HEADER TRANSFERASE 26-APR-06 2GSF TITLE THE HUMAN EPHA3 RECEPTOR TYROSINE KINASE AND JUXTAMEMBRANE TITLE 2 REGION COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN, JUXTAMEMBRANE REGION, RESIDUES COMPND 5 577-947; COMPND 6 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR ETK1, HEK, HEK4; COMPND 7 EC: 2.7.10.1; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: EPHA3, ETK, ETK1, HEK; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-LIC KEYWDS ATP-BINDING, KINASE, MEMBRANE, NUCLEOTIDE-BINDING, KEYWDS 2 PHOSPHORYLATION, RECEPTOR, SIGNAL, TRANSFERASE, KEYWDS 3 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, STRUCTURAL GENOMICS, KEYWDS 4 STRUCTURAL GENOMICS CONSORTIUM, SGC EXPDTA X-RAY DIFFRACTION AUTHOR J.R.WALKER,T.DAVIS,A.DONG,E.M.NEWMAN,F.MACKENZIE,J.WEIGELT, AUTHOR 2 M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE- AUTHOR 3 PAGANON,STRUCTURAL GENOMICS CONSORTIUM (SGC) REVDAT 2 24-FEB-09 2GSF 1 VERSN REVDAT 1 13-JUN-06 2GSF 0 JRNL AUTH T.DAVIS,J.R.WALKER,A.DONG,E.M.NEWMAN,F.MACKENZIE, JRNL AUTH 2 J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS, JRNL AUTH 3 A.BOCHKAREV,S.DHE-PAGANON JRNL TITL STRUCTURE OF THE HUMAN EPHA3 RECEPTOR TYROSINE JRNL TITL 2 KINASE AND JUXTAMEMBRANE REGION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.77 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 28392 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.160 REMARK 3 R VALUE (WORKING SET) : 0.158 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1513 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.77 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2026 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.1560 REMARK 3 BIN FREE R VALUE SET COUNT : 113 REMARK 3 BIN FREE R VALUE : 0.2050 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2233 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 264 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.65 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.24000 REMARK 3 B22 (A**2) : -0.01000 REMARK 3 B33 (A**2) : -0.29000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.24000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.105 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.596 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2277 ; 0.014 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3073 ; 1.415 ; 1.967 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 5.089 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;32.043 ;23.737 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 415 ;12.625 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.989 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 343 ; 0.110 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1679 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1131 ; 0.215 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1602 ; 0.312 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 207 ; 0.164 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 64 ; 0.246 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.178 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1443 ; 1.761 ; 3.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2259 ; 2.573 ; 4.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 965 ; 3.487 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 814 ; 5.096 ; 7.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 595 A 612 REMARK 3 ORIGIN FOR THE GROUP (A): -11.6967 27.4756 51.7155 REMARK 3 T TENSOR REMARK 3 T11: -0.0199 T22: -0.0027 REMARK 3 T33: 0.1051 T12: -0.0100 REMARK 3 T13: 0.0656 T23: -0.0966 REMARK 3 L TENSOR REMARK 3 L11: 37.9840 L22: 5.3050 REMARK 3 L33: 1.7940 L12: 8.2747 REMARK 3 L13: 5.8881 L23: 3.0396 REMARK 3 S TENSOR REMARK 3 S11: -0.0268 S12: -2.6656 S13: 0.7593 REMARK 3 S21: 0.4680 S22: -0.7039 S23: 1.1246 REMARK 3 S31: 0.2506 S32: -0.4992 S33: 0.7307 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 613 A 623 REMARK 3 ORIGIN FOR THE GROUP (A): -22.4452 13.0449 41.8963 REMARK 3 T TENSOR REMARK 3 T11: -0.0182 T22: 0.0664 REMARK 3 T33: 0.0707 T12: 0.0170 REMARK 3 T13: -0.0039 T23: 0.0080 REMARK 3 L TENSOR REMARK 3 L11: 3.5886 L22: 7.9474 REMARK 3 L33: 2.5828 L12: -0.4124 REMARK 3 L13: 1.9579 L23: 3.2341 REMARK 3 S TENSOR REMARK 3 S11: -0.0606 S12: -0.2067 S13: 0.0645 REMARK 3 S21: -0.1637 S22: -0.0930 S23: 0.4442 REMARK 3 S31: -0.1669 S32: -0.1897 S33: 0.1536 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 624 A 634 REMARK 3 ORIGIN FOR THE GROUP (A): -17.3731 4.3270 55.1079 REMARK 3 T TENSOR REMARK 3 T11: 0.0136 T22: 0.0447 REMARK 3 T33: -0.0030 T12: -0.0117 REMARK 3 T13: -0.0107 T23: 0.0997 REMARK 3 L TENSOR REMARK 3 L11: 3.2954 L22: 22.2238 REMARK 3 L33: 28.6398 L12: 0.6714 REMARK 3 L13: 1.7986 L23: 22.8370 REMARK 3 S TENSOR REMARK 3 S11: -0.0248 S12: -0.3530 S13: -0.3466 REMARK 3 S21: 1.1163 S22: 0.4876 S23: -0.6575 REMARK 3 S31: 1.4044 S32: 0.3149 S33: -0.4628 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 635 A 653 REMARK 3 ORIGIN FOR THE GROUP (A): -16.6509 8.1806 39.8354 REMARK 3 T TENSOR REMARK 3 T11: 0.0283 T22: 0.0333 REMARK 3 T33: 0.0721 T12: -0.0050 REMARK 3 T13: -0.0049 T23: 0.0067 REMARK 3 L TENSOR REMARK 3 L11: 2.1152 L22: 1.7809 REMARK 3 L33: 7.2802 L12: -0.6666 REMARK 3 L13: 1.4714 L23: -0.7388 REMARK 3 S TENSOR REMARK 3 S11: 0.0528 S12: -0.1257 S13: -0.1003 REMARK 3 S21: -0.0216 S22: 0.0908 S23: 0.0795 REMARK 3 S31: 0.1286 S32: 0.0034 S33: -0.1436 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 654 A 676 REMARK 3 ORIGIN FOR THE GROUP (A): -18.8027 17.9505 57.4287 REMARK 3 T TENSOR REMARK 3 T11: -0.0095 T22: 0.0957 REMARK 3 T33: 0.0083 T12: -0.0440 REMARK 3 T13: 0.0054 T23: -0.0592 REMARK 3 L TENSOR REMARK 3 L11: 10.3288 L22: 4.8410 REMARK 3 L33: 2.2944 L12: 6.1678 REMARK 3 L13: -4.8466 L23: -3.0471 REMARK 3 S TENSOR REMARK 3 S11: 0.3758 S12: -0.6878 S13: 0.4387 REMARK 3 S21: 0.2611 S22: -0.2614 S23: 0.2704 REMARK 3 S31: -0.1324 S32: 0.1243 S33: -0.1144 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 677 A 700 REMARK 3 ORIGIN FOR THE GROUP (A): -13.7563 15.6859 46.6744 REMARK 3 T TENSOR REMARK 3 T11: 0.0212 T22: 0.0293 REMARK 3 T33: 0.0501 T12: 0.0140 REMARK 3 T13: 0.0014 T23: -0.0065 REMARK 3 L TENSOR REMARK 3 L11: 4.4866 L22: 0.8206 REMARK 3 L33: 1.7743 L12: 0.3562 REMARK 3 L13: -0.6369 L23: 0.0751 REMARK 3 S TENSOR REMARK 3 S11: 0.0012 S12: -0.0552 S13: 0.0389 REMARK 3 S21: -0.0283 S22: -0.0256 S23: 0.1507 REMARK 3 S31: -0.0760 S32: -0.2001 S33: 0.0244 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 701 A 714 REMARK 3 ORIGIN FOR THE GROUP (A): -1.1695 0.0598 51.3146 REMARK 3 T TENSOR REMARK 3 T11: 0.0376 T22: 0.0189 REMARK 3 T33: 0.0550 T12: -0.0025 REMARK 3 T13: -0.0035 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 3.5293 L22: 4.0391 REMARK 3 L33: 1.2275 L12: -2.6923 REMARK 3 L13: 1.9641 L23: -2.0149 REMARK 3 S TENSOR REMARK 3 S11: 0.1545 S12: -0.0549 S13: -0.1237 REMARK 3 S21: -0.0658 S22: -0.0372 S23: 0.1978 REMARK 3 S31: 0.1690 S32: -0.0611 S33: -0.1173 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 715 A 742 REMARK 3 ORIGIN FOR THE GROUP (A): 6.9061 11.2863 48.7399 REMARK 3 T TENSOR REMARK 3 T11: 0.0337 T22: 0.0419 REMARK 3 T33: 0.0304 T12: -0.0107 REMARK 3 T13: -0.0020 T23: 0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.9004 L22: 3.9110 REMARK 3 L33: 0.8044 L12: -0.7131 REMARK 3 L13: 0.1698 L23: -0.0133 REMARK 3 S TENSOR REMARK 3 S11: 0.0406 S12: 0.0437 S13: -0.0141 REMARK 3 S21: -0.0750 S22: -0.0397 S23: -0.0502 REMARK 3 S31: -0.0286 S32: 0.0243 S33: -0.0009 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 743 A 752 REMARK 3 ORIGIN FOR THE GROUP (A): -0.3276 14.1118 58.5797 REMARK 3 T TENSOR REMARK 3 T11: 0.0266 T22: 0.0379 REMARK 3 T33: 0.0207 T12: -0.0065 REMARK 3 T13: 0.0178 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 1.0321 L22: 13.1928 REMARK 3 L33: 1.7134 L12: 0.8468 REMARK 3 L13: 1.2624 L23: 2.4902 REMARK 3 S TENSOR REMARK 3 S11: 0.0076 S12: -0.1671 S13: 0.0683 REMARK 3 S21: 0.5141 S22: -0.0805 S23: 0.3672 REMARK 3 S31: 0.0502 S32: -0.1580 S33: 0.0730 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 753 A 788 REMARK 3 ORIGIN FOR THE GROUP (A): -2.0776 12.6008 53.6126 REMARK 3 T TENSOR REMARK 3 T11: 0.0542 T22: 0.0645 REMARK 3 T33: 0.0584 T12: 0.0184 REMARK 3 T13: 0.0232 T23: -0.0283 REMARK 3 L TENSOR REMARK 3 L11: 1.7089 L22: 2.0847 REMARK 3 L33: 2.5716 L12: -0.1626 REMARK 3 L13: 0.7225 L23: -0.4460 REMARK 3 S TENSOR REMARK 3 S11: 0.0045 S12: -0.3290 S13: 0.1487 REMARK 3 S21: 0.1944 S22: 0.0389 S23: 0.1849 REMARK 3 S31: -0.3087 S32: -0.2874 S33: -0.0434 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 789 A 821 REMARK 3 ORIGIN FOR THE GROUP (A): 7.3355 14.9215 62.6778 REMARK 3 T TENSOR REMARK 3 T11: 0.0228 T22: 0.0513 REMARK 3 T33: 0.0117 T12: -0.0018 REMARK 3 T13: 0.0028 T23: -0.0082 REMARK 3 L TENSOR REMARK 3 L11: 0.5880 L22: 1.6531 REMARK 3 L33: 1.2328 L12: -0.2201 REMARK 3 L13: 0.2588 L23: 0.5196 REMARK 3 S TENSOR REMARK 3 S11: -0.0115 S12: -0.1178 S13: 0.0318 REMARK 3 S21: 0.0836 S22: -0.0266 S23: 0.0406 REMARK 3 S31: -0.0735 S32: -0.0873 S33: 0.0381 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 822 A 833 REMARK 3 ORIGIN FOR THE GROUP (A): 7.0370 5.5369 71.3610 REMARK 3 T TENSOR REMARK 3 T11: 0.0297 T22: 0.0484 REMARK 3 T33: 0.0230 T12: -0.0184 REMARK 3 T13: 0.0151 T23: 0.0196 REMARK 3 L TENSOR REMARK 3 L11: 2.5868 L22: 4.7272 REMARK 3 L33: 8.1581 L12: 1.4857 REMARK 3 L13: 2.5834 L23: 1.5481 REMARK 3 S TENSOR REMARK 3 S11: 0.0374 S12: -0.1811 S13: -0.0377 REMARK 3 S21: 0.2982 S22: -0.1773 S23: 0.1922 REMARK 3 S31: 0.1253 S32: -0.1820 S33: 0.1399 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 834 A 869 REMARK 3 ORIGIN FOR THE GROUP (A): 16.7515 13.0417 63.4230 REMARK 3 T TENSOR REMARK 3 T11: 0.0262 T22: 0.0687 REMARK 3 T33: 0.0336 T12: -0.0254 REMARK 3 T13: -0.0127 T23: 0.0056 REMARK 3 L TENSOR REMARK 3 L11: 1.2700 L22: 1.3261 REMARK 3 L33: 2.2270 L12: 0.0712 REMARK 3 L13: 0.0224 L23: -0.7397 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: -0.0767 S13: 0.0264 REMARK 3 S21: 0.1265 S22: -0.1116 S23: -0.1012 REMARK 3 S31: -0.0722 S32: 0.1178 S33: 0.0717 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 870 A 893 REMARK 3 ORIGIN FOR THE GROUP (A): 18.6513 11.7511 47.6904 REMARK 3 T TENSOR REMARK 3 T11: 0.0202 T22: 0.1144 REMARK 3 T33: 0.0738 T12: -0.0298 REMARK 3 T13: 0.0218 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 3.8342 L22: 5.0299 REMARK 3 L33: 3.3381 L12: -3.0023 REMARK 3 L13: -1.1947 L23: 1.1913 REMARK 3 S TENSOR REMARK 3 S11: -0.0704 S12: 0.1756 S13: -0.0662 REMARK 3 S21: -0.0712 S22: 0.0309 S23: -0.2637 REMARK 3 S31: 0.1036 S32: 0.2909 S33: 0.0395 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 899 A 904 REMARK 3 ORIGIN FOR THE GROUP (A): 18.9354 4.3749 69.2702 REMARK 3 T TENSOR REMARK 3 T11: 0.0458 T22: 0.1045 REMARK 3 T33: 0.0058 T12: 0.0213 REMARK 3 T13: -0.0308 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 24.6003 L22: 21.5685 REMARK 3 L33: 19.6004 L12: 0.2683 REMARK 3 L13: 3.9199 L23: -2.0837 REMARK 3 S TENSOR REMARK 3 S11: 0.3354 S12: 0.1934 S13: -1.0956 REMARK 3 S21: -0.6969 S22: -0.0966 S23: -0.6090 REMARK 3 S31: 1.1106 S32: 0.8117 S33: -0.2388 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2GSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-06. REMARK 100 THE RCSB ID CODE IS RCSB037496. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-FEB-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : COLLECT REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29945 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.03800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 48.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : 64.5 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 0.09900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 21.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.23 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML PROTEIN, 25% PEG 3350, REMARK 280 0.2M AMMONIUM SULFATE, 0.1M HEPES, 20% GLYCEROL, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298.0K, PH 7.50 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 19.13700 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 575 REMARK 465 SER A 576 REMARK 465 ASP A 577 REMARK 465 GLU A 578 REMARK 465 LYS A 579 REMARK 465 ARG A 580 REMARK 465 LEU A 581 REMARK 465 HIS A 582 REMARK 465 PHE A 583 REMARK 465 GLY A 584 REMARK 465 ASN A 585 REMARK 465 GLY A 586 REMARK 465 HIS A 587 REMARK 465 LEU A 588 REMARK 465 LYS A 589 REMARK 465 LEU A 590 REMARK 465 PRO A 591 REMARK 465 GLY A 592 REMARK 465 LEU A 593 REMARK 465 ARG A 594 REMARK 465 THR A 601 REMARK 465 TYR A 602 REMARK 465 GLU A 603 REMARK 465 ASP A 604 REMARK 465 PRO A 605 REMARK 465 THR A 606 REMARK 465 GLN A 607 REMARK 465 THR A 608 REMARK 465 LEU A 771 REMARK 465 GLU A 772 REMARK 465 ASP A 773 REMARK 465 ASP A 774 REMARK 465 PRO A 775 REMARK 465 GLU A 776 REMARK 465 ALA A 777 REMARK 465 ALA A 778 REMARK 465 TYR A 779 REMARK 465 THR A 780 REMARK 465 THR A 781 REMARK 465 ARG A 782 REMARK 465 GLY A 783 REMARK 465 GLY A 784 REMARK 465 LYS A 785 REMARK 465 ILE A 786 REMARK 465 ALA A 894 REMARK 465 ALA A 895 REMARK 465 ALA A 896 REMARK 465 ARG A 897 REMARK 465 PRO A 898 REMARK 465 GLN A 905 REMARK 465 SER A 906 REMARK 465 ASN A 907 REMARK 465 VAL A 908 REMARK 465 ASP A 909 REMARK 465 ILE A 910 REMARK 465 THR A 911 REMARK 465 THR A 912 REMARK 465 PHE A 913 REMARK 465 ARG A 914 REMARK 465 THR A 915 REMARK 465 THR A 916 REMARK 465 GLY A 917 REMARK 465 ASP A 918 REMARK 465 TRP A 919 REMARK 465 LEU A 920 REMARK 465 ASN A 921 REMARK 465 GLY A 922 REMARK 465 VAL A 923 REMARK 465 TRP A 924 REMARK 465 THR A 925 REMARK 465 ALA A 926 REMARK 465 HIS A 927 REMARK 465 CYS A 928 REMARK 465 LYS A 929 REMARK 465 GLU A 930 REMARK 465 ILE A 931 REMARK 465 PHE A 932 REMARK 465 THR A 933 REMARK 465 GLY A 934 REMARK 465 VAL A 935 REMARK 465 GLU A 936 REMARK 465 TYR A 937 REMARK 465 SER A 938 REMARK 465 SER A 939 REMARK 465 CYS A 940 REMARK 465 ASP A 941 REMARK 465 THR A 942 REMARK 465 ILE A 943 REMARK 465 ALA A 944 REMARK 465 LYS A 945 REMARK 465 ILE A 946 REMARK 465 SER A 947 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 742 OG SER A 768 2.13 REMARK 500 OD1 ASP A 624 O HOH A 176 2.19 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 VAL A 627 68.82 -116.04 REMARK 500 LYS A 645 -6.67 81.34 REMARK 500 ARG A 745 -12.11 76.26 REMARK 500 ASP A 764 76.56 60.33 REMARK 500 TYR A 798 27.00 -151.26 REMARK 500 TRP A 826 -131.56 49.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE IS IN ACCORDANCE WITH THE REFERENCE CHIARI ET REMARK 999 AL., 2000, CANCER RES., 60, 4855-4863 DBREF 2GSF A 577 947 UNP P29320 EPHA3_HUMAN 577 947 SEQADV 2GSF GLY A 575 UNP P29320 CLONING ARTIFACT SEQADV 2GSF SER A 576 UNP P29320 CLONING ARTIFACT SEQADV 2GSF THR A 608 UNP P29320 ALA 608 ENGINEERED SEQADV 2GSF THR A 911 UNP P29320 SER 911 SEE REMARK 999 SEQADV 2GSF TRP A 924 UNP P29320 ARG 924 SEE REMARK 999 SEQRES 1 A 373 GLY SER ASP GLU LYS ARG LEU HIS PHE GLY ASN GLY HIS SEQRES 2 A 373 LEU LYS LEU PRO GLY LEU ARG THR TYR VAL ASP PRO HIS SEQRES 3 A 373 THR TYR GLU ASP PRO THR GLN THR VAL HIS GLU PHE ALA SEQRES 4 A 373 LYS GLU LEU ASP ALA THR ASN ILE SER ILE ASP LYS VAL SEQRES 5 A 373 VAL GLY ALA GLY GLU PHE GLY GLU VAL CYS SER GLY ARG SEQRES 6 A 373 LEU LYS LEU PRO SER LYS LYS GLU ILE SER VAL ALA ILE SEQRES 7 A 373 LYS THR LEU LYS VAL GLY TYR THR GLU LYS GLN ARG ARG SEQRES 8 A 373 ASP PHE LEU GLY GLU ALA SER ILE MET GLY GLN PHE ASP SEQRES 9 A 373 HIS PRO ASN ILE ILE ARG LEU GLU GLY VAL VAL THR LYS SEQRES 10 A 373 SER LYS PRO VAL MET ILE VAL THR GLU TYR MET GLU ASN SEQRES 11 A 373 GLY SER LEU ASP SER PHE LEU ARG LYS HIS ASP ALA GLN SEQRES 12 A 373 PHE THR VAL ILE GLN LEU VAL GLY MET LEU ARG GLY ILE SEQRES 13 A 373 ALA SER GLY MET LYS TYR LEU SER ASP MET GLY TYR VAL SEQRES 14 A 373 HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU ILE ASN SER SEQRES 15 A 373 ASN LEU VAL CYS LYS VAL SER ASP PHE GLY LEU SER ARG SEQRES 16 A 373 VAL LEU GLU ASP ASP PRO GLU ALA ALA TYR THR THR ARG SEQRES 17 A 373 GLY GLY LYS ILE PRO ILE ARG TRP THR SER PRO GLU ALA SEQRES 18 A 373 ILE ALA TYR ARG LYS PHE THR SER ALA SER ASP VAL TRP SEQRES 19 A 373 SER TYR GLY ILE VAL LEU TRP GLU VAL MET SER TYR GLY SEQRES 20 A 373 GLU ARG PRO TYR TRP GLU MET SER ASN GLN ASP VAL ILE SEQRES 21 A 373 LYS ALA VAL ASP GLU GLY TYR ARG LEU PRO PRO PRO MET SEQRES 22 A 373 ASP CYS PRO ALA ALA LEU TYR GLN LEU MET LEU ASP CYS SEQRES 23 A 373 TRP GLN LYS ASP ARG ASN ASN ARG PRO LYS PHE GLU GLN SEQRES 24 A 373 ILE VAL SER ILE LEU ASP LYS LEU ILE ARG ASN PRO GLY SEQRES 25 A 373 SER LEU LYS ILE ILE THR SER ALA ALA ALA ARG PRO SER SEQRES 26 A 373 ASN LEU LEU LEU ASP GLN SER ASN VAL ASP ILE THR THR SEQRES 27 A 373 PHE ARG THR THR GLY ASP TRP LEU ASN GLY VAL TRP THR SEQRES 28 A 373 ALA HIS CYS LYS GLU ILE PHE THR GLY VAL GLU TYR SER SEQRES 29 A 373 SER CYS ASP THR ILE ALA LYS ILE SER FORMUL 2 HOH *264(H2 O) HELIX 1 1 ASP A 617 THR A 619 5 3 HELIX 2 2 THR A 660 GLY A 675 1 16 HELIX 3 3 SER A 706 LYS A 713 1 8 HELIX 4 4 THR A 719 MET A 740 1 22 HELIX 5 5 ALA A 748 ARG A 750 5 3 HELIX 6 6 PRO A 787 THR A 791 5 5 HELIX 7 7 SER A 792 ARG A 799 1 8 HELIX 8 8 THR A 802 SER A 819 1 18 HELIX 9 9 SER A 829 GLY A 840 1 12 HELIX 10 10 PRO A 850 TRP A 861 1 12 HELIX 11 11 ASP A 864 ARG A 868 5 5 HELIX 12 12 LYS A 870 ASN A 884 1 15 HELIX 13 13 PRO A 885 ILE A 890 5 6 SHEET 1 A 5 ILE A 621 ALA A 629 0 SHEET 2 A 5 GLU A 634 LYS A 641 -1 O VAL A 635 N VAL A 627 SHEET 3 A 5 GLU A 647 THR A 654 -1 O ILE A 652 N CYS A 636 SHEET 4 A 5 MET A 696 GLU A 700 -1 O THR A 699 N ALA A 651 SHEET 5 A 5 LEU A 685 VAL A 689 -1 N GLY A 687 O VAL A 698 SHEET 1 B 2 ILE A 752 ILE A 754 0 SHEET 2 B 2 CYS A 760 VAL A 762 -1 O LYS A 761 N LEU A 753 SHEET 1 C 2 TYR A 841 ARG A 842 0 SHEET 2 C 2 LEU A 902 LEU A 903 -1 O LEU A 902 N ARG A 842 CISPEP 1 LYS A 693 PRO A 694 0 4.18 CRYST1 54.163 38.274 76.333 90.00 102.39 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 0.018463 0.000000 0.004056 0.00000 SCALE2 0.000000 0.026127 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013413 0.00000 ATOM 1 N THR A 595 -1.801 30.661 47.388 1.00 29.24 N ANISOU 1 N THR A 595 4110 3141 3859 -166 -968 777 N ATOM 2 CA THR A 595 -2.062 30.725 48.866 1.00 30.91 C ANISOU 2 CA THR A 595 4407 3069 4268 145 -809 393 C ATOM 3 C THR A 595 -3.367 30.056 49.285 1.00 31.12 C ANISOU 3 C THR A 595 4452 3075 4298 210 -594 200 C ATOM 4 O THR A 595 -4.446 30.331 48.737 1.00 34.14 O ANISOU 4 O THR A 595 4685 3302 4985 129 -718 240 O ATOM 5 CB THR A 595 -2.133 32.194 49.410 1.00 33.39 C ANISOU 5 CB THR A 595 4378 3024 5283 222 -1101 204 C ATOM 6 OG1 THR A 595 -1.106 32.994 48.842 1.00 26.80 O ANISOU 6 OG1 THR A 595 3403 2074 4706 90 -1415 576 O ATOM 7 CG2 THR A 595 -1.943 32.210 50.909 1.00 38.36 C ANISOU 7 CG2 THR A 595 4938 3879 5758 424 -868 -429 C ATOM 8 N TYR A 596 -3.237 29.215 50.289 1.00 31.37 N ANISOU 8 N TYR A 596 4585 3305 4029 302 -330 116 N ATOM 9 CA TYR A 596 -4.329 28.606 51.006 1.00 34.35 C ANISOU 9 CA TYR A 596 4882 3838 4330 284 -116 55 C ATOM 10 C TYR A 596 -5.064 29.701 51.797 1.00 40.59 C ANISOU 10 C TYR A 596 5339 4811 5272 302 -120 -501 C ATOM 11 O TYR A 596 -4.443 30.614 52.351 1.00 41.28 O ANISOU 11 O TYR A 596 5215 5031 5439 359 -217 -887 O ATOM 12 CB TYR A 596 -3.745 27.572 51.970 1.00 36.58 C ANISOU 12 CB TYR A 596 5175 4445 4279 239 19 423 C ATOM 13 CG TYR A 596 -4.700 27.070 53.019 1.00 36.85 C ANISOU 13 CG TYR A 596 4974 4990 4036 64 204 589 C ATOM 14 CD1 TYR A 596 -5.699 26.165 52.697 1.00 39.91 C ANISOU 14 CD1 TYR A 596 5316 5130 4717 -18 301 839 C ATOM 15 CD2 TYR A 596 -4.588 27.483 54.340 1.00 45.61 C ANISOU 15 CD2 TYR A 596 5785 7026 4521 -100 289 464 C ATOM 16 CE1 TYR A 596 -6.585 25.694 53.657 1.00 43.36 C ANISOU 16 CE1 TYR A 596 5459 6154 4863 -277 466 1131 C ATOM 17 CE2 TYR A 596 -5.470 27.015 55.322 1.00 49.82 C ANISOU 17 CE2 TYR A 596 5947 8429 4554 -428 481 678 C ATOM 18 CZ TYR A 596 -6.462 26.117 54.973 1.00 52.27 C ANISOU 18 CZ TYR A 596 6261 8403 5196 -525 561 1106 C ATOM 19 OH TYR A 596 -7.335 25.644 55.942 1.00 55.61 O ANISOU 19 OH TYR A 596 6242 9795 5091 -943 744 1460 O ATOM 20 N VAL A 597 -6.389 29.589 51.845 1.00 41.98 N ANISOU 20 N VAL A 597 5344 4987 5620 250 -12 -711 N ATOM 21 CA VAL A 597 -7.200 30.474 52.666 1.00 49.05 C ANISOU 21 CA VAL A 597 5715 6146 6777 240 45 -1528 C ATOM 22 C VAL A 597 -7.916 29.632 53.721 1.00 53.60 C ANISOU 22 C VAL A 597 6106 7608 6651 18 434 -1584 C ATOM 23 O VAL A 597 -8.574 28.641 53.389 1.00 50.51 O ANISOU 23 O VAL A 597 5909 7096 6185 -67 549 -1067 O ATOM 24 CB VAL A 597 -8.207 31.260 51.791 1.00 50.96 C ANISOU 24 CB VAL A 597 5703 5641 8019 309 -246 -1765 C ATOM 25 CG1 VAL A 597 -9.248 31.980 52.658 1.00 58.08 C ANISOU 25 CG1 VAL A 597 5878 6747 9442 303 -146 -2864 C ATOM 26 CG2 VAL A 597 -7.462 32.267 50.900 1.00 52.05 C ANISOU 26 CG2 VAL A 597 5778 5097 8902 369 -750 -1464 C ATOM 27 N ASP A 598 -7.778 30.015 54.990 1.00 60.48 N ANISOU 27 N ASP A 598 6480 9513 6989 -151 622 -2202 N ATOM 28 CA ASP A 598 -8.439 29.278 56.062 1.00 68.96 C ANISOU 28 CA ASP A 598 7192 11847 7162 -551 970 -2107 C ATOM 29 C ASP A 598 -9.953 29.482 56.030 1.00 73.45 C ANISOU 29 C ASP A 598 7358 12450 8101 -622 1152 -2812 C ATOM 30 O ASP A 598 -10.419 30.619 56.040 1.00 76.46 O ANISOU 30 O ASP A 598 7209 12622 9221 -480 1098 -4058 O ATOM 31 CB ASP A 598 -7.907 29.692 57.430 1.00 76.99 C ANISOU 31 CB ASP A 598 7578 14428 7245 -858 1134 -2707 C ATOM 32 CG ASP A 598 -8.019 28.580 58.451 1.00 84.63 C ANISOU 32 CG ASP A 598 8293 16921 6941 -1442 1335 -1740 C ATOM 33 OD1 ASP A 598 -7.113 27.719 58.492 1.00 83.75 O ANISOU 33 OD1 ASP A 598 8539 16735 6547 -1526 1128 -411 O ATOM 34 OD2 ASP A 598 -9.011 28.566 59.206 1.00 90.88 O ANISOU 34 OD2 ASP A 598 8412 19006 7112 -1871 1649 -2245 O ATOM 35 N PRO A 599 -10.723 28.378 55.971 1.00 75.57 N ANISOU 35 N PRO A 599 7770 12842 8100 -836 1316 -2039 N ATOM 36 CA PRO A 599 -12.180 28.473 56.065 1.00 80.33 C ANISOU 36 CA PRO A 599 7938 13653 8930 -964 1538 -2693 C ATOM 37 C PRO A 599 -12.640 28.688 57.506 1.00 92.18 C ANISOU 37 C PRO A 599 8518 17064 9442 -1484 1938 -3512 C ATOM 38 O PRO A 599 -13.696 29.282 57.734 1.00 97.79 O ANISOU 38 O PRO A 599 8569 18108 10479 -1551 2138 -4767 O ATOM 39 CB PRO A 599 -12.662 27.099 55.559 1.00 77.51 C ANISOU 39 CB PRO A 599 7999 12837 8614 -1064 1563 -1470 C ATOM 40 CG PRO A 599 -11.427 26.388 55.037 1.00 72.38 C ANISOU 40 CG PRO A 599 7936 11508 8055 -909 1300 -398 C ATOM 41 CD PRO A 599 -10.285 26.984 55.781 1.00 73.92 C ANISOU 41 CD PRO A 599 8008 12422 7655 -957 1250 -577 C ATOM 42 N HIS A 600 -11.842 28.212 58.459 1.00 98.39 N ANISOU 42 N HIS A 600 9137 19223 9024 -1905 2024 -2840 N ATOM 43 CA HIS A 600 -12.224 28.180 59.872 1.00112.57 C ANISOU 43 CA HIS A 600 9942 23407 9423 -2638 2409 -3288 C ATOM 44 C HIS A 600 -11.790 29.452 60.598 1.00118.85 C ANISOU 44 C HIS A 600 9925 25288 9946 -2662 2530 -5141 C ATOM 45 O HIS A 600 -11.200 30.351 59.995 1.00113.52 O ANISOU 45 O HIS A 600 9492 23255 10384 -2077 2259 -5904 O ATOM 46 CB HIS A 600 -11.629 26.940 60.562 1.00117.94 C ANISOU 46 CB HIS A 600 10654 25235 8924 -3241 2323 -1309 C ATOM 47 CG HIS A 600 -11.861 25.656 59.819 1.00115.02 C ANISOU 47 CG HIS A 600 10929 23481 9294 -3157 2094 444 C ATOM 48 ND1 HIS A 600 -12.861 24.768 60.156 1.00121.78 N ANISOU 48 ND1 HIS A 600 11399 25002 9870 -3699 2246 1325 N ATOM 49 CD2 HIS A 600 -11.219 25.111 58.756 1.00105.78 C ANISOU 49 CD2 HIS A 600 10595 20355 9241 -2628 1727 1310 C ATOM 50 CE1 HIS A 600 -12.826 23.733 59.334 1.00116.64 C ANISOU 50 CE1 HIS A 600 11309 22684 10324 -3453 1947 2630 C ATOM 51 NE2 HIS A 600 -11.839 23.917 58.474 1.00107.20 N ANISOU 51 NE2 HIS A 600 10820 19957 9954 -2810 1651 2527 N ATOM 52 N VAL A 609 -16.989 23.544 50.945 1.00 63.19 N ANISOU 52 N VAL A 609 6863 7060 10085 -620 1383 -493 N ATOM 53 CA VAL A 609 -17.574 24.811 50.508 1.00 59.49 C ANISOU 53 CA VAL A 609 6355 6492 9757 -446 1236 -1270 C ATOM 54 C VAL A 609 -17.687 24.841 48.984 1.00 55.00 C ANISOU 54 C VAL A 609 5960 5297 9641 -263 896 -1347 C ATOM 55 O VAL A 609 -16.889 24.218 48.280 1.00 52.43 O ANISOU 55 O VAL A 609 5820 4808 9291 -229 797 -1087 O ATOM 56 CB VAL A 609 -16.773 26.053 51.036 1.00 59.23 C ANISOU 56 CB VAL A 609 6295 6776 9432 -368 1125 -1619 C ATOM 57 CG1 VAL A 609 -15.527 26.326 50.190 1.00 53.74 C ANISOU 57 CG1 VAL A 609 5990 5686 8743 -185 788 -1300 C ATOM 58 CG2 VAL A 609 -17.659 27.284 51.080 1.00 63.37 C ANISOU 58 CG2 VAL A 609 6375 7183 10518 -282 996 -2513 C ATOM 59 N HIS A 610 -18.676 25.573 48.479 1.00 53.66 N ANISOU 59 N HIS A 610 5583 4915 9892 -206 691 -1755 N ATOM 60 CA HIS A 610 -18.857 25.674 47.042 1.00 51.37 C ANISOU 60 CA HIS A 610 5307 4376 9835 -178 295 -1675 C ATOM 61 C HIS A 610 -17.838 26.578 46.357 1.00 50.12 C ANISOU 61 C HIS A 610 5253 4274 9517 -176 -149 -1353 C ATOM 62 O HIS A 610 -17.707 26.546 45.133 1.00 51.99 O ANISOU 62 O HIS A 610 5432 4721 9599 -313 -471 -1111 O ATOM 63 CB HIS A 610 -20.307 26.008 46.676 1.00 54.47 C ANISOU 63 CB HIS A 610 5352 4532 10812 -184 128 -1993 C ATOM 64 CG HIS A 610 -21.242 24.852 46.859 1.00 55.43 C ANISOU 64 CG HIS A 610 5370 4632 11059 -246 510 -2192 C ATOM 65 ND1 HIS A 610 -20.993 23.604 46.326 1.00 55.02 N ANISOU 65 ND1 HIS A 610 5383 4573 10950 -298 650 -2084 N ATOM 66 CD2 HIS A 610 -22.417 24.748 47.524 1.00 59.23 C ANISOU 66 CD2 HIS A 610 5557 5079 11869 -293 769 -2556 C ATOM 67 CE1 HIS A 610 -21.975 22.783 46.653 1.00 54.31 C ANISOU 67 CE1 HIS A 610 5066 4316 11252 -362 932 -2236 C ATOM 68 NE2 HIS A 610 -22.855 23.452 47.376 1.00 60.40 N ANISOU 68 NE2 HIS A 610 5663 5151 12136 -384 1031 -2460 N ATOM 69 N GLU A 611 -17.087 27.356 47.138 1.00 47.09 N ANISOU 69 N GLU A 611 4917 3876 9098 -99 -165 -1352 N ATOM 70 CA GLU A 611 -15.982 28.105 46.567 1.00 46.35 C ANISOU 70 CA GLU A 611 4906 3816 8889 -131 -558 -937 C ATOM 71 C GLU A 611 -14.948 27.154 45.953 1.00 43.49 C ANISOU 71 C GLU A 611 4843 3858 7824 -225 -415 -688 C ATOM 72 O GLU A 611 -14.443 27.419 44.864 1.00 45.96 O ANISOU 72 O GLU A 611 5079 4515 7869 -418 -750 -357 O ATOM 73 CB GLU A 611 -15.322 29.035 47.592 1.00 47.82 C ANISOU 73 CB GLU A 611 5010 3883 9278 -10 -563 -1155 C ATOM 74 CG GLU A 611 -14.238 29.938 46.977 1.00 51.52 C ANISOU 74 CG GLU A 611 5464 4248 9862 -66 -1047 -639 C ATOM 75 CD GLU A 611 -13.707 30.996 47.931 1.00 53.26 C ANISOU 75 CD GLU A 611 5414 4201 10622 75 -1134 -1037 C ATOM 76 OE1 GLU A 611 -14.251 31.124 49.048 1.00 59.72 O ANISOU 76 OE1 GLU A 611 5944 5081 11666 181 -821 -1879 O ATOM 77 OE2 GLU A 611 -12.745 31.707 47.558 1.00 59.21 O ANISOU 77 OE2 GLU A 611 6124 4806 11566 28 -1510 -591 O ATOM 78 N PHE A 612 -14.669 26.039 46.631 1.00 37.95 N ANISOU 78 N PHE A 612 4313 3180 6926 -158 33 -837 N ATOM 79 CA PHE A 612 -13.591 25.131 46.212 1.00 35.40 C ANISOU 79 CA PHE A 612 4084 3029 6340 -196 140 -804 C ATOM 80 C PHE A 612 -14.019 23.707 45.913 1.00 34.56 C ANISOU 80 C PHE A 612 3753 2773 6606 -224 365 -1109 C ATOM 81 O PHE A 612 -13.164 22.858 45.635 1.00 38.11 O ANISOU 81 O PHE A 612 4063 3197 7221 -231 437 -1301 O ATOM 82 CB PHE A 612 -12.501 25.084 47.278 1.00 34.48 C ANISOU 82 CB PHE A 612 4178 2877 6047 -103 292 -576 C ATOM 83 CG PHE A 612 -11.882 26.415 47.555 1.00 33.66 C ANISOU 83 CG PHE A 612 4184 2875 5729 -60 75 -456 C ATOM 84 CD1 PHE A 612 -11.004 26.993 46.632 1.00 34.89 C ANISOU 84 CD1 PHE A 612 4362 3217 5679 -149 -223 -277 C ATOM 85 CD2 PHE A 612 -12.164 27.090 48.742 1.00 36.66 C ANISOU 85 CD2 PHE A 612 4488 3279 6160 7 167 -606 C ATOM 86 CE1 PHE A 612 -10.428 28.248 46.884 1.00 36.23 C ANISOU 86 CE1 PHE A 612 4522 3314 5931 -124 -495 -88 C ATOM 87 CE2 PHE A 612 -11.583 28.349 49.011 1.00 37.17 C ANISOU 87 CE2 PHE A 612 4468 3313 6340 71 -67 -718 C ATOM 88 CZ PHE A 612 -10.712 28.917 48.082 1.00 36.73 C ANISOU 88 CZ PHE A 612 4483 3162 6311 30 -426 -376 C ATOM 89 N ALA A 613 -15.313 23.417 45.991 1.00 37.21 N ANISOU 89 N ALA A 613 4065 4184 5889 263 -579 -594 N ATOM 90 CA ALA A 613 -15.775 22.060 45.699 1.00 35.58 C ANISOU 90 CA ALA A 613 3901 4164 5454 252 -440 -487 C ATOM 91 C ALA A 613 -16.874 22.101 44.650 1.00 34.33 C ANISOU 91 C ALA A 613 3878 3990 5174 205 -400 -335 C ATOM 92 O ALA A 613 -17.761 22.957 44.711 1.00 35.94 O ANISOU 92 O ALA A 613 4124 4133 5400 287 -540 -369 O ATOM 93 CB ALA A 613 -16.266 21.370 46.991 1.00 32.29 C ANISOU 93 CB ALA A 613 3463 3944 4861 428 -501 -584 C ATOM 94 N LYS A 614 -16.804 21.209 43.669 1.00 30.84 N ANISOU 94 N LYS A 614 3507 3583 4630 92 -250 -201 N ATOM 95 CA LYS A 614 -17.889 21.049 42.708 1.00 31.65 C ANISOU 95 CA LYS A 614 3754 3672 4600 87 -266 -85 C ATOM 96 C LYS A 614 -19.064 20.326 43.350 1.00 26.94 C ANISOU 96 C LYS A 614 3070 3250 3916 225 -308 -141 C ATOM 97 O LYS A 614 -18.860 19.322 44.036 1.00 23.53 O ANISOU 97 O LYS A 614 2548 2971 3421 246 -221 -165 O ATOM 98 CB LYS A 614 -17.415 20.203 41.524 1.00 32.56 C ANISOU 98 CB LYS A 614 3974 3786 4610 -55 -94 39 C ATOM 99 CG LYS A 614 -18.479 19.975 40.429 1.00 38.40 C ANISOU 99 CG LYS A 614 4909 4485 5196 -39 -161 145 C ATOM 100 CD LYS A 614 -17.911 19.142 39.272 1.00 37.13 C ANISOU 100 CD LYS A 614 4878 4334 4895 -167 18 237 C ATOM 101 CE LYS A 614 -18.920 18.886 38.131 1.00 41.08 C ANISOU 101 CE LYS A 614 5619 4771 5218 -124 -100 321 C ATOM 102 NZ LYS A 614 -20.179 18.251 38.653 1.00 41.66 N ANISOU 102 NZ LYS A 614 5532 4948 5348 42 -267 240 N ATOM 103 N GLU A 615 -20.280 20.810 43.093 1.00 25.44 N ANISOU 103 N GLU A 615 2910 3011 3743 308 -443 -171 N ATOM 104 CA GLU A 615 -21.495 20.084 43.502 1.00 24.81 C ANISOU 104 CA GLU A 615 2709 3077 3642 399 -431 -246 C ATOM 105 C GLU A 615 -21.743 19.004 42.459 1.00 26.29 C ANISOU 105 C GLU A 615 2964 3271 3753 335 -382 -128 C ATOM 106 O GLU A 615 -21.998 19.303 41.288 1.00 27.46 O ANISOU 106 O GLU A 615 3278 3268 3887 321 -502 -63 O ATOM 107 CB GLU A 615 -22.714 21.004 43.633 1.00 25.66 C ANISOU 107 CB GLU A 615 2750 3115 3885 530 -615 -402 C ATOM 108 CG GLU A 615 -24.018 20.300 44.088 1.00 29.43 C ANISOU 108 CG GLU A 615 3029 3736 4417 600 -548 -536 C ATOM 109 CD GLU A 615 -24.036 19.867 45.564 1.00 27.96 C ANISOU 109 CD GLU A 615 2704 3769 4149 616 -330 -632 C ATOM 110 OE1 GLU A 615 -23.258 20.403 46.387 1.00 29.29 O ANISOU 110 OE1 GLU A 615 2910 3968 4249 645 -324 -670 O ATOM 111 OE2 GLU A 615 -24.851 18.984 45.912 1.00 29.77 O ANISOU 111 OE2 GLU A 615 2807 4125 4378 594 -166 -674 O ATOM 112 N LEU A 616 -21.652 17.752 42.880 1.00 22.42 N ANISOU 112 N LEU A 616 2385 2932 3200 304 -236 -102 N ATOM 113 CA LEU A 616 -21.891 16.641 41.961 1.00 21.75 C ANISOU 113 CA LEU A 616 2339 2852 3074 259 -211 -20 C ATOM 114 C LEU A 616 -23.369 16.275 41.935 1.00 24.59 C ANISOU 114 C LEU A 616 2575 3226 3541 328 -274 -104 C ATOM 115 O LEU A 616 -24.076 16.422 42.936 1.00 25.36 O ANISOU 115 O LEU A 616 2510 3408 3719 372 -217 -219 O ATOM 116 CB LEU A 616 -21.068 15.425 42.396 1.00 19.06 C ANISOU 116 CB LEU A 616 1958 2621 2665 194 -70 35 C ATOM 117 CG LEU A 616 -19.564 15.695 42.447 1.00 20.23 C ANISOU 117 CG LEU A 616 2152 2740 2794 135 -20 48 C ATOM 118 CD1 LEU A 616 -18.870 14.482 43.089 1.00 21.33 C ANISOU 118 CD1 LEU A 616 2233 2961 2912 120 35 49 C ATOM 119 CD2 LEU A 616 -18.993 16.020 41.082 1.00 21.23 C ANISOU 119 CD2 LEU A 616 2415 2755 2894 50 5 104 C ATOM 120 N ASP A 617 -23.823 15.795 40.784 1.00 24.60 N ANISOU 120 N ASP A 617 2647 3141 3557 