C ATOM 38 C ALA A 6 15.821 6.798 18.197 1.00 11.94 C ANISOU 38 C ALA A 6 1372 1651 1513 -10 -204 -198 C ATOM 39 O ALA A 6 16.190 6.186 17.186 1.00 12.47 O ANISOU 39 O ALA A 6 1562 1690 1487 -47 6 -240 O ATOM 40 CB ALA A 6 17.270 8.670 19.010 1.00 16.99 C ANISOU 40 CB ALA A 6 1608 1932 2916 -166 -566 -376 C ATOM 41 N LYS A 7 15.286 6.212 19.253 1.00 11.86 N ANISOU 41 N LYS A 7 1471 1756 1281 5 -159 -287 N ATOM 42 CA LYS A 7 15.038 4.788 19.283 1.00 11.90 C ANISOU 42 CA LYS A 7 1464 1724 1333 32 -250 -131 C ATOM 43 C LYS A 7 14.027 4.424 18.187 1.00 10.67 C ANISOU 43 C LYS A 7 1308 1599 1146 12 -28 -176 C ATOM 44 O LYS A 7 14.189 3.397 17.512 1.00 11.38 O ANISOU 44 O LYS A 7 1630 1475 1219 141 -27 -143 O ATOM 45 CB LYS A 7 14.582 4.324 20.663 1.00 14.28 C ANISOU 45 CB LYS A 7 1996 2220 1210 129 -204 23 C ATOM 46 CG LYS A 7 14.239 2.871 20.752 1.00 20.61 C ANISOU 46 CG LYS A 7 3523 2321 1985 -171 -223 548 C ATOM 47 CD LYS A 7 13.844 2.489 22.181 1.00 33.82 C ANISOU 47 CD LYS A 7 6893 3477 2481 -1081 499 925 C ATOM 48 CE LYS A 7 12.577 1.630 22.285 1.00 56.62 C ANISOU 48 CE LYS A 7 8529 8070 4915 -3643 1497 2270 C ATOM 49 NZ LYS A 7 12.119 1.480 23.708 1.00 71.15 N ANISOU 49 NZ LYS A 7 11203 10922 4908 -5828 2856 -168 N ATOM 50 N PHE A 8 12.979 5.212 18.007 1.00 10.63 N ANISOU 50 N PHE A 8 1306 1534 1198 36 -96 -235 N ATOM 51 CA PHE A 8 12.024 4.949 16.930 1.00 10.36 C ANISOU 51 CA PHE A 8 1276 1369 1293 -16 -90 -179 C ATOM 52 C PHE A 8 12.746 4.945 15.574 1.00 9.83 C ANISOU 52 C PHE A 8 1278 1227 1228 59 -134 -134 C ATOM 53 O PHE A 8 12.465 4.063 14.745 1.00 10.75 O ANISOU 53 O PHE A 8 1398 1348 1338 -59 -64 -252 O ATOM 54 CB PHE A 8 10.911 6.004 16.958 1.00 11.68 C ANISOU 54 CB PHE A 8 1301 1682 1457 170 -23 -325 C ATOM 55 CG PHE A 8 9.907 5.830 15.848 1.00 10.85 C ANISOU 55 CG PHE A 8 1330 1493 1300 114 -28 -233 C ATOM 56 CD1 PHE A 8 10.090 6.395 14.605 1.00 12.15 C ANISOU 56 CD1 PHE A 8 1399 1761 1455 117 41 -25 C ATOM 57 CD2 PHE A 8 8.759 5.057 16.001 1.00 11.89 C ANISOU 57 CD2 PHE A 8 1299 1642 1575 53 -5 -31 C ATOM 58 CE1 PHE A 8 9.227 6.194 13.576 1.00 13.59 C ANISOU 58 CE1 PHE A 8 1514 2334 1313 327 -27 -103 C ATOM 59 CE2 PHE A 8 7.864 4.915 14.984 1.00 13.17 C ANISOU 59 CE2 PHE A 8 1506 1668 1831 -1 -222 -187 C ATOM 60 CZ PHE A 8 8.101 5.431 13.749 1.00 13.43 C ANISOU 60 CZ PHE A 8 1502 1915 1685 359 -352 -221 C ATOM 61 N GLU A 9 13.593 5.901 15.318 1.00 10.42 N ANISOU 61 N GLU A 9 1367 1228 1363 -32 -38 -162 N ATOM 62 CA GLU A 9 14.305 5.925 14.052 1.00 10.60 C ANISOU 62 CA GLU A 9 1498 1230 1298 1 -94 -36 C ATOM 63 C GLU A 9 15.155 4.670 13.882 1.00 9.91 C ANISOU 63 C GLU A 9 1349 1284 1133 -77 57 -23 C ATOM 64 O GLU A 9 15.195 4.088 12.797 1.00 10.76 O ANISOU 64 O GLU A 9 1508 1466 1115 2 54 -2 O ATOM 65 CB AGLU A 9 15.212 7.143 13.913 0.56 12.10 C ANISOU 65 CB AGLU A 9 1800 1340 1457 -195 -29 72 C ATOM 66 CB BGLU A 9 15.095 7.234 13.927 0.44 12.66 C ANISOU 66 CB BGLU A 9 1536 1271 2001 36 281 19 C ATOM 67 CG AGLU A 9 14.414 8.420 13.864 0.56 14.71 C ANISOU 67 CG AGLU A 9 2095 1311 2184 -149 -167 346 C ATOM 68 CG BGLU A 9 15.679 7.482 12.555 0.44 15.54 C ANISOU 68 CG BGLU A 9 2183 1550 2170 -395 589 -84 C ATOM 69 CD AGLU A 9 15.281 9.640 13.695 0.56 18.19 C ANISOU 69 CD AGLU A 9 2444 1407 3062 -411 -619 427 C ATOM 70 CD BGLU A 9 16.805 8.490 12.468 0.44 24.25 C ANISOU 70 CD BGLU A 9 3202 3246 2765 -1731 863 -280 C ATOM 71 OE1AGLU A 9 14.894 10.738 14.137 0.56 23.84 O ANISOU 71 OE1AGLU A 9 4025 1450 3582 -495 -192 115 O ATOM 72 OE1BGLU A 9 17.366 8.922 13.475 0.44 37.01 O ANISOU 72 OE1BGLU A 9 5354 4828 3879 -3288 -1290 1009 O ATOM 73 OE2AGLU A 9 16.386 9.500 13.092 0.56 22.58 O ANISOU 73 OE2AGLU A 9 1961 1799 4820 -766 -502 523 O ATOM 74 OE2BGLU A 9 17.087 8.800 11.302 0.44 26.30 O ANISOU 74 OE2BGLU A 9 2108 4527 3360 -979 578 1295 O ATOM 75 N ARG A 10 15.903 4.299 14.908 1.00 9.80 N ANISOU 75 N ARG A 10 1296 1202 1225 -7 -16 -120 N ATOM 76 CA ARG A 10 16.781 3.140 14.837 1.00 9.97 C ANISOU 76 CA ARG A 10 1252 1372 1164 7 62 -107 C ATOM 77 C ARG A 10 15.996 1.862 14.630 1.00 9.17 C ANISOU 77 C ARG A 10 1107 1227 1151 56 1 6 C ATOM 78 O ARG A 10 16.394 0.976 13.866 1.00 10.49 O ANISOU 78 O ARG A 10 1409 1352 1226 72 124 -53 O ATOM 79 CB ARG A 10 17.626 3.049 16.113 1.00 11.27 C ANISOU 79 CB ARG A 10 1200 1717 1367 51 -108 -164 C ATOM 80 CG ARG A 10 18.528 1.829 16.173 1.00 11.63 C ANISOU 80 CG ARG A 10 1521 1640 1259 166 -111 -100 C ATOM 81 CD ARG A 10 19.506 1.845 17.333 1.00 12.82 C ANISOU 81 CD ARG A 10 1733 1746 1391 302 -275 -121 C ATOM 82 NE ARG A 10 18.868 1.925 18.639 1.00 13.06 N ANISOU 82 NE ARG A 10 1945 1634 1383 163 -266 -165 N ATOM 83 CZ ARG A 10 18.403 0.886 19.306 1.00 16.04 C ANISOU 83 CZ ARG A 10 2984 1749 1363 -25 -54 -201 C ATOM 84 NH1 ARG A 10 18.441 -0.325 18.809 1.00 19.46 N ANISOU 84 NH1 ARG A 10 3953 1738 1704 -268 394 -352 N ATOM 85 NH2 ARG A 10 17.859 1.111 20.500 1.00 20.53 N ANISOU 85 NH2 ARG A 10 4020 2382 1397 -418 381 -312 N ATOM 86 N AGLN A 11 14.878 1.702 15.326 0.54 9.53 N ANISOU 86 N AGLN A 11 1326 1209 1085 -3 66 -58 N ATOM 87 N BGLN A 11 14.883 1.729 15.314 0.46 9.50 N ANISOU 87 N BGLN A 11 1326 1180 1103 -5 70 -72 N ATOM 88 CA AGLN A 11 14.096 0.483 15.233 0.54 9.22 C ANISOU 88 CA AGLN A 11 1384 1147 971 8 74 137 C ATOM 89 CA BGLN A 11 14.123 0.491 15.227 0.46 9.60 C ANISOU 89 CA BGLN A 11 1290 1170 1189 14 -57 76 C ATOM 90 C AGLN A 11 13.279 0.385 13.943 0.54 9.45 C ANISOU 90 C AGLN A 11 1410 1130 1052 -31 32 -12 C ATOM 91 C BGLN A 11 13.265 0.389 13.973 0.46 9.43 C ANISOU 91 C BGLN A 11 1467 1112 1006 -66 25 13 C ATOM 92 O AGLN A 11 13.013 -0.724 13.527 0.54 11.97 O ANISOU 92 O AGLN A 11 1967 1120 1462 -71 -206 -102 O ATOM 93 O BGLN A 11 13.005 -0.720 13.535 0.46 11.93 O ANISOU 93 O BGLN A 11 1969 1111 1452 -74 -221 -108 O ATOM 94 CB AGLN A 11 13.153 0.280 16.415 0.54 9.75 C ANISOU 94 CB AGLN A 11 1259 1404 1042 123 120 25 C ATOM 95 CB BGLN A 11 13.329 0.361 16.514 0.46 13.81 C ANISOU 95 CB BGLN A 11 2772 1485 991 -447 200 346 C ATOM 96 CG AGLN A 11 13.849 0.187 17.734 0.54 11.13 C ANISOU 96 CG AGLN A 11 1737 1500 993 248 106 363 C ATOM 97 CG BGLN A 11 12.514 -0.916 16.652 0.46 15.66 C ANISOU 97 CG BGLN A 11 2203 1452 2296 -165 404 526 C ATOM 98 CD AGLN A 11 12.923 -0.244 18.858 0.54 16.09 C ANISOU 98 CD AGLN A 11 2486 2431 1195 -51 405 563 C ATOM 99 CD BGLN A 11 12.165 -1.068 18.123 0.46 25.01 C ANISOU 99 CD BGLN A 11 3794 3024 2685 -1040 894 1490 C ATOM 100 OE1AGLN A 11 13.372 -0.912 19.820 0.54 31.54 O ANISOU 100 OE1AGLN A 11 3853 5920 2212 701 775 2553 O ATOM 101 OE1BGLN A 11 12.980 -1.379 18.992 0.46 38.92 O ANISOU 101 OE1BGLN A 11 4866 7319 2603 874 1551 3213 O ATOM 102 NE2AGLN A 11 11.731 0.249 18.859 0.54 22.15 N ANISOU 102 NE2AGLN A 11 2247 4532 1639 64 774 654 N ATOM 103 NE2BGLN A 11 10.912 -0.925 18.478 0.46 49.31 N ANISOU 103 NE2BGLN A 11 5909 8843 3982 4625 2904 4708 N ATOM 104 N HIS A 12 12.793 1.512 13.424 1.00 9.06 N ANISOU 104 N HIS A 12 1358 1076 1009 -101 -14 45 N ATOM 105 CA HIS A 12 11.717 1.457 12.431 1.00 9.84 C ANISOU 105 CA HIS A 12 1506 1247 986 -183 -91 102 C ATOM 106 C HIS A 12 11.971 2.122 11.115 1.00 10.53 C ANISOU 106 C HIS A 12 1790 1179 1032 -246 -170 63 C ATOM 107 O HIS A 12 11.237 1.875 10.183 1.00 16.06 O ANISOU 107 O HIS A 12 2932 1965 1205 -1053 -672 380 O ATOM 108 CB HIS A 12 10.403 1.967 13.013 1.00 10.73 C ANISOU 108 CB HIS A 12 1528 1300 1251 -1 -176 139 C ATOM 109 CG HIS A 12 9.960 1.240 14.189 1.00 9.93 C ANISOU 109 CG HIS A 12 1302 1341 1132 27 -29 -17 C ATOM 110 ND1 HIS A 12 9.551 -0.069 14.126 1.00 11.13 N ANISOU 110 ND1 HIS A 12 1561 1424 1246 -139 273 -32 N ATOM 111 CD2 HIS A 12 9.802 1.594 15.486 1.00 11.29 C ANISOU 111 CD2 HIS A 12 1427 1635 1226 100 -51 -151 C ATOM 112 CE1 HIS A 12 9.232 -0.464 15.386 1.00 12.32 C ANISOU 112 CE1 HIS A 12 1783 1615 1284 -79 495 -63 C ATOM 113 NE2 HIS A 12 9.375 0.535 16.213 1.00 11.82 N ANISOU 113 NE2 HIS A 12 1558 1748 1184 107 181 -119 N ATOM 114 N MET A 13 12.965 3.010 10.985 1.00 9.90 N ANISOU 114 N MET A 13 1488 1321 952 -57 37 75 N ATOM 115 CA MET A 13 13.115 3.755 9.740 1.00 9.98 C ANISOU 115 CA MET A 13 1565 1326 901 -32 86 107 C ATOM 116 C MET A 13 14.139 3.163 8.816 1.00 10.14 C ANISOU 116 C MET A 13 1444 1402 1005 50 81 143 C ATOM 117 O MET A 13 15.280 2.912 9.268 1.00 12.38 O ANISOU 117 O MET A 13 1592 2053 1060 297 -28 105 O ATOM 118 CB MET A 13 13.469 5.201 10.016 1.00 11.40 C ANISOU 118 CB MET A 13 1746 1275 1309 52 66 74 C ATOM 119 CG MET A 13 12.329 5.989 10.661 1.00 12.84 C ANISOU 119 CG MET A 13 2055 1417 1406 222 -9 -144 C ATOM 120 SD MET A 13 10.844 6.133 9.690 1.00 14.26 S ANISOU 120 SD MET A 13 2082 1932 1403 546 -23 -2 S ATOM 121 CE MET A 13 11.465 6.737 8.141 1.00 16.55 C ANISOU 121 CE MET A 13 2536 2228 1526 612 49 302 C ATOM 122 N ASP A 14 13.840 2.986 7.554 1.00 9.61 N ANISOU 122 N ASP A 14 1442 1312 899 -38 91 91 N ATOM 123 CA ASP A 14 14.857 2.688 6.571 1.00 9.92 C ANISOU 123 CA ASP A 14 1513 1270 986 30 196 124 C ATOM 124 C ASP A 14 14.553 3.435 5.273 1.00 10.47 C ANISOU 124 C ASP A 14 1539 1457 981 12 161 193 C ATOM 125 O ASP A 14 13.978 2.927 4.323 1.00 12.65 O ANISOU 125 O ASP A 14 1952 1863 990 -196 -10 114 O ATOM 126 CB ASP A 14 14.995 1.188 6.270 1.00 12.04 C ANISOU 126 CB ASP A 14 2056 1264 1253 -24 362 91 C ATOM 127 CG ASP A 14 16.148 0.926 5.327 1.00 13.11 C ANISOU 127 CG ASP A 14 2233 1360 1389 229 490 44 C ATOM 128 OD1 ASP A 14 16.934 1.839 5.052 1.00 15.22 O ANISOU 128 OD1 ASP A 14 2029 1812 1942 69 630 124 O ATOM 129 OD2 ASP A 14 16.219 -0.235 4.830 1.00 17.19 O ANISOU 129 OD2 ASP A 14 3245 1545 1744 243 919 -26 O ATOM 130 N SER A 15 14.983 4.697 5.250 1.00 11.44 N ANISOU 130 N SER A 15 1831 1385 1131 -89 61 280 N ATOM 131 CA SER A 15 14.768 5.604 4.104 1.00 13.23 C ANISOU 131 CA SER A 15 2016 1668 1344 33 211 478 C ATOM 132 C SER A 15 15.772 5.302 2.993 1.00 13.12 C ANISOU 132 C SER A 15 2105 1629 1250 -57 216 376 C ATOM 133 O SER A 15 15.666 5.925 1.942 1.00 17.31 O ANISOU 133 O SER A 15 3260 1945 1372 301 447 577 O ATOM 134 CB ASER A 15 15.020 7.028 4.590 0.63 17.47 C ANISOU 134 CB ASER A 15 3082 1368 2189 579 629 410 C ATOM 135 CB BSER A 15 14.896 7.065 4.499 0.37 14.16 C ANISOU 135 CB BSER A 15 2183 1554 1645 86 938 637 C ATOM 136 OG ASER A 15 14.201 7.360 5.694 0.63 14.87 O ANISOU 136 OG ASER A 15 2084 1628 1938 75 147 164 O ATOM 137 OG BSER A 15 16.195 7.311 5.001 0.37 18.38 O ANISOU 137 OG BSER A 15 2657 1659 2666 -210 352 28 O ATOM 138 N SER A 16 16.706 4.397 3.189 1.00 14.08 N ANISOU 138 N SER A 16 2021 1959 1368 31 373 464 N ATOM 139 CA SER A 16 17.786 4.110 2.245 1.00 14.34 C ANISOU 139 CA SER A 16 1874 2122 1451 -124 358 427 C ATOM 140 C SER A 16 17.364 3.097 1.183 1.00 13.76 C ANISOU 140 C SER A 16 1954 1898 1376 73 351 453 C ATOM 141 O SER A 16 18.092 2.949 0.189 1.00 16.33 O ANISOU 141 O SER A 16 2321 2396 1487 100 574 368 O ATOM 142 CB ASER A 16 19.017 3.511 2.946 0.68 16.53 C ANISOU 142 CB ASER A 16 1726 2788 1767 -200 260 429 C ATOM 143 CB BSER A 16 19.033 3.717 3.032 0.32 21.53 C ANISOU 143 CB BSER A 16 1813 2876 3491 -69 -496 -298 C ATOM 144 OG ASER A 16 18.894 2.116 3.262 0.68 19.16 O ANISOU 144 OG ASER A 16 2228 2885 2165 490 434 863 O ATOM 145 OG BSER A 16 19.485 4.758 3.895 0.32 30.92 O ANISOU 145 OG BSER A 16 1809 5413 4525 -1159 25 -1898 O ATOM 146 N THR A 17 16.218 2.445 1.348 1.00 14.13 N ANISOU 146 N THR A 17 2098 1532 1737 49 381 382 N ATOM 147 CA THR A 17 15.748 1.491 0.368 1.00 14.70 C ANISOU 147 CA THR A 17 2179 1578 1827 136 419 233 C ATOM 148 C THR A 17 14.258 1.716 0.173 1.00 13.80 C ANISOU 148 C THR A 17 2237 1617 1388 103 393 195 C ATOM 149 O THR A 17 13.583 2.170 1.082 1.00 14.83 O ANISOU 149 O THR A 17 2108 2050 1476 112 258 -9 O ATOM 150 CB ATHR A 17 15.963 0.031 0.864 0.63 14.67 C ANISOU 150 CB ATHR A 17 2122 1632 1821 69 332 256 C ATOM 151 CB BTHR A 17 15.998 -0.006 0.603 0.37 18.40 C ANISOU 151 CB BTHR A 17 3292 1635 2062 740 647 -37 C ATOM 152 OG1ATHR A 17 15.258 -0.186 2.078 0.63 15.24 O ANISOU 152 OG1ATHR A 17 2004 1756 2031 25 353 556 O ATOM 153 OG1BTHR A 17 15.658 -0.773 -0.577 0.37 18.11 O ANISOU 153 OG1BTHR A 17 2626 1722 2531 100 342 -64 O ATOM 154 CG2ATHR A 17 17.454 -0.208 1.155 0.63 18.63 C ANISOU 154 CG2ATHR A 17 2031 2114 2933 513 559 91 C ATOM 155 CG2BTHR A 17 15.131 -0.572 1.704 0.37 25.09 C ANISOU 155 CG2BTHR A 17 5231 1523 2780 472 1353 570 C ATOM 156 N SER A 18 13.708 1.374 -0.975 1.00 14.19 N ANISOU 156 N SER A 18 2508 1487 1397 124 371 156 N ATOM 157 CA SER A 18 12.309 1.581 -1.249 1.00 14.54 C ANISOU 157 CA SER A 18 2600 1595 1330 154 138 181 C ATOM 158 C SER A 18 11.442 0.407 -0.822 1.00 13.08 C ANISOU 158 C SER A 18 2348 1513 1108 247 52 68 C ATOM 159 O SER A 18 10.209 0.598 -0.681 1.00 14.49 O ANISOU 159 O SER A 18 2321 1759 1427 321 42 116 O ATOM 160 CB ASER A 18 12.043 2.025 -2.686 0.54 27.18 C ANISOU 160 CB ASER A 18 4212 3844 2272 -1410 -1051 1707 C ATOM 161 CB BSER A 18 12.067 1.782 -2.755 0.21 22.03 C ANISOU 161 CB BSER A 18 4517 2075 1777 -814 -808 951 C ATOM 162 CB CSER A 18 12.000 1.802 -2.737 0.25 15.87 C ANISOU 162 CB CSER A 18 3235 1383 1414 118 30 258 C ATOM 163 OG ASER A 18 12.876 3.140 -3.032 0.54 21.49 O ANISOU 163 OG ASER A 18 3800 2392 1973 -354 -273 952 O ATOM 164 OG BSER A 18 12.346 0.569 -3.437 0.21 22.19 O ANISOU 164 OG BSER A 18 4405 3129 896 -1259 -79 225 O ATOM 165 OG CSER A 18 10.630 2.150 -2.918 0.25 28.30 O ANISOU 165 OG CSER A 18 3393 5003 2356 242 -985 -77 O ATOM 166 N ALA A 19 12.011 -0.759 -0.632 1.00 13.65 N ANISOU 166 N ALA A 19 2209 1565 1413 221 230 213 N ATOM 167 CA ALA A 19 11.361 -1.991 -0.255 1.00 13.51 C ANISOU 167 CA ALA A 19 2296 1447 1390 124 149 -35 C ATOM 168 C ALA A 19 12.448 -2.996 0.096 1.00 13.12 C ANISOU 168 C ALA A 19 2236 1469 1280 132 218 13 C ATOM 169 O ALA A 19 13.592 -2.816 -0.297 1.00 17.02 O ANISOU 169 O ALA A 19 2399 1666 2400 189 565 317 O ATOM 170 CB ALA A 19 10.474 -2.561 -1.379 1.00 17.64 C ANISOU 170 CB ALA A 19 2903 1931 1869 113 -489 -82 C ATOM 171 N ALA A 20 12.089 -4.048 0.770 1.00 12.88 N ANISOU 171 N ALA A 20 2105 1421 1369 149 245 -74 N ATOM 172 CA ALA A 20 13.019 -5.139 1.009 1.00 13.04 C ANISOU 172 CA ALA A 20 2179 1336 1441 150 237 -146 C ATOM 173 C ALA A 20 13.351 -5.803 -0.326 1.00 15.32 C ANISOU 173 C ALA A 20 2809 1477 1535 262 639 -33 C ATOM 174 O ALA A 20 12.492 -6.137 -1.092 1.00 21.94 O ANISOU 174 O ALA A 20 3699 2869 1768 55 271 -802 O ATOM 175 CB ALA A 20 12.437 -6.168 1.944 1.00 14.80 C ANISOU 175 CB ALA A 20 2504 1712 1405 445 344 240 C ATOM 176 N SER A 21 14.611 -6.107 -0.543 1.00 18.91 N ANISOU 176 N SER A 21 3172 1936 2075 650 1123 322 N ATOM 177 CA SER A 21 15.043 -6.605 -1.825 1.00 22.39 C ANISOU 177 CA SER A 21 4174 2027 2305 1179 1600 471 C ATOM 178 C SER A 21 15.370 -8.086 -1.843 1.00 17.70 C ANISOU 178 C SER A 21 3277 1794 1655 513 958 317 C ATOM 179 O SER A 21 15.662 -8.639 -2.897 1.00 20.17 O ANISOU 179 O SER A 21 3831 2271 1560 946 992 312 O ATOM 180 CB SER A 21 16.330 -5.892 -2.353 1.00 34.53 C ANISOU 180 CB SER A 21 6740 1591 4790 479 4178 373 C ATOM 181 OG SER A 21 17.341 -5.985 -1.348 1.00 51.66 O ANISOU 181 OG SER A 21 4629 3149 11849 -906 1787 929 O ATOM 182 N SER A 22 15.355 -8.761 -0.704 1.00 15.28 N ANISOU 182 N SER A 22 2891 1504 1412 324 545 12 N ATOM 183 CA SER A 22 15.643 -10.167 -0.638 1.00 13.64 C ANISOU 183 CA SER A 22 2642 1384 1158 123 433 -154 C ATOM 184 C SER A 22 15.092 -10.720 0.664 1.00 12.84 C ANISOU 184 C SER A 22 2442 1357 1081 131 290 -183 C ATOM 185 O SER A 22 14.757 -10.008 1.596 1.00 13.26 O ANISOU 185 O SER A 22 2393 1485 1162 71 397 -260 O ATOM 186 CB SER A 22 17.118 -10.505 -0.737 1.00 16.84 C ANISOU 186 CB SER A 22 2772 1945 1682 451 673 12 C ATOM 187 OG SER A 22 17.740 -10.359 0.528 1.00 19.68 O ANISOU 187 OG SER A 22 2573 2866 2038 27 335 -206 O ATOM 188 N SER A 23 15.050 -12.038 0.726 1.00 13.74 N ANISOU 188 N SER A 23 2799 1401 1020 -83 345 -310 N ATOM 189 CA SER A 23 14.613 -12.760 1.922 1.00 14.27 C ANISOU 189 CA SER A 23 2950 1353 1119 -99 164 -203 C ATOM 190 C SER A 23 15.502 -12.494 3.119 1.00 13.61 C ANISOU 190 C SER A 23 2777 1331 1063 -110 237 -246 C ATOM 191 O SER A 23 15.014 -12.752 4.230 1.00 16.74 O ANISOU 191 O SER A 23 2994 2245 1120 -431 229 -133 O ATOM 192 CB ASER A 23 14.496 -14.237 1.598 0.86 17.94 C ANISOU 192 CB ASER A 23 3969 1398 1450 -481 -113 -219 C ATOM 193 CB BSER A 23 14.667 -14.251 1.537 0.14 17.86 C ANISOU 193 CB BSER A 23 3190 1302 2296 -614 -169 -375 C ATOM 194 OG ASER A 23 15.733 -14.770 1.306 0.86 23.29 O ANISOU 194 OG ASER A 23 4944 1391 2515 289 585 -436 O ATOM 195 OG BSER A 23 14.630 -15.048 2.699 0.14 19.44 O ANISOU 195 OG BSER A 23 3424 1205 2756 -410 -345 -46 