HEADER ELECTRON TRANSPORT 08-AUG-95 1CTJ TITLE CRYSTAL STRUCTURE OF CYTOCHROME C6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C6; COMPND 3 CHAIN: NULL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MONORAPHIDIUM BRAUNII KEYWDS CYTOCHROME, ELECTRON TRANSPORT, HEME EXPDTA X-RAY DIFFRACTION AUTHOR G.M.SHELDRICK REVDAT 1 10-JUN-96 1CTJ 0 JRNL AUTH C.FRAZAO,C.M.SOARES,M.A.CARRONDO,E.POHL,Z.DAUTER, JRNL AUTH 2 K.S.WILSON,M.HERVAS,J.A.NAVARRO,M.A.DE LA ROSA, JRNL AUTH 3 G.M.SHELDRICK JRNL TITL AB INITIO DETERMINATION OF THE CRYSTAL STRUCTURE O JRNL TITL 2 CYTOCHROME C6; COMPARISON WITH PLASTOCYANIN JRNL REF TO BE PUBLISHED JRNL REFN 0353 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.1 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) : 1.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : EVERY 10TH REFLECTION REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1397 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1377 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.1883 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.0 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3265 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 32653 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1198 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.1179 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.1669 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 9.9 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2428 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 24566 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 724 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 43 REMARK 3 SOLVENT ATOMS : 151 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 822.83 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 642.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 12 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 8268 REMARK 3 NUMBER OF RESTRAINTS : 10326 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 ANGLE DISTANCES (A) : 0.033 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.014 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.016 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.148 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.130 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.010 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.043 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.108 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL. V. 91 REMARK 3 (1973) 201-228. REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REMARK 3 REDUCED FREE R (NO CUTOFF) BY 0.077. CHEMICALLY REMARK 3 EQUIVALENT BONDS AND ANGLE DISTANCES IN HEME RESTRAINED REMARK 3 TO BE EQUAL WITHOUT TARGET VALUES. NO GEOMETRIC OR ADP REMARK 3 RESTRAINTS APPLIED TO IRON ATOM. REMARK 4 REMARK 4 1CTJ COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996 REMARK 6 REMARK 6 THE HEME CAB IS COVALENTLY BONDED TO SG CYS 15 AND REMARK 6 THE HEME CAC IS COVALENTLY BONDED TO SG CYS 18. REMARK 6 REMARK 6 THE IRON ATOM IS COORDINATED BY NE2 HIS 19 AND SD MET 61. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAY-1993, JUL-1994 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY REMARK 200 BEAMLINE : X11 AND BW7B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.80, 0.87 REMARK 200 MONOCHROMATOR : GE SINGLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE 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 : 32653 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.10 REMARK 200 RESOLUTION RANGE LOW (A) : 25.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 8.4 REMARK 200 R MERGE (I) : 0.058 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.6 REMARK 200 R MERGE FOR SHELL (I) : 0.520 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.4 REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO REMARK 200 SOFTWARE USED: SHELX REMARK 200 STARTING MODEL FOR MOLECULAR REPLACEMENT: NONE REMARK 200 REMARK 200 REMARK: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: R 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 Z,X,Y REMARK 290 3555 Y,Z,X 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 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 0.169343 0.142722 0.975177 0.00000 REMARK 290 SMTRY2 2 0.985536 -0.024531 -0.167546 0.00000 REMARK 290 SMTRY3 2 0.000000 0.989473 -0.144812 0.00000 REMARK 290 SMTRY1 3 0.169334 0.985580 0.000010 0.00000 REMARK 290 SMTRY2 3 0.142717 -0.024523 0.989445 0.00000 REMARK 290 SMTRY3 3 0.975162 -0.167560 -0.144812 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 HOH 301 LIES ON A SPECIAL POSITION. REMARK 850 REMARK 850 CORRECTION BEFORE RELEASE REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE REMARK 850 DATE REVISED: 05-MAR-1996 TRACKING NUMBER: T6869 DBREF 1CTJ 1 89 SWS Q09099 CYC6_MONBR 1 89 SEQRES 1 89 GLU ALA ASP LEU ALA LEU GLY LYS ALA VAL PHE ASP GLY SEQRES 2 89 ASN CYS ALA ALA CYS HIS ALA GLY GLY GLY ASN ASN VAL SEQRES 3 89 ILE PRO ASP HIS THR LEU GLN LYS ALA ALA ILE GLU GLN SEQRES 4 89 PHE LEU ASP GLY GLY PHE ASN ILE GLU ALA ILE VAL TYR SEQRES 5 89 GLN ILE GLU ASN GLY LYS GLY ALA MET PRO ALA TRP ASP SEQRES 6 89 GLY ARG LEU ASP GLU ASP GLU ILE ALA GLY VAL ALA ALA SEQRES 7 89 TYR VAL TYR ASP GLN ALA ALA GLY ASN LYS TRP HET HEM 91 43 PROTOPORPHYRIN IX CONTAINS FE(II) HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 HEM C34 H32 N4 O4 FE1 FORMUL 3 HOH *151(H2 O1) HELIX 1 1 LEU 4 ASN 14 1 11 HELIX 2 2 ALA 16 GLY 22 1 7 HELIX 3 3 LYS 34 PHE 40 1 7 HELIX 4 4 ILE 47 ASN 56 1 10 HELIX 5 5 GLU 70 ALA 85 1 16 LINK FE HEM 91 NE2 HIS 19 LINK FE HEM 91 SD MET 61 LINK CAB HEM 91 SG CYS 15 LINK CAC HEM 91 SG CYS 18 CRYST1 40.430 40.430 40.430 80.25 80.25 80.25 R 3 3 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 0.024734 -0.004250 -0.003673 0.00000 SCALE2 0.000000 0.025097 -0.003673 0.00000 SCALE3 0.000000 0.000000 0.025364 0.00000 ATOM 1 N AGLU 1 4.127 26.179 -7.903 0.49 57.53 N ANISOU 1 N AGLU 1 9336 7394 4591 4 2737 2771 N ATOM 2 N BGLU 1 3.535 25.488 -12.889 0.51 54.52 N ANISOU 2 N BGLU 1 8406 5015 6783 -887 3093 161 N ATOM 3 CA AGLU 1 5.490 26.607 -8.207 0.49 52.50 C ANISOU 3 CA AGLU 1 9283 5563 4611 -256 2331 1241 C ATOM 4 CA BGLU 1 2.754 26.395 -12.051 0.51 51.27 C ANISOU 4 CA BGLU 1 7663 5124 6212 -653 2258 184 C ATOM 5 C AGLU 1 5.550 27.734 -9.233 0.49 47.55 C ANISOU 5 C AGLU 1 8593 4752 4275 -880 1820 625 C ATOM 6 C BGLU 1 3.471 27.729 -11.891 0.51 49.70 C ANISOU 6 C BGLU 1 7569 5007 5842 -508 1940 356 C ATOM 7 O AGLU 1 4.982 28.809 -8.942 0.49 50.34 O ANISOU 7 O AGLU 1 9167 4991 4495 -653 2505 654 O ATOM 8 O BGLU 1 2.870 28.781 -12.098 0.51 49.78 O ANISOU 8 O BGLU 1 7480 5159 5807 -675 1263 786 O ATOM 9 CB AGLU 1 6.372 25.388 -8.512 0.49 54.41 C ANISOU 9 CB AGLU 1 9844 5815 4504 202 2655 1662 C ATOM 10 CB BGLU 1 2.416 25.770 -10.696 0.51 52.50 C ANISOU 10 CB BGLU 1 7993 5029 6431 -498 2625 275 C ATOM 11 CG AGLU 1 7.853 25.736 -8.366 0.49 54.45 C ANISOU 11 CG AGLU 1 9709 5838 4630 270 3137 1883 C ATOM 12 CG BGLU 1 1.268 26.491 -10.006 0.51 54.28 C ANISOU 12 CG BGLU 1 8362 5060 6692 -274 2826 316 C ATOM 13 CD AGLU 1 8.764 24.531 -8.316 0.49 56.31 C ANISOU 13 CD AGLU 1 9833 5902 5134 390 3584 1746 C ATOM 14 CD BGLU 1 1.720 27.296 -8.799 0.51 55.22 C ANISOU 14 CD BGLU 1 8453 4839 7170 -189 2771 27 C ATOM 15 OE1AGLU 1 8.298 23.411 -8.022 0.49 60.72 O ANISOU 15 OE1AGLU 1 10531 5801 6168 538 4387 1847 O ATOM 16 OE1BGLU 1 2.727 28.028 -8.909 0.51 55.30 O ANISOU 16 OE1BGLU 1 8215 4830 7449 -39 2589 221 O ATOM 17 OE2AGLU 1 9.986 24.743 -8.482 0.49 59.28 O ANISOU 17 OE2AGLU 1 9923 6552 5493 543 4193 1705 O ATOM 18 OE2BGLU 1 1.068 27.166 -7.733 0.51 55.05 O ANISOU 18 OE2BGLU 1 8644 3813 7943 68 3745 -1319 O ATOM 19 N AALA 2 6.254 27.610 -10.341 0.49 39.82 N ANISOU 19 N AALA 2 7654 3389 3714 -1807 1080 -42 N ATOM 20 N BALA 2 4.759 27.656 -11.589 0.51 47.24 N ANISOU 20 N BALA 2 7631 4590 5285 -409 1906 542 N ATOM 21 CA AALA 2 6.531 28.549 -11.391 0.49 40.63 C ANISOU 21 CA AALA 2 7361 3602 4095 -1222 1225 351 C ATOM 22 CA BALA 2 5.670 28.786 -11.571 0.51 44.89 C ANISOU 22 CA BALA 2 7675 4427 4532 -347 1605 344 C ATOM 23 C AALA 2 6.980 27.926 -12.710 0.49 38.03 C ANISOU 23 C AALA 2 6825 3486 3780 -1419 913 486 C ATOM 24 C BALA 2 5.766 29.304 -13.027 0.51 42.80 C ANISOU 24 C BALA 2 7076 4319 4465 -656 1067 288 C ATOM 25 O AALA 2 7.831 27.034 -12.721 0.49 32.72 O ANISOU 25 O AALA 2 6176 3181 2768 -1904 955 767 O ATOM 26 O BALA 2 5.165 30.351 -13.297 0.51 41.12 O ANISOU 26 O BALA 2 6460 4299 4478 -808 844 85 O ATOM 27 CB AALA 2 7.686 29.468 -10.955 0.49 40.12 C ANISOU 27 CB AALA 2 7798 3061 4009 -1414 1633 120 C ATOM 28 CB BALA 2 7.039 28.354 -11.070 0.51 43.42 C ANISOU 28 CB BALA 2 8061 3737 4290 -344 1209 342 C ATOM 29 N ASP 3 6.482 28.531 -13.792 1.00 36.71 N ANISOU 29 N ASP 3 5896 3597 4111 -1331 966 632 N ATOM 30 CA ASP 3 6.844 28.172 -15.120 1.00 32.51 C ANISOU 30 CA ASP 3 4585 3556 3905 -1164 821 1133 C ATOM 31 C ASP 3 8.056 28.945 -15.623 1.00 30.43 C ANISOU 31 C ASP 3 4412 2909 3955 -1173 125 1268 C ATOM 32 O ASP 3 7.982 29.944 -16.316 1.00 26.86 O ANISOU 32 O ASP 3 4464 2724 2767 -534 924 734 O ATOM 33 CB ASP 3 5.712 28.262 -16.130 1.00 31.89 C ANISOU 33 CB ASP 3 3993 3698 4128 -1237 1046 1260 C ATOM 34 CG ASP 3 5.940 27.498 -17.420 1.00 34.79 C ANISOU 34 CG ASP 3 4742 4113 4037 -1367 616 1086 C ATOM 35 OD1 ASP 3 7.066 27.105 -17.813 1.00 31.55 O ANISOU 35 OD1 ASP 3 5104 3035 3550 -597 -175 403 O ATOM 36 OD2 ASP 3 4.871 27.304 -18.059 1.00 41.40 O ANISOU 36 OD2 ASP 3 4765 5332 5244 -1726 456 324 O ATOM 37 N LEU 4 9.232 28.418 -15.235 1.00 29.63 N ANISOU 37 N LEU 4 4479 2960 3541 -1017 207 1165 N ATOM 38 CA LEU 4 10.475 29.110 -15.536 1.00 27.52 C ANISOU 38 CA LEU 4 4296 2448 3452 -703 270 873 C ATOM 39 C LEU 4 10.887 29.007 -16.996 1.00 25.31 C ANISOU 39 C LEU 4 3783 2092 3505 -542 207 698 C