HEADER HYDROLASE 19-NOV-01 1KF8 TITLE ATOMIC RESOLUTION STRUCTURE OF RNASE A AT PH 8.8 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 1KF8 1 VERSN REVDAT 2 06-MAR-02 1KF8 1 JRNL REVDAT 1 19-DEC-01 1KF8 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 (%) : NULL 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) : NULL 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) : 41615 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)) : 35681 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1049 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 236 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1140.49 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 899.84 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 24 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11411 REMARK 3 NUMBER OF RESTRAINTS : 14195 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.016 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) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-22 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: PLEASE NOTE: CHOH 48 IS ALTERNATIVE REMARK 3 ONLY TO THE A CONFORMER OF LYS 41. REMARK 4 REMARK 4 1KF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-01. REMARK 100 THE RCSB ID CODE IS RCSB014891. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 8.8 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 : 41621 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 (%) : 97.9 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : 0.02700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.0000 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 (%) : 94.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.39000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 7RSA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.74 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL, PH 8.8, 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. = 3.4 DEGREES REMARK 500 ARG A 39 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 CYS A 72 CA - CB - SG ANGL. DEV. = -13.7 DEGREES REMARK 500 ASP A 83 CB - CG - OD2 ANGL. DEV. = -5.7 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 64.57 -103.32 REMARK 500 GLN A 60 -138.73 -102.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 310 DISTANCE = 5.36 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KF2 RELATED DB: PDB REMARK 900 1KF2 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 5.2. REMARK 900 RELATED ID: 1KF3 RELATED DB: PDB REMARK 900 1KF3 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 5.9. REMARK 900 RELATED ID: 1KF4 RELATED DB: PDB REMARK 900 1KF4 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 6.3. REMARK 900 RELATED ID: 1KF5 RELATED DB: PDB REMARK 900 1KF5 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 7.1. REMARK 900 RELATED ID: 1KF7 RELATED DB: PDB REMARK 900 1KF7 IS THE ATOMIC RESOLUTION STRUCTURES OF RNASE AT PH 8.0. DBREF 1KF8 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 *234(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 2.02 SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.00 SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.02 CISPEP 1 TYR A 92 PRO A 93 0 6.53 CISPEP 2 ASN A 113 PRO A 114 0 2.14 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 21.623 8.965 27.233 1.00 60.64 N ANISOU 1 N LYS A 1 7595 9508 5937 -3230 -5088 1242 N ATOM 2 CA LYS A 1 20.844 7.840 26.821 1.00 35.61 C ANISOU 2 CA LYS A 1 3059 8061 2412 -641 -1076 -891 C ATOM 3 C LYS A 1 20.117 8.202 25.534 1.00 26.92 C ANISOU 3 C LYS A 1 2240 6007 1983 -289 -338 -1123 C ATOM 4 O LYS A 1 19.732 9.324 25.264 1.00 31.46 O ANISOU 4 O LYS A 1 2977 5632 3343 -382 -1054 -1733 O ATOM 5 CB LYS A 1 19.845 7.472 27.905 1.00 45.33 C ANISOU 5 CB LYS A 1 5763 9397 2063 151 119 -460 C ATOM 6 CG LYS A 1 20.236 6.220 28.683 1.00 60.56 C ANISOU 6 CG LYS A 1 5762 10102 7146 -1328 -245 2332 C ATOM 7 CD LYS A 1 19.460 5.034 28.118 1.00 81.94 C ANISOU 7 CD LYS A 1 8463 9696 12975 -684 -3431 1376 C ATOM 8 CE LYS A 1 19.650 3.768 28.938 1.00 77.47 C ANISOU 8 CE LYS A 1 7079 7323 15035 2879 -2691 -276 C ATOM 9 NZ LYS A 1 20.920 3.065 28.566 1.00 90.94 N ANISOU 9 NZ LYS A 1 3356 13731 17465 1276 -1130 862 N ATOM 10 N GLU A 2 19.941 7.165 24.749 1.00 23.10 N ANISOU 10 N GLU A 2 1653 5371 1752 -36 -123 -761 N ATOM 11 CA GLU A 2 19.151 7.323 23.524 1.00 20.40 C ANISOU 11 CA GLU A 2 1625 4291 1833 -14 -84 -935 C ATOM 12 C GLU A 2 17.760 7.795 23.841 1.00 20.64 C ANISOU 12 C GLU A 2 1674 4344 1826 22 -314 -1244 C ATOM 13 O GLU A 2 17.063 7.249 24.662 1.00 25.26 O ANISOU 13 O GLU A 2 1772 5528 2297 168 121 -875 O ATOM 14 CB GLU A 2 19.148 5.934 22.903 1.00 21.23 C ANISOU 14 CB GLU A 2 1957 4239 1869 366 -219 -806 C ATOM 15 CG GLU A 2 18.617 5.957 21.505 1.00 19.54 C ANISOU 15 CG GLU A 2 2239 3185 2001 152 -460 -570 C ATOM 16 CD GLU A 2 18.606 4.613 20.840 1.00 18.07 C ANISOU 16 CD GLU A 2 1985 3141 1740 7 -5 -355 C ATOM 17 OE1 GLU A 2 18.366 3.598 21.573 1.00 23.13 O ANISOU 17 OE1 GLU A 2 3628 3320 1840 -465 153 -255 O ATOM 18 OE2 GLU A 2 18.772 4.477 19.635 1.00 18.33 O ANISOU 18 OE2 GLU A 2 2206 3015 1745 -48 -47 -416 O ATOM 19 N THR A 3 17.293 8.795 23.108 1.00 22.58 N ANISOU 19 N THR A 3 1946 4470 2162 229 -762 -1378 N ATOM 20 CA THR A 3 15.935 9.253 23.280 1.00 24.41 C ANISOU 20 CA THR A 3 2138 4637 2499 526 -721 -1728 C ATOM 21 C THR A 3 14.942 8.300 22.635 1.00 20.91 C ANISOU 21 C THR A 3 1781 4227 1939 322 -353 -1230 C ATOM 22 O THR A 3 15.271 7.529 21.750 1.00 19.26 O ANISOU 22 O THR A 3 1720 3817 1779 248 -355 -956 O ATOM 23 CB THR A 3 15.716 10.669 22.686 1.00 28.58 C ANISOU 23 CB THR A 3 3269 3924 3668 567 -1078 -2233 C ATOM 24 OG1 THR A 3 15.859 10.562 21.263 1.00 26.40 O ANISOU 24 OG1 THR A 3 3133 3410 3487 362 -1034 -1388 O ATOM 25 CG2 THR A 3 16.679 11.651 23.341 1.00 36.53 C ANISOU 25 CG2 THR A 3 3948 4881 5051 43 -1540 -2733 C ATOM 26 N ALA A 4 13.689 8.408 23.052 1.00 22.20 N ANISOU 26 N ALA A 4 1954 4572 1910 624 -322 -1160 N ATOM 27 CA ALA A 4 12.654 7.584 22.426 1.00 21.37 C ANISOU 27 CA ALA A 4 1663 4765 1690 306 -145 -717 C ATOM 28 C ALA A 4 12.534 7.881 20.958 1.00 18.48 C ANISOU 28 C ALA A 4 1664 3596 1762 369 -59 -788 C ATOM 29 O ALA A 4 12.299 6.958 20.151 1.00 17.89 O ANISOU 29 O ALA A 4 1837 3267 1695 153 -88 -579 O ATOM 30 CB ALA A 4 11.316 7.842 23.143 1.00 27.93 C ANISOU 30 CB ALA A 4 2030 6726 1856 327 195 -1012 C ATOM 31 N ALA A 5 12.656 9.128 20.553 1.00 19.27 N ANISOU 31 N ALA A 5 1913 3326 2083 464 -391 -1080 N ATOM 32 CA ALA A 5 12.559 9.500 19.145 1.00 18.88 C ANISOU 32 CA ALA A 5 1893 3018 2262 356 -346 -731 C ATOM 33 C ALA A 5 13.708 8.866 18.365 1.00 15.97 C ANISOU 33 C ALA A 5 1735 2326 2007 -96 -246 -557 C ATOM 34 O ALA A 5 13.500 8.398 17.248 1.00 16.39 O ANISOU 34 O ALA A 5 2009 2325 1895 -128 -359 -413 O ATOM 35 CB ALA A 5 12.559 10.991 18.945 1.00 24.43 C ANISOU 35 CB ALA A 5 3100 2894 3288 809 -488 -889 C ATOM 36 N ALA A 6 14.911 8.854 18.918 1.00 16.83 N ANISOU 36 N ALA A 6 1774 2340 2281 -10 -430 -836 N ATOM 37 CA ALA A 6 16.053 8.282 18.207 1.00 15.77 C ANISOU 37 CA ALA A 6 1727 2271 1995 -116 -245 -452 C ATOM 38 C ALA A 6 15.896 6.794 18.123 1.00 13.87 C ANISOU 38 C ALA A 6 1424 2262 1583 -141 -160 -355 C ATOM 39 O ALA A 6 16.259 6.165 17.116 1.00 14.32 O ANISOU 39 O ALA A 6 1628 2260 1551 -165 2 -327 O ATOM 40 CB ALA A 6 17.369 8.659 18.934 1.00 20.80 C ANISOU 40 CB ALA A 6 1736 2818 3347 -395 -490 -722 C ATOM 41 N LYS A 7 15.368 6.169 19.164 1.00 14.57 N ANISOU 41 N LYS A 7 1514 2520 1500 -45 -126 -276 N ATOM 42 CA LYS A 7 15.141 4.726 19.160 1.00 14.35 C ANISOU 42 CA LYS A 7 1525 2476 1450 -47 -99 -95 C ATOM 43 C LYS A 7 14.128 4.365 18.086 1.00 12.91 C ANISOU 43 C LYS A 7 1392 2212 1300 -88 155 -117 C ATOM 44 O LYS A 7 14.280 3.370 17.400 1.00 13.73 O ANISOU 44 O LYS A 7 1696 2132 1390 51 23 -97 O ATOM 45 CB ALYS A 7 14.540 4.402 20.531 0.65 18.67 C ANISOU 45 CB ALYS A 7 2004 3699 1390 -467 -179 236 C ATOM 46 CB BLYS A 7 14.762 4.196 20.541 0.35 15.06 C ANISOU 46 CB BLYS A 7 1599 2778 1346 352 -4 -8 C ATOM 47 CG ALYS A 7 14.294 2.937 20.677 0.65 25.63 C ANISOU 47 CG ALYS A 7 3712 3924 2102 -1072 -171 722 C ATOM 48 CG BLYS A 7 14.338 2.734 20.527 0.35 21.41 C ANISOU 48 CG BLYS A 7 3670 3158 1307 -521 -102 383 C ATOM 49 CD ALYS A 7 15.369 2.034 20.200 0.65 39.37 C ANISOU 49 CD ALYS A 7 5453 4005 5502 108 -807 -991 C ATOM 50 CD BLYS A 7 14.022 2.331 21.982 0.35 31.25 C ANISOU 50 CD BLYS A 7 5005 5125 1744 -304 -205 1693 C ATOM 51 CE ALYS A 7 15.239 0.570 20.562 0.65 54.98 C ANISOU 51 CE ALYS A 7 8870 4565 7454 1178 -4517 1007 C ATOM 52 CE BLYS A 7 13.348 0.961 21.992 0.35 46.79 C ANISOU 52 CE BLYS A 7 7260 7273 3245 -2963 -1142 3249 C ATOM 53 NZ ALYS A 7 14.020 0.100 21.285 0.65 69.36 N ANISOU 53 NZ ALYS A 7 11510 5232 9614 -2900 -5125 2942 N ATOM 54 NZ BLYS A 7 14.394 -0.115 22.047 0.35 74.14 N ANISOU 54 NZ BLYS A 7 9665 4110 14395 -3129 -10242 3661 N ATOM 55 N PHE A 8 13.085 5.175 17.933 1.00 12.83 N ANISOU 55 N PHE A 8 1411 2125 1338 -34 -61 -242 N ATOM 56 CA PHE A 8 12.125 4.921 16.833 1.00 12.50 C ANISOU 56 CA PHE A 8 1357 1998 1397 -114 69 -328 C ATOM 57 C PHE A 8 12.817 4.917 15.498 1.00 11.73 C ANISOU 57 C PHE A 8 1362 1732 1364 -42 -7 -188 C ATOM 58 O PHE A 8 12.559 4.066 14.651 1.00 12.46 O ANISOU 58 O PHE A 8 1500 1843 1393 -107 1 -326 O ATOM 59 CB PHE A 8 11.009 5.972 16.923 1.00 13.69 C ANISOU 59 CB PHE A 8 1574 2105 1524 160 -15 -395 C ATOM 60 CG PHE A 8 9.998 5.840 15.789 1.00 12.82 C ANISOU 60 CG PHE A 8 1402 1941 1526 113 51 -374 C ATOM 61 CD1 PHE A 8 10.174 6.409 14.554 1.00 14.59 C ANISOU 61 CD1 PHE A 8 1512 2426 1607 71 173 -102 C ATOM 62 CD2 PHE A 8 8.845 5.093 16.007 1.00 13.95 C ANISOU 62 CD2 PHE A 8 1387 2201 1713 68 89 -91 C ATOM 63 CE1 PHE A 8 9.299 6.206 13.520 1.00 15.11 C ANISOU 63 CE1 PHE A 8 1626 2585 1529 341 68 -109 C ATOM 64 CE2 PHE A 8 7.950 4.920 14.976 1.00 14.71 C ANISOU 64 CE2 PHE A 8 1586 2078 1924 -18 -193 -219 C ATOM 65 CZ PHE A 8 8.173 5.447 13.764 1.00 15.63 C ANISOU 65 CZ PHE A 8 1692 2488 1760 213 -161 -385 C ATOM 66 N GLU A 9 13.701 5.883 15.250 1.00 12.24 N ANISOU 66 N GLU A 9 1477 1792 1382 -151 50 -256 N ATOM 67 CA GLU A 9 14.403 5.927 13.984 1.00 12.37 C ANISOU 67 CA GLU A 9 1564 1783 1353 -143 -15 -179 C ATOM 68 C GLU A 9 15.251 4.662 13.788 1.00 11.96 C ANISOU 68 C GLU A 9 1412 1808 1323 -170 104 -167 C ATOM 69 O GLU A 9 15.265 4.072 12.724 1.00 12.56 O ANISOU 69 O GLU A 9 1590 1904 1278 -28 107 -131 O ATOM 70 CB AGLU A 9 15.319 7.137 13.837 0.59 13.18 C ANISOU 70 CB AGLU A 9 1898 1790 1319 -232 -130 174 C ATOM 71 CB BGLU A 9 15.183 7.231 13.873 0.41 16.30 C ANISOU 71 CB BGLU A 9 1567 1825 2801 -126 766 -303 C ATOM 72 CG AGLU A 9 14.513 8.420 13.903 0.59 16.19 C ANISOU 72 CG AGLU A 9 2322 1777 2053 -96 -212 227 C ATOM 73 CG BGLU A 9 15.861 7.458 12.567 0.41 16.19 C ANISOU 73 CG BGLU A 9 2052 1762 2338 -123 255 369 C ATOM 74 CD AGLU A 9 15.347 9.645 13.616 0.59 20.16 C ANISOU 74 CD AGLU A 9 2773 1789 3096 -245 -181 248 C ATOM 75 CD BGLU A 9 16.858 8.594 12.462 0.41 20.56 C ANISOU 75 CD BGLU A 9 2362 2288 3163 -567 767 -4 C ATOM 76 OE1AGLU A 9 16.414 9.468 12.957 0.59 22.71 O ANISOU 76 OE1AGLU A 9 1984 2073 4572 -526 -290 200 O ATOM 77 OE1BGLU A 9 17.237 9.218 13.471 0.41 33.26 O ANISOU 77 OE1BGLU A 9 3854 5013 3770 -2595 -226 -137 O ATOM 78 OE2AGLU A 9 14.889 10.737 14.030 0.59 24.05 O ANISOU 78 OE2AGLU A 9 3453 1840 3847 -317 27 -71 O ATOM 79 OE2BGLU A 9 17.309 8.818 11.325 0.41 28.72 O ANISOU 79 OE2BGLU A 9 2891 4604 3415 -1610 536 939 O ATOM 80 N ARG A 10 16.001 4.272 14.824 1.00 11.86 N ANISOU 80 N ARG A 10 1431 1751 1323 -119 40 -159 N ATOM 81 CA ARG A 10 16.849 3.107 14.737 1.00 11.80 C ANISOU 81 CA ARG A 10 1416 1809 1257 -149 77 -112 C ATOM 82 C ARG A 10 16.061 1.837 14.530 1.00 10.89 C ANISOU 82 C ARG A 10 1252 1650 1237 -59 80 64 C ATOM 83 O ARG A 10 16.469 0.953 13.773 1.00 12.10 O ANISOU 83 O ARG A 10 1469 1769 1360 -45 167 -28 O ATOM 84 CB ARG A 10 17.696 2.985 16.018 1.00 13.20 C ANISOU 84 CB ARG A 10 1415 2068 1531 -152 -183 -104 C ATOM 85 CG ARG A 10 18.590 1.778 16.064 1.00 13.56 C ANISOU 85 CG ARG A 10 1546 2182 1422 77 -92 -171 C ATOM 86 CD ARG A 10 19.605 1.871 17.194 1.00 15.31 C ANISOU 86 CD ARG A 10 1726 2645 1445 254 -245 -139 C ATOM 87 NE ARG A 10 18.991 1.890 18.500 1.00 16.34 N ANISOU 87 NE ARG A 10 2097 2669 1443 -144 -221 -150 N ATOM 88 CZ ARG A 10 18.690 0.841 19.217 1.00 21.76 C ANISOU 88 CZ ARG A 10 3714 2919 1633 -748 142 -238 C ATOM 89 NH1 ARG A 10 18.763 -0.390 18.743 1.00 25.61 N ANISOU 89 NH1 ARG A 10 5222 2821 1688 -933 105 -247 N ATOM 90 NH2 ARG A 10 18.276 1.019 20.460 1.00 28.47 N ANISOU 90 NH2 ARG A 10 6066 3173 1579 -1171 597 -227 N ATOM 91 N AGLN A 11 14.942 1.692 15.224 0.35 11.42 N ANISOU 91 N AGLN A 11 1429 1811 1100 -125 90 9 N ATOM 92 N BGLN A 11 14.952 1.691 15.224 0.65 11.45 N ANISOU 92 N BGLN A 11 1428 1775 1146 -117 72 -55 N ATOM 93 CA AGLN A 11 14.149 0.490 15.153 0.35 10.63 C ANISOU 93 CA AGLN A 11 1330 1620 1089 -13 168 63 C ATOM 94 CA BGLN A 11 14.193 0.476 15.147 0.65 11.51 C ANISOU 94 CA BGLN A 11 1365 1712 1298 -161 -3 129 C ATOM 95 C AGLN A 11 13.341 0.356 13.873 0.35 11.14 C ANISOU 95 C AGLN A 11 1564 1570 1099 -33 96 -54 C ATOM 96 C BGLN A 11 13.329 0.364 13.905 0.65 11.09 C ANISOU 96 C BGLN A 11 1604 1554 1057 -130 108 10 C ATOM 97 O AGLN A 11 13.094 -0.758 13.443 0.35 12.93 O ANISOU 97 O AGLN A 11 1984 1520 1409 -157 -65 -4 O ATOM 98 O BGLN A 11 13.099 -0.744 13.467 0.65 13.18 O ANISOU 98 O BGLN A 11 2031 1523 1453 -144 -117 -22 O ATOM 99 CB AGLN A 11 13.148 0.425 16.311 0.35 12.19 C ANISOU 99 CB AGLN A 11 1354 2163 1113 42 204 166 C ATOM 100 CB BGLN A 11 13.360 0.310 16.411 0.65 12.15 C ANISOU 100 CB BGLN A 11 1821 1713 1084 -81 -6 232 C ATOM 101 CG AGLN A 11 13.807 0.140 17.640 0.35 15.69 C ANISOU 101 CG AGLN A 11 2327 2628 1005 199 22 89 C ATOM 102 CG BGLN A 11 12.575 -0.991 16.443 0.65 13.12 C ANISOU 102 CG BGLN A 11 1678 1738 1567 -158 241 254 C ATOM 103 CD AGLN A 11 12.816 -0.512 18.606 0.35 25.82 C ANISOU 103 CD AGLN A 11 2830 5418 1564 475 677 1250 C ATOM 104 CD BGLN A 11 11.898 -1.274 17.730 0.65 17.30 C ANISOU 104 CD BGLN A 11 2222 2663 1687 -341 407 422 C ATOM 105 OE1AGLN A 11 13.076 -1.557 19.215 0.35 33.00 O ANISOU 105 OE1AGLN A 11 2485 7173 2882 399 702 3101 O ATOM 106 OE1BGLN A 11 12.095 -0.595 18.722 0.65 25.12 O ANISOU 106 OE1BGLN A 11 3914 4261 1370 -1338 322 212 O ATOM 107 NE2AGLN A 11 11.655 0.128 18.711 0.35 31.80 N ANISOU 107 NE2AGLN A 11 3391 6391 2301 1160 1354 1359 N ATOM 108 NE2BGLN A 11 10.955 -2.227 17.710 0.65 19.54 N ANISOU 108 NE2BGLN A 11 2405 3054 1964 -655 426 656 N ATOM 109 N HIS A 12 12.851 1.484 13.362 1.00 10.57 N ANISOU 109 N HIS A 12 1421 1532 1063 -206 68 43 N ATOM 110 CA HIS A 12 11.790 1.407 12.378 1.00 11.29 C ANISOU 110 CA HIS A 12 1614 1593 1083 -229 -70 14 C ATOM 111 C HIS A 12 12.070 2.067 11.058 1.00 12.16 C ANISOU 111 C HIS A 12 1932 1586 1103 -289 -109 86 C ATOM 112 O HIS A 12 11.329 1.815 10.127 1.00 18.07 O ANISOU 112 O HIS A 12 3254 2262 1349 -1167 -747 411 O ATOM 113 CB HIS A 12 10.474 1.982 12.929 1.00 11.89 C ANISOU 113 CB HIS A 12 1540 1601 1375 -74 -100 37 C ATOM 114 CG HIS A 12 10.012 1.261 14.121 1.00 11.64 C ANISOU 114 CG HIS A 12 1392 1696 1334 -101 33 -24 C ATOM 115 ND1 HIS A 12 9.577 -0.046 14.080 1.00 12.55 N ANISOU 115 ND1 HIS A 12 1655 1715 1400 -66 373 -38 N ATOM 116 CD2 HIS A 12 9.868 1.596 15.408 1.00 12.66 C ANISOU 116 CD2 HIS A 12 1521 1873 1415 -31 -9 -158 C ATOM 117 CE1 HIS A 12 9.243 -0.418 15.316 1.00 13.35 C ANISOU 117 CE1 HIS A 12 1734 1753 1584 17 480 76 C ATOM 118 NE2 HIS A 12 9.387 0.582 16.165 1.00 13.26 N ANISOU 118 NE2 HIS A 12 1668 2000 1369 91 240 -90 N ATOM 119 N MET A 13 13.018 2.986 10.922 1.00 11.56 N ANISOU 119 N MET A 13 1662 1681 1051 -162 103 25 N ATOM 120 CA MET A 13 13.163 3.740 9.678 1.00 11.34 C ANISOU 120 CA MET A 13 1640 1624 1046 -24 90 113 C ATOM 121 C MET A 13 14.206 3.131 8.793 1.00 11.21 C ANISOU 121 C MET A 13 1597 1569 1094 -86 141 123 C ATOM 122 O MET A 13 15.338 2.903 9.220 1.00 14.01 O ANISOU 122 O MET A 13 1655 2347 1319 141 68 183 O ATOM 123 CB MET A 13 13.533 5.193 9.988 1.00 12.76 C ANISOU 123 CB MET A 13 1888 1551 1410 -6 19 37 C ATOM 124 CG MET A 13 12.400 5.983 10.606 1.00 14.26 C ANISOU 124 CG MET A 13 2142 1788 1488 168 31 -158 C ATOM 125 SD MET A 13 10.902 6.094 9.671 1.00 15.50 S ANISOU 125 SD MET A 13 2112 2254 1526 405 48 -77 S ATOM 126 CE MET A 13 11.516 6.678 8.094 1.00 19.25 C ANISOU 126 CE MET A 13 3109 2671 1535 511 120 248 C ATOM 127 N ASP A 14 13.904 2.973 7.523 1.00 11.31 N ANISOU 127 N ASP A 14 1587 1635 1075 -63 183 59 N ATOM 128 CA ASP A 14 14.918 2.653 6.527 1.00 11.68 C ANISOU 128 CA ASP A 14 1684 1605 1149 6 267 118 C ATOM 129 C ASP A 14 14.584 3.392 5.241 1.00 11.75 C ANISOU 129 C ASP A 14 1619 1694 1151 -65 231 128 C ATOM 130 O ASP A 14 14.028 2.859 4.305 1.00 14.24 O ANISOU 130 O ASP A 14 2089 2167 1156 -238 63 75 O ATOM 131 CB ASP A 14 15.071 1.164 6.264 1.00 13.80 C ANISOU 131 CB ASP A 14 2247 1605 1390 38 467 81 C ATOM 132 CG ASP A 14 16.244 0.907 5.322 1.00 14.60 C ANISOU 132 CG ASP A 14 2319 1723 1504 279 476 96 C ATOM 133 OD1 ASP A 14 17.005 1.858 5.022 1.00 15.93 O ANISOU 133 OD1 ASP A 14 2171 2001 1882 67 605 169 O ATOM 134 OD2 ASP A 14 16.352 -0.241 4.855 1.00 17.80 O ANISOU 134 OD2 ASP A 14 3050 1851 1861 313 743 -68 O ATOM 135 N SER A 15 14.997 4.660 5.188 1.00 13.17 N ANISOU 135 N SER A 15 1921 1776 1306 -191 155 280 N ATOM 136 CA SER A 15 14.795 5.525 4.039 1.00 