336 -383 -76 N ATOM 121 CA ASP A 617 -25.164 15.241 40.629 1.00 28.22 C ANISOU 121 CA ASP A 617 2946 3584 4191 395 -464 -184 C ATOM 122 C ASP A 617 -25.053 13.762 41.040 1.00 29.60 C ANISOU 122 C ASP A 617 3010 3877 4361 308 -281 -123 C ATOM 123 O ASP A 617 -24.262 13.004 40.459 1.00 27.50 O ANISOU 123 O ASP A 617 2858 3610 3980 258 -263 -17 O ATOM 124 CB ASP A 617 -25.560 15.375 39.165 1.00 28.90 C ANISOU 124 CB ASP A 617 3217 3488 4277 466 -729 -187 C ATOM 125 CG ASP A 617 -26.989 14.917 38.888 1.00 38.07 C ANISOU 125 CG ASP A 617 4188 4577 5702 561 -901 -359 C ATOM 126 OD1 ASP A 617 -27.508 14.038 39.619 1.00 37.29 O ANISOU 126 OD1 ASP A 617 3816 4588 5765 509 -729 -420 O ATOM 127 OD2 ASP A 617 -27.591 15.451 37.930 1.00 41.25 O ANISOU 127 OD2 ASP A 617 4728 4784 6161 683 -1222 -440 O ATOM 128 N ALA A 618 -25.836 13.344 42.036 1.00 30.46 N ANISOU 128 N ALA A 618 2905 4073 4594 281 -135 -197 N ATOM 129 CA ALA A 618 -25.774 11.958 42.544 1.00 31.12 C ANISOU 129 CA ALA A 618 2930 4228 4668 174 38 -108 C ATOM 130 C ALA A 618 -26.115 10.881 41.505 1.00 29.76 C ANISOU 130 C ALA A 618 2730 3961 4616 164 -79 -92 C ATOM 131 O ALA A 618 -25.771 9.711 41.693 1.00 29.44 O ANISOU 131 O ALA A 618 2698 3937 4553 81 1 8 O ATOM 132 CB ALA A 618 -26.677 11.804 43.776 1.00 35.89 C ANISOU 132 CB ALA A 618 3350 4922 5367 112 270 -188 C ATOM 133 N THR A 619 -26.817 11.260 40.434 1.00 29.04 N ANISOU 133 N THR A 619 2624 3747 4663 266 -311 -206 N ATOM 134 CA THR A 619 -27.088 10.305 39.342 1.00 29.04 C ANISOU 134 CA THR A 619 2638 3641 4756 296 -483 -220 C ATOM 135 C THR A 619 -25.776 9.841 38.696 1.00 27.90 C ANISOU 135 C THR A 619 2732 3517 4350 274 -489 -83 C ATOM 136 O THR A 619 -25.734 8.791 38.036 1.00 27.46 O ANISOU 136 O THR A 619 2686 3415 4331 278 -571 -83 O ATOM 137 CB THR A 619 -28.040 10.856 38.245 1.00 32.57 C ANISOU 137 CB THR A 619 3097 3915 5362 450 -813 -389 C ATOM 138 OG1 THR A 619 -27.407 11.900 37.502 1.00 34.20 O ANISOU 138 OG1 THR A 619 3621 4060 5315 526 -965 -334 O ATOM 139 CG2 THR A 619 -29.348 11.369 38.842 1.00 33.51 C ANISOU 139 CG2 THR A 619 2912 3996 5823 492 -830 -605 C ATOM 140 N ASN A 620 -24.707 10.618 38.904 1.00 21.54 N ANISOU 140 N ASN A 620 2086 2774 3324 250 -399 -2 N ATOM 141 CA ASN A 620 -23.398 10.293 38.347 1.00 19.73 C ANISOU 141 CA ASN A 620 2027 2570 2899 213 -352 74 C ATOM 142 C ASN A 620 -22.514 9.430 39.263 1.00 20.15 C ANISOU 142 C ASN A 620 2002 2713 2941 132 -202 134 C ATOM 143 O ASN A 620 -21.391 9.082 38.878 1.00 21.10 O ANISOU 143 O ASN A 620 2196 2851 2970 109 -168 140 O ATOM 144 CB ASN A 620 -22.635 11.583 37.998 1.00 17.98 C ANISOU 144 CB ASN A 620 2002 2327 2503 207 -327 107 C ATOM 145 CG ASN A 620 -23.209 12.290 36.786 1.00 24.14 C ANISOU 145 CG ASN A 620 3001 2964 3205 286 -526 83 C ATOM 146 OD1 ASN A 620 -23.313 13.522 36.745 1.00 27.39 O ANISOU 146 OD1 ASN A 620 3535 3295 3575 306 -592 95 O ATOM 147 ND2 ASN A 620 -23.576 11.518 35.783 1.00 21.36 N ANISOU 147 ND2 ASN A 620 2736 2553 2828 344 -664 42 N ATOM 148 N ILE A 621 -23.010 9.152 40.460 1.00 20.82 N ANISOU 148 N ILE A 621 1959 2840 3112 92 -116 160 N ATOM 149 CA ILE A 621 -22.255 8.390 41.472 1.00 22.94 C ANISOU 149 CA ILE A 621 2232 3149 3334 31 -31 234 C ATOM 150 C ILE A 621 -22.887 7.001 41.630 1.00 25.03 C ANISOU 150 C ILE A 621 2421 3357 3733 -26 -43 278 C ATOM 151 O ILE A 621 -24.091 6.879 41.777 1.00 25.10 O ANISOU 151 O ILE A 621 2308 3341 3887 -59 3 259 O ATOM 152 CB ILE A 621 -22.234 9.141 42.835 1.00 24.45 C ANISOU 152 CB ILE A 621 2438 3413 3440 17 87 254 C ATOM 153 CG1 ILE A 621 -21.475 10.463 42.692 1.00 21.50 C ANISOU 153 CG1 ILE A 621 2127 3059 2984 68 66 203 C ATOM 154 CG2 ILE A 621 -21.567 8.279 43.930 1.00 23.69 C ANISOU 154 CG2 ILE A 621 2428 3317 3254 -27 114 338 C ATOM 155 CD1 ILE A 621 -21.865 11.489 43.726 1.00 25.20 C ANISOU 155 CD1 ILE A 621 2578 3583 3413 96 132 162 C ATOM 156 N SER A 622 -22.064 5.957 41.573 1.00 21.64 N ANISOU 156 N SER A 622 2041 2884 3299 -40 -114 313 N ATOM 157 CA SER A 622 -22.514 4.634 41.936 1.00 24.76 C ANISOU 157 CA SER A 622 2403 3186 3817 -113 -139 387 C ATOM 158 C SER A 622 -21.601 4.060 43.004 1.00 27.76 C ANISOU 158 C SER A 622 2927 3530 4089 -147 -159 483 C ATOM 159 O SER A 622 -20.382 4.271 42.978 1.00 27.49 O ANISOU 159 O SER A 622 2955 3514 3978 -77 -248 424 O ATOM 160 CB SER A 622 -22.550 3.730 40.713 1.00 29.15 C ANISOU 160 CB SER A 622 2898 3656 4521 -68 -310 310 C ATOM 161 OG SER A 622 -21.264 3.612 40.163 1.00 34.37 O ANISOU 161 OG SER A 622 3625 4336 5097 2 -398 234 O ATOM 162 N ILE A 623 -22.201 3.369 43.961 1.00 28.18 N ANISOU 162 N ILE A 623 3046 3514 4146 -259 -79 619 N ATOM 163 CA ILE A 623 -21.436 2.762 45.050 1.00 30.61 C ANISOU 163 CA ILE A 623 3585 3738 4308 -286 -150 738 C ATOM 164 C ILE A 623 -21.243 1.278 44.733 1.00 35.37 C ANISOU 164 C ILE A 623 4215 4151 5072 -315 -351 786 C ATOM 165 O ILE A 623 -22.220 0.594 44.391 1.00 34.30 O ANISOU 165 O ILE A 623 3975 3933 5123 -413 -300 832 O ATOM 166 CB ILE A 623 -22.123 3.000 46.418 1.00 31.91 C ANISOU 166 CB ILE A 623 3912 3929 4282 -403 84 880 C ATOM 167 CG1 ILE A 623 -22.077 4.508 46.762 1.00 32.15 C ANISOU 167 CG1 ILE A 623 3917 4138 4159 -326 211 781 C ATOM 168 CG2 ILE A 623 -21.478 2.132 47.521 1.00 33.90 C ANISOU 168 CG2 ILE A 623 4508 4029 4344 -441 -36 1044 C ATOM 169 CD1 ILE A 623 -22.929 4.920 47.961 1.00 33.97 C ANISOU 169 CD1 ILE A 623 4251 4445 4209 -427 499 848 C ATOM 170 N ASP A 624 -19.989 0.817 44.830 1.00 31.02 N ANISOU 170 N ASP A 624 4435 3632 3720 -433 139 293 N ATOM 171 CA ASP A 624 -19.555 -0.539 44.456 1.00 35.59 C ANISOU 171 CA ASP A 624 4855 4143 4523 -594 310 269 C ATOM 172 C ASP A 624 -19.252 -1.449 45.657 1.00 37.93 C ANISOU 172 C ASP A 624 4951 4390 5071 -700 384 395 C ATOM 173 O ASP A 624 -19.400 -2.677 45.568 1.00 39.47 O ANISOU 173 O ASP A 624 5272 4385 5340 -795 394 348 O ATOM 174 CB ASP A 624 -18.235 -0.464 43.650 1.00 39.61 C ANISOU 174 CB ASP A 624 5588 4530 4931 -730 615 182 C ATOM 175 CG ASP A 624 -18.411 0.123 42.257 1.00 47.85 C ANISOU 175 CG ASP A 624 7381 5341 5459 -784 663 85 C ATOM 176 OD1 ASP A 624 -19.548 0.493 41.891 1.00 56.67 O ANISOU 176 OD1 ASP A 624 8860 6367 6305 -429 197 61 O ATOM 177 OD2 ASP A 624 -17.400 0.216 41.517 1.00 55.81 O ANISOU 177 OD2 ASP A 624 8692 6251 6261 -1169 1148 -127 O ATOM 178 N LYS A 625 -18.765 -0.849 46.745 1.00 35.87 N ANISOU 178 N LYS A 625 4635 4178 4818 -646 383 535 N ATOM 179 CA LYS A 625 -18.121 -1.571 47.842 1.00 39.36 C ANISOU 179 CA LYS A 625 5256 4402 5295 -506 258 611 C ATOM 180 C LYS A 625 -18.171 -0.714 49.093 1.00 37.76 C ANISOU 180 C LYS A 625 5035 4308 5002 -498 231 759 C ATOM 181 O LYS A 625 -17.881 0.476 49.039 1.00 34.90 O ANISOU 181 O LYS A 625 4391 4198 4674 -476 288 716 O ATOM 182 CB LYS A 625 -16.651 -1.843 47.463 1.00 42.09 C ANISOU 182 CB LYS A 625 5397 4777 5818 -141 110 249 C ATOM 183 CG LYS A 625 -15.821 -2.628 48.477 1.00 50.03 C ANISOU 183 CG LYS A 625 6689 5512 6807 441 -405 56 C ATOM 184 CD LYS A 625 -14.382 -2.835 47.976 1.00 54.73 C ANISOU 184 CD LYS A 625 6667 6409 7719 933 -642 -785 C ATOM 185 CE LYS A 625 -14.338 -3.680 46.697 1.00 61.09 C ANISOU 185 CE LYS A 625 7421 7162 8626 883 -521 -1024 C ATOM 186 NZ LYS A 625 -12.946 -4.104 46.348 1.00 71.59 N ANISOU 186 NZ LYS A 625 8064 8847 10287 1454 -818 -2136 N ATOM 187 N VAL A 626 -18.523 -1.313 50.224 1.00 38.50 N ANISOU 187 N VAL A 626 5652 4109 4868 -599 199 918 N ATOM 188 CA VAL A 626 -18.503 -0.586 51.486 1.00 40.31 C ANISOU 188 CA VAL A 626 5978 4401 4938 -577 166 1039 C ATOM 189 C VAL A 626 -17.227 -0.956 52.240 1.00 45.57 C ANISOU 189 C VAL A 626 7058 4764 5493 57 -358 966 C ATOM 190 O VAL A 626 -16.913 -2.135 52.394 1.00 50.42 O ANISOU 190 O VAL A 626 8493 4815 5849 362 -694 945 O ATOM 191 CB VAL A 626 -19.760 -0.882 52.339 1.00 45.40 C ANISOU 191 CB VAL A 626 7075 4930 5244 -1225 576 1087 C ATOM 192 CG1 VAL A 626 -19.695 -0.166 53.674 1.00 45.63 C ANISOU 192 CG1 VAL A 626 7310 4996 5032 -1215 569 1196 C ATOM 193 CG2 VAL A 626 -21.022 -0.482 51.571 1.00 43.37 C ANISOU 193 CG2 VAL A 626 6057 5200 5220 -1629 897 710 C ATOM 194 N VAL A 627 -16.493 0.061 52.677 1.00 45.98 N ANISOU 194 N VAL A 627 6596 5165 5710 339 -520 784 N ATOM 195 CA VAL A 627 -15.234 -0.104 53.394 1.00 54.10 C ANISOU 195 CA VAL A 627 7688 6132 6735 1105 -1169 358 C ATOM 196 C VAL A 627 -15.383 0.449 54.812 1.00 57.04 C ANISOU 196 C VAL A 627 8502 6404 6768 1196 -1334 557 C ATOM 197 O VAL A 627 -14.802 1.488 55.150 1.00 57.39 O ANISOU 197 O VAL A 627 7854 6901 7052 1317 -1389 250 O ATOM 198 CB VAL A 627 -14.069 0.644 52.683 1.00 54.37 C ANISOU 198 CB VAL A 627 6540 6815 7303 1220 -1114 -403 C ATOM 199 CG1 VAL A 627 -12.717 0.220 53.268 1.00 63.26 C ANISOU 199 CG1 VAL A 627 7400 8069 8569 2192 -1944 -1340 C ATOM 200 CG2 VAL A 627 -14.093 0.405 51.173 1.00 53.71 C ANISOU 200 CG2 VAL A 627 6084 6874 7448 828 -668 -544 C ATOM 201 N GLY A 628 -16.183 -0.230 55.633 1.00 61.58 N ANISOU 201 N GLY A 628 10331 6355 6714 975 -1286 1009 N ATOM 202 CA GLY A 628 -16.357 0.139 57.051 1.00 63.78 C ANISOU 202 CA GLY A 628 11361 6401 6470 992 -1391 1195 C ATOM 203 C GLY A 628 -16.781 1.576 57.362 1.00 57.46 C ANISOU 203 C GLY A 628 9630 6257 5945 571 -949 1236 C ATOM 204 O GLY A 628 -17.259 2.315 56.487 1.00 52.56 O ANISOU 204 O GLY A 628 8032 6152 5786 157 -496 1211 O ATOM 205 N ALA A 629 -16.602 1.971 58.620 1.00 58.43 N ANISOU 205 N ALA A 629 10272 6253 5677 792 -1197 1264 N ATOM 206 CA ALA A 629 -17.024 3.286 59.076 1.00 53.94 C ANISOU 206 CA ALA A 629 9009 6209 5278 454 -843 1277 C ATOM 207 C ALA A 629 -15.855 4.269 59.234 1.00 51.82 C ANISOU 207 C ALA A 629 7899 6366 5422 1034 -1311 853 C ATOM 208 O ALA A 629 -14.713 3.867 59.452 1.00 57.15 O ANISOU 208 O ALA A 629 8631 6957 6125 1810 -2032 392 O ATOM 209 CB ALA A 629 -17.824 3.170 60.363 1.00 59.04 C ANISOU 209 CB ALA A 629 10734 6517 5182 6 -534 1506 C ATOM 210 N GLY A 630 -16.159 5.556 59.084 1.00 45.36 N ANISOU 210 N GLY A 630 6310 6010 4914 669 -927 827 N ATOM 211 CA GLY A 630 -15.200 6.638 59.302 1.00 43.26 C ANISOU 211 CA GLY A 630 5364 6110 4961 877 -1112 368 C ATOM 212 C GLY A 630 -15.644 7.458 60.505 1.00 44.17 C ANISOU 212 C GLY A 630 5708 6281 4794 827 -1098 515 C ATOM 213 O GLY A 630 -16.586 7.075 61.209 1.00 43.26 O ANISOU 213 O GLY A 630 6292 5940 4207 631 -932 877 O ATOM 214 N GLU A 631 -14.977 8.590 60.732 1.00 43.13 N ANISOU 214 N GLU A 631 5012 6457 4917 852 -1145 121 N ATOM 215 CA GLU A 631 -15.298 9.481 61.847 1.00 43.98 C ANISOU 215 CA GLU A 631 5259 6648 4802 848 -1168 182 C ATOM 216 C GLU A 631 -16.736 9.979 61.783 1.00 40.70 C ANISOU 216 C GLU A 631 4987 6243 4233 423 -700 568 C ATOM 217 O GLU A 631 -17.425 10.051 62.810 1.00 39.60 O ANISOU 217 O GLU A 631 5200 6119 3725 363 -626 674 O ATOM 218 CB GLU A 631 -14.335 10.678 61.862 1.00 46.34 C ANISOU 218 CB GLU A 631 4897 7255 5453 768 -1168 -415 C ATOM 219 CG GLU A 631 -14.594 11.707 62.973 1.00 46.54 C ANISOU 219 CG GLU A 631 5032 7363 5287 785 -1219 -406 C ATOM 220 CD GLU A 631 -13.434 12.678 63.185 1.00 52.46 C ANISOU 220 CD GLU A 631 5177 8406 6351 691 -1272 -1193 C ATOM 221 OE1 GLU A 631 -12.399 12.573 62.483 1.00 60.74 O ANISOU 221 OE1 GLU A 631 5603 9688 7786 504 -1170 -1922 O ATOM 222 OE2 GLU A 631 -13.555 13.552 64.068 1.00 58.77 O ANISOU 222 OE2 GLU A 631 6052 9261 7015 709 -1337 -1244 O ATOM 223 N PHE A 632 -17.185 10.318 60.574 1.00 37.16 N ANISOU 223 N PHE A 632 4297 5804 4017 180 -434 604 N ATOM 224 CA PHE A 632 -18.453 11.023 60.402 1.00 35.44 C ANISOU 224 CA PHE A 632 4051 5684 3729 94 -281 596 C ATOM 225 C PHE A 632 -19.590 10.222 59.779 1.00 35.28 C ANISOU 225 C PHE A 632 3956 5753 3695 -41 -103 573 C ATOM 226 O PHE A 632 -20.693 10.730 59.657 1.00 35.23 O ANISOU 226 O PHE A 632 3707 5990 3690 45 -114 222 O ATOM 227 CB PHE A 632 -18.213 12.300 59.588 1.00 37.56 C ANISOU 227 CB PHE A 632 4450 5753 4068 117 -334 464 C ATOM 228 CG PHE A 632 -17.313 13.278 60.287 1.00 38.65 C ANISOU 228 CG PHE A 632 4623 5859 4204 43 -356 287 C ATOM 229 CD1 PHE A 632 -17.797 14.054 61.336 1.00 40.99 C ANISOU 229 CD1 PHE A 632 4930 6285 4358 230 -498 196 C ATOM 230 CD2 PHE A 632 -15.972 13.394 59.920 1.00 41.26 C ANISOU 230 CD2 PHE A 632 4841 6129 4706 -289 -173 6 C ATOM 231 CE1 PHE A 632 -16.968 14.942 62.002 1.00 44.91 C ANISOU 231 CE1 PHE A 632 5443 6760 4862 138 -523 -24 C ATOM 232 CE2 PHE A 632 -15.132 14.288 60.579 1.00 43.22 C ANISOU 232 CE2 PHE A 632 4966 6453 5005 -483 -119 -407 C ATOM 233 CZ PHE A 632 -15.626 15.061 61.618 1.00 45.49 C ANISOU 233 CZ PHE A 632 5379 6778 5129 -245 -327 -348 C ATOM 234 N GLY A 633 -19.315 8.984 59.383 1.00 34.30 N ANISOU 234 N GLY A 633 3984 5470 3577 -184 -8 762 N ATOM 235 CA GLY A 633 -20.278 8.190 58.632 1.00 35.29 C ANISOU 235 CA GLY A 633 3999 5670 3738 -410 208 648 C ATOM 236 C GLY A 633 -19.582 7.006 57.997 1.00 35.71 C ANISOU 236 C GLY A 633 4330 5406 3832 -450 194 911 C ATOM 237 O GLY A 633 -18.596 6.512 58.531 1.00 38.98 O ANISOU 237 O GLY A 633 5111 5571 4128 -272 -8 1070 O ATOM 238 N GLU A 634 -20.091 6.547 56.859 1.00 33.75 N ANISOU 238 N GLU A 634 3911 5176 3736 -538 275 821 N ATOM 239 CA GLU A 634 -19.539 5.358 56.215 1.00 32.26 C ANISOU 239 CA GLU A 634 3978 4693 3585 -574 270 1005 C ATOM 240 C GLU A 634 -18.493 5.765 55.178 1.00 28.38 C ANISOU 240 C GLU A 634 3313 4131 3339 -329 95 1001 C ATOM 241 O GLU A 634 -18.450 6.925 54.747 1.00 28.28 O ANISOU 241 O GLU A 634 3232 4164 3348 -290 83 908 O ATOM 242 CB GLU A 634 -20.630 4.552 55.522 1.00 33.86 C ANISOU 242 CB GLU A 634 4082 4974 3809 -920 537 803 C ATOM 243 CG GLU A 634 -21.724 3.972 56.444 1.00 41.06 C ANISOU 243 CG GLU A 634 5167 6006 4430 -1590 1060 506 C ATOM 244 CD GLU A 634 -22.722 3.100 55.676 1.00 48.26 C ANISOU 244 CD GLU A 634 5825 7078 5432 -2098 1429 41 C ATOM 245 OE1 GLU A 634 -23.114 3.481 54.546 1.00 54.26 O ANISOU 245 OE1 GLU A 634 5917 8158 6541 -1725 1128 -297 O ATOM 246 OE2 GLU A 634 -23.122 2.033 56.196 1.00 58.63 O ANISOU 246 OE2 GLU A 634 7780 8122 6374 -2905 2020 -57 O ATOM 247 N VAL A 635 -17.661 4.795 54.813 1.00 36.39 N ANISOU 247 N VAL A 635 4468 5496 3864 215 165 820 N ATOM 248 CA VAL A 635 -16.643 4.955 53.803 1.00 33.07 C ANISOU 248 CA VAL A 635 4094 4887 3586 239 79 672 C ATOM 249 C VAL A 635 -16.881 3.860 52.767 1.00 31.74 C ANISOU 249 C VAL A 635 3984 4540 3538 107 25 768 C ATOM 250 O VAL A 635 -17.116 2.712 53.119 1.00 34.52 O ANISOU 250 O VAL A 635 4440 4830 3848 21 -13 931 O ATOM 251 CB VAL A 635 -15.249 4.857 54.424 1.00 35.57 C ANISOU 251 CB VAL A 635 4485 5188 3843 352 -7 592 C ATOM 252 CG1 VAL A 635 -14.174 5.032 53.349 1.00 34.66 C ANISOU 252 CG1 VAL A 635 4361 4961 3847 375 -82 456 C ATOM 253 CG2 VAL A 635 -15.089 5.927 55.514 1.00 35.25 C ANISOU 253 CG2 VAL A 635 4423 5311 3658 454 21 495 C ATOM 254 N CYS A 636 -16.899 4.223 51.489 1.00 27.85 N ANISOU 254 N CYS A 636 3454 3951 3177 78 13 676 N ATOM 255 CA CYS A 636 -17.117 3.230 50.453 1.00 27.52 C ANISOU 255 CA CYS A 636 3498 3728 3230 -34 -55 740 C ATOM 256 C CYS A 636 -16.325 3.609 49.211 1.00 25.54 C ANISOU 256 C CYS A 636 3248 3370 3085 35 -94 582 C ATOM 257 O CYS A 636 -15.574 4.583 49.221 1.00 25.18 O ANISOU 257 O CYS A 636 3133 3396 3038 129 -74 448 O ATOM 258 CB CYS A 636 -18.616 3.069 50.148 1.00 31.74 C ANISOU 258 CB CYS A 636 3949 4331 3780 -220 -11 875 C ATOM 259 SG CYS A 636 -19.396 4.598 49.728 1.00 37.88 S ANISOU 259 SG CYS A 636 4517 5297 4578 -161 95 776 S ATOM 260 N SER A 637 -16.414 2.801 48.177 1.00 24.97 N ANISOU 260 N SER A 637 3276 3129 3082 -22 -163 601 N ATOM 261 CA SER A 637 -15.807 3.205 46.910 1.00 23.98 C ANISOU 261 CA SER A 637 3132 2946 3034 42 -181 463 C ATOM 262 C SER A 637 -16.799 2.934 45.815 1.00 24.22 C ANISOU 262 C SER A 637 3185 2882 3137 -94 -203 500 C ATOM 263 O SER A 637 -17.780 2.212 46.026 1.00 23.86 O ANISOU 263 O SER A 637 3190 2795 3079 -252 -234 638 O ATOM 264 CB SER A 637 -14.502 2.477 46.651 1.00 25.81 C ANISOU 264 CB SER A 637 3476 3095 3236 206 -261 400 C ATOM 265 OG SER A 637 -14.695 1.078 46.648 1.00 28.43 O ANISOU 265 OG SER A 637 4035 3230 3536 199 -360 493 O ATOM 266 N GLY A 638 -16.539 3.504 44.645 1.00 22.24 N ANISOU 266 N GLY A 638 2891 2614 2946 -56 -196 391 N ATOM 267 CA GLY A 638 -17.488 3.382 43.551 1.00 21.99 C ANISOU 267 CA GLY A 638 2867 2518 2972 -175 -224 412 C ATOM 268 C GLY A 638 -16.941 4.050 42.316 1.00 20.09 C ANISOU 268 C GLY A 638 2595 2269 2768 -96 -212 286 C ATOM 269 O GLY A 638 -15.720 4.055 42.092 1.00 17.68 O ANISOU 269 O GLY A 638 2314 1966 2438 37 -216 199 O ATOM 270 N ARG A 639 -17.858 4.571 41.507 1.00 19.85 N ANISOU 270 N ARG A 639 2499 2263 2780 -177 -199 291 N ATOM 271 CA ARG A 639 -17.526 5.127 40.203 1.00 18.77 C ANISOU 271 CA ARG A 639 2359 2108 2666 -129 -196 198 C ATOM 272 C ARG A 639 -18.220 6.467 40.085 1.00 19.21 C ANISOU 272 C ARG A 639 2291 2270 2737 -143 -126 194 C ATOM 273 O ARG A 639 -19.345 6.652 40.603 1.00 20.37 O ANISOU 273 O ARG A 639 2355 2506 2880 -195 -107 271 O ATOM 274 CB ARG A 639 -18.024 4.210 39.080 1.00 19.71 C ANISOU 274 CB ARG A 639 2596 2097 2795 -192 -296 204 C ATOM 275 CG ARG A 639 -17.148 3.020 38.759 1.00 27.69 C ANISOU 275 CG ARG A 639 3806 2954 3760 -96 -382 157 C ATOM 276 CD ARG A 639 -17.865 2.133 37.692 1.00 31.04 C ANISOU 276 CD ARG A 639 4402 3214 4177 -189 -512 159 C ATOM 277 NE ARG A 639 -17.751 2.427 36.226 1.00 34.71 N ANISOU 277 NE ARG A 639 4892 3673 4623 -125 -527 64 N ATOM 278 CZ ARG A 639 -16.666 2.162 35.476 1.00 37.16 C ANISOU 278 CZ ARG A 639 5304 3957 4859 78 -532 -45 C ATOM 279 NH1 ARG A 639 -15.553 1.743 36.063 1.00 40.97 N ANISOU 279 NH1 ARG A 639 5831 4449 5286 257 -515 -80 N ATOM 280 NH2 ARG A 639 -16.662 2.338 34.143 1.00 26.64 N ANISOU 280 NH2 ARG A 639 4009 2629 3484 129 -549 -118 N ATOM 281 N LEU A 640 -17.577 7.377 39.367 1.00 16.21 N ANISOU 281 N LEU A 640 1908 1896 2355 -89 -94 116 N ATOM 282 CA LEU A 640 -18.146 8.698 39.114 1.00 16.46 C ANISOU 282 CA LEU A 640 1900 1970 2383 -75 -51 106 C ATOM 283 C LEU A 640 -18.132 8.915 37.605 1.00 15.10 C ANISOU 283 C LEU A 640 1768 1754 2217 -79 -75 76 C ATOM 284 O LEU A 640 -17.092 8.715 36.948 1.00 16.76 O ANISOU 284 O LEU A 640 2016 1943 2407 -67 -77 30 O ATOM 285 CB LEU A 640 -17.300 9.774 39.787 1.00 15.78 C ANISOU 285 CB LEU A 640 1832 1903 2262 -43 -7 55 C ATOM 286 CG LEU A 640 -17.738 11.232 39.484 1.00 17.31 C ANISOU 286 CG LEU A 640 2081 2070 2427 -10 13 32 C ATOM 287 CD1 LEU A 640 -19.174 11.560 39.990 1.00 18.11 C ANISOU 287 CD1 LEU A 640 2141 2237 2502 85 29 72 C ATOM 288 CD2 LEU A 640 -16.702 12.205 40.043 1.00 16.96 C ANISOU 288 CD2 LEU A 640 2114 1993 2335 -44 18 -22 C ATOM 289 N LYS A 641 -19.277 9.307 37.059 1.00 14.85 N ANISOU 289 N LYS A 641 1709 1745 2188 -77 -91 109 N ATOM 290 CA LYS A 641 -19.357 9.666 35.642 1.00 16.05 C ANISOU 290 CA LYS A 641 1908 1864 2326 -68 -116 87 C ATOM 291 C LYS A 641 -19.125 11.178 35.537 1.00 17.31 C ANISOU 291 C LYS A 641 2124 2003 2448 -15 -70 69 C ATOM 292 O LYS A 641 -19.876 12.000 36.112 1.00 18.08 O ANISOU 292 O LYS A 641 2221 2125 2524 61 -56 85 O ATOM 293 CB LYS A 641 -20.734 9.290 35.081 1.00 19.47 C ANISOU 293 CB LYS A 641 2284 2349 2764 -95 -182 138 C ATOM 294 CG LYS A 641 -20.750 9.341 33.543 1.00 25.19 C ANISOU 294 CG LYS A 641 3076 3035 3461 -89 -232 110 C ATOM 295 CD LYS A 641 -21.803 8.423 32.952 1.00 29.41 C ANISOU 295 CD LYS A 641 3576 3603 3996 -175 -342 145 C ATOM 296 CE LYS A 641 -21.729 8.417 31.424 1.00 24.80 C ANISOU 296 CE LYS A 641 3085 2976 3362 -155 -402 101 C ATOM 297 NZ LYS A 641 -20.655 7.494 30.896 1.00 21.31 N ANISOU 297 NZ LYS A 641 2787 2420 2891 -150 -427 26 N ATOM 298 N LEU A 642 -18.061 11.538 34.830 1.00 16.05 N ANISOU 298 N LEU A 642 2033 1807 2260 -52 -53 41 N ATOM 299 CA LEU A 642 -17.675 12.926 34.667 1.00 17.55 C ANISOU 299 CA LEU A 642 2329 1939 2400 -70 -31 42 C ATOM 300 C LEU A 642 -18.547 13.608 33.598 1.00 17.86 C ANISOU 300 C LEU A 642 2450 1933 2403 -8 -61 72 C ATOM 301 O LEU A 642 -19.321 12.945 32.877 1.00 16.84 O ANISOU 301 O LEU A 642 2262 1852 2285 31 -99 85 O ATOM 302 CB LEU A 642 -16.190 12.971 34.294 1.00 16.32 C ANISOU 302 CB LEU A 642 2173 1823 2206 -179 0 33 C ATOM 303 CG LEU A 642 -15.275 12.343 35.375 1.00 18.06 C ANISOU 303 CG LEU A 642 2297 2123 2441 -207 17 3 C ATOM 304 CD1 LEU A 642 -13.877 12.301 34.826 1.00 25.59 C ANISOU 304 CD1 LEU A 642 3187 3205 3329 -287 49 5 C ATOM 305 CD2 LEU A 642 -15.281 13.219 36.642 1.00 21.87 C ANISOU 305 CD2 LEU A 642 2838 2552 2920 -238 12 -8 C ATOM 306 N PRO A 643 -18.494 14.946 33.540 1.00 19.35 N ANISOU 306 N PRO A 643 2801 2018 2534 3 -65 86 N ATOM 307 CA PRO A 643 -19.359 15.624 32.574 1.00 19.31 C ANISOU 307 CA PRO A 643 2900 1962 2475 104 -105 122 C ATOM 308 C PRO A 643 -19.070 15.256 31.134 1.00 19.19 C ANISOU 308 C PRO A 643 2879 1982 2430 44 -111 149 C ATOM 309 O PRO A 643 -19.990 15.289 30.300 1.00 21.84 O ANISOU 309 O PRO A 643 3225 2339 2735 143 -158 171 O ATOM 310 CB PRO A 643 -19.050 17.111 32.810 1.00 19.83 C ANISOU 310 CB PRO A 643 3221 1849 2465 101 -123 133 C ATOM 311 CG PRO A 643 -18.644 17.166 34.251 1.00 21.36 C ANISOU 311 CG PRO A 643 3407 2026 2682 74 -106 83 C ATOM 312 CD PRO A 643 -17.789 15.910 34.403 1.00 18.50 C ANISOU 312 CD PRO A 643 2827 1811 2392 -63 -60 70 C ATOM 313 N SER A 644 -17.810 14.937 30.852 1.00 18.19 N ANISOU 313 N SER A 644 2726 1896 2288 -97 -67 147 N ATOM 314 CA SER A 644 -17.375 14.443 29.529 1.00 19.45 C ANISOU 314 CA SER A 644 2864 2138 2388 -128 -55 160 C ATOM 315 C SER A 644 -17.817 12.994 29.239 1.00 17.99 C ANISOU 315 C SER A 644 2562 2032 2241 -53 -90 105 C ATOM 316 O SER A 644 -17.480 12.451 28.184 1.00 20.01 O ANISOU 316 O SER A 644 2824 2352 2429 -39 -92 90 O ATOM 317 CB SER A 644 -15.846 14.432 29.510 1.00 19.94 C ANISOU 317 CB SER A 644 2877 2299 2398 -270 15 173 C ATOM 318 OG SER A 644 -15.412 13.470 30.478 1.00 22.95 O ANISOU 318 OG SER A 644 3118 2755 2846 -250 30 112 O ATOM 319 N LYS A 645 -18.509 12.370 30.192 1.00 17.34 N ANISOU 319 N LYS A 645 2399 1943 2246 -18 -122 79 N ATOM 320 CA LYS A 645 -18.956 10.954 30.150 1.00 17.58 C ANISOU 320 CA LYS A 645 2364 2002 2315 -6 -184 42 C ATOM 321 C LYS A 645 -17.904 9.924 30.537 1.00 18.59 C ANISOU 321 C LYS A 645 2472 2145 2448 -16 -162 -8 C ATOM 322 O LYS A 645 -18.209 8.738 30.623 1.00 17.42 O ANISOU 322 O LYS A 645 2336 1963 2321 -10 -230 -37 O ATOM 323 CB LYS A 645 -19.573 10.573 28.802 1.00 17.92 C ANISOU 323 CB LYS A 645 2453 2056 2299 21 -262 33 C ATOM 324 CG LYS A 645 -20.615 11.551 28.253 1.00 20.82 C ANISOU 324 CG LYS A 645 2839 2438 2633 73 -300 86 C ATOM 325 CD LYS A 645 -21.767 11.773 29.245 1.00 22.75 C ANISOU 325 CD LYS A 645 2975 2730 2938 106 -325 124 C ATOM 326 CE LYS A 645 -22.932 12.483 28.545 1.00 27.60 C ANISOU 326 CE LYS A 645 3581 3414 3491 213 -390 169 C ATOM 327 NZ LYS A 645 -23.866 13.046 29.577 1.00 26.76 N ANISOU 327 NZ LYS A 645 3369 3399 3399 319 -379 207 N ATOM 328 N LYS A 646 -16.662 10.360 30.741 1.00 18.05 N ANISOU 328 N LYS A 646 2384 2131 2341 -32 -82 -12 N ATOM 329 CA LYS A 646 -15.640 9.455 31.219 1.00 17.60 C ANISOU 329 CA LYS A 646 2281 2136 2270 8 -62 -57 C ATOM 330 C LYS A 646 -16.059 8.950 32.587 1.00 17.50 C ANISOU 330 C LYS A 646 2239 2063 2348 -4 -90 -54 C ATOM 331 O LYS A 646 -16.643 9.711 33.370 1.00 19.90 O ANISOU 331 O LYS A 646 2519 2340 2704 -53 -76 -16 O ATOM 332 CB LYS A 646 -14.303 10.187 31.323 1.00 17.65 C ANISOU 332 CB LYS A 646 2213 2281 2211 -44 25 -38 C ATOM 333 CG LYS A 646 -13.143 9.213 31.673 1.00 25.71 C ANISOU 333 CG LYS A 646 3148 3440 3178 56 46 -86 C ATOM 334 CD LYS A 646 -11.790 9.885 31.488 1.00 34.17 C ANISOU 334 CD LYS A 646 4088 4749 4147 -12 129 -51 C ATOM 335 CE LYS A 646 -10.727 9.215 32.353 1.00 44.47 C ANISOU 335 CE LYS A 646 5259 6221 5416 76 143 -83 C ATOM 336 NZ LYS A 646 -9.650 10.175 32.666 1.00 50.53 N ANISOU 336 NZ LYS A 646 5867 7212 6122 -98 198 -22 N ATOM 337 N GLU A 647 -15.720 7.702 32.906 1.00 17.11 N ANISOU 337 N GLU A 647 2214 1993 2293 62 -130 -90 N ATOM 338 CA GLU A 647 -16.057 7.127 34.215 1.00 16.16 C ANISOU 338 CA GLU A 647 2085 1818 2237 39 -158 -66 C ATOM 339 C GLU A 647 -14.749 6.814 34.956 1.00 17.10 C ANISOU 339 C GLU A 647 2162 2019 2318 118 -122 -94 C ATOM 340 O GLU A 647 -13.803 6.197 34.370 1.00 18.66 O ANISOU 340 O GLU A 647 2382 2279 2428 249 -125 -147 O ATOM 341 CB GLU A 647 -16.856 5.821 33.998 1.00 16.08 C ANISOU 341 CB GLU A 647 2194 1677 2238 26 -272 -64 C ATOM 342 CG GLU A 647 -18.264 6.118 33.511 1.00 20.25 C ANISOU 342 CG GLU A 647 2703 2187 2803 -84 -322 -16 C ATOM 343 CD GLU A 647 -19.056 4.894 33.028 1.00 19.92 C ANISOU 343 CD GLU A 647 2790 2028 2752 -165 -466 -11 C ATOM 344 OE1 GLU A 647 -18.716 3.752 33.376 1.00 22.21 O ANISOU 344 OE1 GLU A 647 3223 2193 3022 -156 -537 -25 O ATOM 345 OE2 GLU A 647 -20.073 5.114 32.302 1.00 23.23 O ANISOU 345 OE2 GLU A 647 3180 2475 3172 -247 -524 15 O ATOM 346 N ILE A 648 -14.674 7.220 36.224 1.00 14.35 N ANISOU 346 N ILE A 648 1747 1698 2006 71 -93 -64 N ATOM 347 CA ILE A 648 -13.468 6.963 37.020 1.00 14.89 C ANISOU 347 CA ILE A 648 1755 1874 2029 141 -74 -84 C ATOM 348 C ILE A 648 -13.828 6.299 38.326 1.00 14.38 C ANISOU 348 C ILE A 648 1725 1742 1995 149 -110 -49 C ATOM 349 O ILE A 648 -14.975 6.403 38.769 1.00 17.20 O ANISOU 349 O ILE A 648 2105 2023 2409 63 -120 3 O ATOM 350 CB ILE A 648 -12.673 8.278 37.317 1.00 15.50 C ANISOU 350 CB ILE A 648 1715 2093 2079 48 -12 -83 C ATOM 351 CG1 ILE A 648 -13.567 9.320 38.021 1.00 17.75 C ANISOU 351 CG1 ILE A 648 2033 2290 2420 -61 -3 -54 C ATOM 352 CG2 ILE A 648 -12.087 8.822 36.017 1.00 18.73 C ANISOU 352 CG2 ILE A 648 2085 2608 2424 20 28 -89 C ATOM 353 CD1 ILE A 648 -12.763 10.456 38.684 1.00 19.54 C ANISOU 353 CD1 ILE A 648 2222 2594 2607 -167 14 -62 C ATOM 354 N SER A 649 -12.862 5.597 38.931 1.00 16.94 N ANISOU 354 N SER A 649 2044 2128 2263 268 -130 -67 N ATOM 355 CA SER A 649 -13.108 5.036 40.261 1.00 17.97 C ANISOU 355 CA SER A 649 2218 2205 2403 272 -162 -18 C ATOM 356 C SER A 649 -12.941 6.177 41.263 1.00 18.96 C ANISOU 356 C SER A 649 2224 2445 2533 188 -108 -10 C ATOM 357 O SER A 649 -12.083 7.052 41.078 1.00 17.58 O ANISOU 357 O SER A 649 1947 2407 2326 160 -75 -52 O ATOM 358 CB SER A 649 -12.095 3.936 40.583 1.00 21.42 C ANISOU 358 CB SER A 649 2718 2666 2755 468 -216 -40 C ATOM 359 OG SER A 649 -12.336 2.780 39.790 1.00 23.50 O ANISOU 359 OG SER A 649 3180 2757 2991 568 -296 -56 O ATOM 360 N VAL A 650 -13.707 6.120 42.343 1.00 15.47 N ANISOU 360 N VAL A 650 1809 1961 2109 141 -109 46 N ATOM 361 CA VAL A 650 -13.635 7.144 43.388 1.00 16.23 C ANISOU 361 CA VAL A 650 1843 2144 2181 96 -72 37 C ATOM 362 C VAL A 650 -13.821 6.532 44.767 1.00 16.16 C ANISOU 362 C VAL A 650 1862 2149 2129 132 -87 95 C ATOM 363 O VAL A 650 -14.413 5.430 44.908 1.00 17.47 O ANISOU 363 O VAL A 650 2109 2229 2302 136 -118 175 O ATOM 364 CB VAL A 650 -14.710 8.248 43.210 1.00 14.16 C ANISOU 364 CB VAL A 650 1583 1847 1951 22 -29 40 C ATOM 365 CG1 VAL A 650 -14.350 9.170 41.982 1.00 16.89 C ANISOU 365 CG1 VAL A 650 1925 2179 2313 -27 -17 -13 C ATOM 366 CG2 VAL A 650 -16.156 7.664 43.052 1.00 17.52 C ANISOU 366 CG2 VAL A 650 2024 2220 2414 -2 -26 121 C ATOM 367 N ALA A 651 -13.274 7.237 45.765 1.00 16.69 N ANISOU 367 N ALA A 651 1887 2318 2136 138 -80 60 N ATOM 368 CA ALA A 651 -13.551 6.982 47.186 1.00 17.00 C ANISOU 368 CA ALA A 651 1951 2401 2108 170 -80 111 C ATOM 369 C ALA A 651 -14.716 7.884 47.558 1.00 19.36 C ANISOU 369 C ALA A 651 2253 2707 2396 135 -20 120 C ATOM 370 O ALA A 651 -14.816 9.026 47.062 1.00 18.19 O ANISOU 370 O ALA A 651 2111 2538 2263 108 -4 48 O ATOM 371 CB ALA A 651 -12.328 7.308 48.031 1.00 20.19 C ANISOU 371 CB ALA A 651 2313 2931 2426 210 -122 52 C ATOM 372 N ILE A 652 -15.635 7.352 48.375 1.00 17.92 N ANISOU 372 N ILE A 652 2075 2564 2168 145 11 220 N ATOM 373 CA ILE A 652 -16.842 8.109 48.753 1.00 20.38 C ANISOU 373 CA ILE A 652 2352 2957 2434 167 82 240 C ATOM 374 C ILE A 652 -17.016 8.027 50.268 1.00 22.20 C ANISOU 374 C ILE A 652 2586 3320 2528 232 113 287 C ATOM 375 O ILE A 652 -16.838 6.952 50.864 1.00 24.54 O ANISOU 375 O ILE A 652 2900 3632 2793 205 93 387 O ATOM 376 CB ILE A 652 -18.112 7.539 48.043 1.00 20.84 C ANISOU 376 CB ILE A 652 2346 3026 2547 91 109 352 C ATOM 377 CG1 ILE A 652 -17.936 7.560 46.518 1.00 21.14 C ANISOU 377 CG1 ILE A 652 2400 2933 2700 39 69 302 C ATOM 378 CG2 ILE A 652 -19.366 8.333 48.441 1.00 24.69 C ANISOU 378 CG2 ILE A 652 2745 3683 2955 164 190 379 C ATOM 379 CD1 ILE A 652 -18.774 6.561 45.801 1.00 24.60 C ANISOU 379 CD1 ILE A 652 2819 3335 3192 -76 39 407 C ATOM 380 N LYS A 653 -17.284 9.164 50.912 1.00 22.40 N ANISOU 380 N LYS A 653 2634 3423 2453 336 149 207 N ATOM 381 CA LYS A 653 -17.559 9.179 52.345 1.00 26.12 C ANISOU 381 CA LYS A 653 3113 4051 2760 431 189 242 C ATOM 382 C LYS A 653 -18.881 9.856 52.531 1.00 25.66 C ANISOU 382 C LYS A 653 2999 4144 2608 552 282 259 C ATOM 383 O LYS A 653 -19.156 10.827 51.834 1.00 23.59 O ANISOU 383 O LYS A 653 2775 3815 2373 621 281 162 O ATOM 384 CB LYS A 653 -16.507 10.002 53.103 1.00 26.83 C ANISOU 384 CB LYS A 653 3321 4115 2758 496 123 95 C ATOM 385 CG LYS A 653 -15.207 9.220 53.318 1.00 36.40 C ANISOU 385 CG LYS A 653 4536 5298 3997 426 37 103 C ATOM 386 CD LYS A 653 -14.267 9.933 54.276 1.00 40.67 C ANISOU 386 CD LYS A 653 5159 5881 4411 465 -41 -18 C ATOM 387 CE LYS A 653 -13.952 11.373 53.853 1.00 41.75 C ANISOU 387 CE LYS A 653 5402 5914 4549 425 -96 -178 C ATOM 388 NZ LYS A 653 -12.938 11.940 54.814 1.00 43.59 N ANISOU 388 NZ LYS A 653 5725 6188 4649 403 -209 -287 N ATOM 389 N THR A 654 -19.699 9.353 53.459 1.00 25.99 N ANISOU 389 N THR A 654 3154 3197 3525 -678 781 -392 N ATOM 390 CA THR A 654 -20.991 9.963 53.678 1.00 25.95 C ANISOU 390 CA THR A 654 3166 3442 3250 -704 515 -404 C ATOM 391 C THR A 654 -21.044 10.488 55.117 1.00 27.59 C ANISOU 391 C THR A 654 3250 3773 3462 -489 323 -222 C ATOM 392 O THR A 654 -20.295 10.057 55.985 1.00 28.75 O ANISOU 392 O THR A 654 3281 3885 3760 -383 372 -43 O ATOM 393 CB THR A 654 -22.144 8.971 53.467 1.00 28.21 C ANISOU 393 CB THR A 654 3489 3728 3502 -880 636 -506 C ATOM 394 OG1 THR A 654 -21.954 7.876 54.366 1.00 29.93 O ANISOU 394 OG1 THR A 654 3605 3759 4009 -751 832 -395 O ATOM 395 CG2 THR A 654 -22.170 8.437 52.024 1.00 35.04 C ANISOU 395 CG2 THR A 654 4496 4555 4261 -1256 875 -766 C ATOM 396 N LEU A 655 -21.918 11.454 55.334 1.00 26.84 N ANISOU 396 N LEU A 655 3147 3838 3214 -480 136 -246 N ATOM 397 CA LEU A 655 -22.172 11.974 56.673 1.00 25.10 C ANISOU 397 CA LEU A 655 2839 3739 2957 -390 48 -189 C ATOM 398 C LEU A 655 -23.326 11.163 57.277 1.00 27.33 C ANISOU 398 C LEU A 655 3089 4058 3238 -408 77 -164 C ATOM 399 O LEU A 655 -24.379 10.996 56.644 1.00 25.33 O ANISOU 399 O LEU A 655 2862 3794 2969 -477 68 -214 O ATOM 400 CB LEU A 655 -22.547 13.444 56.538 1.00 26.10 C ANISOU 400 CB LEU A 655 2948 3906 3062 -380 -34 -261 C ATOM 401 CG LEU A 655 -22.891 14.266 57.791 1.00 27.48 C ANISOU 401 CG LEU A 655 3055 4159 3228 -380 0 -335 C ATOM 402 CD1 LEU A 655 -21.732 14.293 58.771 1.00 27.98 C ANISOU 402 CD1 LEU A 655 3103 4368 3160 -442 2 -329 C ATOM 403 CD2 LEU A 655 -23.244 15.685 57.334 1.00 27.03 C ANISOU 403 CD2 LEU A 655 2937 3998 3335 -355 38 -391 C ATOM 404 N LYS A 656 -23.148 10.689 58.512 1.00 27.05 N ANISOU 404 N LYS A 656 2968 4118 3193 -385 89 -46 N ATOM 405 CA LYS A 656 -24.142 9.845 59.174 1.00 28.44 C ANISOU 405 CA LYS A 656 3099 4332 3375 -399 126 6 C ATOM 406 C LYS A 656 -25.544 10.465 59.229 1.00 26.09 C ANISOU 406 C LYS A 656 2823 