ATOM 40 O LEU 4 11.545 29.902 -17.487 1.00 25.04 O ANISOU 40 O LEU 4 3736 1950 3591 -330 231 975 O ATOM 41 CB LEU 4 11.613 28.571 -14.648 1.00 28.52 C ANISOU 41 CB LEU 4 4427 2620 3521 -541 231 916 C ATOM 42 CG LEU 4 11.456 28.737 -13.141 1.00 30.06 C ANISOU 42 CG LEU 4 4620 2978 3541 -600 83 903 C ATOM 43 CD1 LEU 4 12.684 28.114 -12.481 1.00 34.36 C ANISOU 43 CD1 LEU 4 5087 4058 3588 171 309 1353 C ATOM 44 CD2 LEU 4 11.245 30.212 -12.805 1.00 36.41 C ANISOU 44 CD2 LEU 4 6307 3354 3830 279 190 517 C ATOM 45 N ALA 5 10.452 27.940 -17.673 1.00 25.52 N ANISOU 45 N ALA 5 3717 2003 3736 -373 183 681 N ATOM 46 CA ALA 5 10.822 27.868 -19.105 1.00 24.02 C ANISOU 46 CA ALA 5 3151 1934 3815 -179 147 403 C ATOM 47 C ALA 5 10.081 28.943 -19.872 1.00 19.56 C ANISOU 47 C ALA 5 2687 1468 3094 -319 330 -48 C ATOM 48 O ALA 5 10.654 29.635 -20.711 1.00 20.74 O ANISOU 48 O ALA 5 2734 1631 3322 -219 620 81 O ATOM 49 CB ALA 5 10.527 26.477 -19.667 1.00 29.14 C ANISOU 49 CB ALA 5 4541 1532 4726 97 993 289 C ATOM 50 N LEU 6 8.812 29.076 -19.527 1.00 19.79 N ANISOU 50 N LEU 6 2916 1473 2946 -245 738 218 N ATOM 51 CA LEU 6 8.007 30.156 -20.133 1.00 19.22 C ANISOU 51 CA LEU 6 2503 1596 3024 -447 436 93 C ATOM 52 C LEU 6 8.600 31.515 -19.791 1.00 17.06 C ANISOU 52 C LEU 6 2325 1406 2590 -240 745 6 C ATOM 53 O LEU 6 8.741 32.377 -20.664 1.00 17.55 O ANISOU 53 O LEU 6 2356 1541 2607 -137 571 167 O ATOM 54 CB LEU 6 6.525 30.073 -19.719 1.00 20.86 C ANISOU 54 CB LEU 6 2446 2007 3278 -512 480 -22 C ATOM 55 CG LEU 6 5.587 31.190 -20.187 1.00 23.72 C ANISOU 55 CG LEU 6 2618 2255 3917 -241 600 141 C ATOM 56 CD1 LEU 6 5.527 31.116 -21.700 1.00 25.58 C ANISOU 56 CD1 LEU 6 3476 2036 3965 261 124 80 C ATOM 57 CD2 LEU 6 4.185 31.110 -19.583 1.00 31.74 C ANISOU 57 CD2 LEU 6 2559 4190 5013 251 687 1412 C ATOM 58 N GLY 7 8.931 31.681 -18.498 1.00 18.07 N ANISOU 58 N GLY 7 2471 1635 2591 -277 669 68 N ATOM 59 CA GLY 7 9.479 32.968 -18.135 1.00 16.99 C ANISOU 59 CA GLY 7 2351 1612 2334 -254 643 92 C ATOM 60 C GLY 7 10.761 33.312 -18.862 1.00 15.95 C ANISOU 60 C GLY 7 2260 1492 2158 -95 524 164 C ATOM 61 O GLY 7 10.985 34.474 -19.189 1.00 16.58 O ANISOU 61 O GLY 7 2497 1419 2227 -202 681 46 O ATOM 62 N LYS 8 11.650 32.326 -19.080 1.00 16.64 N ANISOU 62 N LYS 8 2248 1531 2388 -102 476 169 N ATOM 63 CA LYS 8 12.885 32.617 -19.813 1.00 16.76 C ANISOU 63 CA LYS 8 2151 1708 2350 -14 462 183 C ATOM 64 C LYS 8 12.566 32.997 -21.259 1.00 15.57 C ANISOU 64 C LYS 8 2173 1372 2223 29 495 -76 C ATOM 65 O LYS 8 13.218 33.892 -21.810 1.00 15.82 O ANISOU 65 O LYS 8 2274 1464 2126 37 381 -7 O ATOM 66 CB ALYS 8 13.723 31.323 -19.829 0.55 19.80 C ANISOU 66 CB ALYS 8 2247 2136 2955 346 176 158 C ATOM 67 CB BLYS 8 13.887 31.468 -19.713 0.45 19.88 C ANISOU 67 CB BLYS 8 2252 2239 2877 324 144 87 C ATOM 68 CG ALYS 8 14.938 31.471 -20.772 0.55 21.53 C ANISOU 68 CG ALYS 8 2299 2680 2999 479 255 -166 C ATOM 69 CG BLYS 8 15.287 31.806 -20.269 0.45 19.35 C ANISOU 69 CG BLYS 8 1920 2092 3159 85 -238 -569 C ATOM 70 CD ALYS 8 15.673 30.146 -20.835 0.55 24.31 C ANISOU 70 CD ALYS 8 2866 2962 3179 862 263 -217 C ATOM 71 CD BLYS 8 16.261 30.680 -20.023 0.45 21.77 C ANISOU 71 CD BLYS 8 2210 2532 3326 437 -456 -650 C ATOM 72 CE ALYS 8 17.118 30.365 -21.275 0.55 25.41 C ANISOU 72 CE ALYS 8 2599 3074 3745 923 -20 -550 C ATOM 73 CE BLYS 8 17.688 30.890 -20.511 0.45 23.91 C ANISOU 73 CE BLYS 8 2129 3132 3599 632 -478 -588 C ATOM 74 NZ ALYS 8 17.216 31.254 -22.466 0.55 28.30 N ANISOU 74 NZ ALYS 8 2886 2496 5105 713 930 17 N ATOM 75 NZ BLYS 8 18.400 29.574 -20.644 0.45 33.84 N ANISOU 75 NZ BLYS 8 3413 4001 5126 1668 390 -534 N ATOM 76 N ALA 9 11.618 32.312 -21.895 1.00 16.25 N ANISOU 76 N ALA 9 2362 1468 2193 -75 609 -127 N ATOM 77 CA ALA 9 11.279 32.689 -23.275 1.00 16.04 C ANISOU 77 CA ALA 9 2236 1509 2196 82 506 -282 C ATOM 78 C ALA 9 10.775 34.122 -23.374 1.00 15.54 C ANISOU 78 C ALA 9 2211 1475 2074 -22 666 -192 C ATOM 79 O ALA 9 11.110 34.909 -24.256 1.00 15.41 O ANISOU 79 O ALA 9 2177 1620 1914 43 526 -150 O ATOM 80 CB ALA 9 10.261 31.696 -23.840 1.00 18.69 C ANISOU 80 CB ALA 9 3031 1560 2338 -269 293 -243 C ATOM 81 N VAL 10 9.900 34.494 -22.382 1.00 14.67 N ANISOU 81 N VAL 10 1912 1420 2104 -35 513 -122 N ATOM 82 CA VAL 10 9.374 35.863 -22.333 1.00 14.03 C ANISOU 82 CA VAL 10 1687 1503 2008 -41 335 -286 C ATOM 83 C VAL 10 10.525 36.838 -22.076 1.00 12.58 C ANISOU 83 C VAL 10 1679 1410 1574 -18 393 -223 C ATOM 84 O VAL 10 10.605 37.893 -22.682 1.00 14.00 O ANISOU 84 O VAL 10 1906 1476 1807 113 401 -62 O ATOM 85 CB VAL 10 8.263 35.953 -21.275 1.00 14.54 C ANISOU 85 CB VAL 10 1851 1506 2031 14 518 101 C ATOM 86 CG1 VAL 10 7.805 37.404 -21.067 1.00 16.97 C ANISOU 86 CG1 VAL 10 1910 1721 2658 205 740 -169 C ATOM 87 CG2 VAL 10 7.059 35.108 -21.654 1.00 19.50 C ANISOU 87 CG2 VAL 10 1988 2110 3129 -444 697 -36 C ATOM 88 N PHE 11 11.431 36.505 -21.177 1.00 12.93 N ANISOU 88 N PHE 11 1689 1462 1640 -38 379 -180 N ATOM 89 CA PHE 11 12.547 37.360 -20.851 1.00 12.11 C ANISOU 89 CA PHE 11 1790 1343 1354 -113 421 -27 C ATOM 90 C PHE 11 13.384 37.618 -22.101 1.00 12.76 C ANISOU 90 C PHE 11 1848 1459 1420 -8 476 -113 C ATOM 91 O PHE 11 13.745 38.748 -22.429 1.00 13.26 O ANISOU 91 O PHE 11 1809 1553 1550 -130 541 -26 O ATOM 92 CB PHE 11 13.390 36.740 -19.721 1.00 13.00 C ANISOU 92 CB PHE 11 1852 1410 1557 43 327 -8 C ATOM 93 CG PHE 11 14.499 37.664 -19.247 1.00 12.81 C ANISOU 93 CG PHE 11 1892 1338 1517 -15 213 168 C ATOM 94 CD1 PHE 11 15.764 37.669 -19.833 1.00 14.74 C ANISOU 94 CD1 PHE 11 1902 1773 1787 68 335 167 C ATOM 95 CD2 PHE 11 14.248 38.518 -18.196 1.00 13.63 C ANISOU 95 CD2 PHE 11 1889 1588 1574 -17 196 50 C ATOM 96 CE1 PHE 11 16.738 38.539 -19.377 1.00 15.40 C ANISOU 96 CE1 PHE 11 1871 1804 2034 -12 191 426 C ATOM 97 CE2 PHE 11 15.237 39.374 -17.734 1.00 14.71 C ANISOU 97 CE2 PHE 11 2361 1532 1559 -58 -45 20 C ATOM 98 CZ PHE 11 16.476 39.352 -18.295 1.00 15.91 C ANISOU 98 CZ PHE 11 2144 1903 1849 -415 -115 356 C ATOM 99 N ASP 12 13.793 36.527 -22.787 1.00 13.88 N ANISOU 99 N ASP 12 1904 1624 1615 30 628 -155 N ATOM 100 CA ASP 12 14.673 36.680 -23.952 1.00 15.28 C ANISOU 100 CA ASP 12 2121 1866 1674 290 762 -201 C ATOM 101 C ASP 12 13.994 37.450 -25.062 1.00 15.53 C ANISOU 101 C ASP 12 2260 1923 1572 194 784 -154 C ATOM 102 O ASP 12 14.667 38.220 -25.752 1.00 19.71 O ANISOU 102 O ASP 12 2728 2970 1606 -121 872 210 O ATOM 103 CB ASP 12 15.182 35.307 -24.355 1.00 19.23 C ANISOU 103 CB ASP 12 2750 2121 2255 597 965 -263 C ATOM 104 CG ASP 12 16.187 34.671 -23.394 1.00 20.36 C ANISOU 104 CG ASP 12 2245 2087 3211 474 801 -35 C ATOM 105 OD1 ASP 12 16.755 35.349 -22.507 1.00 23.88 O ANISOU 105 OD1 ASP 12 2851 2735 3261 760 321 -216 O ATOM 106 OD2 ASP 12 16.400 33.435 -23.537 1.00 29.91 O ANISOU 106 OD2 ASP 12 4021 2476 4586 1391 217 -533 O ATOM 107 N GLY 13 12.679 37.294 -25.213 1.00 15.89 N ANISOU 107 N GLY 13 2393 1908 1586 192 505 -320 N ATOM 108 CA GLY 13 11.980 37.998 -26.241 1.00 17.18 C ANISOU 108 CA GLY 13 2712 1984 1671 -54 131 -429 C ATOM 109 C GLY 13 11.676 39.449 -26.007 1.00 15.97 C ANISOU 109 C GLY 13 2505 1949 1466 68 347 -101 C ATOM 110 O GLY 13 11.441 40.200 -26.969 1.00 21.33 O ANISOU 110 O GLY 13 3824 2500 1579 196 -92 184 O ATOM 111 N ASN 14 11.606 39.862 -24.752 1.00 13.90 N ANISOU 111 N ASN 14 2052 1658 1442 41 219 -91 N ATOM 112 CA ASN 14 11.131 41.181 -24.429 1.00 14.03 C ANISOU 112 CA ASN 14 2043 1666 1489 160 67 -2 C ATOM 113 C ASN 14 12.007 41.979 -23.482 1.00 14.18 C ANISOU 113 C ASN 14 2227 1519 1510 -164 30 202 C ATOM 114 O ASN 14 11.957 43.214 -23.540 1.00 20.59 O ANISOU 114 O ASN 14 3673 1511 2445 -99 -723 292 O ATOM 115 CB ASN 14 9.759 41.042 -23.735 1.00 15.06 C ANISOU 115 CB ASN 14 2020 1873 1688 78 227 -82 C ATOM 116 CG ASN 14 8.736 40.424 -24.648 1.00 16.53 C ANISOU 116 CG ASN 14 2062 2081 1982 126 16 47 C ATOM 117 OD1 ASN 14 8.158 41.015 -25.547 1.00 20.29 O ANISOU 117 OD1 ASN 14 2564 2575 2381 226 -399 272 O ATOM 118 ND2 ASN 14 8.535 39.109 -24.471 1.00 16.92 N ANISOU 118 ND2 ASN 14 1938 2103 2228 -89 101 -31 N ATOM 119 N CYS 15 12.749 41.389 -22.612 1.00 12.20 N ANISOU 119 N CYS 15 1698 1490 1335 114 285 -77 N ATOM 120 CA CYS 15 13.466 42.024 -21.546 1.00 11.82 C ANISOU 120 CA CYS 15 1679 1486 1217 66 398 -186 C ATOM 121 C CYS 15 14.973 42.084 -21.765 1.00 12.19 C ANISOU 121 C CYS 15 1666 1516 1335 47 375 -87 C ATOM 122 O CYS 15 15.606 42.977 -21.258 1.00 12.74 O ANISOU 122 O CYS 15 1790 1620 1311 -118 553 2 O ATOM 123 CB CYS 15 13.204 41.333 -20.194 1.00 12.23 C ANISOU 123 CB CYS 15 1651 1618 1264 143 446 -41 C ATOM 124 SG CYS 15 11.507 40.860 -19.873 1.00 13.03 S ANISOU 124 SG CYS 15 1910 1464 1454 6 600 -77 S ATOM 125 N ALA 16 15.504 41.147 -22.538 1.00 13.33 N ANISOU 125 N ALA 16 1528 1765 1649 214 192 -293 N ATOM 126 CA ALA 16 16.947 41.058 -22.779 1.00 13.94 C ANISOU 126 CA ALA 16 1606 1801 1759 175 399 -88 C ATOM 127 C ALA 16 17.482 42.245 -23.545 1.00 15.17 C ANISOU 127 C ALA 16 2043 2043 1535 173 536 7 C ATOM 128 O ALA 16 18.688 42.503 -23.517 1.00 16.69 O ANISOU 128 O ALA 16 1990 1905 2289 99 631 187 O ATOM 129 CB ALA 16 17.246 39.782 -23.543 1.00 17.22 C ANISOU 129 CB ALA 16 1784 2083 2513 126 660 -560 C ATOM 130 N ALA 17 16.618 43.036 -24.196 1.00 14.81 N ANISOU 130 N ALA 17 2198 2142 1147 60 449 10 N ATOM 131 CA ALA 17 17.036 44.269 -24.876 1.00 16.50 C ANISOU 131 CA ALA 17 2769 2203 1143 109 445 61 C ATOM 132 C ALA 17 17.685 45.228 -23.897 1.00 14.58 C ANISOU 132 C ALA 17 2173 1986 1246 155 553 191 C ATOM 133 O ALA 17 18.468 46.083 -24.325 1.00 16.53 O ANISOU 133 O ALA 17 2578 2114 1434 6 724 294 O ATOM 134 CB ALA 17 15.804 44.929 -25.465 1.00 23.94 C ANISOU 134 CB ALA 17 3894 2695 2281 248 -901 299 C ATOM 135 N CYS 18 17.279 45.186 -22.618 1.00 12.61 N ANISOU 135 N CYS 18 1977 1630 1064 156 286 233 N ATOM 136 CA CYS 18 17.810 46.086 -21.627 1.00 11.93 C ANISOU 136 CA CYS 18 1653 1602 1167 36 333 313 C