14.42 C ANISOU 136 CA SER A 15 2067 1931 1482 71 274 456 C ATOM 137 C SER A 15 15.763 5.242 2.927 1.00 14.48 C ANISOU 137 C SER A 15 2127 1984 1390 -13 266 385 C ATOM 138 O SER A 15 15.639 5.851 1.864 1.00 18.49 O ANISOU 138 O SER A 15 3253 2304 1469 196 437 532 O ATOM 139 CB ASER A 15 15.000 6.989 4.501 0.64 16.51 C ANISOU 139 CB ASER A 15 2603 1809 1861 210 414 385 C ATOM 140 CB BSER A 15 14.839 7.008 4.421 0.36 17.89 C ANISOU 140 CB BSER A 15 3056 1899 1844 429 491 439 C ATOM 141 OG ASER A 15 14.185 7.313 5.621 0.64 16.70 O ANISOU 141 OG ASER A 15 2325 2101 1919 37 225 67 O ATOM 142 OG BSER A 15 16.145 7.310 4.872 0.36 22.69 O ANISOU 142 OG BSER A 15 3866 2205 2551 -516 -50 82 O ATOM 143 N SER A 16 16.686 4.336 3.105 1.00 15.47 N ANISOU 143 N SER A 16 1943 2402 1532 21 462 485 N ATOM 144 CA SER A 16 17.740 4.034 2.133 1.00 16.45 C ANISOU 144 CA SER A 16 2013 2542 1697 -98 466 309 C ATOM 145 C SER A 16 17.338 3.017 1.088 1.00 16.15 C ANISOU 145 C SER A 16 2203 2306 1628 -43 533 398 C ATOM 146 O SER A 16 18.055 2.850 0.125 1.00 18.84 O ANISOU 146 O SER A 16 2493 2902 1762 64 724 269 O ATOM 147 CB ASER A 16 18.983 3.490 2.845 0.64 18.13 C ANISOU 147 CB ASER A 16 1733 3092 2065 -180 549 437 C ATOM 148 CB BSER A 16 19.084 3.809 2.800 0.36 20.04 C ANISOU 148 CB BSER A 16 1825 3439 2349 -142 439 118 C ATOM 149 OG ASER A 16 18.905 2.090 3.155 0.64 19.07 O ANISOU 149 OG ASER A 16 2070 3171 2003 461 600 613 O ATOM 150 OG BSER A 16 19.498 5.024 3.431 0.36 29.60 O ANISOU 150 OG BSER A 16 2535 5091 3621 -1066 454 -1190 O ATOM 151 N THR A 17 16.205 2.390 1.287 1.00 15.88 N ANISOU 151 N THR A 17 2185 2044 1807 -7 506 298 N ATOM 152 CA THR A 17 15.709 1.441 0.323 1.00 16.26 C ANISOU 152 CA THR A 17 2313 2050 1813 123 510 169 C ATOM 153 C THR A 17 14.222 1.679 0.165 1.00 15.20 C ANISOU 153 C THR A 17 2312 1896 1567 -55 491 216 C ATOM 154 O THR A 17 13.545 2.182 1.044 1.00 17.02 O ANISOU 154 O THR A 17 2167 2711 1591 129 358 -22 O ATOM 155 CB ATHR A 17 15.907 0.014 0.869 0.50 18.17 C ANISOU 155 CB ATHR A 17 2449 2056 2398 183 477 234 C ATOM 156 CB BTHR A 17 15.998 -0.039 0.552 0.50 18.10 C ANISOU 156 CB BTHR A 17 2791 2088 1997 254 332 130 C ATOM 157 OG1ATHR A 17 15.255 -0.155 2.125 0.50 17.19 O ANISOU 157 OG1ATHR A 17 2229 2098 2204 -172 99 543 O ATOM 158 OG1BTHR A 17 15.691 -0.866 -0.605 0.50 21.48 O ANISOU 158 OG1BTHR A 17 3597 2291 2275 -246 645 -211 O ATOM 159 CG2ATHR A 17 17.393 -0.271 1.086 0.50 21.26 C ANISOU 159 CG2ATHR A 17 2511 2651 2916 553 540 335 C ATOM 160 CG2BTHR A 17 15.124 -0.630 1.643 0.50 18.25 C ANISOU 160 CG2BTHR A 17 2771 2113 2051 343 207 508 C ATOM 161 N SER A 18 13.698 1.314 -0.975 1.00 15.99 N ANISOU 161 N SER A 18 2499 1953 1623 74 432 95 N ATOM 162 CA SER A 18 12.303 1.506 -1.255 1.00 15.64 C ANISOU 162 CA SER A 18 2609 1912 1420 142 228 217 C ATOM 163 C SER A 18 11.425 0.355 -0.815 1.00 14.27 C ANISOU 163 C SER A 18 2348 1855 1220 207 169 88 C ATOM 164 O SER A 18 10.209 0.557 -0.641 1.00 15.90 O ANISOU 164 O SER A 18 2411 2109 1520 262 210 136 O ATOM 165 CB ASER A 18 12.079 1.885 -2.712 0.51 26.38 C ANISOU 165 CB ASER A 18 4343 3532 2147 -1375 -813 1436 C ATOM 166 CB BSER A 18 12.083 1.675 -2.767 0.26 21.43 C ANISOU 166 CB BSER A 18 3767 2781 1594 -66 -17 823 C ATOM 167 CB CSER A 18 12.079 1.717 -2.758 0.23 20.98 C ANISOU 167 CB CSER A 18 3569 2816 1588 151 123 814 C ATOM 168 OG ASER A 18 12.884 3.003 -3.081 0.51 24.96 O ANISOU 168 OG ASER A 18 4243 2904 2337 -854 42 1053 O ATOM 169 OG BSER A 18 12.444 0.510 -3.493 0.26 21.25 O ANISOU 169 OG BSER A 18 3082 4012 980 -69 278 165 O ATOM 170 OG CSER A 18 10.755 2.161 -2.996 0.23 29.69 O ANISOU 170 OG CSER A 18 3285 5499 2497 -373 -914 716 O ATOM 171 N ALA A 19 11.967 -0.820 -0.619 1.00 15.05 N ANISOU 171 N ALA A 19 2264 1804 1649 122 284 81 N ATOM 172 CA ALA A 19 11.342 -2.061 -0.225 1.00 15.02 C ANISOU 172 CA ALA A 19 2224 1840 1642 29 158 129 C ATOM 173 C ALA A 19 12.433 -3.060 0.099 1.00 14.77 C ANISOU 173 C ALA A 19 2309 1862 1440 188 234 28 C ATOM 174 O ALA A 19 13.571 -2.881 -0.319 1.00 18.72 O ANISOU 174 O ALA A 19 2475 1995 2644 187 629 371 O ATOM 175 CB ALA A 19 10.448 -2.608 -1.349 1.00 19.00 C ANISOU 175 CB ALA A 19 2685 2286 2247 -55 -430 167 C ATOM 176 N ALA A 20 12.075 -4.103 0.798 1.00 14.64 N ANISOU 176 N ALA A 20 2257 1839 1468 285 289 -39 N ATOM 177 CA ALA A 20 13.026 -5.166 1.081 1.00 14.51 C ANISOU 177 CA ALA A 20 2190 1642 1681 231 287 -86 C ATOM 178 C ALA A 20 13.406 -5.845 -0.244 1.00 16.46 C ANISOU 178 C ALA A 20 2663 1893 1696 365 584 67 C ATOM 179 O ALA A 20 12.587 -6.160 -1.034 1.00 22.14 O ANISOU 179 O ALA A 20 3500 3255 1655 407 284 -445 O ATOM 180 CB ALA A 20 12.453 -6.199 1.980 1.00 16.08 C ANISOU 180 CB ALA A 20 2662 1986 1461 374 314 133 C ATOM 181 N SER A 21 14.679 -6.112 -0.408 1.00 20.24 N ANISOU 181 N SER A 21 2909 2267 2515 693 1164 398 N ATOM 182 CA SER A 21 15.122 -6.634 -1.717 1.00 24.31 C ANISOU 182 CA SER A 21 4112 2531 2595 1317 1663 623 C ATOM 183 C SER A 21 15.445 -8.107 -1.749 1.00 18.20 C ANISOU 183 C SER A 21 2918 2247 1750 582 800 373 C ATOM 184 O SER A 21 15.750 -8.649 -2.803 1.00 21.26 O ANISOU 184 O SER A 21 3512 2888 1678 868 1014 380 O ATOM 185 CB SER A 21 16.378 -5.922 -2.213 1.00 37.63 C ANISOU 185 CB SER A 21 6851 1864 5583 435 4526 129 C ATOM 186 OG SER A 21 17.373 -5.744 -1.204 1.00 61.38 O ANISOU 186 OG SER A 21 5406 7188 10728 -2462 3142 -453 O ATOM 187 N SER A 22 15.426 -8.771 -0.619 1.00 16.53 N ANISOU 187 N SER A 22 2857 1886 1537 390 604 17 N ATOM 188 CA SER A 22 15.691 -10.196 -0.571 1.00 15.61 C ANISOU 188 CA SER A 22 2778 1808 1344 146 502 -93 C ATOM 189 C SER A 22 15.113 -10.769 0.703 1.00 14.81 C ANISOU 189 C SER A 22 2800 1666 1161 178 308 -155 C ATOM 190 O SER A 22 14.790 -10.030 1.649 1.00 14.79 O ANISOU 190 O SER A 22 2445 1839 1335 99 405 -264 O ATOM 191 CB SER A 22 17.163 -10.533 -0.653 1.00 18.23 C ANISOU 191 CB SER A 22 2995 2267 1664 613 569 9 C ATOM 192 OG SER A 22 17.788 -10.378 0.581 1.00 20.54 O ANISOU 192 OG SER A 22 2885 3122 1796 225 374 -57 O ATOM 193 N SER A 23 15.056 -12.083 0.750 1.00 16.04 N ANISOU 193 N SER A 23 3162 1715 1218 -24 429 -300 N ATOM 194 CA SER A 23 14.653 -12.810 1.941 1.00 15.80 C ANISOU 194 CA SER A 23 2880 1799 1323 -132 294 -111 C ATOM 195 C SER A 23 15.514 -12.562 3.149 1.00 14.93 C ANISOU 195 C SER A 23 2802 1581 1291 -125 351 -159 C ATOM 196 O SER A 23 15.032 -12.849 4.242 1.00 18.59 O ANISOU 196 O SER A 23 3361 2427 1275 -464 366 -11 O ATOM 197 CB SER A 23 14.584 -14.328 1.624 1.00 21.27 C ANISOU 197 CB SER A 23 4624 1755 1703 -712 174 -287 C ATOM 198 OG SER A 23 15.852 -14.797 1.326 1.00 29.09 O ANISOU 198 OG SER A 23 5965 2084 3005 692 999 -292 O ATOM 199 N AASN A 24 16.742 -12.084 2.973 0.75 14.64 N ANISOU 199 N AASN A 24 2510 1643 1411 342 389 -247 N ATOM 200 N BASN A 24 16.721 -12.064 2.982 0.25 16.81 N ANISOU 200 N BASN A 24 3080 1846 1459 -440 208 53 N ATOM 201 CA AASN A 24 17.662 -11.808 4.053 0.75 14.55 C ANISOU 201 CA AASN A 24 2439 1560 1529 180 331 -54 C ATOM 202 CA BASN A 24 17.643 -11.852 4.082 0.25 14.91 C ANISOU 202 CA BASN A 24 2421 1733 1512 319 375 -263 C ATOM 203 C AASN A 24 17.563 -10.443 4.638 0.75 14.08 C ANISOU 203 C AASN A 24 2402 1553 1395 101 233 -4 C ATOM 204 C BASN A 24 17.547 -10.457 4.665 0.25 12.79 C ANISOU 204 C BASN A 24 1981 1670 1209 212 628 -127 C ATOM 205 O AASN A 24 18.279 -10.170 5.618 0.75 15.62 O ANISOU 205 O AASN A 24 2443 1996 1496 173 118 -143 O ATOM 206 O BASN A 24 18.285 -10.173 5.618 0.25 15.04 O ANISOU 206 O BASN A 24 2288 1875 1552 771 233 -472 O ATOM 207 CB AASN A 24 19.090 -12.100 3.653 0.75 21.24 C ANISOU 207 CB AASN A 24 2545 2595 2929 741 222 -424 C ATOM 208 CB BASN A 24 19.062 -12.084 3.583 0.25 14.80 C ANISOU 208 CB BASN A 24 2805 1506 1313 296 854 -250 C ATOM 209 CG AASN A 24 19.348 -13.597 3.509 0.75 29.37 C ANISOU 209 CG AASN A 24 3066 2961 5134 1311 -1003 -1748 C ATOM 210 CG BASN A 24 19.848 -12.937 4.562 0.25 25.09 C ANISOU 210 CG BASN A 24 3079 4169 2284 1961 1629 939 C ATOM 211 OD1AASN A 24 19.986 -13.913 2.528 0.75 42.13 O ANISOU 211 OD1AASN A 24 3962 5273 6772 1281 -324 -3839 O ATOM 212 OD1BASN A 24 19.258 -13.599 5.404 0.25 27.17 O ANISOU 212 OD1BASN A 24 3851 4079 2395 2613 1921 1422 O ATOM 213 ND2AASN A 24 19.024 -14.398 4.496 0.75 41.10 N ANISOU 213 ND2AASN A 24 6176 1806 7634 1410 -686 -582 N ATOM 214 ND2BASN A 24 21.166 -12.962 4.400 0.25 46.91 N ANISOU 214 ND2BASN A 24 3086 12132 2607 2496 1603 2843 N ATOM 215 N TYR A 25 16.700 -9.585 4.135 1.00 13.47 N ANISOU 215 N TYR A 25 2237 1602 1279 82 239 -161 N ATOM 216 CA TYR A 25 16.606 -8.203 4.610 1.00 12.34 C ANISOU 216 CA TYR A 25 1917 1496 1275 -2 281 -86 C ATOM 217 C TYR A 25 16.422 -8.144 6.117 1.00 11.84 C ANISOU 217 C TYR A 25 1805 1429 1264 21 165 -91 C ATOM 218 O TYR A 25 17.151 -7.447 6.799 1.00 12.94 O ANISOU 218 O TYR A 25 1868 1684 1363 -126 218 -64 O ATOM 219 CB TYR A 25 15.487 -7.468 3.864 1.00 14.06 C ANISOU 219 CB TYR A 25 2448 1558 1335 73 62 -31 C ATOM 220 CG TYR A 25 15.298 -6.042 4.353 1.00 13.09 C ANISOU 220 CG TYR A 25 2040 1660 1273 114 53 -106 C ATOM 221 CD1 TYR A 25 16.026 -4.996 3.823 1.00 14.62 C ANISOU 221 CD1 TYR A 25 2513 1654 1389 104 384 36 C ATOM 222 CD2 TYR A 25 14.419 -5.712 5.362 1.00 14.00 C ANISOU 222 CD2 TYR A 25 1966 1709 1642 139 307 -8 C ATOM 223 CE1 TYR A 25 15.857 -3.705 4.286 1.00 14.79 C ANISOU 223 CE1 TYR A 25 2561 1712 1347 -66 232 38 C ATOM 224 CE2 TYR A 25 14.256 -4.455 5.836 1.00 14.71 C ANISOU 224 CE2 TYR A 25 2079 1741 1769 166 336 -103 C ATOM 225 CZ TYR A 25 14.994 -3.428 5.295 1.00 14.11 C ANISOU 225 CZ TYR A 25 2300 1656 1407 207 66 -53 C ATOM 226 OH TYR A 25 14.831 -2.168 5.816 1.00 15.65 O ANISOU 226 OH TYR A 25 2452 1650 1846 246 146 -90 O ATOM 227 N CYS A 26 15.415 -8.824 6.651 1.00 12.08 N ANISOU 227 N CYS A 26 1816 1594 1179 -81 198 -129 N ATOM 228 CA CYS A 26 15.168 -8.722 8.063 1.00 11.84 C ANISOU 228 CA CYS A 26 1743 1549 1206 -7 165 -143 C ATOM 229 C CYS A 26 16.349 -9.260 8.889 1.00 11.83 C ANISOU 229 C CYS A 26 1687 1656 1152 -81 223 -56 C ATOM 230 O CYS A 26 16.719 -8.662 9.888 1.00 13.24 O ANISOU 230 O CYS A 26 1854 1917 1261 -57 127 -161 O ATOM 231 CB CYS A 26 13.878 -9.457 8.445 1.00 12.15 C ANISOU 231 CB CYS A 26 1711 1690 1217 -53 120 -30 C ATOM 232 SG CYS A 26 12.384 -8.615 7.904 1.00 12.66 S ANISOU 232 SG CYS A 26 1787 1755 1270 -18 94 -31 S ATOM 233 N ASN A 27 16.905 -10.393 8.490 1.00 12.55 N ANISOU 233 N ASN A 27 1873 1629 1267 81 121 -32 N ATOM 234 CA ASN A 27 18.030 -10.921 9.239 1.00 13.18 C ANISOU 234 CA ASN A 27 1807 1844 1358 98 194 23 C ATOM 235 C ASN A 27 19.159 -9.891 9.351 1.00 13.85 C ANISOU 235 C ASN A 27 1798 1930 1534 114 180 21 C ATOM 236 O ASN A 27 19.744 -9.703 10.405 1.00 16.39 O ANISOU 236 O ASN A 27 1963 2534 1730 -76 -31 104 O ATOM 237 CB ASN A 27 18.571 -12.169 8.588 1.00 14.41 C ANISOU 237 CB ASN A 27 1958 1825 1692 268 183 78 C ATOM 238 CG ASN A 27 17.649 -13.363 8.774 1.00 15.65 C ANISOU 238 CG ASN A 27 2259 1810 1876 163 396 13 C ATOM 239 OD1 ASN A 27 16.848 -13.387 9.669 1.00 17.32 O ANISOU 239 OD1 ASN A 27 2604 2057 1920 -175 410 145 O ATOM 240 ND2 ASN A 27 17.746 -14.383 7.915 1.00 22.17 N ANISOU 240 ND2 ASN A 27 3445 1775 3204 93 756 -535 N ATOM 241 N GLN A 28 19.446 -9.249 8.223 1.00 13.32 N ANISOU 241 N GLN A 28 1786 1755 1521 38 270 -41 N ATOM 242 CA GLN A 28 20.554 -8.294 8.207 1.00 14.79 C ANISOU 242 CA GLN A 28 1731 2034 1857 20 432 -84 C ATOM 243 C GLN A 28 20.211 -7.019 8.987 1.00 13.47 C ANISOU 243 C GLN A 28 1593 1795 1729 -73 256 66 C ATOM 244 O GLN A 28 21.061 -6.529 9.747 1.00 15.47 O ANISOU 244 O GLN A 28 1588 2159 2133 -24 35 -149 O ATOM 245 CB AGLN A 28 20.849 -7.881 6.773 0.60 17.50 C ANISOU 245 CB AGLN A 28 2353 2199 2096 -98 935 2 C ATOM 246 CB BGLN A 28 20.922 -7.994 6.758 0.40 18.61 C ANISOU 246 CB BGLN A 28 2363 2660 2047 -648 886 -281 C ATOM 247 CG AGLN A 28 21.352 -9.008 5.928 0.60 23.74 C ANISOU 247 CG AGLN A 28 2890 3265 2863 -423 1280 -1107 C ATOM 248 CG BGLN A 28 22.110 -7.045 6.770 0.40 26.09 C ANISOU 248 CG BGLN A 28 2421 4948 2545 -1629 1072 -672 C ATOM 249 CD AGLN A 28 21.599 -8.692 4.484 0.60 39.30 C ANISOU 249 CD AGLN A 28 8228 3577 3128 -955 2757 -1087 C ATOM 250 CD BGLN A 28 23.333 -7.788 7.291 0.40 41.92 C ANISOU 250 CD BGLN A 28 1957 8424 5548 -275 1185 -873 C ATOM 251 OE1AGLN A 28 22.142 -9.530 3.768 0.60 55.46 O ANISOU 251 OE1AGLN A 28 10600 6526 3946 1867 3857 -813 O ATOM 252 OE1BGLN A 28 23.534 -8.983 7.092 0.40 58.68 O ANISOU 252 OE1BGLN A 28 5358 10785 6153 3957 1441 -2985 O ATOM 253 NE2AGLN A 28 21.212 -7.521 4.013 0.60 52.84 N ANISOU 253 NE2AGLN A 28 11884 4533 3660 169 3562 5 N ATOM 254 NE2BGLN A 28 24.117 -6.983 7.986 0.40 67.57 N ANISOU 254 NE2BGLN A 28 2918 11187 11570 -2164 -2388 -542 N ATOM 255 N MET A 29 19.001 -6.485 8.830 1.00 12.60 N ANISOU 255 N MET A 29 1504 1803 1482 -108 183 -41 N ATOM 256 CA MET A 29 18.645 -5.242 9.460 1.00 12.66 C ANISOU 256 CA MET A 29 1605 1747 1457 -92 234 -2 C ATOM 257 C MET A 29 18.431 -5.385 10.952 1.00 12.29 C ANISOU 257 C MET A 29 1670 1533 1467 -79 112 40 C ATOM 258 O MET A 29 18.773 -4.490 11.716 1.00 14.12 O ANISOU 258 O MET A 29 2074 1659 1630 -217 -7 -123 O ATOM 259 CB MET A 29 17.393 -4.674 8.790 1.00 13.71 C ANISOU 259 CB MET A 29 1835 1782 1592 13 -50 5 C ATOM 260 CG MET A 29 17.600 -4.183 7.428 1.00 17.58 C ANISOU 260 CG MET A 29 2954 2134 1594 12 -21 34 C ATOM 261 SD MET A 29 18.718 -2.795 7.296 1.00 23.40 S ANISOU 261 SD MET A 29 3897 2600 2393 -653 124 736 S ATOM 262 CE MET A 29 17.757 -1.551 8.141 1.00 33.54 C ANISOU 262 CE MET A 29 8017 2530 2197 -1115 1092 -736 C ATOM 263 N MET A 30 17.825 -6.479 11.381 1.00 12.17 N ANISOU 263 N MET A 30 1663 1601 1359 -118 135 31 N ATOM 264 CA MET A 30 17.610 -6.661 12.803 1.00 12.57 C ANISOU 264 CA MET A 30 1832 1646 1297 19 87 64 C ATOM 265 C MET A 30 18.954 -6.705 13.523 1.00 13.47 C ANISOU 265 C MET A 30 1812 1790 1517 -104 14 129 C ATOM 266 O MET A 30 19.087 -6.200 14.637 1.00 16.17 O ANISOU 266 O MET A 30 2189 2368 1589 -130 -132 -191 O ATOM 267 CB MET A 30 16.781 -7.926 13.059 1.00 12.80 C ANISOU 267 CB MET A 30 1834 1621 1410 -33 141 -2 C ATOM 268 CG MET A 30 15.372 -7.861 12.541 1.00 13.31 C ANISOU 268 CG MET A 30 1845 1769 1443 -7 141 -35 C ATOM 269 SD MET A 30 14.334 -6.655 13.361 1.00 14.42 S ANISOU 269 SD MET A 30 2003 1877 1597 180 318 114 S ATOM 270 CE MET A 30 14.048 -7.443 14.933 1.00 17.74 C ANISOU 270 CE MET A 30 2798 2233 1709 265 770 186 C ATOM 271 N LYS A 31 19.930 -7.349 12.905 1.00 14.21 N ANISOU 271 N LYS A 31 1758 1988 1652 -29 -34 136 N ATOM 272 CA LYS A 31 21.260 -7.419 13.492 1.00 15.96 C ANISOU 272 CA LYS A 31 1871 2144 2049 70 -221 152 C ATOM 273 C LYS A 31 21.948 -6.084 13.438 1.00 15.76 C ANISOU 273 C LYS A 31 1684 2289 2016 -2 -207 139 C ATOM 274 O LYS A 31 22.466 -5.585 14.451 1.00 17.77 O ANISOU 274 O LYS A 31 2091 2585 2077 -119 -395 70 O ATOM 275 CB LYS A 31 22.070 -8.474 12.768 1.00 18.55 C ANISOU 275 CB LYS A 31 1967 2544 2536 330 -248 -147 C ATOM 276 CG LYS A 31 23.469 -8.657 13.412 1.00 24.99 C ATOM 277 CD LYS A 31 23.954 -10.017 12.964 1.00 42.72 C ATOM 278 CE LYS A 31 25.365 -10.396 13.430 1.00 66.21 C ATOM 279 NZ LYS A 31 25.941 -11.425 12.470 1.00 86.83 N ATOM 280 N SER A 32 21.952 -5.407 12.267 1.00 15.64 N ANISOU 280 N SER A 32 1782 2275 1887 -170 -37 56 N ATOM 281 CA SER A 32 22.697 -4.165 12.082 1.00 17.43 C ANISOU 281 CA SER A 32 1776 2556 2291 -238 208 219 C ATOM 282 C SER A 32 22.171 -3.014 12.909 1.00 16.73 C ANISOU 282 C SER A 32 1836 2322 2198 -484 -208 142 C ATOM 283 O SER A 32 22.935 -2.124 13.292 1.00 20.89 O ANISOU 283 O SER A 32 2250 2808 2880 -870 13 -104 O ATOM 284 CB ASER A 32 22.510 -3.792 10.586 0.35 21.41 C ANISOU 284 CB ASER A 32 2614 3299 2220 -371 879 427 C ATOM 285 CB BSER A 32 22.931 -3.822 10.618 0.56 20.10 C ANISOU 285 CB BSER A 32 2753 2636 2250 -602 66 224 C ATOM 286 CB CSER A 32 22.644 -3.790 10.590 0.09 21.99 C ANISOU 286 CB CSER A 32 3207 2931 2217 -1135 323 132 C ATOM 287 OG ASER A 32 23.371 -4.619 9.812 0.35 25.00 O ANISOU 287 OG ASER A 32 3577 2995 2927 -959 1468 -329 O ATOM 288 OG BSER A 32 21.706 -3.364 10.097 0.56 23.49 O ANISOU 288 OG BSER A 32 2742 3663 2521 -802 -215 758 O ATOM 289 OG CSER A 32 23.481 -2.671 10.358 0.09 25.17 O ANISOU 289 OG CSER A 32 5682 1715 2166 -1386 1103 -702 O ATOM 290 N ARG A 33 20.879 -2.990 13.204 1.00 14.34 N ANISOU 290 N ARG A 33 1871 1857 1722 -326 -173 101 N ATOM 291 CA ARG A 33 20.284 -1.933 14.027 1.00 14.62 C ANISOU 291 CA ARG A 33 2170 1760 1625 -274 -306 150 C ATOM 292 C ARG A 33 20.346 -2.283 15.513 1.00 15.65 C ANISOU 292 C ARG A 33 2511 1771 1664 -335 -378 140 C ATOM 293 O ARG A 33 19.801 -1.539 16.312 1.00 18.41 O ANISOU 293 O ARG A 33 3273 1989 1735 -212 -372 -81 O ATOM 294 CB ARG A 33 18.857 -1.706 13.581 1.00 14.50 C ANISOU 294 CB ARG A 33 2075 1772 1663 -207 -112 163 C ATOM 295 CG ARG A 33 18.712 -1.110 12.197 1.00 13.94 C ANISOU 295 CG ARG A 33 1853 1879 1565 74 34 115 C ATOM 296 CD ARG A 33 19.323 0.245 12.050 1.00 14.08 C ANISOU 296 CD ARG A 33 1599 1968 1784 -169 -29 313 C ATOM 297 NE ARG A 33 19.167 0.824 10.722 1.00 14.40 N ANISOU 297 NE ARG A 33 1556 2266 1648 136 278 301 N ATOM 298 CZ ARG A 33 18.081 1.429 10.301 1.00 13.08 C ANISOU 298 CZ ARG A 33 1515 2024 1432 -3 263 195 C ATOM 299 NH1 ARG A 33 17.053 1.653 11.094 1.00 13.82 N ANISOU 299 NH1 ARG A 33 1613 2177 1460 191 210 207 N ATOM 300 NH2 ARG A 33 18.033 1.904 9.062 1.00 15.85 N ANISOU 300 NH2 ARG A 33 1870 2555 1599 309 427 491 N ATOM 301 N ASN A 34 21.055 -3.358 15.870 1.00 