4068 3020 -424 90 -131 C ATOM 407 O LYS A 656 -25.693 11.686 59.318 1.00 26.28 O ANISOU 407 O LYS A 656 2840 4116 3032 -428 70 -230 O ATOM 408 CB LYS A 656 -23.697 9.525 60.608 1.00 30.58 C ANISOU 408 CB LYS A 656 3234 4814 3572 -436 98 215 C ATOM 409 CG LYS A 656 -23.560 10.750 61.488 1.00 32.51 C ANISOU 409 CG LYS A 656 3474 5300 3576 -563 29 101 C ATOM 410 CD LYS A 656 -23.159 10.387 62.919 1.00 38.42 C ANISOU 410 CD LYS A 656 4073 6405 4122 -747 -24 331 C ATOM 411 CE LYS A 656 -24.387 10.101 63.785 1.00 45.20 C ANISOU 411 CE LYS A 656 4926 7386 4863 -847 26 266 C ATOM 412 NZ LYS A 656 -24.060 10.208 65.239 1.00 51.29 N ANISOU 412 NZ LYS A 656 5579 8628 5282 -1176 -24 391 N ATOM 413 N VAL A 657 -26.561 9.611 59.198 1.00 25.32 N ANISOU 413 N VAL A 657 2719 3939 2963 -442 129 -116 N ATOM 414 CA VAL A 657 -27.935 10.078 59.389 1.00 26.65 C ANISOU 414 CA VAL A 657 2849 4132 3143 -457 111 -169 C ATOM 415 C VAL A 657 -28.037 10.682 60.789 1.00 28.03 C ANISOU 415 C VAL A 657 2976 4416 3257 -475 167 -228 C ATOM 416 O VAL A 657 -27.449 10.154 61.750 1.00 28.51 O ANISOU 416 O VAL A 657 3015 4628 3189 -529 175 -152 O ATOM 417 CB VAL A 657 -28.982 8.946 59.186 1.00 28.50 C ANISOU 417 CB VAL A 657 3078 4341 3410 -504 143 -136 C ATOM 418 CG1 VAL A 657 -30.378 9.503 59.252 1.00 29.43 C ANISOU 418 CG1 VAL A 657 3109 4477 3595 -515 113 -126 C ATOM 419 CG2 VAL A 657 -28.797 8.267 57.836 1.00 31.53 C ANISOU 419 CG2 VAL A 657 3534 4659 3785 -628 172 -171 C ATOM 420 N GLY A 658 -28.746 11.808 60.920 1.00 27.77 N ANISOU 420 N GLY A 658 2893 4321 3339 -482 245 -338 N ATOM 421 CA GLY A 658 -28.892 12.417 62.238 1.00 27.08 C ANISOU 421 CA GLY A 658 2784 4316 3190 -603 417 -508 C ATOM 422 C GLY A 658 -27.654 13.136 62.740 1.00 27.38 C ANISOU 422 C GLY A 658 2861 4486 3056 -736 455 -628 C ATOM 423 O GLY A 658 -27.476 13.304 63.949 1.00 29.84 O ANISOU 423 O GLY A 658 3179 5018 3143 -972 569 -762 O ATOM 424 N TYR A 659 -26.806 13.563 61.806 1.00 26.34 N ANISOU 424 N TYR A 659 2753 4268 2988 -643 364 -584 N ATOM 425 CA TYR A 659 -25.614 14.345 62.109 1.00 29.54 C ANISOU 425 CA TYR A 659 3185 4777 3263 -763 394 -692 C ATOM 426 C TYR A 659 -25.955 15.648 62.827 1.00 32.27 C ANISOU 426 C TYR A 659 3510 5061 3692 -946 699 -1015 C ATOM 427 O TYR A 659 -27.061 16.200 62.658 1.00 33.95 O ANISOU 427 O TYR A 659 3647 5008 4245 -872 903 -1098 O ATOM 428 CB TYR A 659 -24.867 14.665 60.806 1.00 27.67 C ANISOU 428 CB TYR A 659 2970 4387 3157 -604 277 -600 C ATOM 429 CG TYR A 659 -25.717 15.455 59.836 1.00 28.65 C ANISOU 429 CG TYR A 659 3024 4258 3604 -480 333 -589 C ATOM 430 CD1 TYR A 659 -25.772 16.839 59.913 1.00 28.79 C ANISOU 430 CD1 TYR A 659 2963 4108 3869 -500 543 -729 C ATOM 431 CD2 TYR A 659 -26.498 14.811 58.856 1.00 28.82 C ANISOU 431 CD2 TYR A 659 3012 4226 3711 -392 202 -394 C ATOM 432 CE1 TYR A 659 -26.566 17.577 59.044 1.00 34.03 C ANISOU 432 CE1 TYR A 659 3457 4535 4937 -376 601 -570 C ATOM 433 CE2 TYR A 659 -27.292 15.546 57.974 1.00 30.41 C ANISOU 433 CE2 TYR A 659 3064 4296 4194 -338 200 -241 C ATOM 434 CZ TYR A 659 -27.319 16.935 58.079 1.00 34.44 C ANISOU 434 CZ TYR A 659 3438 4620 5028 -301 390 -276 C ATOM 435 OH TYR A 659 -28.107 17.696 57.236 1.00 35.46 O ANISOU 435 OH TYR A 659 3317 4606 5551 -233 400 15 O ATOM 436 N THR A 660 -25.004 16.144 63.624 1.00 34.56 N ANISOU 436 N THR A 660 3836 5586 3709 -1224 775 -1187 N ATOM 437 CA THR A 660 -25.155 17.449 64.254 1.00 38.03 C ANISOU 437 CA THR A 660 4277 5936 4237 -1486 1172 -1597 C ATOM 438 C THR A 660 -24.599 18.501 63.304 1.00 38.63 C ANISOU 438 C THR A 660 4327 5722 4629 -1329 1239 -1639 C ATOM 439 O THR A 660 -23.825 18.177 62.388 1.00 34.81 O ANISOU 439 O THR A 660 3859 5252 4116 -1120 936 -1380 O ATOM 440 CB THR A 660 -24.382 17.551 65.572 1.00 41.62 C ANISOU 440 CB THR A 660 4782 6867 4163 -2000 1249 -1806 C ATOM 441 OG1 THR A 660 -22.983 17.387 65.319 1.00 38.30 O ANISOU 441 OG1 THR A 660 4359 6700 3493 -2023 954 -1588 O ATOM 442 CG2 THR A 660 -24.856 16.509 66.567 1.00 43.47 C ANISOU 442 CG2 THR A 660 5003 7469 4042 -2207 1155 -1687 C ATOM 443 N GLU A 661 -24.982 19.757 63.516 1.00 42.10 N ANISOU 443 N GLU A 661 4709 5865 5421 -1445 1690 -1967 N ATOM 444 CA GLU A 661 -24.488 20.834 62.660 1.00 42.95 C ANISOU 444 CA GLU A 661 4747 5665 5906 -1299 1803 -1976 C ATOM 445 C GLU A 661 -22.963 20.946 62.720 1.00 42.49 C ANISOU 445 C GLU A 661 4799 5902 5443 -1466 1620 -2031 C ATOM 446 O GLU A 661 -22.331 21.208 61.701 1.00 38.91 O ANISOU 446 O GLU A 661 4323 5322 5140 -1232 1442 -1836 O ATOM 447 CB GLU A 661 -25.190 22.174 62.937 1.00 48.71 C ANISOU 447 CB GLU A 661 5336 5933 7239 -1395 2436 -2300 C ATOM 448 CG GLU A 661 -26.616 22.245 62.318 1.00 53.54 C ANISOU 448 CG GLU A 661 5707 6130 8506 -1066 2549 -1999 C ATOM 449 CD GLU A 661 -26.643 21.841 60.823 1.00 58.88 C ANISOU 449 CD GLU A 661 6272 6795 9305 -672 2051 -1415 C ATOM 450 OE1 GLU A 661 -25.776 22.316 60.045 1.00 58.80 O ANISOU 450 OE1 GLU A 661 6251 6759 9330 -580 1916 -1297 O ATOM 451 OE2 GLU A 661 -27.525 21.045 60.424 1.00 54.55 O ANISOU 451 OE2 GLU A 661 5651 6299 8775 -513 1809 -1094 O ATOM 452 N LYS A 662 -22.388 20.709 63.899 1.00 44.05 N ANISOU 452 N LYS A 662 5088 6541 5108 -1902 1640 -2242 N ATOM 453 CA LYS A 662 -20.938 20.686 64.043 1.00 45.25 C ANISOU 453 CA LYS A 662 5286 7062 4844 -2103 1410 -2187 C ATOM 454 C LYS A 662 -20.292 19.551 63.246 1.00 40.05 C ANISOU 454 C LYS A 662 4609 6524 4082 -1763 896 -1667 C ATOM 455 O LYS A 662 -19.235 19.745 62.647 1.00 36.90 O ANISOU 455 O LYS A 662 4210 6131 3680 -1673 737 -1542 O ATOM 456 CB LYS A 662 -20.519 20.618 65.514 1.00 50.06 C ANISOU 456 CB LYS A 662 5932 8244 4845 -2743 1499 -2419 C ATOM 457 CG LYS A 662 -19.021 20.813 65.717 1.00 55.13 C ANISOU 457 CG LYS A 662 6561 9304 5082 -3038 1299 -2346 C ATOM 458 CD LYS A 662 -18.604 20.435 67.121 1.00 65.03 C ANISOU 458 CD LYS A 662 7780 11307 5622 -3718 1225 -2355 C ATOM 459 CE LYS A 662 -17.113 20.137 67.163 1.00 67.36 C ANISOU 459 CE LYS A 662 7955 12090 5548 -3882 817 -1945 C ATOM 460 NZ LYS A 662 -16.861 19.068 68.173 1.00 74.54 N ANISOU 460 NZ LYS A 662 8694 13720 5909 -4259 484 -1482 N ATOM 461 N GLN A 663 -20.916 18.371 63.248 1.00 37.07 N ANISOU 461 N GLN A 663 4213 6208 3663 -1599 699 -1396 N ATOM 462 CA GLN A 663 -20.410 17.260 62.444 1.00 34.17 C ANISOU 462 CA GLN A 663 3820 5843 3320 -1300 355 -969 C ATOM 463 C GLN A 663 -20.439 17.616 60.961 1.00 30.53 C ANISOU 463 C GLN A 663 3389 4989 3223 -955 326 -919 C ATOM 464 O GLN A 663 -19.455 17.388 60.243 1.00 29.32 O ANISOU 464 O GLN A 663 3242 4819 3078 -837 167 -743 O ATOM 465 CB GLN A 663 -21.184 15.965 62.717 1.00 34.77 C ANISOU 465 CB GLN A 663 3862 5993 3356 -1216 245 -743 C ATOM 466 CG GLN A 663 -20.855 15.357 64.078 1.00 39.15 C ANISOU 466 CG GLN A 663 4326 7038 3510 -1562 166 -596 C ATOM 467 CD GLN A 663 -21.835 14.295 64.524 1.00 44.23 C ANISOU 467 CD GLN A 663 4929 7734 4141 -1520 139 -441 C ATOM 468 OE1 GLN A 663 -22.996 14.280 64.111 1.00 40.04 O ANISOU 468 OE1 GLN A 663 4465 6903 3845 -1331 255 -589 O ATOM 469 NE2 GLN A 663 -21.377 13.410 65.403 1.00 48.49 N ANISOU 469 NE2 GLN A 663 5316 8685 4423 -1720 -23 -81 N ATOM 470 N ARG A 664 -21.520 18.245 60.516 1.00 28.90 N ANISOU 470 N ARG A 664 3162 4488 3330 -836 498 -1039 N ATOM 471 CA ARG A 664 -21.615 18.649 59.092 1.00 28.79 C ANISOU 471 CA ARG A 664 3116 4200 3622 -587 437 -897 C ATOM 472 C ARG A 664 -20.515 19.637 58.728 1.00 29.81 C ANISOU 472 C ARG A 664 3252 4267 3809 -605 480 -979 C ATOM 473 O ARG A 664 -19.841 19.485 57.700 1.00 27.36 O ANISOU 473 O ARG A 664 2968 3921 3508 -473 307 -808 O ATOM 474 CB ARG A 664 -22.998 19.226 58.752 1.00 30.88 C ANISOU 474 CB ARG A 664 3248 4202 4281 -487 604 -869 C ATOM 475 CG ARG A 664 -23.200 19.492 57.264 1.00 28.95 C ANISOU 475 CG ARG A 664 2904 3815 4279 -310 461 -576 C ATOM 476 CD ARG A 664 -24.564 20.100 56.925 1.00 36.53 C ANISOU 476 CD ARG A 664 3621 4558 5702 -227 597 -380 C ATOM 477 NE ARG A 664 -24.461 20.741 55.614 1.00 47.28 N ANISOU 477 NE ARG A 664 4819 5848 7296 -140 480 -51 N ATOM 478 CZ ARG A 664 -25.168 20.414 54.537 1.00 52.57 C ANISOU 478 CZ ARG A 664 5346 6634 7996 -138 248 348 C ATOM 479 NH1 ARG A 664 -26.108 19.470 54.593 1.00 58.01 N ANISOU 479 NH1 ARG A 664 6036 7461 8546 -191 134 439 N ATOM 480 NH2 ARG A 664 -24.958 21.064 53.402 1.00 53.61 N ANISOU 480 NH2 ARG A 664 5310 6784 8278 -133 131 679 N ATOM 481 N ARG A 665 -20.321 20.642 59.578 1.00 31.09 N ANISOU 481 N ARG A 665 3396 4417 3998 -816 756 -1280 N ATOM 482 CA ARG A 665 -19.286 21.655 59.368 1.00 33.69 C ANISOU 482 CA ARG A 665 3728 4684 4388 -880 852 -1412 C ATOM 483 C ARG A 665 -17.890 21.041 59.357 1.00 31.26 C ANISOU 483 C ARG A 665 3493 4671 3714 -936 569 -1275 C ATOM 484 O ARG A 665 -17.076 21.353 58.469 1.00 29.30 O ANISOU 484 O ARG A 665 3252 4322 3560 -800 472 -1172 O ATOM 485 CB ARG A 665 -19.354 22.756 60.430 1.00 36.08 C ANISOU 485 CB ARG A 665 4013 4941 4752 -1213 1293 -1856 C ATOM 486 CG ARG A 665 -20.582 23.647 60.328 1.00 45.14 C ANISOU 486 CG ARG A 665 5016 5636 6498 -1128 1719 -1981 C ATOM 487 CD ARG A 665 -20.430 24.951 61.126 1.00 50.83 C ANISOU 487 CD ARG A 665 5710 6165 7437 -1469 2306 -2492 C ATOM 488 NE ARG A 665 -20.108 24.711 62.535 1.00 60.74 N ANISOU 488 NE ARG A 665 7112 7847 8121 -2000 2436 -2893 N ATOM 489 CZ ARG A 665 -20.999 24.601 63.516 1.00 65.69 C ANISOU 489 CZ ARG A 665 7753 8507 8699 -2278 2756 -3177 C ATOM 490 NH1 ARG A 665 -22.302 24.717 63.272 1.00 68.07 N ANISOU 490 NH1 ARG A 665 7918 8375 9571 -2026 3008 -3106 N ATOM 491 NH2 ARG A 665 -20.579 24.381 64.756 1.00 72.38 N ANISOU 491 NH2 ARG A 665 8725 9865 8911 -2857 2824 -3499 N ATOM 492 N ASP A 666 -17.611 20.168 60.319 1.00 29.04 N ANISOU 492 N ASP A 666 3222 4752 3061 -1139 443 -1212 N ATOM 493 CA ASP A 666 -16.293 19.521 60.346 1.00 32.53 C ANISOU 493 CA ASP A 666 3634 5457 3271 -1179 189 -946 C ATOM 494 C ASP A 666 -16.067 18.610 59.144 1.00 29.11 C ANISOU 494 C ASP A 666 3209 4821 3032 -836 8 -637 C ATOM 495 O ASP A 666 -14.989 18.591 58.548 1.00 29.13 O ANISOU 495 O ASP A 666 3198 4785 3084 -757 -78 -500 O ATOM 496 CB ASP A 666 -16.059 18.786 61.661 1.00 35.33 C ANISOU 496 CB ASP A 666 3901 6288 3236 -1505 84 -803 C ATOM 497 CG ASP A 666 -15.932 19.739 62.840 1.00 42.05 C ANISOU 497 CG ASP A 666 4757 7461 3758 -2020 284 -1159 C ATOM 498 OD1 ASP A 666 -15.588 20.922 62.617 1.00 43.62 O ANISOU 498 OD1 ASP A 666 5011 7505 4057 -2111 492 -1480 O ATOM 499 OD2 ASP A 666 -16.187 19.315 63.989 1.00 47.91 O ANISOU 499 OD2 ASP A 666 5446 8621 4137 -2384 270 -1139 O ATOM 500 N PHE A 667 -17.112 17.881 58.772 1.00 27.11 N ANISOU 500 N PHE A 667 2981 4429 2891 -680 0 -569 N ATOM 501 CA PHE A 667 -17.042 16.950 57.667 1.00 25.62 C ANISOU 501 CA PHE A 667 2823 4066 2847 -475 -80 -375 C ATOM 502 C PHE A 667 -16.734 17.671 56.365 1.00 25.76 C ANISOU 502 C PHE A 667 2899 3873 3014 -365 -70 -426 C ATOM 503 O PHE A 667 -15.760 17.348 55.693 1.00 26.32 O ANISOU 503 O PHE A 667 2992 3883 3127 -314 -98 -328 O ATOM 504 CB PHE A 667 -18.378 16.223 57.548 1.00 25.26 C ANISOU 504 CB PHE A 667 2798 3952 2847 -418 -61 -363 C ATOM 505 CG PHE A 667 -18.429 15.194 56.448 1.00 24.02 C ANISOU 505 CG PHE A 667 2691 3643 2791 -327 -67 -252 C ATOM 506 CD1 PHE A 667 -17.692 14.024 56.528 1.00 26.52 C ANISOU 506 CD1 PHE A 667 2964 3931 3181 -308 -26 -77 C ATOM 507 CD2 PHE A 667 -19.269 15.375 55.362 1.00 25.92 C ANISOU 507 CD2 PHE A 667 2985 3784 3078 -320 -70 -302 C ATOM 508 CE1 PHE A 667 -17.786 13.041 55.527 1.00 27.77 C ANISOU 508 CE1 PHE A 667 3181 3890 3478 -298 104 -78 C ATOM 509 CE2 PHE A 667 -19.363 14.401 54.343 1.00 25.13 C ANISOU 509 CE2 PHE A 667 2957 3610 2984 -377 -22 -283 C ATOM 510 CZ PHE A 667 -18.623 13.244 54.426 1.00 26.09 C ANISOU 510 CZ PHE A 667 3085 3633 3195 -375 110 -234 C ATOM 511 N LEU A 668 -17.534 18.681 56.046 1.00 24.48 N ANISOU 511 N LEU A 668 2724 3597 2979 -343 0 -541 N ATOM 512 CA LEU A 668 -17.379 19.419 54.800 1.00 22.42 C ANISOU 512 CA LEU A 668 2459 3189 2872 -265 -14 -491 C ATOM 513 C LEU A 668 -16.160 20.326 54.831 1.00 23.57 C ANISOU 513 C LEU A 668 2604 3308 3043 -280 24 -573 C ATOM 514 O LEU A 668 -15.610 20.670 53.790 1.00 24.59 O ANISOU 514 O LEU A 668 2749 3353 3241 -224 -17 -498 O ATOM 515 CB LEU A 668 -18.632 20.241 54.511 1.00 24.50 C ANISOU 515 CB LEU A 668 2596 3330 3381 -229 60 -444 C ATOM 516 CG LEU A 668 -19.879 19.412 54.152 1.00 26.55 C ANISOU 516 CG LEU A 668 2826 3641 3619 -235 -22 -293 C ATOM 517 CD1 LEU A 668 -21.108 20.311 53.969 1.00 27.54 C ANISOU 517 CD1 LEU A 668 2731 3644 4089 -194 59 -133 C ATOM 518 CD2 LEU A 668 -19.630 18.603 52.866 1.00 30.64 C ANISOU 518 CD2 LEU A 668 3429 4252 3960 -306 -168 -163 C ATOM 519 N GLY A 669 -15.752 20.732 56.033 1.00 24.15 N ANISOU 519 N GLY A 669 2658 3496 3023 -415 112 -737 N ATOM 520 CA GLY A 669 -14.554 21.556 56.212 1.00 25.79 C ANISOU 520 CA GLY A 669 2861 3738 3202 -503 155 -840 C ATOM 521 C GLY A 669 -13.331 20.922 55.567 1.00 26.84 C ANISOU 521 C GLY A 669 3022 3905 3270 -426 -3 -645 C ATOM 522 O GLY A 669 -12.535 21.626 54.938 1.00 25.86 O ANISOU 522 O GLY A 669 2907 3683 3236 -385 9 -662 O ATOM 523 N GLU A 670 -13.198 19.593 55.681 1.00 26.08 N ANISOU 523 N GLU A 670 2920 3895 3095 -399 -99 -450 N ATOM 524 CA GLU A 670 -12.090 18.889 55.018 1.00 29.65 C ANISOU 524 CA GLU A 670 3361 4272 3632 -317 -135 -255 C ATOM 525 C GLU A 670 -12.114 19.091 53.517 1.00 27.75 C ANISOU 525 C GLU A 670 3227 3804 3514 -216 -87 -306 C ATOM 526 O GLU A 670 -11.055 19.257 52.880 1.00 27.68 O ANISOU 526 O GLU A 670 3230 3704 3583 -186 -63 -269 O ATOM 527 CB GLU A 670 -12.119 17.389 55.289 1.00 34.90 C ANISOU 527 CB GLU A 670 3957 4948 4357 -289 -127 -26 C ATOM 528 CG GLU A 670 -11.396 16.592 54.176 1.00 35.51 C ANISOU 528 CG GLU A 670 4053 4759 4678 -190 6 76 C ATOM 529 CD GLU A 670 -11.011 15.225 54.582 1.00 44.98 C ANISOU 529 CD GLU A 670 5089 5889 6111 -157 111 369 C ATOM 530 OE1 GLU A 670 -11.941 14.397 54.762 1.00 46.75 O ANISOU 530 OE1 GLU A 670 5323 6083 6355 -158 172 370 O ATOM 531 OE2 GLU A 670 -9.775 14.993 54.696 1.00 47.79 O ANISOU 531 OE2 GLU A 670 5270 6198 6688 -125 153 637 O ATOM 532 N ALA A 671 -13.305 19.054 52.923 1.00 26.02 N ANISOU 532 N ALA A 671 3063 3534 3291 -210 -81 -356 N ATOM 533 CA ALA A 671 -13.407 19.273 51.477 1.00 28.15 C ANISOU 533 CA ALA A 671 3399 3719 3579 -233 -74 -347 C ATOM 534 C ALA A 671 -13.055 20.700 51.078 1.00 27.24 C ANISOU 534 C ALA A 671 3236 3563 3552 -198 -97 -351 C ATOM 535 O ALA A 671 -12.450 20.934 50.032 1.00 28.83 O ANISOU 535 O ALA A 671 3478 3723 3753 -227 -96 -315 O ATOM 536 CB ALA A 671 -14.780 18.890 50.957 1.00 29.45 C ANISOU 536 CB ALA A 671 3573 3943 3675 -316 -107 -309 C ATOM 537 N SER A 672 -13.421 21.666 51.911 1.00 25.98 N ANISOU 537 N SER A 672 2982 3393 3498 -165 -63 -417 N ATOM 538 CA SER A 672 -13.112 23.048 51.607 1.00 27.56 C ANISOU 538 CA SER A 672 3101 3481 3891 -129 1 -429 C ATOM 539 C SER A 672 -11.595 23.255 51.664 1.00 27.56 C ANISOU 539 C SER A 672 3155 3478 3840 -135 6 -503 C ATOM 540 O SER A 672 -11.076 24.139 50.987 1.00 31.29 O ANISOU 540 O SER A 672 3596 3852 4443 -100 34 -476 O ATOM 541 CB SER A 672 -13.839 24.019 52.542 1.00 31.80 C ANISOU 541 CB SER A 672 3514 3921 4648 -139 181 -558 C ATOM 542 OG SER A 672 -13.307 23.955 53.849 1.00 42.58 O ANISOU 542 OG SER A 672 4927 5399 5853 -271 260 -798 O ATOM 543 N ILE A 673 -10.886 22.445 52.455 1.00 22.60 N ANISOU 543 N ILE A 673 2561 2970 3057 -185 -28 -528 N ATOM 544 CA ILE A 673 -9.417 22.525 52.441 1.00 22.75 C ANISOU 544 CA ILE A 673 2574 3006 3065 -198 -46 -496 C ATOM 545 C ILE A 673 -8.809 21.791 51.239 1.00 22.74 C ANISOU 545 C ILE A 673 2642 2878 3119 -129 -38 -377 C ATOM 546 O ILE A 673 -8.010 22.356 50.471 1.00 22.97 O ANISOU 546 O ILE A 673 2695 2814 3220 -103 -13 -378 O ATOM 547 CB ILE A 673 -8.809 22.017 53.778 1.00 23.52 C ANISOU 547 CB ILE A 673 2583 3340 3015 -330 -100 -435 C ATOM 548 CG1 ILE A 673 -9.221 22.960 54.933 1.00 26.85 C ANISOU 548 CG1 ILE A 673 2966 3927 3307 -538 -29 -669 C ATOM 549 CG2 ILE A 673 -7.298 22.028 53.673 1.00 22.29 C ANISOU 549 CG2 ILE A 673 2357 3213 2900 -342 -139 -293 C ATOM 550 CD1 ILE A 673 -8.929 22.400 56.372 1.00 31.21 C ANISOU 550 CD1 ILE A 673 3413 4871 3573 -809 -115 -584 C ATOM 551 N MET A 674 -9.161 20.519 51.093 1.00 21.11 N ANISOU 551 N MET A 674 2470 2651 2902 -134 -2 -306 N ATOM 552 CA MET A 674 -8.640 19.665 50.013 1.00 22.06 C ANISOU 552 CA MET A 674 2666 2607 3109 -155 142 -284 C ATOM 553 C MET A 674 -8.873 20.292 48.648 1.00 21.89 C ANISOU 553 C MET A 674 2751 2565 3002 -242 152 -365 C ATOM 554 O MET A 674 -7.993 20.218 47.766 1.00 23.16 O ANISOU 554 O MET A 674 2974 2615 3212 -297 277 -397 O ATOM 555 CB MET A 674 -9.330 18.288 50.070 1.00 22.96 C ANISOU 555 CB MET A 674 2803 2674 3248 -204 257 -272 C ATOM 556 CG MET A 674 -8.816 17.281 49.024 1.00 24.94 C ANISOU 556 CG MET A 674 3135 2691 3652 -306 557 -341 C ATOM 557 SD MET A 674 -9.694 15.684 49.162 1.00 28.87 S ANISOU 557 SD MET A 674 3645 3081 4244 -399 785 -383 S ATOM 558 CE MET A 674 -9.925 15.650 50.931 1.00 33.28 C ANISOU 558 CE MET A 674 3995 3810 4841 -208 545 -112 C ATOM 559 N GLY A 675 -10.038 20.926 48.476 1.00 20.08 N ANISOU 559 N GLY A 675 2503 2456 2670 -278 32 -347 N ATOM 560 CA GLY A 675 -10.426 21.479 47.184 1.00 21.80 C ANISOU 560 CA GLY A 675 2738 2759 2788 -419 -13 -276 C ATOM 561 C GLY A 675 -9.536 22.648 46.776 1.00 21.78 C ANISOU 561 C GLY A 675 2688 2695 2891 -353 -32 -228 C ATOM 562 O GLY A 675 -9.532 23.043 45.618 1.00 22.97 O ANISOU 562 O GLY A 675 2840 2935 2952 -498 -61 -125 O ATOM 563 N GLN A 676 -8.775 23.193 47.720 1.00 20.74 N ANISOU 563 N GLN A 676 2505 2460 2917 -189 -15 -291 N ATOM 564 CA GLN A 676 -7.860 24.296 47.396 1.00 20.51 C ANISOU 564 CA GLN A 676 2433 2350 3010 -132 -2 -278 C ATOM 565 C GLN A 676 -6.610 23.832 46.669 1.00 20.20 C ANISOU 565 C GLN A 676 2496 2236 2944 -177 85 -314 C ATOM 566 O GLN A 676 -5.893 24.665 46.077 1.00 21.18 O ANISOU 566 O GLN A 676 2605 2308 3136 -163 95 -286 O ATOM 567 CB GLN A 676 -7.467 25.064 48.653 1.00 20.50 C ANISOU 567 CB GLN A 676 2344 2306 3139 -46 25 -386 C ATOM 568 CG GLN A 676 -8.703 25.729 49.267 1.00 24.74 C ANISOU 568 CG GLN A 676 2769 2832 3798 -33 61 -406 C ATOM 569 CD GLN A 676 -8.374 26.642 50.415 1.00 26.97 C ANISOU 569 CD GLN A 676 2982 3067 4197 -68 199 -616 C ATOM 570 OE1 GLN A 676 -7.428 27.409 50.347 1.00 28.51 O ANISOU 570 OE1 GLN A 676 3159 3195 4479 -78 262 -687 O ATOM 571 NE2 GLN A 676 -9.171 26.582 51.463 1.00 26.92 N ANISOU 571 NE2 GLN A 676 2944 3108 4178 -142 280 -750 N ATOM 572 N PHE A 677 -6.356 22.515 46.687 1.00 19.59 N ANISOU 572 N PHE A 677 2597 2024 2821 7 125 -178 N ATOM 573 CA PHE A 677 -5.103 21.985 46.184 1.00 20.76 C ANISOU 573 CA PHE A 677 2759 2229 2901 -42 115 -132 C ATOM 574 C PHE A 677 -5.358 21.209 44.895 1.00 22.26 C ANISOU 574 C PHE A 677 2966 2451 3039 -9 83 -21 C ATOM 575 O PHE A 677 -6.384 20.501 44.740 1.00 25.78 O ANISOU 575 O PHE A 677 3402 2934 3458 38 59 -4 O ATOM 576 CB PHE A 677 -4.453 21.087 47.253 1.00 20.33 C ANISOU 576 CB PHE A 677 2666 2307 2750 -74 111 -194 C ATOM 577 CG PHE A 677 -4.306 21.753 48.576 1.00 22.71 C ANISOU 577 CG PHE A 677 2928 2642 3059 -114 138 -324 C ATOM 578 CD1 PHE A 677 -3.690 23.014 48.667 1.00 24.78 C ANISOU 578 CD1 PHE A 677 3190 2818 3408 -174 173 -406 C ATOM 579 CD2 PHE A 677 -4.791 21.155 49.742 1.00 19.65 C ANISOU 579 CD2 PHE A 677 2490 2382 2593 -104 136 -373 C ATOM 580 CE1 PHE A 677 -3.558 23.676 49.902 1.00 32.16 C ANISOU 580 CE1 PHE A 677 4072 3796 4349 -225 205 -574 C ATOM 581 CE2 PHE A 677 -4.652 21.803 50.972 1.00 23.02 C ANISOU 581 CE2 PHE A 677 2863 2887 2998 -150 163 -518 C ATOM 582 CZ PHE A 677 -4.068 23.059 51.059 1.00 25.42 C ANISOU 582 CZ PHE A 677 3164 3108 3386 -211 198 -637 C ATOM 583 N ASP A 678 -4.473 21.389 43.933 1.00 18.01 N ANISOU 583 N ASP A 678 2444 1913 2487 -41 87 43 N ATOM 584 CA ASP A 678 -4.558 20.619 42.719 1.00 18.42 C ANISOU 584 CA ASP A 678 2495 2038 2464 -24 63 114 C ATOM 585 C ASP A 678 -3.142 20.223 42.362 1.00 19.49 C ANISOU 585 C ASP A 678 2624 2236 2545 -75 79 112 C ATOM 586 O ASP A 678 -2.420 20.978 41.727 1.00 21.32 O ANISOU 586 O ASP A 678 2861 2453 2786 -115 98 167 O ATOM 587 CB ASP A 678 -5.168 21.500 41.610 1.00 17.66 C ANISOU 587 CB ASP A 678 2407 1906 2396 2 53 230 C ATOM 588 CG ASP A 678 -5.367 20.754 40.296 1.00 28.55 C ANISOU 588 CG ASP A 678 3766 3415 3665 12 25 288 C ATOM 589 OD1 ASP A 678 -5.090 19.544 40.207 1.00 24.78 O ANISOU 589 OD1 ASP A 678 3275 3023 3116 -1 21 215 O ATOM 590 OD2 ASP A 678 -5.827 21.410 39.326 1.00 32.27 O ANISOU 590 OD2 ASP A 678 4227 3908 4127 33 11 408 O ATOM 591 N HIS A 679 -2.747 19.031 42.788 1.00 17.54 N ANISOU 591 N HIS A 679 2354 2056 2254 -71 76 57 N ATOM 592 CA HIS A 679 -1.365 18.593 42.640 1.00 17.78 C ANISOU 592 CA HIS A 679 2360 2147 2249 -105 94 43 C ATOM 593 C HIS A 679 -1.366 17.064 42.592 1.00 17.26 C ANISOU 593 C HIS A 679 2265 2131 2162 -68 90 11 C ATOM 594 O HIS A 679 -2.183 16.405 43.267 1.00 16.48 O ANISOU 594 O HIS A 679 2161 2012 2089 -34 77 -4 O ATOM 595 CB HIS A 679 -0.559 19.081 43.861 1.00 18.16 C ANISOU 595 CB HIS A 679 2387 2193 2319 -144 106 0 C ATOM 596 CG HIS A 679 0.912 18.805 43.768 1.00 16.93 C ANISOU 596 CG HIS A 679 2188 2112 2130 -181 123 -8 C ATOM 597 ND1 HIS A 679 1.458 17.579 44.065 1.00 18.01 N ANISOU 597 ND1 HIS A 679 2278 2322 2243 -146 120 -17 N ATOM 598 CD2 HIS A 679 1.951 19.616 43.424 1.00 19.15 C ANISOU 598 CD2 HIS A 679 2456 2405 2414 -248 148 -1 C ATOM 599 CE1 HIS A 679 2.772 17.635 43.903 1.00 18.11 C ANISOU 599 CE1 HIS A 679 2246 2401 2235 -181 138 -22 C ATOM 600 NE2 HIS A 679 3.093 18.862 43.497 1.00 20.17 N ANISOU 600 NE2 HIS A 679 2526 2633 2503 -251 155 -16 N ATOM 601 N PRO A 680 -0.481 16.475 41.767 1.00 16.91 N ANISOU 601 N PRO A 680 2193 2147 2086 -76 110 -2 N ATOM 602 CA PRO A 680 -0.510 15.015 41.611 1.00 19.09 C ANISOU 602 CA PRO A 680 2434 2434 2384 -37 119 -51 C ATOM 603 C PRO A 680 -0.179 14.225 42.863 1.00 17.91 C ANISOU 603 C PRO A 680 2251 2260 2295 -5 122 -43 C ATOM 604 O PRO A 680 -0.500 13.026 42.914 1.00 18.95 O ANISOU 604 O PRO A 680 2358 2354 2490 33 132 -61 O ATOM 605 CB PRO A 680 0.581 14.737 40.576 1.00 19.32 C ANISOU 605 CB PRO A 680 2427 2539 2374 -53 152 -84 C ATOM 606 CG PRO A 680 1.416 15.940 40.543 1.00 25.04 C ANISOU 606 CG PRO A 680 3159 3297 3059 -104 158 -33 C ATOM 607 CD PRO A 680 0.520 17.108 40.902 1.00 17.91 C ANISOU 607 CD PRO A 680 2310 2327 2167 -122 133 22 C ATOM 608 N ASN A 681 0.448 14.861 43.870 1.00 14.88 N ANISOU 608 N ASN A 681 1854 1904 1895 -23 114 -13 N ATOM 609 CA ASN A 681 0.720 14.170 45.130 1.00 15.15 C ANISOU 609 CA ASN A 681 1838 1964 1956 9 109 25 C ATOM 610 C ASN A 681 -0.127 14.628 46.320 1.00 15.17 C ANISOU 610 C ASN A 681 1850 1978 1937 0 88 41 C ATOM 611 O ASN A 681 0.237 14.418 47.479 1.00 14.78 O ANISOU 611 O ASN A 681 1747 2007 1863 6 79 79 O ATOM 612 CB ASN A 681 2.222 14.229 45.477 1.00 15.54 C ANISOU 612 CB ASN A 681 1822 2102 1981 -1 116 38 C ATOM 613 CG ASN A 681 3.080 13.567 44.412 1.00 16.47 C ANISOU 613 CG ASN A 681 1908 2222 2129 22 147 15 C ATOM 614 OD1 ASN A 681 3.697 14.269 43.627 1.00 18.94 O ANISOU 614 OD1 ASN A 681 2228 2573 2397 -24 162 -17 O ATOM 615 ND2 ASN A 681 3.087 12.212 44.349 1.00 15.90 N ANISOU 615 ND2 ASN A 681 1793 2103 2144 92 167 27 N ATOM 616 N ILE A 682 -1.271 15.232 46.007 1.00 16.26 N ANISOU 616 N ILE A 682 2043 2058 2077 -11 80 15 N ATOM 617 CA ILE A 682 -2.241 15.583 47.029 1.00 14.80 C ANISOU 617 CA ILE A 682 1859 1883 1881 -11 70 11 C ATOM 618 C ILE A 682 -3.562 14.943 46.581 1.00 14.01 C ANISOU 618 C ILE A 682 1779 1720 1822 20 67 21 C ATOM 619 O ILE A 682 -3.941 15.048 45.409 1.00 15.24 O ANISOU 619 O ILE A 682 1968 1832 1990 21 63 1 O ATOM 620 CB ILE A 682 -2.382 17.117 47.182 1.00 15.67 C ANISOU 620 CB ILE A 682 1998 1975 1980 -52 72 -48 C ATOM 621 CG1 ILE A 682 -1.066 17.717 47.730 1.00 18.46 C ANISOU 621 CG1 ILE A 682 2315 2400 2299 -104 79 -83 C ATOM 622 CG2 ILE A 682 -3.530 17.429 48.140 1.00 17.50 C ANISOU 622 CG2 ILE A 682 2222 2218 2209 -42 71 -80 C ATOM 623 CD1 ILE A 682 -0.998 19.220 47.601 1.00 25.19 C ANISOU 623 CD1 ILE A 682 3195 3188 3188 -158 96 -151 C ATOM 624 N ILE A 683 -4.259 14.288 47.492 1.00 14.90 N ANISOU 624 N ILE A 683 1862 1854 1945 36 68 55 N ATOM 625 CA ILE A 683 -5.505 13.595 47.095 1.00 15.29 C ANISOU 625 CA ILE A 683 1916 1848 2045 51 69 58 C ATOM 626 C ILE A 683 -6.469 14.603 46.436 1.00 16.13 C ANISOU 626 C ILE A 683 2061 1930 2138 48 53 8 C ATOM 627 O ILE A 683 -6.722 15.693 46.988 1.00 18.10 O ANISOU 627 O ILE A 683 2318 2194 2363 46 51 -15 O ATOM 628 CB ILE A 683 -6.173 12.895 48.311 1.00 15.83 C ANISOU 628 CB ILE A 683 1937 1955 2125 57 80 121 C ATOM 629 CG1 ILE A 683 -5.383 11.642 48.707 1.00 21.62 C ANISOU 629 CG1 ILE A 683 2621 2683 2912 77 98 214 C ATOM 630 CG2 ILE A 683 -7.646 12.483 47.987 1.00 19.79 C ANISOU 630 CG2 ILE A 683 2436 2409 2673 55 82 106 C ATOM 631 CD1 ILE A 683 -5.514 10.474 47.699 1.00 21.84 C ANISOU 631 CD1 ILE A 683 2648 2584 3064 87 119 200 C ATOM 632 N ARG A 684 -6.981 14.232 45.257 1.00 17.76 N ANISOU 632 N ARG A 684 2277 2105 2364 51 44 -12 N ATOM 633 CA ARG A 684 -7.901 15.095 44.495 1.00 16.48 C ANISOU 633 CA ARG A 684 2132 1944 2184 60 21 -26 C ATOM 634 C ARG A 684 -9.321 15.020 45.009 1.00 16.20 C ANISOU 634 C ARG A 684 2069 1916 2169 75 15 -31 C ATOM 635 O ARG A 684 -9.841 13.912 45.231 1.00 17.80 O ANISOU 635 O ARG A 684 2238 2119 2405 62 24 -35 O ATOM 636 CB ARG A 684 -7.886 14.655 43.057 1.00 16.48 C ANISOU 636 CB ARG A 684 2129 1968 2164 49 10 -50 C ATOM 637 CG ARG A 684 -8.763 15.466 42.126 1.00 19.65 C ANISOU 637 CG ARG A 684 2528 2411 2526 64 -22 -30 C ATOM 638 CD ARG A 684 -8.441 15.027 40.686 1.00 23.50 C ANISOU 638 CD ARG A 684 2998 2980 2951 39 -31 -60 C ATOM 639 NE ARG A 684 -9.388 15.640 39.764 1.00 25.35 N ANISOU 639 NE ARG A 684 3205 3300 3125 54 -70 -21 N ATOM 640 CZ ARG A 684 -9.229 16.864 39.250 1.00 34.52 C ANISOU 640 CZ ARG A 684 4381 4482 4252 76 -85 82 C ATOM 641 NH1 ARG A 684 -8.158 17.586 39.552 1.00 33.74 N ANISOU 641 NH1 ARG A 684 4327 4314 4178 70 -59 128 N ATOM 642 NH2 ARG A 684 -10.135 17.366 38.411 1.00 35.40 N ANISOU 642 NH2 ARG A 684 4450 4689 4311 102 -126 149 N ATOM 643 N LEU A 685 -9.939 16.179 45.214 1.00 16.84 N ANISOU 643 N LEU A 685 2155 1993 2251 101 7 -30 N ATOM 644 CA LEU A 685 -11.373 16.197 45.534 1.00 16.78 C ANISOU 644 CA LEU A 685 2106 2007 2262 124 1 -40 C ATOM 645 C LEU A 685 -12.138 16.215 44.210 1.00 17.26 C ANISOU 645 C LEU A 685 2150 2096 2314 139 -36 -28 C ATOM 646 O LEU A 685 -11.987 17.166 43.406 1.00 18.71 O ANISOU 646 O LEU A 685 2351 2273 2487 166 -55 12 O ATOM 647 CB LEU A 685 -11.686 17.487 46.299 1.00 17.65 C ANISOU 647 CB LEU A 685 2214 2096 2396 158 15 -62 C ATOM 648 CG LEU A 685 -13.156 17.765 46.608 1.00 18.96 C ANISOU 648 CG LEU A 685 2327 2287 2590 198 15 -80 C ATOM 649 CD1 LEU A 685 -13.700 16.692 47.555 1.00 19.10 C ANISOU 649 CD1 LEU A 685 2296 2376 2585 167 36 -92 C ATOM 650 CD2 LEU A 685 -13.315 19.171 47.145 1.00 20.30 C ANISOU 650 CD2 LEU A 685 2493 2404 2816 242 40 -123 C ATOM 651 N GLU A 686 -12.935 15.178 43.955 1.00 17.47 N ANISOU 651 N GLU A 686 2130 2165 2343 115 -44 -55 N ATOM 652 CA GLU A 686 -13.788 15.198 42.772 1.00 18.27 C ANISOU 652 CA GLU A 686 2189 2341 2412 121 -85 -60 C ATOM 653 C GLU A 686 -15.012 16.084 42.973 1.00 19.93 C ANISOU 653 C GLU A 686 2353 2581 2638 180 -104 -29 C ATOM 654 O GLU A 686 -15.486 16.753 42.034 1.00 22.07 O ANISOU 654 O GLU A 686 2594 2912 2879 220 -145 20 O ATOM 655 CB GLU A 686 -14.155 13.757 42.344 1.00 18.17 C ANISOU 655 CB GLU A 686 2130 2364 2408 58 -82 -134 C ATOM 656 CG GLU A 686 -12.939 12.969 41.812 1.00 18.51 C ANISOU 656 CG GLU A 686 2205 2377 2452 17 -61 -179 C ATOM 657 CD GLU A 686 -12.374 13.527 40.500 1.00 22.22 C ANISOU 657 CD GLU A 686 2685 2930 2828 22 -89 -176 C ATOM 658 OE1 GLU A 686 -13.097 14.212 39.727 1.00 22.37 O ANISOU 658 OE1 GLU A 686 2667 3055 2777 44 -133 -141 O ATOM 659 OE2 GLU A 686 -11.207 13.225 40.195 1.00 23.84 O ANISOU 659 OE2 GLU A 686 2920 3113 3025 4 -65 -200 O ATOM 660 N GLY A 687 -15.528 16.124 44.192 1.00 18.83 N ANISOU 660 N GLY A 687 2195 2417 2542 191 -74 -47 N ATOM 661 CA GLY A 687 -16.633 17.027 44.477 1.00 18.56 C ANISOU 661 CA GLY A 687 2109 2403 2540 258 -80 -35 C ATOM 662 C GLY A 687 -17.380 16.584 45.722 1.00 18.99 C ANISOU 662 C GLY A 687 2114 2486 2617 243 -41 -80 C ATOM 663 O GLY A 687 -16.935 15.680 46.456 1.00 17.78 O ANISOU 663 O GLY A 687 1973 2328 2453 183 -9 -93 O ATOM 664 N VAL A 688 -18.470 17.286 45.977 1.00 19.13 N ANISOU 664 N VAL A 688 2065 2537 2666 305 -40 -88 N ATOM 665 CA VAL A 688 -19.326 16.995 47.104 1.00 18.04 C ANISOU 665 CA VAL A 688 1859 2458 2536 295 1 -132 C ATOM 666 C VAL A 688 -20.778 16.868 46.642 1.00 19.74 C ANISOU 666 C VAL A 688 1969 2768 2764 320 -26 -132 C ATOM 667 O VAL A 688 -21.175 17.379 45.567 1.00 20.98 O ANISOU 667 O VAL A 688 2097 2946 2928 375 -78 -92 O ATOM 668 CB VAL A 688 -19.214 18.101 48.217 1.00 21.93 C ANISOU 668 CB VAL A 688 2352 2920 3059 349 51 -188 C ATOM 669 CG1 VAL A 688 -17.757 18.207 48.752 1.00 20.11 C ANISOU 669 CG1 VAL A 688 2207 2632 2801 309 75 -203 C ATOM 670 CG2 VAL A 688 -19.717 19.472 47.705 1.00 22.25 C ANISOU 670 CG2 VAL A 688 2368 2899 3187 458 39 -185 C ATOM 671 N VAL A 689 -21.578 16.175 47.456 1.00 19.09 N ANISOU 671 N VAL A 689 1813 2763 2677 275 9 -162 N ATOM 672 CA VAL A 689 -23.045 16.224 47.286 1.00 21.80 C ANISOU 672 CA VAL A 689 2032 3213 3037 304 -4 -176 C ATOM 673 C VAL A 689 -23.609 16.825 48.573 1.00 23.72 C ANISOU 673 C VAL A 689 2217 3497 3298 350 60 -225 C ATOM 674 O VAL A 689 -23.459 16.240 49.654 1.00 23.23 O ANISOU 674 O VAL A 689 2151 3476 3200 284 116 -240 O ATOM 675 CB VAL A 689 -23.690 14.837 47.034 1.00 24.10 C ANISOU 675 CB VAL A 689 2257 3582 3317 194 -10 -184 C ATOM 676 CG1 VAL A 689 -25.221 14.992 46.868 1.00 25.86 C ANISOU 676 CG1 VAL A 689 2334 3939 3552 224 -27 -206 C ATOM 677 CG2 VAL A 689 -23.100 14.190 45.800 1.00 23.81 C ANISOU 677 CG2 VAL A 689 2268 3516 3264 139 -61 -182 C ATOM 678 N THR A 690 -24.232 18.002 48.456 1.00 24.96 N ANISOU 678 N THR A 690 2320 3652 3513 467 56 -245 N ATOM 679 CA THR A 690 -24.822 18.664 49.619 1.00 27.66 C ANISOU 679 CA THR A 690 2588 4037 3883 521 125 -329 C ATOM 680 C THR A 690 -26.334 18.931 49.458 1.00 31.02 C ANISOU 680 C THR A 690 2862 4569 4354 594 120 -343 C ATOM 681 O THR A 690 -27.071 19.096 50.445 1.00 32.96 O ANISOU 681 O THR A 690 3012 4908 4603 612 185 -422 O ATOM 682 CB THR A 690 -24.099 19.998 49.921 1.00 28.88 C ANISOU 682 CB THR A 690 2803 4059 4111 607 156 -384 C ATOM 683 OG1 THR A 690 -24.259 20.900 48.816 1.00 34.98 O ANISOU 683 OG1 THR A 690 3575 4732 4983 716 106 -317 O ATOM 684 CG2 THR A 690 -22.603 19.762 50.172 1.00 27.73 C ANISOU 684 CG2 THR A 690 2788 3837 3911 530 163 -381 C ATOM 685 N LYS A 691 -26.797 18.953 48.217 1.00 29.15 N ANISOU 685 N LYS A 691 2588 4350 4138 633 44 -268 N ATOM 686 CA LYS A 691 -28.192 19.276 47.933 1.00 32.03 C ANISOU 686 CA LYS A 691 2793 4830 4545 716 25 -262 C ATOM 687 C LYS A 691 -29.130 18.101 48.118 1.00 30.97 C ANISOU 687 C LYS A 691 2551 4869 4348 608 28 -286 C ATOM 688 O LYS A 691 -30.352 18.224 47.940 1.00 34.44 O ANISOU 688 O LYS A 691 2837 5439 4809 658 14 -291 O ATOM 689 CB LYS A 691 -28.313 19.895 46.545 1.00 33.10 C ANISOU 689 CB LYS A 691 2910 4949 4717 813 -63 -152 C ATOM 690 CG LYS A 691 -27.420 21.117 46.408 1.00 36.08 C