ATOM 137 C CYS 18 18.467 45.400 -20.445 1.00 11.31 C ANISOU 137 C CYS 18 1607 1517 1069 15 344 167 C ATOM 138 O CYS 18 19.165 46.052 -19.684 1.00 13.34 O ANISOU 138 O CYS 18 1918 1599 1426 -146 24 262 O ATOM 139 CB CYS 18 16.691 46.988 -21.097 1.00 12.28 C ANISOU 139 CB CYS 18 1961 1352 1237 149 325 233 C ATOM 140 SG CYS 18 16.018 48.028 -22.425 1.00 14.00 S ANISOU 140 SG CYS 18 2167 1759 1262 258 447 470 S ATOM 141 N HIS 19 18.241 44.119 -20.249 1.00 11.81 N ANISOU 141 N HIS 19 1860 1430 1085 98 355 207 N ATOM 142 CA HIS 19 18.626 43.402 -19.037 1.00 11.21 C ANISOU 142 CA HIS 19 1753 1419 983 45 263 122 C ATOM 143 C HIS 19 19.331 42.091 -19.280 1.00 11.46 C ANISOU 143 C HIS 19 1689 1474 1083 122 275 150 C ATOM 144 O HIS 19 19.430 41.268 -18.363 1.00 12.87 O ANISOU 144 O HIS 19 1865 1635 1269 261 440 281 O ATOM 145 CB HIS 19 17.385 43.116 -18.171 1.00 11.83 C ANISOU 145 CB HIS 19 1959 1308 1117 187 504 141 C ATOM 146 CG HIS 19 16.646 44.283 -17.629 1.00 11.48 C ANISOU 146 CG HIS 19 2079 1165 1012 303 327 182 C ATOM 147 ND1 HIS 19 17.192 45.153 -16.726 1.00 12.11 N ANISOU 147 ND1 HIS 19 2039 1410 1038 288 270 37 N ATOM 148 CD2 HIS 19 15.354 44.655 -17.762 1.00 11.28 C ANISOU 148 CD2 HIS 19 1914 1220 1046 133 353 74 C ATOM 149 CE1 HIS 19 16.223 46.009 -16.352 1.00 12.49 C ANISOU 149 CE1 HIS 19 2019 1418 1190 340 74 -60 C ATOM 150 NE2 HIS 19 15.074 45.737 -16.966 1.00 11.37 N ANISOU 150 NE2 HIS 19 1964 1248 1001 236 227 63 N ATOM 151 N ALA 20 19.896 41.838 -20.483 1.00 12.23 N ANISOU 151 N ALA 20 1664 1583 1285 206 480 258 N ATOM 152 CA ALA 20 20.590 40.564 -20.699 1.00 13.89 C ANISOU 152 CA ALA 20 1994 1761 1393 397 484 88 C ATOM 153 C ALA 20 21.715 40.399 -19.681 1.00 13.70 C ANISOU 153 C ALA 20 1983 1581 1512 340 382 146 C ATOM 154 O ALA 20 22.408 41.371 -19.355 1.00 15.35 O ANISOU 154 O ALA 20 1894 1821 1973 174 369 245 O ATOM 155 CB ALA 20 21.131 40.466 -22.123 1.00 16.23 C ANISOU 155 CB ALA 20 2486 2053 1477 495 630 112 C ATOM 156 N GLY 21 21.859 39.177 -19.146 1.00 14.58 N ANISOU 156 N GLY 21 2039 1584 1779 357 305 41 N ATOM 157 CA GLY 21 22.878 38.914 -18.160 1.00 16.60 C ANISOU 157 CA GLY 21 2531 1698 1923 844 233 221 C ATOM 158 C GLY 21 22.533 39.438 -16.774 1.00 15.55 C ANISOU 158 C GLY 21 2335 1557 1869 529 86 143 C ATOM 159 O GLY 21 23.389 39.418 -15.878 1.00 19.71 O ANISOU 159 O GLY 21 2597 2664 2043 634 -154 393 O ATOM 160 N GLY 22 21.339 39.974 -16.592 1.00 14.21 N ANISOU 160 N GLY 22 2139 1529 1596 284 165 87 N ATOM 161 CA GLY 22 20.891 40.484 -15.305 1.00 14.60 C ANISOU 161 CA GLY 22 2556 1439 1416 279 193 239 C ATOM 162 C GLY 22 21.279 41.905 -15.006 1.00 13.46 C ANISOU 162 C GLY 22 2231 1361 1397 343 205 235 C ATOM 163 O GLY 22 21.107 42.343 -13.851 1.00 16.59 O ANISOU 163 O GLY 22 2883 1906 1359 104 351 30 O ATOM 164 N GLY 23 21.789 42.639 -15.986 1.00 13.65 N ANISOU 164 N GLY 23 2250 1420 1387 237 93 222 N ATOM 165 CA GLY 23 22.174 44.005 -15.812 1.00 14.21 C ANISOU 165 CA GLY 23 2048 1448 1771 22 63 182 C ATOM 166 C GLY 23 21.054 45.000 -16.116 1.00 13.37 C ANISOU 166 C GLY 23 2079 1438 1436 19 64 156 C ATOM 167 O GLY 23 19.893 44.629 -16.119 1.00 14.19 O ANISOU 167 O GLY 23 2036 1468 1755 -40 80 189 O ATOM 168 N ASN 24 21.467 46.234 -16.375 1.00 13.58 N ANISOU 168 N ASN 24 1902 1459 1670 20 138 272 N ATOM 169 CA ASN 24 20.513 47.284 -16.795 1.00 13.79 C ANISOU 169 CA ASN 24 2013 1479 1619 77 194 231 C ATOM 170 C ASN 24 21.307 48.244 -17.703 1.00 14.11 C ANISOU 170 C ASN 24 2115 1529 1585 -65 -12 379 C ATOM 171 O ASN 24 22.195 48.961 -17.214 1.00 17.44 O ANISOU 171 O ASN 24 2543 1985 1934 -523 -154 359 O ATOM 172 CB ASN 24 19.960 47.997 -15.594 1.00 13.72 C ANISOU 172 CB ASN 24 2203 1358 1524 -101 107 130 C ATOM 173 CG ASN 24 18.865 48.943 -15.965 1.00 14.81 C ANISOU 173 CG ASN 24 2712 1517 1258 300 131 -28 C ATOM 174 OD1 ASN 24 18.874 49.632 -17.022 1.00 15.79 O ANISOU 174 OD1 ASN 24 2628 1631 1592 32 253 397 O ATOM 175 ND2 ASN 24 17.843 49.015 -15.134 1.00 14.49 N ANISOU 175 ND2 ASN 24 2485 1473 1411 161 167 396 N ATOM 176 N ASN 25 20.988 48.235 -19.000 1.00 14.08 N ANISOU 176 N ASN 25 1920 1754 1544 -218 313 181 N ATOM 177 CA ASN 25 21.797 49.056 -19.915 1.00 16.64 C ANISOU 177 CA ASN 25 2368 1853 1947 -193 424 612 C ATOM 178 C ASN 25 21.492 50.548 -19.805 1.00 17.26 C ANISOU 178 C ASN 25 2413 1896 2086 -221 280 647 C ATOM 179 O ASN 25 22.197 51.362 -20.383 1.00 23.87 O ANISOU 179 O ASN 25 3321 1999 3527 -397 1234 789 O ATOM 180 CB ASN 25 21.529 48.620 -21.323 1.00 16.41 C ANISOU 180 CB ASN 25 2221 2017 1844 -9 673 710 C ATOM 181 CG ASN 25 21.802 47.178 -21.598 1.00 16.18 C ANISOU 181 CG ASN 25 2128 2102 1765 40 789 547 C ATOM 182 OD1 ASN 25 22.549 46.503 -20.854 1.00 17.87 O ANISOU 182 OD1 ASN 25 2404 2007 2212 176 502 418 O ATOM 183 ND2 ASN 25 21.250 46.651 -22.676 1.00 17.98 N ANISOU 183 ND2 ASN 25 2440 2404 1819 332 766 330 N ATOM 184 N VAL 26 20.345 50.879 -19.215 1.00 15.94 N ANISOU 184 N VAL 26 2522 1622 1763 -234 262 365 N ATOM 185 CA VAL 26 19.861 52.270 -19.156 1.00 17.76 C ANISOU 185 CA VAL 26 3046 1583 1951 -129 194 452 C ATOM 186 C VAL 26 20.304 52.939 -17.885 1.00 18.10 C ANISOU 186 C VAL 26 3261 1373 2072 -128 8 543 C ATOM 187 O VAL 26 20.876 54.043 -17.978 1.00 23.25 O ANISOU 187 O VAL 26 4457 1700 2457 -724 -543 729 O ATOM 188 CB VAL 26 18.338 52.323 -19.352 1.00 18.22 C ANISOU 188 CB VAL 26 3142 1780 1828 284 -9 454 C ATOM 189 CG1 VAL 26 17.845 53.755 -19.341 1.00 21.81 C ANISOU 189 CG1 VAL 26 3660 1818 2603 342 -229 394 C ATOM 190 CG2 VAL 26 17.957 51.618 -20.644 1.00 20.35 C ANISOU 190 CG2 VAL 26 3342 2233 1967 146 -110 275 C ATOM 191 N ILE 27 20.099 52.336 -16.736 1.00 18.78 N ANISOU 191 N ILE 27 3432 1608 1918 -1 -160 531 N ATOM 192 CA ILE 27 20.505 52.839 -15.425 1.00 20.98 C ANISOU 192 CA ILE 27 3815 1866 2093 -352 -347 312 C ATOM 193 C ILE 27 21.332 51.743 -14.754 1.00 19.34 C ANISOU 193 C ILE 27 3453 1847 1868 -506 -419 251 C ATOM 194 O ILE 27 20.796 50.758 -14.250 1.00 18.20 O ANISOU 194 O ILE 27 3111 1691 1941 -326 -300 53 O ATOM 195 CB ILE 27 19.319 53.198 -14.538 1.00 22.58 C ANISOU 195 CB ILE 27 4419 1818 2129 114 -147 236 C ATOM 196 CG1 ILE 27 18.335 54.164 -15.179 1.00 24.97 C ANISOU 196 CG1 ILE 27 4866 1738 2648 410 -104 252 C ATOM 197 CG2 ILE 27 19.840 53.671 -13.175 1.00 28.67 C ANISOU 197 CG2 ILE 27 5492 2665 2466 409 -453 -370 C ATOM 198 CD1 ILE 27 17.161 54.495 -14.305 1.00 37.60 C ANISOU 198 CD1 ILE 27 5798 3608 4526 1588 648 -541 C ATOM 199 N PRO 28 22.645 51.761 -14.978 1.00 23.21 N ANISOU 199 N PRO 28 3447 2260 2894 -732 -446 628 N ATOM 200 CA PRO 28 23.470 50.586 -14.688 1.00 22.54 C ANISOU 200 CA PRO 28 3350 2468 2533 -479 -158 389 C ATOM 201 C PRO 28 23.445 50.045 -13.273 1.00 21.59 C ANISOU 201 C PRO 28 3363 2119 2519 -705 -526 336 C ATOM 202 O PRO 28 23.631 48.822 -13.137 1.00 25.17 O ANISOU 202 O PRO 28 4011 2269 3046 -186 -227 379 O ATOM 203 CB PRO 28 24.897 51.035 -15.090 1.00 28.30 C ANISOU 203 CB PRO 28 3451 3599 3437 -584 53 859 C ATOM 204 CG PRO 28 24.605 52.054 -16.119 1.00 32.21 C ANISOU 204 CG PRO 28 4099 3789 4047 -696 458 1418 C ATOM 205 CD PRO 28 23.398 52.841 -15.682 1.00 28.26 C ANISOU 205 CD PRO 28 3979 2952 3541 -904 -39 1132 C ATOM 206 N ASP 29 23.113 50.832 -12.246 1.00 22.84 N ANISOU 206 N ASP 29 3955 2152 2357 -396 -750 381 N ATOM 207 CA ASP 29 23.111 50.207 -10.928 1.00 22.30 C ANISOU 207 CA ASP 29 4025 1801 2439 -427 -822 278 C ATOM 208 C ASP 29 21.777 49.565 -10.599 1.00 20.11 C ANISOU 208 C ASP 29 3856 1577 2019 -139 -626 76 C ATOM 209 O ASP 29 21.699 48.822 -9.609 1.00 21.05 O ANISOU 209 O ASP 29 3840 2092 1867 -13 -488 100 O ATOM 210 CB AASP 29 23.287 51.321 -9.870 0.35 25.48 C ANISOU 210 CB AASP 29 4532 2344 2566 -689 -1207 38 C ATOM 211 CB BASP 29 23.577 51.167 -9.853 0.65 25.70 C ANISOU 211 CB BASP 29 4566 2352 2605 -757 -1111 144 C ATOM 212 CG AASP 29 24.657 51.958 -9.850 0.35 27.52 C ANISOU 212 CG AASP 29 4589 2699 2908 -849 -1163 -12 C ATOM 213 CG BASP 29 22.649 52.344 -9.710 0.65 26.54 C ANISOU 213 CG BASP 29 5070 2325 2440 -609 -1428 -416 C ATOM 214 OD1AASP 29 25.663 51.230 -9.749 0.35 32.39 O ANISOU 214 OD1AASP 29 4466 3317 4219 -716 -537 804 O ATOM 215 OD1BASP 29 21.772 52.591 -10.548 0.65 31.14 O ANISOU 215 OD1BASP 29 5768 2761 3010 -125 -1819 52 O ATOM 216 OD2AASP 29 24.712 53.195 -9.983 0.35 34.82 O ANISOU 216 OD2AASP 29 4759 2766 5379 -963 -134 116 O ATOM 217 OD2BASP 29 22.903 53.117 -8.752 0.65 38.07 O ANISOU 217 OD2BASP 29 7651 3647 2811 -319 -1600 -1308 O ATOM 218 N HIS 30 20.759 49.759 -11.454 1.00 20.10 N ANISOU 218 N HIS 30 3598 1832 2018 139 -406 27 N ATOM 219 CA HIS 30 19.443 49.198 -11.120 1.00 18.22 C ANISOU 219 CA HIS 30 3612 1689 1450 207 -144 -112 C ATOM 220 C HIS 30 19.269 47.830 -11.762 1.00 17.20 C ANISOU 220 C HIS 30 3556 1649 1170 220 15 -54 C ATOM 221 O HIS 30 18.461 47.578 -12.647 1.00 16.40 O ANISOU 221 O HIS 30 3089 1588 1399 43 146 55 O ATOM 222 CB AHIS 30 18.297 50.130 -11.517 0.35 19.99 C ANISOU 222 CB AHIS 30 3672 1757 1979 390 87 -79 C ATOM 223 CB BHIS 30 18.331 50.149 -11.568 0.65 20.69 C ANISOU 223 CB BHIS 30 3694 1805 2167 461 130 1 C ATOM 224 CG AHIS 30 17.948 51.228 -10.563 0.35 20.83 C ANISOU 224 CG AHIS 30 3854 1862 2003 382 101 -153 C ATOM 225 CG BHIS 30 18.246 51.407 -10.762 0.65 20.75 C ANISOU 225 CG BHIS 30 3814 1929 1948 453 63 -9 C ATOM 226 ND1AHIS 30 16.653 51.587 -10.259 0.35 20.51 N ANISOU 226 ND1AHIS 30 3879 1866 1856 457 11 -241 N ATOM 227 ND1BHIS 30 19.273 52.041 -10.104 0.65 23.23 N ANISOU 227 ND1BHIS 30 3779 2023 2807 304 138 -305 N ATOM 228 CD2AHIS 30 18.711 52.087 -9.847 0.35 21.71 C ANISOU 228 CD2AHIS 30 3832 1860 2356 328 263 -340 C ATOM 229 CD2BHIS 30 17.178 52.226 -10.610 0.65 20.33 C ANISOU 229 CD2BHIS 30 3716 1852 1967 331 358 -50 C ATOM 230 CE1AHIS 30 16.651 52.590 -9.389 0.35 19.95 C ANISOU 230 CE1AHIS 30 3720 1647 2025 304 -14 -194 C ATOM 231 CE1BHIS 30 18.846 53.136 -9.488 0.65 21.73 C ANISOU 