16.05 N ANISOU 301 N ASN A 34 2453 1940 1704 -327 -496 285 N ATOM 302 CA ASN A 34 21.285 -3.704 17.254 1.00 16.83 C ANISOU 302 CA ASN A 34 2572 2107 1714 -501 -566 241 C ATOM 303 C ASN A 34 20.007 -4.081 17.945 1.00 16.19 C ANISOU 303 C ASN A 34 2442 2308 1401 -123 -462 62 C ATOM 304 O ASN A 34 19.875 -3.919 19.141 1.00 23.76 O ANISOU 304 O ASN A 34 3318 4165 1543 -703 -316 -409 O ATOM 305 CB AASN A 34 22.146 -2.739 18.056 0.56 20.01 C ANISOU 305 CB AASN A 34 2742 2735 2127 -420 -894 -74 C ATOM 306 CB BASN A 34 21.973 -2.512 17.953 0.44 19.62 C ANISOU 306 CB BASN A 34 3396 1995 2062 -553 -1204 461 C ATOM 307 CG AASN A 34 23.508 -2.465 17.470 0.56 22.92 C ANISOU 307 CG AASN A 34 2539 3097 3074 -637 -965 -273 C ATOM 308 CG BASN A 34 22.820 -2.983 19.111 0.44 15.84 C ANISOU 308 CG BASN A 34 2209 2201 1607 -1014 -438 777 C ATOM 309 OD1AASN A 34 23.957 -1.309 17.520 0.56 28.09 O ANISOU 309 OD1AASN A 34 3319 3186 4170 -911 -597 -60 O ATOM 310 OD1BASN A 34 23.285 -4.102 19.068 0.44 21.41 O ANISOU 310 OD1BASN A 34 3000 2366 2769 -607 -1249 829 O ATOM 311 ND2AASN A 34 24.196 -3.485 17.000 0.56 26.04 N ANISOU 311 ND2AASN A 34 2524 3396 3973 -476 -619 -286 N ATOM 312 ND2BASN A 34 23.008 -2.130 20.108 0.44 20.24 N ANISOU 312 ND2BASN A 34 2879 2964 1849 -1262 -769 407 N ATOM 313 N LEU A 35 19.057 -4.652 17.227 1.00 14.72 N ANISOU 313 N LEU A 35 2190 1973 1430 -150 -190 139 N ATOM 314 CA LEU A 35 17.779 -5.075 17.751 1.00 16.21 C ANISOU 314 CA LEU A 35 2099 2494 1564 -30 -139 164 C ATOM 315 C LEU A 35 17.766 -6.476 18.314 1.00 17.46 C ANISOU 315 C LEU A 35 1877 2932 1826 -293 14 693 C ATOM 316 O LEU A 35 16.812 -6.880 18.910 1.00 24.44 O ANISOU 316 O LEU A 35 2326 3895 3064 -295 630 1309 O ATOM 317 CB LEU A 35 16.650 -4.907 16.725 1.00 16.88 C ANISOU 317 CB LEU A 35 2156 2561 1698 379 -218 -33 C ATOM 318 CG LEU A 35 16.551 -3.456 16.205 1.00 18.06 C ANISOU 318 CG LEU A 35 2661 2314 1888 313 -517 -233 C ATOM 319 CD1 LEU A 35 15.558 -3.388 15.080 1.00 21.94 C ANISOU 319 CD1 LEU A 35 3477 2655 2204 991 -994 -407 C ATOM 320 CD2 LEU A 35 16.178 -2.436 17.253 1.00 21.51 C ANISOU 320 CD2 LEU A 35 3086 2755 2331 429 -622 -646 C ATOM 321 N THR A 36 18.843 -7.184 18.126 1.00 16.20 N ANISOU 321 N THR A 36 1897 2257 2000 -428 -198 659 N ATOM 322 CA THR A 36 18.997 -8.565 18.603 1.00 18.89 C ANISOU 322 CA THR A 36 2381 2336 2460 -892 -633 1126 C ATOM 323 C THR A 36 20.110 -8.719 19.639 1.00 19.74 C ANISOU 323 C THR A 36 2155 2836 2510 -769 -544 1138 C ATOM 324 O THR A 36 20.534 -9.820 19.930 1.00 23.03 O ANISOU 324 O THR A 36 2881 3174 2697 -166 -611 1243 O ATOM 325 CB THR A 36 19.202 -9.560 17.472 1.00 22.19 C ANISOU 325 CB THR A 36 3454 1827 3149 -758 -1271 862 C ATOM 326 OG1 THR A 36 20.411 -9.225 16.816 1.00 23.56 O ANISOU 326 OG1 THR A 36 3799 2340 2812 -163 -525 234 O ATOM 327 CG2 THR A 36 18.067 -9.565 16.478 1.00 27.03 C ANISOU 327 CG2 THR A 36 4292 2299 3680 -371 -2044 533 C ATOM 328 N LYS A 37 20.544 -7.583 20.197 1.00 22.83 N ANISOU 328 N LYS A 37 2760 3142 2774 -1121 -1060 1238 N ATOM 329 CA LYS A 37 21.724 -7.682 21.065 1.00 26.16 C ANISOU 329 CA LYS A 37 3215 4079 2645 -1452 -1253 1478 C ATOM 330 C LYS A 37 21.491 -8.487 22.308 1.00 21.29 C ANISOU 330 C LYS A 37 2518 2961 2612 -545 -673 1040 C ATOM 331 O LYS A 37 22.329 -9.312 22.717 1.00 26.80 O ANISOU 331 O LYS A 37 2921 4255 3007 152 -915 1152 O ATOM 332 CB LYS A 37 22.241 -6.270 21.347 1.00 38.38 C ANISOU 332 CB LYS A 37 5573 4964 4045 -3579 -2513 2389 C ATOM 333 CG LYS A 37 23.231 -6.103 22.476 1.00 43.89 C ANISOU 333 CG LYS A 37 5370 5715 5592 -3417 -3295 2334 C ATOM 334 CD LYS A 37 23.477 -4.623 22.759 1.00 59.49 C ANISOU 334 CD LYS A 37 8848 6316 7440 -5381 -4798 2212 C ATOM 335 CE LYS A 37 23.655 -4.242 24.214 1.00 72.04 C ANISOU 335 CE LYS A 37 9436 9666 8271 -6014 -2835 -616 C ATOM 336 NZ LYS A 37 23.513 -2.757 24.417 1.00 70.46 N ANISOU 336 NZ LYS A 37 7207 10098 9468 -4734 3339 -1185 N ATOM 337 N ASP A 38 20.385 -8.271 22.993 1.00 19.94 N ANISOU 337 N ASP A 38 2753 2089 2735 -748 -514 139 N ATOM 338 CA ASP A 38 20.117 -8.908 24.288 1.00 18.60 C ANISOU 338 CA ASP A 38 2502 2221 2343 -315 -446 -145 C ATOM 339 C ASP A 38 19.176 -10.095 24.201 1.00 15.23 C ANISOU 339 C ASP A 38 2258 2036 1493 -77 -232 -50 C ATOM 340 O ASP A 38 19.211 -10.971 25.036 1.00 16.48 O ANISOU 340 O ASP A 38 2302 2311 1649 -2 -344 153 O ATOM 341 CB ASP A 38 19.479 -7.873 25.241 1.00 26.22 C ANISOU 341 CB ASP A 38 3998 2769 3197 -234 -375 -1101 C ATOM 342 CG ASP A 38 20.432 -6.722 25.561 1.00 40.77 C ANISOU 342 CG ASP A 38 6134 3393 5963 -909 -2045 -1831 C ATOM 343 OD1 ASP A 38 21.581 -7.071 25.861 1.00 50.97 O ANISOU 343 OD1 ASP A 38 5783 4944 8639 -1354 -2673 -2492 O ATOM 344 OD2 ASP A 38 19.988 -5.568 25.496 1.00 47.01 O ANISOU 344 OD2 ASP A 38 6628 3145 8087 -902 1067 -2405 O ATOM 345 N ARG A 39 18.345 -10.150 23.186 1.00 14.80 N ANISOU 345 N ARG A 39 2310 1762 1553 -265 -270 226 N ATOM 346 CA ARG A 39 17.359 -11.162 22.943 1.00 14.20 C ANISOU 346 CA ARG A 39 2281 1755 1361 -249 -139 197 C ATOM 347 C ARG A 39 16.873 -10.997 21.522 1.00 13.18 C ANISOU 347 C ARG A 39 1893 1686 1427 -152 -68 225 C ATOM 348 O ARG A 39 17.039 -9.938 20.910 1.00 15.98 O ANISOU 348 O ARG A 39 2582 1861 1629 -342 -323 427 O ATOM 349 CB ARG A 39 16.204 -11.098 23.913 0.90 15.06 C ANISOU 349 CB ARG A 39 2325 2091 1305 -302 -129 206 C ATOM 350 CG ARG A 39 15.372 -9.837 23.806 1.00 21.24 C ANISOU 350 CG ARG A 39 3026 2408 2637 228 406 132 C ATOM 351 CD ARG A 39 14.281 -9.689 24.788 1.00 32.25 C ANISOU 351 CD ARG A 39 4218 4923 3111 1434 1120 272 C ATOM 352 NE ARG A 39 13.623 -8.431 24.477 1.00 47.25 N ANISOU 352 NE ARG A 39 6355 6604 4993 3801 991 -52 N ATOM 353 CZ ARG A 39 12.471 -8.275 23.857 1.00 69.06 C ANISOU 353 CZ ARG A 39 10495 9449 6297 4228 -2858 2121 C ATOM 354 NH1 ARG A 39 11.749 -9.285 23.377 1.00 59.73 N ANISOU 354 NH1 ARG A 39 7051 13009 2633 4133 122 -732 N ATOM 355 NH2 ARG A 39 12.055 -7.016 23.716 1.00 77.07 N ANISOU 355 NH2 ARG A 39 10940 10993 7352 6488 -393 2956 N ATOM 356 N CYS A 40 16.255 -12.005 20.982 1.00 13.70 N ANISOU 356 N CYS A 40 2123 1738 1344 -81 -89 170 N ATOM 357 CA CYS A 40 15.615 -11.874 19.673 1.00 14.34 C ANISOU 357 CA CYS A 40 1999 1969 1481 -64 -162 101 C ATOM 358 C CYS A 40 14.275 -11.168 19.854 1.00 15.48 C ANISOU 358 C CYS A 40 2124 2399 1358 114 -167 77 C ATOM 359 O CYS A 40 13.354 -11.710 20.458 1.00 21.52 O ANISOU 359 O CYS A 40 2231 2799 3146 216 303 619 O ATOM 360 CB CYS A 40 15.361 -13.235 19.033 1.00 15.77 C ANISOU 360 CB CYS A 40 2004 2199 1790 -76 -293 -107 C ATOM 361 SG CYS A 40 16.809 -14.279 18.830 1.00 15.35 S ANISOU 361 SG CYS A 40 2335 1921 1576 -85 -124 8 S ATOM 362 N LYS A 41 14.105 -10.014 19.247 1.00 17.24 N ANISOU 362 N LYS A 41 2631 2416 1504 493 70 53 N ATOM 363 CA LYS A 41 12.794 -9.374 19.226 1.00 18.54 C ANISOU 363 CA LYS A 41 2694 2885 1467 789 324 107 C ATOM 364 C LYS A 41 11.880 -10.214 18.345 1.00 18.12 C ANISOU 364 C LYS A 41 2512 3178 1195 1081 121 125 C ATOM 365 O LYS A 41 12.305 -10.561 17.251 1.00 21.74 O ANISOU 365 O LYS A 41 2649 4351 1261 1285 226 -175 O ATOM 366 CB ALYS A 41 13.030 -7.939 18.811 0.48 22.84 C ANISOU 366 CB ALYS A 41 3128 2907 2641 972 469 379 C ATOM 367 CB BLYS A 41 12.806 -8.019 18.504 0.52 21.15 C ANISOU 367 CB BLYS A 41 3019 2983 2034 1084 390 319 C ATOM 368 CG ALYS A 41 11.972 -6.909 18.693 0.48 20.77 C ANISOU 368 CG ALYS A 41 2037 2674 3180 335 791 463 C ATOM 369 CG BLYS A 41 13.240 -6.975 19.517 0.52 23.22 C ANISOU 369 CG BLYS A 41 2600 3140 3083 -128 119 403 C ATOM 370 CD ALYS A 41 12.323 -5.464 18.451 0.48 24.38 C ANISOU 370 CD ALYS A 41 3411 2452 3401 385 1079 59 C ATOM 371 CD BLYS A 41 13.212 -5.585 18.910 0.52 24.23 C ANISOU 371 CD BLYS A 41 2735 3294 3179 -460 1142 625 C ATOM 372 CE ALYS A 41 13.787 -5.142 18.636 0.48 37.79 C ANISOU 372 CE ALYS A 41 4494 4433 5432 -1731 39 746 C ATOM 373 CE BLYS A 41 13.553 -4.541 19.965 0.52 31.20 C ANISOU 373 CE BLYS A 41 3431 3351 5070 -702 -379 137 C ATOM 374 NZ ALYS A 41 14.211 -4.769 20.015 0.48 51.17 N ANISOU 374 NZ ALYS A 41 7008 5693 6743 -826 -2010 -290 N ATOM 375 NZ BLYS A 41 14.986 -4.585 20.401 0.52 28.96 N ANISOU 375 NZ BLYS A 41 2958 3680 4367 -591 416 872 N ATOM 376 N PRO A 42 10.656 -10.489 18.752 1.00 17.17 N ANISOU 376 N PRO A 42 2727 2660 1139 832 266 179 N ATOM 377 CA PRO A 42 9.852 -11.439 17.962 1.00 18.27 C ANISOU 377 CA PRO A 42 3247 2326 1370 651 256 240 C ATOM 378 C PRO A 42 9.329 -10.879 16.672 1.00 15.11 C ANISOU 378 C PRO A 42 2407 1965 1369 347 366 146 C ATOM 379 O PRO A 42 9.101 -11.649 15.741 1.00 18.03 O ANISOU 379 O PRO A 42 3355 1986 1508 227 143 -17 O ATOM 380 CB PRO A 42 8.676 -11.811 18.888 1.00 21.36 C ANISOU 380 CB PRO A 42 3712 2872 1533 74 418 606 C ATOM 381 CG PRO A 42 8.654 -10.713 19.875 1.00 29.38 C ANISOU 381 CG PRO A 42 3889 4854 2419 -1008 1414 -882 C ATOM 382 CD PRO A 42 10.098 -10.275 20.093 1.00 21.04 C ANISOU 382 CD PRO A 42 3405 3194 1393 314 689 -18 C ATOM 383 N VAL A 43 9.066 -9.587 16.639 1.00 13.78 N ANISOU 383 N VAL A 43 2128 1832 1275 2 370 197 N ATOM 384 CA VAL A 43 8.469 -8.940 15.476 1.00 13.58 C ANISOU 384 CA VAL A 43 1831 1867 1461 -201 159 330 C ATOM 385 C VAL A 43 9.038 -7.546 15.364 1.00 12.90 C ANISOU 385 C VAL A 43 1832 1855 1215 -139 141 181 C ATOM 386 O VAL A 43 9.386 -6.937 16.379 1.00 15.79 O ANISOU 386 O VAL A 43 2623 2065 1313 -435 -27 201 O ATOM 387 CB AVAL A 43 6.938 -8.816 15.554 0.59 17.27 C ANISOU 387 CB AVAL A 43 1830 2042 2690 -302 95 505 C ATOM 388 CB BVAL A 43 6.938 -9.013 15.593 0.41 16.12 C ANISOU 388 CB BVAL A 43 1801 2054 2271 -95 382 454 C ATOM 389 CG1AVAL A 43 6.255 -10.142 15.717 0.59 23.13 C ANISOU 389 CG1AVAL A 43 2406 2373 4008 -697 705 859 C ATOM 390 CG1BVAL A 43 6.455 -8.400 16.886 0.41 20.38 C ANISOU 390 CG1BVAL A 43 2541 2212 2990 -141 981 -32 C ATOM 391 CG2AVAL A 43 6.526 -7.803 16.601 0.59 21.23 C ANISOU 391 CG2AVAL A 43 2216 2645 3204 108 850 397 C ATOM 392 CG2BVAL A 43 6.289 -8.339 14.393 0.41 23.31 C ANISOU 392 CG2BVAL A 43 1822 3792 3243 -634 -513 1231 C ATOM 393 N ASN A 44 9.108 -7.009 14.176 1.00 12.09 N ANISOU 393 N ASN A 44 1696 1657 1242 -188 115 83 N ATOM 394 CA ASN A 44 9.440 -5.619 13.946 1.00 11.60 C ANISOU 394 CA ASN A 44 1545 1568 1293 -76 159 20 C ATOM 395 C ASN A 44 8.928 -5.211 12.595 1.00 11.99 C ANISOU 395 C ASN A 44 1766 1583 1208 -134 157 -36 C ATOM 396 O ASN A 44 8.703 -6.061 11.745 1.00 14.68 O ANISOU 396 O ASN A 44 2742 1584 1253 -69 35 -107 O ATOM 397 CB ASN A 44 10.952 -5.395 14.066 1.00 12.69 C ANISOU 397 CB ASN A 44 1612 1672 1538 -204 138 115 C ATOM 398 CG ASN A 44 11.309 -3.952 14.156 1.00 12.36 C ANISOU 398 CG ASN A 44 1678 1651 1366 -146 109 -33 C ATOM 399 OD1 ASN A 44 10.642 -3.193 14.861 1.00 16.74 O ANISOU 399 OD1 ASN A 44 2227 1905 2228 -280 615 -332 O ATOM 400 ND2 ASN A 44 12.285 -3.497 13.442 1.00 14.16 N ANISOU 400 ND2 ASN A 44 1766 1764 1852 -335 276 -110 N ATOM 401 N THR A 45 8.802 -3.914 12.403 1.00 11.35 N ANISOU 401 N THR A 45 1647 1590 1075 -164 148 -21 N ATOM 402 CA THR A 45 8.421 -3.314 11.118 1.00 11.12 C ANISOU 402 CA THR A 45 1536 1592 1096 -151 89 -8 C ATOM 403 C THR A 45 9.391 -2.218 10.744 1.00 11.11 C ANISOU 403 C THR A 45 1521 1661 1038 -114 45 -16 C ATOM 404 O THR A 45 9.695 -1.362 11.605 1.00 12.86 O ANISOU 404 O THR A 45 2088 1695 1105 -358 221 -69 O ATOM 405 CB THR A 45 6.993 -2.725 11.200 1.00 12.82 C ANISOU 405 CB THR A 45 1595 1901 1376 -105 122 -12 C ATOM 406 OG1 THR A 45 6.109 -3.767 11.598 1.00 16.33 O ANISOU 406 OG1 THR A 45 1521 2451 2235 -315 117 278 O ATOM 407 CG2 THR A 45 6.566 -2.161 9.858 1.00 15.36 C ANISOU 407 CG2 THR A 45 1806 2403 1628 315 -3 110 C ATOM 408 N PHE A 46 9.842 -2.204 9.518 1.00 10.81 N ANISOU 408 N PHE A 46 1580 1502 1025 -161 53 -1 N ATOM 409 CA PHE A 46 10.644 -1.126 8.963 1.00 11.21 C ANISOU 409 CA PHE A 46 1535 1681 1042 -153 7 83 C ATOM 410 C PHE A 46 9.803 -0.361 7.943 1.00 11.44 C ANISOU 410 C PHE A 46 1673 1644 1030 -118 -50 82 C ATOM 411 O PHE A 46 9.001 -0.940 7.237 1.00 13.18 O ANISOU 411 O PHE A 46 2049 1594 1363 -42 -384 -54 O ATOM 412 CB PHE A 46 11.893 -1.670 8.263 1.00 12.53 C ANISOU 412 CB PHE A 46 1764 1649 1349 -34 160 154 C ATOM 413 CG PHE A 46 12.901 -2.232 9.243 1.00 11.73 C ANISOU 413 CG PHE A 46 1423 1838 1195 -94 169 73 C ATOM 414 CD1 PHE A 46 13.749 -1.406 9.942 1.00 14.34 C ANISOU 414 CD1 PHE A 46 1509 2071 1868 -139 85 -65 C ATOM 415 CD2 PHE A 46 12.967 -3.600 9.469 1.00 12.94 C ANISOU 415 CD2 PHE A 46 1682 1863 1370 98 148 103 C ATOM 416 CE1 PHE A 46 14.651 -1.939 10.857 1.00 15.73 C ANISOU 416 CE1 PHE A 46 1613 2653 1710 -113 -147 -162 C ATOM 417 CE2 PHE A 46 13.859 -4.125 10.361 1.00 14.99 C ANISOU 417 CE2 PHE A 46 1979 2110 1607 346 118 93 C ATOM 418 CZ PHE A 46 14.704 -3.300 11.023 1.00 15.75 C ANISOU 418 CZ PHE A 46 1746 2808 1432 282 4 55 C ATOM 419 N VAL A 47 10.010 0.957 7.906 1.00 11.92 N ANISOU 419 N VAL A 47 1767 1628 1135 -188 -129 137 N ATOM 420 CA VAL A 47 9.273 1.880 7.052 1.00 11.46 C ANISOU 420 CA VAL A 47 1725 1562 1069 -130 26 19 C ATOM 421 C VAL A 47 10.210 2.483 6.049 1.00 11.14 C ANISOU 421 C VAL A 47 1621 1535 1078 -77 39 6 C ATOM 422 O VAL A 47 11.221 3.082 6.407 1.00 12.66 O ANISOU 422 O VAL A 47 1698 1864 1249 -195 1 15 O ATOM 423 CB VAL A 47 8.583 2.961 7.883 1.00 12.40 C ANISOU 423 CB VAL A 47 1890 1676 1145 -76 184 -22 C ATOM 424 CG1 VAL A 47 7.762 3.836 6.971 1.00 15.59 C ANISOU 424 CG1 VAL A 47 2235 1937 1753 307 253 18 C ATOM 425 CG2 VAL A 47 7.753 2.359 9.006 1.00 15.88 C ANISOU 425 CG2 VAL A 47 2289 2195 1549 -123 476 -86 C ATOM 426 N HIS A 48 9.873 2.346 4.771 1.00 11.57 N ANISOU 426 N HIS A 48 1567 1753 1075 -158 62 41 N ATOM 427 CA HIS A 48 10.715 2.754 3.663 1.00 12.03 C ANISOU 427 CA HIS A 48 1802 1637 1131 -137 167 95 C ATOM 428 C HIS A 48 10.205 4.038 3.086 1.00 12.82 C ANISOU 428 C HIS A 48 2037 1664 1169 -59 212 43 C ATOM 429 O HIS A 48 9.748 4.105 1.948 1.00 16.41 O ANISOU 429 O HIS A 48 3010 1920 1306 122 -196 27 O ATOM 430 CB HIS A 48 10.697 1.663 2.576 1.00 12.72 C ANISOU 430 CB HIS A 48 1940 1663 1230 89 191 31 C ATOM 431 CG HIS A 48 11.142 0.344 3.089 1.00 12.51 C ANISOU 431 CG HIS A 48 1713 1707 1333 22 169 172 C ATOM 432 ND1 HIS A 48 12.410 0.049 3.409 1.00 21.45 N ANISOU 432 ND1 HIS A 48 1812 2419 3918 -238 -303 1436 N ATOM 433 CD2 HIS A 48 10.456 -0.787 3.371 1.00 13.43 C ANISOU 433 CD2 HIS A 48 1853 1713 1538 -94 295 42 C ATOM 434 CE1 HIS A 48 12.466 -1.199 3.823 1.00 21.81 C ANISOU 434 CE1 HIS A 48 1986 2381 3919 -70 -163 1387 C ATOM 435 NE2 HIS A 48 11.311 -1.766 3.844 1.00 14.47 N ANISOU 435 NE2 HIS A 48 2018 1707 1772 9 289 118 N ATOM 436 N GLU A 49 10.250 5.089 3.871 1.00 13.71 N ANISOU 436 N GLU A 49 2337 1599 1275 -66 120 74 N ATOM 437 CA GLU A 49 9.778 6.426 3.531 1.00 13.18 C ANISOU 437 CA GLU A 49 2128 1622 1259 -75 162 52 C ATOM 438 C GLU A 49 10.743 7.423 4.137 1.00 13.23 C ANISOU 438 C GLU A 49 2116 1604 1305 26 226 53 C ATOM 439 O GLU A 49 11.566 7.088 4.968 1.00 14.88 O ANISOU 439 O GLU A 49 2200 1851 1603 -122 8 92 O ATOM 440 CB GLU A 49 8.379 6.647 4.064 1.00 14.76 C ANISOU 440 CB GLU A 49 2181 1785 1644 -97 260 81 C ATOM 441 CG GLU A 49 7.324 5.663 3.576 1.00 16.47 C ANISOU 441 CG GLU A 49 2237 2127 1895 -274 26 139 C ATOM 442 CD GLU A 49 6.940 5.772 2.135 1.00 16.79 C ANISOU 442 CD GLU A 49 2308 1993 2080 -157 -230 314 C ATOM 443 OE1 GLU A 49 7.279 6.800 1.498 1.00 22.14 O ANISOU 443 OE1 GLU A 49 3900 2116 2395 -535 -815 573 O ATOM 444 OE2 GLU A 49 6.262 4.826 1.652 1.00 18.43 O ANISOU 444 OE2 GLU A 49 2516 2320 2165 -373 -388 261 O ATOM 445 N SER A 50 10.634 8.682 3.674 1.00 13.87 N ANISOU 445 N SER A 50 2229 1551 1492 -100 338 38 N ATOM 446 CA SER A 50 11.443 9.726 4.300 1.00 14.22 C ANISOU 446 CA SER A 50 2031 1756 1616 -281 440 -37 C ATOM 447 C SER A 50 11.014 9.918 5.764 1.00 13.73 C ANISOU 447 C SER A 50 1889 1774 1553 -199 368 -56 C ATOM 448 O SER A 50 9.889 9.727 6.160 1.00 14.30 O ANISOU 448 O SER A 50 1903 1856 1674 -258 370 -178 O ATOM 449 CB SER A 50 11.249 10.999 3.587 1.00 16.52 C ANISOU 449 CB SER A 50 2725 1740 1811 -259 722 70 C ATOM 450 OG SER A 50 10.037 11.607 3.843 1.00 20.47 O ANISOU 450 OG SER A 50 3020 2333 2423 355 658 465 O ATOM 451 N LEU A 51 11.985 10.317 6.549 1.00 14.29 N ANISOU 451 N LEU A 51 1716 2098 1615 -187 456 -62 N ATOM 452 CA LEU A 51 11.732 10.616 7.948 1.00 15.24 C ANISOU 452 CA LEU A 51 2006 2166 1617 -156 375 -97 C ATOM 453 C LEU A 51 10.694 11.708 8.053 1.00 14.82 C ANISOU 453 C LEU A 51 1985 1895 1752 -324 532 -227 C ATOM 454 O LEU A 51 9.819 11.613 8.932 1.00 15.62 O ANISOU 454 O LEU A 51 1947 2353 1633 -242 389 -67 O ATOM 455 CB LEU A 51 13.034 10.956 8.657 1.00 17.75 C ANISOU 455 CB LEU A 51 2206 2530 2008 -219 168 -385 C ATOM 456 CG LEU A 51 12.890 11.236 10.115 1.00 18.05 C ANISOU 456 CG LEU A 51 2553 2225 2082 -108 10 -454 C ATOM 457 CD1 LEU A 51 12.362 10.049 10.875 1.00 22.42 C ANISOU 457 CD1 LEU A 51 4238 2314 1966 -38 -32 -22 C ATOM 458 CD2 LEU A 51 14.243 11.667 10.682 1.00 27.19 C ANISOU 458 CD2 LEU A 51 3206 3771 3352 -275 -984 -964 C ATOM 459 N ALA A 52 10.756 12.728 7.217 1.00 15.62 N ANISOU 459 N ALA A 52 2140 1799 1996 -318 639 -165 N ATOM 460 CA ALA A 52 9.805 13.810 7.329 1.00 16.86 C ANISOU 460 CA ALA A 52 2294 1894 2216 -269 659 -56 C ATOM 461 C ALA A 52 8.375 13.336 7.123 1.00 15.00 C ANISOU 461 C ALA A 52 2278 1710 1711 -42 499 78 C ATOM 462 O ALA A 52 7.463 13.819 7.769 1.00 16.79 O ANISOU 462 O ALA A 52 2375 1938 2066 -2 626 -106 O ATOM 463 CB ALA A 52 10.178 14.921 6.345 1.00 21.16 C ANISOU 463 CB ALA A 52 