ANISOU 690 CG LYS A 691 3385 5133 5191 917 -53 -110 C ATOM 691 CD LYS A 691 -27.744 21.935 45.184 1.00 43.80 C ANISOU 691 CD LYS A 691 4308 6104 6229 1044 -126 38 C ATOM 692 CE LYS A 691 -27.168 23.324 45.314 1.00 48.78 C ANISOU 692 CE LYS A 691 4996 6515 7022 1167 -86 73 C ATOM 693 NZ LYS A 691 -28.164 24.327 44.806 1.00 54.78 N ANISOU 693 NZ LYS A 691 5616 7274 7923 1348 -110 183 N ATOM 694 N SER A 692 -28.575 16.965 48.491 1.00 30.36 N ANISOU 694 N SER A 692 2540 4787 4207 461 52 -293 N ATOM 695 CA SER A 692 -29.372 15.806 48.850 1.00 31.99 C ANISOU 695 CA SER A 692 2650 5121 4382 338 78 -310 C ATOM 696 C SER A 692 -28.626 15.112 49.964 1.00 33.26 C ANISOU 696 C SER A 692 2888 5242 4508 236 152 -306 C ATOM 697 O SER A 692 -27.428 15.338 50.152 1.00 31.17 O ANISOU 697 O SER A 692 2754 4861 4229 246 158 -291 O ATOM 698 CB SER A 692 -29.597 14.867 47.654 1.00 31.98 C ANISOU 698 CB SER A 692 2622 5163 4367 244 7 -290 C ATOM 699 OG SER A 692 -28.371 14.346 47.157 1.00 31.26 O ANISOU 699 OG SER A 692 2673 4945 4259 178 -15 -268 O ATOM 700 N LYS A 693 -29.335 14.267 50.691 1.00 32.29 N ANISOU 700 N LYS A 693 2670 5229 4369 138 208 -303 N ATOM 701 CA LYS A 693 -28.768 13.602 51.841 1.00 34.35 C ANISOU 701 CA LYS A 693 2971 5493 4587 47 282 -260 C ATOM 702 C LYS A 693 -28.858 12.085 51.619 1.00 36.32 C ANISOU 702 C LYS A 693 3206 5719 4875 -111 289 -191 C ATOM 703 O LYS A 693 -29.828 11.616 51.026 1.00 36.22 O ANISOU 703 O LYS A 693 3090 5767 4905 -165 268 -215 O ATOM 704 CB LYS A 693 -29.510 14.054 53.110 1.00 34.66 C ANISOU 704 CB LYS A 693 2895 5699 4576 75 365 -303 C ATOM 705 CG LYS A 693 -29.351 15.570 53.436 1.00 33.00 C ANISOU 705 CG LYS A 693 2695 5481 4362 229 378 -408 C ATOM 706 CD LYS A 693 -30.242 15.990 54.607 1.00 39.22 C ANISOU 706 CD LYS A 693 3338 6459 5104 257 469 -493 C ATOM 707 CE LYS A 693 -30.169 17.485 54.896 1.00 40.28 C ANISOU 707 CE LYS A 693 3465 6561 5277 409 495 -634 C ATOM 708 NZ LYS A 693 -30.930 17.870 56.139 1.00 39.93 N ANISOU 708 NZ LYS A 693 3275 6721 5176 428 599 -753 N ATOM 709 N PRO A 694 -27.854 11.310 52.086 1.00 35.75 N ANISOU 709 N PRO A 694 3225 5556 4803 -188 321 -107 N ATOM 710 CA PRO A 694 -26.700 11.729 52.868 1.00 33.74 C ANISOU 710 CA PRO A 694 3070 5267 4482 -145 345 -71 C ATOM 711 C PRO A 694 -25.753 12.626 52.086 1.00 30.43 C ANISOU 711 C PRO A 694 2773 4726 4063 -46 280 -125 C ATOM 712 O PRO A 694 -25.577 12.451 50.870 1.00 28.87 O ANISOU 712 O PRO A 694 2621 4432 3917 -47 217 -140 O ATOM 713 CB PRO A 694 -25.971 10.409 53.164 1.00 36.58 C ANISOU 713 CB PRO A 694 3475 5541 4881 -258 376 58 C ATOM 714 CG PRO A 694 -26.996 9.320 52.927 1.00 38.66 C ANISOU 714 CG PRO A 694 3635 5817 5238 -376 401 89 C ATOM 715 CD PRO A 694 -27.820 9.858 51.806 1.00 37.95 C ANISOU 715 CD PRO A 694 3498 5752 5171 -331 336 -40 C ATOM 716 N VAL A 695 -25.148 13.569 52.802 1.00 27.06 N ANISOU 716 N VAL A 695 2389 4320 3574 27 302 -160 N ATOM 717 CA VAL A 695 -24.122 14.452 52.258 1.00 25.04 C ANISOU 717 CA VAL A 695 2247 3941 3325 106 258 -199 C ATOM 718 C VAL A 695 -22.905 13.578 51.969 1.00 23.66 C ANISOU 718 C VAL A 695 2177 3656 3156 39 239 -117 C ATOM 719 O VAL A 695 -22.618 12.639 52.721 1.00 22.96 O ANISOU 719 O VAL A 695 2077 3600 3046 -39 280 -31 O ATOM 720 CB VAL A 695 -23.797 15.548 53.310 1.00 26.59 C ANISOU 720 CB VAL A 695 2441 4198 3464 169 305 -282 C ATOM 721 CG1 VAL A 695 -22.655 16.430 52.879 1.00 29.91 C ANISOU 721 CG1 VAL A 695 2975 4482 3907 228 273 -320 C ATOM 722 CG2 VAL A 695 -25.053 16.383 53.565 1.00 28.92 C ANISOU 722 CG2 VAL A 695 2617 4587 3783 246 336 -381 C ATOM 723 N MET A 696 -22.207 13.854 50.866 1.00 22.76 N ANISOU 723 N MET A 696 2153 3418 3077 73 180 -129 N ATOM 724 CA MET A 696 -21.089 12.986 50.463 1.00 24.32 C ANISOU 724 CA MET A 696 2436 3510 3294 16 165 -70 C ATOM 725 C MET A 696 -19.866 13.806 50.084 1.00 23.00 C ANISOU 725 C MET A 696 2373 3259 3107 72 136 -89 C ATOM 726 O MET A 696 -19.981 14.928 49.589 1.00 20.77 O ANISOU 726 O MET A 696 2106 2957 2830 148 108 -139 O ATOM 727 CB MET A 696 -21.478 12.155 49.232 1.00 26.28 C ANISOU 727 CB MET A 696 2670 3705 3608 -34 127 -80 C ATOM 728 CG MET A 696 -22.493 11.071 49.442 1.00 30.70 C ANISOU 728 CG MET A 696 3132 4309 4222 -125 159 -63 C ATOM 729 SD MET A 696 -22.692 10.152 47.863 1.00 33.78 S ANISOU 729 SD MET A 696 3510 4634 4691 -199 114 -133 S ATOM 730 CE MET A 696 -21.279 10.705 46.968 1.00 40.50 C ANISOU 730 CE MET A 696 4486 5397 5503 -136 65 -153 C ATOM 731 N ILE A 697 -18.683 13.237 50.327 1.00 19.70 N ANISOU 731 N ILE A 697 2017 2788 2680 36 145 -35 N ATOM 732 CA ILE A 697 -17.448 13.813 49.789 1.00 20.13 C ANISOU 732 CA ILE A 697 2165 2760 2724 70 116 -50 C ATOM 733 C ILE A 697 -16.821 12.741 48.879 1.00 18.58 C ANISOU 733 C ILE A 697 2008 2474 2579 25 98 -17 C ATOM 734 O ILE A 697 -16.688 11.564 49.284 1.00 19.89 O ANISOU 734 O ILE A 697 2151 2619 2787 -31 128 45 O ATOM 735 CB ILE A 697 -16.460 14.178 50.913 1.00 22.32 C ANISOU 735 CB ILE A 697 2465 3079 2938 72 145 -37 C ATOM 736 CG1 ILE A 697 -17.026 15.352 51.742 1.00 23.53 C ANISOU 736 CG1 ILE A 697 2573 3318 3049 114 173 -124 C ATOM 737 CG2 ILE A 697 -15.065 14.471 50.337 1.00 21.95 C ANISOU 737 CG2 ILE A 697 2504 2946 2891 82 119 -37 C ATOM 738 CD1 ILE A 697 -16.176 15.686 52.986 1.00 22.89 C ANISOU 738 CD1 ILE A 697 2485 3336 2878 96 206 -147 C ATOM 739 N VAL A 698 -16.483 13.140 47.648 1.00 17.24 N ANISOU 739 N VAL A 698 1883 2255 2412 48 55 -55 N ATOM 740 CA VAL A 698 -15.988 12.183 46.655 1.00 16.15 C ANISOU 740 CA VAL A 698 1766 2056 2315 5 42 -68 C ATOM 741 C VAL A 698 -14.552 12.564 46.263 1.00 18.47 C ANISOU 741 C VAL A 698 2137 2299 2582 27 32 -61 C ATOM 742 O VAL A 698 -14.285 13.698 45.840 1.00 18.25 O ANISOU 742 O VAL A 698 2144 2281 2508 72 6 -69 O ATOM 743 CB VAL A 698 -16.897 12.166 45.377 1.00 17.84 C ANISOU 743 CB VAL A 698 1937 2316 2525 -5 0 -131 C ATOM 744 CG1 VAL A 698 -16.408 11.087 44.383 1.00 17.83 C ANISOU 744 CG1 VAL A 698 1940 2272 2563 -65 -1 -191 C ATOM 745 CG2 VAL A 698 -18.378 11.900 45.735 1.00 17.78 C ANISOU 745 CG2 VAL A 698 1835 2378 2540 -28 7 -145 C ATOM 746 N THR A 699 -13.643 11.613 46.433 1.00 16.70 N ANISOU 746 N THR A 699 1930 2015 2401 -2 58 -36 N ATOM 747 CA THR A 699 -12.207 11.855 46.257 1.00 17.54 C ANISOU 747 CA THR A 699 2092 2088 2485 16 57 -23 C ATOM 748 C THR A 699 -11.573 10.796 45.364 1.00 17.96 C ANISOU 748 C THR A 699 2147 2075 2603 -11 68 -61 C ATOM 749 O THR A 699 -12.191 9.769 45.028 1.00 16.90 O ANISOU 749 O THR A 699 1970 1900 2550 -52 85 -102 O ATOM 750 CB THR A 699 -11.440 11.910 47.625 1.00 17.78 C ANISOU 750 CB THR A 699 2122 2138 2494 27 82 52 C ATOM 751 OG1 THR A 699 -11.685 10.693 48.357 1.00 20.74 O ANISOU 751 OG1 THR A 699 2448 2495 2937 0 117 127 O ATOM 752 CG2 THR A 699 -11.929 13.082 48.449 1.00 19.07 C ANISOU 752 CG2 THR A 699 2278 2379 2587 49 79 39 C ATOM 753 N GLU A 700 -10.329 11.028 44.942 1.00 19.13 N ANISOU 753 N GLU A 700 2334 2209 2725 6 66 -67 N ATOM 754 CA GLU A 700 -9.726 10.039 44.039 1.00 20.32 C ANISOU 754 CA GLU A 700 2474 2305 2941 -14 87 -132 C ATOM 755 C GLU A 700 -9.530 8.691 44.734 1.00 19.91 C ANISOU 755 C GLU A 700 2384 2147 3032 -24 136 -89 C ATOM 756 O GLU A 700 -9.265 8.608 45.939 1.00 20.71 O ANISOU 756 O GLU A 700 2477 2245 3149 -3 149 30 O ATOM 757 CB GLU A 700 -8.454 10.551 43.346 1.00 27.58 C ANISOU 757 CB GLU A 700 3428 3251 3800 4 81 -153 C ATOM 758 CG GLU A 700 -7.192 10.260 43.981 1.00 24.87 C ANISOU 758 CG GLU A 700 3088 2869 3492 28 107 -97 C ATOM 759 CD GLU A 700 -6.003 10.973 43.303 1.00 19.29 C ANISOU 759 CD GLU A 700 2408 2212 2709 37 100 -118 C ATOM 760 OE1 GLU A 700 -5.393 10.438 42.345 1.00 21.94 O ANISOU 760 OE1 GLU A 700 2727 2546 3063 30 121 -193 O ATOM 761 OE2 GLU A 700 -5.669 12.072 43.797 1.00 16.94 O ANISOU 761 OE2 GLU A 700 2140 1958 2341 43 81 -66 O ATOM 762 N TYR A 701 -9.720 7.644 43.954 1.00 18.83 N ANISOU 762 N TYR A 701 2047 2086 3020 16 -290 86 N ATOM 763 CA TYR A 701 -9.601 6.289 44.462 1.00 19.22 C ANISOU 763 CA TYR A 701 2141 2092 3069 -7 -343 71 C ATOM 764 C TYR A 701 -8.131 5.895 44.560 1.00 16.83 C ANISOU 764 C TYR A 701 1929 1855 2612 60 -281 41 C ATOM 765 O TYR A 701 -7.353 6.136 43.625 1.00 18.62 O ANISOU 765 O TYR A 701 2233 2130 2712 169 -275 38 O ATOM 766 CB TYR A 701 -10.339 5.356 43.501 1.00 19.67 C ANISOU 766 CB TYR A 701 2272 2029 3175 17 -571 45 C ATOM 767 CG TYR A 701 -10.218 3.915 43.863 1.00 22.44 C ANISOU 767 CG TYR A 701 2666 2296 3564 -1 -682 32 C ATOM 768 CD1 TYR A 701 -10.880 3.394 44.982 1.00 23.52 C ANISOU 768 CD1 TYR A 701 2664 2386 3888 -118 -658 128 C ATOM 769 CD2 TYR A 701 -9.417 3.061 43.097 1.00 24.36 C ANISOU 769 CD2 TYR A 701 3086 2513 3654 122 -805 -59 C ATOM 770 CE1 TYR A 701 -10.751 2.038 45.310 1.00 27.44 C ANISOU 770 CE1 TYR A 701 3179 2790 4457 -143 -776 144 C ATOM 771 CE2 TYR A 701 -9.300 1.742 43.415 1.00 26.65 C ANISOU 771 CE2 TYR A 701 3418 2705 4003 107 -936 -80 C ATOM 772 CZ TYR A 701 -9.961 1.236 44.511 1.00 27.55 C ANISOU 772 CZ TYR A 701 3376 2754 4339 -41 -930 26 C ATOM 773 OH TYR A 701 -9.797 -0.095 44.806 1.00 32.57 O ANISOU 773 OH TYR A 701 4037 3279 5059 -60 -1074 28 O ATOM 774 N MET A 702 -7.762 5.205 45.646 1.00 16.64 N ANISOU 774 N MET A 702 1891 1833 2598 12 -233 44 N ATOM 775 CA MET A 702 -6.362 4.824 45.895 1.00 14.49 C ANISOU 775 CA MET A 702 1685 1612 2209 60 -174 27 C ATOM 776 C MET A 702 -6.361 3.360 46.257 1.00 14.57 C ANISOU 776 C MET A 702 1745 1561 2231 39 -259 12 C ATOM 777 O MET A 702 -6.679 2.979 47.409 1.00 18.89 O ANISOU 777 O MET A 702 2222 2101 2855 -41 -218 54 O ATOM 778 CB MET A 702 -5.737 5.692 47.023 1.00 14.86 C ANISOU 778 CB MET A 702 1661 1716 2268 26 -43 44 C ATOM 779 CG MET A 702 -5.784 7.207 46.694 1.00 16.53 C ANISOU 779 CG MET A 702 1805 1949 2526 40 -3 63 C ATOM 780 SD MET A 702 -4.699 7.683 45.341 1.00 18.11 S ANISOU 780 SD MET A 702 2025 2192 2666 143 11 133 S ATOM 781 CE MET A 702 -3.099 7.666 46.172 1.00 19.89 C ANISOU 781 CE MET A 702 2226 2430 2901 148 69 170 C ATOM 782 N GLU A 703 -6.046 2.525 45.269 1.00 17.16 N ANISOU 782 N GLU A 703 2197 1844 2479 134 -386 -40 N ATOM 783 CA GLU A 703 -6.289 1.078 45.409 1.00 19.64 C ANISOU 783 CA GLU A 703 2560 2045 2857 116 -546 -66 C ATOM 784 C GLU A 703 -5.588 0.415 46.615 1.00 20.91 C ANISOU 784 C GLU A 703 2688 2228 3029 55 -464 -32 C ATOM 785 O GLU A 703 -6.169 -0.492 47.255 1.00 20.77 O ANISOU 785 O GLU A 703 2613 2125 3155 -29 -546 20 O ATOM 786 CB GLU A 703 -5.903 0.401 44.102 1.00 21.16 C ANISOU 786 CB GLU A 703 2935 2190 2916 289 -713 -165 C ATOM 787 CG GLU A 703 -5.996 -1.112 44.101 1.00 30.46 C ANISOU 787 CG GLU A 703 4195 3218 4163 304 -936 -224 C ATOM 788 CD GLU A 703 -5.669 -1.664 42.732 1.00 32.48 C ANISOU 788 CD GLU A 703 4673 3425 4243 538 -1127 -358 C ATOM 789 OE1 GLU A 703 -6.145 -1.092 41.738 1.00 42.54 O ANISOU 789 OE1 GLU A 703 6017 4705 5441 641 -1197 -396 O ATOM 790 OE2 GLU A 703 -4.951 -2.669 42.647 1.00 45.53 O ANISOU 790 OE2 GLU A 703 6443 5037 5819 642 -1212 -429 O ATOM 791 N ASN A 704 -4.393 0.913 46.940 1.00 18.48 N ANISOU 791 N ASN A 704 2394 2025 2602 94 -313 -33 N ATOM 792 CA ASN A 704 -3.536 0.322 47.955 1.00 18.25 C ANISOU 792 CA ASN A 704 2361 2017 2556 61 -253 -14 C ATOM 793 C ASN A 704 -3.651 0.938 49.341 1.00 21.17 C ANISOU 793 C ASN A 704 2633 2445 2966 -23 -127 40 C ATOM 794 O ASN A 704 -2.933 0.539 50.280 1.00 19.86 O ANISOU 794 O ASN A 704 2473 2302 2772 -40 -83 55 O ATOM 795 CB ASN A 704 -2.089 0.203 47.450 1.00 18.43 C ANISOU 795 CB ASN A 704 2466 2088 2448 177 -211 -38 C ATOM 796 CG ASN A 704 -1.949 -0.828 46.342 1.00 19.67 C ANISOU 796 CG ASN A 704 2759 2188 2525 312 -351 -106 C ATOM 797 OD1 ASN A 704 -1.356 -0.572 45.281 1.00 23.63 O ANISOU 797 OD1 ASN A 704 3341 2748 2889 479 -324 -118 O ATOM 798 ND2 ASN A 704 -2.498 -2.002 46.577 1.00 17.20 N ANISOU 798 ND2 ASN A 704 2476 1757 2301 266 -512 -140 N ATOM 799 N GLY A 705 -4.582 1.881 49.492 1.00 19.72 N ANISOU 799 N GLY A 705 2375 2283 2836 -53 -82 63 N ATOM 800 CA GLY A 705 -4.961 2.355 50.837 1.00 18.98 C ANISOU 800 CA GLY A 705 2211 2246 2754 -80 22 107 C ATOM 801 C GLY A 705 -3.890 3.150 51.549 1.00 17.20 C ANISOU 801 C GLY A 705 2018 2072 2445 -40 85 59 C ATOM 802 O GLY A 705 -3.052 3.797 50.901 1.00 18.54 O ANISOU 802 O GLY A 705 2207 2233 2603 -13 69 25 O ATOM 803 N SER A 706 -3.912 3.099 52.887 1.00 17.96 N ANISOU 803 N SER A 706 2116 2215 2495 -20 142 77 N ATOM 804 CA SER A 706 -2.935 3.871 53.689 1.00 18.09 C ANISOU 804 CA SER A 706 2183 2246 2443 35 139 8 C ATOM 805 C SER A 706 -1.539 3.273 53.571 1.00 19.15 C ANISOU 805 C SER A 706 2364 2344 2569 18 87 -1 C ATOM 806 O SER A 706 -1.382 2.036 53.539 1.00 18.25 O ANISOU 806 O SER A 706 2267 2224 2444 -13 82 39 O ATOM 807 CB SER A 706 -3.354 3.889 55.159 1.00 22.29 C ANISOU 807 CB SER A 706 2742 2850 2878 115 201 20 C ATOM 808 OG SER A 706 -4.646 4.491 55.251 1.00 33.90 O ANISOU 808 OG SER A 706 4155 4367 4358 161 274 51 O ATOM 809 N LEU A 707 -0.540 4.149 53.504 1.00 17.18 N ANISOU 809 N LEU A 707 2116 2054 2357 39 36 -37 N ATOM 810 CA LEU A 707 0.827 3.714 53.217 1.00 16.39 C ANISOU 810 CA LEU A 707 2021 1916 2292 30 -1 -7 C ATOM 811 C LEU A 707 1.393 2.845 54.337 1.00 17.22 C ANISOU 811 C LEU A 707 2187 2022 2334 30 -24 -15 C ATOM 812 O LEU A 707 2.108 1.877 54.057 1.00 16.85 O ANISOU 812 O LEU A 707 2150 1963 2289 13 -24 23 O ATOM 813 CB LEU A 707 1.731 4.926 52.970 1.00 15.35 C ANISOU 813 CB LEU A 707 1829 1719 2286 45 -67 12 C ATOM 814 CG LEU A 707 3.219 4.622 52.655 1.00 17.84 C ANISOU 814 CG LEU A 707 2100 1991 2688 49 -92 101 C ATOM 815 CD1 LEU A 707 3.334 3.803 51.384 1.00 19.64 C ANISOU 815 CD1 LEU A 707 2321 2278 2865 82 4 176 C ATOM 816 CD2 LEU A 707 3.920 5.976 52.472 1.00 18.14 C ANISOU 816 CD2 LEU A 707 2026 1938 2927 53 -179 167 C ATOM 817 N ASP A 708 1.084 3.158 55.592 1.00 16.62 N ANISOU 817 N ASP A 708 2163 1967 2185 75 -42 -64 N ATOM 818 CA ASP A 708 1.689 2.371 56.674 1.00 15.73 C ANISOU 818 CA ASP A 708 2119 1864 1996 96 -70 -63 C ATOM 819 C ASP A 708 1.184 0.922 56.653 1.00 18.81 C ANISOU 819 C ASP A 708 2498 2304 2346 52 8 21 C ATOM 820 O ASP A 708 1.991 -0.026 56.776 1.00 19.67 O ANISOU 820 O ASP A 708 2626 2386 2463 21 -21 51 O ATOM 821 CB ASP A 708 1.482 3.036 58.045 1.00 20.84 C ANISOU 821 CB ASP A 708 2858 2537 2525 212 -116 -139 C ATOM 822 CG ASP A 708 0.011 3.108 58.469 1.00 25.20 C ANISOU 822 CG ASP A 708 3411 3202 2960 288 10 -112 C ATOM 823 OD1 ASP A 708 -0.886 3.349 57.636 1.00 23.52 O ANISOU 823 OD1 ASP A 708 3116 3005 2813 245 80 -78 O ATOM 824 OD2 ASP A 708 -0.253 2.914 59.671 1.00 29.86 O ANISOU 824 OD2 ASP A 708 4082 3876 3388 411 45 -105 O ATOM 825 N SER A 709 -0.136 0.751 56.512 1.00 19.37 N ANISOU 825 N SER A 709 2524 2427 2409 46 86 72 N ATOM 826 CA SER A 709 -0.696 -0.615 56.497 1.00 20.54 C ANISOU 826 CA SER A 709 2630 2583 2593 -6 115 182 C ATOM 827 C SER A 709 -0.246 -1.357 55.240 1.00 21.25 C ANISOU 827 C SER A 709 2715 2586 2774 -68 41 166 C ATOM 828 O SER A 709 -0.005 -2.545 55.305 1.00 20.22 O ANISOU 828 O SER A 709 2587 2417 2678 -101 -1 212 O ATOM 829 CB SER A 709 -2.222 -0.609 56.634 1.00 23.74 C ANISOU 829 CB SER A 709 2950 3039 3032 1 196 284 C ATOM 830 OG SER A 709 -2.837 0.144 55.609 1.00 27.30 O ANISOU 830 OG SER A 709 3362 3460 3552 -19 184 239 O ATOM 831 N PHE A 710 -0.147 -0.661 54.107 1.00 18.45 N ANISOU 831 N PHE A 710 2358 2204 2447 -59 22 106 N ATOM 832 CA PHE A 710 0.373 -1.289 52.870 1.00 17.07 C ANISOU 832 CA PHE A 710 2213 1974 2298 -46 -38 83 C ATOM 833 C PHE A 710 1.810 -1.804 53.044 1.00 16.84 C ANISOU 833 C PHE A 710 2223 1929 2247 -20 -53 80 C ATOM 834 O PHE A 710 2.126 -2.960 52.711 1.00 18.24 O ANISOU 834 O PHE A 710 2438 2062 2431 -7 -108 81 O ATOM 835 CB PHE A 710 0.290 -0.291 51.700 1.00 17.42 C ANISOU 835 CB PHE A 710 2248 2027 2343 0 -25 51 C ATOM 836 CG PHE A 710 0.827 -0.832 50.389 1.00 16.70 C ANISOU 836 CG PHE A 710 2212 1914 2218 85 -64 34 C ATOM 837 CD1 PHE A 710 0.081 -1.762 49.639 1.00 16.90 C ANISOU 837 CD1 PHE A 710 2295 1880 2248 111 -170 -3 C ATOM 838 CD2 PHE A 710 2.046 -0.379 49.889 1.00 16.72 C ANISOU 838 CD2 PHE A 710 2210 1950 2195 167 -9 67 C ATOM 839 CE1 PHE A 710 0.561 -2.252 48.418 1.00 17.95 C ANISOU 839 CE1 PHE A 710 2525 1998 2299 253 -226 -48 C ATOM 840 CE2 PHE A 710 2.537 -0.839 48.686 1.00 16.33 C ANISOU 840 CE2 PHE A 710 2220 1915 2070 306 -10 72 C ATOM 841 CZ PHE A 710 1.787 -1.804 47.937 1.00 18.31 C ANISOU 841 CZ PHE A 710 2576 2118 2263 368 -122 -9 C ATOM 842 N LEU A 711 2.695 -0.966 53.578 1.00 16.50 N ANISOU 842 N LEU A 711 2167 1900 2201 -8 -32 79 N ATOM 843 CA LEU A 711 4.093 -1.409 53.752 1.00 15.71 C ANISOU 843 CA LEU A 711 2078 1771 2121 10 -54 103 C ATOM 844 C LEU A 711 4.223 -2.535 54.775 1.00 16.64 C ANISOU 844 C LEU A 711 2234 1877 2213 -27 -87 115 C ATOM 845 O LEU A 711 5.087 -3.399 54.626 1.00 18.41 O ANISOU 845 O LEU A 711 2474 2067 2454 -13 -113 134 O ATOM 846 CB LEU A 711 4.964 -0.229 54.160 1.00 15.95 C ANISOU 846 CB LEU A 711 2064 1778 2220 19 -78 117 C ATOM 847 CG LEU A 711 5.129 0.858 53.088 1.00 16.29 C ANISOU 847 CG LEU A 711 2029 1819 2340 57 -47 162 C ATOM 848 CD1 LEU A 711 6.009 1.971 53.675 1.00 20.52 C ANISOU 848 CD1 LEU A 711 2496 2280 3019 46 -132 196 C ATOM 849 CD2 LEU A 711 5.752 0.321 51.791 1.00 19.44 C ANISOU 849 CD2 LEU A 711 2407 2246 2734 142 20 240 C ATOM 850 N ARG A 712 3.388 -2.537 55.815 1.00 16.82 N ANISOU 850 N ARG A 712 2265 1937 2190 -54 -75 125 N ATOM 851 CA ARG A 712 3.438 -3.642 56.790 1.00 17.98 C ANISOU 851 CA ARG A 712 2432 2088 2313 -78 -90 181 C ATOM 852 C ARG A 712 3.107 -4.989 56.152 1.00 19.47 C ANISOU 852 C ARG A 712 2603 2220 2574 -115 -133 222 C ATOM 853 O ARG A 712 3.599 -6.051 56.608 1.00 21.86 O ANISOU 853 O ARG A 712 2916 2487 2902 -136 -177 265 O ATOM 854 CB ARG A 712 2.488 -3.410 57.948 1.00 18.61 C ANISOU 854 CB ARG A 712 2510 2249 2311 -54 -33 233 C ATOM 855 CG ARG A 712 3.075 -2.374 58.906 1.00 21.10 C ANISOU 855 CG ARG A 712 2898 2593 2526 23 -57 164 C ATOM 856 CD ARG A 712 2.410 -2.413 60.235 1.00 26.92 C ANISOU 856 CD ARG A 712 3677 3434 3117 113 3 220 C ATOM 857 NE ARG A 712 1.091 -1.849 60.103 1.00 27.45 N ANISOU 857 NE ARG A 712 3697 3573 3160 155 102 252 N ATOM 858 CZ ARG A 712 0.792 -0.555 60.265 1.00 30.66 C ANISOU 858 CZ ARG A 712 4148 4006 3495 248 102 156 C ATOM 859 NH1 ARG A 712 1.732 0.329 60.547 1.00 28.38 N ANISOU 859 NH1 ARG A 712 3950 3654 3178 301 -25 19 N ATOM 860 NH2 ARG A 712 -0.462 -0.146 60.116 1.00 29.08 N ANISOU 860 NH2 ARG A 712 3888 3874 3285 286 206 206 N ATOM 861 N LYS A 713 2.292 -4.949 55.099 1.00 18.54 N ANISOU 861 N LYS A 713 2466 2074 2504 -114 -152 200 N ATOM 862 CA LYS A 713 1.944 -6.198 54.376 1.00 19.27 C ANISOU 862 CA LYS A 713 2564 2067 2689 -126 -265 206 C ATOM 863 C LYS A 713 3.086 -6.682 53.473 1.00 20.53 C ANISOU 863 C LYS A 713 2803 2178 2818 -42 -321 125 C ATOM 864 O LYS A 713 3.043 -7.797 52.931 1.00 22.53 O ANISOU 864 O LYS A 713 3099 2333 3127 -11 -450 96 O ATOM 865 CB LYS A 713 0.701 -5.981 53.527 1.00 20.60 C ANISOU 865 CB LYS A 713 2705 2199 2923 -131 -314 196 C ATOM 866 CG LYS A 713 -0.573 -5.933 54.371 1.00 24.44 C ANISOU 866 CG LYS A 713 3080 2711 3496 -204 -272 331 C ATOM 867 CD LYS A 713 -1.713 -5.419 53.558 1.00 36.70 C ANISOU 867 CD LYS A 713 4591 4233 5119 -210 -306 323 C ATOM 868 CE LYS A 713 -3.009 -5.418 54.312 1.00 43.85 C ANISOU 868 CE LYS A 713 5353 5162 6144 -266 -252 499 C ATOM 869 NZ LYS A 713 -4.115 -5.031 53.365 1.00 50.48 N ANISOU 869 NZ LYS A 713 6145 5936 7100 -282 -327 492 N ATOM 870 N HIS A 714 4.077 -5.831 53.249 1.00 19.06 N ANISOU 870 N HIS A 714 2630 2051 2562 18 -237 101 N ATOM 871 CA HIS A 714 5.105 -6.117 52.244 1.00 18.50 C ANISOU 871 CA HIS A 714 2610 1968 2451 145 -239 68 C ATOM 872 C HIS A 714 6.513 -5.889 52.792 1.00 20.52 C ANISOU 872 C HIS A 714 2830 2248 2719 155 -177 125 C ATOM 873 O HIS A 714 7.391 -5.416 52.097 1.00 19.65 O ANISOU 873 O HIS A 714 2696 2170 2598 257 -109 163 O ATOM 874 CB HIS A 714 4.850 -5.242 51.002 1.00 19.27 C ANISOU 874 CB HIS A 714 2722 2113 2488 248 -191 42 C ATOM 875 CG HIS A 714 3.552 -5.547 50.343 1.00 19.28 C ANISOU 875 CG HIS A 714 2772 2065 2491 254 -294 -23 C ATOM 876 ND1 HIS A 714 3.315 -6.746 49.699 1.00 19.90 N ANISOU 876 ND1 HIS A 714 2947 2044 2571 335 -453 -97 N ATOM 877 CD2 HIS A 714 2.395 -4.842 50.276 1.00 20.10 C ANISOU 877 CD2 HIS A 714 2836 2177 2624 190 -295 -23 C ATOM 878 CE1 HIS A 714 2.072 -6.755 49.248 1.00 19.63 C ANISOU 878 CE1 HIS A 714 2926 1947 2588 310 -568 -136 C ATOM 879 NE2 HIS A 714 1.494 -5.616 49.583 1.00 19.22 N ANISOU 879 NE2 HIS A 714 2783 1967 2551 219 -457 -82 N ATOM 880 N ASP A 715 6.717 -6.298 54.037 1.00 20.64 N ANISOU 880 N ASP A 715 2797 2104 2940 -101 -142 172 N ATOM 881 CA ASP A 715 7.991 -6.047 54.704 1.00 23.93 C ANISOU 881 CA ASP A 715 3272 2544 3277 -53 -191 185 C ATOM 882 C ASP A 715 9.180 -6.542 53.863 1.00 21.53 C ANISOU 882 C ASP A 715 2925 2249 3005 -6 -267 131 C ATOM 883 O ASP A 715 9.200 -7.711 53.450 1.00 21.62 O ANISOU 883 O ASP A 715 2938 2202 3074 4 -288 117 O ATOM 884 CB ASP A 715 7.971 -6.697 56.075 1.00 22.84 C ANISOU 884 CB ASP A 715 3256 2327 3097 -44 -174 258 C ATOM 885 CG ASP A 715 9.225 -6.403 56.881 1.00 30.18 C ANISOU 885 CG ASP A 715 4262 3260 3946 12 -261 269 C ATOM 886 OD1 ASP A 715 9.632 -5.244 56.950 1.00 30.86 O ANISOU 886 OD1 ASP A 715 4330 3409 3987 20 -287 248 O ATOM 887 OD2 ASP A 715 9.804 -7.337 57.444 1.00 34.77 O ANISOU 887 OD2 ASP A 715 4920 3771 4521 47 -319 296 O ATOM 888 N ALA A 716 10.114 -5.634 53.576 1.00 21.03 N ANISOU 888 N ALA A 716 2820 2251 2920 22 -296 103 N ATOM 889 CA ALA A 716 11.365 -5.921 52.818 1.00 22.51 C ANISOU 889 CA ALA A 716 2951 2445 3157 74 -336 58 C ATOM 890 C ALA A 716 11.135 -6.377 51.370 1.00 23.98 C ANISOU 890 C ALA A 716 3102 2633 3376 84 -306 1 C ATOM 891 O ALA A 716 12.003 -7.042 50.774 1.00 26.63 O ANISOU 891 O ALA A 716 3418 2944 3757 135 -316 -33 O ATOM 892 CB ALA A 716 12.240 -6.946 53.581 1.00 23.97 C ANISOU 892 CB ALA A 716 3174 2557 3375 118 -409 81 C ATOM 893 N GLN A 717 9.969 -6.060 50.802 1.00 19.76 N ANISOU 893 N GLN A 717 2569 2116 2824 43 -275 -14 N ATOM 894 CA GLN A 717 9.603 -6.584 49.485 1.00 21.77 C ANISOU 894 CA GLN A 717 2828 2349 3093 57 -279 -74 C ATOM 895 C GLN A 717 9.772 -5.590 48.341 1.00 21.09 C ANISOU 895 C GLN A 717 2731 2323 2958 78 -248 -116 C ATOM 896 O GLN A 717 9.592 -5.954 47.179 1.00 22.41 O ANISOU 896 O GLN A 717 2938 2468 3109 107 -256 -171 O ATOM 897 CB GLN A 717 8.152 -7.091 49.474 1.00 22.38 C ANISOU 897 CB GLN A 717 2918 2373 3212 5 -299 -72 C ATOM 898 CG GLN A 717 7.919 -8.325 50.370 1.00 23.96 C ANISOU 898 CG GLN A 717 3145 2485 3474 -14 -311 -30 C ATOM 899 CD GLN A 717 6.455 -8.678 50.464 1.00 23.22 C ANISOU 899 CD GLN A 717 3033 2330 3460 -78 -308 -15 C ATOM 900 OE1 GLN A 717 5.671 -8.244 49.639 1.00 21.11 O ANISOU 900 OE1 GLN A 717 2732 2072 3218 -97 -332 -57 O ATOM 901 NE2 GLN A 717 6.078 -9.462 51.471 1.00 22.48 N ANISOU 901 NE2 GLN A 717 2962 2159 3419 -108 -278 47 N ATOM 902 N PHE A 718 10.100 -4.346 48.651 1.00 19.39 N ANISOU 902 N PHE A 718 2482 2172 2711 68 -215 -91 N ATOM 903 CA PHE A 718 10.322 -3.351 47.608 1.00 18.69 C ANISOU 903 CA PHE A 718 2393 2133 2577 88 -170 -119 C ATOM 904 C PHE A 718 11.797 -2.998 47.488 1.00 18.51 C ANISOU 904 C PHE A 718 2325 2127 2579 131 -117 -115 C ATOM 905 O PHE A 718 12.595 -3.225 48.423 1.00 21.28 O ANISOU 905 O PHE A 718 2629 2465 2991 136 -142 -88 O ATOM 906 CB PHE A 718 9.516 -2.076 47.911 1.00 19.23 C ANISOU 906 CB PHE A 718 2448 2250 2611 41 -165 -95 C ATOM 907 CG PHE A 718 8.034 -2.315 47.899 1.00 18.22 C ANISOU 907 CG PHE A 718 2334 2095 2494 2 -205 -100 C ATOM 908 CD1 PHE A 718 7.406 -2.734 46.722 1.00 23.05 C ANISOU 908 CD1 PHE A 718 2987 2672 3098 19 -248 -153 C ATOM 909 CD2 PHE A 718 7.272 -2.164 49.052 1.00 21.16 C ANISOU 909 CD2 PHE A 718 2682 2461 2896 -46 -201 -56 C ATOM 910 CE1 PHE A 718 6.022 -2.969 46.686 1.00 22.84 C ANISOU 910 CE1 PHE A 718 2947 2602 3128 -20 -308 -162 C ATOM 911 CE2 PHE A 718 5.897 -2.399 49.023 1.00 21.90 C ANISOU 911 CE2 PHE A 718 2759 2515 3046 -84 -220 -57 C ATOM 912 CZ PHE A 718 5.287 -2.832 47.847 1.00 20.92 C ANISOU 912 CZ PHE A 718 2646 2354 2950 -74 -284 -112 C ATOM 913 N THR A 719 12.176 -2.458 46.330 1.00 19.54 N ANISOU 913 N THR A 719 2474 2274 2675 167 -45 -140 N ATOM 914 CA THR A 719 13.569 -2.028 46.153 1.00 19.87 C ANISOU 914 CA THR A 719 2450 2322 2778 203 36 -129 C ATOM 915 C THR A 719 13.747 -0.688 46.848 1.00 21.03 C ANISOU 915 C THR A 719 2531 2512 2946 157 34 -89 C ATOM 916 O THR A 719 12.769 0.059 47.031 1.00 17.71 O ANISOU 916 O THR A 719 2144 2126 2460 113 6 -79 O ATOM 917 CB THR A 719 13.912 -1.870 44.676 1.00 22.02 C ANISOU 917 CB THR A 719 2785 2583 2998 261 149 -158 C ATOM 918 OG1 THR A 719 13.142 -0.807 44.095 1.00 21.99 O ANISOU 918 OG1 THR A 719 2845 2614 2897 240 165 -155 O ATOM 919 CG2 THR A 719 13.643 -3.199 43.927 1.00 24.39 C ANISOU 919 CG2 THR A 719 3184 2827 3255 315 136 -211 C ATOM 920 N VAL A 720 14.992 -0.337 47.176 1.00 21.19 N ANISOU 920 N VAL A 720 2454 2522 3074 169 60 -71 N ATOM 921 CA VAL A 720 15.213 0.997 47.757 1.00 20.80 C ANISOU 921 CA VAL A 720 2347 2500 3056 126 47 -41 C ATOM 922 C VAL A 720 14.753 2.097 46.793 1.00 18.61 C ANISOU 922 C VAL A 720 2113 2255 2702 115 136 -37 C ATOM 923 O VAL A 720 14.194 3.105 47.232 1.00 19.94 O ANISOU 923 O VAL A 720 2289 2454 2832 70 101 -20 O ATOM 924 CB VAL A 720 16.695 1.222 48.174 1.00 22.26 C ANISOU 924 CB VAL A 720 2399 2647 3411 140 45 -28 C ATOM 925 CG1 VAL A 720 16.860 2.594 48.714 1.00 24.21 C ANISOU 925 CG1 VAL A 720 2597 2908 3694 93 15 -5 C ATOM 926 CG2 VAL A 720 17.089 0.220 49.240 1.00 29.28 C ANISOU 926 CG2 VAL A 720 3264 3496 4367 156 -79 -29 C ATOM 927 N ILE A 721 14.976 1.924 45.494 1.00 19.27 N ANISOU 927 N ILE A 721 2244 2326 2753 163 250 -53 N ATOM 928 CA ILE A 721 14.469 2.953 44.522 1.00 21.45 C ANISOU 928 CA ILE A 721 2601 2621 2927 162 326 -45 C ATOM 929 C ILE A 721 12.951 3.110 44.527 1.00 20.88 C ANISOU 929 C ILE A 721 2622 2577 2732 135 233 -60 C ATOM 930 O ILE A 721 12.430 4.247 44.441 1.00 19.52 O ANISOU 930 O ILE A 721 2472 2431 2515 108 232 -42 O ATOM 931 CB ILE A 721 15.044 2.700 43.100 1.00 24.57 C ANISOU 931 CB ILE A 721 3071 2980 3285 235 480 -56 C ATOM 932 CG1 ILE A 721 16.515 3.134 43.071 1.00 32.57 C ANISOU 932 CG1 ILE A 721 3956 3961 4457 247 614 -21 C ATOM 933 CG2 ILE A 721 14.298 3.515 42.040 1.00 29.77 C ANISOU 933 CG2 ILE A 721 3875 3646 3792 250 527 -53 C ATOM 934 CD1 ILE A 721 16.713 4.676 42.925 1.00 37.56 C ANISOU 934 CD1 ILE A 721 4557 4599 5113 208 687 26 C ATOM 935 N GLN A 722 12.223 2.001 44.683 1.00 18.99 N ANISOU 935 N GLN A 722 2424 2326 2465 140 150 -91 N ATOM 936 CA GLN A 722 10.760 2.110 44.806 1.00 18.43 C ANISOU 936 CA GLN A 722 2404 2268 2333 107 59 -102 C ATOM 937 C GLN A 722 10.349 2.915 46.039 1.00 18.94 C ANISOU 937 C GLN A 722 2401 2364 2430 48 15 -68 C ATOM 938 O GLN A 722 9.454 3.778 45.967 1.00 18.32 O ANISOU 938 O GLN A 722 2344 2305 2313 26 -6 -63 O ATOM 939 CB GLN A 722 10.107 0.744 44.867 1.00 19.39 C ANISOU 939 CB GLN A 722 2556 2352 2460 113 -18 -135 C ATOM 940 CG GLN A 722 10.048 0.008 43.531 1.00 18.65 C ANISOU 940 CG GLN A 722 2573 2214 2300 175 -12 -186 C ATOM 941 CD GLN A 722 9.436 -1.392 43.696 1.00 21.80 C ANISOU 941 CD GLN A 722 2989 2560 2733 172 -103 -221 C ATOM 942 OE1 GLN A 722 9.950 -2.233 44.466 1.00 21.87 O ANISOU 942 OE1 GLN A 722 2942 2554 2815 166 -104 -209 O ATOM 943 NE2 GLN A 722 8.342 -1.650 42.977 1.00 22.52 N ANISOU 943 NE2 GLN A 722 3159 2612 2784 178 -194 -264 N ATOM 944 N LEU A 723 10.983 2.612 47.163 1.00 16.08 N ANISOU 944 N LEU A 723 1975 2000 2137 31 -6 -49 N ATOM 945 CA LEU A 723 10.725 3.373 48.411 1.00 16.33 C ANISOU 945 CA LEU A 723 1977 2049 2179 -12 -46 -20 C ATOM 946 C LEU A 723 11.051 4.861 48.232 1.00 16.66 C ANISOU 946 C LEU A 723 1998 2114 2218 -26 -10 -5 C ATOM 947 O LEU A 723 10.307 5.743 48.677 1.00 16.11 O ANISOU 947 O LEU A 723 1943 2062 2115 -53 -28 6 O ATOM 948 CB LEU A 723 11.505 2.764 49.578 1.00 17.73 C ANISOU 948 CB LEU A 723 2122 2201 2413 -12 -95 -5 C ATOM 949 CG LEU A 723 11.128 1.310 49.948 1.00 16.29 C ANISOU 949 CG LEU A 723 1971 1983 2234 -3 -132 -9 C ATOM 950 CD1 LEU A 723 12.105 0.826 51.033 1.00 20.84 C ANISOU 950 CD1 LEU A 723 2530 2525 2861 11 -192 9 C ATOM 951 CD2 LEU A 723 9.670 1.142 50.392 1.00 22.74 C ANISOU 951 CD2 LEU A 723 2833 2796 3011 -35 -142 2 C ATOM 952 N VAL A 724 12.177 5.155 47.598 1.00 16.03 N ANISOU 952 N VAL A 724 1879 2024 2186 -5 53 -1 N ATOM 953 CA VAL A 724 12.552 6.570 47.397 1.00 15.80 C ANISOU 953 CA VAL A 724 1825 2002 2175 -24 98 21 C ATOM 954 C VAL A 724 11.543 7.271 46.487 1.00 17.22 C ANISOU 954 C VAL A 724 2087 2200 2255 -20 129 19 C ATOM 955 O VAL A 724 11.232 8.437 46.675 1.00 17.45 O ANISOU 955 O VAL A 724 2120 2240 2271 -45 124 35 O ATOM 956 CB VAL A 724 13.983 6.674 46.864 1.00 17.96 C ANISOU 956 CB VAL A 724 2026 2244 2555 -4 185 33 C ATOM 957 CG1 VAL A 724 14.323 8.142 46.414 1.00 19.84 C ANISOU 957 CG1 VAL A 724 2245 2474 2820 -25 260 63 C ATOM 958 CG2 VAL A 724 14.945 6.222 47.964 1.00 19.36 C ANISOU 958 CG2 VAL A 724 2103 2392 2859 -11 110 33 C ATOM 959 N GLY A 725 11.015 6.560 45.503 1.00 16.87 N ANISOU 959 N GLY A 725 2118 2150 2140 17 142 -4 N ATOM 960 CA GLY A 725 9.991 7.145 44.641 1.00 17.73 C ANISOU 960 CA GLY A 725 2318 2262 2155 30 132 -11 C ATOM 961 C GLY A 725 8.755 7.529 45.441 1.00 17.13 C ANISOU 961 C GLY A 725 2225 2204 2078 -7 45 -13 C ATOM 962 O GLY A 725 8.164 8.603 45.203 1.00 17.19 O ANISOU 962 O GLY A 725 2261 2217 2054 -12 37 -4 O ATOM 963 N MET A 726 8.354 6.655 46.355 1.00 15.91 N ANISOU 963 N MET A 726 2032 2050 1965 -27 -7 -23 N ATOM 964 CA MET A 726 7.207 6.951 47.242 1.00 14.13 C ANISOU 964 CA MET A 726 1784 1829 1756 -58 -53 -17 C ATOM 965 C MET A 726 7.490 8.227 48.057 1.00 15.77 C ANISOU 965 C MET A 726 1970 2054 1969 -81 -33 8 C ATOM 966 O MET A 726 6.670 9.153 48.116 1.00 15.91 O ANISOU 966 O MET A 726 1996 2075 1973 -88 -40 12 O ATOM 967 CB MET A 726 6.961 5.790 48.233 1.00 16.65 C ANISOU 967 CB MET A 726 2076 2131 2117 -74 -76 -16 C ATOM 968 CG MET A 726 6.509 4.500 47.541 1.00 17.54 C ANISOU 968 CG MET A 726 2206 2212 2245 -59 -111 -44 C ATOM 969 SD MET A 726 6.459 3.167 48.760 1.00 18.20 S ANISOU 969 SD MET A 726 2266 2265 2384 -80 -119 -28 S ATOM 970 CE MET A 726 6.253 1.789 47.642 1.00 17.08 C ANISOU 970 CE MET A 726 2151 2078 2263 -55 -166 -71 C ATOM 971 N LEU A 727 8.673 8.268 48.647 1.00 14.81 N ANISOU 971 N LEU A 727 1820 1931 1877 -88 -21 21 N ATOM 972 CA LEU A 727 9.115 9.380 49.509 1.00 15.87 C ANISOU 972 CA LEU A 727 1939 2063 2027 -110 -30 36 C ATOM 973 C LEU A 727 9.194 10.697 48.743 1.00 17.25 C ANISOU 973 C LEU A 727 2120 2240 2193 -113 5 46 C ATOM 974 O LEU A 727 8.839 11.770 49.261 1.00 16.39 O ANISOU 974 O LEU A 727 2024 2128 2077 -128 -8 51 O ATOM 975 CB LEU A 727 10.471 9.012 50.111 1.00 15.33 C ANISOU 975 CB LEU A 727 1828 1974 2023 -112 -56 39 C ATOM 976 CG LEU A 727 10.280 7.954 51.217 1.00 19.69 C ANISOU 976 CG LEU A 727 2405 2513 2564 -108 -109 38 C ATOM 977 CD1 LEU A 727 11.607 7.302 51.559 1.00 22.10 C ANISOU 977 CD1 LEU A 727 2666 2788 2942 -96 -153 37 C ATOM 978 CD2 LEU A 727 9.573 8.537 52.459 1.00 19.38 C ANISOU 978 CD2 LEU A 727 2429 2464 2472 -118 -137 44 C ATOM 979 N ARG A 728 9.667 10.624 47.504 1.00 14.94 N ANISOU 979 N ARG A 728 1837 1943 1895 -92 61 50 N ATOM 980 CA ARG A 728 9.736 11.811 46.625 1.00 16.19 C ANISOU 980 CA ARG A 728 2030 