O ATOM 196 N AASN A 24 16.719 -12.017 2.926 0.63 13.10 N ANISOU 196 N AASN A 24 2503 1283 1191 299 221 -179 N ATOM 197 N BASN A 24 16.724 -12.031 2.934 0.37 14.59 N ANISOU 197 N BASN A 24 2784 1438 1321 -99 311 -274 N ATOM 198 CA AASN A 24 17.646 -11.762 4.007 0.63 13.73 C ANISOU 198 CA AASN A 24 2375 1295 1545 284 66 -192 C ATOM 199 CA BASN A 24 17.619 -11.818 4.061 0.37 12.67 C ANISOU 199 CA BASN A 24 2223 1256 1336 182 447 -124 C ATOM 200 C AASN A 24 17.518 -10.393 4.667 0.63 12.51 C ANISOU 200 C AASN A 24 2221 1305 1228 214 75 -66 C ATOM 201 C BASN A 24 17.550 -10.404 4.620 0.37 10.91 C ANISOU 201 C BASN A 24 1902 1267 977 128 374 -31 C ATOM 202 O AASN A 24 18.255 -10.122 5.608 0.63 13.23 O ANISOU 202 O AASN A 24 2146 1551 1332 218 80 -237 O ATOM 203 O BASN A 24 18.272 -10.116 5.576 0.37 13.82 O ANISOU 203 O BASN A 24 2279 1599 1372 295 -11 -246 O ATOM 204 CB AASN A 24 19.111 -11.902 3.565 0.63 16.75 C ANISOU 204 CB AASN A 24 2463 1744 2158 278 258 -655 C ATOM 205 CB BASN A 24 19.056 -12.198 3.704 0.37 15.94 C ANISOU 205 CB BASN A 24 2348 1179 2528 80 893 -364 C ATOM 206 CG AASN A 24 19.437 -13.363 3.311 0.63 29.32 C ANISOU 206 CG AASN A 24 2815 2379 5944 1191 -883 -1852 C ATOM 207 CG BASN A 24 19.804 -12.848 4.850 0.37 21.97 C ANISOU 207 CG BASN A 24 2265 2956 3127 1118 748 -169 C ATOM 208 OD1AASN A 24 19.095 -14.203 4.130 0.63 38.59 O ANISOU 208 OD1AASN A 24 5264 1427 7970 1141 -2347 -606 O ATOM 209 OD1BASN A 24 19.352 -13.812 5.470 0.37 31.73 O ANISOU 209 OD1BASN A 24 3703 5656 2696 1394 1949 1704 O ATOM 210 ND2AASN A 24 20.083 -13.609 2.188 0.63 43.85 N ANISOU 210 ND2AASN A 24 3325 5052 8283 918 339 -4825 N ATOM 211 ND2BASN A 24 20.984 -12.308 5.141 0.37 41.47 N ANISOU 211 ND2BASN A 24 3416 7277 5065 -245 -775 -594 N ATOM 212 N TYR A 25 16.674 -9.545 4.122 1.00 11.48 N ANISOU 212 N TYR A 25 2030 1212 1121 97 214 -96 N ATOM 213 CA TYR A 25 16.571 -8.175 4.612 1.00 10.82 C ANISOU 213 CA TYR A 25 1803 1192 1117 30 206 -123 C ATOM 214 C TYR A 25 16.418 -8.103 6.123 1.00 10.42 C ANISOU 214 C TYR A 25 1645 1210 1105 -51 105 -31 C ATOM 215 O TYR A 25 17.131 -7.398 6.814 1.00 11.13 O ANISOU 215 O TYR A 25 1758 1322 1151 -144 155 -112 O ATOM 216 CB TYR A 25 15.441 -7.442 3.884 1.00 11.80 C ANISOU 216 CB TYR A 25 2219 1190 1075 95 5 -5 C ATOM 217 CG TYR A 25 15.241 -6.014 4.375 1.00 11.72 C ANISOU 217 CG TYR A 25 2018 1270 1164 48 -13 -58 C ATOM 218 CD1 TYR A 25 15.912 -4.946 3.805 1.00 12.58 C ANISOU 218 CD1 TYR A 25 2230 1271 1280 63 260 45 C ATOM 219 CD2 TYR A 25 14.353 -5.709 5.394 1.00 12.34 C ANISOU 219 CD2 TYR A 25 1885 1262 1541 109 213 -2 C ATOM 220 CE1 TYR A 25 15.737 -3.669 4.269 1.00 13.06 C ANISOU 220 CE1 TYR A 25 2461 1276 1225 56 219 100 C ATOM 221 CE2 TYR A 25 14.183 -4.446 5.868 1.00 13.09 C ANISOU 221 CE2 TYR A 25 2057 1331 1584 101 322 -3 C ATOM 222 CZ TYR A 25 14.871 -3.403 5.296 1.00 12.17 C ANISOU 222 CZ TYR A 25 2137 1220 1266 74 57 3 C ATOM 223 OH TYR A 25 14.707 -2.162 5.826 1.00 13.93 O ANISOU 223 OH TYR A 25 2485 1201 1608 221 162 -19 O ATOM 224 N CYS A 26 15.440 -8.795 6.661 1.00 10.09 N ANISOU 224 N CYS A 26 1755 1113 965 -91 98 -177 N ATOM 225 CA CYS A 26 15.159 -8.707 8.079 1.00 10.36 C ANISOU 225 CA CYS A 26 1668 1254 1015 -23 148 -94 C ATOM 226 C CYS A 26 16.331 -9.246 8.892 1.00 10.25 C ANISOU 226 C CYS A 26 1696 1229 969 -35 168 -120 C ATOM 227 O CYS A 26 16.710 -8.651 9.901 1.00 11.74 O ANISOU 227 O CYS A 26 1751 1537 1174 -91 97 -199 O ATOM 228 CB CYS A 26 13.865 -9.440 8.448 1.00 10.82 C ANISOU 228 CB CYS A 26 1696 1331 1083 -66 120 50 C ATOM 229 SG CYS A 26 12.353 -8.597 7.906 1.00 11.08 S ANISOU 229 SG CYS A 26 1688 1403 1117 -20 36 -23 S ATOM 230 N ASN A 27 16.888 -10.380 8.508 1.00 11.00 N ANISOU 230 N ASN A 27 1792 1320 1066 89 46 -74 N ATOM 231 CA ASN A 27 18.030 -10.908 9.276 1.00 11.59 C ANISOU 231 CA ASN A 27 1757 1430 1216 115 65 5 C ATOM 232 C ASN A 27 19.149 -9.882 9.378 1.00 12.23 C ANISOU 232 C ASN A 27 1632 1675 1338 83 114 -10 C ATOM 233 O ASN A 27 19.742 -9.702 10.456 1.00 14.66 O ANISOU 233 O ASN A 27 1836 2248 1486 -116 -111 31 O ATOM 234 CB ASN A 27 18.575 -12.167 8.591 1.00 12.80 C ANISOU 234 CB ASN A 27 1787 1524 1552 205 202 96 C ATOM 235 CG ASN A 27 17.648 -13.339 8.785 1.00 14.13 C ANISOU 235 CG ASN A 27 2208 1383 1778 102 283 42 C ATOM 236 OD1 ASN A 27 16.846 -13.404 9.677 1.00 15.69 O ANISOU 236 OD1 ASN A 27 2540 1608 1814 -177 423 108 O ATOM 237 ND2 ASN A 27 17.783 -14.345 7.947 1.00 21.41 N ANISOU 237 ND2 ASN A 27 3435 1542 3157 -153 1029 -622 N ATOM 238 N GLN A 28 19.441 -9.211 8.272 1.00 11.51 N ANISOU 238 N GLN A 28 1632 1458 1282 -6 207 -148 N ATOM 239 CA GLN A 28 20.525 -8.233 8.263 1.00 12.05 C ANISOU 239 CA GLN A 28 1494 1541 1542 19 208 -155 C ATOM 240 C GLN A 28 20.174 -6.986 9.046 1.00 11.27 C ANISOU 240 C GLN A 28 1492 1437 1354 -55 176 -61 C ATOM 241 O GLN A 28 21.010 -6.504 9.809 1.00 13.97 O ANISOU 241 O GLN A 28 1559 1867 1882 -17 -9 -386 O ATOM 242 CB AGLN A 28 20.852 -7.877 6.820 0.60 15.35 C ANISOU 242 CB AGLN A 28 2110 2018 1706 -451 653 -304 C ATOM 243 CB BGLN A 28 20.874 -7.855 6.831 0.40 17.19 C ANISOU 243 CB BGLN A 28 2670 2064 1798 -819 909 -516 C ATOM 244 CG AGLN A 28 21.424 -9.025 6.023 0.60 21.31 C ANISOU 244 CG AGLN A 28 2861 3008 2228 -429 831 -1196 C ATOM 245 CG BGLN A 28 22.073 -6.915 6.802 0.40 25.18 C ANISOU 245 CG BGLN A 28 3110 4585 1872 -2170 1096 -1021 C ATOM 246 CD AGLN A 28 21.597 -8.846 4.543 0.60 41.94 C ANISOU 246 CD AGLN A 28 8431 5238 2265 1798 1686 -876 C ATOM 247 CD BGLN A 28 23.345 -7.628 7.207 0.40 41.76 C ANISOU 247 CD BGLN A 28 2502 7473 5890 -1439 1324 -658 C ATOM 248 OE1AGLN A 28 22.316 -9.618 3.879 0.60 46.37 O ANISOU 248 OE1AGLN A 28 9432 5454 2732 1740 2346 -1068 O ATOM 249 OE1BGLN A 28 23.659 -8.766 6.854 0.40 77.22 O ANISOU 249 OE1BGLN A 28 5249 13623 10470 4139 -115 -6792 O ATOM 250 NE2AGLN A 28 20.928 -7.894 3.903 0.60 46.02 N ANISOU 250 NE2AGLN A 28 10659 3925 2900 1337 2408 264 N ATOM 251 NE2BGLN A 28 24.091 -6.818 7.957 0.40 65.75 N ANISOU 251 NE2BGLN A 28 2354 11567 11061 -1222 -1281 -3176 N ATOM 252 N MET A 29 18.956 -6.474 8.887 1.00 10.73 N ANISOU 252 N MET A 29 1478 1388 1210 -86 121 -171 N ATOM 253 CA MET A 29 18.563 -5.231 9.529 1.00 10.63 C ANISOU 253 CA MET A 29 1467 1295 1277 -93 80 -52 C ATOM 254 C MET A 29 18.339 -5.347 11.027 1.00 10.43 C ANISOU 254 C MET A 29 1516 1223 1226 -6 50 -86 C ATOM 255 O MET A 29 18.671 -4.461 11.789 1.00 11.96 O ANISOU 255 O MET A 29 1862 1241 1442 -163 -13 -195 O ATOM 256 CB MET A 29 17.353 -4.628 8.834 1.00 12.14 C ANISOU 256 CB MET A 29 1784 1428 1401 -18 -91 29 C ATOM 257 CG MET A 29 17.620 -4.180 7.453 1.00 16.95 C ANISOU 257 CG MET A 29 3264 1748 1427 -45 -216 226 C ATOM 258 SD MET A 29 18.668 -2.747 7.376 1.00 21.71 S ANISOU 258 SD MET A 29 3861 2201 2187 -631 114 751 S ATOM 259 CE MET A 29 17.714 -1.458 8.110 1.00 30.57 C ANISOU 259 CE MET A 29 7618 2132 1866 -909 946 -618 C ATOM 260 N MET A 30 17.764 -6.474 11.440 1.00 10.17 N ANISOU 260 N MET A 30 1545 1208 1109 -49 42 -55 N ATOM 261 CA MET A 30 17.535 -6.673 12.866 1.00 10.50 C ANISOU 261 CA MET A 30 1663 1242 1085 58 -1 -75 C ATOM 262 C MET A 30 18.858 -6.696 13.595 1.00 10.88 C ANISOU 262 C MET A 30 1644 1296 1195 -28 -36 12 C ATOM 263 O MET A 30 19.019 -6.185 14.699 1.00 13.55 O ANISOU 263 O MET A 30 1919 1909 1322 37 -133 -288 O ATOM 264 CB MET A 30 16.725 -7.946 13.088 1.00 10.75 C ANISOU 264 CB MET A 30 1595 1208 1282 24 68 4 C ATOM 265 CG MET A 30 15.317 -7.916 12.572 1.00 11.21 C ANISOU 265 CG MET A 30 1663 1314 1284 -53 109 -45 C ATOM 266 SD MET A 30 14.232 -6.704 13.372 1.00 12.47 S ANISOU 266 SD MET A 30 1813 1499 1424 186 212 117 S ATOM 267 CE MET A 30 13.929 -7.517 14.939 1.00 15.17 C ANISOU 267 CE MET A 30 2338 2012 1414 405 573 189 C ATOM 268 N LYS A 31 19.873 -7.328 13.002 1.00 11.71 N ANISOU 268 N LYS A 31 1668 1414 1366 12 -90 -49 N ATOM 269 CA LYS A 31 21.206 -7.379 13.573 1.00 12.92 C ANISOU 269 CA LYS A 31 1724 1482 1701 207 -214 49 C ATOM 270 C LYS A 31 21.874 -6.018 13.561 1.00 12.61 C ANISOU 270 C LYS A 31 1511 1642 1639 152 -199 31 C ATOM 271 O LYS A 31 22.405 -5.549 14.573 1.00 14.39 O ANISOU 271 O LYS A 31 1778 1913 1777 24 -331 -90 O ATOM 272 CB LYS A 31 22.041 -8.408 12.852 1.00 16.05 C ANISOU 272 CB LYS A 31 1971 1927 2199 414 -303 -301 C ATOM 273 CG LYS A 31 23.440 -8.530 13.446 1.00 20.58 C ATOM 274 CD LYS A 31 24.030 -9.866 13.046 1.00 31.82 C ATOM 275 CE LYS A 31 24.890 -10.293 14.265 1.00 72.76 C ATOM 276 NZ LYS A 31 24.075 -11.010 15.296 1.00 99.05 N ATOM 277 N SER A 32 21.890 -5.353 12.404 1.00 12.51 N ANISOU 277 N SER A 32 1534 1628 1591 -14 6 -68 N ATOM 278 CA SER A 32 22.628 -4.117 12.202 1.00 14.11 C ANISOU 278 CA SER A 32 1542 1887 1931 -336 224 -219 C ATOM 279 C SER A 32 22.086 -2.967 13.043 1.00 13.04 C ANISOU 279 C SER A 32 1620 1658 1676 -232 -69 -111 C ATOM 280 O SER A 32 22.846 -2.093 13.421 1.00 16.75 O ANISOU 280 O SER A 32 1948 1948 2468 -539 128 -412 O ATOM 281 CB ASER A 32 22.521 -3.695 10.725 0.36 20.74 C ANISOU 281 CB ASER A 32 4142 1859 1879 -710 752 -151 C ATOM 282 CB BSER A 32 22.826 -3.719 10.757 0.47 15.37 C ANISOU 282 CB BSER A 32 1801 2002 2037 -480 498 -167 C ATOM 283 CB CSER A 32 22.486 -3.663 10.735 0.17 17.85 C ANISOU 283 CB CSER A 32 2023 2808 1953 454 1733 307 C ATOM 284 OG ASER A 32 23.386 -4.477 9.910 0.36 23.75 O ANISOU 284 OG ASER A 32 4210 2571 2245 -944 1227 -451 O ATOM 285 OG BSER A 32 21.580 -3.305 10.242 0.47 17.61 O ANISOU 285 OG BSER A 32 2101 2543 2046 -470 105 118 O ATOM 286 OG CSER A 32 23.563 -2.790 10.420 0.17 31.24 O ANISOU 286 OG CSER A 32 6991 1876 3004 -2727 1164 -408 O ATOM 287 N ARG A 33 20.788 -2.965 13.334 1.00 11.55 N ANISOU 287 N ARG A 33 1595 1391 1403 -112 -114 -3 N ATOM 288 CA ARG A 33 20.142 -1.952 14.144 1.00 11.76 C ANISOU 288 CA ARG A 33 1850 1295 1322 -77 -179 -30 C ATOM 289 C ARG A 33 20.204 -2.313 15.639 1.00 12.52 C ANISOU 289 C ARG A 33 2160 1267 1332 -37 -222 -28 C ATOM 290 O ARG A 33 19.612 -1.590 16.466 1.00 14.78 O ANISOU 290 O ARG A 33 2767 1383 1466 178 -246 -179 O ATOM 291 CB ARG A 33 18.728 -1.699 13.686 1.00 11.50 C ANISOU 291 CB ARG A 33 1739 1275 1356 -68 -28 93 C ATOM 292 CG ARG A 33 18.616 -1.109 12.265 1.00 11.80 C ANISOU 292 CG ARG A 33 1755 1409 1321 89 -33 -12 C ATOM 293 CD ARG A 33 19.244 0.248 12.170 1.00 11.82 C ANISOU 293 CD ARG A 33 1447 1558 1488 71 24 354 C ATOM 294 NE ARG A 33 19.096 0.807 10.823 1.00 13.03 N ANISOU 294 NE ARG A 33 1555 1887 1510 341 297 389 N ATOM 295 CZ ARG A 33 18.043 1.463 10.397 1.00 11.39 C ANISOU 295 CZ ARG A 33 1483 1583 1260 104 144 169 C ATOM 296 NH1 ARG A 33 17.000 1.672 11.168 1.00 11.90 N ANISOU 296 NH1 ARG A 33 1504 1775 1243 255 136 149 N ATOM 297 NH2 ARG A 33 18.022 1.938 9.164 1.00 14.33 N ANISOU 297 NH2 ARG A 33 1968 2090 1385 461 361 492 N ATOM 298 N ASN A 34 20.884 -3.369 16.023 1.00 12.13 N ANISOU 298 N ASN A 34 2005 1246 1358 -87 -295 62 N ATOM 299 CA ASN A 34 21.111 -3.736 17.414 1.00 13.21 C ANISOU 299 CA ASN A 34 2049 1583 1386 -284 -409 105 C ATOM 300 C ASN A 34 19.825 -4.172 18.086 1.00 13.29 C ANISOU 300 C ASN A 34 2109 1722 1218 -148 -283 -49 C ATOM 301 O ASN A 34 19.742 -4.074 19.295 1.00 19.31 O ANISOU 301 O ASN A 34 2623 3431 1284 -568 -207 -316 O ATOM 302 CB AASN A 34 21.952 -2.731 18.215 0.56 18.13 C ANISOU 302 CB AASN A 34 2184 2629 2075 -455 -734 -472 C ATOM 303 CB BASN A 34 21.739 -2.556 18.182 0.44 16.03 C ANISOU 303 CB BASN A 34 3100 1509 1481 -651 -776 418 C ATOM 304 CG AASN A 34 23.320 -2.418 17.634 0.56 17.77 C ANISOU 304 CG AASN A 34 1948 2126 2678 -333 -935 -84 C ATOM 305 CG BASN A 34 22.729 -2.987 19.232 0.44 14.74 C ANISOU 305 CG BASN A 34 2064 1844 1690 -651 -485 254 C ATOM 306 OD1AASN A 34 23.730 -1.229 17.558 0.56 23.82 O ANISOU 306 OD1AASN A 34 3523 2533 2995 -1024 -580 183 O ATOM 307 OD1BASN A 34 23.204 -4.108 19.126 0.44 18.53 O ANISOU 307 OD1BASN A 34 2841 2041 2157 -213 -675 319 O ATOM 308 ND2AASN A 34 24.026 -3.444 17.208 0.56 22.51 N ANISOU 308 ND2AASN A 34 1740 2975 3837 161 -1162 -403 N ATOM 309 ND2BASN A 34 22.965 -2.100 20.201 0.44 17.73 N ANISOU 309 ND2BASN A 34 2444 2450 1842 -699 -698 -39 N ATOM 310 N LEU A 35 18.911 -4.734 17.338 1.00 11.81 N ANISOU 310 N LEU A 35 1738 1577 1171 -33 -160 42 N ATOM 311 CA LEU A 35 17.635 -5.187 17.879 1.00 13.66 C ANISOU 311 CA LEU A 35 1735 2080 1372 91 -104 125 C ATOM 312 C LEU A 35 17.709 -6.589 18.428 1.00 15.53 C ANISOU 312 C LEU A 35 1736 2441 1722 -159 -149 715 C ATOM 313 O LEU A 35 16.759 -7.068 19.018 1.00 24.74 O ANISOU 313 O LEU A 35 1956 4042 3401 7 284 2068 O ATOM 314 CB LEU A 35 16.503 -5.054 16.866 1.00 13.63 C ANISOU 314 CB LEU A 35 1734 1885 1561 171 -173 18 C ATOM 315 CG LEU A 35 16.374 -3.618 16.338 1.00 16.15 C ANISOU 315 CG LEU A 35 2422 1738 1976 425 -601 -136 C ATOM 316 CD1 LEU A 35 15.328 -3.537 15.246 1.00 20.07 C ANISOU 316 CD1 LEU A 35 3231 1999 2394 802 -1104 -318 C ATOM 317 CD2 LEU A 35 16.124 -2.606 17.391 1.00 23.40 C ANISOU 317 CD2 LEU A 35 3929 2328 2635 744 -1022 -794 C ATOM 318 N THR A 36 18.805 -7.288 18.205 1.00 13.68 N ANISOU 318 N THR A 36 1882 1751 1566 -262 -206 534 N ATOM 319 CA THR A 36 19.004 -8.661 18.654 1.00 16.55 C ANISOU 319 CA THR A 36 2374 1719 2196 -666 -707 917 C ATOM 320 C THR A 36 20.116 -8.799 19.667 1.00 16.98 C ANISOU 320 C THR A 36 2163 2113 2177 -641 -608 1037 C ATOM 321 O THR A 36 20.571 -9.874 19.982 1.00 19.08 O ANISOU 321 O THR A 36 2758 2294 2198 -103 -682 927 O ATOM 322 CB THR A 36 19.226 -9.609 17.473 1.00 18.68 C ANISOU 322 CB THR A 36 3025 1350 2723 -533 -1053 647 C ATOM 323 OG1 THR A 36 20.437 -9.246 16.815 1.00 20.89 O ANISOU 323 OG1 THR A 36 3568 1922 2447 -414 -489 320 O ATOM 324 CG2 THR A 36 18.099 -9.606 16.467 1.00 22.78 C ANISOU 324 CG2 THR A 36 4016 1741 2896 -455 -1691 668 C ATOM 325 N LYS A 37 20.582 -7.678 20.240 1.00 18.05 N ANISOU 325 N LYS A 37 2169 2336 2352 -635 -789 939 N ATOM 326 CA LYS A 37 21.770 -7.728 21.104 1.00 22.16 C ANISOU 326 CA LYS A 37 2665 3140 2616 -1301 -1197 1463 C ATOM 327 C LYS A 37 21.516 -8.490 22.388 1.00 17.59 C ANISOU 327 C LYS A 37 2293 1989 2400 -622 -826 929 C ATOM 328 O LYS A 37 22.384 -9.285 22.793 1.00 19.48 O ANISOU 328 O LYS A 37 2592 2266 2545 -244 -814 729 O ATOM 329 CB LYS A 37 22.163 -6.267 21.439 0.84 31.51 C ANISOU 329 CB LYS A 37 4619 3372 3980 -2593 -2608 2341 C ATOM 330 CG LYS A 37 23.270 -6.085 22.433 0.84 39.41 C ANISOU 330 CG LYS A 37 5478 4365 5130 -3302 -3485 2733 C ATOM 331 CD LYS A 37 23.472 -4.614 22.857 0.84 51.90 C ANISOU 331 CD LYS A 37 8641 4784 6295 -4887 -4469 2652 C ATOM 332 CE LYS A 37 24.469 -4.474 24.002 0.84 75.69 C ANISOU 332 CE LYS A 37 12919 7733 8106 -5625 -7330 2088 C ATOM 333 NZ LYS A 37 24.381 -5.443 25.136 0.84 88.94 N ANISOU 333 NZ LYS A 37 12226 11596 9970 -5903 -9040 4916 N ATOM 334 N ASP A 38 20.394 -8.273 23.043 1.00 16.49 N ANISOU 334 N ASP A 38 2353 1701 2212 -557 -988 470 N ATOM 335 CA ASP A 38 20.119 -8.914 24.347 1.00 15.24 C ANISOU 335 CA ASP A 38 2294 1687 1810 -135 -726 55 C ATOM 336 C ASP A 38 19.204 -10.116 24.217 1.00 12.67 C ANISOU 336 C ASP A 38 2116 1533 1164 27 -338 117 C ATOM 337 O ASP A 38 19.248 -10.991 25.068 1.00 14.19 O ANISOU 337 O ASP A 38 2207 1797 1390 44 -444 303 O ATOM 338 CB ASP A 38 19.483 -7.923 25.329 1.00 20.53 C ANISOU 338 CB ASP A 38 3234 1993 2575 186 -890 -525 C ATOM 339 CG ASP A 38 20.405 -6.818 25.749 1.00 29.17 C ANISOU 339 CG ASP A 38 3921 1974 5189 280 -1482 -1301 C ATOM 340 OD1 ASP A 38 21.573 -7.120 26.069 1.00 43.91 O ANISOU 340 OD1 ASP A 38 4470 3105 9108 -8 -3492 -1367 O ATOM 341 OD2 ASP A 38 19.976 -5.655 25.615 1.00 37.72 O ANISOU 341 OD2 ASP A 38 5769 1981 6582 541 -1854 -1111 O ATOM 342 N ARG A 39 18.345 -10.150 23.249 1.00 12.52 N ANISOU 342 N ARG A 39 2086 1347 1325 -83 -392 260 N ATOM 343 CA ARG A 39 17.375 -11.189 22.965 1.00 12.23 C ANISOU 343 CA ARG A 39 2128 1331 1187 -163 -205 137 C ATOM 344 C ARG A 39 16.905 -11.025 21.522 1.00 11.57 C ANISOU 344 C ARG A 39 1908 1217 1270 -63 -173 88 C ATOM 345 O ARG A 39 17.059 -9.964 20.951 1.00 14.02 O ANISOU 345 O ARG A 39 2522 1424 1381 -345 -364 309 O ATOM 346 CB ARG A 39 16.209 -11.133 23.956 1.00 14.36 C ANISOU 346 CB ARG A 39 2229 1925 1300 -161 -143 103 C ATOM 347 CG ARG A 39 15.403 -9.838 23.916 1.00 18.61 C ANISOU 347 CG ARG A 39 2706 2335 2031 324 137 138 C ATOM 348 CD ARG A 39 14.246 -9.795 24.868 1.00 28.66 C ANISOU 348 CD ARG A 39 4000 4403 2487 1465 1047 620 C ATOM 349 NE ARG A 39 13.504 -8.554 24.790 1.00 36.63 N ANISOU 349 NE ARG A 39 5051 5345 3521 2590 1165 505 N ATOM 350 CZ ARG A 39 12.339 -8.361 24.192 1.00 52.35 C ANISOU 350 CZ ARG A 39 8110 5559 6220 3517 -2231 238 C ATOM 351 NH1 ARG A 39 11.717 -9.298 23.471 1.00 48.88 N ANISOU 351 