2946 1982 3112 -198 1050 361 C ATOM 464 N ASP A 53 8.190 12.422 6.189 1.00 14.84 N ANISOU 464 N ASP A 53 2197 1686 1755 -9 490 80 N ATOM 465 CA ASP A 53 6.841 11.901 5.924 1.00 14.74 C ANISOU 465 CA ASP A 53 2157 1849 1594 32 302 175 C ATOM 466 C ASP A 53 6.303 11.097 7.079 1.00 13.64 C ANISOU 466 C ASP A 53 1856 1771 1555 68 163 83 C ATOM 467 O ASP A 53 5.096 11.125 7.340 1.00 16.27 O ANISOU 467 O ASP A 53 1819 2372 1989 113 202 466 O ATOM 468 CB ASP A 53 6.817 11.089 4.622 1.00 16.09 C ANISOU 468 CB ASP A 53 2287 2233 1592 -5 198 105 C ATOM 469 CG ASP A 53 6.914 11.917 3.362 1.00 19.92 C ANISOU 469 CG ASP A 53 2974 2925 1668 780 401 445 C ATOM 470 OD1 ASP A 53 6.638 13.123 3.407 1.00 27.92 O ANISOU 470 OD1 ASP A 53 5556 2931 2121 1125 704 671 O ATOM 471 OD2 ASP A 53 7.150 11.309 2.339 1.00 25.65 O ANISOU 471 OD2 ASP A 53 4804 3269 1671 1097 553 450 O ATOM 472 N VAL A 54 7.149 10.356 7.778 1.00 12.85 N ANISOU 472 N VAL A 54 1759 1665 1458 56 288 47 N ATOM 473 CA VAL A 54 6.733 9.621 8.945 1.00 12.79 C ANISOU 473 CA VAL A 54 1831 1566 1462 -150 194 11 C ATOM 474 C VAL A 54 6.483 10.558 10.116 1.00 12.95 C ANISOU 474 C VAL A 54 1779 1639 1502 -132 281 6 C ATOM 475 O VAL A 54 5.503 10.400 10.838 1.00 14.20 O ANISOU 475 O VAL A 54 1806 1938 1651 -131 348 43 O ATOM 476 CB VAL A 54 7.737 8.497 9.250 1.00 13.07 C ANISOU 476 CB VAL A 54 1793 1713 1461 3 66 -40 C ATOM 477 CG1 VAL A 54 7.374 7.771 10.542 1.00 15.99 C ANISOU 477 CG1 VAL A 54 2377 2056 1643 120 75 243 C ATOM 478 CG2 VAL A 54 7.784 7.523 8.087 1.00 15.72 C ANISOU 478 CG2 VAL A 54 2241 1904 1828 111 137 -222 C ATOM 479 N GLN A 55 7.360 11.551 10.335 1.00 13.54 N ANISOU 479 N GLN A 55 2016 1642 1485 -239 390 -93 N ATOM 480 CA GLN A 55 7.110 12.506 11.383 1.00 14.34 C ANISOU 480 CA GLN A 55 2054 1821 1574 -140 315 -187 C ATOM 481 C GLN A 55 5.806 13.243 11.188 1.00 14.08 C ANISOU 481 C GLN A 55 1918 1786 1646 -213 358 -264 C ATOM 482 O GLN A 55 5.140 13.584 12.176 1.00 16.06 O ANISOU 482 O GLN A 55 2141 2073 1889 -42 441 -363 O ATOM 483 CB GLN A 55 8.277 13.491 11.493 1.00 16.39 C ANISOU 483 CB GLN A 55 2024 2108 2097 -309 293 -435 C ATOM 484 CG GLN A 55 9.570 12.894 11.996 1.00 17.93 C ANISOU 484 CG GLN A 55 2087 2731 1993 -284 209 -289 C ATOM 485 CD GLN A 55 10.767 13.871 11.812 1.00 18.24 C ANISOU 485 CD GLN A 55 2055 2101 2775 -193 203 -649 C ATOM 486 OE1 GLN A 55 10.732 14.758 10.942 1.00 25.58 O ANISOU 486 OE1 GLN A 55 2916 2944 3859 -719 -150 358 O ATOM 487 NE2 GLN A 55 11.790 13.656 12.560 1.00 20.57 N ANISOU 487 NE2 GLN A 55 2354 2424 3038 -305 -32 -617 N ATOM 488 N ALA A 56 5.439 13.491 9.961 1.00 15.17 N ANISOU 488 N ALA A 56 2092 1876 1795 -33 432 8 N ATOM 489 CA ALA A 56 4.210 14.224 9.646 1.00 15.63 C ANISOU 489 CA ALA A 56 2260 1537 2142 85 521 165 C ATOM 490 C ALA A 56 2.973 13.466 10.083 1.00 15.02 C ANISOU 490 C ALA A 56 2126 1763 1817 137 398 118 C ATOM 491 O ALA A 56 1.903 14.100 10.246 1.00 16.20 O ANISOU 491 O ALA A 56 2043 1936 2178 263 163 197 O ATOM 492 CB ALA A 56 4.137 14.502 8.168 1.00 18.78 C ANISOU 492 CB ALA A 56 2659 2309 2168 288 549 590 C ATOM 493 N VAL A 57 3.065 12.157 10.317 1.00 13.92 N ANISOU 493 N VAL A 57 1801 1658 1829 31 329 25 N ATOM 494 CA VAL A 57 1.908 11.401 10.745 1.00 13.86 C ANISOU 494 CA VAL A 57 1779 1824 1663 11 173 53 C ATOM 495 C VAL A 57 1.369 11.916 12.064 1.00 13.29 C ANISOU 495 C VAL A 57 1598 1722 1729 178 149 65 C ATOM 496 O VAL A 57 0.194 11.786 12.333 1.00 14.71 O ANISOU 496 O VAL A 57 1724 1934 1930 70 191 11 O ATOM 497 CB VAL A 57 2.213 9.876 10.759 1.00 13.84 C ANISOU 497 CB VAL A 57 1814 1740 1703 -87 161 -88 C ATOM 498 CG1 VAL A 57 1.064 9.062 11.286 1.00 15.26 C ANISOU 498 CG1 VAL A 57 2050 1786 1961 -153 272 15 C ATOM 499 CG2 VAL A 57 2.565 9.429 9.318 1.00 15.79 C ANISOU 499 CG2 VAL A 57 2203 2006 1791 -85 329 -235 C ATOM 500 N CYS A 58 2.212 12.516 12.890 1.00 14.05 N ANISOU 500 N CYS A 58 1743 1888 1708 1 312 -67 N ATOM 501 CA CYS A 58 1.791 13.078 14.168 1.00 14.80 C ANISOU 501 CA CYS A 58 1914 1825 1885 29 283 -149 C ATOM 502 C CYS A 58 0.833 14.248 14.035 1.00 15.62 C ANISOU 502 C CYS A 58 2067 1862 2007 151 346 -217 C ATOM 503 O CYS A 58 0.273 14.652 15.053 1.00 20.20 O ANISOU 503 O CYS A 58 2826 2497 2352 640 658 -155 O ATOM 504 CB CYS A 58 2.965 13.487 15.012 1.00 15.86 C ANISOU 504 CB CYS A 58 2133 2020 1874 -96 159 -135 C ATOM 505 SG CYS A 58 4.095 12.149 15.467 1.00 15.89 S ANISOU 505 SG CYS A 58 1924 2322 1790 54 158 -183 S ATOM 506 N SER A 59 0.609 14.735 12.823 1.00 16.54 N ANISOU 506 N SER A 59 2205 1852 2228 289 256 -112 N ATOM 507 CA SER A 59 -0.350 15.769 12.538 1.00 18.90 C ANISOU 507 CA SER A 59 2557 1939 2685 393 84 -28 C ATOM 508 C SER A 59 -1.502 15.248 11.729 1.00 18.34 C ANISOU 508 C SER A 59 2473 2078 2416 582 71 -13 C ATOM 509 O SER A 59 -2.286 16.062 11.198 1.00 23.32 O ANISOU 509 O SER A 59 2888 2276 3696 685 -326 289 O ATOM 510 CB ASER A 59 0.297 17.031 11.994 0.47 26.23 C ANISOU 510 CB ASER A 59 4316 2071 3578 -312 -883 513 C ATOM 511 CB BSER A 59 0.329 16.929 11.813 0.53 21.80 C ANISOU 511 CB BSER A 59 3109 1846 3329 329 279 98 C ATOM 512 OG ASER A 59 0.856 16.757 10.722 0.47 27.49 O ANISOU 512 OG ASER A 59 3369 2494 4584 445 482 1675 O ATOM 513 OG BSER A 59 1.434 17.430 12.536 0.53 30.10 O ANISOU 513 OG BSER A 59 4166 3580 3691 -1215 81 240 O ATOM 514 N GLN A 60 -1.664 13.952 11.576 1.00 16.66 N ANISOU 514 N GLN A 60 2083 2155 2093 500 61 52 N ATOM 515 CA GLN A 60 -2.671 13.316 10.735 1.00 17.60 C ANISOU 515 CA GLN A 60 2036 2515 2138 379 -25 142 C ATOM 516 C GLN A 60 -3.817 12.785 11.562 1.00 18.70 C ANISOU 516 C GLN A 60 2036 2416 2654 525 187 254 C ATOM 517 O GLN A 60 -4.274 13.520 12.457 1.00 21.65 O ANISOU 517 O GLN A 60 2316 2758 3150 235 594 -176 O ATOM 518 CB GLN A 60 -2.026 12.362 9.735 1.00 16.71 C ANISOU 518 CB GLN A 60 2188 2160 2000 294 -47 210 C ATOM 519 CG GLN A 60 -1.099 13.150 8.836 1.00 17.88 C ANISOU 519 CG GLN A 60 2492 2032 2269 344 189 309 C ATOM 520 CD GLN A 60 -0.318 12.324 7.839 1.00 16.85 C ANISOU 520 CD GLN A 60 2276 2078 2046 222 40 307 C ATOM 521 OE1 GLN A 60 -0.583 11.179 7.556 1.00 19.57 O ANISOU 521 OE1 GLN A 60 2685 2249 2501 77 297 96 O ATOM 522 NE2 GLN A 60 0.729 12.940 7.284 1.00 22.11 N ANISOU 522 NE2 GLN A 60 2997 2873 2530 -315 641 54 N ATOM 523 N LYS A 61 -4.347 11.621 11.293 1.00 17.71 N ANISOU 523 N LYS A 61 2072 2626 2032 347 86 230 N ATOM 524 CA LYS A 61 -5.627 11.226 11.916 1.00 18.84 C ANISOU 524 CA LYS A 61 1979 2733 2445 482 87 359 C ATOM 525 C LYS A 61 -5.395 10.689 13.316 1.00 16.82 C ANISOU 525 C LYS A 61 1751 2331 2308 329 285 151 C ATOM 526 O LYS A 61 -4.786 9.629 13.493 1.00 18.46 O ANISOU 526 O LYS A 61 2011 2759 2245 800 192 30 O ATOM 527 CB ALYS A 61 -6.262 10.147 11.042 0.46 21.52 C ATOM 528 CB BLYS A 61 -6.221 10.114 11.035 0.54 18.57 C ATOM 529 CG ALYS A 61 -7.566 9.535 11.569 0.46 36.87 C ATOM 530 CG BLYS A 61 -7.566 9.662 11.623 0.54 20.74 C ATOM 531 CD ALYS A 61 -8.756 10.449 11.450 0.46 37.77 C ATOM 532 CD BLYS A 61 -8.387 8.747 10.760 0.54 28.51 C ATOM 533 CE ALYS A 61 -10.136 9.791 11.318 0.46 27.86 C ATOM 534 CE BLYS A 61 -9.830 8.661 11.264 0.54 32.45 C ATOM 535 NZ ALYS A 61 -11.153 10.588 12.085 0.46 29.46 N ATOM 536 NZ BLYS A 61 -10.103 9.512 12.467 0.54 34.84 N ATOM 537 N ASN A 62 -5.920 11.329 14.329 1.00 17.20 N ANISOU 537 N ASN A 62 1926 2235 2373 504 225 208 N ATOM 538 CA ASN A 62 -5.798 10.863 15.692 1.00 16.64 C ANISOU 538 CA ASN A 62 1763 2286 2273 353 217 41 C ATOM 539 C ASN A 62 -6.719 9.660 15.893 1.00 17.27 C ANISOU 539 C ASN A 62 1625 2601 2335 183 141 186 C ATOM 540 O ASN A 62 -7.892 9.748 15.581 1.00 20.75 O ANISOU 540 O ASN A 62 1608 3099 3178 292 181 446 O ATOM 541 CB ASN A 62 -6.150 12.015 16.646 1.00 20.42 C ANISOU 541 CB ASN A 62 2247 2767 2745 677 227 -435 C ATOM 542 CG ASN A 62 -5.989 11.751 18.100 1.00 22.54 C ANISOU 542 CG ASN A 62 2405 3535 2624 926 403 -446 C ATOM 543 OD1 ASN A 62 -6.762 12.256 18.911 1.00 35.79 O ANISOU 543 OD1 ASN A 62 4215 6511 2871 3063 556 -423 O ATOM 544 ND2 ASN A 62 -4.988 11.029 18.581 1.00 20.01 N ANISOU 544 ND2 ASN A 62 2228 2831 2545 518 429 -336 N ATOM 545 N VAL A 63 -6.181 8.583 16.445 1.00 16.37 N ANISOU 545 N VAL A 63 1608 2443 2169 76 151 100 N ATOM 546 CA VAL A 63 -6.873 7.338 16.705 1.00 16.61 C ANISOU 546 CA VAL A 63 1637 2580 2093 46 105 134 C ATOM 547 C VAL A 63 -6.405 6.783 18.035 1.00 15.47 C ANISOU 547 C VAL A 63 1491 2334 2052 87 154 0 C ATOM 548 O VAL A 63 -5.321 7.119 18.527 1.00 17.62 O ANISOU 548 O VAL A 63 1473 2871 2349 -130 42 184 O ATOM 549 CB VAL A 63 -6.635 6.309 15.590 1.00 17.96 C ANISOU 549 CB VAL A 63 2077 2593 2155 -74 -69 24 C ATOM 550 CG1 VAL A 63 -7.211 6.777 14.280 1.00 22.75 C ANISOU 550 CG1 VAL A 63 2877 3575 2192 -327 -449 159 C ATOM 551 CG2 VAL A 63 -5.181 5.896 15.472 1.00 19.30 C ANISOU 551 CG2 VAL A 63 2159 2895 2278 97 343 -183 C ATOM 552 N ALA A 64 -7.191 5.883 18.610 1.00 15.61 N ANISOU 552 N ALA A 64 1410 2671 1852 -72 77 12 N ATOM 553 CA ALA A 64 -6.752 5.125 19.767 1.00 15.00 C ANISOU 553 CA ALA A 64 1553 2511 1635 -85 135 -104 C ATOM 554 C ALA A 64 -5.650 4.144 19.365 1.00 13.89 C ANISOU 554 C ALA A 64 1596 2245 1438 -203 79 -60 C ATOM 555 O ALA A 64 -5.738 3.425 18.389 1.00 17.52 O ANISOU 555 O ALA A 64 2008 3035 1614 37 -168 -522 O ATOM 556 CB ALA A 64 -7.899 4.445 20.435 1.00 19.34 C ANISOU 556 CB ALA A 64 1754 3280 2313 -70 398 423 C ATOM 557 N CYS A 65 -4.633 4.052 20.216 1.00 13.98 N ANISOU 557 N CYS A 65 1663 2154 1496 -148 16 -168 N ATOM 558 CA CYS A 65 -3.659 2.998 20.116 1.00 13.69 C ANISOU 558 CA CYS A 65 1501 2187 1515 -128 156 -29 C ATOM 559 C CYS A 65 -4.292 1.662 20.508 1.00 13.88 C ANISOU 559 C CYS A 65 1549 2261 1463 -213 110 -42 C ATOM 560 O CYS A 65 -5.342 1.590 21.136 1.00 16.11 O ANISOU 560 O CYS A 65 1640 2582 1901 -435 271 -162 O ATOM 561 CB ACYS A 65 -2.533 3.292 21.116 0.87 14.92 C ANISOU 561 CB ACYS A 65 1785 2260 1622 -296 -85 67 C ATOM 562 CB BCYS A 65 -2.351 3.111 20.877 0.13 12.24 C ANISOU 562 CB BCYS A 65 1821 2091 738 -313 7 508 C ATOM 563 SG ACYS A 65 -1.763 4.917 21.003 0.87 14.61 S ANISOU 563 SG ACYS A 65 1786 2202 1563 -295 4 -52 S ATOM 564 SG BCYS A 65 -1.003 3.924 19.973 0.13 12.85 S ANISOU 564 SG BCYS A 65 1624 1555 1705 -209 402 28 S ATOM 565 N LYS A 66 -3.621 0.570 20.173 1.00 14.59 N ANISOU 565 N LYS A 66 1738 2154 1650 -236 62 -5 N ATOM 566 CA LYS A 66 -4.135 -0.747 20.499 1.00 17.03 C ANISOU 566 CA LYS A 66 2229 2301 1939 -522 115 -154 C ATOM 567 C LYS A 66 -4.420 -0.933 21.977 1.00 17.02 C ANISOU 567 C LYS A 66 2436 2113 1918 -649 143 -92 C ATOM 568 O LYS A 66 -5.348 -1.646 22.335 1.00 21.46 O ANISOU 568 O LYS A 66 3031 2809 2316 -1286 175 8 O ATOM 569 CB LYS A 66 -3.169 -1.839 20.061 1.00 20.69 C ATOM 570 CG LYS A 66 -3.023 -2.047 18.586 1.00 33.66 C ATOM 571 CD LYS A 66 -1.925 -3.124 18.447 1.00 65.39 C ATOM 572 CE LYS A 66 -2.462 -4.439 17.892 1.00 95.90 C ATOM 573 NZ LYS A 66 -1.815 -4.852 16.603 1.00110.00 N ATOM 574 N ASN A 67 -3.611 -0.327 22.836 1.00 16.62 N ANISOU 574 N ASN A 67 2304 2270 1740 -534 54 56 N ATOM 575 CA ASN A 67 -3.750 -0.432 24.290 1.00 19.06 C ANISOU 575 CA ASN A 67 3005 2507 1730 -355 68 164 C ATOM 576 C ASN A 67 -4.661 0.638 24.880 1.00 19.22 C ANISOU 576 C ASN A 67 2649 2799 1855 -622 458 78 C ATOM 577 O ASN A 67 -4.812 0.706 26.095 1.00 24.42 O ANISOU 577 O ASN A 67 3502 3919 1859 68 407 24 O ATOM 578 CB ASN A 67 -2.390 -0.264 24.969 1.00 20.73 C ANISOU 578 CB ASN A 67 3276 2873 1729 3 -381 227 C ATOM 579 CG ASN A 67 -1.839 1.124 24.998 1.00 25.34 C ANISOU 579 CG ASN A 67 3464 3326 2837 -878 -844 1013 C ATOM 580 OD1 ASN A 67 -2.253 2.079 24.358 1.00 21.49 O ANISOU 580 OD1 ASN A 67 2729 3144 2291 -45 -11 531 O ATOM 581 ND2 ASN A 67 -0.851 1.316 25.922 1.00 47.21 N ANISOU 581 ND2 ASN A 67 7349 3402 7188 -825 -4954 834 N ATOM 582 N GLY A 68 -5.325 1.430 24.051 1.00 18.27 N ANISOU 582 N GLY A 68 2407 2635 1898 -492 359 -249 N ATOM 583 CA GLY A 68 -6.314 2.387 24.490 1.00 19.48 C ANISOU 583 CA GLY A 68 2192 2919 2291 -601 643 -498 C ATOM 584 C GLY A 68 -5.803 3.789 24.681 1.00 17.63 C ANISOU 584 C GLY A 68 1937 2919 1844 -383 266 -642 C ATOM 585 O GLY A 68 -6.619 4.713 24.847 1.00 20.40 O ANISOU 585 O GLY A 68 1916 3182 2653 -273 312 -1018 O ATOM 586 N GLN A 69 -4.494 4.046 24.658 1.00 17.01 N ANISOU 586 N GLN A 69 1886 2688 1890 -294 110 -491 N ATOM 587 CA GLN A 69 -4.008 5.426 24.745 1.00 17.59 C ANISOU 587 CA GLN A 69 2145 2632 1908 -367 25 -335 C ATOM 588 C GLN A 69 -4.498 6.198 23.534 1.00 15.77 C ANISOU 588 C GLN A 69 1600 2779 1612 -329 222 -466 C ATOM 589 O GLN A 69 -4.758 5.668 22.474 1.00 19.53 O ANISOU 589 O GLN A 69 2184 3474 1760 -85 6 -753 O ATOM 590 CB GLN A 69 -2.456 5.449 24.682 1.00 18.44 C ANISOU 590 CB GLN A 69 2142 2398 2465 -276 -335 -434 C ATOM 591 CG GLN A 69 -1.761 4.906 25.800 1.00 21.79 C ANISOU 591 CG GLN A 69 2871 2893 2514 -114 -653 -654 C ATOM 592 CD GLN A 69 -0.257 4.794 25.740 1.00 23.23 C ANISOU 592 CD GLN A 69 2625 2692 3508 37 -670 -759 C ATOM 593 OE1 GLN A 69 0.339 4.029 26.458 1.00 27.36 O ANISOU 593 OE1 GLN A 69 3439 3682 3275 522 -408 -229 O ATOM 594 NE2 GLN A 69 0.362 5.630 24.829 1.00 25.57 N ANISOU 594 NE2 GLN A 69 2564 3653 3500 296 -745 -95 N ATOM 595 N THR A 70 -4.524 7.507 23.705 1.00 15.64 N ANISOU 595 N THR A 70 1566 2957 1421 -114 30 -313 N ATOM 596 CA THR A 70 -5.109 8.336 22.673 1.00 16.48 C ANISOU 596 CA THR A 70 1601 3164 1497 -12 128 -203 C ATOM 597 C THR A 70 -4.143 9.289 21.986 1.00 15.62 C ANISOU 597 C THR A 70 1660 2638 1637 91 176 -346 C ATOM 598 O THR A 70 -4.530 10.159 21.224 1.00 19.86 O ANISOU 598 O THR A 70 1883 3058 2606 332 387 190 O ATOM 599 CB THR A 70 -6.360 9.041 23.108 1.00 21.79 C ANISOU 599 CB THR A 70 1706 4765 1807 622 198 210 C ATOM 600 OG1 THR A 70 -6.086 9.692 24.313 1.00 29.30 O ANISOU 600 OG1 THR A 70 3873 5305 1957 2609 -120 -546 O ATOM 601 CG2 THR A 70 -7.485 8.017 23.338 1.00 36.75 C ANISOU 601 CG2 THR A 70 1636 7923 4403 -437 508 1593 C ATOM 602 N ASN A 71 -2.849 9.027 22.106 1.00 15.87 N ANISOU 602 N ASN A 71 1600 2622 1807 -47 349 -196 N ATOM 603 CA ASN A 71 -1.811 9.762 21.398 1.00 15.63 C ANISOU 603 CA ASN A 71 1667 2374 1896 7 389 -279 C ATOM 604 C ASN A 71 -1.288 9.046 20.167 1.00 14.41 C ANISOU 604 C ASN A 71 1543 2257 1675 -17 259 -129 C ATOM 605 O ASN A 71 -0.125 9.160 19.826 1.00 15.46 O ANISOU 605 O ASN A 71 1561 2264 2049 -104 430 -151 O ATOM 606 CB ASN A 71 -0.649 10.123 22.311 1.00 17.06 C ANISOU 606 CB ASN A 71 1808 2541 2132 -239 354 -540 C ATOM 607 CG ASN A 71 0.116 8.946 22.865 1.00 17.37 C ANISOU 607 CG ASN A 71 1930 3058 1611 -299 132 -275 C ATOM 608 OD1 ASN A 71 -0.481 7.931 23.210 1.00 19.27 O ANISOU 608 OD1 ASN A 71 1770 3241 2311 -274 10 417 O ATOM 609 ND2 ASN A 71 1.429 9.087 22.963 1.00 18.49 N ANISOU 609 ND2 ASN A 71 1853 2850 2323 -316 114 -49 N ATOM 610 N CYS A 72 -2.131 8.233 19.523 1.00 14.76 N ANISOU 610 N CYS A 72 1413 2519 1676 33 305 -246 N ATOM 611 CA CYS A 72 -1.795 7.571 18.292 1.00 13.49 C ANISOU 611 CA CYS A 72 1411 2145 1570 17 218 -42 C ATOM 612 C CYS A 72 -2.361 8.281 17.088 1.00 13.03 C ANISOU 612 C CYS A 72 1253 2097 1599 7 261 -30 C ATOM 613 O CYS A 72 -3.375 9.006 17.181 1.00 14.44 O ANISOU 613 O CYS A 72 1513 2075 1897 87 257 -34 O ATOM 614 CB ACYS A 72 -2.164 6.097 18.234 0.87 14.29 C ANISOU 614 CB ACYS A 72 1639 2153 1636 -16 194 6 C ATOM 615 CB BCYS A 72 -2.289 6.169 18.606 0.13 13.16 C ANISOU 615 CB BCYS A 72 1266 2248 1487 60 290 81 C ATOM 616 SG ACYS A 72 -1.037 4.991 19.125 0.87 14.31 S ANISOU 616 SG ACYS A 72 1488 2103 1848 7 279 -60 S ATOM 617 SG BCYS A 72 -1.432 5.870 20.246 0.13 12.56 S ANISOU 617 SG BCYS A 72 1574 1636 1561 -23 51 -150 S ATOM 618 N TYR A 73 -1.739 8.093 15.971 1.00 12.91 N ANISOU 618 N TYR A 73 1450 1927 1527 90 176 11 N ATOM 619 CA TYR A 73 -2.042 8.788 14.736 1.00 13.25 C ANISOU 619 CA TYR A 73 1570 1881 1585 170 171 0 C ATOM 620 C TYR A 73 -1.854 7.783 13.601 1.00 13.30 C ANISOU 620 C TYR A 73 1666 1841 1545 124 148 83 C ATOM 621 O TYR A 73 -0.875 7.055 13.540 1.00 14.66 O ANISOU 621 O TYR A 73 1660 2061 1850 265 57 -154 O ATOM 622 CB TYR A 73 -1.134 10.000 14.496 1.00 15.12 C ANISOU 622 CB TYR A 73 2056 1824 1865 46 291 24 C ATOM 623 CG TYR A 73 -1.372 11.054 15.549 1.00 15.03 C ANISOU 623 CG TYR A 73 1822 1868 2022 54 479 -88 C ATOM 624 CD1 TYR A 73 -0.690 11.015 16.751 1.00 16.58 C ANISOU 624 CD1 TYR A 73 2170 2067 2062 -314 251 -76 C ATOM 625 CD2 TYR A 73 -2.315 12.032 15.352 1.00 18.96 C ANISOU 625 CD2 TYR A 73 2303 2085 2817 338 304 -168 C ATOM 626 CE1 TYR A 73 -0.970 11.903 17.769 1.00 21.37 C ANISOU 626 CE1 TYR A 73 3071 2830 2218 -734 566 -546 C ATOM 627 CE2 TYR A 73 -2.556 12.938 16.338 1.00 22.60 C ANISOU 627 CE2 TYR A 73 2181 2333 4073 88 701 -888 C ATOM 628 CZ TYR A 73 -1.898 12.896 17.520 1.00 23.36 C ANISOU 628 CZ TYR A 73 2597 2876 3404 -492 1114 -1254 C ATOM 629 OH TYR A 73 -2.332 13.953 18.289 1.00 33.98 O ANISOU 629 OH TYR A 73 4271 3527 5111 -873 2065 -2364 O ATOM 630 N GLN A 74 -2.819 7.805 12.692 1.00 15.25 N ANISOU 630 N GLN A 74 1770 2346 1678 357 47 -132 N ATOM 631 CA GLN A 74 -2.818 6.986 11.508 1.00 14.26 C ANISOU 631 CA GLN A 74 1573 2214 1629 322 42 0 C ATOM 632 C GLN A 74 -2.491 7.844 10.277 1.00 14.47 C ANISOU 632 C GLN A 74 1784 2057 1656 257 -20 56 C ATOM 633 O GLN A 74 -3.019 8.917 10.081 1.00 16.61 O ANISOU 633 O GLN A 74 2188 2117 2008 437 62 149 O ATOM 634 CB GLN A 74 -4.191 6.368 11.328 1.00 16.35 C ANISOU 634 CB GLN A 74 1772 2650 1791 -45 3 142 C ATOM 635 CG GLN A 74 -4.245 5.458 10.122 1.00 19.09 C ANISOU 635 