231 CE1BHIS 30 3622 1895 2534 251 306 -129 C ATOM 232 NE2AHIS 30 17.897 52.909 -9.121 0.35 20.65 N ANISOU 232 NE2AHIS 30 3645 1696 2311 296 222 -206 N ATOM 233 NE2BHIS 30 17.569 53.256 -9.819 0.65 21.31 N ANISOU 233 NE2BHIS 30 3706 2073 2119 340 193 -197 N ATOM 234 N THR 31 20.130 46.886 -11.381 1.00 17.35 N ANISOU 234 N THR 31 3538 1519 1372 -1 -97 116 N ATOM 235 CA THR 31 20.243 45.583 -11.943 1.00 15.49 C ANISOU 235 CA THR 31 2979 1621 1141 -37 33 24 C ATOM 236 C THR 31 19.203 44.604 -11.427 1.00 14.64 C ANISOU 236 C THR 31 2643 1541 1240 131 62 42 C ATOM 237 O THR 31 18.343 44.911 -10.586 1.00 16.49 O ANISOU 237 O THR 31 3132 1700 1279 288 353 28 O ATOM 238 CB THR 31 21.632 44.940 -11.734 1.00 16.64 C ANISOU 238 CB THR 31 2817 1809 1538 -118 33 168 C ATOM 239 OG1 THR 31 21.633 44.585 -10.328 1.00 18.94 O ANISOU 239 OG1 THR 31 2971 2479 1569 109 -76 283 O ATOM 240 CG2 THR 31 22.770 45.863 -12.059 1.00 19.41 C ANISOU 240 CG2 THR 31 3172 1957 2062 -449 275 -234 C ATOM 241 N LEU 32 19.218 43.392 -11.989 1.00 14.70 N ANISOU 241 N LEU 32 2690 1482 1276 155 462 140 N ATOM 242 CA LEU 32 18.297 42.352 -11.566 1.00 13.24 C ANISOU 242 CA LEU 32 2264 1389 1253 279 317 129 C ATOM 243 C LEU 32 18.870 41.404 -10.507 1.00 15.67 C ANISOU 243 C LEU 32 2786 1664 1358 283 136 299 C ATOM 244 O LEU 32 18.347 40.333 -10.270 1.00 18.07 O ANISOU 244 O LEU 32 3052 1913 1729 -11 21 683 O ATOM 245 CB LEU 32 17.782 41.558 -12.760 1.00 14.74 C ANISOU 245 CB LEU 32 2771 1559 1132 75 329 181 C ATOM 246 CG LEU 32 17.143 42.345 -13.886 1.00 16.27 C ANISOU 246 CG LEU 32 3139 1544 1347 215 31 145 C ATOM 247 CD1 LEU 32 16.520 41.412 -14.914 1.00 16.87 C ANISOU 247 CD1 LEU 32 2810 2060 1383 -362 160 194 C ATOM 248 CD2 LEU 32 16.151 43.377 -13.423 1.00 20.21 C ANISOU 248 CD2 LEU 32 3502 2665 1322 933 207 136 C ATOM 249 N GLN 33 19.933 41.853 -9.852 1.00 15.92 N ANISOU 249 N GLN 33 3039 1583 1279 228 -25 214 N ATOM 250 CA GLN 33 20.487 41.143 -8.674 1.00 16.04 C ANISOU 250 CA GLN 33 2955 1589 1399 286 39 235 C ATOM 251 C GLN 33 19.641 41.472 -7.431 1.00 16.11 C ANISOU 251 C GLN 33 2960 1650 1358 374 23 299 C ATOM 252 O GLN 33 19.069 42.547 -7.305 1.00 17.51 O ANISOU 252 O GLN 33 3183 1919 1387 719 -78 98 O ATOM 253 CB AGLN 33 21.967 41.394 -8.495 0.56 19.11 C ANISOU 253 CB AGLN 33 2869 2255 1957 279 -46 327 C ATOM 254 CB BGLN 33 21.852 41.778 -8.385 0.44 18.14 C ANISOU 254 CB BGLN 33 2889 2125 1707 208 -74 339 C ATOM 255 CG AGLN 33 22.770 41.007 -9.714 0.56 22.51 C ANISOU 255 CG AGLN 33 3033 2963 2346 436 263 318 C ATOM 256 CG BGLN 33 22.983 41.428 -9.300 0.44 20.59 C ANISOU 256 CG BGLN 33 2963 2509 2159 264 133 450 C ATOM 257 CD AGLN 33 24.162 41.581 -9.781 0.56 23.78 C ANISOU 257 CD AGLN 33 2772 3373 2668 627 98 493 C ATOM 258 CD BGLN 33 23.366 39.978 -9.407 0.44 22.90 C ANISOU 258 CD BGLN 33 3038 2887 2562 943 -8 378 C ATOM 259 OE1AGLN 33 24.365 42.751 -10.143 0.56 29.70 O ANISOU 259 OE1AGLN 33 3391 3063 4551 -145 -757 -27 O ATOM 260 OE1BGLN 33 23.978 39.572 -10.389 0.44 30.63 O ANISOU 260 OE1BGLN 33 3960 3482 3908 430 1148 -365 O ATOM 261 NE2AGLN 33 25.122 40.712 -9.503 0.56 28.14 N ANISOU 261 NE2AGLN 33 3357 4343 2727 1325 -307 177 N ATOM 262 NE2BGLN 33 23.066 39.194 -8.372 0.44 25.17 N ANISOU 262 NE2BGLN 33 2927 2472 3927 779 458 823 N ATOM 263 N LYS 34 19.545 40.494 -6.521 1.00 17.34 N ANISOU 263 N LYS 34 2963 2011 1450 443 88 478 N ATOM 264 CA LYS 34 18.741 40.606 -5.329 1.00 18.75 C ANISOU 264 CA LYS 34 3189 2232 1526 322 246 487 C ATOM 265 C LYS 34 18.989 41.872 -4.538 1.00 17.40 C ANISOU 265 C LYS 34 2856 2295 1295 688 37 504 C ATOM 266 O LYS 34 18.051 42.597 -4.236 1.00 19.92 O ANISOU 266 O LYS 34 3209 2563 1609 902 218 487 O ATOM 267 CB ALYS 34 18.998 39.378 -4.423 0.63 19.52 C ANISOU 267 CB ALYS 34 3255 2413 1567 612 307 607 C ATOM 268 CB BLYS 34 18.688 39.300 -4.562 0.37 19.70 C ANISOU 268 CB BLYS 34 3188 2393 1720 561 345 698 C ATOM 269 CG ALYS 34 18.123 39.410 -3.175 0.63 19.98 C ANISOU 269 CG ALYS 34 2702 2898 1804 250 310 824 C ATOM 270 CG BLYS 34 19.281 39.180 -3.183 0.37 22.82 C ANISOU 270 CG BLYS 34 3284 3169 2003 755 119 996 C ATOM 271 CD ALYS 34 18.357 38.196 -2.288 0.63 25.20 C ANISOU 271 CD ALYS 34 3362 3713 2264 689 497 1500 C ATOM 272 CD BLYS 34 19.131 37.748 -2.666 0.37 27.58 C ANISOU 272 CD BLYS 34 3983 3719 2520 651 370 1738 C ATOM 273 CE ALYS 34 19.669 38.282 -1.528 0.63 29.71 C ANISOU 273 CE ALYS 34 3877 4453 2680 546 -48 2023 C ATOM 274 CE BLYS 34 20.493 37.069 -2.651 0.37 31.92 C ANISOU 274 CE BLYS 34 4684 4040 3103 1406 589 2591 C ATOM 275 NZ ALYS 34 20.264 36.960 -1.149 0.63 36.41 N ANISOU 275 NZ ALYS 34 4534 4922 4035 1273 -459 1964 N ATOM 276 NZ BLYS 34 20.890 36.566 -3.994 0.37 41.50 N ANISOU 276 NZ BLYS 34 6865 4523 3990 2523 1849 2389 N ATOM 277 N ALA 35 20.233 42.197 -4.227 1.00 18.72 N ANISOU 277 N ALA 35 3124 2320 1493 707 -153 144 N ATOM 278 CA ALA 35 20.532 43.345 -3.368 1.00 19.49 C ANISOU 278 CA ALA 35 3615 2432 1177 746 -84 47 C ATOM 279 C ALA 35 20.148 44.659 -4.068 1.00 20.07 C ANISOU 279 C ALA 35 3755 2408 1276 909 59 37 C ATOM 280 O ALA 35 19.810 45.623 -3.379 1.00 22.90 O ANISOU 280 O ALA 35 4266 2678 1542 1127 -96 -226 O ATOM 281 CB ALA 35 21.972 43.336 -2.933 1.00 23.92 C ANISOU 281 CB ALA 35 4137 2661 2067 703 -960 -134 C ATOM 282 N ALA 36 20.245 44.713 -5.416 1.00 18.41 N ANISOU 282 N ALA 36 3208 2380 1235 584 -217 29 N ATOM 283 CA ALA 36 19.881 45.898 -6.172 1.00 18.89 C ANISOU 283 CA ALA 36 3410 2136 1453 367 8 126 C ATOM 284 C ALA 36 18.366 46.077 -6.121 1.00 17.62 C ANISOU 284 C ALA 36 3512 1767 1252 677 105 177 C ATOM 285 O ALA 36 17.801 47.113 -5.866 1.00 21.20 O ANISOU 285 O ALA 36 4008 1883 1965 866 -59 38 O ATOM 286 CB ALA 36 20.417 45.818 -7.582 1.00 19.37 C ANISOU 286 CB ALA 36 3342 2271 1567 272 159 294 C ATOM 287 N ILE 37 17.648 44.938 -6.369 1.00 17.80 N ANISOU 287 N ILE 37 3272 1920 1403 624 64 256 N ATOM 288 CA ILE 37 16.196 45.010 -6.301 1.00 18.49 C ANISOU 288 CA ILE 37 3326 2360 1168 765 15 110 C ATOM 289 C ILE 37 15.693 45.477 -4.928 1.00 18.91 C ANISOU 289 C ILE 37 3351 2401 1256 827 87 163 C ATOM 290 O ILE 37 14.769 46.299 -4.798 1.00 23.86 O ANISOU 290 O ILE 37 4327 3060 1456 1682 -159 -247 O ATOM 291 CB ILE 37 15.585 43.683 -6.758 1.00 18.48 C ANISOU 291 CB ILE 37 3111 2407 1328 673 149 204 C ATOM 292 CG1 ILE 37 15.852 43.386 -8.235 1.00 18.25 C ANISOU 292 CG1 ILE 37 3015 2535 1215 -12 66 123 C ATOM 293 CG2 ILE 37 14.102 43.581 -6.434 1.00 21.20 C ANISOU 293 CG2 ILE 37 3317 2550 1989 636 609 832 C ATOM 294 CD1 ILE 37 15.647 41.945 -8.658 1.00 22.91 C ANISOU 294 CD1 ILE 37 4006 2873 1609 -884 337 -164 C ATOM 295 N GLU 38 16.298 44.918 -3.872 1.00 20.63 N ANISOU 295 N GLU 38 3567 2898 1182 1066 118 63 N ATOM 296 CA GLU 38 15.901 45.242 -2.513 1.00 25.91 C ANISOU 296 CA GLU 38 4799 3576 1227 1703 161 -4 C ATOM 297 C GLU 38 16.059 46.748 -2.259 1.00 27.90 C ANISOU 297 C GLU 38 5301 3556 1482 1901 47 -373 C ATOM 298 O GLU 38 15.231 47.292 -1.535 1.00 31.96 O ANISOU 298 O GLU 38 5550 4499 1795 2393 -65 -709 O ATOM 299 CB GLU 38 16.766 44.481 -1.504 1.00 27.72 C ANISOU 299 CB GLU 38 5066 3941 1263 1826 131 239 C ATOM 300 CG GLU 38 16.561 42.987 -1.369 1.00 31.29 C ANISOU 300 CG GLU 38 5643 4123 1828 1607 357 808 C ATOM 301 CD GLU 38 17.433 42.238 -0.386 1.00 34.70 C ANISOU 301 CD GLU 38 5972 4441 2447 1527 138 1348 C ATOM 302 OE1 GLU 38 18.506 42.737 0.014 1.00 39.09 O ANISOU 302 OE1 GLU 38 5593 4836 4057 1847 -236 1553 O ATOM 303 OE2 GLU 38 17.077 41.096 0.055 1.00 43.54 O ANISOU 303 OE2 GLU 38 7244 4527 4362 1354 -172 1949 O ATOM 304 N GLN 39 17.084 47.372 -2.875 1.00 27.54 N ANISOU 304 N GLN 39 5401 3354 1452 1630 -371 -137 N ATOM 305 CA GLN 39 17.316 48.805 -2.691 1.00 30.19 C ANISOU 305 CA GLN 39 5450 3528 2210 1558 -1166 -447 C ATOM 306 C GLN 39 16.495 49.735 -3.603 1.00 27.80 C ANISOU 306 C GLN 39 5334 2895 2072 1719 -995 -856 C ATOM 307 O GLN 39 16.014 50.800 -3.185 1.00 28.04 O ANISOU 307 O GLN 39 5046 3018 2326 1447 -410 -1010 O ATOM 308 CB GLN 39 18.801 49.146 -2.865 1.00 33.72 C ANISOU 308 CB GLN 39 5416 4159 2919 1214 -1877 -1024 C ATOM 309 CG GLN 39 19.798 48.539 -1.868 1.00 38.88 C ANISOU 309 CG GLN 39 5901 5201 3306 1256 -2243 -586 C ATOM 310 CD GLN 39 19.543 49.050 -0.457 1.00 38.02 C ANISOU 310 CD GLN 39 5431 5272 3386 1434 -2634 -830 C ATOM 311 OE1 GLN 39 19.493 50.257 -0.273 1.00 43.96 O ANISOU 311 OE1 GLN 39 6440 5356 4494 541 -2502 -1375 O ATOM 312 NE2 GLN 39 19.286 48.206 0.538 1.00 40.25 N ANISOU 312 NE2 GLN 39 5445 5845 3624 817 -1355 -1007 N ATOM 313 N PHE 40 16.339 49.357 -4.888 1.00 26.47 N ANISOU 313 N PHE 40 4969 2680 2160 1417 -1237 -887 N ATOM 314 CA PHE 40 15.827 50.278 -5.889 1.00 26.50 C ANISOU 314 CA PHE 40 5100 2536 2186 1287 -1110 -728 C ATOM 315 C PHE 40 14.442 49.989 -6.444 1.00 27.04 C ANISOU 315 C PHE 40 5224 2435 2362 1298 -1306 -699 C ATOM 316 O PHE 40 13.886 50.878 -7.107 1.00 31.52 O ANISOU 316 O PHE 40 5482 2118 4080 927 -2159 -500 O ATOM 317 CB PHE 40 16.833 50.264 -7.056 1.00 27.87 C ANISOU 317 CB PHE 40 5552 2363 2412 1017 -762 -996 C ATOM 318 CG PHE 40 18.223 50.749 -6.708 1.00 30.27 C ANISOU 318 CG PHE 40 5607 3130 2480 771 -540 -1129 C ATOM 319 CD1 PHE 40 18.431 51.975 -6.080 1.00 32.59 C ANISOU 319 CD1 PHE 40 5375 3215 3488 457 -473 -1379 C ATOM 320 CD2 PHE 40 19.287 49.921 -7.068 1.00 28.99 C ANISOU 320 CD2 PHE 40 5417 2793 2533 629 -517 -661 C ATOM 321 CE1 PHE 40 19.745 52.329 -5.825 1.00 36.15 C ANISOU 321 CE1 PHE 40 5358 4052 3988 333 -531 -1309 C ATOM 322 CE2 PHE 40 20.595 50.224 -6.759 1.00 33.67 C ANISOU 322 CE2 PHE 40 5387 3492 3599 230 -266 -666 C ATOM 323 CZ PHE 40 20.765 51.436 -6.118 1.00 35.47 C ANISOU 323 CZ PHE 40 5174 3980 3990 125 -327 -1265 C ATOM 324 N LEU 41 13.953 48.755 -6.237 1.00 24.88 N ANISOU 324 N LEU 41 4929 2532 1758 1295 -769 -505 N ATOM 325 CA LEU 41 12.616 48.446 -6.754 1.00 23.83 C ANISOU 325 CA LEU 41 4463 2450 1917 1560 -321 -443 C ATOM 