NH1 ARG A 39 7015 8729 2829 2620 429 -1203 N ATOM 352 NH2 ARG A 39 11.770 -7.149 24.268 1.00 56.81 N ANISOU 352 NH2 ARG A 39 7615 5467 8501 3440 -187 2222 N ATOM 353 N CYS A 40 16.258 -12.052 20.994 1.00 11.62 N ANISOU 353 N CYS A 40 1992 1220 1203 -71 -208 149 N ATOM 354 CA CYS A 40 15.643 -11.914 19.671 1.00 12.30 C ANISOU 354 CA CYS A 40 1760 1608 1305 -16 -246 -22 C ATOM 355 C CYS A 40 14.313 -11.187 19.813 1.00 13.42 C ANISOU 355 C CYS A 40 1881 1849 1370 177 -288 44 C ATOM 356 O CYS A 40 13.349 -11.715 20.340 1.00 18.97 O ANISOU 356 O CYS A 40 1995 2367 2846 180 138 510 O ATOM 357 CB CYS A 40 15.380 -13.246 19.005 1.00 13.44 C ANISOU 357 CB CYS A 40 1988 1594 1526 -94 -181 -30 C ATOM 358 SG CYS A 40 16.823 -14.329 18.851 1.00 13.25 S ANISOU 358 SG CYS A 40 2177 1396 1463 -29 -180 -12 S ATOM 359 N LYS A 41 14.229 -9.959 19.296 1.00 14.92 N ANISOU 359 N LYS A 41 2296 2060 1313 489 110 145 N ATOM 360 CA LYS A 41 12.941 -9.256 19.315 1.00 15.41 C ANISOU 360 CA LYS A 41 2383 2306 1164 723 67 45 C ATOM 361 C LYS A 41 11.997 -10.016 18.405 1.00 14.98 C ANISOU 361 C LYS A 41 2301 2296 1096 819 91 110 C ATOM 362 O LYS A 41 12.381 -10.347 17.261 1.00 17.36 O ANISOU 362 O LYS A 41 2441 3036 1118 811 187 -111 O ATOM 363 CB ALYS A 41 13.191 -7.794 18.886 0.54 20.42 C ANISOU 363 CB ALYS A 41 3129 2117 2514 716 433 -68 C ATOM 364 CB BLYS A 41 13.176 -7.827 18.783 0.46 15.68 C ANISOU 364 CB BLYS A 41 2240 2436 1283 698 -57 283 C ATOM 365 CG ALYS A 41 12.020 -6.891 18.809 0.54 16.15 C ANISOU 365 CG ALYS A 41 2606 1879 1653 213 161 -34 C ATOM 366 CG BLYS A 41 12.047 -6.847 18.880 0.46 24.22 C ANISOU 366 CG BLYS A 41 2609 2107 4487 681 230 -182 C ATOM 367 CD ALYS A 41 12.121 -5.463 18.327 0.54 20.09 C ANISOU 367 CD ALYS A 41 2178 2244 3213 209 934 701 C ATOM 368 CD BLYS A 41 12.421 -5.433 18.480 0.46 23.27 C ANISOU 368 CD BLYS A 41 4018 2017 2805 561 -399 -368 C ATOM 369 CE ALYS A 41 10.865 -4.692 18.740 0.54 27.38 C ANISOU 369 CE ALYS A 41 4015 2630 3757 1315 789 -1250 C ATOM 370 CE BLYS A 41 11.302 -4.407 18.508 0.46 22.69 C ANISOU 370 CE BLYS A 41 2729 2268 3625 51 -669 1119 C ATOM 371 NZ ALYS A 41 10.678 -3.467 17.925 0.54 41.30 N ANISOU 371 NZ ALYS A 41 6142 7245 2306 4818 554 641 N ATOM 372 NZ BLYS A 41 10.149 -4.811 17.656 0.46 27.19 N ANISOU 372 NZ BLYS A 41 3407 4200 2724 -552 -443 299 N ATOM 373 N PRO A 42 10.775 -10.358 18.792 1.00 14.97 N ANISOU 373 N PRO A 42 2527 2067 1093 561 223 156 N ATOM 374 CA PRO A 42 9.965 -11.295 18.011 1.00 15.34 C ANISOU 374 CA PRO A 42 2745 1721 1363 528 137 226 C ATOM 375 C PRO A 42 9.371 -10.781 16.719 1.00 13.14 C ANISOU 375 C PRO A 42 2279 1463 1251 217 352 191 C ATOM 376 O PRO A 42 9.195 -11.536 15.773 1.00 15.71 O ANISOU 376 O PRO A 42 2815 1690 1462 137 90 -35 O ATOM 377 CB PRO A 42 8.821 -11.731 18.946 1.00 20.04 C ANISOU 377 CB PRO A 42 3648 2377 1587 -280 205 829 C ATOM 378 CG PRO A 42 8.815 -10.698 20.007 1.00 27.30 C ANISOU 378 CG PRO A 42 3591 4696 2087 -853 1139 -568 C ATOM 379 CD PRO A 42 10.224 -10.189 20.154 1.00 18.22 C ANISOU 379 CD PRO A 42 3155 2608 1161 252 522 164 C ATOM 380 N VAL A 43 9.048 -9.512 16.671 1.00 11.79 N ANISOU 380 N VAL A 43 1927 1401 1152 61 196 184 N ATOM 381 CA VAL A 43 8.424 -8.860 15.541 1.00 11.90 C ANISOU 381 CA VAL A 43 1667 1517 1336 -165 129 305 C ATOM 382 C VAL A 43 8.987 -7.461 15.437 1.00 11.59 C ANISOU 382 C VAL A 43 1797 1465 1140 -83 16 216 C ATOM 383 O VAL A 43 9.275 -6.824 16.434 1.00 14.51 O ANISOU 383 O VAL A 43 2640 1640 1233 -360 -119 140 O ATOM 384 CB AVAL A 43 6.887 -8.795 15.634 0.53 14.47 C ANISOU 384 CB AVAL A 43 1734 1685 2080 -137 132 496 C ATOM 385 CB BVAL A 43 6.879 -8.834 15.677 0.47 19.43 C ANISOU 385 CB BVAL A 43 1638 2402 3342 -225 -65 828 C ATOM 386 CG1AVAL A 43 6.219 -10.139 15.840 0.53 20.49 C ANISOU 386 CG1AVAL A 43 1950 2313 3522 -788 -80 1052 C ATOM 387 CG1BVAL A 43 6.420 -7.919 16.792 0.47 31.44 C ANISOU 387 CG1BVAL A 43 1278 7088 3581 78 909 -570 C ATOM 388 CG2AVAL A 43 6.512 -7.893 16.787 0.53 25.86 C ANISOU 388 CG2AVAL A 43 3442 2800 3585 1104 1200 -249 C ATOM 389 CG2BVAL A 43 6.193 -8.400 14.389 0.47 22.75 C ANISOU 389 CG2BVAL A 43 1325 3908 3409 -394 -275 793 C ATOM 390 N ASN A 44 9.055 -6.943 14.212 1.00 10.79 N ANISOU 390 N ASN A 44 1617 1303 1180 -91 113 115 N ATOM 391 CA ASN A 44 9.407 -5.562 13.998 1.00 10.08 C ANISOU 391 CA ASN A 44 1490 1259 1082 4 160 34 C ATOM 392 C ASN A 44 8.943 -5.134 12.637 1.00 11.07 C ANISOU 392 C ASN A 44 1842 1280 1083 27 183 48 C ATOM 393 O ASN A 44 8.818 -5.961 11.753 1.00 17.01 O ANISOU 393 O ASN A 44 4036 1358 1068 444 -52 -95 O ATOM 394 CB ASN A 44 10.907 -5.349 14.135 1.00 11.47 C ANISOU 394 CB ASN A 44 1546 1252 1559 -55 105 92 C ATOM 395 CG ASN A 44 11.299 -3.934 14.274 1.00 11.59 C ANISOU 395 CG ASN A 44 1752 1246 1404 -47 20 -92 C ATOM 396 OD1 ASN A 44 10.760 -3.216 15.096 1.00 19.75 O ANISOU 396 OD1 ASN A 44 3184 1696 2626 -382 1259 -558 O ATOM 397 ND2 ASN A 44 12.199 -3.432 13.443 1.00 12.48 N ANISOU 397 ND2 ASN A 44 1822 1277 1643 -216 154 -81 N ATOM 398 N THR A 45 8.727 -3.855 12.441 1.00 9.94 N ANISOU 398 N THR A 45 1657 1198 923 34 86 -5 N ATOM 399 CA THR A 45 8.381 -3.274 11.160 1.00 9.81 C ANISOU 399 CA THR A 45 1478 1250 999 -56 71 3 C ATOM 400 C THR A 45 9.348 -2.160 10.807 1.00 9.44 C ANISOU 400 C THR A 45 1526 1154 906 -29 -44 25 C ATOM 401 O THR A 45 9.651 -1.304 11.642 1.00 11.44 O ANISOU 401 O THR A 45 1925 1371 1050 -231 108 -87 O ATOM 402 CB THR A 45 6.951 -2.696 11.197 1.00 11.90 C ANISOU 402 CB THR A 45 1448 1725 1349 62 8 85 C ATOM 403 OG1 THR A 45 6.062 -3.739 11.612 1.00 15.76 O ANISOU 403 OG1 THR A 45 1483 2326 2179 -237 120 403 O ATOM 404 CG2 THR A 45 6.513 -2.128 9.858 1.00 14.32 C ANISOU 404 CG2 THR A 45 1660 2280 1502 291 -108 212 C ATOM 405 N PHE A 46 9.806 -2.159 9.557 1.00 9.42 N ANISOU 405 N PHE A 46 1631 1005 942 -112 0 15 N ATOM 406 CA PHE A 46 10.608 -1.080 8.986 1.00 9.72 C ANISOU 406 CA PHE A 46 1460 1251 982 -39 -42 97 C ATOM 407 C PHE A 46 9.780 -0.329 7.970 1.00 9.68 C ANISOU 407 C PHE A 46 1619 1188 872 -3 -89 87 C ATOM 408 O PHE A 46 8.973 -0.913 7.223 1.00 12.29 O ANISOU 408 O PHE A 46 2112 1240 1319 -27 -515 -28 O ATOM 409 CB PHE A 46 11.873 -1.618 8.307 1.00 10.94 C ANISOU 409 CB PHE A 46 1542 1441 1176 42 120 115 C ATOM 410 CG PHE A 46 12.863 -2.197 9.296 1.00 10.08 C ANISOU 410 CG PHE A 46 1290 1446 1095 -44 138 33 C ATOM 411 CD1 PHE A 46 13.724 -1.384 9.989 1.00 12.40 C ANISOU 411 CD1 PHE A 46 1477 1539 1696 -42 -55 45 C ATOM 412 CD2 PHE A 46 12.932 -3.555 9.536 1.00 11.53 C ANISOU 412 CD2 PHE A 46 1744 1453 1182 -3 84 94 C ATOM 413 CE1 PHE A 46 14.616 -1.882 10.919 1.00 14.07 C ANISOU 413 CE1 PHE A 46 1465 2165 1717 118 -262 -141 C ATOM 414 CE2 PHE A 46 13.832 -4.075 10.447 1.00 14.10 C ANISOU 414 CE2 PHE A 46 1947 1835 1577 512 14 23 C ATOM 415 CZ PHE A 46 14.678 -3.257 11.147 1.00 13.76 C ANISOU 415 CZ PHE A 46 1609 2303 1315 396 9 208 C ATOM 416 N VAL A 47 9.953 0.983 7.925 1.00 9.99 N ANISOU 416 N VAL A 47 1600 1179 1017 -80 -124 130 N ATOM 417 CA VAL A 47 9.196 1.895 7.060 1.00 9.68 C ANISOU 417 CA VAL A 47 1586 1142 951 17 -46 76 C ATOM 418 C VAL A 47 10.158 2.496 6.043 1.00 9.71 C ANISOU 418 C VAL A 47 1579 1136 973 75 -6 67 C ATOM 419 O VAL A 47 11.178 3.108 6.403 1.00 11.16 O ANISOU 419 O VAL A 47 1560 1576 1104 -198 -79 73 O ATOM 420 CB VAL A 47 8.477 2.974 7.874 1.00 10.71 C ANISOU 420 CB VAL A 47 1600 1373 1096 96 80 -38 C ATOM 421 CG1 VAL A 47 7.668 3.856 6.958 1.00 14.08 C ANISOU 421 CG1 VAL A 47 2197 1509 1646 444 -11 65 C ATOM 422 CG2 VAL A 47 7.659 2.369 8.994 1.00 13.70 C ANISOU 422 CG2 VAL A 47 1772 1994 1438 -125 262 0 C ATOM 423 N HIS A 48 9.831 2.350 4.756 1.00 9.97 N ANISOU 423 N HIS A 48 1413 1440 935 -26 -10 93 N ATOM 424 CA HIS A 48 10.671 2.781 3.660 1.00 10.75 C ANISOU 424 CA HIS A 48 1612 1452 1019 -18 127 149 C ATOM 425 C HIS A 48 10.179 4.077 3.071 1.00 11.36 C ANISOU 425 C HIS A 48 1977 1367 971 -17 158 79 C ATOM 426 O HIS A 48 9.679 4.158 1.957 1.00 14.69 O ANISOU 426 O HIS A 48 2888 1624 1071 174 -172 89 O ATOM 427 CB HIS A 48 10.672 1.686 2.566 1.00 11.30 C ANISOU 427 CB HIS A 48 1810 1467 1018 84 129 79 C ATOM 428 CG HIS A 48 11.121 0.391 3.033 1.00 11.51 C ANISOU 428 CG HIS A 48 1810 1499 1063 44 -10 119 C ATOM 429 ND1 HIS A 48 12.447 0.061 3.194 1.00 18.72 N ANISOU 429 ND1 HIS A 48 1899 1807 3409 -97 -448 910 N ATOM 430 CD2 HIS A 48 10.485 -0.744 3.355 1.00 12.40 C ANISOU 430 CD2 HIS A 48 1791 1447 1474 99 303 30 C ATOM 431 CE1 HIS A 48 12.509 -1.189 3.603 1.00 21.11 C ANISOU 431 CE1 HIS A 48 1943 1871 4209 33 -510 1105 C ATOM 432 NE2 HIS A 48 11.328 -1.713 3.751 1.00 13.43 N ANISOU 432 NE2 HIS A 48 1955 1546 1601 142 79 177 N ATOM 433 N GLU A 49 10.218 5.119 3.871 1.00 12.09 N ANISOU 433 N GLU A 49 2261 1289 1042 -101 21 184 N ATOM 434 CA GLU A 49 9.756 6.445 3.545 1.00 11.94 C ANISOU 434 CA GLU A 49 2091 1271 1175 61 151 115 C ATOM 435 C GLU A 49 10.734 7.451 4.135 1.00 11.89 C ANISOU 435 C GLU A 49 2063 1300 1154 33 226 115 C ATOM 436 O GLU A 49 11.543 7.126 5.009 1.00 13.54 O ANISOU 436 O GLU A 49 2242 1483 1421 -72 -8 62 O ATOM 437 CB GLU A 49 8.346 6.681 4.087 1.00 13.55 C ANISOU 437 CB GLU A 49 2118 1583 1447 -100 257 1 C ATOM 438 CG GLU A 49 7.313 5.684 3.597 1.00 14.09 C ANISOU 438 CG GLU A 49 2176 1492 1686 -2 79 92 C ATOM 439 CD GLU A 49 6.884 5.796 2.145 1.00 15.52 C ANISOU 439 CD GLU A 49 2264 1765 1868 -273 -219 348 C ATOM 440 OE1 GLU A 49 7.191 6.843 1.541 1.00 20.29 O ANISOU 440 OE1 GLU A 49 3507 1915 2289 -523 -984 732 O ATOM 441 OE2 GLU A 49 6.228 4.857 1.688 1.00 17.16 O ANISOU 441 OE2 GLU A 49 2500 1984 2036 -323 -435 274 O ATOM 442 N SER A 50 10.627 8.699 3.696 1.00 12.46 N ANISOU 442 N SER A 50 2022 1365 1347 -30 134 98 N ATOM 443 CA SER A 50 11.401 9.747 4.305 1.00 12.85 C ANISOU 443 CA SER A 50 1859 1484 1540 -250 339 -17 C ATOM 444 C SER A 50 11.006 9.920 5.793 1.00 12.03 C ANISOU 444 C SER A 50 1729 1283 1559 -174 307 1 C ATOM 445 O SER A 50 9.838 9.758 6.183 1.00 12.83 O ANISOU 445 O SER A 50 1751 1592 1530 -188 265 -35 O ATOM 446 CB SER A 50 11.223 11.070 3.611 1.00 15.28 C ANISOU 446 CB SER A 50 2443 1609 1753 -216 752 217 C ATOM 447 OG SER A 50 10.007 11.611 3.842 1.00 18.61 O ANISOU 447 OG SER A 50 2674 2098 2300 266 550 563 O ATOM 448 N LEU A 51 11.949 10.363 6.592 1.00 12.80 N ANISOU 448 N LEU A 51 1676 1744 1445 -66 320 28 N ATOM 449 CA LEU A 51 11.666 10.638 8.005 1.00 13.32 C ANISOU 449 CA LEU A 51 1881 1736 1445 -8 289 -11 C ATOM 450 C LEU A 51 10.611 11.725 8.082 1.00 12.74 C ANISOU 450 C LEU A 51 1908 1460 1473 -194 280 -113 C ATOM 451 O LEU A 51 9.711 11.620 8.931 1.00 14.02 O ANISOU 451 O LEU A 51 1942 1913 1472 0 325 -42 O ATOM 452 CB LEU A 51 12.957 11.020 8.724 1.00 16.09 C ANISOU 452 CB LEU A 51 2112 2207 1794 -90 52 -166 C ATOM 453 CG LEU A 51 12.789 11.284 10.187 1.00 16.56 C ANISOU 453 CG LEU A 51 2665 1812 1815 5 -89 -323 C ATOM 454 CD1 LEU A 51 12.270 10.068 10.926 1.00 21.21 C ANISOU 454 CD1 LEU A 51 4085 2051 1922 267 74 251 C ATOM 455 CD2 LEU A 51 14.120 11.670 10.846 1.00 23.86 C ANISOU 455 CD2 LEU A 51 3139 3002 2926 249 -1096 -672 C ATOM 456 N ALA A 52 10.682 12.756 7.266 1.00 13.38 N ANISOU 456 N ALA A 52 2012 1487 1584 -173 258 -15 N ATOM 457 CA ALA A 52 9.711 13.850 7.356 1.00 15.04 C ANISOU 457 CA ALA A 52 2351 1342 2024 -163 532 -109 C ATOM 458 C ALA A 52 8.299 13.336 7.116 1.00 13.74 C ANISOU 458 C ALA A 52 2157 1364 1702 82 427 139 C ATOM 459 O ALA A 52 7.344 13.792 7.741 1.00 15.28 O ANISOU 459 O ALA A 52 2254 1566 1986 141 486 -80 O ATOM 460 CB ALA A 52 10.040 14.939 6.365 1.00 18.58 C ANISOU 460 CB ALA A 52 2464 1504 3091 -68 763 427 C ATOM 461 N ASP A 53 8.101 12.413 6.160 1.00 13.45 N ANISOU 461 N ASP A 53 2046 1487 1578 57 352 145 N ATOM 462 CA ASP A 53 6.781 11.889 5.889 1.00 13.33 C ANISOU 462 CA ASP A 53 2131 1415 1517 77 260 190 C ATOM 463 C ASP A 53 6.213 11.079 7.049 1.00 12.51 C ANISOU 463 C ASP A 53 1852 1478 1422 156 190 166 C ATOM 464 O ASP A 53 5.007 11.074 7.270 1.00 14.38 O ANISOU 464 O ASP A 53 1796 1903 1765 258 63 509 O ATOM 465 CB ASP A 53 6.691 11.092 4.589 1.00 14.78 C ANISOU 465 CB ASP A 53 2416 1820 1379 93 27 177 C ATOM 466 CG ASP A 53 6.778 11.888 3.318 1.00 18.03 C ANISOU 466 CG ASP A 53 3097 2248 1503 570 258 396 C ATOM 467 OD1 ASP A 53 6.606 13.084 3.353 1.00 25.04 O ANISOU 467 OD1 ASP A 53 5326 2290 1898 953 565 684 O ATOM 468 OD2 ASP A 53 7.030 11.304 2.286 1.00 24.49 O ANISOU 468 OD2 ASP A 53 4921 2882 1504 1200 510 317 O ATOM 469 N VAL A 54 7.084 10.371 7.768 1.00 11.59 N ANISOU 469 N VAL A 54 1738 1364 1301 72 212 121 N ATOM 470 CA VAL A 54 6.640 9.635 8.930 1.00 11.12 C ANISOU 470 CA VAL A 54 1649 1271 1304 -76 169 45 C ATOM 471 C VAL A 54 6.376 10.555 10.101 1.00 11.24 C ANISOU 471 C VAL A 54 1757 1277 1236 -47 141 97 C ATOM 472 O VAL A 54 5.381 10.399 10.786 1.00 12.26 O ANISOU 472 O VAL A 54 1824 1446 1387 -130 277 34 O ATOM 473 CB VAL A 54 7.626 8.482 9.254 1.00 11.39 C ANISOU 473 CB VAL A 54 1650 1371 1307 22 -16 37 C ATOM 474 CG1 VAL A 54 7.250 7.759 10.523 1.00 13.89 C ANISOU 474 CG1 VAL A 54 2134 1683 1462 127 65 211 C ATOM 475 CG2 VAL A 54 7.683 7.496 8.094 1.00 13.90 C ANISOU 475 CG2 VAL A 54 2094 1505 1683 144 -52 -228 C ATOM 476 N GLN A 55 7.243 11.528 10.314 1.00 11.92 N ANISOU 476 N GLN A 55 1777 1400 1353 -118 237 -36 N ATOM 477 CA GLN A 55 6.985 12.492 11.371 1.00 13.09 C ANISOU 477 CA GLN A 55 2014 1475 1484 -76 162 -241 C ATOM 478 C GLN A 55 5.688 13.236 11.151 1.00 12.93 C ANISOU 478 C GLN A 55 1947 1438 1527 -90 281 -151 C ATOM 479 O GLN A 55 4.987 13.575 12.128 1.00 14.51 O ANISOU 479 O GLN A 55 1983 1763 1768 -44 362 -290 O ATOM 480 CB GLN A 55 8.171 13.462 11.387 1.00 15.97 C ANISOU 480 CB GLN A 55 1959 1864 2245 -186 204 -549 C ATOM 481 CG GLN A 55 9.406 13.034 12.131 1.00 16.81 C ANISOU 481 CG GLN A 55 2110 2336 1943 -189 150 -235 C ATOM 482 CD GLN A 55 10.644 13.914 11.880 1.00 17.28 C ANISOU 482 CD GLN A 55 1941 1703 2922 52 309 -647 C ATOM 483 OE1 GLN A 55 10.577 14.869 11.084 1.00 23.66 O ANISOU 483 OE1 GLN A 55 2711 2655 3622 -510 -100 270 O ATOM 484 NE2 GLN A 55 11.749 13.645 12.434 1.00 19.19 N ANISOU 484 NE2 GLN A 55 2068 2182 3042 -404 229 -169 N ATOM 485 N ALA A 56 5.294 13.481 9.907 1.00 13.59 N ANISOU 485 N ALA A 56 1945 1486 1732 12 331 130 N ATOM 486 CA ALA A 56 4.101 14.223 9.607 1.00 14.02 C ANISOU 486 CA ALA A 56 2177 1346 1802 234 474 199 C ATOM 487 C ALA A 56 2.851 13.446 10.043 1.00 12.99 C ANISOU 487 C ALA A 56 1873 1539 1523 235 89 368 C ATOM 488 O ALA A 56 1.766 14.057 10.192 1.00 15.41 O ANISOU 488 O ALA A 56 2030 1700 2126 404 282 240 O ATOM 489 CB ALA A 56 3.973 14.475 8.097 1.00 17.97 C ANISOU 489 CB ALA A 56 2518 2404 1906 275 480 816 C ATOM 490 N VAL A 57 2.949 12.141 10.269 1.00 12.70 N ANISOU 490 N VAL A 57 1913 1414 1498 195 348 180 N ATOM 491 CA VAL A 57 1.762 11.358 10.649 1.00 12.57 C ANISOU 491 CA VAL A 57 1698 1538 1541 91 99 144 C ATOM 492 C VAL A 57 1.229 11.873 11.979 1.00 12.03 C ANISOU 492 C VAL A 57 1594 1389 1586 263 150 128 C ATOM 493 O VAL A 57 0.033 11.742 12.232 1.00 13.17 O ANISOU 493 O VAL A 57 1677 1665 1661 150 138 204 O ATOM 494 CB VAL A 57 2.100 9.855 10.671 1.00 12.53 C ANISOU 494 CB VAL A 57 1685 1494 1582 104 106 41 C ATOM 495 CG1 VAL A 57 0.928 9.035 11.204 1.00 13.99 C ANISOU 495 CG1 VAL A 57 1872 1495 1947 -53 130 139 C ATOM 496 CG2 VAL A 57 2.459 9.403 9.248 1.00 13.71 C ANISOU 496 CG2 VAL A 57 1938 1708 1565 126 64 -17 C ATOM 497 N CYS A 58 2.065 12.463 12.819 1.00 12.48 N ANISOU 497 N CYS A 58 1629 1499 1613 99 308 71 N ATOM 498 CA CYS A 58 1.626 13.032 14.096 1.00 13.30 C ANISOU 498 CA CYS A 58 1926 1575 1552 168 255 86 C ATOM 499 C CYS A 58 0.662 14.195 13.953 1.00 14.39 C ANISOU 499 C CYS A 58 2037 1652 1780 271 331 -77 C ATOM 500 O CYS A 58 0.110 14.559 14.964 1.00 17.63 O ANISOU 500 O CYS A 58 2680 1969 2050 579 562 -5 O ATOM 501 CB CYS A 58 2.829 13.457 14.948 1.00 13.95 C ANISOU 501 CB CYS A 58 2019 1469 1813 12 224 -66 C ATOM 502 SG CYS A 58 3.941 12.121 15.410 1.00 14.24 S ANISOU 502 SG CYS A 58 1783 1989 1638 169 79 -78 S ATOM 503 N SER A 59 0.452 14.692 12.773 1.00 14.41 N ANISOU 503 N SER A 59 1972 1572 1933 321 63 37 N ATOM 504 CA SER A 59 -0.525 15.711 12.440 1.00 17.37 C ANISOU 504 CA SER A 59 2481 1681 2439 544 85 43 C ATOM 505 C SER A 59 -1.680 15.189 11.610 1.00 16.58 C ANISOU 505 C SER A 59 2149 1865 2284 665 56 279 C ATOM 506 O SER A 59 -2.452 16.007 11.097 1.00 21.50 O ANISOU 506 O SER A 59 2942 2025 3202 854 -333 383 O ATOM 507 CB ASER A 59 0.187 16.900 11.810 0.50 22.62 C ANISOU 507 CB ASER A 59 3187 1764 3644 181 -590 622 C ATOM 508 CB BSER A 59 0.130 16.895 11.742 0.50 21.07 C ANISOU 508 CB BSER A 59 3453 1316 3238 259 -227 