CG GLN A 74 2288 2940 2025 -2 -268 -189 C ATOM 636 CD GLN A 74 -5.553 4.714 10.005 1.00 27.97 C ANISOU 636 CD GLN A 74 2629 4592 3407 -728 -36 -1193 C ATOM 637 OE1 GLN A 74 -6.131 4.272 10.994 1.00 39.30 O ANISOU 637 OE1 GLN A 74 3075 7336 4523 -1765 1050 -1171 O ATOM 638 NE2 GLN A 74 -5.922 4.458 8.767 1.00 43.03 N ANISOU 638 NE2 GLN A 74 3509 8780 4061 -1218 -1286 -1344 N ATOM 639 N SER A 75 -1.621 7.276 9.442 1.00 14.06 N ANISOU 639 N SER A 75 1709 1956 1676 152 -15 95 N ATOM 640 CA SER A 75 -1.254 8.001 8.250 1.00 14.63 C ANISOU 640 CA SER A 75 1856 2116 1585 103 -54 83 C ATOM 641 C SER A 75 -2.448 8.091 7.294 1.00 15.79 C ANISOU 641 C SER A 75 2029 2260 1711 216 -91 158 C ATOM 642 O SER A 75 -3.181 7.128 7.104 1.00 17.67 O ANISOU 642 O SER A 75 2087 2581 2047 -7 -375 103 O ATOM 643 CB SER A 75 -0.074 7.313 7.578 1.00 14.55 C ANISOU 643 CB SER A 75 1859 1952 1719 7 15 81 C ATOM 644 OG SER A 75 -0.346 6.017 7.173 1.00 15.46 O ANISOU 644 OG SER A 75 2067 2134 1674 62 -137 8 O ATOM 645 N TYR A 76 -2.532 9.210 6.617 1.00 17.08 N ANISOU 645 N TYR A 76 2239 2273 1978 434 -164 211 N ATOM 646 CA TYR A 76 -3.551 9.372 5.588 1.00 18.90 C ANISOU 646 CA TYR A 76 2394 2793 1994 612 -194 300 C ATOM 647 C TYR A 76 -3.275 8.486 4.390 1.00 20.30 C ANISOU 647 C TYR A 76 2652 3073 1988 468 -333 189 C ATOM 648 O TYR A 76 -4.208 8.003 3.736 1.00 26.98 O ANISOU 648 O TYR A 76 3134 4476 2642 578 -909 -499 O ATOM 649 CB TYR A 76 -3.650 10.840 5.156 1.00 23.63 C ANISOU 649 CB TYR A 76 3528 3006 2444 1225 -75 580 C ATOM 650 CG TYR A 76 -4.168 11.797 6.195 1.00 26.62 C ANISOU 650 CG TYR A 76 3979 3299 2834 1983 -525 379 C ATOM 651 CD1 TYR A 76 -5.296 11.486 6.948 1.00 32.63 C ANISOU 651 CD1 TYR A 76 5049 4425 2923 2356 508 313 C ATOM 652 CD2 TYR A 76 -3.642 13.072 6.318 1.00 32.76 C ANISOU 652 CD2 TYR A 76 4950 3272 4224 2020 -1115 -187 C ATOM 653 CE1 TYR A 76 -5.856 12.328 7.893 1.00 36.83 C ANISOU 653 CE1 TYR A 76 6451 4693 2848 2964 420 243 C ATOM 654 CE2 TYR A 76 -4.197 13.920 7.252 1.00 37.07 C ANISOU 654 CE2 TYR A 76 5040 4144 4900 2563 -1491 -941 C ATOM 655 CZ TYR A 76 -5.276 13.565 8.015 1.00 37.20 C ANISOU 655 CZ TYR A 76 5514 5133 3489 3057 -1516 -529 C ATOM 656 OH TYR A 76 -5.791 14.479 8.927 1.00 43.50 O ANISOU 656 OH TYR A 76 5791 5945 4792 3479 -1577 -1469 O ATOM 657 N SER A 77 -2.017 8.247 4.077 1.00 20.31 N ANISOU 657 N SER A 77 2855 2802 2059 829 -257 31 N ATOM 658 CA SER A 77 -1.636 7.454 2.920 1.00 22.18 C ANISOU 658 CA SER A 77 3625 3051 1752 945 -260 107 C ATOM 659 C SER A 77 -0.997 6.146 3.350 1.00 17.50 C ANISOU 659 C SER A 77 2165 2926 1558 557 -249 -1 C ATOM 660 O SER A 77 -0.545 5.980 4.445 1.00 18.05 O ANISOU 660 O SER A 77 2579 2701 1576 428 -330 -49 O ATOM 661 CB ASER A 77 -0.687 8.289 2.078 0.25 29.16 C ANISOU 661 CB ASER A 77 5863 2625 2593 715 1138 -73 C ATOM 662 CB BSER A 77 -0.707 8.236 2.015 0.37 28.18 C ANISOU 662 CB BSER A 77 5389 2881 2438 843 800 173 C ATOM 663 CB CSER A 77 -0.617 8.231 2.099 0.39 29.74 C ANISOU 663 CB CSER A 77 5819 2819 2663 736 1204 120 C ATOM 664 OG ASER A 77 0.003 7.541 1.102 0.25 35.24 O ANISOU 664 OG ASER A 77 8006 3620 1764 1512 1719 476 O ATOM 665 OG BSER A 77 0.536 8.479 2.654 0.37 45.09 O ANISOU 665 OG BSER A 77 5602 6442 5087 -1862 1017 -1373 O ATOM 666 OG CSER A 77 -1.223 9.482 1.686 0.39 46.55 O ANISOU 666 OG CSER A 77 11720 2657 3311 1680 941 562 O ATOM 667 N THR A 78 -0.989 5.173 2.459 1.00 17.88 N ANISOU 667 N THR A 78 1991 3067 1735 468 -402 -183 N ATOM 668 CA THR A 78 -0.245 3.955 2.704 1.00 17.65 C ANISOU 668 CA THR A 78 1904 2940 1863 377 -344 -142 C ATOM 669 C THR A 78 1.237 4.244 2.491 1.00 16.17 C ANISOU 669 C THR A 78 2044 2435 1665 294 -252 74 C ATOM 670 O THR A 78 1.643 5.187 1.809 1.00 19.51 O ANISOU 670 O THR A 78 2447 2850 2116 414 -128 578 O ATOM 671 CB THR A 78 -0.673 2.770 1.827 1.00 19.95 C ANISOU 671 CB THR A 78 2298 3193 2088 162 -301 -481 C ATOM 672 OG1 THR A 78 -0.463 3.132 0.465 1.00 24.06 O ANISOU 672 OG1 THR A 78 3252 3829 2060 165 -361 -447 O ATOM 673 CG2 THR A 78 -2.137 2.421 1.968 1.00 25.60 C ANISOU 673 CG2 THR A 78 2583 4493 2651 -461 -569 -449 C ATOM 674 N MET A 79 2.045 3.415 3.127 1.00 14.75 N ANISOU 674 N MET A 79 1747 2116 1743 47 -104 44 N ATOM 675 CA MET A 79 3.475 3.489 3.108 1.00 14.10 C ANISOU 675 CA MET A 79 1691 2020 1648 21 -11 29 C ATOM 676 C MET A 79 4.090 2.136 2.797 1.00 13.23 C ANISOU 676 C MET A 79 1687 1914 1424 -50 -108 75 C ATOM 677 O MET A 79 3.515 1.104 3.139 1.00 14.81 O ANISOU 677 O MET A 79 1838 2014 1776 -57 81 65 O ATOM 678 CB MET A 79 4.016 4.014 4.466 1.00 14.86 C ANISOU 678 CB MET A 79 1822 2223 1601 -20 17 -141 C ATOM 679 CG MET A 79 3.610 5.501 4.657 1.00 18.33 C ANISOU 679 CG MET A 79 2259 2549 2157 475 -381 -475 C ATOM 680 SD MET A 79 4.379 6.127 6.120 1.00 18.93 S ANISOU 680 SD MET A 79 2753 2505 1935 -88 -82 -286 S ATOM 681 CE MET A 79 3.806 7.805 6.046 1.00 24.24 C ANISOU 681 CE MET A 79 3740 2736 2735 663 -100 -988 C ATOM 682 N SER A 80 5.263 2.156 2.218 1.00 13.28 N ANISOU 682 N SER A 80 1701 1885 1461 53 -51 126 N ATOM 683 CA SER A 80 6.018 0.930 1.991 1.00 13.21 C ANISOU 683 CA SER A 80 1818 1933 1269 56 -76 68 C ATOM 684 C SER A 80 6.657 0.456 3.269 1.00 12.31 C ANISOU 684 C SER A 80 1597 1856 1225 -20 -82 47 C ATOM 685 O SER A 80 7.406 1.237 3.878 1.00 13.69 O ANISOU 685 O SER A 80 1784 1958 1461 -69 -150 -2 O ATOM 686 CB SER A 80 7.085 1.208 0.966 1.00 14.65 C ANISOU 686 CB SER A 80 2002 2251 1313 24 153 56 C ATOM 687 OG SER A 80 7.859 0.013 0.789 1.00 17.73 O ANISOU 687 OG SER A 80 2312 2573 1852 228 350 -59 O ATOM 688 N ILE A 81 6.343 -0.743 3.704 1.00 12.31 N ANISOU 688 N ILE A 81 1699 1757 1222 89 -127 -75 N ATOM 689 CA ILE A 81 6.830 -1.298 4.925 1.00 12.01 C ANISOU 689 CA ILE A 81 1721 1733 1111 61 -75 -114 C ATOM 690 C ILE A 81 7.343 -2.709 4.694 1.00 12.06 C ANISOU 690 C ILE A 81 1812 1622 1150 21 -60 -114 C ATOM 691 O ILE A 81 6.971 -3.427 3.752 1.00 13.59 O ANISOU 691 O ILE A 81 2027 1840 1295 126 -272 -274 O ATOM 692 CB ILE A 81 5.777 -1.267 6.061 1.00 13.32 C ANISOU 692 CB ILE A 81 1801 2022 1239 161 13 -106 C ATOM 693 CG1 ILE A 81 4.620 -2.168 5.780 1.00 15.37 C ANISOU 693 CG1 ILE A 81 1850 2176 1815 -41 125 -98 C ATOM 694 CG2 ILE A 81 5.352 0.178 6.354 1.00 15.78 C ANISOU 694 CG2 ILE A 81 2178 2149 1670 406 87 -360 C ATOM 695 CD1 ILE A 81 3.739 -2.384 7.002 1.00 21.52 C ANISOU 695 CD1 ILE A 81 2259 3782 2134 -650 259 98 C ATOM 696 N THR A 82 8.191 -3.150 5.628 1.00 12.04 N ANISOU 696 N THR A 82 1818 1564 1191 74 -102 -178 N ATOM 697 CA THR A 82 8.634 -4.503 5.715 1.00 11.92 C ANISOU 697 CA THR A 82 1809 1509 1209 -26 -28 -95 C ATOM 698 C THR A 82 8.318 -5.066 7.089 1.00 11.89 C ANISOU 698 C THR A 82 1673 1570 1276 0 69 -133 C ATOM 699 O THR A 82 8.688 -4.448 8.094 1.00 13.21 O ANISOU 699 O THR A 82 2101 1721 1197 -215 -54 -118 O ATOM 700 CB THR A 82 10.134 -4.658 5.463 1.00 12.45 C ANISOU 700 CB THR A 82 1800 1664 1265 8 80 -63 C ATOM 701 OG1 THR A 82 10.397 -4.218 4.127 1.00 13.97 O ANISOU 701 OG1 THR A 82 2272 1718 1318 42 277 -82 O ATOM 702 CG2 THR A 82 10.627 -6.066 5.633 1.00 15.04 C ANISOU 702 CG2 THR A 82 2082 1686 1947 178 327 181 C ATOM 703 N ASP A 83 7.626 -6.181 7.152 1.00 12.27 N ANISOU 703 N ASP A 83 1816 1614 1231 -108 -49 -81 N ATOM 704 CA ASP A 83 7.378 -6.916 8.384 1.00 12.88 C ANISOU 704 CA ASP A 83 1803 1646 1443 -104 203 -122 C ATOM 705 C ASP A 83 8.431 -7.976 8.555 1.00 12.42 C ANISOU 705 C ASP A 83 1842 1516 1362 -123 130 -32 C ATOM 706 O ASP A 83 8.755 -8.720 7.636 1.00 14.33 O ANISOU 706 O ASP A 83 2308 1777 1360 202 -60 -219 O ATOM 707 CB AASP A 83 5.982 -7.531 8.159 0.46 17.07 C ANISOU 707 CB AASP A 83 1636 2562 2287 -239 371 10 C ATOM 708 CB BASP A 83 5.981 -7.514 8.466 0.54 15.49 C ANISOU 708 CB BASP A 83 1766 2196 1924 -125 68 412 C ATOM 709 CG AASP A 83 5.495 -8.349 9.323 0.46 19.71 C ANISOU 709 CG AASP A 83 1960 2852 2676 -412 694 137 C ATOM 710 CG BASP A 83 4.923 -6.465 8.753 0.54 18.23 C ANISOU 710 CG BASP A 83 1745 2117 3064 -144 10 109 C ATOM 711 OD1AASP A 83 4.865 -7.786 10.218 0.46 27.56 O ANISOU 711 OD1AASP A 83 4476 2789 3208 -1044 1955 -326 O ATOM 712 OD1BASP A 83 5.123 -5.473 9.459 0.54 22.58 O ANISOU 712 OD1BASP A 83 2219 2104 4258 -162 -270 -266 O ATOM 713 OD2AASP A 83 5.762 -9.557 9.356 0.46 25.12 O ANISOU 713 OD2AASP A 83 3909 2597 3039 -800 1433 93 O ATOM 714 OD2BASP A 83 3.818 -6.749 8.252 0.54 25.98 O ANISOU 714 OD2BASP A 83 1931 3371 4568 216 -555 -962 O ATOM 715 N CYS A 84 8.933 -8.069 9.773 1.00 12.40 N ANISOU 715 N CYS A 84 1935 1529 1246 -63 200 -43 N ATOM 716 CA CYS A 84 9.908 -9.070 10.141 1.00 12.50 C ANISOU 716 CA CYS A 84 2062 1440 1249 1 156 -76 C ATOM 717 C CYS A 84 9.336 -9.897 11.296 1.00 13.52 C ANISOU 717 C CYS A 84 2220 1655 1261 -19 131 -3 C ATOM 718 O CYS A 84 8.948 -9.310 12.305 1.00 17.05 O ANISOU 718 O CYS A 84 3302 1747 1428 -36 632 -23 O ATOM 719 CB CYS A 84 11.185 -8.393 10.625 1.00 13.09 C ANISOU 719 CB CYS A 84 1941 1721 1312 109 170 -192 C ATOM 720 SG CYS A 84 12.001 -7.339 9.425 1.00 13.41 S ANISOU 720 SG CYS A 84 2052 1523 1521 -32 126 -66 S ATOM 721 N ARG A 85 9.290 -11.191 11.152 1.00 14.14 N ANISOU 721 N ARG A 85 2325 1558 1488 -84 236 80 N ATOM 722 CA ARG A 85 8.719 -12.074 12.199 1.00 15.78 C ANISOU 722 CA ARG A 85 2410 1699 1886 -33 425 246 C ATOM 723 C ARG A 85 9.680 -13.224 12.404 1.00 13.82 C ANISOU 723 C ARG A 85 2121 1598 1532 -104 390 81 C ATOM 724 O ARG A 85 10.168 -13.849 11.469 1.00 15.09 O ANISOU 724 O ARG A 85 2516 1796 1420 -52 294 43 O ATOM 725 CB AARG A 85 7.353 -12.600 11.755 0.59 23.43 C ATOM 726 CB BARG A 85 7.437 -12.714 11.545 0.41 18.11 C ATOM 727 CG AARG A 85 6.332 -12.578 12.882 0.59 52.78 C ATOM 728 CG BARG A 85 6.638 -13.608 12.496 0.41 26.82 C ATOM 729 CD AARG A 85 5.345 -11.454 12.622 0.59 69.54 C ATOM 730 CD BARG A 85 5.228 -13.677 11.872 0.41 33.73 C ATOM 731 NE AARG A 85 4.687 -11.543 11.312 0.59 64.49 N ATOM 732 NE BARG A 85 4.887 -12.343 11.333 0.41 52.30 N ATOM 733 CZ AARG A 85 3.672 -10.741 11.005 0.59 80.89 C ATOM 734 CZ BARG A 85 4.507 -11.344 12.134 0.41 74.55 C ATOM 735 NH1AARG A 85 3.248 -9.840 11.892 0.59 63.79 N ATOM 736 NH1BARG A 85 4.410 -11.506 13.450 0.41 98.95 N ATOM 737 NH2AARG A 85 3.102 -10.851 9.812 0.59131.00 N ATOM 738 NH2BARG A 85 4.237 -10.150 11.631 0.41 37.56 N ATOM 739 N GLU A 86 9.917 -13.556 13.647 1.00 14.49 N ANISOU 739 N GLU A 86 2290 1674 1540 -112 415 51 N ATOM 740 CA GLU A 86 10.873 -14.612 13.996 1.00 14.56 C ANISOU 740 CA GLU A 86 2368 1636 1529 -249 244 195 C ATOM 741 C GLU A 86 10.386 -15.938 13.452 1.00 15.93 C ANISOU 741 C GLU A 86 2259 1598 2196 -199 -5 337 C ATOM 742 O GLU A 86 9.216 -16.273 13.552 1.00 19.83 O ANISOU 742 O GLU A 86 2397 1926 3213 -468 105 231 O ATOM 743 CB GLU A 86 10.957 -14.633 15.535 1.00 19.26 C ANISOU 743 CB GLU A 86 2980 2835 1505 -164 288 421 C ATOM 744 CG GLU A 86 12.117 -15.352 16.050 1.00 20.69 C ANISOU 744 CG GLU A 86 3098 3194 1570 75 53 54 C ATOM 745 CD GLU A 86 12.298 -15.225 17.534 1.00 18.43 C ANISOU 745 CD GLU A 86 2895 2514 1592 -305 150 205 C ATOM 746 OE1 GLU A 86 11.331 -14.906 18.277 1.00 22.18 O ANISOU 746 OE1 GLU A 86 3376 3340 1712 21 484 189 O ATOM 747 OE2 GLU A 86 13.385 -15.566 17.914 1.00 18.29 O ANISOU 747 OE2 GLU A 86 2914 2375 1662 -466 -91 -158 O ATOM 748 N THR A 87 11.312 -16.719 12.913 1.00 16.80 N ANISOU 748 N THR A 87 2533 1379 2473 -123 -158 79 N ATOM 749 CA THR A 87 10.999 -18.046 12.429 1.00 17.43 C ANISOU 749 CA THR A 87 2861 1547 2215 -321 -245 55 C ATOM 750 C THR A 87 11.245 -19.090 13.473 1.00 15.24 C ANISOU 750 C THR A 87 2232 1440 2117 -154 244 27 C ATOM 751 O THR A 87 11.836 -18.862 14.495 1.00 16.53 O ANISOU 751 O THR A 87 2797 1534 1951 -259 144 -44 O ATOM 752 CB THR A 87 11.806 -18.423 11.201 1.00 19.53 C ANISOU 752 CB THR A 87 3557 1993 1872 -872 74 -16 C ATOM 753 OG1 THR A 87 13.148 -18.622 11.625 1.00 21.28 O ANISOU 753 OG1 THR A 87 3320 2498 2266 -641 476 -209 O ATOM 754 CG2 THR A 87 11.736 -17.293 10.194 1.00 27.16 C ANISOU 754 CG2 THR A 87 6022 2200 2097 -390 -11 157 C ATOM 755 N GLY A 88 10.776 -20.315 13.121 1.00 17.02 N ANISOU 755 N GLY A 88 2529 1548 2388 -417 165 -72 N ATOM 756 CA GLY A 88 10.899 -21.414 14.055 1.00 17.43 C ANISOU 756 CA GLY A 88 2610 1558 2455 -487 328 26 C ATOM 757 C GLY A 88 12.272 -21.844 14.323 1.00 17.28 C ANISOU 757 C GLY A 88 2712 1716 2140 -632 144 324 C ATOM 758 O GLY A 88 12.503 -22.509 15.308 1.00 23.91 O ANISOU 758 O GLY A 88 3482 2919 2683 -733 -208 1034 O ATOM 759 N SER A 89 13.244 -21.530 13.478 1.00 16.12 N ANISOU 759 N SER A 89 2499 1562 2062 -175 135 -88 N ATOM 760 CA SER A 89 14.630 -21.861 13.658 1.00 18.87 C ANISOU 760 CA SER A 89 2521 1878 2770 -139 -46 -347 C ATOM 761 C SER A 89 15.437 -20.807 14.377 1.00 18.93 C ANISOU 761 C SER A 89 2563 1873 2758 -157 -85 -286 C ATOM 762 O SER A 89 16.631 -20.984 14.605 1.00 25.26 O ANISOU 762 O SER A 89 2684 2383 4531 149 -608 -1020 O ATOM 763 CB ASER A 89 15.297 -22.098 12.305 0.78 22.72 C ANISOU 763 CB ASER A 89 2451 2952 3231 -70 125 -1064 C ATOM 764 CB BSER A 89 15.264 -22.270 12.326 0.22 18.05 C ANISOU 764 CB BSER A 89 2368 1075 3415 -735 559 -499 C ATOM 765 OG ASER A 89 14.711 -23.298 11.791 0.78 24.61 O ANISOU 765 OG ASER A 89 2624 2965 3762 104 110 -1490 O ATOM 766 OG BSER A 89 15.101 -21.283 11.317 0.22 32.04 O ANISOU 766 OG BSER A 89 2356 6262 3554 209 -79 1887 O ATOM 767 N SER A 90 14.794 -19.684 14.728 1.00 16.22 N ANISOU 767 N SER A 90 2502 1724 1938 -260 -5 -55 N ATOM 768 CA SER A 90 15.516 -18.631 15.439 1.00 16.17 C ANISOU 768 CA SER A 90 2785 1737 1622 -430 1 60 C ATOM 769 C SER A 90 15.918 -19.093 16.822 1.00 18.73 C ANISOU 769 C SER A 90 3088 2151 1876 -755 -268 322 C ATOM 770 O SER A 90 15.069 -19.603 17.548 1.00 21.74 O ANISOU 770 O SER A 90 3313 2923 2025 -911 -240 704 O ATOM 771 CB SER A 90 14.540 -17.481 15.529 1.00 16.84 C ANISOU 771 CB SER A 90 2706 1568 2123 -537 176 -46 C ATOM 772 OG SER A 90 15.152 -16.374 16.191 1.00 16.65 O ANISOU 772 OG SER A 90 2717 1745 1864 -597 76 33 O ATOM 773 N LYS A 91 17.155 -18.864 17.184 1.00 17.31 N ANISOU 773 N LYS A 91 3001 1813 1762 -409 -202 90 N ATOM 774 CA LYS A 91 17.674 -19.220 18.502 1.00 19.85 C ANISOU 774 CA LYS A 91 3587 2160 1794 -349 -451 136 C ATOM 775 C LYS A 91 18.805 -18.301 18.844 1.00 19.30 C ANISOU 775 C LYS A 91 3199 2486 1650 -246 -332 19 C ATOM 776 O LYS A 91 19.840 -18.309 18.182 1.00 21.25 O ANISOU 776 O LYS A 91 3221 2794 2059 -26 -54 -193 O ATOM 777 CB LYS A 91 18.123 -20.687 18.526 1.00 23.48 C ANISOU 777 CB LYS A 91 3818 2288 2815 -49 -866 158 C ATOM 778 CG LYS A 91 18.486 -21.187 19.899 1.00 29.41 C ANISOU 778 CG LYS A 91 4820 3044 3309 393 -987 694 C ATOM 779 CD LYS A 91 18.974 -22.634 19.815 1.00 38.11 C ANISOU 779 CD LYS A 91 6808 2960 4710 682 -626 1298 C ATOM 780 CE LYS A 91 19.431 -23.096 21.181 1.00 48.70 C ANISOU 780 CE LYS A 91 8417 4558 5527 1540 -1447 2020 C ATOM 781 NZ LYS A 91 20.827 -22.734 21.540 1.00 97.12 N ANISOU 781 NZ LYS A 91 14305 7144 15453 -5019 -9790 5704 N ATOM 782 N TYR A 92 18.572 -17.486 19.863 1.00 18.00 N ANISOU 782 N TYR A 92 2615 2282 1940 -136 -234 63 N ATOM 783 CA TYR A 92 19.557 -16.487 20.261 1.00 16.71 C ANISOU 783 CA TYR A 92 2181 2293 1876 65 -235 -101 C ATOM 784 C TYR A 92 20.939 -17.145 20.451 1.00 17.63 C ANISOU 784 C TYR A 92 2364 2490 1846 399 -156 -55 C ATOM 785 O TYR A 92 21.008 -18.195 21.087 1.00 21.11 O ANISOU 785 O TYR A 92 3170 2590 2262 473 -267 39 O ATOM 786 CB TYR A 92 19.123 -15.864 21.593 1.00 16.54 C ANISOU 786 CB TYR A 92 2141 2244 1900 -3 14 -4 C ATOM 787 CG TYR A 92 20.017 -14.754 22.028 1.00 16.01 C ANISOU 787 CG TYR A 92 2228 2213 1644 1 -73 51 C ATOM 788 CD1 TYR A 92 19.884 -13.488 21.556 1.00 15.79 C ANISOU 788 CD1 TYR A 92 2047 2122 1830 121 -70 -71 C ATOM 789 CD2 TYR A 92 21.026 -15.018 22.953 1.00 17.51 C ANISOU 789 CD2 TYR A 92 2415 2507 1733 232 -254 31 C ATOM 790 CE1 TYR A 92 20.706 -12.439 21.926 1.00 18.29 C ANISOU 790 CE1 TYR A 92 2304 2203 2441 -123 45 -339 C ATOM 791 CE2 TYR A 92 21.835 -14.002 23.315 1.00 20.66 C ANISOU 791 CE2 TYR A 92 2739 3098 2013 86 -449 -545 C ATOM 792 CZ TYR A 92 21.710 -12.738 22.874 1.00 18.80 C ANISOU 792 CZ TYR A 92 2109 2742 2292 -173 92 -763 C ATOM 793 OH TYR A 92 22.581 -11.739 23.309 1.00 27.08 O ANISOU 793 OH TYR A 92 2772 3841 3676 -950 -54 -1283 O ATOM 794 N PRO A 93 22.015 -16.542 19.967 1.00 19.03 N ANISOU 794 N PRO A 93 2222 2831 2180 253 -184 -354 N ATOM 795 CA PRO A 93 22.103 -15.236 19.365 1.00 19.23 C ANISOU 795 CA PRO A 93 2111 2866 2327 -26 -35 -270 C ATOM 796 C PRO A 93 21.866 -15.177 17.880 1.00 19.25 C ANISOU 796 C PRO A 93 2126 2981 2206 -128 163 -230 C ATOM 797 O PRO A 93 21.991 -14.101 17.289 1.00 22.86 O ANISOU 797 O PRO A 93 3140 3041 2506 -183 255 -75 O ATOM 798 CB PRO A 93 23.522 -14.773 19.663 1.00 23.72 C ANISOU 798 CB PRO A 93 2218 3987 2809 -397 -165 -246 C ATOM 799 CG PRO A 93 24.317 -16.059 19.629 1.00 29.72 C ANISOU 799 CG PRO A 93 2177 4971 4143 401 120 254 C ATOM 800 CD PRO A 93 23.383 -17.078 20.250 1.00 22.91 C ANISOU 800 CD PRO A 93 2297 3891 2517 705 -190 -233 C ATOM 801 N ASN A 94 21.549 -16.338 17.308 1.00 19.13 N ANISOU 801 N ASN A 94 2505 2776 1988 442 40 -142 N ATOM 802 CA ASN A 94 21.313 -16.452 15.874 1.00 20.93 C ANISOU 802 CA ASN A 94 2546 3318 2088 389 -110 -371 C ATOM 803 C ASN A 94 19.829 -16.309 15.579 1.00 18.32 C ANISOU 803 C ASN A 94 2483 2642 1835 63 70 -443 C ATOM 804 O ASN A 94 19.097 -17.263 15.263 1.00 19.15 O ANISOU 804 O ASN A 94 2713 2423 2141 186 -106 -339 O ATOM 805 CB ASN A 94 21.881 -17.764 15.316 1.00 