2091 2032 -88 113 70 C ATOM 981 C ARG A 728 8.355 12.375 46.329 1.00 16.25 C ANISOU 981 C ARG A 728 2096 2106 1973 -78 75 63 C ATOM 982 O ARG A 728 8.168 13.600 46.379 1.00 16.73 O ANISOU 982 O ARG A 728 2170 2157 2030 -88 78 78 O ATOM 983 CB ARG A 728 10.476 11.458 45.313 1.00 17.93 C ANISOU 983 CB ARG A 728 2283 2293 2235 -53 205 81 C ATOM 984 CG ARG A 728 10.992 12.698 44.513 1.00 20.87 C ANISOU 984 CG ARG A 728 2688 2635 2607 -52 298 121 C ATOM 985 CD ARG A 728 9.962 13.214 43.516 1.00 28.41 C ANISOU 985 CD ARG A 728 3771 3584 3440 -17 290 123 C ATOM 986 NE ARG A 728 10.558 14.273 42.687 1.00 25.80 N ANISOU 986 NE ARG A 728 3495 3211 3097 -9 400 171 N ATOM 987 CZ ARG A 728 9.898 15.259 42.081 1.00 27.63 C ANISOU 987 CZ ARG A 728 3827 3422 3250 9 392 192 C ATOM 988 NH1 ARG A 728 8.573 15.353 42.179 1.00 27.14 N ANISOU 988 NH1 ARG A 728 3807 3376 3128 23 268 162 N ATOM 989 NH2 ARG A 728 10.596 16.186 41.401 1.00 26.11 N ANISOU 989 NH2 ARG A 728 3683 3179 3059 12 516 247 N ATOM 990 N GLY A 729 7.385 11.497 46.060 1.00 17.19 N ANISOU 990 N GLY A 729 2240 2231 2060 -58 28 38 N ATOM 991 CA GLY A 729 5.995 11.939 45.818 1.00 16.80 C ANISOU 991 CA GLY A 729 2218 2174 1989 -45 -29 26 C ATOM 992 C GLY A 729 5.472 12.682 47.046 1.00 15.94 C ANISOU 992 C GLY A 729 2063 2072 1922 -72 -39 32 C ATOM 993 O GLY A 729 4.916 13.776 46.930 1.00 16.14 O ANISOU 993 O GLY A 729 2105 2086 1941 -65 -48 38 O ATOM 994 N ILE A 730 5.667 12.089 48.230 1.00 14.48 N ANISOU 994 N ILE A 730 1837 1894 1768 -94 -33 31 N ATOM 995 CA ILE A 730 5.178 12.695 49.487 1.00 15.13 C ANISOU 995 CA ILE A 730 1911 1971 1865 -107 -27 35 C ATOM 996 C ILE A 730 5.834 14.085 49.655 1.00 15.76 C ANISOU 996 C ILE A 730 2011 2042 1934 -116 -20 45 C ATOM 997 O ILE A 730 5.151 15.056 49.942 1.00 15.04 O ANISOU 997 O ILE A 730 1934 1938 1840 -109 -18 44 O ATOM 998 CB ILE A 730 5.498 11.819 50.711 1.00 15.28 C ANISOU 998 CB ILE A 730 1930 1987 1890 -119 -21 37 C ATOM 999 CG1 ILE A 730 4.793 10.452 50.586 1.00 15.85 C ANISOU 999 CG1 ILE A 730 1979 2054 1990 -116 -20 33 C ATOM 1000 CG2 ILE A 730 5.080 12.527 52.035 1.00 16.93 C ANISOU 1000 CG2 ILE A 730 2176 2177 2079 -118 -2 41 C ATOM 1001 CD1 ILE A 730 5.375 9.390 51.534 1.00 17.92 C ANISOU 1001 CD1 ILE A 730 2256 2305 2247 -123 -18 42 C ATOM 1002 N ALA A 731 7.155 14.171 49.460 1.00 14.51 N ANISOU 1002 N ALA A 731 1843 1881 1790 -130 -13 55 N ATOM 1003 CA ALA A 731 7.843 15.453 49.595 1.00 14.78 C ANISOU 1003 CA ALA A 731 1879 1889 1847 -148 -11 66 C ATOM 1004 C ALA A 731 7.338 16.497 48.591 1.00 15.37 C ANISOU 1004 C ALA A 731 1987 1953 1900 -135 13 81 C ATOM 1005 O ALA A 731 7.225 17.678 48.925 1.00 17.33 O ANISOU 1005 O ALA A 731 2253 2176 2157 -143 4 84 O ATOM 1006 CB ALA A 731 9.376 15.241 49.465 1.00 17.61 C ANISOU 1006 CB ALA A 731 2189 2230 2273 -168 -1 77 C ATOM 1007 N SER A 732 7.006 16.055 47.381 1.00 13.75 N ANISOU 1007 N SER A 732 1808 1757 1658 -109 32 87 N ATOM 1008 CA SER A 732 6.528 16.962 46.328 1.00 16.12 C ANISOU 1008 CA SER A 732 2172 2036 1918 -85 40 104 C ATOM 1009 C SER A 732 5.160 17.525 46.724 1.00 16.00 C ANISOU 1009 C SER A 732 2160 2015 1904 -68 -14 87 C ATOM 1010 O SER A 732 4.908 18.724 46.593 1.00 16.12 O ANISOU 1010 O SER A 732 2206 2002 1916 -60 -18 100 O ATOM 1011 CB SER A 732 6.435 16.219 44.971 1.00 17.35 C ANISOU 1011 CB SER A 732 2392 2190 2010 -46 49 106 C ATOM 1012 OG SER A 732 6.123 17.152 43.947 1.00 22.06 O ANISOU 1012 OG SER A 732 3082 2751 2548 -14 53 129 O ATOM 1013 N GLY A 733 4.276 16.652 47.208 1.00 15.36 N ANISOU 1013 N GLY A 733 2041 1951 1844 -60 -47 61 N ATOM 1014 CA GLY A 733 2.978 17.109 47.709 1.00 15.32 C ANISOU 1014 CA GLY A 733 2012 1932 1878 -43 -72 47 C ATOM 1015 C GLY A 733 3.178 18.112 48.843 1.00 15.71 C ANISOU 1015 C GLY A 733 2064 1968 1936 -56 -40 48 C ATOM 1016 O GLY A 733 2.512 19.167 48.905 1.00 15.94 O ANISOU 1016 O GLY A 733 2107 1970 1981 -35 -47 47 O ATOM 1017 N MET A 734 4.064 17.783 49.778 1.00 15.19 N ANISOU 1017 N MET A 734 1999 1912 1861 -84 -20 47 N ATOM 1018 CA MET A 734 4.311 18.726 50.914 1.00 14.24 C ANISOU 1018 CA MET A 734 1912 1763 1734 -90 -15 38 C ATOM 1019 C MET A 734 4.908 20.056 50.494 1.00 16.52 C ANISOU 1019 C MET A 734 2227 2020 2031 -101 -29 49 C ATOM 1020 O MET A 734 4.630 21.121 51.125 1.00 16.30 O ANISOU 1020 O MET A 734 2236 1954 2002 -91 -35 37 O ATOM 1021 CB MET A 734 5.186 18.051 51.970 1.00 15.61 C ANISOU 1021 CB MET A 734 2100 1938 1892 -110 -26 29 C ATOM 1022 CG MET A 734 4.453 16.955 52.762 1.00 16.18 C ANISOU 1022 CG MET A 734 2178 2022 1949 -94 6 23 C ATOM 1023 SD MET A 734 2.855 17.427 53.488 1.00 17.02 S ANISOU 1023 SD MET A 734 2304 2101 2060 -54 77 16 S ATOM 1024 CE MET A 734 3.355 18.799 54.552 1.00 18.00 C ANISOU 1024 CE MET A 734 2537 2178 2127 -40 60 -6 C ATOM 1025 N LYS A 735 5.760 20.017 49.462 1.00 15.76 N ANISOU 1025 N LYS A 735 2120 1925 1943 -119 -21 75 N ATOM 1026 CA LYS A 735 6.339 21.242 48.952 1.00 16.65 C ANISOU 1026 CA LYS A 735 2255 1993 2077 -134 -11 99 C ATOM 1027 C LYS A 735 5.198 22.157 48.454 1.00 17.57 C ANISOU 1027 C LYS A 735 2416 2089 2172 -97 -21 104 C ATOM 1028 O LYS A 735 5.215 23.381 48.706 1.00 17.67 O ANISOU 1028 O LYS A 735 2458 2054 2203 -99 -29 106 O ATOM 1029 CB LYS A 735 7.355 20.930 47.853 1.00 17.32 C ANISOU 1029 CB LYS A 735 2329 2076 2177 -151 39 136 C ATOM 1030 CG LYS A 735 8.328 22.075 47.493 1.00 20.67 C ANISOU 1030 CG LYS A 735 2756 2437 2662 -183 77 173 C ATOM 1031 CD LYS A 735 7.710 23.061 46.512 1.00 22.99 C ANISOU 1031 CD LYS A 735 3130 2697 2909 -156 102 206 C ATOM 1032 CE LYS A 735 8.747 24.148 46.143 1.00 23.66 C ANISOU 1032 CE LYS A 735 3215 2705 3069 -195 163 254 C ATOM 1033 NZ LYS A 735 8.203 25.117 45.104 1.00 21.95 N ANISOU 1033 NZ LYS A 735 3105 2443 2794 -162 195 298 N ATOM 1034 N TYR A 736 4.209 21.572 47.781 1.00 16.39 N ANISOU 1034 N TYR A 736 2268 1962 1996 -59 -35 100 N ATOM 1035 CA TYR A 736 3.066 22.360 47.272 1.00 16.71 C ANISOU 1035 CA TYR A 736 2338 1972 2037 -14 -71 101 C ATOM 1036 C TYR A 736 2.255 22.908 48.433 1.00 18.13 C ANISOU 1036 C TYR A 736 2494 2137 2260 2 -71 71 C ATOM 1037 O TYR A 736 1.921 24.091 48.471 1.00 16.86 O ANISOU 1037 O TYR A 736 2364 1930 2112 22 -81 73 O ATOM 1038 CB TYR A 736 2.172 21.569 46.268 1.00 18.37 C ANISOU 1038 CB TYR A 736 2552 2194 2233 27 -123 95 C ATOM 1039 CG TYR A 736 1.134 22.492 45.606 1.00 20.55 C ANISOU 1039 CG TYR A 736 2866 2421 2522 79 -188 99 C ATOM 1040 CD1 TYR A 736 1.554 23.597 44.897 1.00 24.53 C ANISOU 1040 CD1 TYR A 736 3462 2880 2979 90 -185 135 C ATOM 1041 CD2 TYR A 736 -0.252 22.256 45.702 1.00 24.36 C ANISOU 1041 CD2 TYR A 736 3285 2890 3081 119 -253 68 C ATOM 1042 CE1 TYR A 736 0.650 24.491 44.311 1.00 28.29 C ANISOU 1042 CE1 TYR A 736 3987 3300 3461 144 -257 142 C ATOM 1043 CE2 TYR A 736 -1.176 23.122 45.077 1.00 21.05 C ANISOU 1043 CE2 TYR A 736 2892 2414 2692 174 -335 69 C ATOM 1044 CZ TYR A 736 -0.716 24.237 44.385 1.00 28.55 C ANISOU 1044 CZ TYR A 736 3955 3323 3572 190 -344 105 C ATOM 1045 OH TYR A 736 -1.572 25.138 43.756 1.00 25.78 O ANISOU 1045 OH TYR A 736 3649 2906 3242 251 -435 111 O ATOM 1046 N LEU A 737 1.967 22.078 49.428 1.00 17.26 N ANISOU 1046 N LEU A 737 2341 2054 2165 -2 -46 46 N ATOM 1047 CA LEU A 737 1.137 22.538 50.551 1.00 16.99 C ANISOU 1047 CA LEU A 737 2303 1994 2159 26 -13 21 C ATOM 1048 C LEU A 737 1.812 23.683 51.296 1.00 18.77 C ANISOU 1048 C LEU A 737 2597 2178 2357 16 -10 11 C ATOM 1049 O LEU A 737 1.170 24.677 51.629 1.00 19.55 O ANISOU 1049 O LEU A 737 2723 2233 2473 51 0 -3 O ATOM 1050 CB LEU A 737 0.927 21.396 51.543 1.00 16.41 C ANISOU 1050 CB LEU A 737 2204 1945 2086 21 38 7 C ATOM 1051 CG LEU A 737 0.095 20.262 51.038 1.00 23.54 C ANISOU 1051 CG LEU A 737 3027 2869 3047 29 38 11 C ATOM 1052 CD1 LEU A 737 -0.143 19.335 52.256 1.00 26.21 C ANISOU 1052 CD1 LEU A 737 3358 3211 3388 26 118 6 C ATOM 1053 CD2 LEU A 737 -1.233 20.832 50.536 1.00 28.49 C ANISOU 1053 CD2 LEU A 737 3599 3460 3767 75 20 4 C ATOM 1054 N SER A 738 3.113 23.537 51.532 1.00 17.73 N ANISOU 1054 N SER A 738 2488 2051 2197 -30 -29 15 N ATOM 1055 CA SER A 738 3.888 24.567 52.223 1.00 19.87 C ANISOU 1055 CA SER A 738 2819 2267 2464 -48 -59 0 C ATOM 1056 C SER A 738 3.976 25.831 51.363 1.00 18.99 C ANISOU 1056 C SER A 738 2723 2108 2384 -51 -75 23 C ATOM 1057 O SER A 738 3.883 26.942 51.911 1.00 20.35 O ANISOU 1057 O SER A 738 2950 2220 2564 -39 -92 2 O ATOM 1058 CB SER A 738 5.264 24.047 52.610 1.00 21.98 C ANISOU 1058 CB SER A 738 3080 2536 2735 -97 -98 -2 C ATOM 1059 OG SER A 738 5.943 23.470 51.520 1.00 22.13 O ANISOU 1059 OG SER A 738 3035 2586 2785 -130 -87 35 O ATOM 1060 N ASP A 739 4.093 25.661 50.031 1.00 17.38 N ANISOU 1060 N ASP A 739 2493 1922 2188 -60 -66 65 N ATOM 1061 CA ASP A 739 4.053 26.822 49.101 1.00 18.37 C ANISOU 1061 CA ASP A 739 2659 1994 2327 -52 -71 99 C ATOM 1062 C ASP A 739 2.742 27.571 49.225 1.00 19.08 C ANISOU 1062 C ASP A 739 2773 2054 2423 9 -88 81 C ATOM 1063 O ASP A 739 2.681 28.799 49.006 1.00 21.86 O ANISOU 1063 O ASP A 739 3174 2340 2792 20 -103 93 O ATOM 1064 CB ASP A 739 4.168 26.368 47.636 1.00 16.55 C ANISOU 1064 CB ASP A 739 2438 1783 2067 -47 -53 147 C ATOM 1065 CG ASP A 739 5.613 26.257 47.155 1.00 23.96 C ANISOU 1065 CG ASP A 739 3371 2707 3024 -101 -3 187 C ATOM 1066 OD1 ASP A 739 6.576 26.428 47.945 1.00 21.14 O ANISOU 1066 OD1 ASP A 739 2975 2327 2729 -151 -3 176 O ATOM 1067 OD2 ASP A 739 5.778 25.965 45.957 1.00 26.74 O ANISOU 1067 OD2 ASP A 739 3762 3062 3335 -88 36 229 O ATOM 1068 N MET A 740 1.672 26.832 49.504 1.00 17.48 N ANISOU 1068 N MET A 740 2526 1890 2225 49 -82 55 N ATOM 1069 CA MET A 740 0.342 27.426 49.642 1.00 20.32 C ANISOU 1069 CA MET A 740 2875 2215 2629 114 -88 36 C ATOM 1070 C MET A 740 0.087 28.019 51.048 1.00 22.44 C ANISOU 1070 C MET A 740 3173 2448 2905 135 -45 -7 C ATOM 1071 O MET A 740 -0.972 28.607 51.288 1.00 23.13 O ANISOU 1071 O MET A 740 3252 2496 3042 195 -26 -25 O ATOM 1072 CB MET A 740 -0.732 26.369 49.301 1.00 19.76 C ANISOU 1072 CB MET A 740 2723 2182 2603 147 -96 29 C ATOM 1073 CG MET A 740 -0.734 25.937 47.849 1.00 19.90 C ANISOU 1073 CG MET A 740 2747 2212 2602 150 -165 58 C ATOM 1074 SD MET A 740 -1.426 27.176 46.767 1.00 24.05 S ANISOU 1074 SD MET A 740 3330 2662 3144 211 -250 80 S ATOM 1075 CE MET A 740 -3.208 26.931 47.095 1.00 23.05 C ANISOU 1075 CE MET A 740 3080 2513 3166 280 -287 39 C ATOM 1076 N GLY A 741 1.052 27.874 51.945 1.00 21.25 N ANISOU 1076 N GLY A 741 3066 2299 2707 95 -35 -24 N ATOM 1077 CA GLY A 741 0.939 28.419 53.314 1.00 21.97 C ANISOU 1077 CA GLY A 741 3234 2342 2771 124 -7 -71 C ATOM 1078 C GLY A 741 0.126 27.530 54.267 1.00 22.81 C ANISOU 1078 C GLY A 741 3334 2474 2860 165 80 -93 C ATOM 1079 O GLY A 741 -0.327 27.979 55.327 1.00 25.38 O ANISOU 1079 O GLY A 741 3737 2751 3156 215 138 -129 O ATOM 1080 N TYR A 742 -0.073 26.281 53.875 1.00 19.93 N ANISOU 1080 N TYR A 742 2887 2173 2513 147 100 -71 N ATOM 1081 CA TYR A 742 -0.801 25.335 54.680 1.00 19.93 C ANISOU 1081 CA TYR A 742 2869 2189 2515 176 195 -78 C ATOM 1082 C TYR A 742 0.182 24.541 55.507 1.00 20.75 C ANISOU 1082 C TYR A 742 3046 2313 2525 142 189 -84 C ATOM 1083 O TYR A 742 1.120 23.950 54.953 1.00 23.41 O ANISOU 1083 O TYR A 742 3351 2691 2852 87 119 -67 O ATOM 1084 CB TYR A 742 -1.589 24.400 53.749 1.00 19.87 C ANISOU 1084 CB TYR A 742 2725 2223 2601 173 200 -53 C ATOM 1085 CG TYR A 742 -2.478 23.453 54.472 1.00 24.82 C ANISOU 1085 CG TYR A 742 3305 2850 3275 197 312 -52 C ATOM 1086 CD1 TYR A 742 -3.690 23.890 55.012 1.00 31.26 C ANISOU 1086 CD1 TYR A 742 4090 3612 4176 261 421 -62 C ATOM 1087 CD2 TYR A 742 -2.109 22.105 54.633 1.00 25.21 C ANISOU 1087 CD2 TYR A 742 3337 2943 3299 159 327 -36 C ATOM 1088 CE1 TYR A 742 -4.517 23.008 55.712 1.00 29.71 C ANISOU 1088 CE1 TYR A 742 3843 3401 4045 282 560 -51 C ATOM 1089 CE2 TYR A 742 -2.936 21.212 55.338 1.00 26.97 C ANISOU 1089 CE2 TYR A 742 3521 3151 3575 178 450 -25 C ATOM 1090 CZ TYR A 742 -4.140 21.692 55.871 1.00 30.29 C ANISOU 1090 CZ TYR A 742 3909 3514 4088 238 574 -30 C ATOM 1091 OH TYR A 742 -4.975 20.849 56.579 1.00 31.32 O ANISOU 1091 OH TYR A 742 3994 3613 4292 256 729 -10 O ATOM 1092 N VAL A 743 -0.071 24.464 56.820 1.00 17.49 N ANISOU 1092 N VAL A 743 2360 1907 2378 154 -497 -308 N ATOM 1093 CA VAL A 743 0.670 23.534 57.691 1.00 17.02 C ANISOU 1093 CA VAL A 743 2244 1967 2255 127 -332 -285 C ATOM 1094 C VAL A 743 -0.242 22.366 58.017 1.00 18.18 C ANISOU 1094 C VAL A 743 2293 2177 2438 149 -227 -315 C ATOM 1095 O VAL A 743 -1.403 22.563 58.489 1.00 18.87 O ANISOU 1095 O VAL A 743 2280 2232 2658 205 -177 -415 O ATOM 1096 CB VAL A 743 1.166 24.261 58.992 1.00 20.13 C ANISOU 1096 CB VAL A 743 2671 2356 2620 163 -341 -331 C ATOM 1097 CG1 VAL A 743 1.950 23.368 59.815 1.00 23.11 C ANISOU 1097 CG1 VAL A 743 3087 2762 2931 143 -306 -311 C ATOM 1098 CG2 VAL A 743 1.978 25.510 58.629 1.00 25.78 C ANISOU 1098 CG2 VAL A 743 3445 2982 3370 135 -459 -312 C ATOM 1099 N HIS A 744 0.220 21.165 57.695 1.00 18.44 N ANISOU 1099 N HIS A 744 2329 2264 2413 98 -167 -250 N ATOM 1100 CA HIS A 744 -0.604 19.961 57.770 1.00 18.09 C ANISOU 1100 CA HIS A 744 2205 2258 2411 97 -81 -260 C ATOM 1101 C HIS A 744 -0.895 19.543 59.215 1.00 17.37 C ANISOU 1101 C HIS A 744 2140 2191 2268 96 94 -307 C ATOM 1102 O HIS A 744 -2.071 19.299 59.572 1.00 19.81 O ANISOU 1102 O HIS A 744 2355 2465 2707 99 249 -388 O ATOM 1103 CB HIS A 744 0.052 18.810 57.003 1.00 18.43 C ANISOU 1103 CB HIS A 744 2281 2332 2389 43 -77 -181 C ATOM 1104 CG HIS A 744 -0.856 17.647 56.781 1.00 18.84 C ANISOU 1104 CG HIS A 744 2259 2393 2505 40 -47 -183 C ATOM 1105 ND1 HIS A 744 -1.205 16.774 57.790 1.00 21.10 N ANISOU 1105 ND1 HIS A 744 2510 2720 2786 21 97 -198 N ATOM 1106 CD2 HIS A 744 -1.520 17.225 55.669 1.00 20.61 C ANISOU 1106 CD2 HIS A 744 2481 2546 2804 44 -165 -176 C ATOM 1107 CE1 HIS A 744 -2.013 15.848 57.303 1.00 23.26 C ANISOU 1107 CE1 HIS A 744 2692 2972 3174 7 102 -201 C ATOM 1108 NE2 HIS A 744 -2.225 16.104 56.021 1.00 19.47 N ANISOU 1108 NE2 HIS A 744 2218 2421 2759 33 -91 -192 N ATOM 1109 N ARG A 745 0.171 19.465 60.017 1.00 20.30 N ANISOU 1109 N ARG A 745 2670 2562 2481 81 65 -274 N ATOM 1110 CA ARG A 745 0.130 19.152 61.458 1.00 18.64 C ANISOU 1110 CA ARG A 745 2692 2291 2098 66 168 -304 C ATOM 1111 C ARG A 745 -0.100 17.678 61.765 1.00 21.47 C ANISOU 1111 C ARG A 745 3144 2646 2368 5 278 -267 C ATOM 1112 O ARG A 745 0.067 17.287 62.910 1.00 23.80 O ANISOU 1112 O ARG A 745 3765 2836 2443 -30 321 -269 O ATOM 1113 CB ARG A 745 -0.906 19.986 62.216 1.00 20.16 C ANISOU 1113 CB ARG A 745 2941 2420 2298 86 377 -418 C ATOM 1114 CG ARG A 745 -0.757 21.480 62.010 1.00 17.96 C ANISOU 1114 CG ARG A 745 2597 2124 2104 154 244 -464 C ATOM 1115 CD ARG A 745 -1.624 22.188 63.084 1.00 22.31 C ANISOU 1115 CD ARG A 745 3275 2570 2631 175 489 -606 C ATOM 1116 NE ARG A 745 -1.435 23.622 63.107 1.00 33.69 N ANISOU 1116 NE ARG A 745 4710 3970 4120 248 344 -659 N ATOM 1117 CZ ARG A 745 -1.892 24.383 64.100 1.00 40.95 C ANISOU 1117 CZ ARG A 745 5805 4776 4979 277 521 -788 C ATOM 1118 NH1 ARG A 745 -2.556 23.803 65.105 1.00 43.91 N ANISOU 1118 NH1 ARG A 745 6406 5051 5227 218 908 -877 N ATOM 1119 NH2 ARG A 745 -1.697 25.702 64.092 1.00 44.53 N ANISOU 1119 NH2 ARG A 745 6250 5185 5484 351 353 -836 N ATOM 1120 N ASP A 746 -0.483 16.869 60.767 1.00 19.10 N ANISOU 1120 N ASP A 746 2635 2417 2204 -13 297 -232 N ATOM 1121 CA ASP A 746 -0.764 15.436 61.007 1.00 24.12 C ANISOU 1121 CA ASP A 746 3344 3041 2779 -77 397 -196 C ATOM 1122 C ASP A 746 -0.128 14.585 59.888 1.00 19.89 C ANISOU 1122 C ASP A 746 2673 2568 2315 -71 229 -125 C ATOM 1123 O ASP A 746 -0.699 13.585 59.427 1.00 22.87 O ANISOU 1123 O ASP A 746 2972 2962 2755 -103 283 -104 O ATOM 1124 CB ASP A 746 -2.288 15.212 61.101 1.00 25.83 C ANISOU 1124 CB ASP A 746 3429 3222 3164 -123 688 -274 C ATOM 1125 CG ASP A 746 -2.683 13.881 61.814 1.00 37.56 C ANISOU 1125 CG ASP A 746 5098 4634 4540 -232 907 -252 C ATOM 1126 OD1 ASP A 746 -1.850 13.226 62.502 1.00 39.39 O ANISOU 1126 OD1 ASP A 746 5673 4810 4482 -268 814 -179 O ATOM 1127 OD2 ASP A 746 -3.866 13.500 61.678 1.00 38.88 O ANISOU 1127 OD2 ASP A 746 5066 4752 4956 -287 1152 -323 O ATOM 1128 N LEU A 747 1.063 14.988 59.441 1.00 17.82 N ANISOU 1128 N LEU A 747 2382 2310 2078 -38 58 -108 N ATOM 1129 CA LEU A 747 1.753 14.247 58.386 1.00 16.26 C ANISOU 1129 CA LEU A 747 2081 2129 1967 -45 -4 -79 C ATOM 1130 C LEU A 747 2.321 12.975 59.010 1.00 18.69 C ANISOU 1130 C LEU A 747 2481 2383 2238 -58 -94 -61 C ATOM 1131 O LEU A 747 3.128 13.030 59.943 1.00 22.62 O ANISOU 1131 O LEU A 747 3106 2773 2715 -41 -258 -80 O ATOM 1132 CB LEU A 747 2.874 15.089 57.764 1.00 15.30 C ANISOU 1132 CB LEU A 747 1885 1969 1958 -38 -50 -103 C ATOM 1133 CG LEU A 747 3.767 14.373 56.759 1.00 16.17 C ANISOU 1133 CG LEU A 747 1912 2039 2193 -66 -3 -117 C ATOM 1134 CD1 LEU A 747 2.904 13.822 55.625 1.00 18.84 C ANISOU 1134 CD1 LEU A 747 2307 2412 2439 -86 81 -80 C ATOM 1135 CD2 LEU A 747 4.778 15.406 56.262 1.00 15.53 C ANISOU 1135 CD2 LEU A 747 1763 1872 2268 -99 68 -167 C ATOM 1136 N ALA A 748 1.839 11.836 58.524 1.00 16.14 N ANISOU 1136 N ALA A 748 2130 2090 1914 -83 -46 -30 N ATOM 1137 CA ALA A 748 2.208 10.531 59.077 1.00 17.40 C ANISOU 1137 CA ALA A 748 2406 2177 2027 -100 -150 -8 C ATOM 1138 C ALA A 748 1.912 9.535 57.980 1.00 15.95 C ANISOU 1138 C ALA A 748 2104 2041 1914 -109 -106 11 C ATOM 1139 O ALA A 748 1.036 9.807 57.145 1.00 16.75 O ANISOU 1139 O ALA A 748 2120 2202 2043 -115 -8 18 O ATOM 1140 CB ALA A 748 1.330 10.214 60.281 1.00 19.28 C ANISOU 1140 CB ALA A 748 2905 2358 2063 -162 -55 20 C ATOM 1141 N ALA A 749 2.570 8.375 57.992 1.00 16.36 N ANISOU 1141 N ALA A 749 2180 2027 2010 -103 -230 9 N ATOM 1142 CA ALA A 749 2.327 7.402 56.920 1.00 15.68 C ANISOU 1142 CA ALA A 749 2015 1968 1976 -106 -192 18 C ATOM 1143 C ALA A 749 0.857 6.961 56.844 1.00 17.03 C ANISOU 1143 C ALA A 749 2213 2179 2080 -157 -104 73 C ATOM 1144 O ALA A 749 0.350 6.700 55.748 1.00 17.38 O ANISOU 1144 O ALA A 749 2193 2234 2176 -148 -98 74 O ATOM 1145 CB ALA A 749 3.319 6.194 57.030 1.00 16.67 C ANISOU 1145 CB ALA A 749 2141 1985 2208 -79 -360 -18 C ATOM 1146 N ARG A 750 0.156 6.909 57.996 1.00 16.69 N ANISOU 1146 N ARG A 750 2290 2105 1946 -219 -24 101 N ATOM 1147 CA ARG A 750 -1.273 6.531 57.985 1.00 19.30 C ANISOU 1147 CA ARG A 750 2562 2422 2351 -290 134 111 C ATOM 1148 C ARG A 750 -2.132 7.550 57.228 1.00 20.93 C ANISOU 1148 C ARG A 750 2555 2657 2740 -255 177 58 C ATOM 1149 O ARG A 750 -3.262 7.233 56.821 1.00 21.41 O ANISOU 1149 O ARG A 750 2464 2658 3015 -281 202 31 O ATOM 1150 CB ARG A 750 -1.791 6.333 59.410 1.00 20.70 C ANISOU 1150 CB ARG A 750 2965 2503 2399 -400 337 122 C ATOM 1151 CG ARG A 750 -1.824 7.624 60.227 1.00 21.27 C ANISOU 1151 CG ARG A 750 3133 2564 2383 -400 475 77 C ATOM 1152 CD ARG A 750 -2.355 7.411 61.671 1.00 26.26 C ANISOU 1152 CD ARG A 750 4135 3035 2808 -538 763 74 C ATOM 1153 NE ARG A 750 -2.246 8.717 62.330 1.00 38.00 N ANISOU 1153 NE ARG A 750 5741 4505 4193 -511 855 18 N ATOM 1154 CZ ARG A 750 -1.118 9.169 62.867 1.00 42.20 C ANISOU 1154 CZ ARG A 750 6541 4991 4504 -449 597 40 C ATOM 1155 NH1 ARG A 750 -0.052 8.390 62.851 1.00 44.63 N ANISOU 1155 NH1 ARG A 750 6987 5241 4729 -410 244 97 N ATOM 1156 NH2 ARG A 750 -1.040 10.386 63.405 1.00 39.44 N ANISOU 1156 NH2 ARG A 750 6293 4617 4075 -417 652 -14 N ATOM 1157 N ASN A 751 -1.613 8.771 57.072 1.00 17.43 N ANISOU 1157 N ASN A 751 2103 2259 2261 -196 143 33 N ATOM 1158 CA ASN A 751 -2.311 9.821 56.319 1.00 17.73 C ANISOU 1158 CA ASN A 751 2009 2277 2450 -152 99 -17 C ATOM 1159 C ASN A 751 -1.821 10.049 54.895 1.00 18.63 C ANISOU 1159 C ASN A 751 2189 2367 2520 -101 -78 -4 C ATOM 1160 O ASN A 751 -2.180 11.050 54.246 1.00 20.37 O ANISOU 1160 O ASN A 751 2425 2525 2790 -65 -180 -34 O ATOM 1161 CB ASN A 751 -2.292 11.119 57.101 1.00 18.10 C ANISOU 1161 CB ASN A 751 2057 2342 2477 -139 198 -61 C ATOM 1162 CG ASN A 751 -3.107 11.007 58.369 1.00 24.81 C ANISOU 1162 CG ASN A 751 2912 3143 3373 -210 456 -107 C ATOM 1163 OD1 ASN A 751 -4.062 10.234 58.422 1.00 22.69 O ANISOU 1163 OD1 ASN A 751 2534 2802 3284 -271 577 -136 O ATOM 1164 ND2 ASN A 751 -2.704 11.737 59.421 1.00 23.68 N ANISOU 1164 ND2 ASN A 751 2938 2997 3062 -218 568 -124 N ATOM 1165 N ILE A 752 -1.003 9.122 54.414 1.00 16.75 N ANISOU 1165 N ILE A 752 2046 2136 2181 -106 -101 29 N ATOM 1166 CA ILE A 752 -0.604 9.118 53.020 1.00 14.06 C ANISOU 1166 CA ILE A 752 1867 1716 1758 -88 -172 26 C ATOM 1167 C ILE A 752 -1.308 7.917 52.398 1.00 16.86 C ANISOU 1167 C ILE A 752 2261 1991 2153 -86 -306 39 C ATOM 1168 O ILE A 752 -1.338 6.830 52.997 1.00 17.58 O ANISOU 1168 O ILE A 752 2262 2127 2291 -108 -276 59 O ATOM 1169 CB ILE A 752 0.933 8.879 52.897 1.00 16.03 C ANISOU 1169 CB ILE A 752 2167 1982 1944 -100 -30 5 C ATOM 1170 CG1 ILE A 752 1.735 9.966 53.653 1.00 18.62 C ANISOU 1170 CG1 ILE A 752 2409 2353 2312 -102 55 -21 C ATOM 1171 CG2 ILE A 752 1.325 8.798 51.454 1.00 17.25 C ANISOU 1171 CG2 ILE A 752 2565 2007 1983 -116 29 -20 C ATOM 1172 CD1 ILE A 752 1.448 11.398 53.124 1.00 22.66 C ANISOU 1172 CD1 ILE A 752 3021 2824 2766 -109 63 -22 C ATOM 1173 N LEU A 753 -1.876 8.097 51.204 1.00 15.77 N ANISOU 1173 N LEU A 753 1802 2064 2125 -33 64 -23 N ATOM 1174 CA LEU A 753 -2.564 6.982 50.505 1.00 15.25 C ANISOU 1174 CA LEU A 753 1694 1995 2105 -71 10 42 C ATOM 1175 C LEU A 753 -1.728 6.630 49.294 1.00 16.27 C ANISOU 1175 C LEU A 753 1891 2036 2253 -76 -48 29 C ATOM 1176 O LEU A 753 -1.009 7.497 48.768 1.00 16.52 O ANISOU 1176 O LEU A 753 1973 2025 2277 -43 -33 -16 O ATOM 1177 CB LEU A 753 -3.944 7.426 50.038 1.00 16.55 C ANISOU 1177 CB LEU A 753 1786 2190 2310 -34 13 60 C ATOM 1178 CG LEU A 753 -4.866 7.853 51.184 1.00 18.73 C ANISOU 1178 CG LEU A 753 1978 2574 2564 -3 92 69 C ATOM 1179 CD1 LEU A 753 -6.203 8.279 50.585 1.00 21.64 C ANISOU 1179 CD1 LEU A 753 2253 2979 2991 48 87 91 C ATOM 1180 CD2 LEU A 753 -5.059 6.639 52.122 1.00 23.86 C ANISOU 1180 CD2 LEU A 753 2578 3298 3189 -88 100 144 C ATOM 1181 N ILE A 754 -1.844 5.376 48.817 1.00 14.85 N ANISOU 1181 N ILE A 754 1718 1827 2096 -117 -114 70 N ATOM 1182 CA ILE A 754 -0.956 4.921 47.721 1.00 15.27 C ANISOU 1182 CA ILE A 754 1849 1804 2148 -104 -159 45 C ATOM 1183 C ILE A 754 -1.803 4.213 46.687 1.00 15.58 C ANISOU 1183 C ILE A 754 1903 1802 2217 -121 -240 68 C ATOM 1184 O ILE A 754 -2.669 3.408 47.049 1.00 16.25 O ANISOU 1184 O ILE A 754 1944 1899 2331 -178 -285 120 O ATOM 1185 CB ILE A 754 0.226 4.052 48.306 1.00 17.20 C ANISOU 1185 CB ILE A 754 2125 2036 2376 -116 -168 46 C ATOM 1186 CG1 ILE A 754 1.144 3.520 47.180 1.00 17.18 C ANISOU 1186 CG1 ILE A 754 2192 1968 2368 -77 -200 15 C ATOM 1187 CG2 ILE A 754 -0.279 2.957 49.257 1.00 16.41 C ANISOU 1187 CG2 ILE A 754 1999 1952 2284 -174 -203 109 C ATOM 1188 CD1 ILE A 754 2.469 2.965 47.675 1.00 17.58 C ANISOU 1188 CD1 ILE A 754 2254 2018 2408 -57 -196 6 C ATOM 1189 N ASN A 755 -1.583 4.524 45.413 1.00 16.58 N ANISOU 1189 N ASN A 755 2091 1881 2328 -81 -262 35 N ATOM 1190 CA ASN A 755 -2.462 4.001 44.374 1.00 17.68 C ANISOU 1190 CA ASN A 755 2255 1981 2481 -96 -354 48 C ATOM 1191 C ASN A 755 -1.920 2.725 43.730 1.00 19.13 C ANISOU 1191 C ASN A 755 2535 2088 2646 -102 -426 28 C ATOM 1192 O ASN A 755 -0.896 2.191 44.154 1.00 17.20 O ANISOU 1192 O ASN A 755 2322 1825 2387 -86 -400 11 O ATOM 1193 CB ASN A 755 -2.819 5.107 43.357 1.00 18.19 C ANISOU 1193 CB ASN A 755 2340 2045 2529 -46 -354 33 C ATOM 1194 CG ASN A 755 -1.672 5.494 42.434 1.00 16.22 C ANISOU 1194 CG ASN A 755 2188 1758 2216 4 -320 -8 C ATOM 1195 OD1 ASN A 755 -0.644 4.840 42.368 1.00 19.18 O ANISOU 1195 OD1 ASN A 755 2613 2113 2562 14 -303 -34 O ATOM 1196 ND2 ASN A 755 -1.908 6.553 41.626 1.00 18.16 N ANISOU 1196 ND2 ASN A 755 2463 1998 2438 41 -313 -6 N ATOM 1197 N SER A 756 -2.609 2.239 42.691 1.00 19.68 N ANISOU 1197 N SER A 756 2656 2107 2712 -116 -526 24 N ATOM 1198 CA SER A 756 -2.202 1.016 42.070 1.00 22.97 C ANISOU 1198 CA SER A 756 3186 2434 3106 -113 -606 -10 C ATOM 1199 C SER A 756 -0.778 1.048 41.493 1.00 22.21 C ANISOU 1199 C SER A 756 3182 2318 2939 -18 -543 -76 C ATOM 1200 O SER A 756 -0.169 -0.007 41.360 1.00 22.76 O ANISOU 1200 O SER A 756 3332 2321 2995 10 -579 -109 O ATOM 1201 CB SER A 756 -3.213 0.620 41.000 1.00 23.70 C ANISOU 1201 CB SER A 756 3332 2477 3195 -146 -737 -13 C ATOM 1202 OG SER A 756 -3.106 1.489 39.893 1.00 27.37 O ANISOU 1202 OG SER A 756 3849 2957 3593 -80 -721 -48 O ATOM 1203 N ASN A 757 -0.268 2.238 41.156 1.00 19.44 N ANISOU 1203 N ASN A 757 2816 2024 2549 30 -450 -88 N ATOM 1204 CA ASN A 757 1.056 2.398 40.541 1.00 20.58 C ANISOU 1204 CA ASN A 757 3018 2176 2625 109 -373 -134 C ATOM 1205 C ASN A 757 2.110 2.845 41.556 1.00 21.84 C ANISOU 1205 C ASN A 757 3096 2392 2809 116 -272 -124 C ATOM 1206 O ASN A 757 3.212 3.265 41.179 1.00 21.80 O ANISOU 1206 O ASN A 757 3095 2423 2763 164 -191 -143 O ATOM 1207 CB ASN A 757 0.978 3.446 39.426 1.00 23.42 C ANISOU 1207 CB ASN A 757 3420 2560 2919 139 -342 -137 C ATOM 1208 CG ASN A 757 0.221 2.939 38.233 1.00 30.89 C ANISOU 1208 CG ASN A 757 4472 3454 3809 149 -448 -160 C ATOM 1209 OD1 ASN A 757 -0.557 3.662 37.616 1.00 38.32 O ANISOU 1209 OD1 ASN A 757 5425 4405 4731 139 -484 -136 O ATOM 1210 ND2 ASN A 757 0.414 1.673 37.928 1.00 32.78 N ANISOU 1210 ND2 ASN A 757 4798 3630 4025 173 -513 -209 N ATOM 1211 N LEU A 758 1.745 2.747 42.835 1.00 16.67 N ANISOU 1211 N LEU A 758 2365 1753 2216 61 -282 -88 N ATOM 1212 CA LEU A 758 2.612 3.071 43.987 1.00 17.75 C ANISOU 1212 CA LEU A 758 2430 1941 2374 55 -216 -77 C ATOM 1213 C LEU A 758 2.839 4.566 44.160 1.00 18.36 C ANISOU 1213 C LEU A 758 2460 2071 2446 43 -138 -73 C ATOM 1214 O LEU A 758 3.759 4.989 44.878 1.00 18.71 O ANISOU 1214 O LEU A 758 2458 2155 2496 37 -88 -76 O ATOM 1215 CB LEU A 758 3.965 2.315 43.956 1.00 18.53 C ANISOU 1215 CB LEU A 758 2546 2035 2458 115 -198 -104 C ATOM 1216 CG LEU A 758 3.854 0.789 43.772 1.00 19.84 C ANISOU 1216 CG LEU A 758 2788 2120 2632 145 -285 -117 C ATOM 1217 CD1 LEU A 758 5.243 0.172 43.852 1.00 22.62 C ANISOU 1217 CD1 LEU A 758 3141 2476 2977 232 -258 -145 C ATOM 1218 CD2 LEU A 758 2.909 0.178 44.791 1.00 22.39 C ANISOU 1218 CD2 LEU A 758 3092 2411 3003 64 -356 -64 C ATOM 1219 N VAL A 759 1.992 5.376 43.529 1.00 16.98 N ANISOU 1219 N VAL A 759 2301 1888 2264 39 -142 -66 N ATOM 1220 CA VAL A 759 2.115 6.830 43.724 1.00 17.16 C ANISOU 1220 CA VAL A 759 2300 1932 2289 29 -83 -61 C ATOM 1221 C VAL A 759 1.494 7.190 45.056 1.00 16.19 C ANISOU 1221 C VAL A 759 2113 1835 2202 0 -78 -53 C ATOM 1222 O VAL A 759 0.352 6.827 45.321 1.00 16.63 O ANISOU 1222 O VAL A 759 2141 1897 2280 -10 -116 -33 O ATOM 1223 CB VAL A 759 1.439 7.614 42.610 1.00 17.80 C ANISOU 1223 CB VAL A 759 2430 1985 2348 49 -97 -50 C ATOM 1224 CG1 VAL A 759 1.543 9.159 42.871 1.00 17.14 C ANISOU 1224 CG1 VAL A 759 2340 1895 2276 41 -47 -41 C ATOM 1225 CG2 VAL A 759 2.076 7.250 41.225 1.00 20.45 C ANISOU 1225 CG2 VAL A 759 2846 2308 2617 83 -92 -59 C ATOM 1226 N CYS A 760 2.251 7.945 45.863 1.00 16.41 N ANISOU 1226 N CYS A 760 2120 1885 2232 -17 -29 -67 N ATOM 1227 CA CYS A 760 1.805 8.348 47.222 1.00 17.30 C ANISOU 1227 CA CYS A 760 2192 2028 2353 -34 -15 -74 C ATOM 1228 C CYS A 760 1.302 9.805 47.251 1.00 16.01 C ANISOU 1228 C CYS A 760 2046 1841 2195 -14 12 -93 C ATOM 1229 O CYS A 760 1.850 10.666 46.581 1.00 15.47 O ANISOU 1229 O CYS A 760 2022 1729 2126 -15 26 -99 O ATOM 1230 CB CYS A 760 2.963 8.208 48.198 1.00 15.48 C ANISOU 1230 CB CYS A 760 1942 1828 2109 -63 -1 -87 C ATOM 1231 SG CYS A 760 3.417 6.479 48.429 1.00 18.04 S ANISOU 1231 SG CYS A 760 2251 2170 2435 -65 -45 -60 S ATOM 1232 N LYS A 761 0.221 10.041 48.010 1.00 16.12 N ANISOU 1232 N LYS A 761 2026 1883 2215 9 20 -98 N ATOM 1233 CA LYS A 761 -0.464 11.315 47.969 1.00 14.98 C ANISOU 1233 CA LYS A 761 1902 1708 2083 59 38 -120 C ATOM 1234 C LYS A 761 -0.903 11.669 49.376 1.00 15.66 C ANISOU 1234 C LYS A 761 1961 1842 2148 81 77 -155 C ATOM 1235 O LYS A 761 -1.389 10.817 50.126 1.00 15.50 O ANISOU 1235 O LYS A 761 1879 1899 2112 69 88 -133 O ATOM 1236 CB LYS A 761 -1.722 11.210 47.077 1.00 16.02 C ANISOU 1236 CB LYS A 761 2005 1838 2244 104 4 -86 C ATOM 1237 CG LYS A 761 -1.374 10.807 45.642 1.00 15.95 C ANISOU 1237 CG LYS A 761 2043 1786 2232 89 -41 -57 C ATOM 1238 CD LYS A 761 -2.506 11.006 44.628 1.00 16.11 C ANISOU 1238 CD LYS A 761 2059 1788 2271 134 -95 -27 C ATOM 1239 CE LYS A 761 -2.041 10.449 43.255 1.00 18.08 C ANISOU 1239 CE LYS A 761 2378 2004 2486 115 -140 -7 C ATOM 1240 NZ LYS A 761 -2.675 11.199 42.105 1.00 17.75 N ANISOU 1240 NZ LYS A 761 2386 1921 2439 162 -188 20 N ATOM 1241 N VAL A 762 -0.754 12.941 49.710 1.00 15.29 N ANISOU 1241 N VAL A 762 1972 1744 2093 114 97 -207 N ATOM 1242 CA VAL A 762 -1.066 13.420 51.045 1.00 14.25 C ANISOU 1242 CA VAL A 762 1845 1650 1920 151 137 -262 C ATOM 1243 C VAL A 762 -2.583 13.483 51.191 1.00 16.75 C ANISOU 1243 C VAL A 762 2091 2025 2248 241 171 -254 C ATOM 1244 O VAL A 762 -3.285 13.974 50.290 1.00 17.44 O ANISOU 1244 O VAL A 762 2171 2070 2384 301 152 -238 O ATOM 1245 CB VAL A 762 -0.429 14.817 51.278 1.00 15.94 C ANISOU 1245 CB VAL A 762 2167 1764 2125 160 131 -333 C ATOM 1246 CG1 VAL A 762 -0.766 15.379 52.661 1.00 20.88 C ANISOU 1246 CG1 VAL A 762 2827 2419 2689 215 167 -412 C ATOM 1247 CG2 VAL A 762 1.103 14.713 51.044 1.00 18.32 C ANISOU 1247 CG2 VAL A 762 2504 2027 2429 53 94 -323 C ATOM 1248 N SER A 763 -3.081 13.006 52.337 1.00 16.52 N ANISOU 1248 N SER A 763 2002 2103 2170 252 221 -256 N ATOM 1249 CA SER A 763 -4.517 13.029 52.641 1.00 18.19 C ANISOU 1249 CA SER A 763 2115 2406 2388 336 273 -240 C ATOM 1250 C SER A 763 -4.764 13.593 54.040 1.00 21.47 C ANISOU 1250 C SER A 763 2550 2888 2719 404 354 -310 C ATOM 1251 O SER A 763 -3.849 14.098 54.699 1.00 21.50 O ANISOU 1251 O SER A 763 2663 2843 2662 389 350 -381 O ATOM 1252 CB SER A 763 -5.099 11.600 52.558 1.00 19.96 C ANISOU 1252 CB SER A 763 2221 2730 2633 265 265 -143 C ATOM 1253 OG SER A 763 -6.535 11.688 52.518 1.00 29.85 O ANISOU 1253 OG SER A 763 3350 4070 3922 336 301 -110 O ATOM 1254 N ASP A 764 -6.017 13.515 54.472 1.00 20.60 N ANISOU 1254 N ASP A 764 2329 2896 2602 482 425 -290 N ATOM 1255 CA ASP A 764 -6.430 13.903 55.817 1.00 25.55 C ANISOU 1255 CA ASP A 764 2956 3623 3128 563 525 -349 C ATOM 1256 C ASP A 764 -6.170 15.353 56.172 1.00 25.92 C ANISOU 1256 C ASP A 764 3142 3571 3136 679 538 -482 C ATOM 1257 O ASP A 764 -5.303 15.702 56.991 1.00 29.96 O ANISOU 1257 O ASP A 764 3780 4044 3558 655 533 -559 O ATOM 1258 CB ASP A 764 -5.877 12.970 56.886 1.00 29.76 C ANISOU 1258 CB ASP A 764 3498 4247 3561 463 550 -318 C ATOM 1259 CG ASP A 764 -6.678 13.068 58.207 1.00 38.60 C ANISOU 1259 CG ASP A 764 4572 5529 4564 544 676 -340 C ATOM 1260 OD1 ASP A 764 -6.565 12.151 59.050 1.00 45.94 O ANISOU 1260 OD1 ASP A 764 5475 6569 5411 462 709 -277 O ATOM 1261 OD2 ASP A 764 -7.445 14.046 58.386 1.00 42.86 O ANISOU 1261 OD2 ASP A 764 5102 6089 5092 696 745 -414 O ATOM 1262 N PHE A 765 -7.020 16.197 55.640 1.00 24.91 N ANISOU 1262 N PHE A 765 2990 3406 3070 814 551 -510 N ATOM 1263 CA PHE A 765 -6.910 17.620 55.904 1.00 27.25 C ANISOU 1263 CA PHE A 765 3430 3582 3342 943 554 -637 C ATOM 1264 C PHE A 765 -7.673 18.117 57.161 1.00 34.58 C ANISOU 1264 C PHE A 765 4355 4618 4165 1101 674 -729 C ATOM 1265 O PHE A 765 -7.855 19.319 57.368 1.00 37.45 O ANISOU 1265 O PHE A 765 4831 4885 4513 1251 684 -844 O ATOM 1266 CB PHE A 765 -7.196 18.358 54.599 1.00 27.54 C ANISOU 1266 CB