326 C LEU 41 11.612 48.873 -5.709 1.00 26.84 C ANISOU 326 C LEU 41 5189 2802 1956 1795 -42 -389 C ATOM 327 O LEU 41 11.694 48.474 -4.540 1.00 26.32 O ANISOU 327 O LEU 41 4600 3208 1947 1600 -208 -536 O ATOM 328 CB LEU 41 12.463 46.955 -7.062 1.00 22.14 C ANISOU 328 CB LEU 41 4313 2512 1381 1310 -258 -242 C ATOM 329 CG LEU 41 11.087 46.539 -7.551 1.00 21.93 C ANISOU 329 CG LEU 41 4076 2768 1283 1255 23 -126 C ATOM 330 CD1 LEU 41 10.732 47.206 -8.912 1.00 23.72 C ANISOU 330 CD1 LEU 41 3694 3475 1621 808 -75 443 C ATOM 331 CD2 LEU 41 10.891 45.053 -7.729 1.00 23.14 C ANISOU 331 CD2 LEU 41 4118 2797 1661 873 752 -151 C ATOM 332 N ASP 42 10.832 49.896 -6.092 1.00 27.27 N ANISOU 332 N ASP 42 4739 3327 2039 1974 179 -483 N ATOM 333 CA ASP 42 9.794 50.401 -5.215 1.00 29.11 C ANISOU 333 CA ASP 42 3913 4320 2555 1674 198 -447 C ATOM 334 C ASP 42 8.960 49.177 -4.783 1.00 28.76 C ANISOU 334 C ASP 42 3398 4247 3014 1666 -545 -279 C ATOM 335 O ASP 42 8.538 48.479 -5.710 1.00 39.70 O ANISOU 335 O ASP 42 5279 4886 4546 1424 -116 -1959 O ATOM 336 CB AASP 42 8.949 51.480 -5.894 0.63 30.75 C ANISOU 336 CB AASP 42 3244 4389 3762 1502 338 18 C ATOM 337 CB BASP 42 8.842 51.167 -6.207 0.37 32.01 C ANISOU 337 CB BASP 42 3648 4634 3579 1478 108 245 C ATOM 338 CG AASP 42 9.709 52.743 -6.252 0.63 35.46 C ANISOU 338 CG AASP 42 4024 4505 4609 1543 1195 317 C ATOM 339 CG BASP 42 8.017 52.039 -5.266 0.37 32.08 C ANISOU 339 CG BASP 42 3498 4536 3855 1553 149 283 C ATOM 340 OD1AASP 42 10.830 52.945 -5.723 0.63 38.65 O ANISOU 340 OD1AASP 42 5013 4206 5102 339 566 122 O ATOM 341 OD1BASP 42 8.555 52.166 -4.145 0.37 26.79 O ANISOU 341 OD1BASP 42 3386 2404 4136 408 98 83 O ATOM 342 OD2AASP 42 9.252 53.519 -7.113 0.63 42.52 O ANISOU 342 OD2AASP 42 4062 5524 6169 2236 1853 1646 O ATOM 343 OD2BASP 42 6.928 52.454 -5.636 0.37 40.79 O ANISOU 343 OD2BASP 42 5163 5742 4211 3417 -121 1482 O ATOM 344 N GLY 43 8.828 48.790 -3.538 1.00 35.12 N ANISOU 344 N GLY 43 3456 5925 3635 1832 669 563 N ATOM 345 CA GLY 43 8.110 47.547 -3.143 1.00 31.54 C ANISOU 345 CA GLY 43 3107 5487 3093 1984 701 -131 C ATOM 346 C GLY 43 9.059 46.429 -2.712 1.00 32.30 C ANISOU 346 C GLY 43 3615 5836 2519 2056 261 77 C ATOM 347 O GLY 43 8.759 45.427 -2.032 1.00 38.51 O ANISOU 347 O GLY 43 5515 5720 3034 2340 1134 149 O ATOM 348 N GLY 44 10.347 46.420 -3.111 1.00 31.33 N ANISOU 348 N GLY 44 3714 5954 1942 2761 272 -467 N ATOM 349 CA GLY 44 11.280 45.416 -2.606 1.00 32.21 C ANISOU 349 CA GLY 44 4191 5873 1871 2712 396 43 C ATOM 350 C GLY 44 11.372 44.117 -3.374 1.00 30.46 C ANISOU 350 C GLY 44 4445 5327 1516 2437 679 581 C ATOM 351 O GLY 44 10.803 43.969 -4.438 1.00 27.30 O ANISOU 351 O GLY 44 3825 4656 1637 2151 737 746 O ATOM 352 N PHE 45 12.106 43.149 -2.834 1.00 31.19 N ANISOU 352 N PHE 45 4566 5732 1261 2674 663 584 N ATOM 353 CA PHE 45 12.334 41.872 -3.507 1.00 28.54 C ANISOU 353 CA PHE 45 3604 5040 1934 2016 1463 1046 C ATOM 354 C PHE 45 11.222 40.860 -3.205 1.00 30.24 C ANISOU 354 C PHE 45 2954 5783 2470 2236 1241 2049 C ATOM 355 O PHE 45 11.257 40.083 -2.223 1.00 35.42 O ANISOU 355 O PHE 45 3037 7348 2741 1625 1001 2776 O ATOM 356 CB PHE 45 13.675 41.282 -3.137 1.00 24.63 C ANISOU 356 CB PHE 45 3479 3880 1769 1098 496 437 C ATOM 357 CG PHE 45 14.106 39.986 -3.775 1.00 23.63 C ANISOU 357 CG PHE 45 3254 3826 1676 1431 497 839 C ATOM 358 CD1 PHE 45 14.262 39.933 -5.137 1.00 23.32 C ANISOU 358 CD1 PHE 45 3621 3362 1658 668 431 574 C ATOM 359 CD2 PHE 45 14.331 38.824 -3.065 1.00 24.41 C ANISOU 359 CD2 PHE 45 3129 3778 2138 866 411 1081 C ATOM 360 CE1 PHE 45 14.665 38.822 -5.830 1.00 22.86 C ANISOU 360 CE1 PHE 45 3086 3414 1970 609 819 631 C ATOM 361 CE2 PHE 45 14.702 37.688 -3.756 1.00 26.18 C ANISOU 361 CE2 PHE 45 3522 3565 2616 924 667 1228 C ATOM 362 CZ PHE 45 14.877 37.649 -5.123 1.00 24.42 C ANISOU 362 CZ PHE 45 3348 3109 2591 174 524 634 C ATOM 363 N ASN 46 10.128 40.977 -3.915 1.00 32.78 N ANISOU 363 N ASN 46 3271 6919 1955 1986 1050 1734 N ATOM 364 CA ASN 46 8.889 40.257 -3.786 1.00 36.75 C ANISOU 364 CA ASN 46 3367 7895 2354 1548 1126 2194 C ATOM 365 C ASN 46 8.242 40.111 -5.169 1.00 33.28 C ANISOU 365 C ASN 46 3201 6787 2345 1406 1266 1896 C ATOM 366 O ASN 46 8.417 41.005 -6.008 1.00 31.52 O ANISOU 366 O ASN 46 2601 6789 2291 932 874 1916 O ATOM 367 CB ASN 46 7.858 40.986 -2.855 1.00 45.23 C ANISOU 367 CB ASN 46 4810 9095 2857 386 2869 1244 C ATOM 368 CG ASN 46 8.444 41.285 -1.515 1.00 53.11 C ANISOU 368 CG ASN 46 6158 9518 4005 1558 1563 149 C ATOM 369 OD1 ASN 46 8.525 42.384 -0.977 1.00 66.40 O ANISOU 369 OD1 ASN 46 7883 11499 5224 2957 2984 -2465 O ATOM 370 ND2 ASN 46 8.973 40.217 -0.900 1.00 68.36 N ANISOU 370 ND2 ASN 46 8107 11434 5790 2211 44 1515 N ATOM 371 N ILE 47 7.608 39.003 -5.445 1.00 31.59 N ANISOU 371 N ILE 47 2291 6209 3206 1913 1244 2311 N ATOM 372 CA ILE 47 6.964 38.832 -6.727 1.00 28.94 C ANISOU 372 CA ILE 47 2125 5437 3162 1558 1531 1948 C ATOM 373 C ILE 47 5.962 39.925 -7.069 1.00 28.73 C ANISOU 373 C ILE 47 2874 5627 2144 2058 1193 1446 C ATOM 374 O ILE 47 5.993 40.337 -8.223 1.00 28.12 O ANISOU 374 O ILE 47 2791 5270 2361 1525 1431 1589 O ATOM 375 CB ILE 47 6.301 37.443 -6.830 1.00 33.78 C ANISOU 375 CB ILE 47 2732 5648 4138 1024 1307 2842 C ATOM 376 CG1 ILE 47 7.234 36.256 -6.825 1.00 35.75 C ANISOU 376 CG1 ILE 47 3364 5225 4660 902 1707 2530 C ATOM 377 CG2 ILE 47 5.340 37.439 -8.013 1.00 38.39 C ANISOU 377 CG2 ILE 47 3154 6356 4714 -8 794 2786 C ATOM 378 CD1 ILE 47 7.942 35.979 -8.116 1.00 37.03 C ANISOU 378 CD1 ILE 47 3649 5701 4371 550 935 950 C ATOM 379 N GLU 48 5.119 40.333 -6.109 1.00 29.64 N ANISOU 379 N GLU 48 2485 5973 2526 2017 1567 2005 N ATOM 380 CA GLU 48 4.132 41.350 -6.502 1.00 31.74 C ANISOU 380 CA GLU 48 3055 5922 2785 2397 1707 1836 C ATOM 381 C GLU 48 4.863 42.622 -6.890 1.00 27.61 C ANISOU 381 C GLU 48 2826 5595 1810 2299 1375 1158 C ATOM 382 O GLU 48 4.280 43.389 -7.705 1.00 27.92 O ANISOU 382 O GLU 48 2692 5230 2425 1950 1221 1199 O ATOM 383 CB AGLU 48 3.134 41.513 -5.342 0.60 35.24 C ANISOU 383 CB AGLU 48 3850 5887 3324 2582 2417 1887 C ATOM 384 CB BGLU 48 3.054 41.666 -5.484 0.40 35.56 C ANISOU 384 CB BGLU 48 3817 5916 3443 2581 2461 1912 C ATOM 385 CG AGLU 48 2.733 40.136 -4.819 0.60 40.28 C ANISOU 385 CG AGLU 48 4634 6113 4179 2219 2742 2094 C ATOM 386 CG BGLU 48 3.011 41.087 -4.110 0.40 35.94 C ANISOU 386 CG BGLU 48 4440 5727 3152 2140 2301 1542 C ATOM 387 CD AGLU 48 3.420 39.927 -3.465 0.60 39.47 C ANISOU 387 CD AGLU 48 4828 5876 3923 2465 2998 2373 C ATOM 388 CD BGLU 48 3.668 41.833 -2.980 0.40 37.18 C ANISOU 388 CD BGLU 48 4686 5410 3682 1485 2113 1663 C ATOM 389 OE1AGLU 48 4.664 39.738 -3.496 0.60 37.58 O ANISOU 389 OE1AGLU 48 4398 6201 3327 1416 2837 1504 O ATOM 390 OE1BGLU 48 4.223 42.919 -3.223 0.40 37.99 O ANISOU 390 OE1BGLU 48 5524 4869 3686 2025 1198 2721 O ATOM 391 OE2BGLU 48 3.739 41.355 -1.834 0.40 29.72 O ANISOU 391 OE2BGLU 48 3278 4237 3499 282 2215 1265 O ATOM 392 OE2AGLU 48 2.819 39.905 -2.380 0.60 33.01 O ANISOU 392 OE2AGLU 48 4577 3632 4021 1247 3110 557 O ATOM 393 N ALA 49 5.982 42.976 -6.276 1.00 30.69 N ANISOU 393 N ALA 49 3120 6334 1918 2397 1222 503 N ATOM 394 CA ALA 49 6.648 44.227 -6.659 1.00 27.88 C ANISOU 394 CA ALA 49 2839 5948 1543 2370 550 -35 C ATOM 395 C ALA 49 7.233 44.112 -8.072 1.00 24.13 C ANISOU 395 C ALA 49 2662 4858 1423 1947 383 8 C ATOM 396 O ALA 49 7.116 45.083 -8.811 1.00 25.59 O ANISOU 396 O ALA 49 3515 4486 1482 2141 305 -332 O ATOM 397 CB ALA 49 7.763 44.563 -5.696 1.00 31.79 C ANISOU 397 CB ALA 49 2982 7503 1294 2364 326 390 C ATOM 398 N ILE 50 7.664 42.919 -8.420 1.00 22.34 N ANISOU 398 N ILE 50 2310 4350 1620 1362 897 349 N ATOM 399 CA ILE 50 8.175 42.658 -9.797 1.00 20.61 C ANISOU 399 CA ILE 50 2440 3558 1641 1360 1102 630 C ATOM 400 C ILE 50 7.084 42.732 -10.845 1.00 20.16 C ANISOU 400 C ILE 50 2770 3065 1635 1187 781 455 C ATOM 401 O ILE 50 7.158 43.449 -11.829 1.00 19.74 O ANISOU 401 O ILE 50 2928 2981 1405 975 895 176 O ATOM 402 CB ILE 50 8.959 41.365 -9.787 1.00 20.81 C ANISOU 402 CB ILE 50 2323 3463 1925 1229 1106 850 C ATOM 403 CG1 ILE 50 10.217 41.381 -8.936 1.00 20.94 C ANISOU 403 CG1 ILE 50 2496 3393 1870 1328 1051 816 C ATOM 404 CG2 ILE 50 9.425 41.027 -11.226 1.00 20.83 C ANISOU 404 CG2 ILE 50 2472 3059 2188 501 1078 -69 C ATOM 405 CD1 ILE 50 10.876 40.084 -8.649 1.00 28.69 C ANISOU 405 CD1 ILE 50 2949 4704 2980 2388 1530 1779 C ATOM 406 N VAL 51 5.967 42.021 -10.518 1.00 21.04 N ANISOU 406 N VAL 51 2348 3611 1838 1554 1139 793 N ATOM 407 CA VAL 51 4.785 42.161 -11.350 1.00 21.92 C ANISOU 407 CA VAL 51 2228 3792 2101 1464 1184 969 C ATOM 408 C VAL 51 4.358 43.582 -11.621 1.00 19.30 C ANISOU 408 C VAL 51 1873 3575 1706 1168 720 618 C ATOM 409 O VAL 51 3.993 43.984 -12.703 1.00 20.62 O ANISOU 409 O VAL 51 2581 3373 1685 1239 800 568 O ATOM 410 CB VAL 51 3.638 41.258 -10.847 1.00 22.90 C ANISOU 410 CB VAL 51 2486 3798 2201 1251 1167 847 C ATOM 411 CG1 VAL 51 2.366 41.526 -11.631 1.00 26.59 C ANISOU 411 CG1 VAL 51 2423 4237 3192 1202 897 941 C ATOM 412 CG2 VAL 51 4.117 39.824 -10.843 1.00 28.29 C ANISOU 412 CG2 VAL 51 3038 4014 3433 1456 1658 1796 C ATOM 413 N TYR 52 4.194 44.350 -10.487 1.00 22.35 N ANISOU 413 N TYR 52 2435 4207 1641 1865 773 676 N ATOM 414 CA TYR 52 3.694 45.703 -10.563 1.00 22.94 C ANISOU 414 CA TYR 52 2659 4125 1718 1698 945 219 C ATOM 415 C TYR 52 4.513 46.521 -11.531 1.00 18.89 C ANISOU 415 C TYR 52 2396 3347 1257 1543 624 -332 C ATOM 416 O TYR 52 3.958 47.287 -12.368 1.00 20.88 O ANISOU 416 O TYR 52 2772 3242 1722 1407 499 -85 O ATOM 417 CB TYR 52 3.641 46.227 -9.110 1.00 26.07 C ANISOU 417 CB TYR 52 2781 5081 1801 1534 1091 -1 C ATOM 418 CG TYR 52 2.900 47.537 -9.085 1.00 28.55 C ANISOU 418 CG TYR 52 3262 5293 2024 1843 1059 -654 C ATOM 419 CD1 TYR 52 3.555 48.728 -9.281 1.00 28.15 C ANISOU 419 CD1 TYR 52 3137 5002 2293 1855 137 -1097 C ATOM 420 CD2 TYR 52 1.523 47.569 -8.843 1.00 30.75 C