68 C ATOM 509 OG ASER A 59 0.626 16.645 10.486 0.50 27.86 O ANISOU 509 OG ASER A 59 3946 2064 4574 814 1302 1529 O ATOM 510 OG BSER A 59 1.105 17.481 12.572 0.50 28.05 O ANISOU 510 OG BSER A 59 4483 2004 4169 -522 -866 90 O ATOM 511 N GLN A 60 -1.840 13.876 11.445 1.00 15.01 N ANISOU 511 N GLN A 60 2003 1937 1762 604 -85 236 N ATOM 512 CA GLN A 60 -2.835 13.255 10.606 1.00 15.80 C ANISOU 512 CA GLN A 60 2069 2113 1822 475 -5 323 C ATOM 513 C GLN A 60 -3.993 12.737 11.428 1.00 16.91 C ANISOU 513 C GLN A 60 1956 2158 2311 663 147 444 C ATOM 514 O GLN A 60 -4.479 13.430 12.317 1.00 20.00 O ANISOU 514 O GLN A 60 2323 2548 2727 412 632 121 O ATOM 515 CB GLN A 60 -2.184 12.299 9.624 1.00 15.27 C ANISOU 515 CB GLN A 60 1942 1954 1906 336 7 282 C ATOM 516 CG GLN A 60 -1.250 13.103 8.719 1.00 16.72 C ANISOU 516 CG GLN A 60 2282 2001 2071 342 186 427 C ATOM 517 CD GLN A 60 -0.477 12.268 7.741 1.00 16.11 C ANISOU 517 CD GLN A 60 2133 2142 1846 246 73 313 C ATOM 518 OE1 GLN A 60 -0.742 11.120 7.425 1.00 18.34 O ANISOU 518 OE1 GLN A 60 2608 2151 2209 59 205 240 O ATOM 519 NE2 GLN A 60 0.572 12.891 7.226 1.00 21.09 N ANISOU 519 NE2 GLN A 60 2593 2604 2817 -243 616 -192 N ATOM 520 N LYS A 61 -4.507 11.545 11.225 1.00 16.86 N ANISOU 520 N LYS A 61 1968 2425 2014 405 122 387 N ATOM 521 CA LYS A 61 -5.780 11.112 11.791 1.00 17.25 C ANISOU 521 CA LYS A 61 2020 2385 2148 557 123 607 C ATOM 522 C LYS A 61 -5.569 10.578 13.187 1.00 15.68 C ANISOU 522 C LYS A 61 1681 2252 2026 504 65 420 C ATOM 523 O LYS A 61 -4.963 9.532 13.383 1.00 17.30 O ANISOU 523 O LYS A 61 1957 2560 2056 841 97 400 O ATOM 524 CB ALYS A 61 -6.401 10.049 10.879 0.57 22.24 C ATOM 525 CB BLYS A 61 -6.492 10.096 10.917 0.43 15.52 C ATOM 526 CG ALYS A 61 -7.671 9.360 11.390 0.57 31.48 C ATOM 527 CG BLYS A 61 -7.838 9.617 11.475 0.43 15.98 C ATOM 528 CD ALYS A 61 -8.793 10.371 11.524 0.57 30.62 C ATOM 529 CD BLYS A 61 -8.407 8.520 10.614 0.43 21.86 C ATOM 530 CE ALYS A 61 -10.096 9.733 11.992 0.57 30.35 C ATOM 531 CE BLYS A 61 -9.872 8.272 10.961 0.43 35.61 C ATOM 532 NZ ALYS A 61 -11.180 10.703 12.321 0.57 41.20 N ATOM 533 NZ BLYS A 61 -10.073 8.289 12.440 0.43 55.88 N ATOM 534 N ASN A 62 -6.099 11.245 14.211 1.00 15.80 N ANISOU 534 N ASN A 62 1793 2064 2146 424 209 459 N ATOM 535 CA ASN A 62 -5.943 10.771 15.571 1.00 15.73 C ANISOU 535 CA ASN A 62 1904 1997 2077 461 194 354 C ATOM 536 C ASN A 62 -6.883 9.591 15.773 1.00 16.08 C ANISOU 536 C ASN A 62 1501 2484 2125 280 -5 639 C ATOM 537 O ASN A 62 -8.086 9.630 15.448 1.00 20.18 O ANISOU 537 O ASN A 62 1599 3109 2958 401 -7 993 O ATOM 538 CB ASN A 62 -6.376 11.921 16.513 1.00 19.45 C ANISOU 538 CB ASN A 62 2369 2681 2341 854 165 -53 C ATOM 539 CG ASN A 62 -6.161 11.708 17.985 1.00 23.61 C ANISOU 539 CG ASN A 62 2778 3966 2226 1449 351 64 C ATOM 540 OD1 ASN A 62 -7.005 12.116 18.779 1.00 37.22 O ANISOU 540 OD1 ASN A 62 4267 7327 2550 3678 679 363 O ATOM 541 ND2 ASN A 62 -5.144 11.013 18.472 1.00 18.34 N ANISOU 541 ND2 ASN A 62 2251 2450 2267 545 309 36 N ATOM 542 N VAL A 63 -6.332 8.525 16.350 1.00 14.83 N ANISOU 542 N VAL A 63 1461 2164 2009 100 66 359 N ATOM 543 CA VAL A 63 -7.008 7.289 16.626 1.00 15.33 C ANISOU 543 CA VAL A 63 1369 2278 2178 94 71 350 C ATOM 544 C VAL A 63 -6.551 6.722 17.948 1.00 14.07 C ANISOU 544 C VAL A 63 1323 1963 2060 129 115 186 C ATOM 545 O VAL A 63 -5.456 7.046 18.440 1.00 17.15 O ANISOU 545 O VAL A 63 1383 2660 2473 -147 -49 570 O ATOM 546 CB VAL A 63 -6.771 6.234 15.524 1.00 17.18 C ANISOU 546 CB VAL A 63 1973 2402 2154 -192 -82 136 C ATOM 547 CG1 VAL A 63 -7.327 6.737 14.215 1.00 21.71 C ANISOU 547 CG1 VAL A 63 2840 3151 2258 -489 -349 373 C ATOM 548 CG2 VAL A 63 -5.331 5.799 15.402 1.00 18.61 C ANISOU 548 CG2 VAL A 63 2238 2676 2156 121 474 12 C ATOM 549 N ALA A 64 -7.308 5.819 18.532 1.00 13.63 N ANISOU 549 N ALA A 64 1265 2057 1855 -22 -150 100 N ATOM 550 CA ALA A 64 -6.825 5.101 19.729 1.00 13.19 C ANISOU 550 CA ALA A 64 1428 2004 1580 18 -17 -66 C ATOM 551 C ALA A 64 -5.758 4.103 19.328 1.00 12.08 C ANISOU 551 C ALA A 64 1631 1643 1316 -77 -136 -74 C ATOM 552 O ALA A 64 -5.872 3.385 18.356 1.00 15.43 O ANISOU 552 O ALA A 64 2009 2245 1609 139 -296 -485 O ATOM 553 CB ALA A 64 -8.003 4.463 20.426 1.00 16.90 C ANISOU 553 CB ALA A 64 1687 2827 1908 64 235 386 C ATOM 554 N CYS A 65 -4.733 4.009 20.160 1.00 11.76 N ANISOU 554 N CYS A 65 1452 1650 1365 -32 -50 -118 N ATOM 555 CA CYS A 65 -3.759 2.939 20.060 1.00 11.55 C ANISOU 555 CA CYS A 65 1451 1647 1291 -91 -27 63 C ATOM 556 C CYS A 65 -4.385 1.616 20.455 1.00 11.75 C ANISOU 556 C CYS A 65 1536 1676 1253 -141 -70 -90 C ATOM 557 O CYS A 65 -5.445 1.578 21.080 1.00 13.17 O ANISOU 557 O CYS A 65 1524 1914 1565 -274 160 -100 O ATOM 558 CB ACYS A 65 -2.613 3.232 21.042 0.80 11.78 C ANISOU 558 CB ACYS A 65 1590 1522 1363 -59 -113 30 C ATOM 559 CB BCYS A 65 -2.448 3.091 20.809 0.20 13.30 C ANISOU 559 CB BCYS A 65 1343 1851 1861 -149 -59 261 C ATOM 560 SG ACYS A 65 -1.843 4.863 20.937 0.80 11.76 S ANISOU 560 SG ACYS A 65 1585 1570 1314 -170 -55 48 S ATOM 561 SG BCYS A 65 -1.143 3.937 19.872 0.20 13.16 S ANISOU 561 SG BCYS A 65 1520 1570 1910 -103 173 101 S ATOM 562 N LYS A 66 -3.691 0.509 20.159 1.00 12.92 N ANISOU 562 N LYS A 66 1741 1599 1568 -169 27 -102 N ATOM 563 CA LYS A 66 -4.212 -0.802 20.489 1.00 14.78 C ANISOU 563 CA LYS A 66 2316 1623 1677 -351 -129 -158 C ATOM 564 C LYS A 66 -4.480 -0.956 21.983 1.00 15.16 C ANISOU 564 C LYS A 66 2510 1517 1734 -578 32 -191 C ATOM 565 O LYS A 66 -5.400 -1.656 22.332 1.00 18.81 O ANISOU 565 O LYS A 66 2866 2173 2108 -1131 57 -31 O ATOM 566 CB LYS A 66 -3.222 -1.875 20.056 1.00 19.58 C ANISOU 566 CB LYS A 66 3286 1917 2237 30 284 -308 C ATOM 567 CG LYS A 66 -3.034 -2.128 18.612 1.00 32.31 C ATOM 568 CD LYS A 66 -1.777 -3.027 18.419 1.00 51.97 C ATOM 569 CE LYS A 66 -2.054 -4.182 17.455 1.00 70.50 C ATOM 570 NZ LYS A 66 -1.108 -4.254 16.312 1.00 73.54 N ATOM 571 N ASN A 67 -3.667 -0.333 22.842 1.00 13.69 N ANISOU 571 N ASN A 67 2226 1451 1524 -347 -36 12 N ATOM 572 CA ASN A 67 -3.805 -0.426 24.283 1.00 15.72 C ANISOU 572 CA ASN A 67 2788 1689 1497 -198 -28 40 C ATOM 573 C ASN A 67 -4.743 0.611 24.859 1.00 15.85 C ANISOU 573 C ASN A 67 2528 1871 1624 -343 253 48 C ATOM 574 O ASN A 67 -4.849 0.713 26.095 1.00 19.57 O ANISOU 574 O ASN A 67 3155 2714 1568 -81 361 90 O ATOM 575 CB ASN A 67 -2.412 -0.319 24.977 1.00 17.76 C ANISOU 575 CB ASN A 67 2945 2209 1596 172 -257 116 C ATOM 576 CG ASN A 67 -1.860 1.117 25.013 1.00 18.06 C ANISOU 576 CG ASN A 67 2258 2296 2308 -39 -218 176 C ATOM 577 OD1 ASN A 67 -2.274 2.080 24.332 1.00 18.64 O ANISOU 577 OD1 ASN A 67 2312 2604 2168 -15 -107 562 O ATOM 578 ND2 ASN A 67 -0.862 1.372 25.876 1.00 27.65 N ANISOU 578 ND2 ASN A 67 3995 2813 3699 -184 -1834 329 N ATOM 579 N GLY A 68 -5.402 1.412 24.014 1.00 14.69 N ANISOU 579 N GLY A 68 2132 1873 1575 -318 186 -195 N ATOM 580 CA GLY A 68 -6.361 2.385 24.451 1.00 15.48 C ANISOU 580 CA GLY A 68 1846 2117 1918 -375 331 -237 C ATOM 581 C GLY A 68 -5.889 3.780 24.638 1.00 14.44 C ANISOU 581 C GLY A 68 1712 2129 1647 -212 185 -534 C ATOM 582 O GLY A 68 -6.690 4.706 24.750 1.00 16.10 O ANISOU 582 O GLY A 68 1713 2277 2128 -177 161 -601 O ATOM 583 N GLN A 69 -4.577 4.034 24.604 1.00 13.78 N ANISOU 583 N GLN A 69 1702 1769 1764 -142 19 -405 N ATOM 584 CA GLN A 69 -4.072 5.414 24.650 1.00 13.84 C ANISOU 584 CA GLN A 69 1881 1753 1625 -117 -48 -408 C ATOM 585 C GLN A 69 -4.578 6.205 23.463 1.00 12.31 C ANISOU 585 C GLN A 69 1436 1852 1388 -222 39 -445 C ATOM 586 O GLN A 69 -4.851 5.679 22.413 1.00 15.69 O ANISOU 586 O GLN A 69 2073 2352 1534 50 -180 -673 O ATOM 587 CB GLN A 69 -2.512 5.437 24.603 1.00 15.03 C ANISOU 587 CB GLN A 69 1915 1657 2137 -205 -360 -167 C ATOM 588 CG GLN A 69 -1.806 4.850 25.761 1.00 16.05 C ANISOU 588 CG GLN A 69 2286 1967 1845 -69 -341 -429 C ATOM 589 CD GLN A 69 -0.277 4.826 25.580 1.00 18.51 C ANISOU 589 CD GLN A 69 2046 2331 2656 34 -442 -418 C ATOM 590 OE1 GLN A 69 0.330 4.115 26.376 1.00 22.20 O ANISOU 590 OE1 GLN A 69 2749 2942 2744 339 -338 -51 O ATOM 591 NE2 GLN A 69 0.395 5.657 24.735 1.00 20.36 N ANISOU 591 NE2 GLN A 69 2119 2630 2988 76 -268 -48 N ATOM 592 N THR A 70 -4.644 7.515 23.625 1.00 12.29 N ANISOU 592 N THR A 70 1424 1964 1284 -43 4 -385 N ATOM 593 CA THR A 70 -5.243 8.350 22.603 1.00 13.19 C ANISOU 593 CA THR A 70 1478 2162 1370 45 -40 -262 C ATOM 594 C THR A 70 -4.263 9.265 21.922 1.00 13.93 C ANISOU 594 C THR A 70 1593 2060 1639 292 229 -138 C ATOM 595 O THR A 70 -4.673 10.172 21.198 1.00 17.98 O ANISOU 595 O THR A 70 1803 2613 2417 419 346 445 O ATOM 596 CB THR A 70 -6.480 9.072 23.129 1.00 15.81 C ANISOU 596 CB THR A 70 1498 2862 1645 234 74 -151 C ATOM 597 OG1 THR A 70 -6.113 9.743 24.324 1.00 19.50 O ANISOU 597 OG1 THR A 70 2520 3177 1714 1056 -217 -546 O ATOM 598 CG2 THR A 70 -7.611 8.084 23.437 1.00 25.96 C ANISOU 598 CG2 THR A 70 1553 4248 4063 -289 448 162 C ATOM 599 N ASN A 71 -2.966 9.022 22.048 1.00 13.48 N ANISOU 599 N ASN A 71 1556 2045 1523 94 278 164 N ATOM 600 CA ASN A 71 -1.918 9.733 21.328 1.00 13.86 C ANISOU 600 CA ASN A 71 1658 1966 1642 189 350 2 C ATOM 601 C ASN A 71 -1.417 9.037 20.093 1.00 12.67 C ANISOU 601 C ASN A 71 1432 1876 1504 45 257 152 C ATOM 602 O ASN A 71 -0.266 9.159 19.742 1.00 14.10 O ANISOU 602 O ASN A 71 1497 2018 1841 -18 410 -107 O ATOM 603 CB ASN A 71 -0.764 10.128 22.245 1.00 15.14 C ANISOU 603 CB ASN A 71 1798 2075 1878 -90 390 -259 C ATOM 604 CG ASN A 71 -0.002 8.962 22.808 1.00 14.63 C ANISOU 604 CG ASN A 71 1728 2460 1371 -306 66 -5 C ATOM 605 OD1 ASN A 71 -0.644 7.967 23.162 1.00 17.09 O ANISOU 605 OD1 ASN A 71 1706 2629 2160 -327 -49 507 O ATOM 606 ND2 ASN A 71 1.313 9.060 22.902 1.00 16.38 N ANISOU 606 ND2 ASN A 71 1713 2529 1980 -291 73 16 N ATOM 607 N CYS A 72 -2.277 8.201 19.468 1.00 13.34 N ANISOU 607 N CYS A 72 1331 2255 1485 87 280 56 N ATOM 608 CA CYS A 72 -1.938 7.542 18.226 1.00 11.92 C ANISOU 608 CA CYS A 72 1247 1819 1463 145 147 171 C ATOM 609 C CYS A 72 -2.520 8.251 17.040 1.00 11.47 C ANISOU 609 C CYS A 72 1216 1667 1477 21 146 95 C ATOM 610 O CYS A 72 -3.537 8.973 17.107 1.00 13.30 O ANISOU 610 O CYS A 72 1409 1941 1703 201 203 160 O ATOM 611 CB ACYS A 72 -2.301 6.059 18.154 0.80 12.34 C ANISOU 611 CB ACYS A 72 1288 1902 1499 6 98 307 C ATOM 612 CB BCYS A 72 -2.396 6.136 18.580 0.20 15.86 C ANISOU 612 CB BCYS A 72 2254 1982 1789 -266 -530 403 C ATOM 613 SG ACYS A 72 -1.143 4.952 19.032 0.80 11.86 S ANISOU 613 SG ACYS A 72 1341 1617 1549 127 203 44 S ATOM 614 SG BCYS A 72 -1.569 5.856 20.227 0.20 12.99 S ANISOU 614 SG BCYS A 72 1605 1596 1735 96 -384 175 S ATOM 615 N TYR A 73 -1.871 8.071 15.905 1.00 11.70 N ANISOU 615 N TYR A 73 1386 1676 1384 179 121 80 N ATOM 616 CA TYR A 73 -2.173 8.730 14.649 1.00 12.25 C ANISOU 616 CA TYR A 73 1603 1581 1472 296 97 124 C ATOM 617 C TYR A 73 -2.016 7.742 13.512 1.00 12.01 C ANISOU 617 C TYR A 73 1527 1558 1477 231 50 118 C ATOM 618 O TYR A 73 -1.002 7.014 13.475 1.00 13.33 O ANISOU 618 O TYR A 73 1664 1757 1642 375 -2 -42 O ATOM 619 CB TYR A 73 -1.289 9.955 14.401 1.00 14.01 C ANISOU 619 CB TYR A 73 2072 1545 1705 111 307 76 C ATOM 620 CG TYR A 73 -1.553 11.012 15.453 1.00 13.38 C ANISOU 620 CG TYR A 73 1718 1584 1783 90 294 33 C ATOM 621 CD1 TYR A 73 -0.865 10.983 16.648 1.00 14.82 C ANISOU 621 CD1 TYR A 73 2034 1795 1803 -160 220 104 C ATOM 622 CD2 TYR A 73 -2.483 12.018 15.244 1.00 17.24 C ANISOU 622 CD2 TYR A 73 2325 1680 2545 444 203 68 C ATOM 623 CE1 TYR A 73 -1.111 11.885 17.673 1.00 19.14 C ANISOU 623 CE1 TYR A 73 2494 2713 2065 -712 618 -569 C ATOM 624 CE2 TYR A 73 -2.764 12.894 16.251 1.00 21.78 C ANISOU 624 CE2 TYR A 73 2469 1930 3876 255 540 -707 C ATOM 625 CZ TYR A 73 -2.080 12.831 17.422 1.00 21.27 C ANISOU 625 CZ TYR A 73 2516 2470 3094 -499 1071 -1073 C ATOM 626 OH TYR A 73 -2.536 13.841 18.271 1.00 32.60 O ANISOU 626 OH TYR A 73 4685 3329 4373 -381 2020 -1816 O ATOM 627 N GLN A 74 -2.979 7.742 12.597 1.00 13.68 N ANISOU 627 N GLN A 74 1674 2066 1459 388 -47 45 N ATOM 628 CA GLN A 74 -2.960 6.926 11.400 1.00 13.09 C ANISOU 628 CA GLN A 74 1618 1875 1479 306 -57 128 C ATOM 629 C GLN A 74 -2.619 7.750 10.187 1.00 13.21 C ANISOU 629 C GLN A 74 1754 1865 1398 289 -125 106 C ATOM 630 O GLN A 74 -3.158 8.846 9.984 1.00 15.68 O ANISOU 630 O GLN A 74 2174 1985 1798 556 23 315 O ATOM 631 CB GLN A 74 -4.329 6.269 11.240 1.00 15.45 C ANISOU 631 CB GLN A 74 1726 2465 1678 -17 -70 181 C ATOM 632 CG GLN A 74 -4.393 5.332 10.041 1.00 17.93 C ANISOU 632 CG GLN A 74 2183 2392 2239 45 -360 -180 C ATOM 633 CD GLN A 74 -5.730 4.642 9.947 1.00 29.35 C ANISOU 633 CD GLN A 74 2149 5471 3531 -709 -310 -1513 C ATOM 634 OE1 GLN A 74 -6.270 4.137 10.915 1.00 40.85 O ANISOU 634 OE1 GLN A 74 3174 7243 5104 -2064 1303 -1693 O ATOM 635 NE2 GLN A 74 -6.126 4.505 8.697 1.00 62.45 N ANISOU 635 NE2 GLN A 74 4887 14383 4456 -3182 -1813 -1938 N ATOM 636 N SER A 75 -1.733 7.213 9.348 1.00 12.70 N ANISOU 636 N SER A 75 1713 1717 1396 145 -115 111 N ATOM 637 CA SER A 75 -1.368 7.966 8.146 1.00 13.47 C ANISOU 637 CA SER A 75 1702 1978 1437 171 -87 245 C ATOM 638 C SER A 75 -2.542 7.997 7.154 1.00 15.24 C ANISOU 638 C SER A 75 1887 2277 1626 225 -218 269 C ATOM 639 O SER A 75 -3.287 7.028 7.002 1.00 16.54 O ANISOU 639 O SER A 75 2060 2422 1801 108 -452 205 O ATOM 640 CB SER A 75 -0.177 7.261 7.501 1.00 13.28 C ANISOU 640 CB SER A 75 1652 1826 1566 -56 -95 103 C ATOM 641 OG SER A 75 -0.437 5.981 7.074 1.00 14.42 O ANISOU 641 OG SER A 75 1979 1970 1530 154 -143 159 O ATOM 642 N TYR A 76 -2.689 9.107 6.489 1.00 15.75 N ANISOU 642 N TYR A 76 2083 2164 1738 531 -264 194 N ATOM 643 CA TYR A 76 -3.745 9.211 5.460 1.00 18.41 C ANISOU 643 CA TYR A 76 2498 2700 1797 899 -399 164 C ATOM 644 C TYR A 76 -3.406 8.359 4.239 1.00 18.81 C ANISOU 644 C TYR A 76 2390 2941 1817 704 -529 40 C ATOM 645 O TYR A 76 -4.315 7.884 3.589 1.00 26.87 O ANISOU 645 O TYR A 76 2856 4913 2439 483 -836 -877 O ATOM 646 CB TYR A 76 -3.893 10.671 5.023 1.00 21.56 C ANISOU 646 CB TYR A 76 3209 2885 2097 1263 -196 436 C ATOM 647 CG TYR A 76 -4.419 11.633 6.058 1.00 24.30 C ANISOU 647 CG TYR A 76 3781 3122 2331 2034 -516 372 C ATOM 648 CD1 TYR A 76 -5.515 11.310 6.841 1.00 30.50 C ANISOU 648 CD1 TYR A 76 5093 3954 2540 2543 673 662 C ATOM 649 CD2 TYR A 76 -3.889 12.882 6.216 1.00 30.18 C ANISOU 649 CD2 TYR A 76 4838 2979 3649 2128 -942 -62 C ATOM 650 CE1 TYR A 76 -6.005 12.206 7.763 1.00 35.24 C ANISOU 650 CE1 TYR A 76 6693 4185 2512 3149 667 609 C ATOM 651 CE2 TYR A 76 -4.379 13.829 7.111 1.00 33.73 C ANISOU 651 CE2 TYR A 76 5268 3805 3744 2597 -1421 -627 C ATOM 652 CZ TYR A 76 -5.442 13.456 7.890 1.00 35.31 C ANISOU 652 CZ TYR A 76 4820 5184 3414 3007 -1482 -786 C ATOM 653 OH TYR A 76 -5.970 14.362 8.794 1.00 40.35 O ANISOU 653 OH TYR A 76 5599 5331 4401 3579 -1286 -1052 O ATOM 654 N SER A 77 -2.125 8.208 3.925 1.00 18.71 N ANISOU 654 N SER A 77 2637 2713 1758 889 -294 137 N ATOM 655 CA SER A 77 -1.705 7.432 2.761 1.00 20.74 C ANISOU 655 CA SER A 77 3276 3066 1540 1095 -226 206 C ATOM 656 C SER A 77 -1.076 6.104 3.216 1.00 16.83 C ANISOU 656 C SER A 77 2136 2885 1372 740 -211 89 C ATOM 657 O SER A 77 -0.652 5.940 4.338 1.00 17.09 O ANISOU 657 O SER A 77 2398 2597 1498 506 -452 -52 O ATOM 658 CB ASER A 77 -0.686 8.237 1.962 0.19 25.69 C ANISOU 658 CB ASER A 77 4672 2809 2279 1121 804 281 C ATOM 659 CB BSER A 77 -0.730 8.198 1.890 0.37 24.48 C ANISOU 659 CB BSER A 77 4081 3039 2183 1240 450 480 C ATOM 660 CB CSER A 77 -0.606 8.223 2.050 0.44 28.38 C ANISOU 660 CB CSER A 77 5368 3532 1885 628 855 657 C ATOM 661 OG ASER A 77 -0.139 7.428 0.943 0.19 22.26 O ANISOU 661 OG ASER A 77 4602 2615 1242 759 190 377 O ATOM 662 OG BSER A 77 0.563 8.247 2.470 0.37 31.04 O ANISOU 662 OG BSER A 77 3699 3510 4585 697 321 947 O ATOM 663 OG CSER A 77 -1.217 9.394 1.447 0.44 44.11 O ANISOU 663 OG CSER A 77 10647 3718 2397 2020 1529 1263 O ATOM 664 N THR A 78 -1.076 5.132 2.335 1.00 17.78 N ANISOU 664 N THR A 78 2023 3117 1615 729 -500 -149 N ATOM 665 CA THR A 78 -0.310 3.933 2.579 1.00 16.88 C ANISOU 665 CA THR A 78 1696 2636 2081 270 -363 -164 C ATOM 666 C THR A 78 1.176 4.235 2.378 1.00 15.07 C ANISOU 666 C THR A 78 1759 2206 1761 325 -191 -44 C ATOM 667 O THR A 78 1.608 5.171 1.694 1.00 18.23 O ANISOU 667 O THR A 78 2082 2740 2104 365 -293 567 O ATOM 668 CB THR A 78 -0.735 2.761 1.666 1.00 19.71 C ANISOU 668 CB THR A 78 2220 3145 2122 76 -632 -483 C ATOM 669 OG1 THR A 78 -0.490 3.139 0.317 1.00 24.01 O ANISOU 669 OG1 THR A 78 3177 3745 2199 -169 -532 -307 O ATOM 670 CG2 THR A 78 -2.204 2.388 1.755 1.00 23.12 C ANISOU 670 CG2 THR A 78 2387 3522 2876 -204 -576 -658 C ATOM 671 N MET A 79 1.978 3.407 3.056 1.00 14.03 N ANISOU 