PHE A 765 3486 3480 3499 1005 482 -622 C ATOM 1267 CG PHE A 765 -6.123 18.107 53.561 1.00 25.03 C ANISOU 1267 CG PHE A 765 3235 3039 3237 851 376 -565 C ATOM 1268 CD1 PHE A 765 -4.919 18.812 53.622 1.00 27.91 C ANISOU 1268 CD1 PHE A 765 3771 3251 3581 787 320 -627 C ATOM 1269 CD2 PHE A 765 -6.262 17.096 52.601 1.00 25.72 C ANISOU 1269 CD2 PHE A 765 3211 3173 3386 761 335 -451 C ATOM 1270 CE1 PHE A 765 -3.888 18.560 52.712 1.00 22.62 C ANISOU 1270 CE1 PHE A 765 3142 2496 2955 646 243 -568 C ATOM 1271 CE2 PHE A 765 -5.225 16.819 51.685 1.00 26.89 C ANISOU 1271 CE2 PHE A 765 3424 3227 3566 633 256 -406 C ATOM 1272 CZ PHE A 765 -4.034 17.569 51.747 1.00 25.98 C ANISOU 1272 CZ PHE A 765 3461 2979 3432 580 220 -461 C ATOM 1273 N GLY A 766 -8.047 17.180 58.030 1.00 36.81 N ANISOU 1273 N GLY A 766 4527 5096 4364 1066 764 -679 N ATOM 1274 CA GLY A 766 -8.879 17.508 59.200 1.00 43.25 C ANISOU 1274 CA GLY A 766 5311 6060 5063 1219 904 -746 C ATOM 1275 C GLY A 766 -8.223 18.357 60.278 1.00 45.79 C ANISOU 1275 C GLY A 766 5842 6316 5238 1283 920 -904 C ATOM 1276 O GLY A 766 -8.913 19.057 61.037 1.00 48.96 O ANISOU 1276 O GLY A 766 6269 6781 5551 1468 1024 -1006 O ATOM 1277 N LEU A 767 -6.896 18.294 60.364 1.00 47.61 N ANISOU 1277 N LEU A 767 6222 6426 5440 1136 814 -929 N ATOM 1278 CA LEU A 767 -6.179 18.886 61.497 1.00 52.10 C ANISOU 1278 CA LEU A 767 6987 6953 5855 1153 807 -1065 C ATOM 1279 C LEU A 767 -5.375 20.154 61.226 1.00 54.34 C ANISOU 1279 C LEU A 767 7485 6989 6172 1171 692 -1194 C ATOM 1280 O LEU A 767 -4.809 20.728 62.153 1.00 56.72 O ANISOU 1280 O LEU A 767 7964 7238 6349 1184 667 -1320 O ATOM 1281 CB LEU A 767 -5.266 17.849 62.173 1.00 51.91 C ANISOU 1281 CB LEU A 767 6975 7013 5737 974 774 -1004 C ATOM 1282 CG LEU A 767 -5.745 17.169 63.466 1.00 53.79 C ANISOU 1282 CG LEU A 767 7166 7475 5796 997 897 -983 C ATOM 1283 CD1 LEU A 767 -4.572 16.461 64.144 1.00 52.66 C ANISOU 1283 CD1 LEU A 767 7105 7347 5554 831 816 -953 C ATOM 1284 CD2 LEU A 767 -6.425 18.164 64.442 1.00 55.53 C ANISOU 1284 CD2 LEU A 767 7484 7747 5867 1206 1009 -1139 C ATOM 1285 N SER A 768 -5.304 20.621 59.987 1.00 54.18 N ANISOU 1285 N SER A 768 7466 6811 6310 1162 613 -1161 N ATOM 1286 CA SER A 768 -4.483 21.810 59.804 1.00 55.50 C ANISOU 1286 CA SER A 768 7846 6737 6503 1151 500 -1268 C ATOM 1287 C SER A 768 -5.109 23.050 59.180 1.00 54.89 C ANISOU 1287 C SER A 768 7851 6491 6512 1319 483 -1336 C ATOM 1288 O SER A 768 -6.320 23.095 58.921 1.00 53.67 O ANISOU 1288 O SER A 768 7578 6419 6398 1487 569 -1315 O ATOM 1289 CB SER A 768 -3.214 21.454 59.093 1.00 55.05 C ANISOU 1289 CB SER A 768 7807 6585 6526 931 378 -1187 C ATOM 1290 OG SER A 768 -3.479 20.525 58.057 1.00 61.82 O ANISOU 1290 OG SER A 768 8485 7516 7488 866 388 -1035 O ATOM 1291 N ARG A 769 -4.245 24.048 58.950 1.00 53.13 N ANISOU 1291 N ARG A 769 7831 6031 6325 1266 362 -1408 N ATOM 1292 CA ARG A 769 -4.665 25.437 58.731 1.00 53.06 C ANISOU 1292 CA ARG A 769 7984 5815 6360 1434 327 -1515 C ATOM 1293 C ARG A 769 -3.580 26.321 58.091 1.00 51.03 C ANISOU 1293 C ARG A 769 7915 5284 6189 1296 168 -1524 C ATOM 1294 O ARG A 769 -2.447 25.880 57.896 1.00 41.57 O ANISOU 1294 O ARG A 769 6712 4074 5007 1070 94 -1457 O ATOM 1295 CB ARG A 769 -5.129 26.052 60.064 1.00 59.66 C ANISOU 1295 CB ARG A 769 8952 6673 7044 1622 396 -1699 C ATOM 1296 CG ARG A 769 -4.436 25.491 61.302 1.00 62.19 C ANISOU 1296 CG ARG A 769 9318 7115 7195 1514 410 -1755 C ATOM 1297 CD ARG A 769 -5.370 25.528 62.516 1.00 71.00 C ANISOU 1297 CD ARG A 769 10440 8400 8139 1729 558 -1873 C ATOM 1298 NE ARG A 769 -5.104 24.391 63.394 1.00 75.69 N ANISOU 1298 NE ARG A 769 10940 9226 8592 1618 622 -1822 N ATOM 1299 CZ ARG A 769 -5.805 23.257 63.418 1.00 77.41 C ANISOU 1299 CZ ARG A 769 10919 9695 8797 1617 749 -1690 C ATOM 1300 NH1 ARG A 769 -6.862 23.089 62.625 1.00 77.67 N ANISOU 1300 NH1 ARG A 769 10763 9797 8951 1722 826 -1600 N ATOM 1301 NH2 ARG A 769 -5.446 22.281 64.248 1.00 77.08 N ANISOU 1301 NH2 ARG A 769 10831 9832 8624 1502 785 -1641 N ATOM 1302 N VAL A 770 -3.938 27.570 57.755 1.00 53.02 N ANISOU 1302 N VAL A 770 8328 5317 6501 1433 117 -1599 N ATOM 1303 CA VAL A 770 -2.940 28.587 57.371 1.00 55.83 C ANISOU 1303 CA VAL A 770 8905 5387 6921 1306 -36 -1627 C ATOM 1304 C VAL A 770 -2.098 28.949 58.578 1.00 55.88 C ANISOU 1304 C VAL A 770 9094 5329 6808 1228 -97 -1773 C ATOM 1305 O VAL A 770 -2.645 29.164 59.659 1.00 58.93 O ANISOU 1305 O VAL A 770 9556 5770 7067 1398 -34 -1923 O ATOM 1306 CB VAL A 770 -3.561 29.917 56.839 1.00 58.52 C ANISOU 1306 CB VAL A 770 9412 5475 7347 1488 -91 -1682 C ATOM 1307 CG1 VAL A 770 -3.501 29.981 55.333 1.00 59.48 C ANISOU 1307 CG1 VAL A 770 9476 5506 7617 1407 -149 -1511 C ATOM 1308 CG2 VAL A 770 -4.960 30.112 57.351 1.00 61.64 C ANISOU 1308 CG2 VAL A 770 9765 5962 7692 1801 27 -1779 C ATOM 1309 N PRO A 787 -0.803 14.352 67.683 1.00 43.09 N ANISOU 1309 N PRO A 787 6240 6304 3828 398 522 -897 N ATOM 1310 CA PRO A 787 -0.075 13.104 67.407 1.00 38.83 C ANISOU 1310 CA PRO A 787 5614 5781 3361 248 433 -741 C ATOM 1311 C PRO A 787 1.401 13.275 67.768 1.00 36.13 C ANISOU 1311 C PRO A 787 5387 5353 2986 150 255 -792 C ATOM 1312 O PRO A 787 2.234 13.618 66.902 1.00 31.63 O ANISOU 1312 O PRO A 787 4807 4638 2574 87 144 -812 O ATOM 1313 CB PRO A 787 -0.262 12.926 65.904 1.00 38.46 C ANISOU 1313 CB PRO A 787 5428 5634 3552 225 425 -673 C ATOM 1314 CG PRO A 787 -0.314 14.334 65.387 1.00 41.69 C ANISOU 1314 CG PRO A 787 5914 5902 4026 308 414 -819 C ATOM 1315 CD PRO A 787 -1.037 15.128 66.444 1.00 41.98 C ANISOU 1315 CD PRO A 787 6059 6011 3881 446 513 -944 C ATOM 1316 N ILE A 788 1.680 13.029 69.048 1.00 33.03 N ANISOU 1316 N ILE A 788 5098 5066 2386 137 232 -803 N ATOM 1317 CA ILE A 788 2.965 13.298 69.691 1.00 33.26 C ANISOU 1317 CA ILE A 788 5256 5045 2334 59 59 -869 C ATOM 1318 C ILE A 788 4.146 12.700 68.922 1.00 31.48 C ANISOU 1318 C ILE A 788 4937 4736 2287 -69 -91 -777 C ATOM 1319 O ILE A 788 5.142 13.376 68.734 1.00 28.34 O ANISOU 1319 O ILE A 788 4592 4227 1949 -128 -227 -856 O ATOM 1320 CB ILE A 788 2.947 12.794 71.159 1.00 35.61 C ANISOU 1320 CB ILE A 788 5656 5506 2369 61 66 -847 C ATOM 1321 CG1 ILE A 788 1.976 13.636 72.005 1.00 38.12 C ANISOU 1321 CG1 ILE A 788 6101 5903 2481 203 206 -983 C ATOM 1322 CG2 ILE A 788 4.351 12.703 71.773 1.00 38.16 C ANISOU 1322 CG2 ILE A 788 6073 5801 2626 -45 -142 -862 C ATOM 1323 CD1 ILE A 788 2.388 15.060 72.232 1.00 45.37 C ANISOU 1323 CD1 ILE A 788 7201 6687 3350 252 123 -1200 C ATOM 1324 N ARG A 789 4.042 11.438 68.509 1.00 22.59 N ANISOU 1324 N ARG A 789 2853 3248 2480 -111 266 -39 N ATOM 1325 CA ARG A 789 5.162 10.773 67.804 1.00 22.41 C ANISOU 1325 CA ARG A 789 2848 3185 2481 -117 203 -4 C ATOM 1326 C ARG A 789 5.587 11.449 66.507 1.00 21.59 C ANISOU 1326 C ARG A 789 2702 3062 2438 -93 153 -23 C ATOM 1327 O ARG A 789 6.736 11.289 66.073 1.00 21.60 O ANISOU 1327 O ARG A 789 2720 3035 2453 -88 104 -8 O ATOM 1328 CB ARG A 789 4.816 9.317 67.470 1.00 23.43 C ANISOU 1328 CB ARG A 789 2973 3301 2628 -162 224 36 C ATOM 1329 CG ARG A 789 4.858 8.416 68.693 1.00 23.72 C ANISOU 1329 CG ARG A 789 3086 3332 2593 -192 256 74 C ATOM 1330 CD ARG A 789 4.022 7.140 68.565 1.00 22.94 C ANISOU 1330 CD ARG A 789 2981 3224 2510 -250 307 106 C ATOM 1331 NE ARG A 789 4.561 6.214 69.558 1.00 24.34 N ANISOU 1331 NE ARG A 789 3265 3371 2613 -270 307 155 N ATOM 1332 CZ ARG A 789 4.443 6.347 70.879 1.00 24.69 C ANISOU 1332 CZ ARG A 789 3385 3428 2570 -274 350 164 C ATOM 1333 NH1 ARG A 789 3.705 7.325 71.446 1.00 25.52 N ANISOU 1333 NH1 ARG A 789 3463 3581 2650 -265 412 126 N ATOM 1334 NH2 ARG A 789 5.040 5.462 71.658 1.00 28.70 N ANISOU 1334 NH2 ARG A 789 4004 3895 3006 -283 332 212 N ATOM 1335 N TRP A 790 4.652 12.168 65.877 1.00 18.91 N ANISOU 1335 N TRP A 790 2310 2737 2136 -75 168 -57 N ATOM 1336 CA TRP A 790 4.938 12.791 64.575 1.00 18.37 C ANISOU 1336 CA TRP A 790 2221 2643 2115 -52 125 -71 C ATOM 1337 C TRP A 790 5.207 14.289 64.685 1.00 20.73 C ANISOU 1337 C TRP A 790 2538 2933 2407 -16 103 -105 C ATOM 1338 O TRP A 790 5.552 14.949 63.707 1.00 21.25 O ANISOU 1338 O TRP A 790 2606 2968 2500 1 70 -112 O ATOM 1339 CB TRP A 790 3.761 12.537 63.615 1.00 18.57 C ANISOU 1339 CB TRP A 790 2189 2677 2189 -49 135 -86 C ATOM 1340 CG TRP A 790 3.723 11.121 63.148 1.00 19.25 C ANISOU 1340 CG TRP A 790 2265 2754 2295 -86 137 -53 C ATOM 1341 CD1 TRP A 790 4.328 10.592 62.028 1.00 19.70 C ANISOU 1341 CD1 TRP A 790 2330 2778 2376 -87 99 -34 C ATOM 1342 CD2 TRP A 790 3.115 10.030 63.828 1.00 18.80 C ANISOU 1342 CD2 TRP A 790 2198 2714 2231 -130 182 -34 C ATOM 1343 NE1 TRP A 790 4.088 9.239 61.956 1.00 19.12 N ANISOU 1343 NE1 TRP A 790 2252 2699 2315 -123 109 -9 N ATOM 1344 CE2 TRP A 790 3.329 8.867 63.033 1.00 21.77 C ANISOU 1344 CE2 TRP A 790 2576 3061 2634 -155 159 -6 C ATOM 1345 CE3 TRP A 790 2.357 9.923 65.019 1.00 21.00 C ANISOU 1345 CE3 TRP A 790 2472 3028 2480 -154 247 -39 C ATOM 1346 CZ2 TRP A 790 2.857 7.592 63.409 1.00 22.64 C ANISOU 1346 CZ2 TRP A 790 2689 3167 2747 -206 192 20 C ATOM 1347 CZ3 TRP A 790 1.867 8.649 65.390 1.00 23.25 C ANISOU 1347 CZ3 TRP A 790 2757 3312 2764 -211 291 -10 C ATOM 1348 CH2 TRP A 790 2.136 7.500 64.580 1.00 21.71 C ANISOU 1348 CH2 TRP A 790 2569 3079 2601 -239 258 21 C ATOM 1349 N THR A 791 5.099 14.822 65.902 1.00 20.39 N ANISOU 1349 N THR A 791 2520 2909 2320 -5 121 -125 N ATOM 1350 CA THR A 791 5.127 16.272 66.080 1.00 20.28 C ANISOU 1350 CA THR A 791 2524 2882 2298 33 101 -167 C ATOM 1351 C THR A 791 6.494 16.810 66.544 1.00 19.88 C ANISOU 1351 C THR A 791 2524 2802 2227 28 57 -165 C ATOM 1352 O THR A 791 7.157 16.210 67.403 1.00 23.35 O ANISOU 1352 O THR A 791 2992 3248 2630 11 51 -147 O ATOM 1353 CB THR A 791 4.010 16.672 67.079 1.00 20.92 C ANISOU 1353 CB THR A 791 2596 3005 2347 58 149 -206 C ATOM 1354 OG1 THR A 791 2.756 16.219 66.570 1.00 20.27 O ANISOU 1354 OG1 THR A 791 2448 2953 2303 59 187 -217 O ATOM 1355 CG2 THR A 791 3.928 18.181 67.294 1.00 22.60 C ANISOU 1355 CG2 THR A 791 2833 3201 2551 106 125 -257 C ATOM 1356 N SER A 792 6.881 17.970 66.003 1.00 21.33 N ANISOU 1356 N SER A 792 2722 2947 2434 44 23 -187 N ATOM 1357 CA SER A 792 8.195 18.521 66.340 1.00 19.24 C ANISOU 1357 CA SER A 792 2493 2650 2167 29 -20 -191 C ATOM 1358 C SER A 792 8.250 18.933 67.811 1.00 20.34 C ANISOU 1358 C SER A 792 2673 2804 2251 45 -28 -221 C ATOM 1359 O SER A 792 7.188 19.209 68.425 1.00 20.49 O ANISOU 1359 O SER A 792 2700 2851 2235 77 6 -248 O ATOM 1360 CB SER A 792 8.522 19.728 65.468 1.00 19.98 C ANISOU 1360 CB SER A 792 2603 2693 2297 32 -46 -207 C ATOM 1361 OG SER A 792 7.751 20.827 65.885 1.00 19.80 O ANISOU 1361 OG SER A 792 2607 2660 2254 73 -49 -250 O ATOM 1362 N PRO A 793 9.465 18.991 68.382 1.00 20.06 N ANISOU 1362 N PRO A 793 2664 2751 2209 29 -74 -223 N ATOM 1363 CA PRO A 793 9.556 19.334 69.821 1.00 21.16 C ANISOU 1363 CA PRO A 793 2856 2900 2283 49 -93 -254 C ATOM 1364 C PRO A 793 8.953 20.705 70.145 1.00 22.19 C ANISOU 1364 C PRO A 793 3018 3016 2398 85 -94 -306 C ATOM 1365 O PRO A 793 8.317 20.858 71.219 1.00 23.93 O ANISOU 1365 O PRO A 793 3276 3263 2552 118 -72 -334 O ATOM 1366 CB PRO A 793 11.066 19.357 70.094 1.00 24.16 C ANISOU 1366 CB PRO A 793 3245 3252 2681 27 -163 -259 C ATOM 1367 CG PRO A 793 11.711 18.686 68.957 1.00 25.72 C ANISOU 1367 CG PRO A 793 3387 3440 2943 -7 -163 -223 C ATOM 1368 CD PRO A 793 10.795 18.728 67.783 1.00 21.64 C ANISOU 1368 CD PRO A 793 2842 2924 2457 -6 -112 -205 C ATOM 1369 N GLU A 794 9.169 21.699 69.277 1.00 21.35 N ANISOU 1369 N GLU A 794 2907 2862 2344 81 -118 -321 N ATOM 1370 CA GLU A 794 8.642 23.051 69.539 1.00 21.51 C ANISOU 1370 CA GLU A 794 2967 2853 2351 121 -131 -373 C ATOM 1371 C GLU A 794 7.108 23.083 69.420 1.00 21.55 C ANISOU 1371 C GLU A 794 2953 2895 2342 170 -76 -389 C ATOM 1372 O GLU A 794 6.448 23.834 70.122 1.00 21.77 O ANISOU 1372 O GLU A 794 3011 2928 2334 218 -70 -438 O ATOM 1373 CB GLU A 794 9.318 24.133 68.675 1.00 21.62 C ANISOU 1373 CB GLU A 794 2998 2794 2421 99 -173 -381 C ATOM 1374 CG GLU A 794 8.976 24.091 67.156 1.00 22.09 C ANISOU 1374 CG GLU A 794 3031 2832 2530 90 -151 -348 C ATOM 1375 CD GLU A 794 9.771 23.048 66.338 1.00 21.33 C ANISOU 1375 CD GLU A 794 2889 2745 2471 37 -138 -295 C ATOM 1376 OE1 GLU A 794 10.650 22.325 66.879 1.00 23.81 O ANISOU 1376 OE1 GLU A 794 3182 3081 2784 8 -150 -283 O ATOM 1377 OE2 GLU A 794 9.486 22.957 65.114 1.00 22.18 O ANISOU 1377 OE2 GLU A 794 2984 2836 2606 33 -119 -269 O ATOM 1378 N ALA A 795 6.545 22.274 68.516 1.00 20.34 N ANISOU 1378 N ALA A 795 2743 2765 2219 160 -40 -354 N ATOM 1379 CA ALA A 795 5.096 22.203 68.378 1.00 20.35 C ANISOU 1379 CA ALA A 795 2706 2806 2221 202 7 -375 C ATOM 1380 C ALA A 795 4.498 21.522 69.623 1.00 22.05 C ANISOU 1380 C ALA A 795 2914 3086 2377 208 66 -385 C ATOM 1381 O ALA A 795 3.462 21.948 70.124 1.00 23.40 O ANISOU 1381 O ALA A 795 3075 3289 2528 254 105 -431 O ATOM 1382 CB ALA A 795 4.718 21.461 67.098 1.00 19.68 C ANISOU 1382 CB ALA A 795 2564 2725 2187 185 19 -339 C ATOM 1383 N ILE A 796 5.155 20.481 70.145 1.00 20.41 N ANISOU 1383 N ILE A 796 2720 2895 2138 165 75 -343 N ATOM 1384 CA ILE A 796 4.741 19.908 71.449 1.00 22.81 C ANISOU 1384 CA ILE A 796 3052 3249 2368 167 130 -346 C ATOM 1385 C ILE A 796 4.868 20.898 72.614 1.00 23.32 C ANISOU 1385 C ILE A 796 3187 3307 2365 208 115 -399 C ATOM 1386 O ILE A 796 3.949 21.010 73.451 1.00 23.70 O ANISOU 1386 O ILE A 796 3246 3399 2361 239 179 -433 O ATOM 1387 CB ILE A 796 5.547 18.633 71.775 1.00 22.17 C ANISOU 1387 CB ILE A 796 2993 3170 2258 119 124 -289 C ATOM 1388 CG1 ILE A 796 5.213 17.544 70.738 1.00 22.71 C ANISOU 1388 CG1 ILE A 796 2996 3249 2383 82 151 -242 C ATOM 1389 CG2 ILE A 796 5.248 18.132 73.207 1.00 25.86 C ANISOU 1389 CG2 ILE A 796 3523 3674 2629 121 175 -288 C ATOM 1390 CD1 ILE A 796 6.191 16.368 70.744 1.00 26.37 C ANISOU 1390 CD1 ILE A 796 3482 3698 2840 42 124 -187 C ATOM 1391 N ALA A 797 6.017 21.575 72.683 1.00 20.88 N ANISOU 1391 N ALA A 797 2926 2947 2061 206 34 -409 N ATOM 1392 CA ALA A 797 6.359 22.429 73.847 1.00 22.29 C ANISOU 1392 CA ALA A 797 3185 3111 2174 240 -1 -459 C ATOM 1393 C ALA A 797 5.417 23.609 73.982 1.00 22.75 C ANISOU 1393 C ALA A 797 3251 3167 2226 301 18 -525 C ATOM 1394 O ALA A 797 4.975 23.929 75.081 1.00 23.13 O ANISOU 1394 O ALA A 797 3350 3241 2199 342 47 -569 O ATOM 1395 CB ALA A 797 7.818 22.928 73.760 1.00 22.70 C ANISOU 1395 CB ALA A 797 3269 3100 2254 215 -101 -462 C ATOM 1396 N TYR A 798 5.125 24.274 72.863 1.00 21.94 N ANISOU 1396 N TYR A 798 3107 3031 2198 313 -1 -535 N ATOM 1397 CA TYR A 798 4.287 25.491 72.917 1.00 20.64 C ANISOU 1397 CA TYR A 798 2956 2852 2034 383 -1 -603 C ATOM 1398 C TYR A 798 3.463 25.765 71.642 1.00 22.02 C ANISOU 1398 C TYR A 798 3068 3016 2284 407 5 -606 C ATOM 1399 O TYR A 798 3.139 26.928 71.336 1.00 24.60 O ANISOU 1399 O TYR A 798 3420 3296 2631 460 -33 -654 O ATOM 1400 CB TYR A 798 5.107 26.712 73.333 1.00 20.38 C ANISOU 1400 CB TYR A 798 3008 2749 1989 399 -82 -646 C ATOM 1401 CG TYR A 798 6.121 27.297 72.354 1.00 21.98 C ANISOU 1401 CG TYR A 798 3223 2867 2261 356 -158 -625 C ATOM 1402 CD1 TYR A 798 5.918 28.568 71.799 1.00 25.22 C ANISOU 1402 CD1 TYR A 798 3668 3208 2706 390 -201 -662 C ATOM 1403 CD2 TYR A 798 7.309 26.623 72.012 1.00 23.53 C ANISOU 1403 CD2 TYR A 798 3404 3050 2488 281 -187 -570 C ATOM 1404 CE1 TYR A 798 6.859 29.142 70.942 1.00 23.48 C ANISOU 1404 CE1 TYR A 798 3473 2904 2543 341 -259 -639 C ATOM 1405 CE2 TYR A 798 8.250 27.195 71.120 1.00 20.13 C ANISOU 1405 CE2 TYR A 798 2980 2545 2124 235 -241 -554 C ATOM 1406 CZ TYR A 798 8.011 28.459 70.603 1.00 25.40 C ANISOU 1406 CZ TYR A 798 3690 3143 2819 260 -272 -586 C ATOM 1407 OH TYR A 798 8.914 29.059 69.735 1.00 25.38 O ANISOU 1407 OH TYR A 798 3706 3060 2876 205 -313 -567 O ATOM 1408 N ARG A 799 3.151 24.693 70.925 1.00 22.40 N ANISOU 1408 N ARG A 799 3044 3100 2367 371 43 -557 N ATOM 1409 CA ARG A 799 2.240 24.769 69.766 1.00 24.63 C ANISOU 1409 CA ARG A 799 3262 3383 2714 399 47 -563 C ATOM 1410 C ARG A 799 2.801 25.659 68.659 1.00 24.04 C ANISOU 1410 C ARG A 799 3228 3222 2686 403 -31 -555 C ATOM 1411 O ARG A 799 2.050 26.368 67.965 1.00 22.43 O ANISOU 1411 O ARG A 799 3018 2992 2514 460 -55 -588 O ATOM 1412 CB ARG A 799 0.834 25.265 70.194 1.00 26.72 C ANISOU 1412 CB ARG A 799 3487 3691 2972 478 90 -636 C ATOM 1413 CG ARG A 799 0.157 24.426 71.272 1.00 32.79 C ANISOU 1413 CG ARG A 799 4216 4549 3695 469 188 -646 C ATOM 1414 CD ARG A 799 -1.370 24.669 71.332 1.00 37.78 C ANISOU 1414 CD ARG A 799 4764 5238 4353 536 246 -716 C ATOM 1415 NE ARG A 799 -2.068 23.900 70.292 1.00 51.69 N ANISOU 1415 NE ARG A 799 6424 7026 6191 516 259 -696 N ATOM 1416 CZ ARG A 799 -2.596 24.397 69.165 1.00 56.39 C ANISOU 1416 CZ ARG A 799 6978 7592 6857 565 200 -722 C ATOM 1417 NH1 ARG A 799 -2.550 25.701 68.884 1.00 58.41 N ANISOU 1417 NH1 ARG A 799 7289 7786 7118 638 127 -767 N ATOM 1418 NH2 ARG A 799 -3.187 23.570 68.311 1.00 56.10 N ANISOU 1418 NH2 ARG A 799 6851 7581 6882 542 209 -704 N ATOM 1419 N LYS A 800 4.121 25.629 68.492 1.00 22.91 N ANISOU 1419 N LYS A 800 3129 3032 2546 343 -69 -513 N ATOM 1420 CA LYS A 800 4.752 26.377 67.411 1.00 22.44 C ANISOU 1420 CA LYS A 800 3112 2888 2527 327 -125 -496 C ATOM 1421 C LYS A 800 4.686 25.517 66.154 1.00 22.51 C ANISOU 1421 C LYS A 800 3072 2904 2576 296 -112 -442 C ATOM 1422 O LYS A 800 5.623 24.729 65.901 1.00 21.09 O ANISOU 1422 O LYS A 800 2879 2728 2407 231 -105 -392 O ATOM 1423 CB LYS A 800 6.221 26.689 67.753 1.00 23.92 C ANISOU 1423 CB LYS A 800 3350 3027 2711 267 -163 -480 C ATOM 1424 CG LYS A 800 6.929 27.591 66.746 1.00 23.89 C ANISOU 1424 CG LYS A 800 3398 2929 2749 238 -208 -465 C ATOM 1425 CD LYS A 800 6.088 28.814 66.389 1.00 24.54 C ANISOU 1425 CD LYS A 800 3537 2955 2833 308 -239 -508 C ATOM 1426 CE LYS A 800 6.012 29.812 67.556 1.00 24.23 C ANISOU 1426 CE LYS A 800 3554 2893 2760 350 -269 -574 C ATOM 1427 NZ LYS A 800 5.281 31.085 67.203 1.00 31.30 N ANISOU 1427 NZ LYS A 800 4516 3718 3659 424 -311 -620 N ATOM 1428 N PHE A 801 3.595 25.649 65.397 1.00 22.80 N ANISOU 1428 N PHE A 801 3084 2945 2636 349 -114 -459 N ATOM 1429 CA PHE A 801 3.430 24.862 64.135 1.00 21.37 C ANISOU 1429 CA PHE A 801 2865 2766 2488 329 -111 -415 C ATOM 1430 C PHE A 801 3.792 25.723 62.939 1.00 22.26 C ANISOU 1430 C PHE A 801 3051 2789 2617 336 -162 -400 C ATOM 1431 O PHE A 801 3.258 26.835 62.795 1.00 23.31 O ANISOU 1431 O PHE A 801 3234 2874 2748 398 -202 -440 O ATOM 1432 CB PHE A 801 1.992 24.380 63.990 1.00 22.42 C ANISOU 1432 CB PHE A 801 2920 2957 2640 381 -90 -447 C ATOM 1433 CG PHE A 801 1.606 23.283 64.936 1.00 21.70 C ANISOU 1433 CG PHE A 801 2756 2952 2536 355 -23 -446 C ATOM 1434 CD1 PHE A 801 1.858 21.949 64.614 1.00 24.03 C ANISOU 1434 CD1 PHE A 801 3008 3278 2843 295 5 -394 C ATOM 1435 CD2 PHE A 801 0.963 23.580 66.133 1.00 25.48 C ANISOU 1435 CD2 PHE A 801 3217 3477 2987 391 15 -498 C ATOM 1436 CE1 PHE A 801 1.496 20.917 65.478 1.00 23.39 C ANISOU 1436 CE1 PHE A 801 2876 3265 2747 265 68 -387 C ATOM 1437 CE2 PHE A 801 0.586 22.544 67.001 1.00 26.67 C ANISOU 1437 CE2 PHE A 801 3313 3703 3118 359 89 -491 C ATOM 1438 CZ PHE A 801 0.846 21.223 66.666 1.00 24.21 C ANISOU 1438 CZ PHE A 801 2967 3414 2819 294 114 -433 C ATOM 1439 N THR A 802 4.724 25.230 62.116 1.00 21.72 N ANISOU 1439 N THR A 802 2997 2696 2559 273 -157 -343 N ATOM 1440 CA THR A 802 5.254 25.952 60.947 1.00 22.31 C ANISOU 1440 CA THR A 802 3155 2683 2640 260 -187 -316 C ATOM 1441 C THR A 802 5.525 24.916 59.849 1.00 19.51 C ANISOU 1441 C THR A 802 2777 2341 2295 224 -166 -264 C ATOM 1442 O THR A 802 5.471 23.715 60.098 1.00 17.63 O ANISOU 1442 O THR A 802 2464 2171 2065 202 -135 -250 O ATOM 1443 CB THR A 802 6.603 26.672 61.269 1.00 21.46 C ANISOU 1443 CB THR A 802 3105 2517 2532 196 -190 -303 C ATOM 1444 OG1 THR A 802 7.633 25.711 61.539 1.00 21.39 O ANISOU 1444 OG1 THR A 802 3043 2549 2534 124 -155 -270 O ATOM 1445 CG2 THR A 802 6.482 27.664 62.478 1.00 21.78 C ANISOU 1445 CG2 THR A 802 3176 2542 2559 227 -216 -358 C ATOM 1446 N SER A 803 5.881 25.339 58.639 1.00 18.77 N ANISOU 1446 N SER A 803 2758 2177 2196 214 -180 -234 N ATOM 1447 CA SER A 803 6.212 24.310 57.651 1.00 19.69 C ANISOU 1447 CA SER A 803 2857 2309 2315 181 -155 -189 C ATOM 1448 C SER A 803 7.431 23.510 58.131 1.00 19.69 C ANISOU 1448 C SER A 803 2806 2347 2330 103 -108 -161 C ATOM 1449 O SER A 803 7.587 22.339 57.791 1.00 17.74 O ANISOU 1449 O SER A 803 2509 2141 2089 83 -84 -137 O ATOM 1450 CB SER A 803 6.385 24.901 56.256 1.00 22.25 C ANISOU 1450 CB SER A 803 3286 2551 2616 185 -171 -160 C ATOM 1451 OG SER A 803 5.087 25.248 55.743 1.00 26.84 O ANISOU 1451 OG SER A 803 3897 3114 3186 274 -229 -190 O ATOM 1452 N ALA A 804 8.280 24.119 58.962 1.00 18.45 N ANISOU 1452 N ALA A 804 2658 2172 2181 64 -104 -171 N ATOM 1453 CA ALA A 804 9.416 23.346 59.529 1.00 19.27 C ANISOU 1453 CA ALA A 804 2703 2315 2304 1 -75 -155 C ATOM 1454 C ALA A 804 8.993 22.237 60.511 1.00 18.97 C ANISOU 1454 C ALA A 804 2588 2358 2261 17 -69 -166 C ATOM 1455 O ALA A 804 9.719 21.253 60.701 1.00 17.76 O ANISOU 1455 O ALA A 804 2388 2240 2119 -18 -51 -146 O ATOM 1456 CB ALA A 804 10.462 24.303 60.181 1.00 19.81 C ANISOU 1456 CB ALA A 804 2797 2341 2389 -45 -84 -171 C ATOM 1457 N SER A 805 7.835 22.388 61.165 1.00 19.11 N ANISOU 1457 N SER A 805 2595 2405 2262 71 -81 -198 N ATOM 1458 CA SER A 805 7.352 21.306 62.008 1.00 17.63 C ANISOU 1458 CA SER A 805 2345 2289 2064 77 -61 -202 C ATOM 1459 C SER A 805 6.779 20.227 61.120 1.00 18.53 C ANISOU 1459 C SER A 805 2422 2429 2191 82 -47 -177 C ATOM 1460 O SER A 805 6.865 19.056 61.455 1.00 18.47 O ANISOU 1460 O SER A 805 2371 2464 2183 59 -26 -159 O ATOM 1461 CB SER A 805 6.331 21.772 63.083 1.00 18.39 C ANISOU 1461 CB SER A 805 2434 2415 2138 126 -61 -248 C ATOM 1462 OG SER A 805 5.212 22.418 62.511 1.00 21.42 O ANISOU 1462 OG SER A 805 2827 2783 2528 183 -78 -277 O ATOM 1463 N ASP A 806 6.273 20.603 59.949 1.00 17.49 N ANISOU 1463 N ASP A 806 2318 2262 2067 109 -64 -176 N ATOM 1464 CA ASP A 806 5.869 19.562 58.980 1.00 16.04 C ANISOU 1464 CA ASP A 806 2107 2094 1894 111 -61 -155 C ATOM 1465 C ASP A 806 7.106 18.808 58.436 1.00 16.91 C ANISOU 1465 C ASP A 806 2222 2195 2008 59 -40 -113 C ATOM 1466 O ASP A 806 7.046 17.585 58.162 1.00 15.87 O ANISOU 1466 O ASP A 806 2053 2092 1884 47 -28 -95 O ATOM 1467 CB ASP A 806 5.081 20.145 57.808 1.00 16.37 C ANISOU 1467 CB ASP A 806 2192 2095 1935 161 -97 -167 C ATOM 1468 CG ASP A 806 3.573 20.293 58.077 1.00 20.23 C ANISOU 1468 CG ASP A 806 2636 2614 2437 222 -122 -215 C ATOM 1469 OD1 ASP A 806 3.017 19.810 59.107 1.00 17.86 O ANISOU 1469 OD1 ASP A 806 2266 2374 2148 220 -95 -237 O ATOM 1470 OD2 ASP A 806 2.925 20.940 57.212 1.00 17.78 O ANISOU 1470 OD2 ASP A 806 2366 2264 2126 276 -168 -234 O ATOM 1471 N VAL A 807 8.224 19.518 58.287 1.00 16.96 N ANISOU 1471 N VAL A 807 2269 2160 2014 28 -33 -101 N ATOM 1472 CA VAL A 807 9.484 18.869 57.840 1.00 16.27 C ANISOU 1472 CA VAL A 807 2171 2071 1939 -20 -6 -72 C ATOM 1473 C VAL A 807 9.913 17.842 58.896 1.00 17.06 C ANISOU 1473 C VAL A 807 2210 2223 2050 -39 0 -70 C ATOM 1474 O VAL A 807 10.291 16.726 58.557 1.00 15.89 O ANISOU 1474 O VAL A 807 2033 2094 1910 -51 12 -51 O ATOM 1475 CB VAL A 807 10.602 19.887 57.510 1.00 16.82 C ANISOU 1475 CB VAL A 807 2285 2087 2017 -61 9 -65 C ATOM 1476 CG1 VAL A 807 11.974 19.179 57.358 1.00 17.76 C ANISOU 1476 CG1 VAL A 807 2363 2222 2164 -111 42 -49 C ATOM 1477 CG2 VAL A 807 10.240 20.610 56.183 1.00 17.60 C ANISOU 1477 CG2 VAL A 807 2467 2126 2093 -44 11 -52 C ATOM 1478 N TRP A 808 9.810 18.183 60.181 1.00 15.47 N ANISOU 1478 N TRP A 808 1998 2040 1841 -36 -13 -92 N ATOM 1479 CA TRP A 808 10.059 17.181 61.230 1.00 14.15 C ANISOU 1479 CA TRP A 808 1792 1917 1667 -45 -14 -88 C ATOM 1480 C TRP A 808 9.200 15.915 61.014 1.00 15.69 C ANISOU 1480 C TRP A 808 1960 2143 1856 -34 -1 -71 C ATOM 1481 O TRP A 808 9.700 14.756 61.055 1.00 15.88 O ANISOU 1481 O TRP A 808 1966 2183 1886 -49 2 -50 O ATOM 1482 CB TRP A 808 9.722 17.771 62.619 1.00 17.26 C ANISOU 1482 CB TRP A 808 2197 2326 2034 -31 -27 -117 C ATOM 1483 CG TRP A 808 9.976 16.774 63.736 1.00 16.63 C ANISOU 1483 CG TRP A 808 2103 2284 1932 -38 -29 -109 C ATOM 1484 CD1 TRP A 808 9.186 15.724 64.085 1.00 20.09 C ANISOU 1484 CD1 TRP A 808 2528 2756 2349 -32 -8 -93 C ATOM 1485 CD2 TRP A 808 11.100 16.751 64.629 1.00 18.00 C ANISOU 1485 CD2 TRP A 808 2282 2457 2101 -52 -60 -116 C ATOM 1486 NE1 TRP A 808 9.756 15.028 65.134 1.00 17.20 N ANISOU 1486 NE1 TRP A 808 2173 2405 1955 -41 -21 -84 N ATOM 1487 CE2 TRP A 808 10.929 15.639 65.482 1.00 19.77 C ANISOU 1487 CE2 TRP A 808 2510 2712 2290 -47 -59 -101 C ATOM 1488 CE3 TRP A 808 12.226 17.577 64.803 1.00 20.03 C ANISOU 1488 CE3 TRP A 808 2543 2686 2381 -71 -92 -138 C ATOM 1489 CZ2 TRP A 808 11.840 15.321 66.504 1.00 18.99 C ANISOU 1489 CZ2 TRP A 808 2428 2617 2171 -48 -99 -106 C ATOM 1490 CZ3 TRP A 808 13.143 17.249 65.822 1.00 20.14 C ANISOU 1490 CZ3 TRP A 808 2555 2710 2387 -75 -134 -150 C ATOM 1491 CH2 TRP A 808 12.944 16.119 66.645 1.00 20.16 C ANISOU 1491 CH2 TRP A 808 2571 2743 2347 -58 -142 -133 C ATOM 1492 N SER A 809 7.894 16.131 60.825 1.00 15.33 N ANISOU 1492 N SER A 809 1913 2107 1806 -6 3 -86 N ATOM 1493 CA SER A 809 6.946 15.041 60.605 1.00 16.39 C ANISOU 1493 CA SER A 809 2014 2268 1946 -2 14 -78 C ATOM 1494 C SER A 809 7.359 14.236 59.386 1.00 15.92 C ANISOU 1494 C SER A 809 1957 2190 1903 -11 9 -53 C ATOM 1495 O SER A 809 7.301 12.981 59.399 1.00 16.53 O ANISOU 1495 O SER A 809 2014 2282 1986 -26 14 -36 O ATOM 1496 CB SER A 809 5.516 15.577 60.414 1.00 17.16 C ANISOU 1496 CB SER A 809 2095 2375 2050 35 11 -110 C ATOM 1497 OG SER A 809 5.111 16.302 61.561 1.00 17.26 O ANISOU 1497 OG SER A 809 2106 2408 2045 50 23 -138 O ATOM 1498 N TYR A 810 7.786 14.937 58.330 1.00 16.41 N ANISOU 1498 N TYR A 810 2052 2214 1967 -3 0 -52 N ATOM 1499 CA TYR A 810 8.268 14.244 57.137 1.00 15.33 C ANISOU 1499 CA TYR A 810 1930 2060 1837 -8 3 -32 C ATOM 1500 C TYR A 810 9.443 13.306 57.474 1.00 14.72 C ANISOU 1500 C TYR A 810 1831 1994 1769 -36 17 -14 C ATOM 1501 O TYR A 810 9.533 12.184 56.959 1.00 15.47 O ANISOU 1501 O TYR A 810 1917 2091 1868 -36 16 -1 O ATOM 1502 CB TYR A 810 8.684 15.257 56.041 1.00 14.41 C ANISOU 1502 CB TYR A 810 1869 1896 1709 -1 6 -29 C ATOM 1503 CG TYR A 810 9.111 14.506 54.809 1.00 14.71 C ANISOU 1503 CG TYR A 810 1929 1919 1741 -2 17 -12 C ATOM 1504 CD1 TYR A 810 8.164 14.088 53.879 1.00 15.66 C ANISOU 1504 CD1 TYR A 810 2069 2029 1850 30 -9 -17 C ATOM 1505 CD2 TYR A 810 10.452 14.147 54.628 1.00 14.66 C ANISOU 1505 CD2 TYR A 810 1915 1912 1744 -31 50 2 C ATOM 1506 CE1 TYR A 810 8.578 13.353 52.704 1.00 15.87 C ANISOU 1506 CE1 TYR A 810 2128 2039 1862 35 0 -4 C ATOM 1507 CE2 TYR A 810 10.866 13.403 53.518 1.00 13.90 C ANISOU 1507 CE2 TYR A 810 1838 1806 1639 -26 68 13 C ATOM 1508 CZ TYR A 810 9.931 13.025 52.568 1.00 16.53 C ANISOU 1508 CZ TYR A 810 2207 2123 1948 7 44 11 C ATOM 1509 OH TYR A 810 10.404 12.306 51.501 1.00 17.44 O ANISOU 1509 OH TYR A 810 2351 2227 2048 15 62 18 O ATOM 1510 N GLY A 811 10.363 13.766 58.319 1.00 17.20 N ANISOU 1510 N GLY A 811 2137 2312 2086 -54 19 -17 N ATOM 1511 CA GLY A 811 11.441 12.903 58.783 1.00 16.30 C ANISOU 1511 CA GLY A 811 1997 2212 1986 -69 17 -9 C ATOM 1512 C GLY A 811 10.938 11.623 59.436 1.00 15.56 C ANISOU 1512 C GLY A 811 1892 2139 1881 -64 5 3 C ATOM 1513 O GLY A 811 11.482 10.532 59.215 1.00 15.78 O ANISOU 1513 O GLY A 811 1911 2165 1919 -63 -1 15 O ATOM 1514 N ILE A 812 9.865 11.733 60.207 1.00 15.12 N ANISOU 1514 N ILE A 812 1839 2100 1807 -62 7 -1 N ATOM 1515 CA ILE A 812 9.249 10.552 60.835 1.00 14.80 C ANISOU 1515 CA ILE A 812 1796 2075 1753 -70 9 15 C ATOM 1516 C ILE A 812 8.667 9.646 59.762 1.00 16.45 C ANISOU 1516 C ILE A 812 1997 2271 1980 -70 10 24 C ATOM 1517 O ILE A 812 8.859 8.446 59.805 1.00 14.90 O ANISOU 1517 O ILE A 812 1808 2068 1787 -78 2 42 O ATOM 1518 CB ILE A 812 8.197 10.945 61.885 1.00 15.47 C ANISOU 1518 CB ILE A 812 1880 2184 1813 -73 28 5 C ATOM 1519 CG1 ILE A 812 8.822 11.842 63.008 1.00 14.79 C ANISOU 1519 CG1 ILE A 812 1814 2105 1700 -68 19 -9 C ATOM 1520 CG2 ILE A 812 7.595 9.683 62.518 1.00 16.78 C ANISOU 1520 CG2 ILE A 812 2051 2361 1965 -95 44 27 C ATOM 1521 CD1 ILE A 812 9.957 11.163 63.842 1.00 17.77 C ANISOU 1521 CD1 ILE A 812 2214 2479 2059 -73 -9 6 C ATOM 1522 N VAL A 813 7.956 10.221 58.789 1.00 16.31 N ANISOU 1522 N VAL A 813 1976 2247 1974 -56 10 9 N ATOM 1523 CA VAL A 813 7.384 9.425 57.681 1.00 15.53 C ANISOU 1523 CA VAL A 813 1875 2133 1891 -50 -2 10 C ATOM 1524 C VAL A 813 8.526 8.713 56.907 1.00 15.70 C ANISOU 1524 C VAL A 813 1917 2133 1915 -45 -8 23 C ATOM 1525 O VAL A 813 8.404 7.532 56.516 1.00 15.97 O ANISOU 1525 O VAL A 813 1956 2155 1958 -48 -20 31 O ATOM 1526 CB VAL A 813 6.595 10.353 56.714 1.00 14.92 C ANISOU 1526 CB VAL A 813 1805 2046 1819 -23 -16 -13 C ATOM 1527 CG1 VAL A 813 6.211 9.585 55.389 1.00 17.68 C ANISOU 1527 CG1 VAL A 813 2168 2372 2177 -9 -41 -17 C ATOM 1528 CG2 VAL A 813 5.357 10.928 57.408 1.00 16.20 C ANISOU 1528 CG2 VAL A 813 1934 2233 1988 -18 -13 -38 C ATOM 1529 N LEU A 814 9.623 9.410 56.673 1.00 15.48 N ANISOU 1529 N LEU A 814 1899 2099 1884 -40 3 22 N ATOM 1530 CA LEU A 814 10.804 8.800 56.031 1.00 16.87 C ANISOU 1530 CA LEU A 814 2080 2263 2067 -33 9 27 C ATOM 1531 C LEU A 814 11.235 7.546 56.836 1.00 16.73 C ANISOU 1531 C LEU A 814 2050 2250 2057 -36 -9 37 C ATOM 1532 O LEU A 814 11.473 6.478 56.282 1.00 16.73 O ANISOU 1532 O LEU A 814 2059 2235 2063 -24 -19 40 O ATOM 1533 CB LEU A 814 11.925 9.836 55.934 1.00 18.60 C ANISOU 1533 CB LEU A 814 2294 2481 2292 -41 33 19 C ATOM 1534 CG LEU A 814 13.281 9.488 55.345 1.00 22.76 C ANISOU 1534 CG LEU A 814 2806 3004 2836 -38 55 14 C ATOM 1535 CD1 LEU A 814 13.188 8.697 54.060 1.00 25.45 C ANISOU 1535 CD1 LEU A 814 3174 3329 3166 -16 65 15 C ATOM 1536 CD2 LEU A 814 14.084 10.806 55.165 1.00 24.48 C ANISOU 1536 CD2 LEU A 814 3019 3217 3064 -61 89 5 C ATOM 1537 N TRP A 815 11.308 7.672 58.157 1.00 15.96 N ANISOU 1537 N TRP A 815 1944 2168 1953 -48 -18 43 N ATOM 1538 CA TRP A 815 11.626 6.531 59.001 1.00 17.53 C ANISOU 1538 CA TRP A 815 2153 2362 2146 -48 -42 57 C ATOM 1539 C TRP A 815 10.562 5.424 58.881 1.00 17.09 C ANISOU 1539 C TRP A 815 2117 2289 2085 -60 -46 74 C ATOM 1540 O TRP A 815 10.906 4.245 58.753 1.00 16.71 O ANISOU 1540 O TRP A 815 2090 2217 2042 -52 -67 84 O ATOM 1541 CB TRP A 815 11.788 6.991 60.453 1.00 16.63 C ANISOU 1541 CB TRP A 815 2044 2264 2011 -56 -52 59 C ATOM 1542 CG TRP A 815 12.315 5.894 61.360 1.00 16.36 C ANISOU 1542 CG TRP A 815 2039 2217 1960 -47 -86 75 C ATOM 1543 CD1 TRP A 815 13.636 5.607 61.628 1.00 18.42 C ANISOU 1543 CD1 TRP A 815 2292 2472 2234 -20 -125 64 C ATOM 1544 CD2 TRP A 815 11.536 4.973 62.101 1.00 17.84 C ANISOU 1544 CD2 TRP A 815 2270 2391 2116 -64 -87 104 C ATOM 1545 NE1 TRP A 815 13.713 4.560 62.515 1.00 16.99 N ANISOU 1545 NE1 TRP A 815 2160 2271 2025 -9 -162 85 N ATOM 1546 CE2 TRP A 815 12.435 4.146 62.829 1.00 19.05 C ANISOU 1546 CE2 TRP A 815 2460 2523 2254 -42 -133 114 C ATOM 1547 CE3 TRP A 815 10.152 4.762 62.241 1.00 16.59 C ANISOU 1547 CE3 TRP A 815 2124 2236 1945 -99 -52 119 C ATOM 1548 CZ2 TRP A 815 11.983 3.121 63.700 1.00 18.97 C ANISOU 1548 CZ2 TRP A 815 2519 2486 2202 -55 -143 148 C ATOM 1549 CZ3 TRP A 815 9.699 3.733 63.118 1.00 17.46 C ANISOU 1549 CZ3 TRP A 815 2287 2325 2023 -123 -49 151 C ATOM 1550 CH2 TRP A 815 10.612 2.931 