27.49 C ANISOU 805 CB ASN A 94 3167 4399 2880 1050 76 -1248 C ATOM 806 CG ASN A 94 23.378 -17.913 15.568 1.00 34.60 C ANISOU 806 CG ASN A 94 3255 5086 4804 1324 -116 -1601 C ATOM 807 OD1 ASN A 94 23.847 -18.889 16.193 1.00 53.34 O ANISOU 807 OD1 ASN A 94 4124 6223 9919 2354 -461 233 O ATOM 808 ND2 ASN A 94 24.120 -16.899 15.147 1.00 43.95 N ANISOU 808 ND2 ASN A 94 3056 7425 6216 802 844 -166 N ATOM 809 N CYS A 95 19.414 -15.076 15.792 1.00 17.60 N ANISOU 809 N CYS A 95 2197 2543 1947 11 -41 -282 N ATOM 810 CA CYS A 95 18.070 -14.681 15.545 1.00 16.11 C ANISOU 810 CA CYS A 95 2338 2202 1582 -180 -59 -149 C ATOM 811 C CYS A 95 17.700 -14.721 14.067 1.00 16.03 C ANISOU 811 C CYS A 95 2372 2200 1518 -271 23 100 C ATOM 812 O CYS A 95 18.499 -14.288 13.250 1.00 21.92 O ANISOU 812 O CYS A 95 2819 3746 1762 -986 356 -58 O ATOM 813 CB CYS A 95 17.686 -13.342 16.131 1.00 15.89 C ANISOU 813 CB CYS A 95 2352 2043 1641 -64 75 51 C ATOM 814 SG CYS A 95 18.135 -13.122 17.840 1.00 15.62 S ANISOU 814 SG CYS A 95 2172 2035 1729 -172 -70 -108 S ATOM 815 N ALA A 96 16.593 -15.253 13.642 1.00 14.48 N ANISOU 815 N ALA A 96 2261 1761 1480 -90 46 -75 N ATOM 816 CA ALA A 96 16.223 -15.479 12.294 1.00 15.00 C ANISOU 816 CA ALA A 96 2417 1929 1353 38 91 -94 C ATOM 817 C ALA A 96 14.772 -15.036 12.073 1.00 13.44 C ANISOU 817 C ALA A 96 2230 1500 1377 -268 111 4 C ATOM 818 O ALA A 96 13.905 -15.282 12.891 1.00 14.66 O ANISOU 818 O ALA A 96 2328 1781 1463 -301 152 217 O ATOM 819 CB ALA A 96 16.359 -16.971 11.948 1.00 19.28 C ANISOU 819 CB ALA A 96 3381 2175 1769 640 -267 -442 C ATOM 820 N TYR A 97 14.572 -14.417 10.914 1.00 13.71 N ANISOU 820 N TYR A 97 2289 1629 1292 -53 242 24 N ATOM 821 CA TYR A 97 13.332 -13.738 10.601 1.00 13.59 C ANISOU 821 CA TYR A 97 2271 1491 1402 -100 182 -102 C ATOM 822 C TYR A 97 12.877 -14.037 9.203 1.00 13.53 C ANISOU 822 C TYR A 97 2370 1554 1218 -213 205 17 C ATOM 823 O TYR A 97 13.660 -14.190 8.275 1.00 15.85 O ANISOU 823 O TYR A 97 2476 2234 1311 -213 193 -137 O ATOM 824 CB TYR A 97 13.533 -12.178 10.676 1.00 13.62 C ANISOU 824 CB TYR A 97 2337 1503 1336 -127 150 -17 C ATOM 825 CG TYR A 97 13.857 -11.779 12.078 1.00 13.01 C ANISOU 825 CG TYR A 97 2150 1453 1340 -213 129 5 C ATOM 826 CD1 TYR A 97 12.817 -11.525 12.972 1.00 13.78 C ANISOU 826 CD1 TYR A 97 2098 1661 1478 -184 137 -96 C ATOM 827 CD2 TYR A 97 15.152 -11.690 12.566 1.00 13.21 C ANISOU 827 CD2 TYR A 97 2103 1501 1417 -203 213 -12 C ATOM 828 CE1 TYR A 97 13.082 -11.215 14.292 1.00 14.08 C ANISOU 828 CE1 TYR A 97 2132 1876 1342 -158 224 -41 C ATOM 829 CE2 TYR A 97 15.418 -11.414 13.897 1.00 13.60 C ANISOU 829 CE2 TYR A 97 2145 1604 1419 -114 113 -101 C ATOM 830 CZ TYR A 97 14.376 -11.179 14.752 1.00 13.47 C ANISOU 830 CZ TYR A 97 2164 1634 1321 -146 141 32 C ATOM 831 OH TYR A 97 14.656 -10.903 16.054 1.00 16.14 O ANISOU 831 OH TYR A 97 2439 2322 1371 48 51 -167 O ATOM 832 N LYS A 98 11.569 -14.052 9.031 1.00 13.96 N ANISOU 832 N LYS A 98 2384 1570 1348 -145 154 -79 N ATOM 833 CA LYS A 98 10.869 -14.029 7.762 1.00 14.25 C ANISOU 833 CA LYS A 98 2465 1581 1367 -79 47 -58 C ATOM 834 C LYS A 98 10.591 -12.581 7.385 1.00 13.61 C ANISOU 834 C LYS A 98 2265 1558 1346 -143 91 -178 C ATOM 835 O LYS A 98 10.100 -11.813 8.180 1.00 15.52 O ANISOU 835 O LYS A 98 2790 1636 1469 28 201 -144 O ATOM 836 CB LYS A 98 9.566 -14.800 7.832 1.00 18.04 C ANISOU 836 CB LYS A 98 2951 1875 2030 -630 -230 -28 C ATOM 837 CG LYS A 98 8.852 -14.829 6.512 1.00 24.74 C ANISOU 837 CG LYS A 98 3615 2958 2826 -666 -1081 443 C ATOM 838 CD LYS A 98 7.584 -15.668 6.558 1.00 48.25 C ANISOU 838 CD LYS A 98 5739 7109 5485 -3669 -2664 1205 C ATOM 839 CE LYS A 98 7.155 -15.934 5.119 1.00 61.34 C ANISOU 839 CE LYS A 98 6534 9702 7070 -1250 -3642 -2669 C ATOM 840 NZ LYS A 98 6.553 -17.304 5.046 1.00 96.00 N ANISOU 840 NZ LYS A 98 16098 8250 12125 -379 -3180 -5954 N ATOM 841 N THR A 99 10.914 -12.226 6.146 1.00 13.52 N ANISOU 841 N THR A 99 2298 1463 1374 -24 59 -148 N ATOM 842 CA THR A 99 10.731 -10.926 5.581 1.00 12.87 C ANISOU 842 CA THR A 99 2168 1460 1263 26 53 -186 C ATOM 843 C THR A 99 9.461 -10.903 4.736 1.00 13.62 C ANISOU 843 C THR A 99 2219 1594 1363 -10 -44 -163 C ATOM 844 O THR A 99 9.379 -11.724 3.795 1.00 16.38 O ANISOU 844 O THR A 99 2605 1942 1679 100 -239 -479 O ATOM 845 CB THR A 99 11.925 -10.560 4.688 1.00 13.45 C ANISOU 845 CB THR A 99 2249 1639 1223 -5 93 -135 C ATOM 846 OG1 THR A 99 13.115 -10.518 5.466 1.00 14.54 O ANISOU 846 OG1 THR A 99 2194 1808 1523 56 33 -84 O ATOM 847 CG2 THR A 99 11.775 -9.237 4.000 1.00 14.93 C ANISOU 847 CG2 THR A 99 2470 1783 1420 -10 115 84 C ATOM 848 N THR A 100 8.559 -9.982 4.975 1.00 14.16 N ANISOU 848 N THR A 100 2125 1682 1575 -16 -191 -269 N ATOM 849 CA THR A 100 7.331 -9.823 4.191 1.00 15.99 C ANISOU 849 CA THR A 100 2359 1859 1855 5 -466 -275 C ATOM 850 C THR A 100 7.192 -8.366 3.791 1.00 14.80 C ANISOU 850 C THR A 100 2120 1858 1646 -43 -357 -239 C ATOM 851 O THR A 100 7.293 -7.496 4.614 1.00 16.75 O ANISOU 851 O THR A 100 2930 1854 1579 -54 -353 -331 O ATOM 852 CB THR A 100 6.066 -10.276 4.993 1.00 21.62 C ANISOU 852 CB THR A 100 2298 2540 3377 -746 -637 484 C ATOM 853 OG1 THR A 100 6.276 -11.621 5.357 1.00 23.01 O ANISOU 853 OG1 THR A 100 2950 2494 3298 -532 -409 208 O ATOM 854 CG2 THR A 100 4.853 -10.123 4.112 1.00 30.63 C ANISOU 854 CG2 THR A 100 2638 3872 5129 -815 -1369 1057 C ATOM 855 N GLN A 101 6.947 -8.097 2.529 1.00 17.72 N ANISOU 855 N GLN A 101 3105 1997 1631 138 -564 -316 N ATOM 856 CA GLN A 101 6.753 -6.772 2.022 1.00 18.27 C ANISOU 856 CA GLN A 101 2963 2214 1767 375 -771 -164 C ATOM 857 C GLN A 101 5.285 -6.427 2.145 1.00 17.09 C ANISOU 857 C GLN A 101 2776 1996 1722 -65 -524 -167 C ATOM 858 O GLN A 101 4.424 -7.266 1.889 1.00 21.51 O ANISOU 858 O GLN A 101 3042 2162 2969 -103 -708 -553 O ATOM 859 CB GLN A 101 7.105 -6.737 0.546 1.00 20.61 C ANISOU 859 CB GLN A 101 3189 2781 1861 340 -312 -15 C ATOM 860 CG GLN A 101 8.543 -7.079 0.153 1.00 23.80 C ANISOU 860 CG GLN A 101 3373 3098 2574 674 -367 -496 C ATOM 861 CD GLN A 101 8.707 -7.229 -1.337 1.00 34.49 C ANISOU 861 CD GLN A 101 3670 6810 2626 882 63 -976 C ATOM 862 OE1 GLN A 101 7.832 -7.577 -2.122 1.00 52.59 O ANISOU 862 OE1 GLN A 101 4414 13231 2336 -964 311 -1621 O ATOM 863 NE2 GLN A 101 9.919 -6.938 -1.819 1.00 38.68 N ANISOU 863 NE2 GLN A 101 4421 7196 3080 -204 227 -136 N ATOM 864 N ALA A 102 4.990 -5.145 2.397 1.00 16.89 N ANISOU 864 N ALA A 102 2631 2078 1708 46 -459 -270 N ATOM 865 CA ALA A 102 3.619 -4.718 2.456 1.00 17.66 C ANISOU 865 CA ALA A 102 2470 2178 2062 -224 -316 -361 C ATOM 866 C ALA A 102 3.515 -3.233 2.102 1.00 15.73 C ANISOU 866 C ALA A 102 2123 2276 1578 -8 -297 -342 C ATOM 867 O ALA A 102 4.494 -2.507 2.143 1.00 16.20 O ANISOU 867 O ALA A 102 2178 2129 1847 -13 -424 -207 O ATOM 868 CB ALA A 102 2.988 -5.036 3.776 1.00 20.43 C ANISOU 868 CB ALA A 102 2932 2362 2466 -367 79 -76 C ATOM 869 N ASN A 103 2.283 -2.768 1.828 1.00 17.26 N ANISOU 869 N ASN A 103 2080 2362 2114 20 -231 -636 N ATOM 870 CA ASN A 103 1.981 -1.368 1.624 1.00 16.52 C ANISOU 870 CA ASN A 103 2094 2410 1774 81 -160 -398 C ATOM 871 C ASN A 103 0.731 -1.063 2.425 1.00 17.10 C ANISOU 871 C ASN A 103 1928 2652 1917 58 -311 -602 C ATOM 872 O ASN A 103 -0.320 -1.578 2.086 1.00 20.15 O ANISOU 872 O ASN A 103 2075 3242 2337 -332 -217 -871 O ATOM 873 CB AASN A 103 1.813 -0.993 0.157 0.19 17.68 C ANISOU 873 CB AASN A 103 2943 2179 1598 -226 -356 -877 C ATOM 874 CB BASN A 103 1.728 -1.090 0.149 0.81 21.50 C ANISOU 874 CB BASN A 103 2434 3889 1847 544 -187 -218 C ATOM 875 CG AASN A 103 3.129 -0.977 -0.591 0.19 16.24 C ANISOU 875 CG AASN A 103 2744 2555 872 905 -701 -442 C ATOM 876 CG BASN A 103 1.904 0.387 -0.146 0.81 31.51 C ANISOU 876 CG BASN A 103 4882 4634 2457 -526 -1221 1145 C ATOM 877 OD1AASN A 103 3.574 -2.015 -1.098 0.19 34.24 O ANISOU 877 OD1AASN A 103 7871 3801 1336 3392 979 117 O ATOM 878 OD1BASN A 103 3.043 0.782 -0.391 0.81 49.89 O ANISOU 878 OD1BASN A 103 6170 7729 5058 -3119 -1604 2058 O ATOM 879 ND2AASN A 103 3.832 0.141 -0.585 0.19 26.26 N ANISOU 879 ND2AASN A 103 3394 4987 1596 -1196 -704 358 N ATOM 880 ND2BASN A 103 0.807 1.079 -0.067 0.81 57.38 N ANISOU 880 ND2BASN A 103 8753 4308 8743 2094 2740 2083 N ATOM 881 N LYS A 104 0.884 -0.391 3.549 1.00 15.41 N ANISOU 881 N LYS A 104 1821 2363 1672 -46 -117 -354 N ATOM 882 CA LYS A 104 -0.183 -0.272 4.523 1.00 15.55 C ANISOU 882 CA LYS A 104 1613 2331 1965 -114 -56 -273 C ATOM 883 C LYS A 104 -0.130 1.115 5.144 1.00 14.74 C ANISOU 883 C LYS A 104 1680 2230 1692 -91 -68 -218 C ATOM 884 O LYS A 104 0.887 1.802 5.118 1.00 15.39 O ANISOU 884 O LYS A 104 1810 2243 1796 -165 87 -175 O ATOM 885 CB ALYS A 104 -0.199 -1.343 5.595 0.52 18.51 C ATOM 886 CB BLYS A 104 0.096 -1.259 5.678 0.48 17.05 C ATOM 887 CG ALYS A 104 -0.490 -2.744 5.031 0.52 20.83 C ATOM 888 CG BLYS A 104 0.229 -2.728 5.300 0.48 19.11 C ATOM 889 CD ALYS A 104 -0.277 -3.756 6.172 0.52 25.27 C ATOM 890 CD BLYS A 104 -1.119 -3.444 5.313 0.48 43.69 C ATOM 891 CE ALYS A 104 -1.396 -4.795 6.189 0.52 50.38 C ATOM 892 CE BLYS A 104 -0.964 -4.956 5.168 0.48 26.68 C ATOM 893 NZ ALYS A 104 -1.157 -5.840 7.231 0.52 91.34 N ATOM 894 NZ BLYS A 104 -0.783 -5.334 3.728 0.48 54.72 N ATOM 895 N HIS A 105 -1.237 1.511 5.754 1.00 15.54 N ANISOU 895 N HIS A 105 1694 2364 1847 -156 -91 -319 N ATOM 896 CA HIS A 105 -1.201 2.702 6.636 1.00 15.40 C ANISOU 896 CA HIS A 105 1777 2380 1695 2 -59 -227 C ATOM 897 C HIS A 105 -0.469 2.321 7.907 1.00 14.93 C ANISOU 897 C HIS A 105 1880 2042 1750 -188 -152 -122 C ATOM 898 O HIS A 105 -0.524 1.158 8.335 1.00 17.43 O ANISOU 898 O HIS A 105 2314 2173 2134 -468 -335 101 O ATOM 899 CB HIS A 105 -2.638 3.113 7.009 1.00 17.61 C ANISOU 899 CB HIS A 105 1791 2638 2263 129 -53 -324 C ATOM 900 CG HIS A 105 -3.485 3.499 5.837 1.00 19.87 C ANISOU 900 CG HIS A 105 1892 2965 2693 252 -353 -345 C ATOM 901 ND1 HIS A 105 -3.622 4.770 5.336 1.00 22.79 N ANISOU 901 ND1 HIS A 105 1968 3302 3389 241 -382 281 N ATOM 902 CD2 HIS A 105 -4.284 2.692 5.080 1.00 25.13 C ANISOU 902 CD2 HIS A 105 2314 3745 3488 -216 -994 -240 C ATOM 903 CE1 HIS A 105 -4.439 4.761 4.282 1.00 27.41 C ANISOU 903 CE1 HIS A 105 2703 4210 3500 699 -774 185 C ATOM 904 NE2 HIS A 105 -4.876 3.524 4.150 1.00 28.24 N ANISOU 904 NE2 HIS A 105 2417 4707 3604 227 -1094 -66 N ATOM 905 N ILE A 106 0.243 3.219 8.488 1.00 14.01 N ANISOU 905 N ILE A 106 1989 1896 1437 -169 7 -53 N ATOM 906 CA ILE A 106 0.890 3.061 9.749 1.00 13.30 C ANISOU 906 CA ILE A 106 1786 1847 1422 15 32 -144 C ATOM 907 C ILE A 106 0.182 3.850 10.846 1.00 13.05 C ANISOU 907 C ILE A 106 1721 1808 1429 -30 -66 -130 C ATOM 908 O ILE A 106 -0.399 4.914 10.623 1.00 15.11 O ANISOU 908 O ILE A 106 1924 2107 1711 283 70 55 O ATOM 909 CB ILE A 106 2.393 3.401 9.656 1.00 14.70 C ANISOU 909 CB ILE A 106 1816 2103 1667 232 48 -125 C ATOM 910 CG1 ILE A 106 2.687 4.883 9.512 1.00 16.95 C ANISOU 910 CG1 ILE A 106 1795 2317 2329 -203 175 -26 C ATOM 911 CG2 ILE A 106 3.052 2.557 8.586 1.00 17.85 C ANISOU 911 CG2 ILE A 106 1994 2882 1904 328 344 -398 C ATOM 912 CD1 ILE A 106 4.134 5.251 9.706 1.00 19.46 C ANISOU 912 CD1 ILE A 106 1794 3213 2385 -344 28 128 C ATOM 913 N ILE A 107 0.311 3.319 12.055 1.00 12.78 N ANISOU 913 N ILE A 107 1688 1776 1391 60 21 -104 N ATOM 914 CA ILE A 107 -0.195 3.957 13.248 1.00 12.34 C ANISOU 914 CA ILE A 107 1508 1689 1492 44 39 -159 C ATOM 915 C ILE A 107 0.971 4.070 14.228 1.00 12.15 C ANISOU 915 C ILE A 107 1405 1775 1437 7 123 -157 C ATOM 916 O ILE A 107 1.601 3.049 14.568 1.00 13.40 O ANISOU 916 O ILE A 107 1627 1748 1716 80 -8 -67 O ATOM 917 CB ILE A 107 -1.358 3.175 13.899 1.00 13.77 C ANISOU 917 CB ILE A 107 1511 2060 1660 -168 57 -126 C ATOM 918 CG1 ILE A 107 -2.530 3.050 12.908 1.00 17.44 C ANISOU 918 CG1 ILE A 107 1745 2855 2026 -365 -80 -219 C ATOM 919 CG2 ILE A 107 -1.798 3.855 15.184 1.00 15.43 C ANISOU 919 CG2 ILE A 107 1611 2465 1788 -27 249 -103 C ATOM 920 CD1 ILE A 107 -3.664 2.228 13.384 1.00 23.47 C ANISOU 920 CD1 ILE A 107 2057 3411 3449 -885 -315 -77 C ATOM 921 N VAL A 108 1.257 5.291 14.649 1.00 12.58 N ANISOU 921 N VAL A 108 1462 1723 1597 32 -42 -113 N ATOM 922 CA VAL A 108 2.365 5.576 15.541 1.00 12.31 C ANISOU 922 CA VAL A 108 1326 1883 1468 46 -4 -149 C ATOM 923 C VAL A 108 1.841 6.384 16.728 1.00 12.18 C ANISOU 923 C VAL A 108 1362 1719 1547 -44 90 -113 C ATOM 924 O VAL A 108 0.813 7.047 16.633 1.00 14.93 O ANISOU 924 O VAL A 108 1628 2342 1701 397 -1 -349 O ATOM 925 CB VAL A 108 3.469 6.382 14.851 1.00 13.68 C ANISOU 925 CB VAL A 108 1478 2127 1591 -66 79 -184 C ATOM 926 CG1 VAL A 108 4.095 5.581 13.717 1.00 16.83 C ANISOU 926 CG1 VAL A 108 1858 2768 1771 14 432 -253 C ATOM 927 CG2 VAL A 108 2.988 7.719 14.315 1.00 17.05 C ANISOU 927 CG2 VAL A 108 2078 2112 2289 -176 26 103 C ATOM 928 N ALA A 109 2.537 6.272 17.842 1.00 12.51 N ANISOU 928 N ALA A 109 1414 1882 1458 4 83 -173 N ATOM 929 CA ALA A 109 2.295 7.117 18.997 1.00 12.44 C ANISOU 929 CA ALA A 109 1295 1889 1543 -31 169 -160 C ATOM 930 C ALA A 109 3.300 8.268 18.978 1.00 12.03 C ANISOU 930 C ALA A 109 1366 1843 1361 -55 158 -158 C ATOM 931 O ALA A 109 4.472 8.011 18.679 1.00 13.96 O ANISOU 931 O ALA A 109 1284 2056 1966 -68 232 -244 O ATOM 932 CB ALA A 109 2.359 6.340 20.292 1.00 15.19 C ANISOU 932 CB ALA A 109 2086 2105 1580 -340 272 -57 C ATOM 933 N CYS A 110 2.856 9.447 19.310 1.00 13.26 N ANISOU 933 N CYS A 110 1410 1944 1684 -66 375 -295 N ATOM 934 CA CYS A 110 3.694 10.662 19.280 1.00 13.53 C ANISOU 934 CA CYS A 110 1690 1862 1588 -247 308 -142 C ATOM 935 C CYS A 110 3.773 11.294 20.636 1.00 14.64 C ANISOU 935 C CYS A 110 1804 2019 1738 -293 483 -378 C ATOM 936 O CYS A 110 2.840 11.271 21.416 1.00 16.38 O ANISOU 936 O CYS A 110 1919 2410 1896 -340 625 -394 O ATOM 937 CB CYS A 110 3.121 11.665 18.280 1.00 15.56 C ANISOU 937 CB CYS A 110 2173 1933 1806 22 251 -257 C ATOM 938 SG CYS A 110 2.997 10.942 16.624 1.00 15.96 S ANISOU 938 SG CYS A 110 2316 2011 1739 -9 4 -201 S ATOM 939 N GLU A 111 4.937 11.902 20.923 1.00 14.65 N ANISOU 939 N GLU A 111 1881 2204 1483 -384 410 -401 N ATOM 940 CA GLU A 111 5.197 12.595 22.157 1.00 16.77 C ANISOU 940 CA GLU A 111 2266 2645 1459 -574 385 -496 C ATOM 941 C GLU A 111 6.204 13.717 21.882 1.00 16.99 C ANISOU 941 C GLU A 111 2170 2622 1662 -524 193 -597 C ATOM 942 O GLU A 111 6.991 13.611 20.959 1.00 18.74 O ANISOU 942 O GLU A 111 2606 2714 1799 -834 509 -387 O ATOM 943 CB GLU A 111 5.825 11.649 23.183 1.00 20.98 C ANISOU 943 CB GLU A 111 3142 3219 1609 -454 187 -219 C ATOM 944 CG GLU A 111 4.987 10.551 23.738 1.00 24.74 C ANISOU 944 CG GLU A 111 3573 3819 2008 -687 132 346 C ATOM 945 CD GLU A 111 5.706 9.739 24.822 1.00 29.61 C ANISOU 945 CD GLU A 111 5314 3900 2037 158 -8 286 C ATOM 946 OE1 GLU A 111 6.644 10.280 25.456 0.59 40.78 O ANISOU 946 OE1 GLU A 111 5023 8270 2201 -1134 -663 1762 O ATOM 947 OE2 GLU A 111 5.303 8.571 25.080 1.00 48.31 O ANISOU 947 OE2 GLU A 111 9946 4198 4213 -561 -383 1317 O ATOM 948 N GLY A 112 6.216 14.675 22.794 1.00 20.23 N ANISOU 948 N GLY A 112 3019 2691 1977 -829 488 -687 N ATOM 949 CA GLY A 112 7.270 15.636 22.848 1.00 22.73 C ANISOU 949 CA GLY A 112 3190 2828 2616 -983 315 -1030 C ATOM 950 C GLY A 112 7.003 16.967 22.184 1.00 21.68 C ANISOU 950 C GLY A 112 3340 2655 2241 -1047 803 -1115 C ATOM 951 O GLY A 112 5.927 17.207 21.638 1.00 23.15 O ANISOU 951 O GLY A 112 3320 2735 2742 -677 910 -815 O ATOM 952 N ASN A 113 7.997 17.832 22.267 1.00 25.55 N ANISOU 952 N ASN A 113 3953 3166 2588 -1582 820 -1167 N ATOM 953 CA ASN A 113 8.037 19.080 21.547 1.00 27.74 C ANISOU 953 CA ASN A 113 4444 2993 3103 -1677 1441 -1249 C ATOM 954 C ASN A 113 9.435 19.235 20.972 1.00 30.27 C ANISOU 954 C ASN A 113 4432 4249 2822 -2273 1106 -1279 C ATOM 955 O ASN A 113 10.346 19.475 21.797 1.00 39.37 O ANISOU 955 O ASN A 113 5143 6436 3380 -3471 766 -1676 O ATOM 956 CB ASN A 113 7.570 20.262 22.381 1.00 36.47 C ANISOU 956 CB ASN A 113 7020 3260 3577 -1227 2030 -1452 C ATOM 957 CG ASN A 113 7.845 21.515 21.572 1.00 44.58 C ANISOU 957 CG ASN A 113 8408 2899 5632 -1849 1047 -923 C ATOM 958 OD1 ASN A 113 8.419 22.411 22.193 1.00 72.32 O ANISOU 958 OD1 ASN A 113 11837 4196 11447 -3422 -3717 335 O ATOM 959 ND2 ASN A 113 7.491 21.632 20.326 1.00 41.18 N ANISOU 959 ND2 ASN A 113 6918 3406 5324 84 2231 -191 N ATOM 960 N PRO A 114 9.652 19.085 19.686 1.00 26.28 N ANISOU 960 N PRO A 114 4028 3187 2769 -1595 1139 -902 N ATOM 961 CA PRO A 114 8.687 18.811 18.635 1.00 23.05 C ANISOU 961 CA PRO A 114 3550 2513 2697 -942 1088 -721 C ATOM 962 C PRO A 114 8.007 17.447 18.804 1.00 19.41 C ANISOU 962 C PRO A 114 2728 2295 2353 -494 837 -435 C ATOM 963 O PRO A 114 8.509 16.547 19.443 1.00 19.87 O ANISOU 963 O PRO A 114 2684 2511 2355 -627 295 -542 O ATOM 964 CB PRO A 114 9.499 18.743 17.340 1.00 24.16 C ANISOU 964 CB PRO A 114 3755 2822 2605 -1244 1111 -390 C ATOM 965 CG PRO A 114 10.865 18.960 17.760 1.00 35.00 C ANISOU 965 CG PRO A 114 3697 6852 2751 -1296 1092 -423 C ATOM 966 CD PRO A 114 11.030 19.305 19.173 1.00 30.36 C ANISOU 966 CD PRO A 114 3953 4539 3045 -1914 1011 -775 C ATOM 967 N TYR A 115 6.780 17.421 18.359 1.00 19.36 N ANISOU 967 N TYR A 115 2745 1929 2684 -212 685 -405 N ATOM 968 CA TYR A 115 5.897 16.280 18.580 1.00 17.33 C ANISOU 968 CA TYR A 115 2373 1890 2321 -94 736 -370 C ATOM 969 C TYR A 115 6.182 15.221 17.483 1.00 16.16 C ANISOU 969 C TYR A 115 2366 1828 1948 1 533 -176 C ATOM 970 O TYR A 115 5.942 15.473 16.314 1.00 19.67 O ANISOU 970 O TYR A 115 3179 2195 2100 420 178 -183 O ATOM 