ANISOU 420 CD2 TYR 52 3265 5619 2509 1957 1067 -789 C ATOM 421 CE1 TYR 52 2.860 49.918 -9.247 1.00 30.93 C ANISOU 421 CE1 TYR 52 3403 5183 2877 2070 -142 -1632 C ATOM 422 CE2 TYR 52 0.808 48.753 -8.848 1.00 31.49 C ANISOU 422 CE2 TYR 52 3365 5887 2419 2131 435 -1642 C ATOM 423 CZ TYR 52 1.489 49.932 -9.060 1.00 31.37 C ANISOU 423 CZ TYR 52 3305 5340 2981 2243 -673 -2080 C ATOM 424 OH TYR 52 0.834 51.120 -9.042 1.00 40.84 O ANISOU 424 OH TYR 52 4043 5641 5449 2703 -585 -3192 O ATOM 425 N GLN 53 5.837 46.390 -11.432 1.00 21.18 N ANISOU 425 N GLN 53 2454 3567 1828 1416 642 -556 N ATOM 426 CA GLN 53 6.711 47.180 -12.332 1.00 20.74 C ANISOU 426 CA GLN 53 2613 3461 1609 1114 476 -697 C ATOM 427 C GLN 53 6.718 46.680 -13.757 1.00 17.57 C ANISOU 427 C GLN 53 2480 2486 1544 1131 307 -407 C ATOM 428 O GLN 53 6.663 47.504 -14.669 1.00 18.01 O ANISOU 428 O GLN 53 2491 2378 1805 828 296 -338 O ATOM 429 CB GLN 53 8.163 47.265 -11.810 1.00 22.73 C ANISOU 429 CB GLN 53 2727 4058 1636 774 364 -738 C ATOM 430 CG GLN 53 9.007 48.242 -12.658 1.00 22.72 C ANISOU 430 CG GLN 53 2709 3852 1860 954 200 -373 C ATOM 431 CD GLN 53 10.100 48.910 -11.861 1.00 20.54 C ANISOU 431 CD GLN 53 2737 3443 1431 1013 248 -149 C ATOM 432 OE1 GLN 53 11.282 48.887 -12.232 1.00 24.86 O ANISOU 432 OE1 GLN 53 2969 3649 2593 294 747 -641 O ATOM 433 NE2 GLN 53 9.724 49.650 -10.856 1.00 24.06 N ANISOU 433 NE2 GLN 53 3504 3076 2337 940 526 -540 N ATOM 434 N ILE 54 6.496 45.390 -13.970 1.00 16.88 N ANISOU 434 N ILE 54 2243 2569 1445 727 706 -148 N ATOM 435 CA ILE 54 6.258 44.901 -15.319 1.00 16.62 C ANISOU 435 CA ILE 54 2321 2306 1531 675 675 -221 C ATOM 436 C ILE 54 4.991 45.455 -15.951 1.00 16.29 C ANISOU 436 C ILE 54 2245 2308 1483 473 580 -121 C ATOM 437 O ILE 54 4.954 45.927 -17.086 1.00 17.16 O ANISOU 437 O ILE 54 2275 2495 1588 491 504 -164 O ATOM 438 CB ILE 54 6.321 43.379 -15.356 1.00 17.30 C ANISOU 438 CB ILE 54 2388 2326 1698 570 1011 10 C ATOM 439 CG1 ILE 54 7.662 42.795 -14.984 1.00 17.22 C ANISOU 439 CG1 ILE 54 2748 2057 1575 640 759 -90 C ATOM 440 CG2 ILE 54 5.924 42.832 -16.715 1.00 18.80 C ANISOU 440 CG2 ILE 54 2566 2193 2207 334 547 -260 C ATOM 441 CD1 ILE 54 7.724 41.368 -14.614 1.00 22.91 C ANISOU 441 CD1 ILE 54 3615 2225 2649 1125 1496 230 C ATOM 442 N GLU 55 3.880 45.394 -15.181 1.00 18.85 N ANISOU 442 N GLU 55 2520 2720 1745 1248 795 15 N ATOM 443 CA GLU 55 2.590 45.885 -15.659 1.00 18.79 C ANISOU 443 CA GLU 55 2340 2649 1973 1029 748 -160 C ATOM 444 C GLU 55 2.551 47.338 -16.046 1.00 17.33 C ANISOU 444 C GLU 55 2155 2672 1595 955 286 -105 C ATOM 445 O GLU 55 2.005 47.749 -17.053 1.00 21.02 O ANISOU 445 O GLU 55 2578 3123 2087 921 -72 0 O ATOM 446 CB GLU 55 1.456 45.479 -14.741 1.00 21.65 C ANISOU 446 CB GLU 55 2670 3087 2265 1176 1083 216 C ATOM 447 CG GLU 55 1.161 44.001 -14.650 1.00 25.50 C ANISOU 447 CG GLU 55 3056 3129 3263 1305 1528 772 C ATOM 448 CD GLU 55 0.149 43.591 -13.601 1.00 27.57 C ANISOU 448 CD GLU 55 2460 3842 3915 981 1363 876 C ATOM 449 OE1 GLU 55 -0.158 44.425 -12.737 1.00 35.04 O ANISOU 449 OE1 GLU 55 3855 5258 3872 858 2387 450 O ATOM 450 OE2 GLU 55 -0.287 42.410 -13.643 1.00 40.59 O ANISOU 450 OE2 GLU 55 3402 4723 6917 -360 2041 572 O ATOM 451 N ASN 56 3.104 48.133 -15.073 1.00 18.66 N ANISOU 451 N ASN 56 2145 2841 1930 985 394 -409 N ATOM 452 CA ASN 56 2.927 49.566 -15.101 1.00 20.29 C ANISOU 452 CA ASN 56 2484 2857 2179 1051 165 -606 C ATOM 453 C ASN 56 4.111 50.360 -15.632 1.00 19.25 C ANISOU 453 C ASN 56 2545 2564 2024 1103 29 -431 C ATOM 454 O ASN 56 3.969 51.509 -16.034 1.00 22.94 O ANISOU 454 O ASN 56 3385 2682 2432 1251 116 -212 O ATOM 455 CB ASN 56 2.634 50.085 -13.673 1.00 21.56 C ANISOU 455 CB ASN 56 2723 3050 2218 1230 255 -625 C ATOM 456 CG ASN 56 1.273 49.592 -13.210 1.00 23.64 C ANISOU 456 CG ASN 56 2520 3754 2485 1491 290 -432 C ATOM 457 OD1 ASN 56 0.253 50.003 -13.747 1.00 32.37 O ANISOU 457 OD1 ASN 56 2667 5466 3864 1822 -79 18 O ATOM 458 ND2 ASN 56 1.239 48.625 -12.307 1.00 24.12 N ANISOU 458 ND2 ASN 56 2937 3903 2099 813 325 -593 N ATOM 459 N GLY 57 5.237 49.698 -15.820 1.00 18.66 N ANISOU 459 N GLY 57 2417 2405 2095 808 110 -443 N ATOM 460 CA GLY 57 6.460 50.367 -16.223 1.00 18.85 C ANISOU 460 CA GLY 57 2539 2584 1862 626 44 -420 C ATOM 461 C GLY 57 6.973 51.303 -15.146 1.00 18.69 C ANISOU 461 C GLY 57 3019 2097 1808 563 340 -402 C ATOM 462 O GLY 57 6.395 51.479 -14.054 1.00 22.69 O ANISOU 462 O GLY 57 3185 3001 2222 619 733 -797 O ATOM 463 N LYS 58 8.128 51.915 -15.419 1.00 18.10 N ANISOU 463 N LYS 58 2804 2168 1733 608 80 -253 N ATOM 464 CA LYS 58 8.685 52.925 -14.535 1.00 21.31 C ANISOU 464 CA LYS 58 3117 2596 2185 536 -288 -486 C ATOM 465 C LYS 58 9.747 53.694 -15.308 1.00 19.74 C ANISOU 465 C LYS 58 3078 2041 2196 613 -447 -507 C ATOM 466 O LYS 58 10.732 53.112 -15.756 1.00 19.94 O ANISOU 466 O LYS 58 3658 1957 1774 789 33 -256 O ATOM 467 CB ALYS 58 9.210 52.395 -13.201 0.43 22.82 C ANISOU 467 CB ALYS 58 3200 2894 2363 20 -544 -269 C ATOM 468 CB BLYS 58 9.395 52.287 -13.311 0.57 21.94 C ANISOU 468 CB BLYS 58 2988 2830 2313 176 -373 -259 C ATOM 469 CG ALYS 58 9.124 53.453 -12.093 0.43 25.31 C ANISOU 469 CG ALYS 58 3417 3408 2556 -355 -906 -708 C ATOM 470 CG BLYS 58 10.094 53.362 -12.486 0.57 25.00 C ANISOU 470 CG BLYS 58 3228 3367 2668 -73 -564 -482 C ATOM 471 CD ALYS 58 8.979 52.882 -10.715 0.43 29.59 C ANISOU 471 CD ALYS 58 4457 3888 2619 302 -226 -663 C ATOM 472 CD BLYS 58 10.181 53.129 -11.012 0.57 27.15 C ANISOU 472 CD BLYS 58 3932 3478 2650 -417 -459 -628 C ATOM 473 CE ALYS 58 7.590 52.507 -10.269 0.43 31.62 C ANISOU 473 CE ALYS 58 4785 3781 3151 684 730 -919 C ATOM 474 CE BLYS 58 10.657 54.333 -10.215 0.57 31.04 C ANISOU 474 CE BLYS 58 5050 3455 2997 -260 -656 -903 C ATOM 475 NZ ALYS 58 7.308 52.918 -8.847 0.43 33.27 N ANISOU 475 NZ ALYS 58 5206 3710 3412 1058 472 -1554 N ATOM 476 NZ BLYS 58 11.682 54.047 -9.169 0.57 30.25 N ANISOU 476 NZ BLYS 58 5379 2925 2904 -934 -832 -559 N ATOM 477 N GLY 59 9.570 55.002 -15.474 1.00 23.45 N ANISOU 477 N GLY 59 3778 2166 2746 1002 -39 -387 N ATOM 478 CA GLY 59 10.600 55.780 -16.122 1.00 24.09 C ANISOU 478 CA GLY 59 4397 1695 2836 723 12 -552 C ATOM 479 C GLY 59 10.833 55.337 -17.564 1.00 20.75 C ANISOU 479 C GLY 59 3472 1577 2641 606 -278 -381 C ATOM 480 O GLY 59 9.916 55.295 -18.383 1.00 24.06 O ANISOU 480 O GLY 59 3375 2700 2841 796 -347 65 O ATOM 481 N ALA 60 12.074 54.951 -17.839 1.00 19.12 N ANISOU 481 N ALA 60 3223 1382 2479 235 -275 -100 N ATOM 482 CA ALA 60 12.487 54.467 -19.134 1.00 17.12 C ANISOU 482 CA ALA 60 2844 1431 2068 285 -324 388 C ATOM 483 C ALA 60 12.143 53.007 -19.400 1.00 15.30 C ANISOU 483 C ALA 60 2533 1406 1730 368 -105 229 C ATOM 484 O ALA 60 12.356 52.492 -20.484 1.00 17.07 O ANISOU 484 O ALA 60 2997 1629 1699 405 154 306 O ATOM 485 CB ALA 60 13.955 54.664 -19.402 1.00 20.12 C ANISOU 485 CB ALA 60 2925 2023 2508 -159 -322 547 C ATOM 486 N MET 61 11.616 52.310 -18.367 1.00 15.48 N ANISOU 486 N MET 61 2870 1365 1501 356 14 -3 N ATOM 487 CA MET 61 11.150 50.952 -18.582 1.00 13.70 C ANISOU 487 CA MET 61 2375 1394 1309 355 81 31 C ATOM 488 C MET 61 9.702 50.982 -19.072 1.00 14.38 C ANISOU 488 C MET 61 2425 1489 1414 487 88 -26 C ATOM 489 O MET 61 8.816 51.495 -18.350 1.00 15.90 O ANISOU 489 O MET 61 2482 1757 1652 724 -69 -195 O ATOM 490 CB MET 61 11.228 50.126 -17.291 1.00 13.98 C ANISOU 490 CB MET 61 2277 1500 1403 350 209 109 C ATOM 491 CG MET 61 10.692 48.716 -17.503 1.00 13.60 C ANISOU 491 CG MET 61 2435 1425 1178 443 85 102 C ATOM 492 SD MET 61 11.192 47.599 -16.165 1.00 13.21 S ANISOU 492 SD MET 61 2323 1391 1183 416 420 46 S ATOM 493 CE MET 61 9.859 46.393 -16.206 1.00 15.78 C ANISOU 493 CE MET 61 2107 1723 2018 344 972 167 C ATOM 494 N PRO 62 9.423 50.420 -20.229 1.00 14.34 N ANISOU 494 N PRO 62 2303 1615 1396 306 85 -38 N ATOM 495 CA PRO 62 8.020 50.421 -20.732 1.00 16.18 C ANISOU 495 CA PRO 62 2401 1886 1710 280 -17 32 C ATOM 496 C PRO 62 7.130 49.537 -19.871 1.00 15.34 C ANISOU 496 C PRO 62 2166 1890 1629 389 -123 -23 C ATOM 497 O PRO 62 7.525 48.629 -19.124 1.00 16.51 O ANISOU 497 O PRO 62 2330 1989 1800 503 80 165 O ATOM 498 CB PRO 62 8.133 49.810 -22.093 1.00 19.56 C ANISOU 498 CB PRO 62 2924 2783 1541 -280 -192 -8 C ATOM 499 CG PRO 62 9.533 49.645 -22.408 1.00 19.95 C ANISOU 499 CG PRO 62 3319 2682 1390 478 64 -181 C ATOM 500 CD PRO 62 10.359 49.809 -21.181 1.00 14.90 C ANISOU 500 CD PRO 62 2482 1657 1382 128 309 -7 C ATOM 501 N ALA 63 5.840 49.835 -19.942 1.00 16.41 N ANISOU 501 N ALA 63 2152 2050 1877 556 -2 103 N ATOM 502 CA ALA 63 4.781 49.042 -19.360 1.00 17.07 C ANISOU 502 CA ALA 63 2311 1935 2079 539 355 -158 C ATOM 503 C ALA 63 4.395 47.881 -20.284 1.00 16.26 C ANISOU 503 C ALA 63 2135 2185 1707 300 450 -59 C ATOM 504 O ALA 63 4.388 48.025 -21.517 1.00 21.34 O ANISOU 504 O ALA 63 3380 2699 1827 375 344 35 O ATOM 505 CB ALA 63 3.558 49.936 -19.111 1.00 18.92 C ANISOU 505 CB ALA 63 2421 2453 2138 793 363 -105 C ATOM 506 N TRP 64 4.051 46.771 -19.645 1.00 16.10 N ANISOU 506 N TRP 64 1896 2060 2010 361 524 -148 N ATOM 507 CA TRP 64 3.740 45.574 -20.460 1.00 17.37 C ANISOU 507 CA TRP 64 2304 2177 1955 281 582 -236 C ATOM 508 C TRP 64 2.287 45.128 -20.359 1.00 18.49 C ANISOU 508 C TRP 64 2160 2603 2089 235 341 -558 C ATOM 509 O TRP 64 1.853 44.151 -20.978 1.00 19.86 O ANISOU 509 O TRP 64 2577 2484 2298 31 447 -458 O ATOM 510 CB TRP 64 4.714 44.431 -20.079 1.00 17.69 C ANISOU 510 CB TRP 64 2144 2118 2295 322 646 -287 C ATOM 511 CG TRP 64 6.138 44.825 -20.408 1.00 16.80 C ANISOU 511 CG TRP 64 2308 1874 2044 203 731 -91 C ATOM 512 CD1 TRP 64 7.017 45.506 -19.618 1.00 16.69 C ANISOU 512 CD1 TRP 64 2181 1799 2204 320 706 -212 C ATOM 513 CD2 TRP 64 6.726 44.687 -21.689 1.00 17.29 C ANISOU 513 CD2 TRP 64 2594 1818 1995 143 707 -111 C ATOM 514 NE1 TRP 64 8.164 45.759 -20.333 1.00 17.77 N ANISOU 514 NE1 TRP 64 2306 2225 2053 93 546 187 N ATOM 515 CE2 TRP 64 8.011 45.244 -21.598 1.00 17.48 C ANISOU 515 CE2 TRP 64 2447 1897 2135 291 828 135 C ATOM 516 CE3 TRP 64 6.340 44.095 -22.919 1.00 19.53 C ANISOU 516 CE3 TRP 64 2950 2159 2129 720 475 -412 C ATOM 517 CZ2 TRP 64 8.948 45.315 -22.627 1.00 18.91 C ANISOU 517 CZ2 TRP 64 2674 1988 2347 242 988 114 C ATOM 518 CZ3 TRP 64 7.260 44.175 -23.909 1.00 22.22 C ANISOU 518 CZ3 TRP 64 3670 2465 2100 277 692 -503 C ATOM 519 CH2 TRP 64 8.534 44.742 -23.790 1.00 22.13 C ANISOU 519 CH2 TRP 64 3577 2425 2197 342 1041 54 C ATOM 520 N ASP 65 1.437 45.777 -19.550 1.00 21.18 N ANISOU 520 N ASP 65 2197 3142 2511 254 433 -926 N ATOM 521 CA ASP 65 0.034 45.381 -19.394 1.00 23.88 C ANISOU 521 CA ASP 65 2220 3962 2668 40 524 -922 C ATOM 522 C ASP 65 -0.632 45.380 -20.765 1.00 25.01 C ANISOU 522 C ASP 65 2234 4128 2905 204 271 -501 C ATOM 523 O ASP 65 -0.473 46.333 -21.549 1.00 29.27 O ANISOU 523 O ASP 65 3198 4406 3241 323 508 -193 O ATOM 524 CB ASP 65 -0.627 46.344 -18.407 1.00 31.30 C ANISOU 524 CB ASP 65 2875 5193 3530 -3 1415 -1498 C ATOM 525 CG ASP 65 -2.093 46.070 -18.132 1.00 38.84 C ANISOU 525 CG ASP 65 3109 6280 5002 -236 2021 -1865 C ATOM 526 OD1 ASP 65 -2.503 44.894 -18.095 1.00 46.71 O ANISOU 526 OD1 ASP 65 4080 6966 6263 -1250 2338 -883 O ATOM 527 OD2 ASP 65 -2.765 47.090 -17.865 1.00 56.24 O ANISOU 527 OD2 ASP 65 3772 7682 9388 1052 2756 -1745 O ATOM 528 N GLY 66 -1.340 44.288 -21.075 1.00 25.46 N ANISOU 528 N GLY 66 2197 4319 2920 245 -184 -559 N ATOM 529 CA GLY 66 -1.989 44.167 -22.357 1.00 25.87 C ANISOU 529 CA GLY 66 2815 3860 2911 618 -362 -274 C ATOM 530 C GLY 66 -1.168 43.699 -23.526 1.00 23.36 C ANISOU 530 C GLY 66 2845 3042 2770 623 -457 -181 C ATOM 531 O GLY 66 -1.791 43.255 -24.491 1.00 30.05 O ANISOU 531 O GLY 66 2952 5422 2763 -766 15 -468 O ATOM 532 N ARG 67 0.159 43.769 -23.414 1.00 21.35 N ANISOU 532 N ARG 67 2877 2360 2672 512 -387 -514 N ATOM 533 CA ARG 67 1.093 43.339 -24.432 1.00 21.87 C ANISOU 533 CA ARG 67 3031 2601 2474 376 -208 -181 C ATOM 534 C ARG 67 1.626 41.949 -24.091 1.00 21.80 C ANISOU 534 C ARG 67 2858 2478 2744 414 390 -288 C ATOM 535 O ARG 67 2.038 41.252 -25.035 1.00 25.77 O ANISOU 535 O ARG 67 3793 3025 2730 506 238 -696 O ATOM 536 CB AARG 67 2.322 44.223 -24.597 0.56 23.88 C ANISOU 536 CB AARG 67 3309 2684 2856 249 -175 278 C ATOM 537 CB BARG 67 2.202 44.374 -24.625 0.44 25.47 C ANISOU 537 CB BARG 67 3533 2763 3144 168 -81 381 C ATOM 538 CG AARG 67 2.237 45.381 -25.588 0.56 29.56 C ANISOU 538 CG AARG 67 4401 2944 3608 525 97 763 C ATOM 539 CG BARG 67 1.671 45.788 -24.873 0.44 29.56 C ANISOU 539 CG BARG 67 4186 2863 3904 338 241 745 C ATOM 540 CD AARG 67 3.215 46.484 -25.259 0.56 31.78 C ANISOU 540 CD AARG 67 4457 3026 4295 252 206 1156 C ATOM 541 CD BARG 67 2.700 46.910 -24.984 0.44 33.17 C ANISOU 541 CD BARG 67 4786 2850 4654 110 377 782 C ATOM 542 NE AARG 67 4.510 46.556 -25.889 0.56 34.02 N ANISOU 542 NE AARG 67 4441 3642 4522 497 211 1422 N ATOM 543 NE BARG 67 2.146 48.142 -24.425 0.44 37.03 N ANISOU 543 NE BARG 67 5428 2769 5523 280 503 789 N ATOM 544 CZ AARG 67 5.640 47.008 -25.361 0.56 34.01 C ANISOU 544 CZ AARG 67 4328 3606 4668 497 625 676 C ATOM 545 CZ BARG 67 2.667 49.222 -23.886 0.44 37.44 C ANISOU 545 CZ BARG 67 5663 2699 5511 404 468 734 C ATOM 546 NH1AARG 67 5.739 47.460 -24.105 0.56 34.03 N ANISOU 546 NH1AARG 67 4745 2314 5551 786 868 -461 N ATOM 547 NH1BARG 67 3.982 49.421 -23.764 0.44 37.35 N ANISOU 547 NH1BARG 67 5849 2990 5000 575 -1030 1263 N ATOM 548 NH2AARG 67 6.764 47.035 -26.081 0.56 36.97 N ANISOU 548 NH2AARG 67 3972 4731 4997 1733 544 842 N ATOM 549 NH2BARG 67 1.850 50.187 -23.439 0.44 39.70 N ANISOU 549 NH2BARG 67 6706 2868 5137 606 1579 1072 N ATOM 550 N LEU 68 1.633 41.548 -22.854 1.00 19.18 N ANISOU 550 N LEU 68 2348 1988 2770 516 448 -329 N ATOM 551 CA LEU 68 1.974 40.254 -22.315 1.00 20.35 C ANISOU 551 CA LEU 68 2185 2012 3343 300 671 -112 C ATOM 552 C LEU 68 0.732 39.784 -21.561 1.00 23.35 C ANISOU 552 C LEU 68 2368 2205 4079 662 1175 71 C ATOM 553 O LEU 68 0.084 40.612 -20.915 1.00 27.39 O ANISOU 553 O LEU 68 3087 2525 4538 700 1651 -131 O ATOM 554 CB LEU 68 3.178 40.217 -21.385 1.00 20.56 C ANISOU 554 CB LEU 68 2458 2449 2711 700 773 204 C ATOM 555 CG LEU 68 4.515 40.553 -22.035 1.00 20.45 C ANISOU 555 CG LEU 68 2288 2197 3094 116 432 -135 C ATOM 556 CD1 LEU 68 5.658 40.651 -21.040 1.00 24.57 C ANISOU 556 CD1 LEU 68 2751 2773 3580 514 -85 -51 C ATOM 557 CD2 LEU 68 4.908 39.481 -23.044 1.00 23.43 C ANISOU 557 CD2 LEU 68 1938 3201 3545 473 777 -566 C ATOM 558 N ASP 69 0.395 38.501 -21.604 1.00 23.98 N ANISOU 558 N ASP 69 2095 2292 4498 394 1117 90 N ATOM 559 CA ASP 69 -0.779 38.062 -20.853 1.00 27.42 C ANISOU 559 CA ASP 69 1857 3307 4997 306 945 535 C ATOM 560 C ASP 69 -0.407 37.706 -19.428 1.00 26.33 C ANISOU 560 C ASP 69 1907 3120 4728 138 1220 309 C ATOM 561 O ASP 69 0.756 37.784 -18.988 1.00 26.14 O ANISOU 561 O ASP 69 1953 3417 4318 255 1205 -239 O ATOM 562 CB ASP 69 -1.518 36.955 -21.588 1.00 27.25 C ANISOU 562 CB ASP 69 2137 3299 4663 -9 948 829 C ATOM 563 CG ASP 69 -0.837 35.595 -21.566 1.00 29.50 C ANISOU 563 CG ASP 69 2519 3354 5060 113 335 529 C ATOM 564 OD1 ASP 69 -0.031 35.216 -20.675 1.00 28.23 O ANISOU 564 OD1 ASP 69 2049 3837 4575 418 722 301 O ATOM 565 OD2 ASP 69 -1.193 34.823 -22.512 1.00 33.49 O ANISOU 565 OD2 ASP 69 3384 3015 6012 -70 -787 563 O ATOM 566 N GLU 70 -1.393 37.378 -18.615 1.00 29.12 N ANISOU 566 N GLU 70 2059 3811 4920 1 1412 -77 N ATOM 567 CA GLU 70 -1.227 37.089 -17.231 1.00 31.38 C ANISOU 567 CA GLU 70 2646 4114 4868 126 1941 27 C ATOM 568 C GLU 70 -0.252 35.993 -16.910 1.00 28.38 C ANISOU 568 C GLU 70 2441 3572 4503 -419 1586 114 C ATOM 569 O GLU 70 0.584 36.119 -15.997 1.00 28.51 O ANISOU 569 O GLU 70 2555 3787 4225 -219 1742 -602 O ATOM 570 CB AGLU 70 -2.632 36.741 -16.691 0.49 35.62 C ANISOU 570 CB AGLU 70 2595 4999 5605 -77 1955 312 C ATOM 571 CB BGLU 70 -2.479 37.096 -16.396 0.51 35.59 C ANISOU 571 CB BGLU 70 2616 5129 5444 58 2046 236 C ATOM 572 CG AGLU 70 -3.464 35.822 -17.535 0.49 38.89 C ANISOU 572 CG AGLU 70 2832 5409 6170 -334 1483 405 C ATOM 573 CG BGLU 70 -3.242 35.786 -16.380 0.51 38.38 C ANISOU 573 CG BGLU 70 2734 5459 6027 -239 1978 524 C ATOM 574 CD AGLU 70 -4.323 36.278 -18.677 0.49 40.48 C ANISOU 574 CD AGLU 70 2679 5511 6809 -91 1191 450 C ATOM 575 CD BGLU 70 -4.520 35.926 -15.573 0.51 41.87 C ANISOU 575 CD BGLU 70 2480 6365 6669 -85 2006 882 C ATOM 576 OE1BGLU 70 -4.378 36.180 -14.356 0.51 46.19 O ANISOU 576 OE1BGLU 70 3142 7388 6588 355 2550 598 O ATOM 577 OE1AGLU 70 -4.221 37.412 -19.213 0.49 40.37 O ANISOU 577 OE1AGLU 70 1556 5539 7864 653 1679 837 O ATOM 578 OE2AGLU 70 -5.159 35.424 -19.094 0.49 44.32 O ANISOU 578 OE2AGLU 70 3939 5073 7412 322 341 -427 O ATOM 579 OE2BGLU 70 -5.632 35.772 -16.130 0.51 48.51 O ANISOU 579 OE2BGLU 70 2536 7476 7967 442 1314 1977 O ATOM 580 N ASP 71 -0.281 34.943 -17.744 1.00 25.80 N ANISOU 580 N ASP 71 2072 3679 3809 -100 974 349 N ATOM 581 CA ASP 71 0.653 33.841 -17.516 1.00 25.02 C ANISOU 581 CA ASP 71 2011 3240 4021 -394 792 549 C ATOM 582 C ASP 71 2.087 34.199 -17.890 1.00 21.68 C ANISOU 582 C ASP 71 2066 2438 3529 -204 831 347 C ATOM 583 O ASP 71 3.029 33.741 -17.241 1.00 21.91 O ANISOU 583 O ASP 71 2046 2509 3565 -227 775 439 O ATOM 584 CB ASP 71 0.241 32.568 -18.247 1.00 27.77 C ANISOU 584 CB ASP 71 2214 3517 4560 -698 910 194 C ATOM 585 CG ASP 71 -1.080 32.048 -17.701 1.00 36.77 C ANISOU 585 CG ASP 71 2860 4908 5859 -1628 1125 592 C ATOM 586 OD1 ASP 71 -1.047 31.594 -16.554 1.00 50.91 O ANISOU 586 OD1 ASP 71 4388 6939 7538 -2170 1375 3143 O ATOM 587 OD2 ASP 71 -2.105 32.163 -18.375 1.00 48.35 O ANISOU 587 OD2 ASP 71 2582 7872 7461 -1935 806 1026 O ATOM 588 N GLU 72 2.235 34.982 -18.943 1.00 20.04 N ANISOU 588 N GLU 72 1779 2139 3508 -4 716 223 N ATOM 589 CA GLU 72 3.529 35.459 -19.405 1.00 18.05 C ANISOU 589 CA GLU 72 1760 1925 3006 23 667 157 C ATOM 590 C GLU 72 4.161 36.369 -18.356 1.00 18.93 C ANISOU 590 C GLU 72 1728 2445 2841 -85 1075 -59 C ATOM 591 O GLU 72 5.348 36.218 -18.044 1.00 17.78 O ANISOU 591 O GLU 72 1857 2119 2612 -26 772 -21 O ATOM 592 CB GLU 72 3.424 36.161 -20.765 1.00 18.96 C ANISOU 592 CB GLU 72 2094 1947 2985 214 618 111 C ATOM 593 CG GLU 72 3.086 35.153 -21.866 1.00 19.63 C ANISOU 593 CG GLU 72 2320 1896 3058 403 710 -81 C ATOM 594 CD GLU 72 2.685 35.810 -23.181 1.00 21.70 C ANISOU 594 CD GLU 72 2381 2568 3091 702 412 -147 C ATOM 595 OE1 GLU 72 2.135 36.935 -23.202 1.00 22.67 O ANISOU 595 OE1 GLU 72 2523 2945 2933 1076 588 -22 O ATOM 596 OE2 GLU 72 2.887 35.078 -24.174 1.00 28.40 O ANISOU 596 OE2 GLU 72 4100 3227 3196 1589 177 -365 O ATOM 597 N ILE 73 3.390 37.290 -17.756 1.00 19.43 N ANISOU 597 N ILE 73 2119 2272 2808 174 973 40 N ATOM 598 CA ILE 73 3.908 38.209 -16.740 1.00 19.01 C ANISOU 598 CA ILE 73 2126 2133 2784 208 892 191 C ATOM 599 C ILE 73 4.275 37.417 -15.505 1.00 19.20 C ANISOU 599 C ILE 73 2031 2304 2780 88 964 308 C ATOM 600 O ILE 73 5.341 37.643 -14.897 1.00 20.27 O ANISOU 600 O ILE 73 2228 2817 2466 -43 952 120 O ATOM 601 CB ILE 73 2.938 39.375 -16.501 1.00 20.79 C ANISOU 601 CB ILE 73 2783 2511 2410 624 968 39 C ATOM 602 CG1 ILE 73 2.841 40.258 -17.733 1.00 21.41 C ANISOU 602 CG1 ILE 73 2767 2383 2783 397 664 306 C ATOM 603 CG2 ILE 73 3.276 40.157 -15.234 1.00 24.60 C ANISOU 603 CG2 ILE 73 3062 3473 2581 679 1060 -410 C ATOM 604 CD1 ILE 73 1.739 41.283 -17.690 1.00 30.72 C ANISOU 604 CD1 ILE 73 4549 3270 3565 1771 860 254 C ATOM 605 N ALA 74 3.386 36.513 -15.087 1.00 21.10 N ANISOU 605 N ALA 74 2316 2754 2751 -143 1070 409 N ATOM 606 CA ALA 74 3.724 35.707 -13.910 1.00 21.50 C ANISOU 606 CA ALA 74 2645 2821 2502 -213 1089 280 C ATOM 607 C ALA 74 4.980 34.881 -14.121 1.00 20.94 C ANISOU 607 C ALA 74 2466 2358 2936 -353 840 284 C ATOM 608 O ALA 74 5.794 34.706 -13.208 1.00 22.21 O ANISOU 608 O ALA 74 2714 3026 2491 -292 1116 738 O ATOM 609 CB ALA 74 2.562 34.770 -13.629 1.00 26.70 