671 N MET A 79 1644 2042 1644 192 -100 -6 N ATOM 672 CA MET A 79 3.436 3.530 3.021 1.00 12.65 C ANISOU 672 CA MET A 79 1656 1608 1544 58 -162 211 C ATOM 673 C MET A 79 4.026 2.138 2.719 1.00 12.30 C ANISOU 673 C MET A 79 1698 1625 1349 101 -171 204 C ATOM 674 O MET A 79 3.438 1.097 3.033 1.00 13.40 O ANISOU 674 O MET A 79 1926 1611 1554 35 33 -4 O ATOM 675 CB MET A 79 3.941 4.001 4.409 1.00 13.88 C ANISOU 675 CB MET A 79 1747 1884 1645 -38 -106 -1 C ATOM 676 CG MET A 79 3.535 5.501 4.593 1.00 16.34 C ANISOU 676 CG MET A 79 1968 2251 1988 328 -152 -374 C ATOM 677 SD MET A 79 4.280 6.148 6.064 1.00 17.68 S ANISOU 677 SD MET A 79 2652 2319 1748 -21 -105 -243 S ATOM 678 CE MET A 79 3.792 7.854 5.940 1.00 21.93 C ANISOU 678 CE MET A 79 3458 2363 2512 343 -410 -603 C ATOM 679 N SER A 80 5.250 2.152 2.175 1.00 12.28 N ANISOU 679 N SER A 80 1763 1613 1288 92 -154 145 N ATOM 680 CA SER A 80 5.989 0.932 1.964 1.00 12.36 C ANISOU 680 CA SER A 80 1915 1629 1153 142 -112 114 C ATOM 681 C SER A 80 6.609 0.456 3.250 1.00 10.86 C ANISOU 681 C SER A 80 1520 1375 1230 86 -103 15 C ATOM 682 O SER A 80 7.382 1.223 3.876 1.00 12.70 O ANISOU 682 O SER A 80 1737 1644 1444 -63 -226 -17 O ATOM 683 CB SER A 80 7.079 1.218 0.928 1.00 13.28 C ANISOU 683 CB SER A 80 1976 1828 1243 19 -48 119 C ATOM 684 OG SER A 80 7.906 0.048 0.816 1.00 16.42 O ANISOU 684 OG SER A 80 2413 2149 1675 315 246 12 O ATOM 685 N ILE A 81 6.281 -0.734 3.678 1.00 10.71 N ANISOU 685 N ILE A 81 1562 1362 1144 99 -191 -44 N ATOM 686 CA ILE A 81 6.764 -1.282 4.917 1.00 10.70 C ANISOU 686 CA ILE A 81 1668 1383 1015 14 -142 5 C ATOM 687 C ILE A 81 7.285 -2.701 4.717 1.00 11.13 C ANISOU 687 C ILE A 81 1828 1446 956 87 -258 -101 C ATOM 688 O ILE A 81 6.923 -3.400 3.762 1.00 12.99 O ANISOU 688 O ILE A 81 2009 1660 1268 253 -361 -309 O ATOM 689 CB ILE A 81 5.685 -1.274 6.024 1.00 11.99 C ANISOU 689 CB ILE A 81 1674 1795 1085 231 -117 -25 C ATOM 690 CG1 ILE A 81 4.514 -2.182 5.716 1.00 14.73 C ANISOU 690 CG1 ILE A 81 1757 2084 1755 16 68 -141 C ATOM 691 CG2 ILE A 81 5.256 0.153 6.292 1.00 14.51 C ANISOU 691 CG2 ILE A 81 2057 1897 1560 403 -56 -226 C ATOM 692 CD1 ILE A 81 3.597 -2.379 6.935 1.00 22.47 C ANISOU 692 CD1 ILE A 81 2006 4353 2178 -679 135 369 C ATOM 693 N THR A 82 8.134 -3.136 5.611 1.00 10.60 N ANISOU 693 N THR A 82 1748 1236 1045 51 -191 -93 N ATOM 694 CA THR A 82 8.585 -4.504 5.717 1.00 10.24 C ANISOU 694 CA THR A 82 1659 1208 1023 56 -113 -84 C ATOM 695 C THR A 82 8.289 -5.017 7.109 1.00 10.16 C ANISOU 695 C THR A 82 1468 1221 1170 55 -91 -27 C ATOM 696 O THR A 82 8.693 -4.419 8.101 1.00 12.06 O ANISOU 696 O THR A 82 2076 1456 1051 -234 -80 -65 O ATOM 697 CB THR A 82 10.100 -4.647 5.438 1.00 11.07 C ANISOU 697 CB THR A 82 1704 1358 1145 0 41 -19 C ATOM 698 OG1 THR A 82 10.372 -4.148 4.125 1.00 12.90 O ANISOU 698 OG1 THR A 82 2121 1591 1190 49 249 -86 O ATOM 699 CG2 THR A 82 10.555 -6.076 5.524 1.00 13.14 C ANISOU 699 CG2 THR A 82 1869 1367 1757 182 95 -35 C ATOM 700 N ASP A 83 7.598 -6.144 7.191 1.00 10.91 N ANISOU 700 N ASP A 83 1663 1279 1202 -66 -42 -50 N ATOM 701 CA ASP A 83 7.350 -6.847 8.433 1.00 11.49 C ANISOU 701 CA ASP A 83 1658 1337 1372 -54 103 13 C ATOM 702 C ASP A 83 8.395 -7.932 8.597 1.00 11.07 C ANISOU 702 C ASP A 83 1731 1303 1171 -46 61 7 C ATOM 703 O ASP A 83 8.716 -8.664 7.648 1.00 12.83 O ANISOU 703 O ASP A 83 2100 1529 1248 190 -120 -198 O ATOM 704 CB AASP A 83 5.925 -7.432 8.248 0.52 17.36 C ANISOU 704 CB AASP A 83 1515 2791 2289 -335 285 253 C ATOM 705 CB BASP A 83 5.931 -7.434 8.468 0.47 14.40 C ANISOU 705 CB BASP A 83 1708 1619 2146 -155 170 324 C ATOM 706 CG AASP A 83 5.491 -8.304 9.397 0.52 19.26 C ANISOU 706 CG AASP A 83 1931 2761 2626 -495 638 269 C ATOM 707 CG BASP A 83 4.876 -6.367 8.667 0.47 16.30 C ANISOU 707 CG BASP A 83 1593 2031 2568 -76 64 -106 C ATOM 708 OD1AASP A 83 5.786 -9.509 9.423 0.52 22.97 O ANISOU 708 OD1AASP A 83 3228 2579 2920 -749 497 179 O ATOM 709 OD1BASP A 83 3.751 -6.632 8.169 0.47 23.44 O ANISOU 709 OD1BASP A 83 1789 3174 3943 210 -526 -904 O ATOM 710 OD2AASP A 83 4.883 -7.789 10.328 0.52 27.59 O ANISOU 710 OD2AASP A 83 4451 2918 3113 -1193 1818 -250 O ATOM 711 OD2BASP A 83 5.047 -5.406 9.425 0.47 18.43 O ANISOU 711 OD2BASP A 83 1856 1909 3238 -107 -22 -225 O ATOM 712 N CYS A 84 8.924 -8.019 9.800 1.00 11.08 N ANISOU 712 N CYS A 84 1875 1233 1100 -10 120 24 N ATOM 713 CA CYS A 84 9.916 -9.012 10.176 1.00 11.18 C ANISOU 713 CA CYS A 84 1975 1181 1090 69 83 -29 C ATOM 714 C CYS A 84 9.328 -9.823 11.320 1.00 11.82 C ANISOU 714 C CYS A 84 2150 1281 1059 57 110 6 C ATOM 715 O CYS A 84 8.963 -9.253 12.337 1.00 15.15 O ANISOU 715 O CYS A 84 3100 1372 1284 -6 527 62 O ATOM 716 CB CYS A 84 11.203 -8.371 10.657 1.00 11.48 C ANISOU 716 CB CYS A 84 1894 1338 1128 148 84 -41 C ATOM 717 SG CYS A 84 12.002 -7.306 9.425 1.00 11.87 S ANISOU 717 SG CYS A 84 1965 1154 1389 -26 39 -85 S ATOM 718 N ARG A 85 9.322 -11.141 11.214 1.00 12.64 N ANISOU 718 N ARG A 85 2111 1267 1424 -60 244 125 N ATOM 719 CA ARG A 85 8.712 -12.011 12.238 1.00 14.22 C ANISOU 719 CA ARG A 85 2262 1425 1716 -65 303 192 C ATOM 720 C ARG A 85 9.659 -13.196 12.464 1.00 12.36 C ANISOU 720 C ARG A 85 2052 1273 1371 -278 313 173 C ATOM 721 O ARG A 85 10.146 -13.787 11.496 1.00 13.87 O ANISOU 721 O ARG A 85 2401 1526 1343 -32 271 18 O ATOM 722 CB AARG A 85 7.355 -12.559 11.791 0.52 22.44 C ATOM 723 CB BARG A 85 7.399 -12.609 11.633 0.47 17.90 C ATOM 724 CG AARG A 85 6.372 -12.871 12.881 0.52 46.50 C ATOM 725 CG BARG A 85 6.529 -13.517 12.454 0.47 32.96 C ATOM 726 CD AARG A 85 5.196 -11.906 12.849 0.52 76.07 C ATOM 727 CD BARG A 85 5.211 -13.556 11.649 0.47 28.01 C ATOM 728 NE AARG A 85 4.686 -11.641 11.496 0.52 68.52 N ATOM 729 NE BARG A 85 4.897 -12.163 11.225 0.47 40.54 N ATOM 730 CZ AARG A 85 3.884 -10.613 11.213 0.52 87.15 C ATOM 731 CZ BARG A 85 4.438 -11.259 12.102 0.47 80.84 C ATOM 732 NH1AARG A 85 3.481 -9.787 12.175 0.52 54.88 N ATOM 733 NH1BARG A 85 4.293 -11.592 13.382 0.47122.85 N ATOM 734 NH2AARG A 85 3.483 -10.456 9.961 0.52157.91 N ATOM 735 NH2BARG A 85 4.159 -10.012 11.757 0.47 59.85 N ATOM 736 N GLU A 86 9.943 -13.514 13.709 1.00 13.21 N ANISOU 736 N GLU A 86 2322 1320 1378 -144 364 161 N ATOM 737 CA GLU A 86 10.849 -14.585 14.040 1.00 13.12 C ANISOU 737 CA GLU A 86 2165 1372 1449 -235 187 167 C ATOM 738 C GLU A 86 10.343 -15.915 13.461 1.00 14.65 C ANISOU 738 C GLU A 86 2231 1167 2169 -238 167 414 C ATOM 739 O GLU A 86 9.183 -16.239 13.568 1.00 18.55 O ANISOU 739 O GLU A 86 2362 1534 3154 -447 311 232 O ATOM 740 CB GLU A 86 10.931 -14.640 15.565 1.00 18.64 C ANISOU 740 CB GLU A 86 3271 2397 1415 282 287 472 C ATOM 741 CG GLU A 86 12.134 -15.313 16.090 1.00 19.93 C ANISOU 741 CG GLU A 86 2910 3189 1474 141 64 129 C ATOM 742 CD GLU A 86 12.295 -15.244 17.552 1.00 16.82 C ANISOU 742 CD GLU A 86 2880 2095 1417 -309 159 235 C ATOM 743 OE1 GLU A 86 11.347 -14.936 18.334 1.00 20.46 O ANISOU 743 OE1 GLU A 86 3187 2906 1680 -256 395 -30 O ATOM 744 OE2 GLU A 86 13.409 -15.593 17.939 1.00 17.39 O ANISOU 744 OE2 GLU A 86 2964 1994 1650 -388 -204 -19 O ATOM 745 N THR A 87 11.288 -16.683 12.918 1.00 15.11 N ANISOU 745 N THR A 87 2367 1108 2266 -44 -193 100 N ATOM 746 CA THR A 87 10.934 -18.002 12.423 1.00 16.68 C ANISOU 746 CA THR A 87 2770 1111 2458 -299 -273 129 C ATOM 747 C THR A 87 11.162 -19.065 13.445 1.00 13.84 C ANISOU 747 C THR A 87 2043 1074 2142 -131 154 -26 C ATOM 748 O THR A 87 11.776 -18.840 14.471 1.00 15.28 O ANISOU 748 O THR A 87 2658 1226 1923 -373 176 -26 O ATOM 749 CB THR A 87 11.787 -18.381 11.213 1.00 17.91 C ANISOU 749 CB THR A 87 3666 1434 1703 -466 -397 -31 C ATOM 750 OG1 THR A 87 13.134 -18.619 11.669 1.00 19.23 O ANISOU 750 OG1 THR A 87 3265 2057 1986 -320 256 -18 O ATOM 751 CG2 THR A 87 11.817 -17.298 10.148 1.00 25.31 C ANISOU 751 CG2 THR A 87 5716 1729 2171 -288 -233 375 C ATOM 752 N GLY A 88 10.686 -20.274 13.100 1.00 15.90 N ANISOU 752 N GLY A 88 2566 1132 2344 -337 17 -83 N ATOM 753 CA GLY A 88 10.805 -21.380 14.054 1.00 16.43 C ANISOU 753 CA GLY A 88 2566 1167 2510 -473 294 47 C ATOM 754 C GLY A 88 12.182 -21.792 14.313 1.00 15.12 C ANISOU 754 C GLY A 88 2686 1260 1799 -448 131 109 C ATOM 755 O GLY A 88 12.458 -22.478 15.312 1.00 22.49 O ANISOU 755 O GLY A 88 3554 2493 2499 -828 -416 943 O ATOM 756 N SER A 89 13.140 -21.511 13.459 1.00 14.54 N ANISOU 756 N SER A 89 2363 1270 1892 -160 -13 -58 N ATOM 757 CA SER A 89 14.535 -21.864 13.618 1.00 17.16 C ANISOU 757 CA SER A 89 2487 1414 2617 -59 10 -414 C ATOM 758 C SER A 89 15.342 -20.818 14.330 1.00 17.92 C ANISOU 758 C SER A 89 2801 1430 2576 78 -690 -297 C ATOM 759 O SER A 89 16.531 -20.978 14.573 1.00 23.49 O ANISOU 759 O SER A 89 2808 2160 3956 319 -820 -886 O ATOM 760 CB ASER A 89 15.151 -22.136 12.237 0.63 20.88 C ANISOU 760 CB ASER A 89 2987 1743 3202 -16 508 -1027 C ATOM 761 CB BSER A 89 15.114 -22.154 12.221 0.37 23.09 C ANISOU 761 CB BSER A 89 2394 3066 3311 -1006 562 -1482 C ATOM 762 OG ASER A 89 14.556 -23.348 11.832 0.63 22.65 O ANISOU 762 OG ASER A 89 2668 2262 3675 67 -157 -1550 O ATOM 763 OG BSER A 89 15.093 -21.002 11.398 0.37 37.89 O ANISOU 763 OG BSER A 89 5627 5506 3262 -257 2038 149 O ATOM 764 N SER A 90 14.749 -19.705 14.727 1.00 14.44 N ANISOU 764 N SER A 90 2472 1280 1733 -306 -170 -10 N ATOM 765 CA SER A 90 15.489 -18.664 15.444 1.00 14.46 C ANISOU 765 CA SER A 90 2693 1404 1396 -368 -130 10 C ATOM 766 C SER A 90 15.891 -19.121 16.811 1.00 16.48 C ANISOU 766 C SER A 90 2911 1762 1589 -488 -187 186 C ATOM 767 O SER A 90 15.011 -19.601 17.550 1.00 20.74 O ANISOU 767 O SER A 90 3470 2741 1669 -984 -192 628 O ATOM 768 CB SER A 90 14.524 -17.496 15.549 1.00 14.88 C ANISOU 768 CB SER A 90 2623 1308 1721 -463 -45 -67 C ATOM 769 OG SER A 90 15.111 -16.384 16.201 1.00 15.43 O ANISOU 769 OG SER A 90 2622 1427 1813 -673 -111 -61 O ATOM 770 N LYS A 91 17.144 -18.876 17.170 1.00 16.11 N ANISOU 770 N LYS A 91 2969 1430 1721 -329 -429 145 N ATOM 771 CA LYS A 91 17.654 -19.248 18.472 1.00 18.06 C ANISOU 771 CA LYS A 91 3688 1292 1883 -259 -675 160 C ATOM 772 C LYS A 91 18.812 -18.357 18.860 1.00 16.64 C ANISOU 772 C LYS A 91 3153 1658 1511 -135 -378 46 C ATOM 773 O LYS A 91 19.839 -18.358 18.187 1.00 19.61 O ANISOU 773 O LYS A 91 3346 2150 1955 9 -5 -372 O ATOM 774 CB LYS A 91 18.167 -20.703 18.465 1.00 22.44 C ATOM 775 CG LYS A 91 18.549 -21.121 19.884 1.00 25.66 C ATOM 776 CD LYS A 91 18.934 -22.594 19.893 1.00 39.24 C ATOM 777 CE LYS A 91 19.861 -22.858 21.075 1.00 88.60 C ATOM 778 NZ LYS A 91 21.254 -22.397 20.793 1.00152.00 N ATOM 779 N TYR A 92 18.599 -17.522 19.863 1.00 15.73 N ANISOU 779 N TYR A 92 2429 1743 1804 -72 -380 -104 N ATOM 780 CA TYR A 92 19.595 -16.551 20.292 1.00 14.69 C ANISOU 780 CA TYR A 92 2135 1833 1612 31 -279 -165 C ATOM 781 C TYR A 92 20.958 -17.217 20.477 1.00 15.29 C ANISOU 781 C TYR A 92 2289 1882 1637 330 -309 -194 C ATOM 782 O TYR A 92 21.021 -18.271 21.096 1.00 18.56 O ANISOU 782 O TYR A 92 2865 2146 2040 432 -459 6 O ATOM 783 CB TYR A 92 19.135 -15.921 21.612 1.00 14.50 C ANISOU 783 CB TYR A 92 1999 1809 1701 -106 -4 -165 C ATOM 784 CG TYR A 92 20.037 -14.855 22.107 1.00 13.48 C ANISOU 784 CG TYR A 92 1982 1615 1524 54 -158 -130 C ATOM 785 CD1 TYR A 92 19.908 -13.566 21.631 1.00 14.53 C ANISOU 785 CD1 TYR A 92 2172 1777 1573 23 -287 -59 C ATOM 786 CD2 TYR A 92 21.068 -15.102 23.004 1.00 15.24 C ANISOU 786 CD2 TYR A 92 2609 1868 1313 9 -419 -112 C ATOM 787 CE1 TYR A 92 20.754 -12.545 22.046 1.00 14.45 C ANISOU 787 CE1 TYR A 92 2047 1582 1859 54 -172 23 C ATOM 788 CE2 TYR A 92 21.936 -14.129 23.388 1.00 15.67 C ANISOU 788 CE2 TYR A 92 2402 1907 1645 148 -582 -195 C ATOM 789 CZ TYR A 92 21.769 -12.866 22.942 1.00 15.12 C ANISOU 789 CZ TYR A 92 1959 1884 1903 -111 -237 -121 C ATOM 790 OH TYR A 92 22.647 -11.911 23.409 1.00 18.90 O ANISOU 790 OH TYR A 92 2369 2231 2581 -369 -601 -51 O ATOM 791 N PRO A 93 22.056 -16.643 20.000 1.00 17.02 N ANISOU 791 N PRO A 93 2116 2370 1981 225 -372 -200 N ATOM 792 CA PRO A 93 22.148 -15.298 19.402 1.00 17.49 C ANISOU 792 CA PRO A 93 2067 2451 2129 123 -96 -58 C ATOM 793 C PRO A 93 21.937 -15.251 17.922 1.00 17.92 C ANISOU 793 C PRO A 93 2155 2561 2093 293 -73 -58 C ATOM 794 O PRO A 93 22.063 -14.166 17.309 1.00 21.88 O ANISOU 794 O PRO A 93 3349 2832 2134 -152 85 33 O ATOM 795 CB PRO A 93 23.609 -14.881 19.701 1.00 20.31 C ANISOU 795 CB PRO A 93 2180 3248 2289 -270 -47 -113 C ATOM 796 CG PRO A 93 24.340 -16.191 19.617 1.00 26.43 C ANISOU 796 CG PRO A 93 2004 3774 4263 157 -470 -186 C ATOM 797 CD PRO A 93 23.400 -17.191 20.272 1.00 20.40 C ANISOU 797 CD PRO A 93 2233 2899 2620 694 -439 -353 C ATOM 798 N ASN A 94 21.585 -16.399 17.306 1.00 17.15 N ANISOU 798 N ASN A 94 2036 2640 1839 389 82 -52 N ATOM 799 CA ASN A 94 21.321 -16.507 15.886 1.00 18.93 C ANISOU 799 CA ASN A 94 2342 2997 1853 623 -110 -158 C ATOM 800 C ASN A 94 19.844 -16.364 15.574 1.00 16.25 C ANISOU 800 C ASN A 94 2280 2282 1613 264 36 -330 C ATOM 801 O ASN A 94 19.139 -17.290 15.235 1.00 18.25 O ANISOU 801 O ASN A 94 2733 2099 2101 214 -121 -393 O ATOM 802 CB ASN A 94 21.880 -17.828 15.366 1.00 25.77 C ANISOU 802 CB ASN A 94 3174 4071 2547 1455 -210 -1039 C ATOM 803 CG ASN A 94 23.413 -17.935 15.611 1.00 34.45 C ANISOU 803 CG ASN A 94 3170 5515 4406 2061 -194 -1219 C ATOM 804 OD1 ASN A 94 23.849 -18.845 16.309 1.00 53.42 O ANISOU 804 OD1 ASN A 94 4285 7573 8439 3124 -562 1063 O ATOM 805 ND2 ASN A 94 24.116 -16.928 15.133 1.00 42.92 N ANISOU 805 ND2 ASN A 94 2767 8107 5435 1563 729 -28 N ATOM 806 N CYS A 95 19.413 -15.131 15.778 1.00 15.37 N ANISOU 806 N CYS A 95 1933 2117 1788 40 -172 -213 N ATOM 807 CA CYS A 95 18.059 -14.731 15.560 1.00 13.48 C ANISOU 807 CA CYS A 95 1996 1677 1448 -170 -69 -77 C ATOM 808 C CYS A 95 17.696 -14.761 14.074 1.00 14.23 C ANISOU 808 C CYS A 95 2078 2052 1276 -208 12 95 C ATOM 809 O CYS A 95 18.507 -14.328 13.264 1.00 20.65 O ANISOU 809 O CYS A 95 2710 3531 1605 -1002 201 92 O ATOM 810 CB CYS A 95 17.720 -13.381 16.150 1.00 13.57 C ANISOU 810 CB CYS A 95 2212 1380 1564 -119 -57 116 C ATOM 811 SG CYS A 95 18.181 -13.179 17.870 1.00 13.75 S ANISOU 811 SG CYS A 95 2086 1521 1619 -155 -112 -121 S ATOM 812 N ALA A 96 16.600 -15.276 13.625 1.00 12.79 N ANISOU 812 N ALA A 96 2156 1509 1194 -88 -74 66 N ATOM 813 CA ALA A 96 16.194 -15.508 12.298 1.00 13.18 C ANISOU 813 CA ALA A 96 2312 1610 1086 120 9 -55 C ATOM 814 C ALA A 96 14.756 -15.034 12.075 1.00 11.78 C ANISOU 814 C ALA A 96 2135 1102 1238 -179 -7 26 C ATOM 815 O ALA A 96 13.870 -15.276 12.900 1.00 13.38 O ANISOU 815 O ALA A 96 2285 1409 1392 -225 136 205 O ATOM 816 CB ALA A 96 16.312 -16.998 11.946 1.00 17.71 C ANISOU 816 CB ALA A 96 2950 1840 1938 542 -356 -568 C ATOM 817 N TYR A 97 14.531 -14.425 10.922 1.00 11.69 N ANISOU 817 N TYR A 97 2102 1200 1140 -28 98 12 N ATOM 818 CA TYR A 97 13.317 -13.736 10.589 1.00 11.84 C ANISOU 818 CA TYR A 97 2161 1130 1207 -21 89 -64 C ATOM 819 C TYR A 97 12.836 -14.016 9.185 1.00 12.17 C ANISOU 819 C TYR A 97 2293 1247 1083 -246 109 26 C ATOM 820 O TYR A 97 13.622 -14.155 8.255 1.00 14.36 O ANISOU 820 O TYR A 97 2456 1810 1190 -145 120 -194 O ATOM 821 CB TYR A 97 13.546 -12.174 10.694 1.00 11.95 C ANISOU 821 CB TYR A 97 2302 1102 1135 -62 4 -4 C ATOM 822 CG TYR A 97 13.881 -11.757 12.099 1.00 11.22 C ANISOU 822 CG TYR A 97 2085 1065 1115 -75 73 2 C ATOM 823 CD1 TYR A 97 12.837 -11.496 12.991 1.00 11.64 C ANISOU 823 CD1 TYR A 97 2032 1099 1291 -136 74 -111 C ATOM 824 CD2 TYR A 97 15.165 -11.715 12.581 1.00 11.75 C ANISOU 824 CD2 TYR A 97 2055 1244 1166 -14 134 56 C ATOM 825 CE1 TYR A 97 13.107 -11.185 14.305 1.00 12.10 C ANISOU 825 CE1 TYR A 97 1961 1416 1221 40 117 -159 C ATOM 826 CE2 TYR A 97 15.434 -11.422 13.922 1.00 12.12 C ANISOU 826 CE2 TYR A 97 1868 1344 1393 24 16 -77 C ATOM 827 CZ TYR A 97 14.403 -11.165 14.784 1.00 11.74 C ANISOU 827 CZ TYR A 97 2090 1211 1162 -16 46 -96 C ATOM 828 OH TYR A 97 14.716 -10.877 16.103 1.00 14.16 O ANISOU 828 OH TYR A 97 2240 1907 1231 128 -135 -120 O ATOM 829 N LYS A 98 11.532 -14.015 9.034 1.00 12.59 N ANISOU 829 N LYS A 98 2333 1178 1273 -123 -9 -129 N ATOM 830 CA LYS A 98 10.823 -13.994 7.757 1.00 12.84 C ANISOU 830 CA LYS A 98 2489 1198 1191 -128 -39 -44 C ATOM 831 C LYS A 98 10.548 -12.536 7.382 1.00 12.21 C ANISOU 831 C LYS A 98 2248 1243 1146 -123 36 -132 C ATOM 832 O LYS A 98 10.079 -11.765 8.203 1.00 14.12 O ANISOU 832 O LYS A 98 2693 1315 1358 47 163 -185 O ATOM 833 CB LYS A 98 9.516 -14.764 7.824 1.00 16.41 C ANISOU 833 CB LYS A 98 2795 1395 2044 -425 -401 63 C ATOM 834 CG LYS A 98 8.721 -14.792 6.547 1.00 22.05 C ANISOU 834 CG LYS A 98 3435 2223 2720 -562 -1088 225 C ATOM 835 CD LYS A 98 7.288 -15.312 6.714 1.00 44.64 C ANISOU 835 