971 CB TYR A 115 4.495 16.755 18.467 1.00 20.00 C ANISOU 971 CB TYR A 115 2558 2191 2851 184 677 -328 C ATOM 972 CG TYR A 115 3.380 15.865 18.963 1.00 17.72 C ANISOU 972 CG TYR A 115 2186 2228 2319 261 445 -503 C ATOM 973 CD1 TYR A 115 3.358 15.417 20.285 1.00 19.38 C ANISOU 973 CD1 TYR A 115 2356 2803 2206 -139 434 -544 C ATOM 974 CD2 TYR A 115 2.305 15.526 18.149 1.00 18.50 C ANISOU 974 CD2 TYR A 115 2444 2309 2277 329 295 -491 C ATOM 975 CE1 TYR A 115 2.311 14.646 20.744 1.00 18.95 C ANISOU 975 CE1 TYR A 115 2448 2479 2272 -53 424 -455 C ATOM 976 CE2 TYR A 115 1.234 14.788 18.598 1.00 19.66 C ANISOU 976 CE2 TYR A 115 2285 2698 2486 171 226 -620 C ATOM 977 CZ TYR A 115 1.258 14.371 19.920 1.00 19.10 C ANISOU 977 CZ TYR A 115 2389 2298 2570 -47 410 -496 C ATOM 978 OH TYR A 115 0.275 13.606 20.503 1.00 22.86 O ANISOU 978 OH TYR A 115 2526 3112 3049 -366 716 -691 O ATOM 979 N VAL A 116 6.782 14.113 17.877 1.00 14.84 N ANISOU 979 N VAL A 116 2178 1775 1686 -160 415 -227 N ATOM 980 CA VAL A 116 7.378 13.160 16.937 1.00 13.99 C ANISOU 980 CA VAL A 116 1942 1747 1628 -78 420 -70 C ATOM 981 C VAL A 116 6.983 11.742 17.295 1.00 12.86 C ANISOU 981 C VAL A 116 1716 1820 1351 -259 257 -140 C ATOM 982 O VAL A 116 6.616 11.447 18.440 1.00 13.57 O ANISOU 982 O VAL A 116 1886 1880 1390 -208 360 -187 O ATOM 983 CB VAL A 116 8.892 13.304 16.901 1.00 16.02 C ANISOU 983 CB VAL A 116 1912 1874 2300 -309 521 9 C ATOM 984 CG1 VAL A 116 9.297 14.627 16.268 1.00 20.98 C ANISOU 984 CG1 VAL A 116 2530 2196 3243 -440 862 407 C ATOM 985 CG2 VAL A 116 9.529 13.097 18.232 1.00 18.81 C ANISOU 985 CG2 VAL A 116 2180 2231 2735 -257 -59 -74 C ATOM 986 N PRO A 117 7.124 10.806 16.354 1.00 13.19 N ANISOU 986 N PRO A 117 1848 1830 1333 -188 340 -95 N ATOM 987 CA PRO A 117 6.850 9.408 16.665 1.00 12.77 C ANISOU 987 CA PRO A 117 1563 1798 1490 -186 208 -173 C ATOM 988 C PRO A 117 7.848 8.809 17.639 1.00 12.81 C ANISOU 988 C PRO A 117 1481 1850 1537 -125 237 -248 C ATOM 989 O PRO A 117 9.040 8.968 17.495 1.00 15.19 O ANISOU 989 O PRO A 117 1435 2364 1973 -175 269 -35 O ATOM 990 CB PRO A 117 6.928 8.685 15.324 1.00 15.00 C ANISOU 990 CB PRO A 117 2004 2109 1584 -39 156 -400 C ATOM 991 CG PRO A 117 6.899 9.742 14.340 1.00 18.97 C ANISOU 991 CG PRO A 117 3640 2104 1464 107 240 -375 C ATOM 992 CD PRO A 117 7.441 10.997 14.937 1.00 15.78 C ANISOU 992 CD PRO A 117 2384 2262 1350 -29 408 -145 C ATOM 993 N VAL A 118 7.321 8.069 18.606 1.00 12.91 N ANISOU 993 N VAL A 118 1420 1953 1532 -54 127 -81 N ATOM 994 CA VAL A 118 8.096 7.371 19.591 1.00 13.54 C ANISOU 994 CA VAL A 118 1314 2194 1637 -29 -57 -143 C ATOM 995 C VAL A 118 7.779 5.876 19.652 1.00 13.94 C ANISOU 995 C VAL A 118 1579 2128 1590 -29 -57 23 C ATOM 996 O VAL A 118 8.485 5.142 20.337 1.00 18.44 O ANISOU 996 O VAL A 118 2034 2353 2621 -92 -645 133 O ATOM 997 CB VAL A 118 8.026 8.017 20.977 1.00 15.76 C ANISOU 997 CB VAL A 118 1831 2510 1646 -88 -153 -297 C ATOM 998 CG1 VAL A 118 8.580 9.429 20.930 1.00 18.77 C ANISOU 998 CG1 VAL A 118 2385 2606 2141 -261 -231 -509 C ATOM 999 CG2 VAL A 118 6.592 7.955 21.514 1.00 19.01 C ANISOU 999 CG2 VAL A 118 2222 3191 1810 -112 366 -523 C ATOM 1000 N HIS A 119 6.740 5.424 19.017 1.00 13.73 N ANISOU 1000 N HIS A 119 1651 1982 1582 -51 -1 -63 N ATOM 1001 CA HIS A 119 6.332 4.025 19.110 1.00 13.88 C ANISOU 1001 CA HIS A 119 1775 1923 1574 0 -68 -82 C ATOM 1002 C HIS A 119 5.585 3.694 17.853 1.00 13.16 C ANISOU 1002 C HIS A 119 1400 1880 1718 26 76 -126 C ATOM 1003 O HIS A 119 4.771 4.472 17.380 1.00 14.90 O ANISOU 1003 O HIS A 119 1701 2089 1872 327 -176 -338 O ATOM 1004 CB HIS A 119 5.436 3.877 20.345 1.00 17.87 C ANISOU 1004 CB HIS A 119 2166 2834 1790 -183 319 164 C ATOM 1005 CG HIS A 119 4.546 2.708 20.385 1.00 20.07 C ANISOU 1005 CG HIS A 119 2591 3129 1905 -469 119 133 C ATOM 1006 ND1 HIS A 119 4.999 1.507 20.784 1.00 24.55 N ANISOU 1006 ND1 HIS A 119 3342 3128 2857 -586 120 504 N ATOM 1007 CD2 HIS A 119 3.251 2.578 20.057 1.00 22.62 C ANISOU 1007 CD2 HIS A 119 2602 3379 2613 -598 169 -422 C ATOM 1008 CE1 HIS A 119 4.008 0.612 20.729 1.00 27.00 C ANISOU 1008 CE1 HIS A 119 3738 3757 2763 -1209 -103 1074 C ATOM 1009 NE2 HIS A 119 2.916 1.246 20.269 1.00 24.29 N ANISOU 1009 NE2 HIS A 119 3479 3619 2129 -1003 57 -56 N ATOM 1010 N PHE A 120 5.842 2.511 17.304 1.00 13.19 N ANISOU 1010 N PHE A 120 1501 1907 1602 191 -17 -113 N ATOM 1011 CA PHE A 120 5.122 1.961 16.165 1.00 12.70 C ANISOU 1011 CA PHE A 120 1537 1823 1466 96 87 0 C ATOM 1012 C PHE A 120 4.047 1.023 16.688 1.00 13.16 C ANISOU 1012 C PHE A 120 1562 1890 1547 83 163 25 C ATOM 1013 O PHE A 120 4.329 0.011 17.290 1.00 15.76 O ANISOU 1013 O PHE A 120 1865 2014 2109 122 118 385 O ATOM 1014 CB PHE A 120 6.097 1.206 15.257 1.00 13.93 C ANISOU 1014 CB PHE A 120 1630 1951 1712 101 194 -158 C ATOM 1015 CG PHE A 120 5.471 0.806 13.928 1.00 15.03 C ANISOU 1015 CG PHE A 120 1680 2334 1696 255 248 -282 C ATOM 1016 CD1 PHE A 120 4.709 -0.321 13.783 1.00 18.46 C ANISOU 1016 CD1 PHE A 120 1915 3015 2085 -360 225 -483 C ATOM 1017 CD2 PHE A 120 5.659 1.614 12.824 1.00 18.26 C ANISOU 1017 CD2 PHE A 120 2452 2693 1793 280 158 -84 C ATOM 1018 CE1 PHE A 120 4.082 -0.651 12.597 1.00 20.22 C ANISOU 1018 CE1 PHE A 120 1998 3383 2300 -59 144 -812 C ATOM 1019 CE2 PHE A 120 5.079 1.291 11.588 1.00 21.56 C ANISOU 1019 CE2 PHE A 120 3067 3327 1798 391 -24 -168 C ATOM 1020 CZ PHE A 120 4.241 0.207 11.525 1.00 21.74 C ANISOU 1020 CZ PHE A 120 2660 3118 2481 786 -519 -534 C ATOM 1021 N ASP A 121 2.782 1.405 16.491 1.00 13.11 N ANISOU 1021 N ASP A 121 1549 1835 1597 35 108 85 N ATOM 1022 CA ASP A 121 1.697 0.658 17.087 1.00 13.62 C ANISOU 1022 CA ASP A 121 1581 2088 1505 -51 155 66 C ATOM 1023 C ASP A 121 1.191 -0.472 16.185 1.00 14.53 C ANISOU 1023 C ASP A 121 1784 1951 1786 -111 162 99 C ATOM 1024 O ASP A 121 0.888 -1.517 16.692 1.00 18.54 O ANISOU 1024 O ASP A 121 2819 2183 2041 -508 129 241 O ATOM 1025 CB ASP A 121 0.531 1.585 17.456 1.00 15.42 C ANISOU 1025 CB ASP A 121 1662 2221 1975 33 269 3 C ATOM 1026 CG ASP A 121 -0.358 1.033 18.547 1.00 16.69 C ANISOU 1026 CG ASP A 121 1861 2601 1878 -47 344 -260 C ATOM 1027 OD1 ASP A 121 0.196 0.572 19.566 1.00 21.36 O ANISOU 1027 OD1 ASP A 121 2213 3997 1903 -468 261 360 O ATOM 1028 OD2 ASP A 121 -1.557 1.001 18.368 1.00 18.29 O ANISOU 1028 OD2 ASP A 121 1785 2944 2219 -143 396 -164 O ATOM 1029 N ALA A 122 0.962 -0.185 14.909 1.00 14.46 N ANISOU 1029 N ALA A 122 1770 1976 1747 -222 68 3 N ATOM 1030 CA ALA A 122 0.281 -1.151 14.038 1.00 15.80 C ANISOU 1030 CA ALA A 122 1993 2125 1884 -493 117 -18 C ATOM 1031 C ALA A 122 0.402 -0.674 12.614 1.00 14.62 C ANISOU 1031 C ALA A 122 1952 1711 1893 -160 -5 -45 C ATOM 1032 O ALA A 122 0.644 0.477 12.303 1.00 15.45 O ANISOU 1032 O ALA A 122 2127 1797 1947 -227 160 -82 O ATOM 1033 CB ALA A 122 -1.237 -1.173 14.403 1.00 20.94 C ANISOU 1033 CB ALA A 122 1993 3471 2493 -938 55 179 C ATOM 1034 N SER A 123 0.164 -1.596 11.696 1.00 17.98 N ANISOU 1034 N SER A 123 3029 1834 1970 -487 -227 -36 N ATOM 1035 CA SER A 123 -0.091 -1.298 10.304 1.00 16.94 C ANISOU 1035 CA SER A 123 2363 2140 1935 -455 -157 -80 C ATOM 1036 C SER A 123 -1.476 -1.835 9.976 1.00 18.64 C ANISOU 1036 C SER A 123 2464 2489 2132 -792 3 -3 C ATOM 1037 O SER A 123 -1.890 -2.882 10.465 1.00 24.11 O ANISOU 1037 O SER A 123 3116 2825 3220 -1148 -453 485 O ATOM 1038 CB ASER A 123 0.970 -1.827 9.375 0.70 20.05 C ANISOU 1038 CB ASER A 123 2338 3025 2255 -633 0 -250 C ATOM 1039 CB BSER A 123 0.838 -2.103 9.385 0.30 26.35 C ANISOU 1039 CB BSER A 123 2945 4921 2146 1156 37 66 C ATOM 1040 OG ASER A 123 1.070 -3.219 9.447 0.70 22.59 O ANISOU 1040 OG ASER A 123 2945 3118 2519 178 147 -570 O ATOM 1041 OG BSER A 123 2.182 -1.852 9.678 0.30 37.88 O ANISOU 1041 OG BSER A 123 2773 7406 4213 949 253 177 O ATOM 1042 N VAL A 124 -2.200 -1.120 9.133 1.00 18.13 N ANISOU 1042 N VAL A 124 2114 2699 2076 -750 86 -69 N ATOM 1043 CA VAL A 124 -3.559 -1.492 8.775 1.00 20.43 C ANISOU 1043 CA VAL A 124 2167 3168 2428 -885 50 -270 C ATOM 1044 C VAL A 124 -3.794 -1.285 7.296 1.00 24.54 C ANISOU 1044 C VAL A 124 2202 4521 2603 -1355 -179 15 C ATOM 1045 O VAL A 124 -4.704 -1.934 6.757 1.00 35.46 O ANISOU 1045 O VAL A 124 4201 5807 3466 -2720 -1127 39 O ATOM 1046 CB VAL A 124 -4.588 -0.745 9.628 1.00 22.78 C ANISOU 1046 CB VAL A 124 2216 3278 3162 -495 92 -230 C ATOM 1047 CG1 VAL A 124 -4.471 -1.114 11.113 1.00 30.35 C ANISOU 1047 CG1 VAL A 124 3532 5264 2734 -769 718 -556 C ATOM 1048 CG2 VAL A 124 -4.574 0.764 9.512 1.00 32.19 C ANISOU 1048 CG2 VAL A 124 3076 3204 5951 -490 728 -394 C ATOM 1049 OXT VAL A 124 -3.164 -0.453 6.628 1.00 21.17 O ANISOU 1049 OXT VAL A 124 2086 3524 2432 -494 -37 -8 O TER 1050 VAL A 124 HETATM 1051 O HOH A 125 22.370 11.023 25.801 1.00 57.62 O ANISOU 1051 O HOH A 125 7178 7632 7082 -150 -156 -244 O HETATM 1052 O HOH A 126 24.347 -10.913 20.529 1.00 53.07 O ANISOU 1052 O HOH A 126 6949 6924 6291 308 -330 -70 O HETATM 1053 O HOH A 127 18.582 11.549 26.518 0.50 48.52 O ANISOU 1053 O HOH A 127 6674 6107 5653 311 -546 -644 O HETATM 1054 O HOH A 128 17.169 4.684 25.890 1.00 58.05 O ANISOU 1054 O HOH A 128 7089 7280 7685 -469 631 261 O HETATM 1055 O HOH A 129 17.084 2.971 23.918 1.00 42.28 O ANISOU 1055 O HOH A 129 5391 5625 5047 -538 -88 198 O HETATM 1056 O HOH A 130 20.613 2.417 22.958 1.00 36.60 O ANISOU 1056 O HOH A 130 4477 4560 4870 -98 -44 -3 O HETATM 1057 O HOH A 131 19.611 9.995 21.203 1.00 29.20 O ANISOU 1057 O HOH A 131 3690 3754 3650 -38 52 -174 O HETATM 1058 O HOH A 132 16.030 12.815 20.279 1.00 52.98 O ANISOU 1058 O HOH A 132 6986 6481 6665 -6 -535 -109 O HETATM 1059 O HOH A 133 13.198 9.885 25.566 1.00 40.18 O ANISOU 1059 O HOH A 133 4908 5440 4920 671 494 -910 O HETATM 1060 O HOH A 134 12.163 11.455 22.367 1.00 32.91 O ANISOU 1060 O HOH A 134 4320 4155 4027 297 -76 -463 O HETATM 1061 O HOH A 135 18.762 6.702 15.792 1.00 23.45 O ANISOU 1061 O HOH A 135 2819 3091 3000 -153 116 21 O HETATM 1062 O HOH A 136 11.294 3.088 23.446 0.50 44.26 O ANISOU 1062 O HOH A 136 5442 5989 5386 -180 74 180 O HETATM 1063 O HOH A 137 17.433 5.075 10.650 1.00 37.95 O ANISOU 1063 O HOH A 137 4574 4921 4924 -108 189 3 O HETATM 1064 O HOH A 138 16.188 13.074 13.465 1.00 35.13 O ANISOU 1064 O HOH A 138 4581 4162 4605 -193 -215 220 O HETATM 1065 O HOH A 139 18.273 -2.198 21.025 1.00 47.80 O ANISOU 1065 O HOH A 139 6542 5949 5672 -204 70 504 O HETATM 1066 O HOH A 140 18.587 3.820 6.431 1.00 40.30 O ANISOU 1066 O HOH A 140 5165 5206 4940 -419 131 263 O HETATM 1067 O HOH A 141 18.789 -1.205 4.231 1.00 30.90 O ANISOU 1067 O HOH A 141 3817 4049 3874 246 205 130 O HETATM 1068 O HOH A 142 16.577 5.536 7.551 1.00 26.31 O ANISOU 1068 O HOH A 142 3375 3320 3303 -190 7 -127 O HETATM 1069 O HOH A 143 15.636 8.164 7.974 1.00 46.03 O ANISOU 1069 O HOH A 143 5622 5860 6007 138 157 -554 O HETATM 1070 O HOH A 144 13.723 -8.660 -6.866 1.00 55.10 O ANISOU 1070 O HOH A 144 6714 6979 7244 -87 356 -211 O HETATM 1071 O HOH A 145 18.461 1.208 -2.257 0.50 37.12 O ANISOU 1071 O HOH A 145 4499 4843 4763 -181 327 53 O HETATM 1072 O HOH A 146 20.452 4.053 -0.651 0.50 35.85 O ANISOU 1072 O HOH A 146 4606 4554 4460 -256 112 280 O HETATM 1073 O HOH A 147 22.172 2.884 4.701 0.50 46.44 O ANISOU 1073 O HOH A 147 5832 6100 5714 58 -285 98 O HETATM 1074 O HOH A 148 21.596 0.713 3.925 0.50 48.52 O ANISOU 1074 O HOH A 148 6259 6038 6139 523 176 -385 O HETATM 1075 O HOH A 149 12.717 5.139 0.635 1.00 32.75 O ANISOU 1075 O HOH A 149 4029 3997 4416 -103 46 45 O HETATM 1076 O HOH A 150 15.603 0.537 -3.012 1.00 39.76 O ANISOU 1076 O HOH A 150 4671 5651 4785 214 612 -392 O HETATM 1077 O HOH A 151 16.429 -3.748 0.461 1.00 31.68 O ANISOU 1077 O HOH A 151 4102 3915 4019 -84 75 18 O HETATM 1078 O HOH A 152 14.650 -2.624 -2.940 1.00 51.02 O ANISOU 1078 O HOH A 152 6499 6564 6324 -36 590 199 O HETATM 1079 O HOH A 153 15.760 -8.179 -5.457 1.00 23.97 O ANISOU 1079 O HOH A 153 2856 3342 2908 120 273 64 O HETATM 1080 O HOH A 154 17.455 -3.297 -4.059 1.00 51.36 O ANISOU 1080 O HOH A 154 6690 6413 6412 95 315 -120 O HETATM 1081 O HOH A 155 20.520 -10.145 0.677 1.00 38.29 O ANISOU 1081 O HOH A 155 4793 5263 4494 -249 308 73 O HETATM 1082 O HOH A 156 17.872 -7.659 1.266 1.00 44.74 O ANISOU 1082 O HOH A 156 5884 5782 5334 -232 104 -35 O HETATM 1083 O HOH A 157 15.194 -12.203 6.881 1.00 15.92 O ANISOU 1083 O HOH A 157 2144 1986 1919 0 62 -40 O HETATM 1084 O HOH A 158 14.329 3.487 -5.273 0.50 47.47 O ANISOU 1084 O HOH A 158 5945 6174 5919 358 -67 -368 O HETATM 1085 O HOH A 159 16.428 3.095 -6.329 0.50 45.65 O ANISOU 1085 O HOH A 159 5615 6066 5663 -424 109 685 O HETATM 1086 O HOH A 160 21.656 -13.001 6.759 0.50 47.73 O ANISOU 1086 O HOH A 160 5941 6068 6125 458 -248 -10 O HETATM 1087 O HOH A 161 9.404 2.554 -5.540 0.50 54.06 O ANISOU 1087 O HOH A 161 7112 6605 6823 149 -603 -467 O HETATM 1088 O HOH A 162 19.080 -11.346 12.838 1.00 25.04 O ANISOU 1088 O HOH A 162 3215 3233 3065 -211 9 148 O HETATM 1089 O HOH A 163 24.079 -9.520 1.791 0.50 45.19 O ANISOU 1089 O HOH A 163 5821 5631 5718 -330 -4 -101 O HETATM 1090 O HOH A 164 23.070 0.579 14.558 1.00 56.86 O ANISOU 1090 O HOH A 164 7112 7276 7218 -402 40 -81 O HETATM 1091 O HOH A 165 25.697 -2.462 14.659 1.00 54.75 O ANISOU 1091 O HOH A 165 6521 7078 7204 -114 110 379 O HETATM 1092 O HOH A 166 24.860 -4.363 7.597 1.00 58.18 O ANISOU 1092 O HOH A 166 7639 7030 7435 -610 -9 -27 O HETATM 1093 O HOH A 167 21.642 2.400 8.802 1.00 55.61 O ANISOU 1093 O HOH A 167 6645 7516 6968 224 363 191 O HETATM 1094 O HOH A 168 21.412 -0.346 9.412 1.00 44.53 O ANISOU 1094 O HOH A 168 5070 6296 5554 509 749 -236 O HETATM 1095 O HOH A 169 19.756 1.836 6.774 1.00 41.78 O ANISOU 1095 O HOH A 169 5105 5644 5127 -224 568 -67 O HETATM 1096 O HOH A 170 18.257 -4.694 21.778 0.50 49.55 O ANISOU 1096 O HOH A 170 6447 5882 6499 -1042 -122 560 O HETATM 1097 O CHOH A 171 16.089 -3.750 21.312 0.50 39.36 O ANISOU 1097 O CHOH A 171 5284 4917 4753 -323 -17 105 O HETATM 1098 O HOH A 172 22.424 -11.519 18.444 1.00 35.11 O ANISOU 1098 O HOH A 172 4374 4566 4402 26 80 -265 O HETATM 1099 O HOH A 173 21.817 -6.945 17.013 1.00 23.88 O ANISOU 1099 O HOH A 173 3119 2961 2994 -45 -21 70 O HETATM 1100 O HOH A 174 20.615 -11.541 15.161 1.00 33.17 O ANISOU 1100 O HOH A 174 4200 4225 4177 -25 97 -84 O HETATM 1101 O HOH A 175 17.791 -7.026 21.765 1.00 32.20 O ANISOU 1101 O HOH A 175 4199 3840 4195 146 -138 0 O HETATM 1102 O HOH A 176 23.457 -6.229 27.434 0.50 43.07 O ANISOU 1102 O HOH A 176 5358 5247 5759 364 -98 -113 O HETATM 1103 O HOH A 177 16.839 -5.853 24.983 0.50 44.74 O ANISOU 1103 O HOH A 177 5662 5463 5873 396 166 -510 O HETATM 1104 O HOH A 178 20.556 -3.669 27.021 0.50 59.55 O ANISOU 1104 O HOH A 178 7724 7207 7697 100 -534 -651 O HETATM 1105 O HOH A 179 12.427 -12.224 23.165 1.00 59.98 O ANISOU 1105 O HOH A 179 7763 7716 7311 -24 173 12 O HETATM 1106 O HOH A 180 8.806 -9.643 23.363 1.00 55.15 O ANISOU 1106 O HOH A 180 7155 7216 6585 70 165 -79 O HETATM 1107 O HOH A 181 9.404 -6.941 21.997 0.50 42.67 O ANISOU 1107 O HOH A 181 5595 5058 5559 -199 -348 0 O HETATM 1108 O HOH A 182 15.589 -14.522 22.340 1.00 20.40 O ANISOU 1108 O HOH A 182 2733 2456 2564 -108 -49 105 O HETATM 1109 O HOH A 183 8.827 -7.184 19.119 1.00 42.29 O ANISOU 1109 O HOH A 183 5295 5612 5163 102 178 17 O HETATM 1110 O HOH A 184 7.076 -2.995 15.226 1.00 42.69 O ANISOU 1110 O HOH A 184 5151 5417 5652 -39 138 -124 O HETATM 1111 O HOH A 185 5.894 -4.707 14.143 1.00 40.31 O ANISOU 1111 O HOH A 185 4936 5513 4868 -228 452 557 O HETATM 1112 O HOH A 186 9.367 3.295 -0.657 1.00 22.42 O ANISOU 1112 O HOH A 186 2912 2889 2717 -111 86 110 O HETATM 1113 O HOH A 187 10.550 5.988 -0.349 1.00 53.33 O ANISOU 1113 O HOH A 187 6605 7239 6419 -220 167 162 O HETATM 1114 O HOH A 188 6.524 7.492 -0.975 1.00 49.16 O ANISOU 1114 O HOH A 188 6725 5931 6023 -697 -238 195 O HETATM 1115 O HOH A 189 4.944 4.750 -0.687 1.00 48.19 O ANISOU 1115 O HOH A 189 6115 6141 6055 -266 35 544 O HETATM 1116 O HOH A 190 10.363 14.063 2.533 1.00 44.09 O ANISOU 1116 O HOH A 190 6077 5348 5327 -187 -14 742 O HETATM 1117 O HOH A 191 13.230 13.544 5.851 1.00 24.86 O ANISOU 1117 O HOH A 191 3123 3174 3146 -197 260 122 O HETATM 1118 O HOH A 192 7.359 16.413 9.080 1.00 34.41 O ANISOU 1118 O HOH A 192 4434 4188 4452 135 73 -95 O HETATM 1119 O HOH A 193 2.920 11.669 5.691 1.00 23.54 O ANISOU 1119 O HOH A 193 2895 3126 2924 154 40 11 O HETATM 1120 O HOH A 194 4.023 13.972 4.440 0.50 39.28 O ANISOU 1120 O HOH A 194 5227 4980 4717 -14 -140 490 O HETATM 1121 O HOH A 195 8.612 9.131 1.720 1.00 18.39 O ANISOU 1121 O HOH A 195 2398 2312 2279 -43 -3 90 O HETATM 1122 O HOH A 196 7.208 12.289 -0.031 0.50 55.16 O ANISOU 1122 O HOH A 196 7691 6655 6612 -229 -356 680 O HETATM 1123 O HOH A 197 12.224 11.673 14.597 1.00 33.61 O ANISOU 1123 O HOH A 197 4287 4247 4234 -357 73 201 O HETATM 1124 O HOH A 198 -1.292 16.569 16.067 1.00 40.02 O ANISOU 1124 O HOH A 198 5345 4888 4973 535 140 -360 O HETATM 1125 O HOH A 199 -1.845 16.804 7.990 0.50 49.72 O ANISOU 1125 O HOH A 199 6582 6074 6233 -572 -340 732 O HETATM 1126 O HOH A 200 0.473 16.000 7.664 1.00 43.63 O ANISOU 1126 O HOH A 200 5435 5415 5729 136 187 10 O HETATM 1127 O HOH A 201 3.727 16.238 12.643 1.00 40.62 O ANISOU 1127 O HOH A 201 5231 5108 5094 234 225 -408 O HETATM 1128 O HOH A 202 1.401 20.445 11.473 0.50 41.32 O ANISOU 1128 O HOH A 202 5101 5197 5401 -448 145 146 O HETATM 1129 O HOH A 203 -4.360 15.796 14.124 1.00 48.49 O ANISOU 1129 O HOH A 203 6200 6180 6043 693 58 -687 O HETATM 1130 O HOH A 204 0.372 9.856 