63.830 1.00 17.62 C ANISOU 1550 CH2 TRP A 815 2363 2316 2015 -102 -93 169 C ATOM 1551 N GLU A 816 9.288 5.797 58.874 1.00 17.20 N ANISOU 1551 N GLU A 816 2124 2315 2098 -80 -28 71 N ATOM 1552 CA GLU A 816 8.211 4.794 58.757 1.00 16.67 C ANISOU 1552 CA GLU A 816 2063 2233 2040 -104 -29 81 C ATOM 1553 C GLU A 816 8.326 4.028 57.457 1.00 18.08 C ANISOU 1553 C GLU A 816 2251 2381 2237 -88 -52 74 C ATOM 1554 O GLU A 816 8.167 2.812 57.437 1.00 17.21 O ANISOU 1554 O GLU A 816 2164 2242 2135 -100 -69 86 O ATOM 1555 CB GLU A 816 6.815 5.440 58.802 1.00 17.24 C ANISOU 1555 CB GLU A 816 2101 2327 2121 -122 -8 65 C ATOM 1556 CG GLU A 816 6.471 6.123 60.129 1.00 19.75 C ANISOU 1556 CG GLU A 816 2412 2677 2416 -137 24 66 C ATOM 1557 CD GLU A 816 5.062 6.680 60.056 1.00 19.51 C ANISOU 1557 CD GLU A 816 2336 2671 2405 -147 46 40 C ATOM 1558 OE1 GLU A 816 4.887 7.816 59.580 1.00 19.32 O ANISOU 1558 OE1 GLU A 816 2294 2659 2388 -116 38 13 O ATOM 1559 OE2 GLU A 816 4.137 5.968 60.480 1.00 21.22 O ANISOU 1559 OE2 GLU A 816 2535 2894 2634 -185 70 45 O ATOM 1560 N VAL A 817 8.596 4.742 56.368 1.00 15.75 N ANISOU 1560 N VAL A 817 1951 2087 1945 -60 -52 54 N ATOM 1561 CA VAL A 817 8.696 4.093 55.062 1.00 16.99 C ANISOU 1561 CA VAL A 817 2131 2217 2109 -38 -71 43 C ATOM 1562 C VAL A 817 9.879 3.132 55.035 1.00 15.92 C ANISOU 1562 C VAL A 817 2014 2062 1972 -18 -81 49 C ATOM 1563 O VAL A 817 9.735 1.970 54.643 1.00 16.43 O ANISOU 1563 O VAL A 817 2104 2095 2044 -14 -106 49 O ATOM 1564 CB VAL A 817 8.763 5.115 53.941 1.00 16.19 C ANISOU 1564 CB VAL A 817 2039 2117 1994 -11 -62 25 C ATOM 1565 CG1 VAL A 817 9.156 4.442 52.566 1.00 17.84 C ANISOU 1565 CG1 VAL A 817 2287 2298 2194 20 -75 12 C ATOM 1566 CG2 VAL A 817 7.383 5.792 53.800 1.00 15.74 C ANISOU 1566 CG2 VAL A 817 1969 2069 1944 -17 -75 10 C ATOM 1567 N MET A 818 11.041 3.616 55.457 1.00 16.83 N ANISOU 1567 N MET A 818 2115 2194 2084 -5 -66 49 N ATOM 1568 CA MET A 818 12.235 2.773 55.415 1.00 17.41 C ANISOU 1568 CA MET A 818 2194 2255 2167 25 -80 44 C ATOM 1569 C MET A 818 12.137 1.597 56.412 1.00 18.85 C ANISOU 1569 C MET A 818 2402 2412 2348 19 -117 65 C ATOM 1570 O MET A 818 12.866 0.604 56.267 1.00 20.83 O ANISOU 1570 O MET A 818 2671 2637 2606 51 -144 59 O ATOM 1571 CB MET A 818 13.494 3.605 55.630 1.00 16.21 C ANISOU 1571 CB MET A 818 2005 2130 2026 38 -60 30 C ATOM 1572 CG MET A 818 13.697 4.702 54.534 1.00 17.14 C ANISOU 1572 CG MET A 818 2113 2259 2140 38 -14 15 C ATOM 1573 SD MET A 818 13.486 4.112 52.828 1.00 20.58 S ANISOU 1573 SD MET A 818 2592 2670 2558 67 -2 2 S ATOM 1574 CE MET A 818 14.815 2.876 52.718 1.00 22.75 C ANISOU 1574 CE MET A 818 2850 2938 2855 110 -10 -19 C ATOM 1575 N SER A 819 11.234 1.704 57.401 1.00 17.16 N ANISOU 1575 N SER A 819 2196 2202 2121 -21 -114 87 N ATOM 1576 CA SER A 819 10.997 0.653 58.391 1.00 17.92 C ANISOU 1576 CA SER A 819 2336 2268 2204 -39 -137 115 C ATOM 1577 C SER A 819 9.791 -0.214 58.032 1.00 17.85 C ANISOU 1577 C SER A 819 2350 2226 2205 -77 -139 126 C ATOM 1578 O SER A 819 9.319 -1.001 58.873 1.00 18.64 O ANISOU 1578 O SER A 819 2491 2298 2293 -112 -143 154 O ATOM 1579 CB SER A 819 10.720 1.265 59.776 1.00 19.39 C ANISOU 1579 CB SER A 819 2525 2479 2362 -67 -121 134 C ATOM 1580 OG SER A 819 11.877 1.983 60.207 1.00 24.62 O ANISOU 1580 OG SER A 819 3169 3165 3020 -35 -134 120 O ATOM 1581 N TYR A 820 9.264 -0.035 56.818 1.00 17.79 N ANISOU 1581 N TYR A 820 2323 2220 2218 -73 -136 102 N ATOM 1582 CA TYR A 820 8.082 -0.757 56.372 1.00 16.65 C ANISOU 1582 CA TYR A 820 2186 2046 2094 -109 -147 100 C ATOM 1583 C TYR A 820 6.893 -0.686 57.348 1.00 18.93 C ANISOU 1583 C TYR A 820 2458 2346 2388 -174 -117 118 C ATOM 1584 O TYR A 820 6.228 -1.706 57.641 1.00 18.43 O ANISOU 1584 O TYR A 820 2420 2245 2339 -221 -121 134 O ATOM 1585 CB TYR A 820 8.452 -2.214 56.037 1.00 18.35 C ANISOU 1585 CB TYR A 820 2458 2200 2316 -97 -188 104 C ATOM 1586 CG TYR A 820 9.161 -2.344 54.701 1.00 15.76 C ANISOU 1586 CG TYR A 820 2138 1861 1990 -37 -210 71 C ATOM 1587 CD1 TYR A 820 8.448 -2.621 53.545 1.00 17.98 C ANISOU 1587 CD1 TYR A 820 2427 2120 2284 -36 -231 44 C ATOM 1588 CD2 TYR A 820 10.549 -2.238 54.621 1.00 19.54 C ANISOU 1588 CD2 TYR A 820 2618 2350 2457 19 -209 62 C ATOM 1589 CE1 TYR A 820 9.076 -2.741 52.320 1.00 17.36 C ANISOU 1589 CE1 TYR A 820 2371 2032 2195 21 -244 14 C ATOM 1590 CE2 TYR A 820 11.210 -2.372 53.396 1.00 20.55 C ANISOU 1590 CE2 TYR A 820 2753 2472 2583 72 -213 29 C ATOM 1591 CZ TYR A 820 10.476 -2.647 52.266 1.00 20.12 C ANISOU 1591 CZ TYR A 820 2722 2395 2529 74 -228 8 C ATOM 1592 OH TYR A 820 11.094 -2.797 51.045 1.00 20.11 O ANISOU 1592 OH TYR A 820 2743 2386 2512 128 -227 -26 O ATOM 1593 N GLY A 821 6.621 0.521 57.854 1.00 18.12 N ANISOU 1593 N GLY A 821 2314 2295 2275 -178 -82 113 N ATOM 1594 CA GLY A 821 5.426 0.735 58.669 1.00 19.22 C ANISOU 1594 CA GLY A 821 2424 2457 2422 -233 -42 119 C ATOM 1595 C GLY A 821 5.514 0.361 60.140 1.00 20.60 C ANISOU 1595 C GLY A 821 2639 2628 2560 -269 -11 157 C ATOM 1596 O GLY A 821 4.479 0.216 60.830 1.00 22.10 O ANISOU 1596 O GLY A 821 2815 2827 2754 -326 35 166 O ATOM 1597 N GLU A 822 6.737 0.194 60.643 1.00 22.06 N ANISOU 1597 N GLU A 822 3214 2658 2508 -53 -102 -147 N ATOM 1598 CA GLU A 822 6.960 0.143 62.094 1.00 23.50 C ANISOU 1598 CA GLU A 822 3313 2826 2789 -12 -71 -86 C ATOM 1599 C GLU A 822 6.418 1.432 62.734 1.00 21.83 C ANISOU 1599 C GLU A 822 2945 2700 2651 -101 -70 -2 C ATOM 1600 O GLU A 822 6.450 2.513 62.116 1.00 20.04 O ANISOU 1600 O GLU A 822 2678 2550 2386 -132 -90 15 O ATOM 1601 CB GLU A 822 8.464 0.006 62.344 1.00 25.18 C ANISOU 1601 CB GLU A 822 3475 3131 2963 169 6 -132 C ATOM 1602 CG GLU A 822 8.927 -0.328 63.756 1.00 30.11 C ANISOU 1602 CG GLU A 822 4080 3705 3654 253 -12 -85 C ATOM 1603 CD GLU A 822 10.318 -0.988 63.750 1.00 35.83 C ANISOU 1603 CD GLU A 822 4783 4480 4349 509 -10 -190 C ATOM 1604 OE1 GLU A 822 10.643 -1.693 62.762 1.00 43.68 O ANISOU 1604 OE1 GLU A 822 5855 5464 5278 644 -2 -329 O ATOM 1605 OE2 GLU A 822 11.087 -0.820 64.737 1.00 43.81 O ANISOU 1605 OE2 GLU A 822 5694 5553 5399 597 -31 -156 O ATOM 1606 N ARG A 823 5.894 1.328 63.961 1.00 19.68 N ANISOU 1606 N ARG A 823 2624 2398 2455 -148 -60 42 N ATOM 1607 CA ARG A 823 5.402 2.511 64.648 1.00 19.19 C ANISOU 1607 CA ARG A 823 2422 2418 2452 -180 -50 73 C ATOM 1608 C ARG A 823 6.565 3.370 65.172 1.00 19.44 C ANISOU 1608 C ARG A 823 2420 2514 2451 -111 -7 112 C ATOM 1609 O ARG A 823 7.428 2.869 65.853 1.00 20.73 O ANISOU 1609 O ARG A 823 2604 2676 2595 -60 30 131 O ATOM 1610 CB ARG A 823 4.525 2.083 65.823 1.00 21.23 C ANISOU 1610 CB ARG A 823 2634 2678 2755 -279 -9 80 C ATOM 1611 CG ARG A 823 3.986 3.228 66.651 1.00 21.62 C ANISOU 1611 CG ARG A 823 2530 2833 2851 -270 27 60 C ATOM 1612 CD ARG A 823 2.903 2.660 67.579 1.00 27.22 C ANISOU 1612 CD ARG A 823 3157 3618 3568 -425 106 31 C ATOM 1613 NE ARG A 823 2.474 3.614 68.597 1.00 31.39 N ANISOU 1613 NE ARG A 823 3543 4276 4109 -393 185 -28 N ATOM 1614 CZ ARG A 823 1.498 4.500 68.418 1.00 32.11 C ANISOU 1614 CZ ARG A 823 3426 4492 4281 -309 157 -147 C ATOM 1615 NH1 ARG A 823 0.881 4.562 67.246 1.00 33.94 N ANISOU 1615 NH1 ARG A 823 3577 4728 4591 -270 25 -189 N ATOM 1616 NH2 ARG A 823 1.149 5.325 69.409 1.00 32.17 N ANISOU 1616 NH2 ARG A 823 3324 4614 4285 -237 238 -241 N ATOM 1617 N PRO A 824 6.567 4.683 64.863 1.00 19.37 N ANISOU 1617 N PRO A 824 2384 2545 2430 -121 -50 126 N ATOM 1618 CA PRO A 824 7.612 5.542 65.416 1.00 19.72 C ANISOU 1618 CA PRO A 824 2420 2645 2429 -125 -29 172 C ATOM 1619 C PRO A 824 7.640 5.455 66.953 1.00 21.39 C ANISOU 1619 C PRO A 824 2599 2852 2677 -105 13 186 C ATOM 1620 O PRO A 824 6.609 5.620 67.570 1.00 21.31 O ANISOU 1620 O PRO A 824 2563 2818 2715 -108 20 153 O ATOM 1621 CB PRO A 824 7.182 6.950 64.993 1.00 23.34 C ANISOU 1621 CB PRO A 824 2943 3059 2868 -161 -138 186 C ATOM 1622 CG PRO A 824 6.352 6.759 63.838 1.00 24.15 C ANISOU 1622 CG PRO A 824 3087 3116 2974 -162 -219 157 C ATOM 1623 CD PRO A 824 5.648 5.426 63.991 1.00 19.25 C ANISOU 1623 CD PRO A 824 2387 2498 2428 -137 -165 106 C ATOM 1624 N TYR A 825 8.820 5.210 67.533 1.00 19.13 N ANISOU 1624 N TYR A 825 2301 2617 2353 -86 36 219 N ATOM 1625 CA TYR A 825 8.970 5.119 68.996 1.00 21.30 C ANISOU 1625 CA TYR A 825 2598 2874 2622 -85 44 248 C ATOM 1626 C TYR A 825 8.193 3.952 69.574 1.00 21.26 C ANISOU 1626 C TYR A 825 2662 2789 2629 -98 73 246 C ATOM 1627 O TYR A 825 7.988 3.890 70.791 1.00 22.03 O ANISOU 1627 O TYR A 825 2820 2868 2683 -152 95 270 O ATOM 1628 CB TYR A 825 8.614 6.438 69.720 1.00 21.42 C ANISOU 1628 CB TYR A 825 2637 2881 2619 -131 29 243 C ATOM 1629 CG TYR A 825 9.285 7.653 69.115 1.00 19.45 C ANISOU 1629 CG TYR A 825 2409 2654 2326 -186 -41 267 C ATOM 1630 CD1 TYR A 825 10.585 8.031 69.499 1.00 21.41 C ANISOU 1630 CD1 TYR A 825 2641 2984 2508 -261 -74 318 C ATOM 1631 CD2 TYR A 825 8.630 8.412 68.140 1.00 21.06 C ANISOU 1631 CD2 TYR A 825 2669 2796 2537 -195 -103 246 C ATOM 1632 CE1 TYR A 825 11.224 9.163 68.921 1.00 19.87 C ANISOU 1632 CE1 TYR A 825 2494 2821 2234 -408 -138 357 C ATOM 1633 CE2 TYR A 825 9.249 9.538 67.544 1.00 20.70 C ANISOU 1633 CE2 TYR A 825 2733 2728 2402 -311 -195 296 C ATOM 1634 CZ TYR A 825 10.538 9.899 67.931 1.00 21.47 C ANISOU 1634 CZ TYR A 825 2822 2921 2416 -447 -197 355 C ATOM 1635 OH TYR A 825 11.126 11.002 67.370 1.00 21.14 O ANISOU 1635 OH TYR A 825 2915 2865 2252 -647 -287 418 O ATOM 1636 N TRP A 826 7.742 3.035 68.707 1.00 20.35 N ANISOU 1636 N TRP A 826 2575 2619 2539 -93 69 220 N ATOM 1637 CA TRP A 826 7.075 1.799 69.159 1.00 23.15 C ANISOU 1637 CA TRP A 826 3056 2867 2873 -173 70 235 C ATOM 1638 C TRP A 826 5.980 2.187 70.167 1.00 23.00 C ANISOU 1638 C TRP A 826 2996 2910 2833 -326 154 232 C ATOM 1639 O TRP A 826 5.179 3.090 69.864 1.00 22.50 O ANISOU 1639 O TRP A 826 2776 2948 2824 -327 192 164 O ATOM 1640 CB TRP A 826 8.127 0.815 69.700 1.00 25.79 C ANISOU 1640 CB TRP A 826 3551 3090 3159 -79 -15 279 C ATOM 1641 CG TRP A 826 9.298 0.773 68.775 1.00 27.84 C ANISOU 1641 CG TRP A 826 3733 3401 3443 118 -58 222 C ATOM 1642 CD1 TRP A 826 9.367 0.121 67.581 1.00 28.26 C ANISOU 1642 CD1 TRP A 826 3817 3418 3503 205 -71 145 C ATOM 1643 CD2 TRP A 826 10.539 1.506 68.910 1.00 29.19 C ANISOU 1643 CD2 TRP A 826 3749 3727 3614 217 -68 215 C ATOM 1644 NE1 TRP A 826 10.591 0.358 66.984 1.00 29.99 N ANISOU 1644 NE1 TRP A 826 3892 3787 3715 369 -60 74 N ATOM 1645 CE2 TRP A 826 11.329 1.198 67.780 1.00 29.87 C ANISOU 1645 CE2 TRP A 826 3741 3906 3702 361 -59 122 C ATOM 1646 CE3 TRP A 826 11.075 2.339 69.907 1.00 27.96 C ANISOU 1646 CE3 TRP A 826 3530 3654 3438 177 -87 269 C ATOM 1647 CZ2 TRP A 826 12.626 1.728 67.587 1.00 32.02 C ANISOU 1647 CZ2 TRP A 826 3799 4409 3960 437 -44 77 C ATOM 1648 CZ3 TRP A 826 12.375 2.866 69.724 1.00 30.50 C ANISOU 1648 CZ3 TRP A 826 3672 4162 3756 245 -112 245 C ATOM 1649 CH2 TRP A 826 13.128 2.558 68.567 1.00 29.11 C ANISOU 1649 CH2 TRP A 826 3347 4128 3585 360 -79 149 C ATOM 1650 N GLU A 827 5.914 1.525 71.328 1.00 23.48 N ANISOU 1650 N GLU A 827 3203 2919 2798 -446 175 289 N ATOM 1651 CA GLU A 827 4.908 1.890 72.336 1.00 24.21 C ANISOU 1651 CA GLU A 827 3238 3136 2823 -618 305 258 C ATOM 1652 C GLU A 827 5.449 2.631 73.575 1.00 24.05 C ANISOU 1652 C GLU A 827 3270 3156 2711 -598 337 274 C ATOM 1653 O GLU A 827 4.863 2.545 74.674 1.00 26.29 O ANISOU 1653 O GLU A 827 3613 3515 2861 -774 448 266 O ATOM 1654 CB GLU A 827 4.049 0.670 72.717 1.00 28.18 C ANISOU 1654 CB GLU A 827 3875 3607 3225 -896 350 299 C ATOM 1655 CG GLU A 827 3.068 0.337 71.580 1.00 34.34 C ANISOU 1655 CG GLU A 827 4512 4437 4099 -970 350 235 C ATOM 1656 CD GLU A 827 2.286 -0.911 71.818 1.00 43.26 C ANISOU 1656 CD GLU A 827 5799 5520 5118 -1306 364 288 C ATOM 1657 OE1 GLU A 827 1.360 -0.891 72.668 1.00 48.04 O ANISOU 1657 OE1 GLU A 827 6309 6323 5619 -1577 521 261 O ATOM 1658 OE2 GLU A 827 2.591 -1.913 71.140 1.00 45.24 O ANISOU 1658 OE2 GLU A 827 6281 5545 5365 -1315 221 343 O ATOM 1659 N MET A 828 6.535 3.390 73.391 1.00 23.96 N ANISOU 1659 N MET A 828 3239 3121 2744 -424 247 286 N ATOM 1660 CA MET A 828 7.090 4.209 74.465 1.00 25.94 C ANISOU 1660 CA MET A 828 3549 3400 2908 -415 241 294 C ATOM 1661 C MET A 828 6.013 5.097 75.088 1.00 27.68 C ANISOU 1661 C MET A 828 3689 3745 3082 -465 385 172 C ATOM 1662 O MET A 828 5.150 5.593 74.374 1.00 28.36 O ANISOU 1662 O MET A 828 3600 3906 3270 -400 431 65 O ATOM 1663 CB MET A 828 8.219 5.089 73.913 1.00 23.39 C ANISOU 1663 CB MET A 828 3160 3077 2652 -279 130 304 C ATOM 1664 CG MET A 828 9.484 4.306 73.612 1.00 26.25 C ANISOU 1664 CG MET A 828 3546 3397 3032 -198 3 380 C ATOM 1665 SD MET A 828 10.759 5.451 73.049 1.00 25.33 S ANISOU 1665 SD MET A 828 3285 3388 2950 -145 -77 378 S ATOM 1666 CE MET A 828 10.999 6.487 74.485 1.00 27.95 C ANISOU 1666 CE MET A 828 3732 3719 3168 -240 -122 394 C ATOM 1667 N SER A 829 6.051 5.274 76.404 1.00 29.38 N ANISOU 1667 N SER A 829 4037 3991 3135 -558 442 168 N ATOM 1668 CA SER A 829 5.199 6.272 77.078 1.00 32.89 C ANISOU 1668 CA SER A 829 4409 4573 3513 -546 585 1 C ATOM 1669 C SER A 829 5.327 7.591 76.340 1.00 33.04 C ANISOU 1669 C SER A 829 4333 4552 3667 -327 489 -91 C ATOM 1670 O SER A 829 6.451 7.981 75.956 1.00 28.83 O ANISOU 1670 O SER A 829 3885 3899 3172 -276 328 3 O ATOM 1671 CB SER A 829 5.675 6.520 78.514 1.00 34.97 C ANISOU 1671 CB SER A 829 4897 4830 3559 -639 602 18 C ATOM 1672 OG SER A 829 5.329 5.460 79.373 1.00 45.58 O ANISOU 1672 OG SER A 829 6390 6218 4712 -887 705 87 O ATOM 1673 N ASN A 830 4.204 8.290 76.155 1.00 33.59 N ANISOU 1673 N ASN A 830 4238 4729 3797 -209 569 -281 N ATOM 1674 CA ASN A 830 4.237 9.606 75.491 1.00 34.04 C ANISOU 1674 CA ASN A 830 4295 4682 3958 13 421 -372 C ATOM 1675 C ASN A 830 5.204 10.547 76.199 1.00 32.68 C ANISOU 1675 C ASN A 830 4371 4371 3674 25 316 -351 C ATOM 1676 O ASN A 830 5.948 11.279 75.559 1.00 31.18 O ANISOU 1676 O ASN A 830 4295 4025 3527 61 132 -284 O ATOM 1677 CB ASN A 830 2.834 10.239 75.453 1.00 36.24 C ANISOU 1677 CB ASN A 830 4371 5096 4302 206 491 -627 C ATOM 1678 CG ASN A 830 1.991 9.709 74.312 1.00 41.00 C ANISOU 1678 CG ASN A 830 4724 5787 5068 238 472 -646 C ATOM 1679 OD1 ASN A 830 2.335 8.706 73.696 1.00 42.24 O ANISOU 1679 OD1 ASN A 830 4878 5914 5255 78 460 -479 O ATOM 1680 ND2 ASN A 830 0.894 10.383 74.019 1.00 43.96 N ANISOU 1680 ND2 ASN A 830 4895 6262 5546 468 441 -867 N ATOM 1681 N GLN A 831 5.188 10.511 77.528 1.00 31.68 N ANISOU 1681 N GLN A 831 4352 4313 3373 -53 430 -405 N ATOM 1682 CA GLN A 831 6.067 11.362 78.335 1.00 34.18 C ANISOU 1682 CA GLN A 831 4931 4502 3553 -73 319 -396 C ATOM 1683 C GLN A 831 7.536 11.109 78.002 1.00 29.17 C ANISOU 1683 C GLN A 831 4390 3761 2934 -207 137 -165 C ATOM 1684 O GLN A 831 8.344 12.034 78.000 1.00 27.78 O ANISOU 1684 O GLN A 831 4368 3461 2725 -228 -32 -135 O ATOM 1685 CB GLN A 831 5.810 11.129 79.821 1.00 36.28 C ANISOU 1685 CB GLN A 831 5314 4881 3588 -180 484 -474 C ATOM 1686 CG GLN A 831 4.456 11.689 80.324 1.00 44.81 C ANISOU 1686 CG GLN A 831 6288 6127 4610 -25 686 -778 C ATOM 1687 CD GLN A 831 4.164 11.329 81.800 1.00 48.82 C ANISOU 1687 CD GLN A 831 6911 6810 4828 -199 910 -859 C ATOM 1688 OE1 GLN A 831 4.908 10.562 82.426 1.00 54.45 O ANISOU 1688 OE1 GLN A 831 7814 7486 5387 -447 885 -658 O ATOM 1689 NE2 GLN A 831 3.082 11.892 82.352 1.00 55.51 N ANISOU 1689 NE2 GLN A 831 7650 7857 5585 -58 1118 -1170 N ATOM 1690 N ASP A 832 7.871 9.853 77.716 1.00 26.31 N ANISOU 1690 N ASP A 832 3928 3457 2614 -298 162 -20 N ATOM 1691 CA ASP A 832 9.240 9.497 77.385 1.00 25.03 C ANISOU 1691 CA ASP A 832 3774 3258 2480 -366 2 150 C ATOM 1692 C ASP A 832 9.607 9.841 75.954 1.00 25.15 C ANISOU 1692 C ASP A 832 3662 3253 2639 -322 -80 186 C ATOM 1693 O ASP A 832 10.759 10.169 75.680 1.00 24.37 O ANISOU 1693 O ASP A 832 3561 3163 2536 -397 -209 269 O ATOM 1694 CB ASP A 832 9.515 8.032 77.699 1.00 24.43 C ANISOU 1694 CB ASP A 832 3695 3212 2376 -425 16 262 C ATOM 1695 CG ASP A 832 9.587 7.772 79.203 1.00 26.73 C ANISOU 1695 CG ASP A 832 4205 3495 2457 -539 20 285 C ATOM 1696 OD1 ASP A 832 10.287 8.537 79.906 1.00 31.63 O ANISOU 1696 OD1 ASP A 832 4956 4086 2975 -578 -94 288 O ATOM 1697 OD2 ASP A 832 8.963 6.798 79.678 1.00 31.17 O ANISOU 1697 OD2 ASP A 832 4843 4072 2927 -629 123 309 O ATOM 1698 N VAL A 833 8.643 9.765 75.042 1.00 22.71 N ANISOU 1698 N VAL A 833 3243 2948 2439 -232 -8 121 N ATOM 1699 CA VAL A 833 8.893 10.231 73.677 1.00 20.67 C ANISOU 1699 CA VAL A 833 2935 2652 2268 -216 -97 152 C ATOM 1700 C VAL A 833 9.260 11.704 73.718 1.00 22.16 C ANISOU 1700 C VAL A 833 3306 2721 2392 -255 -240 133 C ATOM 1701 O VAL A 833 10.244 12.136 73.074 1.00 22.17 O ANISOU 1701 O VAL A 833 3341 2717 2364 -393 -347 230 O ATOM 1702 CB VAL A 833 7.661 10.027 72.754 1.00 21.30 C ANISOU 1702 CB VAL A 833 2904 2732 2457 -105 -45 73 C ATOM 1703 CG1 VAL A 833 7.927 10.612 71.343 1.00 21.92 C ANISOU 1703 CG1 VAL A 833 3012 2744 2574 -116 -168 117 C ATOM 1704 CG2 VAL A 833 7.328 8.514 72.671 1.00 23.10 C ANISOU 1704 CG2 VAL A 833 3003 3049 2726 -129 73 104 C ATOM 1705 N ILE A 834 8.500 12.465 74.499 1.00 25.05 N ANISOU 1705 N ILE A 834 3341 3729 2449 -284 220 -93 N ATOM 1706 CA ILE A 834 8.748 13.910 74.581 1.00 24.61 C ANISOU 1706 CA ILE A 834 3365 3622 2362 -244 226 -176 C ATOM 1707 C ILE A 834 10.119 14.178 75.197 1.00 25.45 C ANISOU 1707 C ILE A 834 3558 3694 2417 -307 140 -196 C ATOM 1708 O ILE A 834 10.909 14.946 74.653 1.00 24.59 O ANISOU 1708 O ILE A 834 3479 3519 2347 -319 88 -229 O ATOM 1709 CB ILE A 834 7.629 14.639 75.386 1.00 26.95 C ANISOU 1709 CB ILE A 834 3706 3959 2574 -173 332 -223 C ATOM 1710 CG1 ILE A 834 6.273 14.530 74.643 1.00 27.32 C ANISOU 1710 CG1 ILE A 834 3642 4052 2686 -105 411 -195 C ATOM 1711 CG2 ILE A 834 8.034 16.115 75.664 1.00 27.34 C ANISOU 1711 CG2 ILE A 834 3883 3930 2576 -139 331 -320 C ATOM 1712 CD1 ILE A 834 5.030 14.742 75.574 1.00 28.93 C ANISOU 1712 CD1 ILE A 834 3843 4345 2805 -37 532 -200 C ATOM 1713 N LYS A 835 10.410 13.525 76.325 1.00 24.30 N ANISOU 1713 N LYS A 835 3448 3602 2183 -356 121 -164 N ATOM 1714 CA LYS A 835 11.660 13.806 77.026 1.00 24.88 C ANISOU 1714 CA LYS A 835 3600 3663 2192 -422 32 -177 C ATOM 1715 C LYS A 835 12.877 13.330 76.238 1.00 25.15 C ANISOU 1715 C LYS A 835 3570 3669 2318 -466 -66 -122 C ATOM 1716 O LYS A 835 13.894 14.026 76.175 1.00 23.30 O ANISOU 1716 O LYS A 835 3370 3400 2082 -509 -138 -146 O ATOM 1717 CB LYS A 835 11.642 13.179 78.437 1.00 24.65 C ANISOU 1717 CB LYS A 835 3620 3710 2034 -461 32 -144 C ATOM 1718 CG LYS A 835 12.844 13.584 79.293 1.00 32.65 C ANISOU 1718 CG LYS A 835 4723 4726 2956 -536 -67 -162 C ATOM 1719 CD LYS A 835 12.612 14.951 79.974 1.00 38.41 C ANISOU 1719 CD LYS A 835 5595 5426 3574 -528 -37 -277 C ATOM 1720 CE LYS A 835 13.733 15.350 80.954 1.00 39.12 C ANISOU 1720 CE LYS A 835 5790 5526 3547 -624 -145 -300 C ATOM 1721 NZ LYS A 835 14.931 15.871 80.235 1.00 31.58 N ANISOU 1721 NZ LYS A 835 4815 4511 2673 -688 -254 -301 N ATOM 1722 N ALA A 836 12.783 12.136 75.649 1.00 22.58 N ANISOU 1722 N ALA A 836 3153 3358 2068 -457 -65 -47 N ATOM 1723 CA ALA A 836 13.916 11.560 74.930 1.00 23.73 C ANISOU 1723 CA ALA A 836 3238 3482 2294 -477 -141 9 C ATOM 1724 C ALA A 836 14.301 12.433 73.748 1.00 23.48 C ANISOU 1724 C ALA A 836 3183 3395 2345 -460 -154 -29 C ATOM 1725 O ALA A 836 15.471 12.768 73.574 1.00 22.38 O ANISOU 1725 O ALA A 836 3035 3245 2223 -496 -225 -16 O ATOM 1726 CB ALA A 836 13.614 10.143 74.501 1.00 22.72 C ANISOU 1726 CB ALA A 836 3045 3360 2226 -460 -125 83 C ATOM 1727 N VAL A 837 13.301 12.841 72.977 1.00 23.03 N ANISOU 1727 N VAL A 837 3110 3310 2331 -409 -87 -69 N ATOM 1728 CA VAL A 837 13.559 13.662 71.784 1.00 21.53 C ANISOU 1728 CA VAL A 837 2898 3066 2215 -389 -94 -96 C ATOM 1729 C VAL A 837 14.163 15.002 72.218 1.00 23.65 C ANISOU 1729 C VAL A 837 3249 3297 2440 -424 -129 -150 C ATOM 1730 O VAL A 837 15.140 15.477 71.634 1.00 22.04 O ANISOU 1730 O VAL A 837 3031 3064 2279 -458 -184 -141 O ATOM 1731 CB VAL A 837 12.293 13.847 70.965 1.00 21.33 C ANISOU 1731 CB VAL A 837 2841 3029 2235 -326 -21 -118 C ATOM 1732 CG1 VAL A 837 12.513 14.903 69.852 1.00 23.08 C ANISOU 1732 CG1 VAL A 837 3060 3193 2516 -302 -27 -146 C ATOM 1733 CG2 VAL A 837 11.845 12.469 70.359 1.00 20.74 C ANISOU 1733 CG2 VAL A 837 2688 2980 2210 -317 -8 -63 C ATOM 1734 N ASP A 838 13.604 15.576 73.281 1.00 24.47 N ANISOU 1734 N ASP A 838 3444 3403 2451 -422 -97 -206 N ATOM 1735 CA ASP A 838 14.171 16.804 73.845 1.00 25.97 C ANISOU 1735 CA ASP A 838 3744 3544 2581 -469 -137 -268 C ATOM 1736 C ASP A 838 15.645 16.665 74.258 1.00 27.65 C ANISOU 1736 C ASP A 838 3956 3779 2771 -570 -249 -230 C ATOM 1737 O ASP A 838 16.446 17.559 74.006 1.00 27.62 O ANISOU 1737 O ASP A 838 3985 3728 2782 -627 -307 -249 O ATOM 1738 CB ASP A 838 13.342 17.249 75.039 1.00 27.55 C ANISOU 1738 CB ASP A 838 4054 3751 2663 -444 -79 -335 C ATOM 1739 CG ASP A 838 13.829 18.562 75.610 1.00 28.17 C ANISOU 1739 CG ASP A 838 4276 3757 2670 -491 -116 -417 C ATOM 1740 OD1 ASP A 838 14.003 19.530 74.832 1.00 34.18 O ANISOU 1740 OD1 ASP A 838 5066 4430 3491 -486 -124 -449 O ATOM 1741 OD2 ASP A 838 14.100 18.592 76.804 1.00 28.14 O ANISOU 1741 OD2 ASP A 838 4361 3783 2549 -543 -145 -445 O ATOM 1742 N GLU A 839 16.009 15.516 74.838 1.00 25.59 N ANISOU 1742 N GLU A 839 3646 3594 2482 -592 -282 -163 N ATOM 1743 CA GLU A 839 17.382 15.240 75.273 1.00 28.78 C ANISOU 1743 CA GLU A 839 4026 4044 2867 -675 -390 -106 C ATOM 1744 C GLU A 839 18.359 15.001 74.114 1.00 28.67 C ANISOU 1744 C GLU A 839 3897 4028 2967 -681 -434 -39 C ATOM 1745 O GLU A 839 19.586 14.936 74.319 1.00 30.47 O ANISOU 1745 O GLU A 839 4083 4300 3193 -747 -525 16 O ATOM 1746 CB GLU A 839 17.395 14.054 76.236 1.00 27.44 C ANISOU 1746 CB GLU A 839 3841 3953 2633 -679 -405 -43 C ATOM 1747 CG GLU A 839 16.792 14.402 77.596 1.00 28.55 C ANISOU 1747 CG GLU A 839 4104 4116 2628 -701 -384 -101 C ATOM 1748 CD GLU A 839 16.856 13.263 78.601 1.00 31.14 C ANISOU 1748 CD GLU A 839 4423 4528 2881 -715 -404 -26 C ATOM 1749 OE1 GLU A 839 17.545 12.263 78.332 1.00 32.89 O ANISOU 1749 OE1 GLU A 839 4552 4783 3164 -714 -453 72 O ATOM 1750 OE2 GLU A 839 16.227 13.401 79.670 1.00 30.68 O ANISOU 1750 OE2 GLU A 839 4458 4501 2698 -721 -368 -64 O ATOM 1751 N GLY A 840 17.817 14.885 72.906 1.00 25.25 N ANISOU 1751 N GLY A 840 3411 3558 2626 -610 -370 -41 N ATOM 1752 CA GLY A 840 18.632 14.701 71.707 1.00 25.16 C ANISOU 1752 CA GLY A 840 3300 3546 2713 -601 -391 14 C ATOM 1753 C GLY A 840 18.575 13.304 71.115 1.00 25.16 C ANISOU 1753 C GLY A 840 3213 3573 2772 -533 -362 78 C ATOM 1754 O GLY A 840 19.250 13.025 70.126 1.00 24.80 O ANISOU 1754 O GLY A 840 3089 3534 2800 -510 -368 123 O ATOM 1755 N TYR A 841 17.831 12.399 71.752 1.00 23.25 N ANISOU 1755 N TYR A 841 2991 3348 2494 -506 -330 86 N ATOM 1756 CA TYR A 841 17.672 11.050 71.221 1.00 21.74 C ANISOU 1756 CA TYR A 841 2745 3160 2356 -449 -303 140 C ATOM 1757 C TYR A 841 16.809 11.028 69.953 1.00 21.09 C ANISOU 1757 C TYR A 841 2642 3032 2338 -396 -237 106 C ATOM 1758 O TYR A 841 15.814 11.753 69.833 1.00 22.15 O ANISOU 1758 O TYR A 841 2812 3145 2460 -389 -193 46 O ATOM 1759 CB TYR A 841 17.090 10.111 72.278 1.00 22.87 C ANISOU 1759 CB TYR A 841 2922 3326 2440 -451 -291 167 C ATOM 1760 CG TYR A 841 18.119 9.725 73.312 1.00 23.55 C ANISOU 1760 CG TYR A 841 3006 3467 2475 -488 -366 232 C ATOM 1761 CD1 TYR A 841 18.902 8.564 73.149 1.00 23.10 C ANISOU 1761 CD1 TYR A 841 2893 3423 2463 -451 -395 323 C ATOM 1762 CD2 TYR A 841 18.322 10.522 74.447 1.00 26.49 C ANISOU 1762 CD2 TYR A 841 3440 3877 2750 -554 -410 206 C ATOM 1763 CE1 TYR A 841 19.884 8.209 74.117 1.00 23.53 C ANISOU 1763 CE1 TYR A 841 2931 3538 2470 -478 -472 400 C ATOM 1764 CE2 TYR A 841 19.290 10.159 75.420 1.00 25.17 C ANISOU 1764 CE2 TYR A 841 3265 3773 2525 -596 -494 275 C ATOM 1765 CZ TYR A 841 20.067 9.025 75.217 1.00 26.70 C ANISOU 1765 CZ TYR A 841 3382 3989 2772 -556 -526 377 C ATOM 1766 OH TYR A 841 21.002 8.671 76.165 1.00 27.88 O ANISOU 1766 OH TYR A 841 3515 4212 2867 -590 -612 458 O ATOM 1767 N ARG A 842 17.178 10.151 69.020 1.00 21.24 N ANISOU 1767 N ARG A 842 2610 3040 2421 -353 -230 146 N ATOM 1768 CA ARG A 842 16.420 10.008 67.796 1.00 19.05 C ANISOU 1768 CA ARG A 842 2319 2726 2192 -312 -180 117 C ATOM 1769 C ARG A 842 16.175 8.551 67.469 1.00 18.40 C ANISOU 1769 C ARG A 842 2233 2622 2137 -278 -163 150 C ATOM 1770 O ARG A 842 16.875 7.664 67.956 1.00 20.68 O ANISOU 1770 O ARG A 842 2517 2914 2424 -268 -188 205 O ATOM 1771 CB ARG A 842 17.173 10.690 66.629 1.00 19.24 C ANISOU 1771 CB ARG A 842 2302 2743 2264 -295 -185 116 C ATOM 1772 CG ARG A 842 17.498 12.162 66.866 1.00 20.13 C ANISOU 1772 CG ARG A 842 2431 2859 2360 -340 -209 89 C ATOM 1773 CD ARG A 842 16.246 13.049 66.723 1.00 20.53 C ANISOU 1773 CD ARG A 842 2529 2876 2396 -334 -167 25 C ATOM 1774 NE ARG A 842 16.524 14.486 66.787 1.00 19.46 N ANISOU 1774 NE ARG A 842 2430 2713 2251 -368 -185 -5 N ATOM 1775 CZ ARG A 842 16.362 15.224 67.892 1.00 23.06 C ANISOU 1775 CZ ARG A 842 2957 3155 2648 -406 -199 -44 C ATOM 1776 NH1 ARG A 842 16.040 14.650 69.044 1.00 22.78 N ANISOU 1776 NH1 ARG A 842 2952 3150 2553 -416 -199 -49 N ATOM 1777 NH2 ARG A 842 16.579 16.535 67.885 1.00 19.74 N ANISOU 1777 NH2 ARG A 842 2592 2688 2221 -439 -214 -77 N ATOM 1778 N LEU A 843 15.171 8.309 66.635 1.00 18.75 N ANISOU 1778 N LEU A 843 2283 2639 2203 -264 -124 118 N ATOM 1779 CA LEU A 843 14.909 6.971 66.112 1.00 19.07 C ANISOU 1779 CA LEU A 843 2337 2638 2270 -244 -111 136 C ATOM 1780 C LEU A 843 16.185 6.455 65.419 1.00 19.19 C ANISOU 1780 C LEU A 843 2335 2635 2323 -189 -123 168 C ATOM 1781 O LEU A 843 16.912 7.232 64.786 1.00 19.86 O ANISOU 1781 O LEU A 843 2380 2741 2423 -168 -125 163 O ATOM 1782 CB LEU A 843 13.730 7.009 65.134 1.00 19.40 C ANISOU 1782 CB LEU A 843 2380 2665 2326 -250 -82 93 C ATOM 1783 CG LEU A 843 12.385 7.319 65.781 1.00 19.09 C ANISOU 1783 CG LEU A 843 2340 2657 2256 -292 -60 77 C ATOM 1784 CD1 LEU A 843 11.364 7.750 64.748 1.00 20.22 C ANISOU 1784 CD1 LEU A 843 2458 2811 2415 -291 -41 41 C ATOM 1785 CD2 LEU A 843 11.889 6.096 66.573 1.00 23.01 C ANISOU 1785 CD2 LEU A 843 2864 3142 2737 -331 -59 116 C ATOM 1786 N PRO A 844 16.485 5.165 65.592 1.00 20.30 N ANISOU 1786 N PRO A 844 2504 2735 2476 -161 -126 209 N ATOM 1787 CA PRO A 844 17.699 4.558 65.052 1.00 19.63 C ANISOU 1787 CA PRO A 844 2403 2632 2423 -85 -126 248 C ATOM 1788 C PRO A 844 17.540 4.236 63.562 1.00 20.52 C ANISOU 1788 C PRO A 844 2539 2699 2560 -40 -88 204 C ATOM 1789 O PRO A 844 16.424 4.176 63.066 1.00 21.26 O ANISOU 1789 O PRO A 844 2669 2764 2645 -78 -76 154 O ATOM 1790 CB PRO A 844 17.804 3.244 65.850 1.00 22.60 C ANISOU 1790 CB PRO A 844 2827 2962 2800 -69 -138 304 C ATOM 1791 CG PRO A 844 16.325 2.875 66.111 1.00 22.43 C ANISOU 1791 CG PRO A 844 2863 2902 2758 -141 -127 272 C ATOM 1792 CD PRO A 844 15.662 4.202 66.363 1.00 21.83 C ANISOU 1792 CD PRO A 844 2748 2894 2651 -198 -126 229 C ATOM 1793 N PRO A 845 18.655 3.997 62.856 1.00 20.87 N ANISOU 1793 N PRO A 845 2558 2746 2628 43 -70 228 N ATOM 1794 CA PRO A 845 18.499 3.684 61.440 1.00 19.42 C ANISOU 1794 CA PRO A 845 2410 2520 2448 88 -30 180 C ATOM 1795 C PRO A 845 17.719 2.397 61.223 1.00 21.01 C ANISOU 1795 C PRO A 845 2717 2620 2645 86 -21 150 C ATOM 1796 O PRO A 845 17.989 1.383 61.882 1.00 21.56 O ANISOU 1796 O PRO A 845 2830 2634 2728 114 -28 191 O ATOM 1797 CB PRO A 845 19.952 3.533 60.935 1.00 21.40 C ANISOU 1797 CB PRO A 845 2612 2801 2720 192 -1 225 C ATOM 1798 CG PRO A 845 20.805 3.390 62.169 1.00 24.19 C ANISOU 1798 CG PRO A 845 2911 3193 3088 204 -36 307 C ATOM 1799 CD PRO A 845 20.062 4.038 63.303 1.00 23.09 C ANISOU 1799 CD PRO A 845 2769 3079 2926 96 -85 301 C ATOM 1800 N PRO A 846 16.730 2.430 60.324 1.00 22.13 N ANISOU 1800 N PRO A 846 2905 2736 2769 45 -14 84 N ATOM 1801 CA PRO A 846 16.051 1.190 59.914 1.00 22.35 C ANISOU 1801 CA PRO A 846 3044 2660 2789 30 -13 50 C ATOM 1802 C PRO A 846 17.050 0.176 59.362 1.00 24.07 C ANISOU 1802 C PRO A 846 3329 2801 3016 143 23 54 C ATOM 1803 O PRO A 846 18.129 0.561 58.892 1.00 22.86 O ANISOU 1803 O PRO A 846 3123 2696 2868 235 57 71 O ATOM 1804 CB PRO A 846 15.055 1.670 58.841 1.00 21.18 C ANISOU 1804 CB PRO A 846 2906 2531 2611 -27 -18 -17 C ATOM 1805 CG PRO A 846 14.770 3.136 59.254 1.00 22.73 C ANISOU 1805 CG PRO A 846 2996 2832 2807 -68 -30 -3 C ATOM 1806 CD PRO A 846 16.137 3.645 59.725 1.00 18.39 C ANISOU 1806 CD PRO A 846 2383 2328 2278 0 -17 46 C ATOM 1807 N MET A 847 16.722 -1.111 59.443 1.00 25.49 N ANISOU 1807 N MET A 847 3626 2861 3199 140 20 45 N ATOM 1808 CA MET A 847 17.620 -2.129 58.893 1.00 31.09 C ANISOU 1808 CA MET A 847 4422 3475 3915 265 63 42 C ATOM 1809 C MET A 847 17.948 -1.839 57.432 1.00 29.60 C ANISOU 1809 C MET A 847 4251 3305 3691 331 108 -23 C ATOM 1810 O MET A 847 17.054 -1.557 56.625 1.00 28.85 O ANISOU 1810 O MET A 847 4191 3215 3557 253 93 -92 O ATOM 1811 CB MET A 847 16.996 -3.504 58.992 1.00 30.63 C ANISOU 1811 CB MET A 847 4520 3259 3857 231 48 22 C ATOM 1812 CG MET A 847 17.926 -4.603 58.516 1.00 38.87 C ANISOU 1812 CG MET A 847 5676 4183 4909 378 99 18 C ATOM 1813 SD MET A 847 17.162 -6.203 58.718 1.00 46.17 S ANISOU 1813 SD MET A 847 6808 4894 5839 320 74 -2 S ATOM 1814 CE MET A 847 16.592 -6.093 60.417 1.00 46.11 C ANISOU 1814 CE MET A 847 6723 4931 5865 201 15 99 C ATOM 1815 N ASP A 848 19.236 -1.903 57.113 1.00 31.43 N ANISOU 1815 N ASP A 848 4450 3560 3933 474 165 8 N ATOM 1816 CA ASP A 848 19.744 -1.729 55.750 1.00 33.91 C ANISOU 1816 CA ASP A 848 4781 3898 4207 561 227 -41 C ATOM 1817 C ASP A 848 19.449 -0.332 55.180 1.00 32.21 C ANISOU 1817 C ASP A 848 4464 3811 3963 493 216 -58 C ATOM 1818 O ASP A 848 19.359 -0.161 53.961 1.00 31.39 O ANISOU 1818 O ASP A 848 4401 3719 3806 513 248 -116 O ATOM 1819 CB ASP A 848 19.180 -2.798 54.810 1.00 36.37 C ANISOU 1819 CB ASP A 848 5282 4069 4470 570 243 -136 C ATOM 1820 CG ASP A 848 19.636 -4.213 55.171 1.00 42.94 C ANISOU 1820 CG ASP A 848 6241 4749 5327 669 270 -123 C ATOM 1821 OD1 ASP A 848 20.754 -4.374 55.703 1.00 43.81 O ANISOU 1821 OD1 ASP A 848 6282 4884 5481 797 308 -43 O ATOM 1822 OD2 ASP A 848 18.861 -5.159 54.923 1.00 43.31 O ANISOU 1822 OD2 ASP A 848 6456 4650 5351 614 247 -189 O ATOM 1823 N CYS A 849 19.323 0.663 56.050 1.00 27.98 N ANISOU 1823 N CYS A 849 3808 3366 3459 416 173 -7 N ATOM 1824 CA CYS A 849 18.938 2.016 55.590 1.00 24.54 C ANISOU 1824 CA CYS A 849 3291 3030 3003 347 158 -19 C ATOM 1825 C CYS A 849 20.139 2.670 54.934 1.00 25.91 C ANISOU 1825 C CYS A 849 3378 3294 3172 435 213 19 C ATOM 1826 O CYS A 849 21.218 2.700 55.536 1.00 24.18 O ANISOU 1826 O CYS A 849 3076 3119 2991 496 228 92 O ATOM 1827 CB CYS A 849 18.493 2.894 56.762 1.00 22.46 C ANISOU 1827 CB CYS A 849 2943 2822 2770 250 103 20 C ATOM 1828 SG CYS A 849 17.777 4.476 56.226 1.00 24.38 S ANISOU 1828 SG CYS A 849 3120 3151 2992 169 83 -2 S ATOM 1829 N PRO A 850 19.977 3.166 53.689 1.00 24.47 N ANISOU 1829 N PRO A 850 3209 3148 2940 439 241 -21 N ATOM 1830 CA PRO A 850 21.010 4.001 53.058 1.00 23.05 C ANISOU 1830 CA PRO A 850 2931 3073 2753 496 292 27 C ATOM 1831 C PRO A 850 21.421 5.150 53.962 1.00 22.26 C ANISOU 1831 C PRO A 850 2697 3057 2705 435 254 103 C ATOM 1832 O PRO A 850 20.573 5.830 54.568 1.00 20.61 O ANISOU 1832 O PRO A 850 2478 2846 2508 331 194 92 O ATOM 1833 CB PRO A 850 20.326 4.543 51.803 1.00 24.77 C ANISOU 1833 CB PRO A 850 3192 3315 2905 460 299 -27 C ATOM 1834 CG PRO A 850 19.356 3.413 51.442 1.00 