CD LYS A 98 4636 6577 5747 -3223 -2351 1923 C ATOM 836 CE LYS A 98 6.661 -15.439 5.347 1.00 68.47 C ANISOU 836 CE LYS A 98 6272 11927 7816 -2092 -4771 89 C ATOM 837 NZ LYS A 98 5.565 -16.444 5.340 1.00 80.90 N ANISOU 837 NZ LYS A 98 4569 18128 8040 -3869 -1288 -4793 N ATOM 838 N THR A 99 10.865 -12.196 6.130 1.00 11.96 N ANISOU 838 N THR A 99 2251 1125 1169 -109 -21 -141 N ATOM 839 CA THR A 99 10.648 -10.883 5.581 1.00 11.38 C ANISOU 839 CA THR A 99 2114 1159 1051 11 -27 -246 C ATOM 840 C THR A 99 9.399 -10.852 4.725 1.00 12.64 C ANISOU 840 C THR A 99 2239 1305 1259 -100 -237 -257 C ATOM 841 O THR A 99 9.277 -11.645 3.794 1.00 15.42 O ANISOU 841 O THR A 99 2705 1604 1549 -1 -489 -477 O ATOM 842 CB THR A 99 11.850 -10.534 4.672 1.00 12.16 C ANISOU 842 CB THR A 99 2179 1398 1043 74 -17 -65 C ATOM 843 OG1 THR A 99 13.024 -10.540 5.439 1.00 12.88 O ANISOU 843 OG1 THR A 99 2104 1417 1372 16 17 -88 O ATOM 844 CG2 THR A 99 11.760 -9.221 3.964 1.00 14.12 C ANISOU 844 CG2 THR A 99 2469 1492 1403 52 87 115 C ATOM 845 N THR A 100 8.498 -9.902 4.960 1.00 13.04 N ANISOU 845 N THR A 100 2021 1469 1465 -83 -302 -270 N ATOM 846 CA THR A 100 7.265 -9.713 4.195 1.00 14.51 C ANISOU 846 CA THR A 100 2200 1638 1674 -53 -537 -252 C ATOM 847 C THR A 100 7.152 -8.270 3.803 1.00 13.81 C ANISOU 847 C THR A 100 2022 1714 1512 7 -369 -190 C ATOM 848 O THR A 100 7.231 -7.416 4.644 1.00 16.59 O ANISOU 848 O THR A 100 3236 1599 1468 -34 -437 -269 O ATOM 849 CB THR A 100 6.010 -10.162 5.007 1.00 20.14 C ANISOU 849 CB THR A 100 2137 2317 3196 -661 -508 411 C ATOM 850 OG1 THR A 100 6.204 -11.523 5.387 1.00 21.62 O ANISOU 850 OG1 THR A 100 2772 2248 3195 -668 -389 140 O ATOM 851 CG2 THR A 100 4.779 -10.065 4.101 1.00 28.03 C ANISOU 851 CG2 THR A 100 2433 3823 4393 -983 -1040 1031 C ATOM 852 N AGLN A 101 6.956 -7.981 2.516 0.51 16.84 N ANISOU 852 N AGLN A 101 3052 1851 1496 354 -592 -277 N ATOM 853 N BGLN A 101 6.935 -8.031 2.516 0.49 17.44 N ANISOU 853 N BGLN A 101 3338 1739 1551 215 -712 -299 N ATOM 854 CA AGLN A 101 6.843 -6.588 2.075 0.51 18.11 C ANISOU 854 CA AGLN A 101 3158 2064 1661 749 -643 -104 C ATOM 855 CA BGLN A 101 6.750 -6.705 1.972 0.49 16.57 C ANISOU 855 CA BGLN A 101 2717 2015 1564 379 -210 -14 C ATOM 856 C AGLN A 101 5.346 -6.310 1.938 0.51 19.57 C ANISOU 856 C AGLN A 101 3193 2262 1982 665 -1378 -984 C ATOM 857 C BGLN A 101 5.255 -6.370 2.050 0.49 16.26 C ANISOU 857 C BGLN A 101 2554 1886 1737 58 -476 -565 C ATOM 858 O AGLN A 101 4.550 -7.160 1.562 0.51 24.58 O ANISOU 858 O AGLN A 101 3665 2185 3487 525 -1554 -1233 O ATOM 859 O BGLN A 101 4.412 -7.200 1.743 0.49 22.99 O ANISOU 859 O BGLN A 101 3101 2174 3459 -58 -1234 -884 O ATOM 860 CB AGLN A 101 7.632 -6.411 0.789 0.51 24.07 C ANISOU 860 CB AGLN A 101 4690 2291 2164 764 186 244 C ATOM 861 CB BGLN A 101 7.124 -6.716 0.490 0.49 20.64 C ANISOU 861 CB BGLN A 101 3488 2868 1485 1388 -175 25 C ATOM 862 CG AGLN A 101 7.635 -5.085 0.063 0.51 25.82 C ANISOU 862 CG AGLN A 101 5909 2023 1878 411 -317 -61 C ATOM 863 CG BGLN A 101 8.501 -7.237 0.118 0.49 21.00 C ANISOU 863 CG BGLN A 101 3169 2527 2285 644 190 -365 C ATOM 864 CD AGLN A 101 8.194 -3.899 0.812 0.51 23.52 C ANISOU 864 CD AGLN A 101 3856 2637 2443 88 1008 -710 C ATOM 865 CD BGLN A 101 8.635 -7.312 -1.402 0.49 23.66 C ANISOU 865 CD BGLN A 101 1917 4842 2230 543 -20 -76 C ATOM 866 OE1AGLN A 101 9.182 -4.069 1.533 0.51 24.84 O ANISOU 866 OE1AGLN A 101 3975 3199 2262 -167 954 -580 O ATOM 867 OE1BGLN A 101 7.759 -7.736 -2.152 0.49 39.92 O ANISOU 867 OE1BGLN A 101 4809 7636 2723 -2783 271 -1332 O ATOM 868 NE2AGLN A 101 7.472 -2.775 0.765 0.51 25.25 N ANISOU 868 NE2AGLN A 101 4740 2199 2654 83 1118 -587 N ATOM 869 NE2BGLN A 101 9.784 -6.855 -1.897 0.49 32.79 N ANISOU 869 NE2BGLN A 101 4018 5323 3119 -1613 671 -101 N ATOM 870 N ALA A 102 4.965 -5.091 2.276 1.00 16.10 N ANISOU 870 N ALA A 102 2505 1870 1743 182 -557 -433 N ATOM 871 CA ALA A 102 3.569 -4.678 2.267 1.00 18.20 C ANISOU 871 CA ALA A 102 2410 1979 2525 38 -303 -589 C ATOM 872 C ALA A 102 3.430 -3.204 1.955 1.00 15.27 C ANISOU 872 C ALA A 102 2030 2086 1685 135 -557 -504 C ATOM 873 O ALA A 102 4.429 -2.484 2.094 1.00 15.56 O ANISOU 873 O ALA A 102 2179 2000 1733 69 -543 -132 O ATOM 874 CB ALA A 102 2.892 -5.019 3.601 1.00 22.77 C ANISOU 874 CB ALA A 102 2839 2336 3478 -303 280 62 C ATOM 875 N ASN A 103 2.254 -2.729 1.621 1.00 18.19 N ANISOU 875 N ASN A 103 1901 2227 2784 206 -438 -929 N ATOM 876 CA ASN A 103 1.915 -1.350 1.477 1.00 15.89 C ANISOU 876 CA ASN A 103 1961 2380 1696 333 -469 -516 C ATOM 877 C ASN A 103 0.680 -1.097 2.284 1.00 15.41 C ANISOU 877 C ASN A 103 1711 2257 1888 243 -496 -528 C ATOM 878 O ASN A 103 -0.381 -1.558 1.931 1.00 20.24 O ANISOU 878 O ASN A 103 2042 3311 2338 -305 -352 -928 O ATOM 879 CB AASN A 103 1.670 -0.925 0.010 0.28 20.09 C ANISOU 879 CB AASN A 103 2595 3559 1479 718 -562 -932 C ATOM 880 CB BASN A 103 1.766 -1.048 -0.046 0.72 26.26 C ANISOU 880 CB BASN A 103 2737 5371 1870 -168 -241 336 C ATOM 881 CG AASN A 103 2.951 -1.072 -0.818 0.28 21.12 C ANISOU 881 CG AASN A 103 2734 3875 1418 1452 -492 -175 C ATOM 882 CG BASN A 103 2.512 0.279 -0.369 0.72 34.37 C ANISOU 882 CG BASN A 103 4572 5671 2818 -517 -55 1322 C ATOM 883 OD1AASN A 103 3.112 -2.133 -1.404 0.28 30.86 O ANISOU 883 OD1AASN A 103 3777 4984 2964 494 847 -1717 O ATOM 884 OD1BASN A 103 3.556 0.326 -0.956 0.72 46.57 O ANISOU 884 OD1BASN A 103 5369 8731 3595 -3135 725 -424 O ATOM 885 ND2AASN A 103 3.762 -0.036 -0.819 0.28 23.65 N ANISOU 885 ND2AASN A 103 3291 3642 2052 1419 679 -22 N ATOM 886 ND2BASN A 103 1.737 1.193 0.141 0.72 42.97 N ANISOU 886 ND2BASN A 103 7698 5177 3452 976 16 1772 N ATOM 887 N LYS A 104 0.820 -0.408 3.428 1.00 14.35 N ANISOU 887 N LYS A 104 1644 2166 1644 -91 -260 -257 N ATOM 888 CA LYS A 104 -0.223 -0.285 4.430 1.00 14.36 C ANISOU 888 CA LYS A 104 1710 1939 1808 -48 -142 -145 C ATOM 889 C LYS A 104 -0.185 1.092 5.047 1.00 14.04 C ANISOU 889 C LYS A 104 1724 1903 1708 -35 -63 -74 C ATOM 890 O LYS A 104 0.822 1.768 5.010 1.00 14.66 O ANISOU 890 O LYS A 104 1649 2233 1686 -202 38 -180 O ATOM 891 CB ALYS A 104 -0.108 -1.351 5.511 0.69 15.84 C ATOM 892 CB BLYS A 104 0.095 -1.287 5.557 0.31 18.42 C ATOM 893 CG ALYS A 104 -0.500 -2.735 4.968 0.69 23.78 C ATOM 894 CG BLYS A 104 0.142 -2.742 5.107 0.31 15.07 C ATOM 895 CD ALYS A 104 -0.592 -3.721 6.140 0.69 31.55 C ATOM 896 CD BLYS A 104 -1.135 -3.467 5.510 0.31 30.39 C ATOM 897 CE ALYS A 104 -0.925 -5.140 5.721 0.69 45.99 C ATOM 898 CE BLYS A 104 -1.136 -4.955 5.193 0.31 22.40 C ATOM 899 NZ ALYS A 104 0.186 -6.089 6.072 0.69141.38 N ATOM 900 NZ BLYS A 104 -2.475 -5.358 4.637 0.31 44.80 N ATOM 901 N HIS A 105 -1.304 1.466 5.650 1.00 14.29 N ANISOU 901 N HIS A 105 1381 2147 1902 -136 -262 -357 N ATOM 902 CA HIS A 105 -1.304 2.636 6.528 1.00 13.72 C ANISOU 902 CA HIS A 105 1628 2005 1580 -46 -131 -103 C ATOM 903 C HIS A 105 -0.565 2.290 7.816 1.00 13.38 C ANISOU 903 C HIS A 105 1682 1769 1632 -50 -184 -126 C ATOM 904 O HIS A 105 -0.611 1.127 8.232 1.00 16.63 O ANISOU 904 O HIS A 105 2393 1813 2112 -443 -476 116 O ATOM 905 CB HIS A 105 -2.721 3.047 6.847 1.00 16.47 C ANISOU 905 CB HIS A 105 1667 2524 2069 203 -18 -152 C ATOM 906 CG HIS A 105 -3.587 3.418 5.674 1.00 19.05 C ANISOU 906 CG HIS A 105 1760 3012 2467 209 -453 -242 C ATOM 907 ND1 HIS A 105 -3.776 4.678 5.182 1.00 20.92 N ANISOU 907 ND1 HIS A 105 2015 3122 2811 458 -478 -64 N ATOM 908 CD2 HIS A 105 -4.323 2.580 4.872 1.00 24.46 C ANISOU 908 CD2 HIS A 105 2559 3408 3327 231 -1152 -587 C ATOM 909 CE1 HIS A 105 -4.578 4.662 4.120 1.00 26.96 C ANISOU 909 CE1 HIS A 105 2850 4252 3141 220 -1037 529 C ATOM 910 NE2 HIS A 105 -4.926 3.412 3.938 1.00 27.97 N ANISOU 910 NE2 HIS A 105 2446 4462 3718 414 -1549 -267 N ATOM 911 N ILE A 106 0.157 3.187 8.411 1.00 12.71 N ANISOU 911 N ILE A 106 1803 1653 1372 -108 -105 72 N ATOM 912 CA ILE A 106 0.801 3.008 9.668 1.00 12.41 C ANISOU 912 CA ILE A 106 1712 1673 1330 54 -39 -147 C ATOM 913 C ILE A 106 0.074 3.803 10.782 1.00 11.85 C ANISOU 913 C ILE A 106 1559 1513 1432 79 -88 -41 C ATOM 914 O ILE A 106 -0.531 4.833 10.538 1.00 13.80 O ANISOU 914 O ILE A 106 1908 1790 1545 367 -3 105 O ATOM 915 CB ILE A 106 2.277 3.374 9.591 1.00 13.00 C ANISOU 915 CB ILE A 106 1625 1777 1539 343 -150 -89 C ATOM 916 CG1 ILE A 106 2.564 4.863 9.439 1.00 14.95 C ANISOU 916 CG1 ILE A 106 1668 1936 2075 -15 -77 173 C ATOM 917 CG2 ILE A 106 2.969 2.521 8.531 1.00 17.31 C ANISOU 917 CG2 ILE A 106 2334 2613 1631 613 278 -226 C ATOM 918 CD1 ILE A 106 4.021 5.232 9.675 1.00 17.03 C ANISOU 918 CD1 ILE A 106 1703 2621 2147 -130 -101 82 C ATOM 919 N ILE A 107 0.202 3.285 11.992 1.00 11.19 N ANISOU 919 N ILE A 107 1554 1379 1320 71 -30 -61 N ATOM 920 CA ILE A 107 -0.305 3.902 13.187 1.00 11.51 C ANISOU 920 CA ILE A 107 1311 1617 1443 103 -49 -157 C ATOM 921 C ILE A 107 0.857 4.035 14.159 1.00 10.48 C ANISOU 921 C ILE A 107 1299 1389 1293 58 64 12 C ATOM 922 O ILE A 107 1.497 3.032 14.509 1.00 12.05 O ANISOU 922 O ILE A 107 1529 1442 1609 164 -85 -15 O ATOM 923 CB ILE A 107 -1.477 3.135 13.827 1.00 12.56 C ANISOU 923 CB ILE A 107 1425 1798 1551 -53 9 -7 C ATOM 924 CG1 ILE A 107 -2.648 3.015 12.835 1.00 15.95 C ANISOU 924 CG1 ILE A 107 1624 2347 2089 -237 -298 -116 C ATOM 925 CG2 ILE A 107 -1.908 3.863 15.096 1.00 14.79 C ANISOU 925 CG2 ILE A 107 1777 2026 1818 33 308 -176 C ATOM 926 CD1 ILE A 107 -3.823 2.221 13.308 1.00 22.79 C ANISOU 926 CD1 ILE A 107 1881 3909 2868 -905 -73 -156 C ATOM 927 N VAL A 108 1.134 5.257 14.578 1.00 11.32 N ANISOU 927 N VAL A 108 1400 1406 1495 124 -164 -18 N ATOM 928 CA VAL A 108 2.234 5.560 15.479 1.00 11.14 C ANISOU 928 CA VAL A 108 1315 1478 1440 118 -97 -51 C ATOM 929 C VAL A 108 1.698 6.346 16.682 1.00 10.68 C ANISOU 929 C VAL A 108 1228 1513 1318 36 -7 60 C ATOM 930 O VAL A 108 0.686 7.014 16.600 1.00 13.66 O ANISOU 930 O VAL A 108 1499 2134 1557 478 -120 -247 O ATOM 931 CB VAL A 108 3.361 6.351 14.816 1.00 12.61 C ANISOU 931 CB VAL A 108 1369 1828 1595 -14 85 -94 C ATOM 932 CG1 VAL A 108 4.011 5.544 13.687 1.00 15.27 C ANISOU 932 CG1 VAL A 108 1738 2368 1695 234 217 -148 C ATOM 933 CG2 VAL A 108 2.884 7.682 14.272 1.00 15.93 C ANISOU 933 CG2 VAL A 108 2333 1667 2054 -66 291 114 C ATOM 934 N ALA A 109 2.415 6.243 17.794 1.00 10.99 N ANISOU 934 N ALA A 109 1173 1529 1473 103 -44 -123 N ATOM 935 CA ALA A 109 2.172 7.086 18.978 1.00 11.35 C ANISOU 935 CA ALA A 109 1321 1582 1409 26 84 -36 C ATOM 936 C ALA A 109 3.181 8.249 18.970 1.00 10.82 C ANISOU 936 C ALA A 109 1319 1587 1205 -9 206 -191 C ATOM 937 O ALA A 109 4.344 8.001 18.669 1.00 12.33 O ANISOU 937 O ALA A 109 1276 1594 1816 -47 192 -124 O ATOM 938 CB ALA A 109 2.248 6.336 20.280 1.00 14.44 C ANISOU 938 CB ALA A 109 2051 1869 1566 -289 172 125 C ATOM 939 N CYS A 110 2.726 9.432 19.281 1.00 11.63 N ANISOU 939 N CYS A 110 1337 1596 1487 -25 182 -219 N ATOM 940 CA CYS A 110 3.565 10.635 19.255 1.00 11.92 C ANISOU 940 CA CYS A 110 1515 1592 1423 -94 262 -91 C ATOM 941 C CYS A 110 3.647 11.251 20.643 1.00 12.62 C ANISOU 941 C CYS A 110 1709 1620 1465 -159 329 -204 C ATOM 942 O CYS A 110 2.709 11.241 21.397 1.00 14.86 O ANISOU 942 O CYS A 110 1850 2157 1639 -202 575 -235 O ATOM 943 CB CYS A 110 2.998 11.629 18.245 1.00 14.14 C ANISOU 943 CB CYS A 110 2095 1646 1630 43 24 -120 C ATOM 944 SG CYS A 110 2.853 10.910 16.580 1.00 14.32 S ANISOU 944 SG CYS A 110 2202 1659 1579 81 -53 -97 S ATOM 945 N GLU A 111 4.804 11.876 20.914 1.00 13.26 N ANISOU 945 N GLU A 111 1813 1773 1450 -329 319 -276 N ATOM 946 CA GLU A 111 5.063 12.588 22.170 1.00 14.43 C ANISOU 946 CA GLU A 111 1940 2123 1419 -332 246 -366 C ATOM 947 C GLU A 111 6.013 13.746 21.879 1.00 15.24 C ANISOU 947 C GLU A 111 2027 2220 1545 -431 219 -498 C ATOM 948 O GLU A 111 6.802 13.662 20.950 1.00 16.83 O ANISOU 948 O GLU A 111 2356 2333 1706 -565 439 -412 O ATOM 949 CB GLU A 111 5.698 11.643 23.195 1.00 18.92 C ANISOU 949 CB GLU A 111 3162 2677 1349 -98 82 -183 C ATOM 950 CG GLU A 111 4.913 10.446 23.665 1.00 24.02 C ANISOU 950 CG GLU A 111 4343 3020 1763 -172 481 344 C ATOM 951 CD GLU A 111 5.584 9.579 24.743 1.00 26.25 C ANISOU 951 CD GLU A 111 4715 3177 2083 -579 -452 331 C ATOM 952 OE1 GLU A 111 6.663 9.985 25.214 1.00 38.76 O ANISOU 952 OE1 GLU A 111 5360 5943 3425 -1385 -1283 457 O ATOM 953 OE2 GLU A 111 5.015 8.482 25.021 1.00 34.53 O ANISOU 953 OE2 GLU A 111 5678 3573 3868 -720 -363 1386 O ATOM 954 N GLY A 112 6.056 14.690 22.796 1.00 18.63 N ANISOU 954 N GLY A 112 2823 2343 1913 -669 413 -706 N ATOM 955 CA GLY A 112 7.087 15.672 22.873 1.00 20.85 C ANISOU 955 CA GLY A 112 3091 2609 2220 -931 -116 -669 C ATOM 956 C GLY A 112 6.841 16.966 22.171 1.00 19.51 C ANISOU 956 C GLY A 112 2983 2548 1884 -856 610 -673 C ATOM 957 O GLY A 112 5.780 17.191 21.616 1.00 20.52 O ANISOU 957 O GLY A 112 2885 2191 2721 -387 706 -699 O ATOM 958 N ASN A 113 7.846 17.843 22.280 1.00 21.73 N ANISOU 958 N ASN A 113 3290 2753 2213 -1054 688 -665 N ATOM 959 CA ASN A 113 7.887 19.080 21.556 1.00 26.27 C ANISOU 959 CA ASN A 113 4777 2454 2751 -1091 1503 -861 C ATOM 960 C ASN A 113 9.281 19.274 20.988 1.00 31.28 C ANISOU 960 C ASN A 113 5124 4004 2756 -2673 1506 -1251 C ATOM 961 O ASN A 113 10.199 19.534 21.784 1.00 38.56 O ANISOU 961 O ASN A 113 5742 5698 3213 -3502 1312 -1973 O ATOM 962 CB ASN A 113 7.415 20.314 22.341 1.00 34.92 C ANISOU 962 CB ASN A 113 7360 2777 3131 -854 1404 -1523 C ATOM 963 CG ASN A 113 7.698 21.604 21.466 1.00 51.25 C ANISOU 963 CG ASN A 113 10943 2316 6215 -1897 -157 -660 C ATOM 964 OD1 ASN A 113 8.659 22.305 21.981 1.00 86.80 O ANISOU 964 OD1 ASN A 113 11659 4481 16841 -3742 -4322 2432 O ATOM 965 ND2 ASN A 113 6.812 21.553 20.422 1.00 47.76 N ANISOU 965 ND2 ASN A 113 9904 2789 5454 914 673 -459 N ATOM 966 N PRO A 114 9.515 19.113 19.682 1.00 25.65 N ANISOU 966 N PRO A 114 4235 2788 2725 -1688 1293 -822 N ATOM 967 CA PRO A 114 8.562 18.779 18.620 1.00 23.25 C ANISOU 967 CA PRO A 114 3994 2186 2655 -1066 1201 -617 C ATOM 968 C PRO A 114 7.829 17.443 18.776 1.00 18.08 C ANISOU 968 C PRO A 114 2813 1812 2244 -356 722 -278 C ATOM 969 O PRO A 114 8.371 16.578 19.467 1.00 18.39 O ANISOU 969 O PRO A 114 2558 2226 2205 -415 261 -335 O ATOM 970 CB PRO A 114 9.403 18.725 17.326 1.00 26.24 C ANISOU 970 CB PRO A 114 4626 2735 2607 -1623 1400 -576 C ATOM 971 CG PRO A 114 10.697 19.281 17.729 1.00 38.45 C ANISOU 971 CG PRO A 114 4967 6773 2870 -2887 1587 -962 C ATOM 972 CD PRO A 114 10.916 19.214 19.193 1.00 29.37 C ANISOU 972 CD PRO A 114 4209 3925 3024 -1928 1316 -649 C ATOM 973 N TYR A 115 6.589 17.391 18.369 1.00 17.49 N ANISOU 973 N TYR A 115 2813 1468 2364 -16 561 -183 N ATOM 974 CA TYR A 115 5.711 16.234 18.538 1.00 15.73 C ANISOU 974 CA TYR A 115 2367 1591 2020 115 635 -181 C ATOM 975 C TYR A 115 6.045 15.215 17.455 1.00 14.35 C ANISOU 975 C TYR A 115 2430 1360 1662 114 352 57 C ATOM 976 O TYR A 115 5.754 15.415 16.283 1.00 17.89 O ANISOU 976 O TYR A 115 3267 1728 1804 612 -6 -76 O ATOM 977 CB TYR A 115 4.300 16.735 18.405 1.00 18.86 C ANISOU 977 CB TYR A 115 2525 1862 2780 260 489 -247 C ATOM 978 CG TYR A 115 3.200 15.818 18.913 1.00 16.81 C ANISOU 978 CG TYR A 115 2220 1907 2260 220 387 -435 C ATOM 979 CD1 TYR A 115 3.185 15.412 20.264 1.00 17.97 C ANISOU 979 CD1 TYR A 115 2180 2359 2291 55 160 -364 C ATOM 980 CD2 TYR A 115 2.145 15.494 18.097 1.00 17.68 C ANISOU 980 CD2 TYR A 115 2500 2032 2186 305 217 -459 C ATOM 981 CE1 TYR A 115 2.154 14.617 20.721 1.00 17.65 C ANISOU 981 CE1 TYR A 115 2286 2307 2114 148 333 -313 C ATOM 982 CE2 TYR A 115 1.095 14.727 18.571 1.00 17.70 C ANISOU 982 CE2 TYR A 115 2188 2057 2480 311 -2 -465 C ATOM 983 CZ TYR A 115 1.108 14.323 19.881 1.00 17.98 C ANISOU 983 CZ TYR A 115 2165 2238 2428 73 375 -465 C ATOM 984 OH TYR A 115 0.136 13.567 20.474 1.00 22.49 O ANISOU 984 OH TYR A 115 2691 2782 3071 -387 621 -544 O ATOM 985 N VAL A 116 6.653 14.115 17.861 1.00 12.97 N ANISOU 985 N VAL A 116 2088 1347 1491 -45 241 -86 N ATOM 986 CA VAL A 116 7.242 13.150 16.928 1.00 12.66 C ANISOU 986 CA VAL A 116 1887 1305 1619 13 364 -24 C ATOM 987 C VAL A 116 6.861 11.718 17.286 1.00 11.41 C ANISOU 987 C VAL A 116 1584 1397 1356 -130 249 -26 C ATOM 988 O VAL A 116 6.500 11.428 18.438 1.00 11.89 O ANISOU 988 O VAL A 116 1720 1489 1307 -141 311 -114 O ATOM 989 CB VAL A 116 8.764 13.295 16.868 1.00 14.30 C ANISOU 989 CB VAL A 116 1905 1383 2144 -189 420 87 C ATOM 990 CG1 VAL A 116 9.137 14.643 16.242 1.00 18.32 C ANISOU 990 CG1 VAL A 116 2431 1721 2810 -157 869 491 C ATOM 991 CG2 VAL A 116 9.407 13.091 18.226 1.00 16.40 C ANISOU 991 CG2 VAL A 116 1825 1782 2626 -252 0 181 C ATOM 992 N PRO A 117 7.016 10.789 16.335 1.00 11.84 N ANISOU 992 N PRO A 117 1819 1397 1282 -26 311 -39 N