5.085 1.00 26.39 O ANISOU 1130 O HOH A 204 3395 3363 3269 9 74 -21 O HETATM 1131 O HOH A 205 -9.672 11.724 14.709 1.00 45.78 O ANISOU 1131 O HOH A 205 5375 5984 6035 418 142 109 O HETATM 1132 O HOH A 206 -7.680 13.629 13.709 1.00 34.19 O ANISOU 1132 O HOH A 206 4452 4133 4406 655 -33 -166 O HETATM 1133 O HOH A 207 -10.202 9.041 16.345 1.00 55.95 O ANISOU 1133 O HOH A 207 6549 7614 7097 59 469 -139 O HETATM 1134 O HOH A 208 -10.207 11.659 19.215 0.50 49.73 O ANISOU 1134 O HOH A 208 5967 6460 6469 -361 -200 212 O HETATM 1135 O HOH A 209 -6.256 12.687 21.768 1.00 52.81 O ANISOU 1135 O HOH A 209 6586 6789 6689 765 201 -591 O HETATM 1136 O HOH A 210 -10.036 5.774 17.883 1.00 23.49 O ANISOU 1136 O HOH A 210 2777 3119 3028 -223 -56 145 O HETATM 1137 O HOH A 211 22.683 0.889 18.992 1.00 42.92 O ANISOU 1137 O HOH A 211 4860 5364 6083 88 -169 -363 O HETATM 1138 O HOH A 212 -8.335 0.604 21.841 1.00 49.81 O ANISOU 1138 O HOH A 212 6086 6457 6382 249 17 -215 O HETATM 1139 O HOH A 213 -0.757 -0.186 28.220 1.00 38.59 O ANISOU 1139 O HOH A 213 4983 4900 4779 130 -108 77 O HETATM 1140 O HOH A 214 -9.268 4.514 25.278 1.00 25.65 O ANISOU 1140 O HOH A 214 3041 3487 3219 -57 45 49 O HETATM 1141 O HOH A 215 2.862 2.415 26.779 0.50 51.81 O ANISOU 1141 O HOH A 215 6371 6523 6792 263 -78 -305 O HETATM 1142 O HOH A 216 -3.238 13.023 22.451 1.00 47.87 O ANISOU 1142 O HOH A 216 6197 5899 6092 179 57 -52 O HETATM 1143 O HOH A 217 -3.401 15.982 18.183 0.50 43.07 O ANISOU 1143 O HOH A 217 5582 5471 5312 677 306 -452 O HETATM 1144 O HOH A 218 -7.867 1.586 11.753 1.00 49.56 O ANISOU 1144 O HOH A 218 5770 6857 6204 -134 479 -577 O HETATM 1145 O HOH A 219 -5.989 6.904 7.316 0.50 54.89 O ANISOU 1145 O HOH A 219 7215 6774 6869 -568 47 458 O HETATM 1146 O HOH A 220 -6.769 8.324 3.817 0.50 52.68 O ANISOU 1146 O HOH A 220 6489 6465 7060 -236 -181 -246 O HETATM 1147 O HOH A 221 -4.330 16.654 9.563 1.00 52.63 O ANISOU 1147 O HOH A 221 6637 6517 6843 791 -120 -526 O HETATM 1148 O HOH A 222 -7.999 13.941 10.825 1.00 57.05 O ANISOU 1148 O HOH A 222 7346 6859 7472 369 26 467 O HETATM 1149 O HOH A 223 2.730 10.144 3.169 1.00 51.17 O ANISOU 1149 O HOH A 223 6325 6639 6476 -59 312 0 O HETATM 1150 O HOH A 224 -2.527 5.776 0.166 1.00 53.00 O ANISOU 1150 O HOH A 224 6709 6513 6915 655 -654 -165 O HETATM 1151 O HOH A 225 4.068 7.050 0.505 0.50 48.02 O ANISOU 1151 O HOH A 225 6096 6285 5865 569 -286 144 O HETATM 1152 O HOH A 226 -2.086 2.344 -1.728 1.00 59.50 O ANISOU 1152 O HOH A 226 7225 7822 7559 -423 244 151 O HETATM 1153 O HOH A 227 7.183 -11.424 7.962 1.00 21.40 O ANISOU 1153 O HOH A 227 2789 2658 2685 -191 -32 43 O HETATM 1154 O HOH A 228 3.318 -4.157 10.558 1.00 36.83 O ANISOU 1154 O HOH A 228 4645 4697 4651 -162 -152 -12 O HETATM 1155 O HOH A 229 2.391 -8.044 6.449 0.50 40.10 O ANISOU 1155 O HOH A 229 4947 5117 5174 -238 -37 -57 O HETATM 1156 O HOH A 230 7.486 -16.214 15.655 1.00 43.87 O ANISOU 1156 O HOH A 230 5111 5688 5870 -258 327 51 O HETATM 1157 O HOH A 231 8.720 -15.653 18.162 1.00 33.91 O ANISOU 1157 O HOH A 231 4277 4232 4375 -217 61 189 O HETATM 1158 O HOH A 232 11.520 -14.031 20.747 1.00 36.05 O ANISOU 1158 O HOH A 232 4679 4838 4183 19 231 3 O HETATM 1159 O HOH A 233 13.957 -17.285 19.724 1.00 35.70 O ANISOU 1159 O HOH A 233 4565 4616 4383 -194 140 328 O HETATM 1160 O HOH A 234 9.421 -21.163 10.614 1.00 33.25 O ANISOU 1160 O HOH A 234 4388 4016 4230 -298 -210 74 O HETATM 1161 O HOH A 235 13.297 -24.724 16.711 1.00 41.05 O ANISOU 1161 O HOH A 235 5154 5210 5233 -393 161 447 O HETATM 1162 O HOH A 236 13.372 -21.796 17.684 1.00 42.88 O ANISOU 1162 O HOH A 236 5755 5372 5166 -671 -23 312 O HETATM 1163 O HOH A 237 17.630 -23.451 15.640 1.00 52.82 O ANISOU 1163 O HOH A 237 6651 6684 6735 227 151 137 O HETATM 1164 O HOH A 238 19.021 -19.594 13.972 1.00 38.88 O ANISOU 1164 O HOH A 238 4759 4837 5176 176 -76 -346 O HETATM 1165 O HOH A 239 14.722 -19.228 9.408 1.00 34.57 O ANISOU 1165 O HOH A 239 4539 4477 4118 182 273 -398 O HETATM 1166 O HOH A 240 12.635 -21.972 10.099 1.00 48.51 O ANISOU 1166 O HOH A 240 5969 6320 6143 -570 -255 114 O HETATM 1167 O HOH A 241 17.845 -20.117 10.506 0.50 46.58 O ANISOU 1167 O HOH A 241 5762 5882 6056 155 464 188 O HETATM 1168 O HOH A 242 14.355 -23.255 7.788 0.50 42.63 O ANISOU 1168 O HOH A 242 5471 5160 5565 -182 -336 -296 O HETATM 1169 O HOH A 243 22.149 -20.178 18.466 0.50 41.31 O ANISOU 1169 O HOH A 243 5229 5285 5181 -76 127 155 O HETATM 1170 O HOH A 244 16.006 -17.253 21.291 1.00 25.54 O ANISOU 1170 O HOH A 244 3215 3363 3124 -75 66 92 O HETATM 1171 O HOH A 245 19.523 -19.482 22.946 1.00 27.28 O ANISOU 1171 O HOH A 245 3556 3441 3366 -184 9 92 O HETATM 1172 O HOH A 246 22.616 -20.901 20.592 1.00 53.62 O ANISOU 1172 O HOH A 246 6866 6621 6887 266 51 -254 O HETATM 1173 O HOH A 247 15.565 -16.484 7.964 1.00 32.07 O ANISOU 1173 O HOH A 247 4101 3935 4151 -34 165 -92 O HETATM 1174 O HOH A 248 12.348 -14.201 4.546 1.00 21.23 O ANISOU 1174 O HOH A 248 2811 2640 2615 99 133 -112 O HETATM 1175 O HOH A 249 11.050 -13.609 2.292 0.50 45.77 O ANISOU 1175 O HOH A 249 5758 5882 5748 648 -262 -49 O HETATM 1176 O HOH A 250 8.059 -13.682 2.530 0.50 46.86 O ANISOU 1176 O HOH A 250 6226 5547 6033 -254 -414 -502 O HETATM 1177 O HOH A 251 6.520 -10.443 0.783 1.00 39.01 O ANISOU 1177 O HOH A 251 5549 4559 4713 71 -258 -404 O HETATM 1178 O HOH A 252 3.993 -9.724 0.256 1.00 53.24 O ANISOU 1178 O HOH A 252 6948 6381 6898 142 -65 -301 O HETATM 1179 O HOH A 253 1.852 -8.128 2.079 0.50 38.14 O ANISOU 1179 O HOH A 253 4283 5012 5196 -531 88 28 O HETATM 1180 O HOH A 254 0.183 -4.881 1.468 1.00 34.65 O ANISOU 1180 O HOH A 254 4342 4131 4692 -264 -297 -96 O HETATM 1181 O HOH A 255 6.317 -3.311 -2.213 0.50 44.50 O ANISOU 1181 O HOH A 255 5627 5533 5749 -480 -103 171 O HETATM 1182 O HOH A 256 2.767 3.239 -0.672 1.00 54.78 O ANISOU 1182 O HOH A 256 6856 6956 7001 -245 -231 -445 O HETATM 1183 O HOH A 257 -4.316 -3.049 3.988 0.50 42.94 O ANISOU 1183 O HOH A 257 5845 5398 5074 -421 -277 4 O HETATM 1184 O HOH A 258 -6.201 2.964 2.044 0.50 53.96 O ANISOU 1184 O HOH A 258 6769 6897 6836 -476 -81 198 O HETATM 1185 O HOH A 259 1.664 12.369 23.864 1.00 41.62 O ANISOU 1185 O HOH A 259 5358 5284 5171 -211 28 19 O HETATM 1186 O HOH A 260 9.790 12.878 21.754 1.00 31.88 O ANISOU 1186 O HOH A 260 3990 4031 4091 -20 -64 -187 O HETATM 1187 O HOH A 261 8.765 9.459 25.087 0.50 45.76 O ANISOU 1187 O HOH A 261 5630 6236 5520 588 141 -424 O HETATM 1188 O HOH A 262 3.183 7.209 23.951 1.00 33.35 O ANISOU 1188 O HOH A 262 4041 4420 4210 181 30 -81 O HETATM 1189 O HOH A 263 3.994 14.802 24.672 1.00 38.26 O ANISOU 1189 O HOH A 263 4889 5035 4613 269 414 -307 O HETATM 1190 O HOH A 264 4.030 19.375 21.521 1.00 52.02 O ANISOU 1190 O HOH A 264 7183 5989 6593 431 -65 -602 O HETATM 1191 O HOH A 265 10.330 16.602 23.744 1.00 51.82 O ANISOU 1191 O HOH A 265 6361 6690 6637 -449 -273 -183 O HETATM 1192 O HOH A 266 12.289 21.176 22.448 1.00 52.36 O ANISOU 1192 O HOH A 266 6449 6836 6611 -375 139 219 O HETATM 1193 O HOH A 267 9.417 25.282 22.783 0.50 47.05 O ANISOU 1193 O HOH A 267 6017 5991 5869 371 -266 380 O HETATM 1194 O HOH A 268 10.722 15.580 20.795 1.00 32.51 O ANISOU 1194 O HOH A 268 4085 4205 4063 -168 0 -19 O HETATM 1195 O HOH A 269 5.942 19.732 16.719 1.00 37.94 O ANISOU 1195 O HOH A 269 4863 4613 4937 -291 -189 94 O HETATM 1196 O HOH A 270 6.603 15.287 13.883 1.00 44.38 O ANISOU 1196 O HOH A 270 5598 5892 5374 -346 -3 146 O HETATM 1197 O HOH A 271 5.059 17.123 14.568 1.00 49.19 O ANISOU 1197 O HOH A 271 6611 5952 6128 -371 -241 447 O HETATM 1198 O HOH A 272 -0.295 13.690 23.174 0.50 40.73 O ANISOU 1198 O HOH A 272 5689 4909 4879 -162 -97 -226 O HETATM 1199 O HOH A 273 11.160 9.671 15.827 1.00 20.41 O ANISOU 1199 O HOH A 273 2478 2728 2551 -159 129 17 O HETATM 1200 O HOH A 274 11.057 4.589 20.994 1.00 29.58 O ANISOU 1200 O HOH A 274 3424 4039 3775 -84 108 187 O HETATM 1201 O HOH A 275 7.524 6.750 24.908 0.50 47.23 O ANISOU 1201 O HOH A 275 6261 5937 5748 239 40 264 O HETATM 1202 O HOH A 276 6.382 -1.403 18.536 1.00 41.26 O ANISOU 1202 O HOH A 276 5207 4950 5518 -155 -240 486 O HETATM 1203 O HOH A 277 -0.717 0.342 22.070 1.00 22.45 O ANISOU 1203 O HOH A 277 2823 2943 2766 -38 16 11 O HETATM 1204 O HOH A 278 1.272 -2.103 19.640 1.00 49.44 O ANISOU 1204 O HOH A 278 6376 6433 5977 -187 -19 505 O HETATM 1205 O HOH A 279 -3.970 1.305 16.818 1.00 35.25 O ANISOU 1205 O HOH A 279 4417 4791 4185 15 46 21 O HETATM 1206 O AHOH A 280 2.316 -4.491 12.591 0.50 53.19 O ANISOU 1206 O AHOH A 280 6913 6646 6652 53 35 108 O HETATM 1207 O BHOH A 280 3.637 -4.018 13.268 0.50 47.45 O ANISOU 1207 O BHOH A 280 5805 6178 6046 -86 596 -163 O HETATM 1208 O HOH A 281 -0.167 -4.542 12.698 1.00 46.04 O ANISOU 1208 O HOH A 281 6125 5647 5721 114 112 106 O HETATM 1209 O HOH A 282 -2.011 -5.332 9.324 0.50 44.67 O ANISOU 1209 O HOH A 282 6154 5230 5591 24 -172 14 O HETATM 1210 O HOH A 283 1.732 -5.912 7.763 1.00 51.36 O ANISOU 1210 O HOH A 283 6673 6241 6602 -4 -122 99 O HETATM 1211 O HOH A 284 -3.995 -0.436 4.018 1.00 53.72 O ANISOU 1211 O HOH A 284 6690 7060 6662 395 310 -180 O HETATM 1212 O HOH A 285 8.095 1.054 18.474 1.00 17.35 O ANISOU 1212 O HOH A 285 2164 2327 2102 160 82 -37 O HETATM 1213 O HOH A 286 10.775 2.524 19.064 1.00 34.45 O ANISOU 1213 O HOH A 286 4313 4500 4276 -240 84 -3 O HETATM 1214 O HOH A 287 0.828 2.814 22.769 1.00 43.48 O ANISOU 1214 O HOH A 287 5517 5491 5511 -365 -16 119 O HETATM 1215 O HOH A 288 13.024 -23.544 19.430 1.00 46.15 O ANISOU 1215 O HOH A 288 6014 5672 5849 -15 -42 94 O HETATM 1216 O HOH A 289 20.692 11.381 23.481 1.00 60.55 O ANISOU 1216 O HOH A 289 7487 7692 7827 88 -356 143 O HETATM 1217 O HOH A 290 -10.905 5.234 13.207 1.00 51.45 O ANISOU 1217 O HOH A 290 6044 6790 6714 -1110 264 150 O HETATM 1218 O HOH A 291 10.542 9.827 26.449 1.00 51.78 O ANISOU 1218 O HOH A 291 6494 6695 6484 125 292 -461 O HETATM 1219 O HOH A 292 7.272 17.400 12.746 0.50 48.66 O ANISOU 1219 O HOH A 292 6284 6161 6042 -115 -176 -14 O HETATM 1220 O HOH A 293 18.832 -3.282 1.908 1.00 43.58 O ANISOU 1220 O HOH A 293 5282 5575 5702 193 91 -114 O HETATM 1221 O HOH A 294 -9.515 8.563 19.551 1.00 39.47 O ANISOU 1221 O HOH A 294 4843 5105 5048 101 122 -43 O HETATM 1222 O HOH A 295 7.752 -6.050 -4.745 0.50 47.91 O ANISOU 1222 O HOH A 295 5979 6199 6025 149 277 85 O HETATM 1223 O HOH A 296 3.612 -5.361 -1.384 0.50 41.94 O ANISOU 1223 O HOH A 296 5433 5556 4945 -44 115 368 O HETATM 1224 O HOH A 297 4.552 8.876 2.252 1.00 53.98 O ANISOU 1224 O HOH A 297 6895 6771 6842 -387 -227 143 O HETATM 1225 O HOH A 298 6.828 15.184 26.339 0.50 40.87 O ANISOU 1225 O HOH A 298 5291 5177 5060 163 -182 62 O HETATM 1226 O HOH A 299 3.093 2.002 23.992 0.50 43.20 O ANISOU 1226 O HOH A 299 5203 5733 5480 163 200 118 O HETATM 1227 O HOH A 300 21.239 -21.786 15.362 0.50 43.01 O ANISOU 1227 O HOH A 300 5300 5395 5645 -84 -171 28 O HETATM 1228 O HOH A 301 9.129 13.152 24.944 0.50 44.05 O ANISOU 1228 O HOH A 301 5278 5989 5469 -59 308 91 O HETATM 1229 O HOH A 302 -5.261 15.750 16.667 1.00 52.73 O ANISOU 1229 O HOH A 302 6555 6698 6781 249 380 41 O HETATM 1230 O HOH A 303 10.782 -19.660 7.362 1.00 59.89 O ANISOU 1230 O HOH A 303 7979 7078 7698 61 -204 -543 O HETATM 1231 O HOH A 304 6.936 -13.671 16.349 1.00 51.14 O ANISOU 1231 O HOH A 304 6602 6574 6254 -451 173 286 O HETATM 1232 O HOH A 305 21.992 -0.113 6.090 0.50 49.48 O ANISOU 1232 O HOH A 305 6391 6286 6125 -256 -52 -243 O HETATM 1233 O HOH A 306 6.281 -6.596 22.620 0.50 44.75 O ANISOU 1233 O HOH A 306 5534 5809 5658 -8 -46 -117 O HETATM 1234 O HOH A 307 22.397 -11.426 9.755 0.50 45.15 O ANISOU 1234 O HOH A 307 5737 5899 5520 198 -308 311 O HETATM 1235 O HOH A 308 1.535 15.243 24.357 1.00 59.20 O ANISOU 1235 O HOH A 308 7478 8014 7001 -403 404 260 O HETATM 1236 O HOH A 309 -3.110 -4.424 13.320 0.50 52.66 O ANISOU 1236 O HOH A 309 6647 6871 6490 -9 -172 182 O HETATM 1237 O HOH A 310 4.659 25.209 17.520 0.50 41.85 O ANISOU 1237 O HOH A 310 5024 5404 5472 164 -6 69 O HETATM 1238 O HOH A 311 18.889 13.769 24.616 1.00 60.29 O ANISOU 1238 O HOH A 311 7489 7536 7882 -482 45 160 O HETATM 1239 O HOH A 312 7.855 -16.644 10.989 1.00 56.62 O ANISOU 1239 O HOH A 312 6944 6998 7571 135 -100 -317 O HETATM 1240 O HOH A 313 20.459 -15.868 11.603 0.50 52.32 O ANISOU 1240 O HOH A 313 6199 6808 6872 -62 453 197 O HETATM 1241 O HOH A 314 18.424 15.973 27.223 0.50 47.91 O ANISOU 1241 O HOH A 314 6171 5705 6329 -910 -629 44 O HETATM 1242 O HOH A 315 0.852 18.036 20.815 0.50 46.71 O ANISOU 1242 O HOH A 315 6064 5915 5769 316 82 -293 O HETATM 1243 O HOH A 316 0.009 12.358 3.491 0.50 48.76 O ANISOU 1243 O HOH A 316 5991 6625 5911 -362 483 204 O HETATM 1244 O HOH A 317 22.468 4.942 1.429 0.50 52.84 O ANISOU 1244 O HOH A 317 6361 7215 6502 -302 552 402 O HETATM 1245 O HOH A 318 -9.836 4.417 10.547 0.50 51.65 O ANISOU 1245 O HOH A 318 7023 6245 6357 -700 -700 243 O HETATM 1246 O HOH A 319 -7.418 8.459 20.652 0.50 69.95 O ANISOU 1246 O HOH A 319 9004 8633 8939 -128 -266 -78 O HETATM 1247 O HOH A 320 -9.101 13.538 18.322 0.50 43.53 O ANISOU 1247 O HOH A 320 5631 5380 5529 460 -190 235 O HETATM 1248 O HOH A 321 0.549 -4.167 16.167 1.00 52.41 O ANISOU 1248 O HOH A 321 6890 6525 6499 -332 -143 340 O HETATM 1249 O HOH A 322 -5.879 9.782 2.003 1.00 52.32 O ANISOU 1249 O HOH A 322 6834 6426 6621 534 -483 -25 O HETATM 1250 O HOH A 323 13.333 -20.957 8.183 0.50 38.60 O ANISOU 1250 O HOH A 323 4923 4756 4989 -440 -271 343 O HETATM 1251 O HOH A 324 21.146 -13.892 13.388 0.50 47.44 O ANISOU 1251 O HOH A 324 5777 6283 5964 115 -73 243 O HETATM 1252 O HOH A 325 -3.072 -1.799 2.224 1.00 59.14 O ANISOU 1252 O HOH A 325 7210 7773 7487 190 359 -414 O HETATM 1253 O HOH A 326 4.126 5.064 23.688 1.00 59.21 O ANISOU 1253 O HOH A 326 7887 7536 7074 -115 -455 316 O HETATM 1254 O HOH A 327 3.259 -2.657 17.742 0.50 47.21 O ANISOU 1254 O HOH A 327 5851 5734 6353 63 -189 32 O HETATM 1255 O HOH A 328 5.758 -7.081 20.190 0.50 52.16 O ANISOU 1255 O HOH A 328 6722 6759 6337 -370 50 286 O HETATM 1256 O HOH A 329 3.125 20.622 23.916 0.50 44.11 O ANISOU 1256 O HOH A 329 5487 5555 5717 368 -211 -189 O HETATM 1257 O HOH A 330 -1.823 17.537 19.245 0.50 51.74 O ANISOU 1257 O HOH A 330 6580 6531 6548 117 339 52 O HETATM 1258 O HOH A 331 15.859 12.062 16.887 0.50 41.19 O ANISOU 1258 O HOH A 331 5177 5334 5139 -111 -274 221 O HETATM 1259 O HOH A 332 14.711 4.730 24.259 0.50 50.48 O ANISOU 1259 O HOH A 332 6815 6409 5957 -107 -430 -98 O HETATM 1260 O HOH A 333 -7.733 2.892 16.984 1.00 51.52 O ANISOU 1260 O HOH A 333 6086 6662 6827 -456 182 -69 O HETATM 1261 O HOH A 334 -0.245 -9.563 2.040 0.50 50.45 O ANISOU 1261 O HOH A 334 6225 6220 6724 -240 -85 141 O HETATM 1262 O HOH A 335 5.085 20.930 19.605 0.50 52.42 O ANISOU 1262 O HOH A 335 6627 6901 6390 -30 296 120 O HETATM 1263 O HOH A 336 10.317 -0.500 20.948 0.50 43.47 O ANISOU 1263 O HOH A 336 5472 5724 5320 181 389 44 O HETATM 1264 O HOH A 337 5.184 -13.886 8.559 0.50 39.15 O ANISOU 1264 O HOH A 337 5032 4794 5049 -195 -93 -189 O HETATM 1265 O HOH A 338 9.357 -4.247 1.621 1.00 16.98 O ANISOU 1265 O HOH A 338 2159 2239 2053 -7 71 -24 O HETATM 1266 O HOH A 339 7.165 -2.658 0.758 1.00 20.49 O ANISOU 1266 O HOH A 339 2651 2633 2502 94 102 -55 O HETATM 1267 O HOH A 340 7.676 4.833 23.653 1.00 50.47 O ANISOU 1267 O HOH A 340 6734 6099 6342 -249 -108 451 O HETATM 1268 O HOH A 341 3.593 13.660 1.193 0.50 55.06 O ANISOU 1268 O HOH A 341 7681 6486 6752 -19 -798 20 O HETATM 1269 O HOH A 342 5.861 12.454 -2.050 0.50 41.46 O ANISOU 1269 O HOH A 342 5334 5380 5040 -122 -233 5 O HETATM 1270 O HOH A 343 1.804 10.538 0.690 0.50 57.23 O ANISOU 1270 O HOH A 343 6791 7567 7386 -265 55 421 O HETATM 1271 O HOH A 344 6.923 0.673 22.136 1.00 58.11 O ANISOU 1271 O HOH A 344 7445 7217 7416 348 -157 -255 O HETATM 1272 O HOH A 345 9.543 1.676 20.781 0.50 52.44 O ANISOU 1272 O HOH A 345 6765 6660 6501 47 -223 36 O HETATM 1273 O HOH A 346 13.432 -10.251 -3.484 0.50 50.87 O ANISOU 1273 O HOH A 346 6588 6389 6350 367 -156 -91 O HETATM 1274 O HOH A 347 21.918 -4.211 6.985 0.50 46.71 O ANISOU 1274 O HOH A 347 5830 5982 5937 -95 127 -111 O HETATM 1275 O HOH A 348 6.745 14.858 1.650 1.00 58.02 O ANISOU 1275 O HOH A 348 7335 7338 7374 426 409 -249 O HETATM 1276 O HOH A 349 0.984 -0.991 27.008 0.50 52.61 O ANISOU 1276 O HOH A 349 6853 6757 6381 -106 -172 -42 O HETATM 1277 O HOH A 350 3.957 -7.775 -1.204 0.50 47.34 O ANISOU 1277 O HOH A 350 6555 6017 5416 31 -42 -463 O HETATM 1278 O HOH A 351 -2.254 -0.911 -0.349 0.50 40.19 O ANISOU 1278 O HOH A 351 5177 5084 5009 -170 -483 229 O HETATM 1279 O HOH A 352 -4.139 18.418 13.290 0.50 45.28 O ANISOU 1279 O HOH A 352 6004 5418 5783 -21 -307 -16 O HETATM 1280 O HOH A 353 -4.864 4.164 0.106 0.50 49.66 O ANISOU 1280 O HOH A 353 6024 6389 6454 37 141 -110 O HETATM 1281 O HOH A 354 15.506 16.724 27.779 0.50 63.06 O ANISOU 1281 O HOH A 354 8044 7853 8064 -346 90 176 O HETATM 1282 O HOH A 355 22.853 -12.345 14.054 0.50 46.92 O ANISOU 1282 O HOH A 355 6122 5692 6015 83 -127 -4 O HETATM 1283 O HOH A 356 -5.669 -0.171 1.892 0.50 48.46 O ANISOU 1283 O HOH A 356 6198 6006 6207 -55 -242 -254 O HETATM 1284 O HOH A 357 3.799 -8.894 19.462 0.50 47.13 O ANISOU 1284 O HOH A 357 5856 6099 5951 -102 358 216 O HETATM 1285 O HOH A 358 -6.421 18.240 12.627 0.50 49.47 O ANISOU 1285 O HOH A 358 6528 6008 6260 202 -105 -677 O CONECT 232 720 CONECT 361 814 CONECT 505 938 CONECT 563 616 CONECT 564 617 CONECT 616 563 CONECT 617 564 CONECT 720 232 CONECT 814 361 CONECT 938 505 MASTER 242 0 0 4 7 0 0 6 1284 1 10 10 END