C ANISOU 609 CB ALA 74 2673 3571 3649 -370 1544 914 C ATOM 610 N GLY 75 5.098 34.305 -15.324 1.00 19.41 N ANISOU 610 N GLY 75 2397 1905 2891 -190 825 425 N ATOM 611 CA GLY 75 6.293 33.479 -15.516 1.00 19.43 C ANISOU 611 CA GLY 75 2530 1669 3001 -152 666 619 C ATOM 612 C GLY 75 7.566 34.297 -15.615 1.00 17.82 C ANISOU 612 C GLY 75 2448 1661 2493 -46 890 401 C ATOM 613 O GLY 75 8.558 33.796 -15.040 1.00 17.56 O ANISOU 613 O GLY 75 2444 1702 2361 -65 937 502 O ATOM 614 N VAL 76 7.584 35.427 -16.254 1.00 16.05 N ANISOU 614 N VAL 76 2174 1579 2195 -149 813 246 N ATOM 615 CA VAL 76 8.847 36.194 -16.306 1.00 15.23 C ANISOU 615 CA VAL 76 2117 1476 2050 -51 673 265 C ATOM 616 C VAL 76 9.158 36.728 -14.941 1.00 15.30 C ANISOU 616 C VAL 76 2161 1568 1938 -36 879 214 C ATOM 617 O VAL 76 10.371 36.780 -14.568 1.00 15.97 O ANISOU 617 O VAL 76 2160 2057 1700 58 797 346 O ATOM 618 CB VAL 76 8.832 37.247 -17.405 1.00 14.64 C ANISOU 618 CB VAL 76 1981 1505 1939 -26 785 241 C ATOM 619 CG1 VAL 76 7.922 38.435 -17.108 1.00 17.31 C ANISOU 619 CG1 VAL 76 2475 1648 2293 244 930 296 C ATOM 620 CG2 VAL 76 10.289 37.678 -17.691 1.00 16.13 C ANISOU 620 CG2 VAL 76 2156 1707 2112 -251 938 109 C ATOM 621 N ALA 77 8.175 37.110 -14.153 1.00 16.46 N ANISOU 621 N ALA 77 2086 2119 1895 75 882 437 N ATOM 622 CA ALA 77 8.437 37.589 -12.816 1.00 17.36 C ANISOU 622 CA ALA 77 2382 2081 1971 175 961 230 C ATOM 623 C ALA 77 9.074 36.465 -11.997 1.00 17.57 C ANISOU 623 C ALA 77 2839 2069 1604 432 837 -101 C ATOM 624 O ALA 77 10.045 36.649 -11.246 1.00 20.85 O ANISOU 624 O ALA 77 2823 2946 1958 -309 730 891 O ATOM 625 CB ALA 77 7.142 38.025 -12.126 1.00 19.94 C ANISOU 625 CB ALA 77 2390 2940 2061 448 981 324 C ATOM 626 N ALA 78 8.574 35.204 -12.173 1.00 19.10 N ANISOU 626 N ALA 78 2861 2201 2014 4 1021 621 N ATOM 627 CA ALA 78 9.139 34.091 -11.436 1.00 19.79 C ANISOU 627 CA ALA 78 3025 2344 1963 -25 794 602 C ATOM 628 C ALA 78 10.562 33.745 -11.885 1.00 19.55 C ANISOU 628 C ALA 78 2924 2333 1986 -31 700 822 C ATOM 629 O ALA 78 11.431 33.374 -11.101 1.00 19.95 O ANISOU 629 O ALA 78 3131 2197 2066 -82 541 851 O ATOM 630 CB ALA 78 8.289 32.853 -11.563 1.00 24.95 C ANISOU 630 CB ALA 78 3393 2721 3132 -602 824 1422 C ATOM 631 N TYR 79 10.841 33.893 -13.172 1.00 18.21 N ANISOU 631 N TYR 79 2898 1996 1856 -59 713 632 N ATOM 632 CA TYR 79 12.200 33.728 -13.676 1.00 18.31 C ANISOU 632 CA TYR 79 2822 1994 1968 -87 602 637 C ATOM 633 C TYR 79 13.158 34.796 -13.137 1.00 16.50 C ANISOU 633 C TYR 79 2733 1834 1546 210 376 834 C ATOM 634 O TYR 79 14.222 34.392 -12.690 1.00 17.35 O ANISOU 634 O TYR 79 2632 1978 1819 315 450 722 O ATOM 635 CB TYR 79 12.182 33.773 -15.210 1.00 17.29 C ANISOU 635 CB TYR 79 2857 1720 1830 159 606 413 C ATOM 636 CG TYR 79 13.533 33.697 -15.884 1.00 17.43 C ANISOU 636 CG TYR 79 2590 1996 1873 374 380 687 C ATOM 637 CD1 TYR 79 14.270 32.524 -15.967 1.00 18.53 C ANISOU 637 CD1 TYR 79 2685 2056 2126 440 333 652 C ATOM 638 CD2 TYR 79 14.118 34.821 -16.479 1.00 17.59 C ANISOU 638 CD2 TYR 79 2640 1969 1908 367 499 646 C ATOM 639 CE1 TYR 79 15.513 32.455 -16.602 1.00 19.41 C ANISOU 639 CE1 TYR 79 2618 2154 2422 458 317 397 C ATOM 640 CE2 TYR 79 15.342 34.769 -17.107 1.00 18.02 C ANISOU 640 CE2 TYR 79 2386 2181 2112 155 239 545 C ATOM 641 CZ TYR 79 16.044 33.585 -17.169 1.00 19.11 C ANISOU 641 CZ TYR 79 2670 2316 2096 323 535 220 C ATOM 642 OH TYR 79 17.296 33.588 -17.785 1.00 22.65 O ANISOU 642 OH TYR 79 2682 3468 2242 524 610 551 O ATOM 643 N VAL 80 12.770 36.058 -13.124 1.00 16.16 N ANISOU 643 N VAL 80 2595 1817 1578 248 715 721 N ATOM 644 CA VAL 80 13.636 37.061 -12.504 1.00 17.09 C ANISOU 644 CA VAL 80 2851 1896 1585 261 674 547 C ATOM 645 C VAL 80 13.866 36.727 -11.050 1.00 16.40 C ANISOU 645 C VAL 80 2534 1886 1658 299 699 571 C ATOM 646 O VAL 80 15.009 36.754 -10.605 1.00 17.45 O ANISOU 646 O VAL 80 2488 1990 1988 165 608 958 O ATOM 647 CB VAL 80 13.024 38.459 -12.645 1.00 17.52 C ANISOU 647 CB VAL 80 2808 1838 1847 182 390 622 C ATOM 648 CG1 VAL 80 13.790 39.463 -11.775 1.00 20.92 C ANISOU 648 CG1 VAL 80 3558 2065 2130 -102 671 146 C ATOM 649 CG2 VAL 80 13.089 38.851 -14.109 1.00 19.43 C ANISOU 649 CG2 VAL 80 3149 2060 1991 -13 318 807 C ATOM 650 N TYR 81 12.826 36.343 -10.302 1.00 16.34 N ANISOU 650 N TYR 81 2488 1987 1582 -57 491 572 N ATOM 651 CA TYR 81 12.941 36.010 -8.885 1.00 18.23 C ANISOU 651 CA TYR 81 2527 2580 1649 338 675 688 C ATOM 652 C TYR 81 13.990 34.892 -8.730 1.00 17.61 C ANISOU 652 C TYR 81 2498 2497 1531 209 701 831 C ATOM 653 O TYR 81 14.844 34.940 -7.845 1.00 20.34 O ANISOU 653 O TYR 81 2853 2416 2270 -63 114 1122 O ATOM 654 CB TYR 81 11.574 35.632 -8.308 1.00 18.87 C ANISOU 654 CB TYR 81 2620 2635 1737 175 754 684 C ATOM 655 CG TYR 81 11.603 35.460 -6.811 1.00 19.25 C ANISOU 655 CG TYR 81 2633 2764 1734 -303 595 813 C ATOM 656 CD1 TYR 81 11.979 34.229 -6.236 1.00 21.73 C ANISOU 656 CD1 TYR 81 3351 2598 2104 -699 384 995 C ATOM 657 CD2 TYR 81 11.419 36.542 -5.972 1.00 19.70 C ANISOU 657 CD2 TYR 81 2818 2968 1516 7 182 814 C ATOM 658 CE1 TYR 81 12.085 34.099 -4.866 1.00 24.85 C ANISOU 658 CE1 TYR 81 3673 3312 2224 -313 490 1339 C ATOM 659 CE2 TYR 81 11.514 36.416 -4.604 1.00 21.35 C ANISOU 659 CE2 TYR 81 2963 3468 1481 -267 412 891 C ATOM 660 CZ TYR 81 11.856 35.201 -4.065 1.00 22.35 C ANISOU 660 CZ TYR 81 3106 3512 1664 -564 121 1183 C ATOM 661 OH TYR 81 11.945 35.066 -2.686 1.00 29.91 O ANISOU 661 OH TYR 81 4896 4375 1814 -729 -17 1593 O ATOM 662 N ASP 82 13.778 33.798 -9.488 1.00 19.73 N ANISOU 662 N ASP 82 3155 2094 2064 120 296 1028 N ATOM 663 CA ASP 82 14.606 32.608 -9.372 1.00 19.95 C ANISOU 663 CA ASP 82 3236 2271 1886 260 316 898 C ATOM 664 C ASP 82 16.054 32.900 -9.727 1.00 18.97 C ANISOU 664 C ASP 82 3151 1946 1933 12 83 822 C ATOM 665 O ASP 82 17.030 32.463 -9.076 1.00 21.22 O ANISOU 665 O ASP 82 3441 2070 2353 529 184 1076 O ATOM 666 CB ASP 82 14.118 31.457 -10.287 1.00 20.87 C ANISOU 666 CB ASP 82 3100 2119 2514 -152 196 972 C ATOM 667 CG ASP 82 14.964 30.212 -10.094 1.00 22.65 C ANISOU 667 CG ASP 82 4141 2079 2175 147 -98 1045 C ATOM 668 OD1 ASP 82 14.829 29.519 -9.097 1.00 36.99 O ANISOU 668 OD1 ASP 82 8386 2523 2798 683 827 1629 O ATOM 669 OD2 ASP 82 15.630 29.769 -11.032 1.00 25.31 O ANISOU 669 OD2 ASP 82 4192 2177 3009 122 271 669 O ATOM 670 N GLN 83 16.308 33.688 -10.760 1.00 18.54 N ANISOU 670 N GLN 83 2926 2005 1941 589 369 921 N ATOM 671 CA GLN 83 17.656 34.048 -11.128 1.00 18.05 C ANISOU 671 CA GLN 83 2663 2193 1832 929 535 666 C ATOM 672 C GLN 83 18.343 34.906 -10.047 1.00 17.99 C ANISOU 672 C GLN 83 2613 2097 1956 737 568 855 C ATOM 673 O GLN 83 19.527 34.623 -9.864 1.00 20.66 O ANISOU 673 O GLN 83 2835 2328 2494 1026 241 407 O ATOM 674 CB GLN 83 17.664 34.871 -12.451 1.00 17.17 C ANISOU 674 CB GLN 83 2766 1669 1926 669 399 613 C ATOM 675 CG GLN 83 17.270 34.100 -13.697 1.00 18.98 C ANISOU 675 CG GLN 83 3394 1831 1807 533 535 547 C ATOM 676 CD GLN 83 18.374 33.198 -14.177 1.00 17.57 C ANISOU 676 CD GLN 83 2826 1831 1855 366 217 438 C ATOM 677 OE1 GLN 83 19.401 33.591 -14.790 1.00 23.51 O ANISOU 677 OE1 GLN 83 3013 3081 2618 161 493 700 O ATOM 678 NE2 GLN 83 18.254 31.911 -14.008 1.00 20.43 N ANISOU 678 NE2 GLN 83 3078 1850 2641 607 78 483 N ATOM 679 N ALA 84 17.595 35.803 -9.440 1.00 17.42 N ANISOU 679 N ALA 84 2503 1860 2091 606 440 693 N ATOM 680 CA ALA 84 18.140 36.649 -8.395 1.00 18.00 C ANISOU 680 CA ALA 84 2493 2166 2010 483 311 769 C ATOM 681 C ALA 84 18.367 35.840 -7.133 1.00 19.11 C ANISOU 681 C ALA 84 2763 2270 2049 452 363 770 C ATOM 682 O ALA 84 19.432 35.841 -6.526 1.00 20.81 O ANISOU 682 O ALA 84 2959 2316 2435 506 -52 848 O ATOM 683 CB ALA 84 17.211 37.817 -8.166 1.00 18.73 C ANISOU 683 CB ALA 84 3010 1883 2049 420 382 626 C ATOM 684 N ALA 85 17.394 35.051 -6.670 1.00 20.46 N ANISOU 684 N ALA 85 2851 2340 2390 504 404 1176 N ATOM 685 CA ALA 85 17.425 34.313 -5.431 1.00 21.46 C ANISOU 685 CA ALA 85 2973 2812 2169 485 322 1146 C ATOM 686 C ALA 85 18.537 33.269 -5.488 1.00 20.73 C ANISOU 686 C ALA 85 2935 2749 1996 483 -111 1072 C ATOM 687 O ALA 85 19.160 32.942 -4.473 1.00 25.47 O ANISOU 687 O ALA 85 3848 3022 2567 526 -627 1132 O ATOM 688 CB ALA 85 16.104 33.601 -5.134 1.00 23.85 C ANISOU 688 CB ALA 85 3073 3020 2746 504 476 1733 C ATOM 689 N GLY 86 18.793 32.638 -6.631 1.00 21.84 N ANISOU 689 N GLY 86 3511 2194 2388 396 250 1036 N ATOM 690 CA GLY 86 19.775 31.579 -6.793 1.00 23.31 C ANISOU 690 CA GLY 86 3504 2354 2778 467 142 993 C ATOM 691 C GLY 86 21.115 32.094 -7.223 1.00 22.98 C ANISOU 691 C GLY 86 3240 2539 2739 454 -343 872 C ATOM 692 O GLY 86 22.032 31.313 -7.467 1.00 26.54 O ANISOU 692 O GLY 86 3166 2954 3715 805 -514 1101 O ATOM 693 N ASN 87 21.273 33.405 -7.412 1.00 21.96 N ANISOU 693 N ASN 87 2997 2505 2637 259 -273 709 N ATOM 694 CA ASN 87 22.571 33.950 -7.842 1.00 23.90 C ANISOU 694 CA ASN 87 2825 2901 3132 239 -146 278 C ATOM 695 C ASN 87 22.941 33.334 -9.175 1.00 24.62 C ANISOU 695 C ASN 87 2916 2956 3253 887 -25 345 C ATOM 696 O ASN 87 24.066 32.901 -9.424 1.00 28.91 O ANISOU 696 O ASN 87 2930 4173 3610 1176 -58 444 O ATOM 697 CB ASN 87 23.617 33.836 -6.738 1.00 28.86 C ANISOU 697 CB ASN 87 3022 3871 3802 628 -562 -364 C ATOM 698 CG ASN 87 23.395 34.823 -5.598 1.00 30.78 C ANISOU 698 CG ASN 87 3557 4238 3611 1531 -1070 -385 C ATOM 699 OD1 ASN 87 22.750 35.872 -5.674 1.00 40.43 O ANISOU 699 OD1 ASN 87 5662 4207 5113 2167 -1885 -825 O ATOM 700 ND2 ASN 87 23.934 34.475 -4.442 1.00 41.60 N ANISOU 700 ND2 ASN 87 6652 5949 2816 2464 -247 620 N ATOM 701 N LYS 88 22.008 33.292 -10.122 1.00 20.48 N ANISOU 701 N LYS 88 2640 2158 2790 683 351 540 N ATOM 702 CA LYS 88 22.236 32.568 -11.373 1.00 21.88 C ANISOU 702 CA LYS 88 2909 2282 2916 784 519 473 C ATOM 703 C LYS 88 22.695 33.375 -12.549 1.00 23.05 C ANISOU 703 C LYS 88 3222 2586 2735 336 244 464 C ATOM 704 O LYS 88 23.097 32.789 -13.571 1.00 29.12 O ANISOU 704 O LYS 88 4584 3