ATOM 993 CA PRO A 117 6.740 9.403 16.647 1.00 11.47 C ANISOU 993 CA PRO A 117 1560 1436 1363 -114 135 0 C ATOM 994 C PRO A 117 7.733 8.804 17.632 1.00 11.13 C ANISOU 994 C PRO A 117 1340 1319 1567 84 256 -177 C ATOM 995 O PRO A 117 8.934 8.965 17.498 1.00 13.21 O ANISOU 995 O PRO A 117 1326 1814 1878 -6 242 19 O ATOM 996 CB PRO A 117 6.805 8.662 15.306 1.00 13.33 C ANISOU 996 CB PRO A 117 1918 1646 1499 62 112 -267 C ATOM 997 CG PRO A 117 6.783 9.708 14.301 1.00 18.47 C ANISOU 997 CG PRO A 117 3906 1815 1296 169 158 -294 C ATOM 998 CD PRO A 117 7.306 10.987 14.917 1.00 14.02 C ANISOU 998 CD PRO A 117 2281 1704 1343 170 410 79 C ATOM 999 N VAL A 118 7.198 8.076 18.608 1.00 11.25 N ANISOU 999 N VAL A 118 1248 1564 1463 -7 42 44 N ATOM 1000 CA VAL A 118 8.010 7.374 19.586 1.00 12.22 C ANISOU 1000 CA VAL A 118 1271 1678 1694 98 -104 -67 C ATOM 1001 C VAL A 118 7.700 5.880 19.656 1.00 11.98 C ANISOU 1001 C VAL A 118 1366 1722 1464 73 -65 125 C ATOM 1002 O VAL A 118 8.418 5.165 20.343 1.00 16.78 O ANISOU 1002 O VAL A 118 1840 1823 2711 -7 -774 266 O ATOM 1003 CB VAL A 118 7.892 8.007 21.002 1.00 14.25 C ANISOU 1003 CB VAL A 118 1777 2033 1603 -112 -249 -128 C ATOM 1004 CG1 VAL A 118 8.485 9.400 20.940 1.00 17.12 C ANISOU 1004 CG1 VAL A 118 2459 2036 2009 -290 -467 -330 C ATOM 1005 CG2 VAL A 118 6.465 7.994 21.519 1.00 16.97 C ANISOU 1005 CG2 VAL A 118 2103 2712 1634 -28 238 -238 C ATOM 1006 N HIS A 119 6.638 5.420 19.031 1.00 11.93 N ANISOU 1006 N HIS A 119 1530 1518 1483 79 -76 -31 N ATOM 1007 CA HIS A 119 6.227 4.038 19.096 1.00 12.11 C ANISOU 1007 CA HIS A 119 1610 1482 1510 67 -65 66 C ATOM 1008 C HIS A 119 5.504 3.684 17.824 1.00 11.45 C ANISOU 1008 C HIS A 119 1372 1482 1497 185 -21 -30 C ATOM 1009 O HIS A 119 4.675 4.451 17.349 1.00 13.41 O ANISOU 1009 O HIS A 119 1658 1601 1835 336 -220 -161 O ATOM 1010 CB HIS A 119 5.379 3.824 20.333 1.00 16.19 C ANISOU 1010 CB HIS A 119 2138 2376 1638 -182 266 138 C ATOM 1011 CG HIS A 119 4.481 2.693 20.350 1.00 18.93 C ANISOU 1011 CG HIS A 119 2713 2726 1753 -539 167 395 C ATOM 1012 ND1 HIS A 119 4.902 1.488 20.770 1.00 21.65 N ANISOU 1012 ND1 HIS A 119 3350 2727 2150 -520 238 560 N ATOM 1013 CD2 HIS A 119 3.175 2.533 20.040 1.00 21.55 C ANISOU 1013 CD2 HIS A 119 2744 2759 2684 -566 48 -352 C ATOM 1014 CE1 HIS A 119 3.935 0.595 20.734 1.00 25.58 C ANISOU 1014 CE1 HIS A 119 3558 3088 3073 -902 353 940 C ATOM 1015 NE2 HIS A 119 2.848 1.236 20.251 1.00 21.98 N ANISOU 1015 NE2 HIS A 119 3396 2852 2102 -778 233 -346 N ATOM 1016 N PHE A 120 5.771 2.496 17.296 1.00 11.70 N ANISOU 1016 N PHE A 120 1280 1616 1548 248 -62 -23 N ATOM 1017 CA PHE A 120 5.054 1.939 16.133 1.00 11.39 C ANISOU 1017 CA PHE A 120 1376 1551 1402 214 38 -27 C ATOM 1018 C PHE A 120 3.951 1.036 16.665 1.00 11.29 C ANISOU 1018 C PHE A 120 1377 1546 1369 250 12 27 C ATOM 1019 O PHE A 120 4.257 0.021 17.310 1.00 14.13 O ANISOU 1019 O PHE A 120 1679 1666 2023 201 66 354 O ATOM 1020 CB PHE A 120 6.016 1.168 15.240 1.00 12.70 C ANISOU 1020 CB PHE A 120 1505 1711 1609 122 115 -91 C ATOM 1021 CG PHE A 120 5.386 0.776 13.915 1.00 13.18 C ANISOU 1021 CG PHE A 120 1539 1863 1605 320 273 -274 C ATOM 1022 CD1 PHE A 120 4.621 -0.348 13.775 1.00 15.67 C ANISOU 1022 CD1 PHE A 120 1745 2155 2055 18 292 -607 C ATOM 1023 CD2 PHE A 120 5.569 1.589 12.796 1.00 17.12 C ANISOU 1023 CD2 PHE A 120 2410 2402 1692 202 52 26 C ATOM 1024 CE1 PHE A 120 4.012 -0.647 12.549 1.00 18.47 C ANISOU 1024 CE1 PHE A 120 1899 2958 2163 -122 305 -786 C ATOM 1025 CE2 PHE A 120 5.019 1.274 11.558 1.00 18.85 C ANISOU 1025 CE2 PHE A 120 2489 2964 1710 281 41 -185 C ATOM 1026 CZ PHE A 120 4.172 0.196 11.476 1.00 19.45 C ANISOU 1026 CZ PHE A 120 2159 2867 2366 558 -274 -464 C ATOM 1027 N ASP A 121 2.694 1.364 16.455 1.00 11.54 N ANISOU 1027 N ASP A 121 1391 1513 1482 171 13 23 N ATOM 1028 CA ASP A 121 1.588 0.624 17.021 1.00 12.25 C ANISOU 1028 CA ASP A 121 1476 1818 1361 95 59 110 C ATOM 1029 C ASP A 121 1.089 -0.496 16.116 1.00 12.73 C ANISOU 1029 C ASP A 121 1614 1684 1540 -29 149 123 C ATOM 1030 O ASP A 121 0.824 -1.575 16.606 1.00 16.88 O ANISOU 1030 O ASP A 121 2799 1854 1760 -235 74 297 O ATOM 1031 CB ASP A 121 0.439 1.555 17.399 1.00 13.29 C ANISOU 1031 CB ASP A 121 1567 1946 1536 180 170 18 C ATOM 1032 CG ASP A 121 -0.453 0.972 18.494 1.00 14.32 C ANISOU 1032 CG ASP A 121 1857 1925 1658 -114 301 -197 C ATOM 1033 OD1 ASP A 121 0.112 0.577 19.534 1.00 19.67 O ANISOU 1033 OD1 ASP A 121 2392 3342 1739 -388 273 475 O ATOM 1034 OD2 ASP A 121 -1.646 0.941 18.311 1.00 16.90 O ANISOU 1034 OD2 ASP A 121 1810 2381 2229 -10 539 -109 O ATOM 1035 N ALA A 122 0.868 -0.228 14.849 1.00 12.69 N ANISOU 1035 N ALA A 122 1662 1634 1524 -107 69 133 N ATOM 1036 CA ALA A 122 0.213 -1.203 13.967 1.00 14.20 C ANISOU 1036 CA ALA A 122 1854 1736 1803 -323 -55 70 C ATOM 1037 C ALA A 122 0.352 -0.698 12.543 1.00 13.12 C ANISOU 1037 C ALA A 122 1546 1668 1771 -217 -151 28 C ATOM 1038 O ALA A 122 0.573 0.452 12.249 1.00 14.04 O ANISOU 1038 O ALA A 122 1928 1618 1787 -170 40 45 O ATOM 1039 CB ALA A 122 -1.275 -1.307 14.346 1.00 18.65 C ANISOU 1039 CB ALA A 122 1920 2700 2467 -620 219 318 C ATOM 1040 N SER A 123 0.114 -1.625 11.632 1.00 16.74 N ANISOU 1040 N SER A 123 2734 1767 1860 -527 -197 -28 N ATOM 1041 CA SER A 123 -0.190 -1.320 10.243 1.00 16.42 C ANISOU 1041 CA SER A 123 2231 2161 1849 -390 -220 18 C ATOM 1042 C SER A 123 -1.580 -1.827 9.899 1.00 17.67 C ANISOU 1042 C SER A 123 2276 2314 2125 -757 -97 48 C ATOM 1043 O SER A 123 -1.943 -2.917 10.400 1.00 21.55 O ANISOU 1043 O SER A 123 2930 2421 2839 -880 -403 294 O ATOM 1044 CB ASER A 123 0.847 -1.819 9.259 0.62 18.09 C ANISOU 1044 CB ASER A 123 2205 2649 2021 -611 -46 -18 C ATOM 1045 CB BSER A 123 0.740 -2.136 9.327 0.38 27.67 C ANISOU 1045 CB BSER A 123 3040 5601 1872 1703 314 750 C ATOM 1046 OG ASER A 123 0.969 -3.226 9.342 0.62 19.37 O ANISOU 1046 OG ASER A 123 2284 2651 2426 -229 335 -250 O ATOM 1047 OG BSER A 123 2.099 -1.924 9.616 0.38 36.98 O ANISOU 1047 OG BSER A 123 3117 7688 3245 1737 87 -511 O ATOM 1048 N VAL A 124 -2.306 -1.141 9.022 1.00 17.26 N ANISOU 1048 N VAL A 124 2165 2489 1905 -697 -144 -70 N ATOM 1049 CA VAL A 124 -3.668 -1.526 8.690 1.00 19.66 C ANISOU 1049 CA VAL A 124 2150 2951 2369 -990 -68 -179 C ATOM 1050 C VAL A 124 -3.898 -1.309 7.217 1.00 24.54 C ANISOU 1050 C VAL A 124 2195 4581 2548 -1506 -448 199 C ATOM 1051 O VAL A 124 -4.775 -2.007 6.668 1.00 34.30 O ANISOU 1051 O VAL A 124 4316 5229 3489 -2732 -1634 746 O ATOM 1052 CB VAL A 124 -4.751 -0.803 9.528 1.00 21.47 C ANISOU 1052 CB VAL A 124 2035 3056 3067 -555 -305 -148 C ATOM 1053 CG1 VAL A 124 -4.664 -1.126 11.023 1.00 25.33 C ANISOU 1053 CG1 VAL A 124 3134 3649 2840 -694 622 -385 C ATOM 1054 CG2 VAL A 124 -4.773 0.688 9.310 1.00 26.90 C ANISOU 1054 CG2 VAL A 124 3029 3018 4173 -495 75 -138 C ATOM 1055 OXT VAL A 124 -3.255 -0.473 6.549 1.00 20.75 O ANISOU 1055 OXT VAL A 124 1929 3579 2377 -603 -168 115 O TER 1056 VAL A 124 HETATM 1057 O HOH A 125 22.285 10.476 26.193 1.00 31.73 O ANISOU 1057 O HOH A 125 3703 4598 3757 187 104 -368 O HETATM 1058 O HOH A 126 21.996 8.173 30.733 1.00 44.20 O ANISOU 1058 O HOH A 126 6121 5466 5206 136 -431 -133 O HETATM 1059 O HOH A 127 18.999 10.729 28.939 1.00 53.88 O ANISOU 1059 O HOH A 127 6364 7472 6635 -70 409 282 O HETATM 1060 O HOH A 128 18.988 11.794 25.978 0.50 46.24 O ANISOU 1060 O HOH A 128 5979 5507 6082 79 -576 -209 O HETATM 1061 O HOH A 129 15.319 8.732 27.136 0.50 60.16 O ANISOU 1061 O HOH A 129 7762 7580 7516 -472 -450 105 O HETATM 1062 O HOH A 130 17.286 4.875 26.136 1.00 43.24 O ANISOU 1062 O HOH A 130 5222 5813 5396 -196 373 177 O HETATM 1063 O HOH A 131 16.721 3.436 23.963 1.00 45.15 O ANISOU 1063 O HOH A 131 5986 5709 5459 -165 -44 -30 O HETATM 1064 O HOH A 132 20.420 2.449 23.308 1.00 40.87 O ANISOU 1064 O HOH A 132 5128 4923 5478 -227 -331 209 O HETATM 1065 O HOH A 133 19.491 10.062 21.332 1.00 24.56 O ANISOU 1065 O HOH A 133 3227 3046 3060 -92 -13 -145 O HETATM 1066 O HOH A 134 16.501 12.804 19.884 1.00 43.44 O ANISOU 1066 O HOH A 134 5668 5037 5800 -399 -315 -198 O HETATM 1067 O HOH A 135 13.094 10.198 25.578 1.00 36.54 O ANISOU 1067 O HOH A 135 4295 5087 4501 483 387 -851 O HETATM 1068 O HOH A 136 12.116 11.570 22.405 1.00 28.36 O ANISOU 1068 O HOH A 136 3603 3541 3631 389 -167 -357 O HETATM 1069 O HOH A 137 18.629 6.758 15.856 1.00 22.55 O ANISOU 1069 O HOH A 137 2742 3001 2827 -129 43 99 O HETATM 1070 O HOH A 138 17.450 5.152 10.734 1.00 34.57 O ANISOU 1070 O HOH A 138 4309 4285 4541 -217 109 6 O HETATM 1071 O HOH A 139 16.284 12.983 13.347 1.00 39.91 O ANISOU 1071 O HOH A 139 5145 4762 5258 -353 -240 148 O HETATM 1072 O HOH A 140 16.619 -1.844 20.859 1.00 39.93 O ANISOU 1072 O HOH A 140 5225 5069 4878 -547 -6 15 O HETATM 1073 O HOH A 141 18.465 3.834 6.317 1.00 40.87 O ANISOU 1073 O HOH A 141 5184 5262 5081 -116 55 300 O HETATM 1074 O HOH A 142 18.762 -1.145 4.394 1.00 30.89 O ANISOU 1074 O HOH A 142 3921 4031 3786 123 225 221 O HETATM 1075 O HOH A 143 16.583 5.514 7.704 1.00 24.43 O ANISOU 1075 O HOH A 143 3266 3039 2977 -199 -12 -31 O HETATM 1076 O HOH A 144 15.643 8.285 8.048 0.50 28.44 O ANISOU 1076 O HOH A 144 3527 3570 3708 159 -48 -190 O HETATM 1077 O HOH A 145 13.773 -8.628 -7.228 0.50 33.19 O ANISOU 1077 O HOH A 145 4001 4378 4234 -285 72 -77 O HETATM 1078 O HOH A 146 18.759 1.690 -2.456 1.00 45.07 O ANISOU 1078 O HOH A 146 5604 5854 5665 -54 304 -246 O HETATM 1079 O HOH A 147 20.658 3.894 -0.494 1.00 47.16 O ANISOU 1079 O HOH A 147 5948 6113 5856 -120 197 270 O HETATM 1080 O HOH A 148 12.770 5.029 0.741 1.00 29.39 O ANISOU 1080 O HOH A 148 3709 3540 3916 -70 66 -52 O HETATM 1081 O HOH A 149 15.816 0.760 -3.044 1.00 33.67 O ANISOU 1081 O HOH A 149 4031 4628 4133 295 452 -328 O HETATM 1082 O HOH A 150 16.481 -3.662 0.507 1.00 31.91 O ANISOU 1082 O HOH A 150 4170 3994 3960 -79 44 89 O HETATM 1083 O HOH A 151 15.025 -2.371 -2.682 1.00 50.94 O ANISOU 1083 O HOH A 151 6488 6343 6526 -47 498 -58 O HETATM 1084 O HOH A 152 15.743 -8.164 -5.568 1.00 21.08 O ANISOU 1084 O HOH A 152 2576 2882 2549 126 180 96 O HETATM 1085 O HOH A 153 17.483 -3.360 -4.152 1.00 45.35 O ANISOU 1085 O HOH A 153 5878 5854 5501 241 468 -214 O HETATM 1086 O HOH A 154 20.441 -10.249 0.495 1.00 41.40 O ANISOU 1086 O HOH A 154 5147 5657 4924 -219 215 198 O HETATM 1087 O HOH A 155 17.982 -7.573 1.214 1.00 35.37 O ANISOU 1087 O HOH A 155 4517 4510 4413 -225 72 -145 O HETATM 1088 O HOH A 156 15.221 -12.195 6.878 1.00 14.64 O ANISOU 1088 O HOH A 156 2029 1766 1768 -24 2 -35 O HETATM 1089 O HOH A 157 15.137 2.455 -4.873 0.50 62.01 O ANISOU 1089 O HOH A 157 8048 8003 7510 6 177 -223 O HETATM 1090 O HOH A 158 13.933 -15.462 5.498 0.50 37.46 O ANISOU 1090 O HOH A 158 4709 4550 4973 -54 -32 337 O HETATM 1091 O HOH A 159 19.079 -11.339 12.826 1.00 23.82 O ANISOU 1091 O HOH A 159 3144 3015 2893 -165 -10 142 O HETATM 1092 O HOH A 160 22.704 0.738 14.408 1.00 55.37 O ANISOU 1092 O HOH A 160 7088 6838 7110 -19 95 -472 O HETATM 1093 O HOH A 161 25.587 -2.589 14.655 1.00 41.57 O ANISOU 1093 O HOH A 161 5113 5241 5440 78 66 -55 O HETATM 1094 O HOH A 162 24.083 -3.980 7.576 1.00 60.35 O ANISOU 1094 O HOH A 162 7974 7476 7480 -189 177 45 O HETATM 1095 O HOH A 163 21.193 1.961 8.514 1.00 48.74 O ANISOU 1095 O HOH A 163 5813 6837 5868 343 534 -100 O HETATM 1096 O HOH A 164 21.436 -0.113 9.469 1.00 33.82 O ANISOU 1096 O HOH A 164 3861 4700 4288 376 578 -331 O HETATM 1097 O HOH A 165 19.551 1.610 6.749 1.00 39.65 O ANISOU 1097 O HOH A 165 4787 5325 4954 -169 225 -82 O HETATM 1098 O HOH A 166 19.785 -2.230 21.411 1.00 50.96 O ANISOU 1098 O HOH A 166 6668 6638 6057 197 452 -339 O HETATM 1099 O HOH A 167 18.309 -4.907 21.351 1.00 43.58 O ANISOU 1099 O HOH A 167 5605 5628 5323 -102 249 139 O HETATM 1100 O HOH A 168 15.257 -4.617 20.969 1.00 44.93 O ANISOU 1100 O HOH A 168 5739 5874 5458 35 104 114 O HETATM 1101 O HOH A 169 22.478 -11.619 18.636 1.00 33.58 O ANISOU 1101 O HOH A 169 4277 4300 4181 306 14 -297 O HETATM 1102 O HOH A 170 21.847 -6.933 17.094 1.00 22.00 O ANISOU 1102 O HOH A 170 2894 2666 2800 -94 -26 57 O HETATM 1103 O HOH A 171 20.791 -11.590 15.230 1.00 30.59 O ANISOU 1103 O HOH A 171 3874 3951 3797 -147 140 -64 O HETATM 1104 O HOH A 172 17.902 -7.034 22.085 1.00 27.26 O ANISOU 1104 O HOH A 172 3529 3217 3612 93 -195 97 O HETATM 1105 O HOH A 173 23.527 -6.313 27.559 0.50 41.24 O ANISOU 1105 O HOH A 173 4958 5313 5397 440 -98 -53 O HETATM 1106 O HOH A 174 20.492 -3.582 27.232 0.50 60.43 O ANISOU 1106 O HOH A 174 8136 7257 7566 230 -554 -517 O HETATM 1107 O HOH A 175 12.089 -12.403 23.152 1.00 58.73 O ANISOU 1107 O HOH A 175 7541 7246 7527 -101 -289 321 O HETATM 1108 O HOH A 176 8.846 -9.520 23.670 1.00 59.26 O ANISOU 1108 O HOH A 176 7917 7244 7354 83 14 -179 O HETATM 1109 O HOH A 177 9.644 -7.003 22.121 1.00 51.92 O ANISOU 1109 O HOH A 177 6458 6573 6695 351 377 -269 O HETATM 1110 O HOH A 178 15.639 -14.590 22.392 1.00 17.22 O ANISOU 1110 O HOH A 178 2312 2067 2164 -76 -50 38 O HETATM 1111 O HOH A 179 8.621 -7.249 19.255 1.00 48.33 O ANISOU 1111 O HOH A 179 6136 6315 5913 122 -386 79 O HETATM 1112 O HOH A 180 6.943 -3.168 15.086 1.00 23.39 O ANISOU 1112 O HOH A 180 2926 3032 2931 268 192 -173 O HETATM 1113 O HOH A 181 5.611 -4.673 13.993 0.50 36.02 O ANISOU 1113 O HOH A 181 4341 5000 4347 -381 735 700 O HETATM 1114 O HOH A 182 9.362 3.354 -0.647 1.00 21.23 O ANISOU 1114 O HOH A 182 2858 2624 2584 -50 12 96 O HETATM 1115 O HOH A 183 10.300 6.437 0.115 0.50 55.34 O ANISOU 1115 O HOH A 183 6822 7279 6927 33 -74 447 O HETATM 1116 O HOH A 184 4.765 4.813 -0.632 1.00 40.81 O ANISOU 1116 O HOH A 184 5495 5285 4725 -174 69 603 O HETATM 1117 O HOH A 185 10.341 14.064 2.509 1.00 40.07 O ANISOU 1117 O HOH A 185 5455 4679 5090 103 19 525 O HETATM 1118 O HOH A 186 13.234 13.584 5.908 1.00 23.86 O ANISOU 1118 O HOH A 186 3005 3026 3034 -143 220 82 O HETATM 1119 O HOH A 187 7.246 16.431 8.910 1.00 33.23 O ANISOU 1119 O HOH A 187 4339 3961 4328 126 42 -191 O HETATM 1120 O HOH A 188 2.859 11.646 5.588 1.00 21.47 O ANISOU 1120 O HOH A 188 2717 2775 2667 165 16 13 O HETATM 1121 O HOH A 189 3.588 14.262 4.470 1.00 57.35 O ANISOU 1121 O HOH A 189 7728 7263 6800 320 -265 533 O HETATM 1122 O AHOH A 190 5.969 14.657 0.861 0.50 38.19 O ANISOU 1122 O AHOH A 190 4781 4979 4748 10 316 71 O HETATM 1123 O BHOH A 190 4.247 13.600 0.376 0.50 49.34 O ANISOU 1123 O BHOH A 190 6704 6042 6000 180 -530 251 O HETATM 1124 O HOH A 191 8.556 9.156 1.700 1.00 17.48 O ANISOU 1124 O HOH A 191 2320 2152 2169 -40 -40 157 O HETATM 1125 O HOH A 192 7.375 12.674 -0.049 0.50 42.31 O ANISOU 1125 O HOH A 192 6004 5159 4911 -114 -190 985 O HETATM 1126 O HOH A 193 9.421 12.843 0.799 0.50 40.13 O ANISOU 1126 O HOH A 193 4987 5165 5094 -133 143 504 O HETATM 1127 O HOH A 194 12.269 11.619 14.621 1.00 31.93 O ANISOU 1127 O HOH A 194 4181 3907 4044 -421 -52 292 O HETATM 1128 O HOH A 195 -1.470 16.552 15.967 1.00 36.96 O ANISOU 1128 O HOH A 195 4663 4779 4599 931 448 -579 O HETATM 1129 O HOH A 196 -2.221 17.262 8.536 0.50 46.50 O ANISOU 1129 O HOH A 196 6095 5899 5674 394 -654 673 O HETATM 1130 O HOH A 197 0.410 15.956 7.930 1.00 37.80 O ANISOU 1130 O HOH A 197 4814 4678 4869 164 45 -39 O HETATM 1131 O HOH A 198 3.390 16.215 12.573 1.00 40.20 O ANISOU 1131 O HOH A 198 5226 4944 5104 224 86 -177 O HETATM 1132 O HOH A 199 -4.376 15.459 14.237 0.50 41.64 O ANISOU 1132 O HOH A 199 5300 5229 5292 501 56 -479 O HETATM 1133 O HOH A 200 0.204 9.843 5.016 1.00 24.13 O ANISOU 1133 O HOH A 200 3110 3074 2985 0 86 32 O HETATM 1134 O HOH A 201 -9.875 11.696 14.671 1.00 45.87 O ANISOU 1134 O HOH A 201 5238 5914 6277 318 5 139 O HETATM 1135 O HOH A 202 -7.789 13.698 13.723 1.00 29.83 O ANISOU 1135 O HOH A 202 3878 3630 3828 258 33 75 O HETATM 1136 O HOH A 203 -10.462 9.192 16.270 0.50 31.23 O ANISOU 1136 O HOH A 203 3598 4205 4062 99 308 215 O HETATM 1137 O HOH A 204 -6.426 12.826 21.606 1.00 48.15 O ANISOU 1137 O HOH A 204 6429 5948 5918 250 146 -312 O HETATM 1138 O HOH A 205 -10.207 5.842 17.960 1.00 22.24 O ANISOU 1138 O HOH A 205 2677 2875 2899 -259 -78 227 O HETATM 1139 O HOH A 206 -6.140 1.863 16.052 1.00 56.46 O ANISOU 1139 O HOH A 206 7330 7175 6946 -445 -161 -408 O HETATM 1140 O AHOH A 207 22.443 0.794 19.697 0.50 30.93 O ANISOU 1140 O AHOH A 207 3176 3693 4883 -163 296 -231 O HETATM 1141 O BHOH A 207 22.753 1.047 18.134 0.50 34.03 O ANISOU 1141 O BHOH A 207 3823 4107 4998 -159 -246 -319 O HETATM 1142 O HOH A 208 -8.429 0.677 21.920 1.00 56.53 O ANISOU 1142 O HOH A 208 6692 7318 7469 203 -231 -446 O HETATM 1143 O AHOH A 209 -6.385 -0.502 27.886 0.50 41.28 O ANISOU 1143 O AHOH A 209 5382 5341 4962 -8 111 41 O HETATM 1144 O BHOH A 209 -7.629 0.246 27.385 0.50 43.36 O ANISOU 1144 O BHOH A 209 5435 5731 5310 75 308 -95 O HETATM 1145 O HOH A 210 -0.815 -0.222 28.282 1.00 37.39 O ANISOU 1145 O HOH A 210 4894 4577 4735 -73 -101 221 O HETATM 1146 O HOH A 211 -9.343 4.622 25.451 1.00 21.00 O ANISOU 1146 O HOH A 211 2551 2737 2690 77 44 34 O HETATM 1147 O HOH A 212 -3.000 13.425 22.042 1.00 52.84 O ANISOU 1147 O HOH A 212 6808 6513 6757 686 100 -406 O HETATM 1148 O AHOH A 213 -3.000 16.194 18.824 0.50 46.02 O ANISOU 1148 O AHOH A 213 5776 5980 5729 -295 108 -185 O HETATM 1149 O BHOH A 213 -4.648 14.876 18.941 0.50 42.14 O ANISOU 1149 O BHOH A 213 5103 5431 5476 155 345 -188 O HETATM 1150 O HOH A 214 -7.794 1.928 11.700 1.00 40.26 O ANISOU 1150 O HOH A 214 4577 5408 5312 -239 293 -92 O HETATM 1151 O HOH A 215 -7.120 7.530 7.292 0.50 63.92 O ANISOU 1151 O HOH A 215 8523 8052 7714 -696 -406 376 O HETATM 1152 O HOH A 216 -5.490 5.953 1.444 1.00 53.41 O ANISOU 1152 O HOH A 216 6709 6718 6865 -264 -549 510 O HETATM 1153 O HOH A 217 -7.207 7.956 4.065 0.50 63.89 O ANISOU 1153 O HOH A 217 8071 7910 8296 -56 -207 136 O HETATM 1154 O HOH A 218 -4.723 16.479 9.282 0.50 33.35 O ANISOU 1154 O HOH A 218 4223 4191 4256 387 -197 138 O HETATM 1155 O HOH A 219 -8.219 13.683 10.425 1.00 45.53 O ANISOU 1155 O HOH A 219 5643 5862 5794 22 98 363 O HETATM 1156 O HOH A 220 2.779 10.129 3.019 1.00 54.50 O ANISOU 1156 O HOH A 220 6923 6713 7073 -519 -355 -130 O HETATM 1157 O HOH A 221 1.116 6.402 -0.879 0.50 37.76 O ANISOU 1157 O HOH A 221 4857 4837 4655 180 83 98 O HETATM 1158 O HOH A 222 -2.666 5.614 -0.166 1.00 45.55 O ANISOU 1158 O HOH A 222 5874 5663 5769 505 -127 -83 O HETATM 1159 O HOH A 223 3.511 6.904 0.791 0.50 46.78 O ANISOU 1159 O HOH A 223 6030 6034 5709 -11 -448 310 O HETATM 1160 O HOH A 224 7.115 -11.392 7.985 1.00 20.29 O ANISOU 1160 O HOH A 224 2651 2490 2569 -150 -33 18 O HETATM 1161 O HOH A 225 3.207 -3.914 10.583 1.00 34.04 O ANISOU 1161 O HOH A 225 4248 4454 4231 45 25 -135 O HETATM 1162 O HOH A 226 7.416 -16.139 15.748 1.00 41.49 O ANISOU 1162 O HOH A 226 4796 5556 5411 -263 535 -139 O HETATM 1163 O HOH A 227 8.725 -15.481 18.284 1.00 27.94 O ANISOU 1163 O HOH A 227 3490 3568 3556 -54 195 107 O HETATM 1164 O HOH A 228 11.750 -14.154 20.875 1.00 37.84 O ANISOU 1164 O HOH A 228 5077 4788 4512 -28 183 -55 O HETATM 1165 O HOH A 229 13.856 -17.521 19.678 1.00 27.78 O ANISOU 1165 O HOH A 229 3549 3594 3412 -239 -10 171 O HETATM 1166 O HOH A 230 9.194 -21.127 10.754 1.00 32.37 O ANISOU 1166 O HOH A 230 4215 4010 4073 -216 -248 30 O HETATM 1167 O HOH A 231 13.220 -24.914 16.527 1.00 38.23 O ANISOU 1167 O HOH A 231 4978 4813 4734 -159 -18 157 O HETATM 1168 O HOH A 232 13.610 -21.876 17.488 1.00 46.94 O ANISOU 1168 O HOH A 232 6144 5890 5802 -665 -123 99 O HETATM 1169 O HOH A 233 17.531 -23.656 15.454 1.00 55.90 O ANISOU 1169 O HOH A 233 7407 6642 7192 308 -538 -66 O HETATM 1170 O HOH A 234 18.933 -19.617 13.783 1.00 41.95 O ANISOU 1170 O HOH A 234 5171 5100 5669 198 209 -509 O HETATM 1171 O HOH A 235 14.698 -19.197 9.404 1.00 30.70 O ANISOU 1171 O HOH A 235 3927 3984 3756 -27 188 -297 O HETATM 1172 O HOH A 236 12.467 -22.023 9.923 1.00 44.80 O ANISOU 1172 O HOH A 236 5546 5607 5871 -510 -299 315 O HETATM 1173 O HOH A 237 17.735 -20.020 10.537 1.00 57.26 O ANISOU 1173 O HOH A 237 7148 6743 7866 86 17 -23 O HETATM 1174 O AHOH A 238 14.777 -23.418 8.423 0.50 36.91 O ANISOU 1174 O AHOH A 238 4691 4779 4554 -199 253 -199 O HETATM 1175 O BHOH A 238 16.529 -23.877 9.235 0.50 56.09 O ANISOU 1175 O BHOH A 238 7430 6783 7099 -273 294 30 O HETATM 1176 O HOH A 239 22.106 -20.218 18.762 0.50 40.74 O ANISOU 1176 O HOH A 239 5308 4869 5301 329 112 -382 O HETATM 1177 O HOH A 240 18.782 12.471 19.984 1.00 38.01 O ANISOU 1177 O HOH A 240 5050 4582 4809 9 -35 100 O HETATM 1178 O HOH A 241 16.030 -17.301 21.287 1.00 22.42 O ANISOU 1178 O HOH A 241 2834 2896 2791 -78 5 31 O HETATM 1179 O HOH A 242 19.519 -19.595 22.979 1.00 26.15 O ANISOU 1179 O HOH A 242 3478 3270 3188 -110 -50 15 O HETATM 1180 O HOH A 243 22.954 -20.599 21.083 1.00 50.47 O ANISOU 1180 O HOH A 243 6102 6416 6657 530 105 340 O HETATM 1181 O HOH A 244 15.416 -16.394 7.935 1.00 30.81 O ANISOU 1181 O HOH A 244 3853 3966 3886 49 111 -133 O HETATM 1182 O HOH A 245 12.324 -14.156 4.534 1.00 20.28 O ANISOU 1182 O HOH A 245 2734 2478 2492 116 111 -129 O HETATM 1183 O HOH A 246 11.060 -13.394 2.254 0.50 42.07 O ANISOU 1183 O HOH A 246 5155 5475 5353 46 -100 -603 O HETATM 1184 O HOH A 247 8.740 -14.148 2.813 0.50 50.97 O ANISOU 1184 O HOH A 247 6852 6239 6275 -16 -256 1 O HETATM 1185 O HOH A 248 6.846 -10.275 0.609 1.00 38.08 O ANISOU 1185 O HOH A 248 5399 4530 4539 437 -285 -407 O HETATM 1186 O HOH A 249 3.298 -9.909 0.218 1.00 57.13 O ANISOU 1186 O HOH A 249 7651 7124 6931 -57 -311 -523 O HETATM 1187 O HOH A 250 1.884 -8.488 1.816 1.00 53.49 O ANISOU 1187 O HOH A 250 6116 6879 7330 -526 -335 -77 O HETATM 1188 O HOH A 251 0.209 -4.945 1.148 1.00 36.88 O ANISOU 1188 O HOH A 251 4519 4564 4930 -403 -178 -218 O HETATM 1189 O HOH A 252 6.091 -2.838 -1.897 0.50 43.76 O ANISOU 1189 O HOH A 252 5433 5699 5496 -548 -630 242 O HETATM 1190 O HOH A 253 2.569 3.492 -0.562 0.50 29.77 O ANISOU 1190 O HOH A 253 3812 4031 3468 52 -205 -205 O HETATM 1191 O HOH A 254 -4.744 -3.324 4.186 0.50 41.04 O ANISOU 1191 O HOH A 254 5035 5263 5297 -255 -276 -36 O HETATM 1192 O HOH A 255 1.373 12.287 24.015 1.00 45.74 O ANISOU 1192 O HOH A 255 5946 5655 5779 14 -178 -62 O HETATM 1193 O HOH A 256 9.715 12.925 21.870 1.00 28.75 O ANISOU 1193 O HOH A 256 3610 3591 3722 111 -21 -73 O HETATM 1194 O HOH A 257 9.051 11.435 24.871 1.00 54.21 O ANISOU 1194 O HOH A 257 6625 6998 6977 -711 -195 -36 O HETATM 1195 O HOH A 258 3.270 6.875 23.986 1.00 30.03 O ANISOU 1195 O HOH A 258 3583 4027 3799 56 -54 0 O HETATM 1196 O HOH A 259 4.117 14.773 25.066 1.00 37.49 O ANISOU 1196 O HOH A 259 4857 4741 4644 312 322 -132 O HETATM 1197 O HOH A 260 3.603 19.067 21.694 0.50 35.25 O ANISOU 1197 O HOH A 260 4660 4304 4430 585 48 -211 O HETATM 1198 O HOH A 261 10.386 16.581 23.815 1.00 50.16 O ANISOU 1198 O HOH A 261 6066 6560 6431 -535 -135 -158 O HETATM 1199 O HOH A 262 12.387 20.667 22.191 1.00 50.07 O ANISOU 1199 O HOH A 262 6367 6679 5976 -659 176 945 O HETATM 1200 O HOH A 263 9.330 24.734 22.632 0.50 45.27 O ANISOU 1200 O HOH A 263 5802 5700 5699 -73 88 671 O HETATM 1201 O HOH A 264 10.689 15.685 20.889 1.00 33.02 O ANISOU 1201 O HOH A 264 4223 4233 4088 -257 -198 41 O HETATM 1202 O HOH A 265 5.788 19.741 16.812 1.00 37.32 O ANISOU 1202 O HOH A 265 4596 4493 5090 -241 -199 199 O HETATM 1203 O HOH A 266 6.467 15.326 13.859 1.00 41.19 O ANISOU 1203 O HOH A 266 4955 5517 5178 -271 280 42 O HETATM 1204 O HOH A 267 4.787 17.294 14.456 1.00 48.50 O ANISOU 1204 O HOH A 267 6708 5574 6145 -132 -350 90 O HETATM 1205 O HOH A 268 -0.642 13.473 23.170 1.00 60.76 O ANISOU 1205 O HOH A 268 8012 7411 7664 -214 5 96 O HETATM 1206 O HOH A 269 11.073 9.657 15.813 1.00 18.53 O ANISOU 1206 O HOH A 269 2293 2419 2328 -100 69 16 O HETATM 1207 O HOH A 270 10.950 4.729 21.088 1.00 25.97 O ANISOU 1207 O HOH A 270 3075 3442 3351 -57 29 218 O HETATM 1208 O HOH A 271 8.182 6.570 25.042 1.00 56.16 O ANISOU 1208 O HOH A 271 7361 6875 7100 -399 251 196 O HETATM 1209 O HOH A 272 6.364 -1.645 18.037 0.50 28.52 O ANISOU 1209 O HOH A 272 3626 3385 3825 301 -148 366 O HETATM 1210 O HOH A 273 -0.738 0.318 22.031 1.00 21.87 O ANISOU 1210 O HOH A 273 2792 2873 2643 -7 13 70 O HETATM 1211 O HOH A 274 1.058 -2.054 19.437 1.00 47.82 O ANISOU 1211 O HOH A 274 6108 6092 5968 -85 -175 288 O HETATM 1212 O HOH A 275 -4.002 1.292 16.663 1.00 37.44 O ANISOU 1212 O HOH A 275 4649 5128 4447 97 -7 -94 O HETATM 1213 O HOH A 276 1.827 -4.571 12.744 0.50 43.86 O ANISOU 1213 O HOH A 276 5957 5158 5551 -106 47 356 O HETATM 1214 O HOH A 277 -0.434 -4.613 12.591 1.00 44.66 O ANISOU 1214 O HOH A 277 5934 5303 5731 -13 254 258 O HETATM 1215 O HOH A 278 1.579 -5.825 8.132 0.50 34.79 O ANISOU 1215 O HOH A 278 4256 4339 4626 -177 -118 45 O HETATM 1216 O HOH A 279 -4.038 -0.566 4.057 1.00 52.71 O ANISOU 1216 O HOH A 279 6793 6729 6507 143 -141 -64 O HETATM 1217 O HOH A 280 8.034 1.079 18.565 1.00 16.31 O ANISOU 1217 O HOH A 280 2036 2179 1982 180 108 -4 O HETATM 1218 O HOH A 281 10.531 2.695 18.997 1.00 30.13 O ANISOU 1218 O HOH A 281 3868 3857 3721 -160 184 127 O HETATM 1219 O HOH A 282 0.761 2.754 22.703 1.00 35.94 O ANISOU 1219 O HOH A 282 4519 4695 4443 -65 129 -169 O HETATM 1220 O HOH A 283 12.920 -23.375 19.537 1.00 49.10 O ANISOU 1220 O HOH A 283 6233 6013 6409 -375 -143 272 O HETATM 1221 O HOH A 284 20.648 11.858 23.443 1.00 54.84 O ANISOU 1221 O HOH A 284 6859 6974 7003 -12 -693 0 O HETATM 1222 O HOH A 285 -10.854 5.084 13.033 1.00 52.50 O ANISOU 1222 O HOH A 285 6365 6433 7149 -1194 -25 529 O HETATM 1223 O HOH A 286 10.651 9.793 26.334 1.00 52.28 O ANISOU 1223 O HOH A 286 6616 6572 6678 233 17 -539 O HETATM 1224 O HOH A 287 7.160 17.384 12.663 0.50 47.45 O ANISOU 1224 O HOH A 287 6424 5775 5828 59 -539 -316 O HETATM 1225 O HOH A 288 18.867 -3.531 2.074 0.50 35.01 O ANISOU 1225 O HOH A 288 4350 4442 4512 165 -34 115 O HETATM 1226 O HOH A 289 -9.595 8.396 19.553 1.00 36.16 O ANISOU 1226 O HOH A 289 4574 4578 4586 244 97 -189 O HETATM 1227 O HOH A 290 -9.171 2.649 27.797 1.00 52.62 O ANISOU 1227 O HOH A 290 6717 6868 6407 -631 -291 629 O HETATM 1228 O HOH A 291 14.158 13.832 21.564 1.00 54.68 O ANISOU 1228 O HOH A 291 7379 6687 6712 -215 -209 90 O HETATM 1229 O HOH A 292 4.669 8.700 1.863 1.00 61.36 O ANISOU 1229 O HOH A 292 7670 7200 8443 -144 -23 332 O HETATM 1230 O HOH A 293 6.462 14.527 26.867 1.00 58.04 O ANISOU 1230 O HOH A 293 7619 7077 7356 -71 -291 104 O HETATM 1231 O HOH A 294 3.361 2.233 24.111 0.50 48.56 O ANISOU 1231 O HOH A 294 5890 6444 6117 358 187 -211 O HETATM 1232 O HOH A 295 6.932 17.051 2.896 0.50 45.96 O ANISOU 1232 O HOH A 295 5786 6098 5580 -197 439 -24 O HETATM 1233 O AHOH A 296 20.939 -21.647 15.716 0.50 45.80 O ANISOU 1233 O AHOH A 296 5990 5731 5681 160 -89 -223 O HETATM 1234 O BHOH A 296 20.199 -22.158 13.837 0.50 50.16 O ANISOU 1234 O BHOH A 296 6327 6141 6590 417 -217 258 O HETATM 1235 O HOH A 297 9.507 13.676 25.017 1.00 53.78 O ANISOU 1235 O HOH A 297 6795 6685 6953 254 -307 -12 O HETATM 1236 O HOH A 298 -5.242 15.698 16.657 1.00 55.17 O ANISOU 1236 O HOH A 298 7079 6805 7077 164 213 -69 O HETATM 1237 O HOH A 299 6.920 -13.547 16.556 1.00 45.90 O ANISOU 1237 O HOH A 299 5919 5902 5621 -132 -23 14 O HETATM 1238 O HOH A 300 21.776 -0.343 6.220 0.50 38.59 O ANISOU 1238 O HOH A 300 4773 4707 5183 117 63 -420 O HETATM 1239 O HOH A 301 7.074 -6.442 22.702 0.50 38.34 O ANISOU 1239 O HOH A 301 4802 4857 4907 -130 -160 192 O HETATM 1240 O HOH A 302 0.685 15.665 23.844 0.50 41.45 O ANISOU 1240 O HOH A 302 5164 5501 5084 -273 -15 188 O HETATM 1241 O HOH A 303 -3.259 -4.803 13.364 0.50 45.60 O ANISOU 1241 O HOH A 303 5713 5595 6016 778 -181 -213 O HETATM 1242 O HOH A 304 12.153 18.310 24.920 0.50 59.87 O ANISOU 1242 O HOH A 304 7958 7423 7366 267 58 -132 O HETATM 1243 O HOH A 305 25.719 -20.060 18.724 0.50 57.67 O ANISOU 1243 O HOH A 305 7357 7430 7126 128 -52 -105 O HETATM 1244 O HOH A 306 11.021 4.289 24.007 0.50 44.67 O ANISOU 1244 O HOH A 306 5517 5670 5787 33 291 -59 O HETATM 1245 O HOH A 307 18.395 14.085 24.880 1.00 52.52 O ANISOU 1245 O HOH A 307 6790 6522 6645 -224 7 408 O HETATM 1246 O HOH A 308 15.762 -24.202 17.527 0.50 49.93 O ANISOU 1246 O HOH A 308 6326 6291 6353 754 -150 -72 O HETATM 1247 O HOH A 309 7.623 -16.467 10.991 1.00 50.28 O ANISOU 1247 O HOH A 309 6378 6241 6483 185 95 71 O HETATM 1248 O HOH A 310 11.075 -11.302 -0.414 0.50 44.75 O ANISOU 1248 O HOH A 310 5890 5790 5324 192 69 -253 O HETATM 1249 O HOH A 311 20.415 -15.919 11.407 0.50 38.02 O ANISOU 1249 O HOH A 311 4422 5315 4708 -227 538 125 O HETATM 1250 O HOH A 312 14.144 5.095 25.038 0.50 53.48 O ANISOU 1250 O HOH A 312 7030 6814 6476 -311 -119 1027 O HETATM 1251 O HOH A 313 5.169 -9.467 19.971 0.50 50.67 O ANISOU 1251 O HOH A 313 6381 6489 6381 331 350 326 O HETATM 1252 O HOH A 314 18.786 15.473 26.767 0.50 49.25 O ANISOU 1252 O HOH A 314 6389 5890 6435 -114 -329 392 O HETATM 1253 O HOH A 315 -1.518 19.110 23.541 0.50 47.96 O ANISOU 1253 O HOH A 315 6051 5768 6404 -50 -132 290 O HETATM 1254 O HOH A 316 12.076 -2.471 22.066 0.50 53.44 O ANISOU 1254 O HOH A 316 6647 6959 6697 183 18 -39 O HETATM 1255 O HOH A 317 19.330 -6.037 2.322 0.50 36.03 O ANISOU 1255 O HOH A 317 4557 4494 4638 -277 -18 -278 O HETATM 1256 O HOH A 318 -10.099 4.437 10.807 0.50 46.28 O ANISOU 1256 O HOH A 318 6217 5417 5950 -933 -555 413 O HETATM 1257 O HOH A 319 -7.666 -1.451 24.122 0.50 50.78 O ANISOU 1257 O HOH A 319 5861 6865 6570 -462 556 -89 O HETATM 1258 O HOH A 320 -6.236 9.388 2.000 1.00 54.70 O ANISOU 1258 O HOH A 320 7011 6908 6864 497 -226 -168 O HETATM 1259 O HOH A 321 -3.249 -2.479 1.746 1.00 54.10 O ANISOU 1259 O HOH A 321 6131 7270 7155 -331 230 -116 O HETATM 1260 O HOH A 322 4.231 4.829 23.553 0.50 44.21 O ANISOU 1260 O HOH A 322 6155 5468 5173 -75 -400 118 O HETATM 1261 O HOH A 323 3.875 -2.648 17.968 0.50 39.37 O ANISOU 1261 O HOH A 323 5173 4691 5096 -292 -228 278 O HETATM 1262 O HOH A 324 6.046 -7.221 20.454 0.50 45.19 O ANISOU 1262 O HOH A 324 5829 5962 5379 -617 132 -58 O HETATM 1263 O HOH A 325 20.970 -4.581 29.838 0.50 48.02 O ANISOU 1263 O HOH A 325 5861 6342 6043 -467 295 402 O HETATM 1264 O HOH A 326 -1.053 16.469 21.744 0.50 53.61 O ANISOU 1264 O HOH A 326 6911 6856 6602 109 -344 -379 O HETATM 1265 O HOH A 327 15.972 11.744 16.461 0.50 45.61 O ANISOU 1265 O HOH A 327 5946 5750 5632 61 -489 -80 O HETATM 1266 O HOH A 328 10.652 -0.832 25.497 0.50 41.30 O ANISOU 1266 O HOH A 328 5451 5287 4956 -304 -103 -205 O HETATM 1267 O HOH A 329 17.784 10.502 8.919 0.50 50.60 O ANISOU 1267 O HOH A 329 6537 6283 6406 369 -167 -206 O HETATM 1268 O HOH A 330 13.054 -3.788 -4.411 0.50 49.53 O ANISOU 1268 O HOH A 330 6144 6585 6091 357 487 -204 O HETATM 1269 O HOH A 331 8.456 -2.347 18.695 1.00 45.57 O ANISOU 1269 O HOH A 331 5645 5819 5852 559 309 -61 O HETATM 1270 O HOH A 332 9.840 -0.669 21.122 1.00 45.51 O ANISOU 1270 O HOH A 332 5708 6155 5430 -137 403 288 O HETATM 1271 O HOH A 333 6.127 7.456 -0.862 1.00 53.33 O ANISOU 1271 O HOH A 333 7210 6644 6410 -372 -469 164 O HETATM 1272 O HOH A 334 0.686 -5.880 18.302 0.50 55.27 O ANISOU 1272 O HOH A 334 7257 6251 7493 460 -868 -246 O HETATM 1273 O HOH A 335 5.226 -13.622 8.646 0.50 40.31 O ANISOU 1273 O HOH A 335 5171 4830 5316 -159 -231 147 O HETATM 1274 O CHOH A 336 9.367 -4.180 1.609 0.49 12.10 O ANISOU 1274 O CHOH A 336 1522 1616 1459 20 -14 10 O HETATM 1275 O CHOH A 337 7.224 -2.655 0.722 0.49 16.72 O ANISOU 1275 O CHOH A 337 2278 2038 2038 28 39 0 O HETATM 1276 O HOH A 338 7.487 4.487 23.533 0.50 39.62 O ANISOU 1276 O HOH A 338 5309 4859 4887 -110 -79 -175 O HETATM 1277 O HOH A 339 5.683 13.126 -2.062 0.50 44.00 O ANISOU 1277 O HOH A 339 5334 5545 5839 -32 -247 193 O HETATM 1278 O HOH A 340 17.724 -1.569 -2.160 1.00 68.98 O ANISOU 1278 O HOH A 340 8998 8877 8336 508 -753 -219 O HETATM 1279 O HOH A 341 21.623 -15.549 4.897 0.50 42.67 O ANISOU 1279 O HOH A 341 5188 5622 5403 57 103 -167 O HETATM 1280 O HOH A 342 7.345 6.513 -2.792 0.50 45.09 O ANISOU 1280 O HOH A 342 5655 5934 5544 256 126 236 O HETATM 1281 O HOH A 343 26.060 -5.482 11.029 0.50 40.50 O ANISOU 1281 O HOH A 343 5021 5146 5222 350 -247 -122 O HETATM 1282 O HOH A 344 4.853 11.329 0.267 0.50 42.79 O ANISOU 1282 O HOH A 344 5265 5696 5298 221 136 -457 O HETATM 1283 O HOH A 345 -2.807 18.525 10.910 0.50 43.88 O ANISOU 1283 O HOH A 345 5943 5168 5562 336 -528 167 O HETATM 1284 O HOH A 346 1.568 8.886 -1.006 0.50 50.97 O ANISOU 1284 O HOH A 346 6424 6418 6525 93 291 -332 O HETATM 1285 O HOH A 347 23.337 -14.538 13.719 0.50 56.72 O ANISOU 1285 O HOH A 347 6818 7617 7118 -393 646 340 O HETATM 1286 O HOH A 348 5.954 22.503 17.497 0.50 53.05 O ANISOU 1286 O HOH A 348 6987 6583 6586 -457 -326 -125 O HETATM 1287 O HOH A 349 22.872 4.830 1.881 0.50 44.85 O ANISOU 1287 O HOH A 349 5466 5853 5721 -189 132 271 O HETATM 1288 O HOH A 350 5.268 25.278 18.867 0.50 44.83 O ANISOU 1288 O HOH A 350 5522 5839 5673 -15 204 401 O HETATM 1289 O HOH A 351 20.019 9.536 31.973 0.50 40.99 O ANISOU 1289 O HOH A 351 5317 5047 5209 77 -136 -533 O HETATM 1290 O HOH A 352 11.832 7.604 26.888 0.50 56.04 O ANISOU 1290 O HOH A 352 7421 6887 6984 187 -640 336 O HETATM 1291 O HOH A 353 14.425 -1.692 -6.142 0.50 48.09 O ANISOU 1291 O HOH A 353 6019 6061 6191 135 129 95 O CONECT 229 717 CONECT 358 811 CONECT 502 944 CONECT 560 613 CONECT 561 614 CONECT 613 560 CONECT 614 561 CONECT 717 229 CONECT 811 358 CONECT 944 502 MASTER 231 0 0 4 7 0 0 6 1290 1 10 10 END