26.12 C ANISOU 1834 CG PRO A 850 3515 3375 3032 445 282 -116 C ATOM 1835 CD PRO A 850 18.824 2.944 52.792 1.00 25.58 C ANISOU 1835 CD PRO A 850 3455 3242 3022 383 224 -105 C ATOM 1836 N ALA A 851 22.723 5.351 54.055 1.00 23.37 N ANISOU 1836 N ALA A 851 2736 3272 2870 500 290 180 N ATOM 1837 CA ALA A 851 23.298 6.448 54.827 1.00 22.98 C ANISOU 1837 CA ALA A 851 2561 3306 2863 434 251 255 C ATOM 1838 C ALA A 851 22.666 7.786 54.472 1.00 21.49 C ANISOU 1838 C ALA A 851 2358 3146 2659 332 222 240 C ATOM 1839 O ALA A 851 22.374 8.596 55.354 1.00 21.88 O ANISOU 1839 O ALA A 851 2379 3201 2735 240 162 253 O ATOM 1840 CB ALA A 851 24.834 6.490 54.611 1.00 24.77 C ANISOU 1840 CB ALA A 851 2669 3633 3110 519 303 348 C ATOM 1841 N ALA A 852 22.483 8.023 53.173 1.00 20.82 N ANISOU 1841 N ALA A 852 2303 3079 2528 356 267 214 N ATOM 1842 CA ALA A 852 21.946 9.281 52.696 1.00 19.26 C ANISOU 1842 CA ALA A 852 2094 2907 2315 277 246 213 C ATOM 1843 C ALA A 852 20.544 9.518 53.275 1.00 19.94 C ANISOU 1843 C ALA A 852 2242 2928 2405 196 181 156 C ATOM 1844 O ALA A 852 20.161 10.661 53.541 1.00 20.16 O ANISOU 1844 O ALA A 852 2246 2965 2449 125 145 170 O ATOM 1845 CB ALA A 852 21.891 9.279 51.163 1.00 23.68 C ANISOU 1845 CB ALA A 852 2693 3495 2808 327 304 193 C ATOM 1846 N LEU A 853 19.773 8.444 53.427 1.00 18.86 N ANISOU 1846 N LEU A 853 2188 2725 2254 211 170 96 N ATOM 1847 CA LEU A 853 18.400 8.604 53.914 1.00 17.84 C ANISOU 1847 CA LEU A 853 2101 2553 2126 136 117 51 C ATOM 1848 C LEU A 853 18.363 8.747 55.407 1.00 17.86 C ANISOU 1848 C LEU A 853 2074 2541 2172 90 77 71 C ATOM 1849 O LEU A 853 17.532 9.491 55.929 1.00 18.59 O ANISOU 1849 O LEU A 853 2162 2629 2272 29 43 60 O ATOM 1850 CB LEU A 853 17.491 7.455 53.443 1.00 18.05 C ANISOU 1850 CB LEU A 853 2225 2520 2115 142 113 -16 C ATOM 1851 CG LEU A 853 17.251 7.409 51.929 1.00 18.54 C ANISOU 1851 CG LEU A 853 2336 2597 2110 167 138 -51 C ATOM 1852 CD1 LEU A 853 16.533 6.103 51.543 1.00 19.78 C ANISOU 1852 CD1 LEU A 853 2606 2682 2226 164 127 -121 C ATOM 1853 CD2 LEU A 853 16.484 8.637 51.415 1.00 21.12 C ANISOU 1853 CD2 LEU A 853 2633 2972 2420 115 110 -42 C ATOM 1854 N TYR A 854 19.261 8.048 56.113 1.00 18.26 N ANISOU 1854 N TYR A 854 2104 2588 2247 128 83 105 N ATOM 1855 CA TYR A 854 19.328 8.270 57.563 1.00 16.46 C ANISOU 1855 CA TYR A 854 1846 2360 2047 78 39 132 C ATOM 1856 C TYR A 854 19.821 9.676 57.875 1.00 18.81 C ANISOU 1856 C TYR A 854 2077 2709 2359 26 17 169 C ATOM 1857 O TYR A 854 19.273 10.362 58.748 1.00 18.02 O ANISOU 1857 O TYR A 854 1986 2600 2262 -39 -20 157 O ATOM 1858 CB TYR A 854 20.111 7.190 58.301 1.00 18.09 C ANISOU 1858 CB TYR A 854 2047 2554 2273 128 40 170 C ATOM 1859 CG TYR A 854 19.932 7.287 59.806 1.00 17.54 C ANISOU 1859 CG TYR A 854 1969 2482 2212 69 -11 190 C ATOM 1860 CD1 TYR A 854 18.661 7.199 60.392 1.00 16.77 C ANISOU 1860 CD1 TYR A 854 1928 2344 2100 10 -33 147 C ATOM 1861 CD2 TYR A 854 21.025 7.519 60.646 1.00 21.79 C ANISOU 1861 CD2 TYR A 854 2438 3074 2768 65 -39 257 C ATOM 1862 CE1 TYR A 854 18.469 7.317 61.808 1.00 20.11 C ANISOU 1862 CE1 TYR A 854 2350 2774 2516 -42 -71 165 C ATOM 1863 CE2 TYR A 854 20.849 7.633 62.049 1.00 21.48 C ANISOU 1863 CE2 TYR A 854 2403 3039 2720 5 -91 272 C ATOM 1864 CZ TYR A 854 19.576 7.523 62.619 1.00 21.64 C ANISOU 1864 CZ TYR A 854 2491 3013 2716 -44 -101 223 C ATOM 1865 OH TYR A 854 19.426 7.636 63.997 1.00 21.53 O ANISOU 1865 OH TYR A 854 2487 3013 2679 -97 -142 239 O ATOM 1866 N GLN A 855 20.789 10.165 57.105 1.00 16.91 N ANISOU 1866 N GLN A 855 1779 2522 2124 50 44 213 N ATOM 1867 CA GLN A 855 21.216 11.539 57.311 1.00 17.14 C ANISOU 1867 CA GLN A 855 1758 2586 2168 -18 18 250 C ATOM 1868 C GLN A 855 20.072 12.515 57.062 1.00 17.85 C ANISOU 1868 C GLN A 855 1899 2638 2245 -66 5 206 C ATOM 1869 O GLN A 855 19.921 13.499 57.806 1.00 17.91 O ANISOU 1869 O GLN A 855 1912 2629 2262 -132 -32 206 O ATOM 1870 CB GLN A 855 22.404 11.866 56.391 1.00 18.11 C ANISOU 1870 CB GLN A 855 1803 2780 2297 9 56 316 C ATOM 1871 CG GLN A 855 22.959 13.271 56.616 1.00 22.12 C ANISOU 1871 CG GLN A 855 2260 3319 2825 -82 22 367 C ATOM 1872 CD GLN A 855 23.600 13.440 57.982 1.00 25.85 C ANISOU 1872 CD GLN A 855 2692 3810 3320 -146 -40 401 C ATOM 1873 OE1 GLN A 855 24.505 12.696 58.354 1.00 24.51 O ANISOU 1873 OE1 GLN A 855 2455 3695 3164 -109 -42 452 O ATOM 1874 NE2 GLN A 855 23.121 14.432 58.747 1.00 24.45 N ANISOU 1874 NE2 GLN A 855 2561 3586 3140 -237 -94 373 N ATOM 1875 N LEU A 856 19.269 12.239 56.035 1.00 17.68 N ANISOU 1875 N LEU A 856 1919 2601 2198 -30 33 169 N ATOM 1876 CA LEU A 856 18.109 13.097 55.719 1.00 17.60 C ANISOU 1876 CA LEU A 856 1946 2565 2176 -58 21 138 C ATOM 1877 C LEU A 856 17.135 13.116 56.899 1.00 16.95 C ANISOU 1877 C LEU A 856 1896 2444 2101 -92 -11 99 C ATOM 1878 O LEU A 856 16.643 14.188 57.288 1.00 17.76 O ANISOU 1878 O LEU A 856 2011 2526 2210 -123 -27 93 O ATOM 1879 CB LEU A 856 17.439 12.689 54.409 1.00 16.80 C ANISOU 1879 CB LEU A 856 1877 2470 2038 -19 45 112 C ATOM 1880 CG LEU A 856 16.220 13.517 53.958 1.00 19.19 C ANISOU 1880 CG LEU A 856 2202 2762 2326 -36 29 95 C ATOM 1881 CD1 LEU A 856 16.490 15.027 53.878 1.00 19.07 C ANISOU 1881 CD1 LEU A 856 2171 2744 2332 -62 23 139 C ATOM 1882 CD2 LEU A 856 15.681 12.978 52.635 1.00 19.44 C ANISOU 1882 CD2 LEU A 856 2262 2815 2307 -6 41 75 C ATOM 1883 N MET A 857 16.860 11.951 57.484 1.00 15.66 N ANISOU 1883 N MET A 857 1750 2267 1933 -81 -14 76 N ATOM 1884 CA MET A 857 16.033 11.905 58.717 1.00 16.42 C ANISOU 1884 CA MET A 857 1869 2341 2028 -115 -36 51 C ATOM 1885 C MET A 857 16.608 12.813 59.806 1.00 16.80 C ANISOU 1885 C MET A 857 1909 2390 2084 -156 -61 68 C ATOM 1886 O MET A 857 15.892 13.663 60.398 1.00 17.71 O ANISOU 1886 O MET A 857 2051 2486 2192 -180 -68 44 O ATOM 1887 CB MET A 857 15.963 10.475 59.271 1.00 16.40 C ANISOU 1887 CB MET A 857 1886 2324 2021 -106 -38 45 C ATOM 1888 CG MET A 857 15.210 9.506 58.351 1.00 19.10 C ANISOU 1888 CG MET A 857 2263 2647 2349 -87 -25 15 C ATOM 1889 SD MET A 857 15.266 7.818 58.957 1.00 18.49 S ANISOU 1889 SD MET A 857 2230 2524 2273 -80 -27 16 S ATOM 1890 CE MET A 857 15.145 6.929 57.426 1.00 20.34 C ANISOU 1890 CE MET A 857 2517 2726 2484 -43 -7 -19 C ATOM 1891 N LEU A 858 17.893 12.625 60.104 1.00 16.32 N ANISOU 1891 N LEU A 858 1813 2354 2035 -163 -75 110 N ATOM 1892 CA LEU A 858 18.566 13.444 61.149 1.00 16.86 C ANISOU 1892 CA LEU A 858 1875 2429 2103 -222 -114 129 C ATOM 1893 C LEU A 858 18.454 14.943 60.862 1.00 17.67 C ANISOU 1893 C LEU A 858 1998 2506 2210 -261 -121 121 C ATOM 1894 O LEU A 858 18.322 15.759 61.820 1.00 17.53 O ANISOU 1894 O LEU A 858 2024 2459 2177 -311 -149 99 O ATOM 1895 CB LEU A 858 20.039 13.036 61.288 1.00 17.43 C ANISOU 1895 CB LEU A 858 1881 2552 2190 -224 -133 194 C ATOM 1896 CG LEU A 858 20.310 11.595 61.756 1.00 17.69 C ANISOU 1896 CG LEU A 858 1901 2599 2222 -177 -132 214 C ATOM 1897 CD1 LEU A 858 21.822 11.342 61.964 1.00 20.38 C ANISOU 1897 CD1 LEU A 858 2157 3003 2581 -170 -154 294 C ATOM 1898 CD2 LEU A 858 19.505 11.238 63.065 1.00 21.72 C ANISOU 1898 CD2 LEU A 858 2467 3083 2703 -206 -156 184 C ATOM 1899 N ASP A 859 18.557 15.319 59.585 1.00 18.64 N ANISOU 1899 N ASP A 859 2101 2635 2348 -238 -95 141 N ATOM 1900 CA ASP A 859 18.474 16.732 59.184 1.00 20.26 C ANISOU 1900 CA ASP A 859 2332 2804 2562 -271 -100 147 C ATOM 1901 C ASP A 859 17.038 17.245 59.412 1.00 18.09 C ANISOU 1901 C ASP A 859 2122 2477 2276 -248 -89 93 C ATOM 1902 O ASP A 859 16.845 18.378 59.900 1.00 19.66 O ANISOU 1902 O ASP A 859 2375 2620 2474 -278 -102 77 O ATOM 1903 CB ASP A 859 18.911 16.940 57.727 1.00 19.54 C ANISOU 1903 CB ASP A 859 2202 2741 2481 -249 -71 193 C ATOM 1904 CG ASP A 859 20.428 16.680 57.501 1.00 26.04 C ANISOU 1904 CG ASP A 859 2946 3629 3319 -269 -72 262 C ATOM 1905 OD1 ASP A 859 21.211 16.619 58.467 1.00 27.50 O ANISOU 1905 OD1 ASP A 859 3103 3834 3513 -318 -109 283 O ATOM 1906 OD2 ASP A 859 20.804 16.541 56.325 1.00 32.20 O ANISOU 1906 OD2 ASP A 859 3688 4450 4096 -233 -33 299 O ATOM 1907 N CYS A 860 16.044 16.426 59.068 1.00 16.05 N ANISOU 1907 N CYS A 860 1859 2234 2006 -195 -64 67 N ATOM 1908 CA CYS A 860 14.631 16.789 59.330 1.00 17.23 C ANISOU 1908 CA CYS A 860 2043 2357 2145 -166 -50 28 C ATOM 1909 C CYS A 860 14.352 16.926 60.813 1.00 17.47 C ANISOU 1909 C CYS A 860 2113 2368 2157 -188 -57 -8 C ATOM 1910 O CYS A 860 13.418 17.634 61.201 1.00 17.35 O ANISOU 1910 O CYS A 860 2136 2323 2133 -162 -39 -37 O ATOM 1911 CB CYS A 860 13.657 15.768 58.740 1.00 18.69 C ANISOU 1911 CB CYS A 860 2203 2579 2320 -128 -34 16 C ATOM 1912 SG CYS A 860 13.628 15.768 56.938 1.00 20.21 S ANISOU 1912 SG CYS A 860 2372 2798 2510 -97 -26 44 S ATOM 1913 N TRP A 861 15.136 16.200 61.622 1.00 17.43 N ANISOU 1913 N TRP A 861 2098 2383 2140 -224 -79 -1 N ATOM 1914 CA TRP A 861 14.978 16.189 63.059 1.00 16.88 C ANISOU 1914 CA TRP A 861 2070 2308 2038 -250 -90 -30 C ATOM 1915 C TRP A 861 15.958 17.113 63.781 1.00 16.91 C ANISOU 1915 C TRP A 861 2115 2284 2028 -315 -131 -30 C ATOM 1916 O TRP A 861 16.226 16.929 64.969 1.00 19.76 O ANISOU 1916 O TRP A 861 2504 2655 2350 -353 -156 -43 O ATOM 1917 CB TRP A 861 15.109 14.772 63.624 1.00 18.55 C ANISOU 1917 CB TRP A 861 2254 2561 2235 -254 -96 -16 C ATOM 1918 CG TRP A 861 14.145 13.779 63.054 1.00 15.16 C ANISOU 1918 CG TRP A 861 1799 2148 1812 -216 -67 -19 C ATOM 1919 CD1 TRP A 861 12.884 14.013 62.578 1.00 18.41 C ANISOU 1919 CD1 TRP A 861 2208 2562 2227 -185 -37 -39 C ATOM 1920 CD2 TRP A 861 14.375 12.375 62.931 1.00 17.61 C ANISOU 1920 CD2 TRP A 861 2088 2474 2129 -211 -70 3 C ATOM 1921 NE1 TRP A 861 12.314 12.824 62.147 1.00 18.26 N ANISOU 1921 NE1 TRP A 861 2163 2564 2211 -180 -30 -33 N ATOM 1922 CE2 TRP A 861 13.216 11.810 62.341 1.00 17.55 C ANISOU 1922 CE2 TRP A 861 2074 2471 2124 -194 -48 -11 C ATOM 1923 CE3 TRP A 861 15.470 11.539 63.240 1.00 16.32 C ANISOU 1923 CE3 TRP A 861 1911 2319 1970 -216 -93 39 C ATOM 1924 CZ2 TRP A 861 13.108 10.464 62.060 1.00 17.72 C ANISOU 1924 CZ2 TRP A 861 2096 2488 2150 -194 -49 -2 C ATOM 1925 CZ3 TRP A 861 15.349 10.168 62.959 1.00 17.09 C ANISOU 1925 CZ3 TRP A 861 2009 2408 2075 -194 -84 51 C ATOM 1926 CH2 TRP A 861 14.184 9.656 62.376 1.00 19.00 C ANISOU 1926 CH2 TRP A 861 2264 2637 2317 -189 -63 26 C ATOM 1927 N GLN A 862 16.441 18.150 63.106 1.00 18.28 N ANISOU 1927 N GLN A 862 2300 2420 2227 -336 -142 -14 N ATOM 1928 CA GLN A 862 17.291 19.104 63.847 1.00 19.44 C ANISOU 1928 CA GLN A 862 2500 2528 2358 -419 -190 -19 C ATOM 1929 C GLN A 862 16.499 19.774 64.954 1.00 21.19 C ANISOU 1929 C GLN A 862 2828 2693 2531 -417 -181 -89 C ATOM 1930 O GLN A 862 15.370 20.196 64.752 1.00 20.90 O ANISOU 1930 O GLN A 862 2830 2617 2495 -347 -131 -124 O ATOM 1931 CB GLN A 862 17.879 20.171 62.929 1.00 22.28 C ANISOU 1931 CB GLN A 862 2865 2845 2755 -455 -203 16 C ATOM 1932 CG GLN A 862 18.931 19.642 61.969 1.00 24.61 C ANISOU 1932 CG GLN A 862 3055 3209 3086 -470 -211 92 C ATOM 1933 CD GLN A 862 20.158 19.166 62.690 1.00 36.02 C ANISOU 1933 CD GLN A 862 4448 4716 4523 -540 -264 131 C ATOM 1934 OE1 GLN A 862 20.511 17.985 62.623 1.00 43.54 O ANISOU 1934 OE1 GLN A 862 5323 5741 5480 -502 -256 162 O ATOM 1935 NE2 GLN A 862 20.788 20.063 63.436 1.00 35.55 N ANISOU 1935 NE2 GLN A 862 4435 4624 4448 -642 -323 129 N ATOM 1936 N LYS A 863 17.102 19.898 66.134 1.00 22.64 N ANISOU 1936 N LYS A 863 3060 2876 2666 -490 -229 -108 N ATOM 1937 CA LYS A 863 16.451 20.610 67.246 1.00 24.00 C ANISOU 1937 CA LYS A 863 3355 2990 2774 -490 -218 -185 C ATOM 1938 C LYS A 863 16.013 22.031 66.862 1.00 25.81 C ANISOU 1938 C LYS A 863 3683 3106 3018 -470 -195 -223 C ATOM 1939 O LYS A 863 14.892 22.460 67.158 1.00 25.86 O ANISOU 1939 O LYS A 863 3759 3067 3000 -389 -135 -278 O ATOM 1940 CB LYS A 863 17.409 20.668 68.441 1.00 25.41 C ANISOU 1940 CB LYS A 863 3580 3184 2889 -596 -293 -194 C ATOM 1941 CG LYS A 863 16.839 21.381 69.664 1.00 29.49 C ANISOU 1941 CG LYS A 863 4244 3641 3318 -603 -283 -283 C ATOM 1942 CD LYS A 863 17.854 21.414 70.838 1.00 30.92 C ANISOU 1942 CD LYS A 863 4477 3850 3423 -725 -374 -290 C ATOM 1943 CE LYS A 863 17.844 20.124 71.671 1.00 43.63 C ANISOU 1943 CE LYS A 863 6028 5568 4981 -715 -381 -263 C ATOM 1944 NZ LYS A 863 16.551 19.843 72.359 1.00 38.37 N ANISOU 1944 NZ LYS A 863 5419 4908 4252 -628 -298 -318 N ATOM 1945 N ASP A 864 16.923 22.761 66.238 1.00 25.16 N ANISOU 1945 N ASP A 864 3606 2979 2975 -543 -241 -187 N ATOM 1946 CA ASP A 864 16.667 24.118 65.768 1.00 27.36 C ANISOU 1946 CA ASP A 864 3983 3135 3277 -535 -228 -206 C ATOM 1947 C ASP A 864 15.915 24.044 64.438 1.00 25.53 C ANISOU 1947 C ASP A 864 3682 2911 3106 -432 -169 -165 C ATOM 1948 O ASP A 864 16.467 23.589 63.425 1.00 25.49 O ANISOU 1948 O ASP A 864 3572 2966 3145 -447 -180 -94 O ATOM 1949 CB ASP A 864 18.005 24.823 65.549 1.00 28.88 C ANISOU 1949 CB ASP A 864 4191 3289 3492 -674 -306 -163 C ATOM 1950 CG ASP A 864 17.861 26.262 65.068 1.00 36.31 C ANISOU 1950 CG ASP A 864 5251 4084 4461 -686 -302 -173 C ATOM 1951 OD1 ASP A 864 16.772 26.674 64.613 1.00 35.24 O ANISOU 1951 OD1 ASP A 864 5160 3888 4344 -567 -234 -194 O ATOM 1952 OD2 ASP A 864 18.871 26.996 65.154 1.00 39.74 O ANISOU 1952 OD2 ASP A 864 5734 4464 4900 -821 -371 -151 O ATOM 1953 N ARG A 865 14.663 24.492 64.445 1.00 25.15 N ANISOU 1953 N ARG A 865 3691 2812 3052 -323 -106 -206 N ATOM 1954 CA ARG A 865 13.824 24.377 63.256 1.00 25.12 C ANISOU 1954 CA ARG A 865 3616 2833 3096 -222 -59 -164 C ATOM 1955 C ARG A 865 14.407 25.121 62.041 1.00 24.92 C ANISOU 1955 C ARG A 865 3587 2757 3123 -253 -81 -99 C ATOM 1956 O ARG A 865 14.187 24.715 60.904 1.00 23.23 O ANISOU 1956 O ARG A 865 3283 2602 2940 -210 -65 -43 O ATOM 1957 CB ARG A 865 12.376 24.796 63.554 1.00 24.68 C ANISOU 1957 CB ARG A 865 3609 2742 3025 -94 11 -208 C ATOM 1958 CG ARG A 865 12.173 26.289 63.833 1.00 29.91 C ANISOU 1958 CG ARG A 865 4428 3252 3685 -64 27 -248 C ATOM 1959 CD ARG A 865 10.671 26.604 63.914 1.00 33.27 C ANISOU 1959 CD ARG A 865 4868 3666 4106 97 110 -271 C ATOM 1960 NE ARG A 865 10.376 27.933 64.456 1.00 35.42 N ANISOU 1960 NE ARG A 865 5312 3784 4362 153 142 -328 N ATOM 1961 CZ ARG A 865 10.506 28.236 65.746 1.00 35.80 C ANISOU 1961 CZ ARG A 865 5489 3774 4341 129 150 -416 C ATOM 1962 NH1 ARG A 865 10.940 27.318 66.595 1.00 32.99 N ANISOU 1962 NH1 ARG A 865 5096 3510 3930 47 123 -444 N ATOM 1963 NH2 ARG A 865 10.210 29.443 66.187 1.00 39.03 N ANISOU 1963 NH2 ARG A 865 6072 4029 4730 188 184 -476 N ATOM 1964 N ASN A 866 15.169 26.193 62.282 1.00 25.46 N ANISOU 1964 N ASN A 866 3760 2719 3196 -339 -120 -103 N ATOM 1965 CA ASN A 866 15.787 26.946 61.192 1.00 27.12 C ANISOU 1965 CA ASN A 866 3971 2879 3453 -386 -142 -29 C ATOM 1966 C ASN A 866 16.874 26.177 60.437 1.00 27.29 C ANISOU 1966 C ASN A 866 3858 3014 3495 -461 -172 50 C ATOM 1967 O ASN A 866 17.232 26.540 59.313 1.00 30.91 O ANISOU 1967 O ASN A 866 4283 3472 3988 -476 -171 125 O ATOM 1968 CB ASN A 866 16.319 28.293 61.698 1.00 32.24 C ANISOU 1968 CB ASN A 866 4777 3371 4100 -476 -181 -52 C ATOM 1969 CG ASN A 866 15.202 29.247 62.107 1.00 34.87 C ANISOU 1969 CG ASN A 866 5261 3567 4423 -369 -134 -118 C ATOM 1970 OD1 ASN A 866 15.309 29.929 63.124 1.00 44.66 O ANISOU 1970 OD1 ASN A 866 6648 4696 5625 -411 -151 -192 O ATOM 1971 ND2 ASN A 866 14.135 29.309 61.312 1.00 33.63 N ANISOU 1971 ND2 ASN A 866 5068 3416 4294 -227 -74 -89 N ATOM 1972 N ASN A 867 17.366 25.092 61.030 1.00 25.37 N ANISOU 1972 N ASN A 867 3538 2873 3229 -496 -192 38 N ATOM 1973 CA ASN A 867 18.396 24.271 60.414 1.00 25.11 C ANISOU 1973 CA ASN A 867 3376 2952 3212 -544 -210 109 C ATOM 1974 C ASN A 867 17.839 23.084 59.624 1.00 24.26 C ANISOU 1974 C ASN A 867 3167 2944 3106 -444 -163 124 C ATOM 1975 O ASN A 867 18.601 22.369 58.963 1.00 25.52 O ANISOU 1975 O ASN A 867 3229 3191 3276 -457 -161 179 O ATOM 1976 CB ASN A 867 19.377 23.747 61.467 1.00 27.01 C ANISOU 1976 CB ASN A 867 3586 3247 3428 -637 -265 103 C ATOM 1977 CG ASN A 867 20.203 24.861 62.108 1.00 35.96 C ANISOU 1977 CG ASN A 867 4806 4301 4557 -774 -332 103 C ATOM 1978 OD1 ASN A 867 20.353 25.948 61.547 1.00 39.54 O ANISOU 1978 OD1 ASN A 867 5319 4667 5038 -818 -339 132 O ATOM 1979 ND2 ASN A 867 20.744 24.588 63.295 1.00 37.52 N ANISOU 1979 ND2 ASN A 867 5015 4526 4714 -850 -388 74 N ATOM 1980 N ARG A 868 16.522 22.873 59.682 1.00 19.08 N ANISOU 1980 N ARG A 868 2535 2276 2438 -347 -123 77 N ATOM 1981 CA ARG A 868 15.927 21.787 58.907 1.00 19.26 C ANISOU 1981 CA ARG A 868 2476 2385 2459 -271 -90 88 C ATOM 1982 C ARG A 868 15.871 22.180 57.441 1.00 18.85 C ANISOU 1982 C ARG A 868 2399 2340 2425 -241 -73 147 C ATOM 1983 O ARG A 868 15.691 23.353 57.125 1.00 18.99 O ANISOU 1983 O ARG A 868 2477 2279 2458 -240 -73 168 O ATOM 1984 CB ARG A 868 14.514 21.494 59.414 1.00 18.29 C ANISOU 1984 CB ARG A 868 2372 2259 2317 -191 -60 33 C ATOM 1985 CG ARG A 868 14.523 20.984 60.885 1.00 16.36 C ANISOU 1985 CG ARG A 868 2152 2024 2041 -218 -69 -21 C ATOM 1986 CD ARG A 868 13.115 20.800 61.487 1.00 16.34 C ANISOU 1986 CD ARG A 868 2165 2026 2015 -143 -28 -68 C ATOM 1987 NE ARG A 868 13.249 20.744 62.935 1.00 17.03 N ANISOU 1987 NE ARG A 868 2308 2101 2061 -177 -35 -116 N ATOM 1988 CZ ARG A 868 12.319 21.161 63.770 1.00 18.71 C ANISOU 1988 CZ ARG A 868 2580 2286 2242 -127 3 -166 C ATOM 1989 NH1 ARG A 868 11.114 21.512 63.302 1.00 17.43 N ANISOU 1989 NH1 ARG A 868 2406 2121 2095 -32 52 -165 N ATOM 1990 NH2 ARG A 868 12.569 21.169 65.079 1.00 21.59 N ANISOU 1990 NH2 ARG A 868 3010 2640 2555 -166 -6 -211 N ATOM 1991 N PRO A 869 15.928 21.184 56.531 1.00 18.76 N ANISOU 1991 N PRO A 869 2311 2415 2403 -210 -57 172 N ATOM 1992 CA PRO A 869 15.811 21.519 55.104 1.00 19.12 C ANISOU 1992 CA PRO A 869 2338 2479 2447 -180 -40 227 C ATOM 1993 C PRO A 869 14.387 21.996 54.812 1.00 19.10 C ANISOU 1993 C PRO A 869 2369 2447 2442 -104 -29 214 C ATOM 1994 O PRO A 869 13.474 21.610 55.537 1.00 19.01 O ANISOU 1994 O PRO A 869 2360 2437 2425 -66 -24 162 O ATOM 1995 CB PRO A 869 16.032 20.166 54.396 1.00 20.38 C ANISOU 1995 CB PRO A 869 2429 2736 2579 -155 -23 230 C ATOM 1996 CG PRO A 869 15.681 19.120 55.424 1.00 21.30 C ANISOU 1996 CG PRO A 869 2537 2868 2689 -146 -29 169 C ATOM 1997 CD PRO A 869 16.080 19.737 56.774 1.00 17.85 C ANISOU 1997 CD PRO A 869 2138 2374 2270 -200 -53 149 C ATOM 1998 N LYS A 870 14.208 22.793 53.757 1.00 20.33 N ANISOU 1998 N LYS A 870 2668 2454 2601 -338 -262 -49 N ATOM 1999 CA LYS A 870 12.880 23.114 53.220 1.00 17.86 C ANISOU 1999 CA LYS A 870 2433 2137 2217 -280 -180 57 C ATOM 2000 C LYS A 870 12.379 21.961 52.369 1.00 20.17 C ANISOU 2000 C LYS A 870 2652 2550 2461 -276 -111 136 C ATOM 2001 O LYS A 870 13.181 21.157 51.869 1.00 19.13 O ANISOU 2001 O LYS A 870 2436 2470 2364 -344 -97 135 O ATOM 2002 CB LYS A 870 12.943 24.346 52.311 1.00 20.50 C ANISOU 2002 CB LYS A 870 2820 2340 2629 -340 -119 114 C ATOM 2003 CG LYS A 870 13.601 25.572 52.948 1.00 27.85 C ANISOU 2003 CG LYS A 870 3801 3089 3690 -396 -168 10 C ATOM 2004 CD LYS A 870 12.948 25.870 54.287 1.00 33.22 C ANISOU 2004 CD LYS A 870 4582 3763 4278 -260 -269 -90 C ATOM 2005 CE LYS A 870 13.523 27.171 54.898 1.00 42.03 C ANISOU 2005 CE LYS A 870 5762 4676 5533 -306 -345 -242 C ATOM 2006 NZ LYS A 870 13.101 27.309 56.311 1.00 43.60 N ANISOU 2006 NZ LYS A 870 6065 4899 5601 -140 -472 -380 N ATOM 2007 N PHE A 871 11.061 21.875 52.175 1.00 18.14 N ANISOU 2007 N PHE A 871 2411 2337 2145 -193 -76 180 N ATOM 2008 CA PHE A 871 10.578 20.822 51.279 1.00 18.11 C ANISOU 2008 CA PHE A 871 2311 2435 2134 -202 -42 200 C ATOM 2009 C PHE A 871 11.221 20.816 49.899 1.00 17.65 C ANISOU 2009 C PHE A 871 2235 2403 2069 -256 -27 231 C ATOM 2010 O PHE A 871 11.477 19.738 49.355 1.00 18.06 O ANISOU 2010 O PHE A 871 2212 2527 2124 -288 -15 207 O ATOM 2011 CB PHE A 871 9.054 20.764 51.218 1.00 17.12 C ANISOU 2011 CB PHE A 871 2147 2362 1997 -112 -27 199 C ATOM 2012 CG PHE A 871 8.462 20.116 52.450 1.00 15.34 C ANISOU 2012 CG PHE A 871 1896 2130 1801 -70 36 186 C ATOM 2013 CD1 PHE A 871 8.659 18.736 52.682 1.00 15.93 C ANISOU 2013 CD1 PHE A 871 1902 2218 1931 -115 100 175 C ATOM 2014 CD2 PHE A 871 7.688 20.851 53.336 1.00 16.33 C ANISOU 2014 CD2 PHE A 871 2085 2223 1897 36 65 199 C ATOM 2015 CE1 PHE A 871 8.126 18.120 53.814 1.00 16.68 C ANISOU 2015 CE1 PHE A 871 2008 2280 2051 -55 218 204 C ATOM 2016 CE2 PHE A 871 7.149 20.246 54.483 1.00 17.30 C ANISOU 2016 CE2 PHE A 871 2210 2337 2027 105 177 216 C ATOM 2017 CZ PHE A 871 7.369 18.872 54.718 1.00 19.22 C ANISOU 2017 CZ PHE A 871 2398 2580 2327 59 268 232 C ATOM 2018 N GLU A 872 11.482 21.993 49.335 1.00 17.19 N ANISOU 2018 N GLU A 872 2263 2270 1998 -251 -1 292 N ATOM 2019 CA GLU A 872 12.124 22.044 48.021 1.00 20.27 C ANISOU 2019 CA GLU A 872 2670 2674 2355 -269 68 357 C ATOM 2020 C GLU A 872 13.482 21.341 48.025 1.00 21.00 C ANISOU 2020 C GLU A 872 2674 2773 2531 -385 106 330 C ATOM 2021 O GLU A 872 13.872 20.699 47.037 1.00 21.49 O ANISOU 2021 O GLU A 872 2709 2910 2546 -379 159 350 O ATOM 2022 CB GLU A 872 12.264 23.474 47.515 1.00 21.20 C ANISOU 2022 CB GLU A 872 2925 2660 2470 -239 152 464 C ATOM 2023 CG GLU A 872 12.684 23.510 46.050 1.00 28.89 C ANISOU 2023 CG GLU A 872 3963 3662 3352 -188 269 572 C ATOM 2024 CD GLU A 872 12.872 24.909 45.544 1.00 36.80 C ANISOU 2024 CD GLU A 872 5132 4489 4362 -145 415 720 C ATOM 2025 OE1 GLU A 872 12.753 25.846 46.349 1.00 37.72 O ANISOU 2025 OE1 GLU A 872 5297 4446 4589 -185 409 710 O ATOM 2026 OE2 GLU A 872 13.168 25.062 44.350 1.00 41.27 O ANISOU 2026 OE2 GLU A 872 5798 5061 4820 -60 554 847 O ATOM 2027 N GLN A 873 14.193 21.476 49.137 1.00 20.89 N ANISOU 2027 N GLN A 873 2616 2692 2629 -461 66 266 N ATOM 2028 CA GLN A 873 15.532 20.892 49.269 1.00 21.97 C ANISOU 2028 CA GLN A 873 2638 2845 2866 -548 75 217 C ATOM 2029 C GLN A 873 15.397 19.393 49.413 1.00 20.18 C ANISOU 2029 C GLN A 873 2353 2736 2578 -503 39 177 C ATOM 2030 O GLN A 873 16.220 18.625 48.869 1.00 20.36 O ANISOU 2030 O GLN A 873 2300 2813 2625 -527 83 170 O ATOM 2031 CB GLN A 873 16.261 21.492 50.468 1.00 20.50 C ANISOU 2031 CB GLN A 873 2410 2574 2806 -602 -11 114 C ATOM 2032 CG GLN A 873 16.638 22.945 50.237 1.00 27.07 C ANISOU 2032 CG GLN A 873 3271 3234 3778 -692 53 129 C ATOM 2033 CD GLN A 873 17.245 23.645 51.457 1.00 28.82 C ANISOU 2033 CD GLN A 873 3447 3356 4148 -743 -75 -37 C ATOM 2034 OE1 GLN A 873 16.705 23.603 52.584 1.00 26.62 O ANISOU 2034 OE1 GLN A 873 3236 3105 3772 -640 -216 -125 O ATOM 2035 NE2 GLN A 873 18.332 24.364 51.215 1.00 34.72 N ANISOU 2035 NE2 GLN A 873 4081 3971 5140 -893 -15 -90 N ATOM 2036 N ILE A 874 14.360 18.965 50.125 1.00 16.90 N ANISOU 2036 N ILE A 874 1977 2343 2103 -432 -9 157 N ATOM 2037 CA ILE A 874 14.119 17.525 50.312 1.00 17.48 C ANISOU 2037 CA ILE A 874 2009 2472 2159 -396 0 131 C ATOM 2038 C ILE A 874 13.826 16.885 48.962 1.00 18.08 C ANISOU 2038 C ILE A 874 2053 2610 2209 -403 41 128 C ATOM 2039 O ILE A 874 14.356 15.810 48.636 1.00 17.37 O ANISOU 2039 O ILE A 874 1915 2548 2135 -408 67 96 O ATOM 2040 CB ILE A 874 12.965 17.282 51.302 1.00 16.85 C ANISOU 2040 CB ILE A 874 1973 2371 2059 -326 4 132 C ATOM 2041 CG1 ILE A 874 13.408 17.784 52.697 1.00 16.52 C ANISOU 2041 CG1 ILE A 874 1999 2291 1988 -265 -50 116 C ATOM 2042 CG2 ILE A 874 12.566 15.783 51.329 1.00 19.72 C ANISOU 2042 CG2 ILE A 874 2294 2740 2460 -312 73 121 C ATOM 2043 CD1 ILE A 874 12.289 17.691 53.745 1.00 17.51 C ANISOU 2043 CD1 ILE A 874 2201 2391 2061 -159 -1 143 C ATOM 2044 N VAL A 875 12.968 17.524 48.173 1.00 17.27 N ANISOU 2044 N VAL A 875 1985 2530 2047 -370 33 147 N ATOM 2045 CA VAL A 875 12.663 16.993 46.844 1.00 17.54 C ANISOU 2045 CA VAL A 875 2005 2647 2011 -327 31 109 C ATOM 2046 C VAL A 875 13.961 16.877 46.026 1.00 20.38 C ANISOU 2046 C VAL A 875 2376 3029 2339 -343 105 145 C ATOM 2047 O VAL A 875 14.206 15.855 45.360 1.00 20.85 O ANISOU 2047 O VAL A 875 2406 3146 2370 -320 115 82 O ATOM 2048 CB VAL A 875 11.626 17.862 46.104 1.00 17.15 C ANISOU 2048 CB VAL A 875 2012 2644 1861 -228 -15 125 C ATOM 2049 CG1 VAL A 875 11.423 17.359 44.648 1.00 18.57 C ANISOU 2049 CG1 VAL A 875 2204 2940 1913 -129 -53 60 C ATOM 2050 CG2 VAL A 875 10.262 17.823 46.837 1.00 16.00 C ANISOU 2050 CG2 VAL A 875 1804 2497 1779 -204 -76 67 C ATOM 2051 N SER A 876 14.789 17.913 46.091 1.00 19.15 N ANISOU 2051 N SER A 876 2252 2813 2213 -385 173 234 N ATOM 2052 CA SER A 876 16.039 17.950 45.358 1.00 20.91 C ANISOU 2052 CA SER A 876 2455 3039 2452 -412 294 284 C ATOM 2053 C SER A 876 16.987 16.820 45.792 1.00 19.92 C ANISOU 2053 C SER A 876 2211 2944 2415 -454 290 213 C ATOM 2054 O SER A 876 17.640 16.199 44.952 1.00 20.47 O ANISOU 2054 O SER A 876 2258 3071 2451 -422 371 211 O ATOM 2055 CB SER A 876 16.691 19.322 45.516 1.00 26.41 C ANISOU 2055 CB SER A 876 3168 3615 3251 -487 388 375 C ATOM 2056 OG SER A 876 15.886 20.295 44.847 1.00 35.49 O ANISOU 2056 OG SER A 876 4469 4730 4286 -401 432 473 O ATOM 2057 N ILE A 877 17.043 16.566 47.093 1.00 19.83 N ANISOU 2057 N ILE A 877 2148 2898 2490 -486 201 160 N ATOM 2058 CA ILE A 877 17.895 15.520 47.640 1.00 20.79 C ANISOU 2058 CA ILE A 877 2181 3045 2672 -474 181 102 C ATOM 2059 C ILE A 877 17.468 14.166 47.114 1.00 20.19 C ANISOU 2059 C ILE A 877 2129 3007 2536 -413 197 59 C ATOM 2060 O ILE A 877 18.310 13.350 46.712 1.00 21.35 O ANISOU 2060 O ILE A 877 2225 3189 2696 -381 245 32 O ATOM 2061 CB ILE A 877 17.877 15.552 49.184 1.00 18.71 C ANISOU 2061 CB ILE A 877 1914 2744 2450 -453 74 63 C ATOM 2062 CG1 ILE A 877 18.716 16.734 49.681 1.00 21.72 C ANISOU 2062 CG1 ILE A 877 2226 3088 2937 -517 30 36 C ATOM 2063 CG2 ILE A 877 18.422 14.239 49.769 1.00 23.85 C ANISOU 2063 CG2 ILE A 877 2534 3423 3104 -367 52 24 C ATOM 2064 CD1 ILE A 877 18.337 17.142 51.121 1.00 23.25 C ANISOU 2064 CD1 ILE A 877 2479 3248 3110 -463 -100 -18 C ATOM 2065 N LEU A 878 16.154 13.925 47.140 1.00 17.49 N ANISOU 2065 N LEU A 878 1844 2646 2155 -396 158 33 N ATOM 2066 CA LEU A 878 15.600 12.665 46.679 1.00 17.49 C ANISOU 2066 CA LEU A 878 1845 2645 2157 -365 163 -51 C ATOM 2067 C LEU A 878 15.776 12.495 45.194 1.00 20.19 C ANISOU 2067 C LEU A 878 2203 3066 2402 -320 184 -99 C ATOM 2068 O LEU A 878 16.121 11.400 44.735 1.00 20.70 O ANISOU 2068 O LEU A 878 2260 3134 2473 -284 209 -178 O ATOM 2069 CB LEU A 878 14.117 12.556 47.102 1.00 16.84 C ANISOU 2069 CB LEU A 878 1764 2514 2119 -380 126 -91 C ATOM 2070 CG LEU A 878 13.983 12.515 48.635 1.00 15.67 C ANISOU 2070 CG LEU A 878 1636 2282 2037 -379 152 -29 C ATOM 2071 CD1 LEU A 878 12.490 12.594 48.968 1.00 17.54 C ANISOU 2071 CD1 LEU A 878 1852 2476 2335 -394 161 -50 C ATOM 2072 CD2 LEU A 878 14.590 11.201 49.253 1.00 17.78 C ANISOU 2072 CD2 LEU A 878 1918 2474 2362 -336 220 -27 C ATOM 2073 N ASP A 879 15.585 13.576 44.434 1.00 18.78 N ANISOU 2073 N ASP A 879 2076 2944 2114 -292 188 -44 N ATOM 2074 CA ASP A 879 15.777 13.492 42.988 1.00 22.28 C ANISOU 2074 CA ASP A 879 2583 3479 2402 -190 226 -67 C ATOM 2075 C ASP A 879 17.214 13.101 42.661 1.00 22.17 C ANISOU 2075 C ASP A 879 2541 3483 2399 -179 357 -28 C ATOM 2076 O ASP A 879 17.445 12.351 41.714 1.00 23.20 O ANISOU 2076 O ASP A 879 2709 3676 2430 -83 388 -101 O ATOM 2077 CB ASP A 879 15.417 14.822 42.309 1.00 23.08 C ANISOU 2077 CB ASP A 879 2788 3620 2362 -118 249 37 C ATOM 2078 CG ASP A 879 13.921 14.998 42.107 1.00 27.13 C ANISOU 2078 CG ASP A 879 3328 4178 2801 -44 98 -49 C ATOM 2079 OD1 ASP A 879 13.159 14.002 42.225 1.00 28.35 O ANISOU 2079 OD1 ASP A 879 3403 4344 3024 -56 -16 -220 O ATOM 2080 OD2 ASP A 879 13.515 16.129 41.759 1.00 28.20 O ANISOU 2080 OD2 ASP A 879 3558 4331 2825 37 102 47 O ATOM 2081 N LYS A 880 18.179 13.607 43.435 1.00 22.98 N ANISOU 2081 N LYS A 880 2562 3537 2631 -265 423 61 N ATOM 2082 CA LYS A 880 19.600 13.285 43.167 1.00 26.16 C ANISOU 2082 CA LYS A 880 2881 3969 3092 -257 552 86 C ATOM 2083 C LYS A 880 19.870 11.808 43.450 1.00 24.91 C ANISOU 2083 C LYS A 880 2681 3814 2972 -208 509 -23 C ATOM 2084 O LYS A 880 20.627 11.167 42.732 1.00 27.30 O ANISOU 2084 O LYS A 880 2967 4166 3238 -130 603 -48 O ATOM 2085 CB LYS A 880 20.566 14.137 43.998 1.00 25.57 C ANISOU 2085 CB LYS A 880 2672 3844 3199 -365 592 149 C ATOM 2086 CG LYS A 880 20.819 15.541 43.492 1.00 36.42 C ANISOU 2086 CG LYS A 880 4063 5171 4603 -423 733 271 C ATOM 2087 CD LYS A 880 22.081 16.084 44.159 1.00 45.30 C ANISOU 2087 CD LYS A 880 4984 6244 5983 -544 788 268 C ATOM 2088 CE LYS A 880 22.435 17.473 43.685 1.00 51.07 C ANISOU 2088 CE LYS A 880 5712 6869 6824 -636 979 388 C ATOM 2089 NZ LYS A 880 23.721 17.911 44.279 1.00 56.93 N ANISOU 2089 NZ LYS A 880 6194 7552 7884 -777 1028 332 N ATOM 2090 N LEU A 881 19.247 11.279 44.500 1.00 22.74 N ANISOU 2090 N LEU A 881 2405 3468 2766 -236 396 -73 N ATOM 2091 CA LEU A 881 19.334 9.846 44.802 1.00 22.16 C ANISOU 2091 CA LEU A 881 2336 3346 2739 -178 384 -156 C ATOM 2092 C LEU A 881 18.718 8.980 43.696 1.00 23.14 C ANISOU 2092 C LEU A 881 2535 3471 2785 -120 386 -279 C ATOM 2093 O LEU A 881 19.269 7.925 43.339 1.00 24.38 O ANISOU 2093 O LEU A 881 2701 3613 2951 -43 433 -351 O ATOM 2094 CB LEU A 881 18.716 9.533 46.178 1.00 20.06 C ANISOU 2094 CB LEU A 881 2088 2977 2557 -201 319 -145 C ATOM 2095 CG LEU A 881 19.499 10.136 47.357 1.00 21.46 C ANISOU 2095 CG LEU A 881 2204 3168 2781 -195 279 -75 C ATOM 2096 CD1 LEU A 881 18.661 9.921 48.639 1.00 24.82 C ANISOU 2096 CD1 LEU A 881 2708 3500 3223 -173 237 -47 C ATOM 2097 CD2 LEU A 881 20.897 9.515 47.516 1.00 24.03 C ANISOU 2097 CD2 LEU A 881 2443 3539 3148 -98 299 -90 C ATOM 2098 N ILE A 882 17.602 9.437 43.135 1.00 22.15 N ANISOU 2098 N ILE A 882 2460 3371 2584 -136 318 -327 N ATOM 2099 CA ILE A 882 16.928 8.692 42.056 1.00 24.14 C ANISOU 2099 CA ILE A 882 2767 3644 2759 -64 261 -503 C ATOM 2100 C ILE A 882 17.842 8.684 40.821 1.00 26.74 C ANISOU 2100 C ILE A 882 3159 4091 2910 71 348 -505 C ATOM 2101 O ILE A 882 17.937 7.678 40.121 1.00 28.71 O ANISOU 2101 O ILE A 882 3452 4341 3113 164 342 -657 O ATOM 2102 CB ILE A 882 15.524 9.297 41.761 1.00 24.18 C ANISOU 2102 CB ILE A 882 2783 3685 2718 -77 132 -573 C ATOM 2103 CG1 ILE A 882 14.601 8.948 42.934 1.00 27.30 C ANISOU 2103 CG1 ILE A 882 3099 3944 3329 -200 93 -602 C ATOM 2104 CG2 ILE A 882 14.953 8.776 40.425 1.00 29.12 C ANISOU 2104 CG2 ILE A 882 3461 4394 3210 47 26 -790 C ATOM 2105 CD1 ILE A 882 13.256 9.666 42.936 1.00 29.47 C ANISOU 2105 CD1 ILE A 882 3333 4253 3611 -224 -17 -646 C ATOM 2106 N ARG A 883 18.528 9.802 40.595 1.00 27.83 N ANISOU 2106 N ARG A 883 3303 4305 2965 84 455 -334 N ATOM 2107 CA ARG A 883 19.411 9.975 39.427 1.00 32.82 C ANISOU 2107 CA ARG A 883 4000 5042 3427 222 610 -282 C ATOM 2108 C ARG A 883 20.718 9.230 39.546 1.00 32.67 C ANISOU 2108 C ARG A 883 3896 5017 3499 247 741 -273 C ATOM 2109 O ARG A 883 21.302 8.811 38.537 1.00 35.19 O ANISOU 2109 O ARG A 883 4277 5412 3681 397 857 -303 O ATOM 2110 CB ARG A 883 19.710 11.449 39.204 1.00 33.03 C ANISOU 2110 CB ARG A 883 4051 5101 3397 206 741 -78 C ATOM 2111 CG ARG A 883 18.800 12.099 38.179 1.00 44.73 C ANISOU 2111 CG ARG A 883 5711 6663 4621 353 704 -70 C ATOM 2112 CD ARG A 883 19.372 13.435 37.692 1.00 52.67 C ANISOU 2112 CD ARG A 883 6793 7671 5549 390 934 171 C ATOM 2113 NE ARG A 883 19.515 14.380 38.799 1.00 53.59 N ANISOU 2113 NE ARG A 883 6793 7666 5905 184 952 289 N ATOM 2114 CZ ARG A 883 18.517 15.091 39.329 1.00 53.02 C ANISOU 2114 CZ ARG A 883 6752 7544 5847 132 814 301 C ATOM 2115 NH1 ARG A 883 17.269 14.993 38.852 1.00 47.92 N ANISOU 2115 NH1 ARG A 883 6222 6972 5012 265 642 205 N ATOM 2116 NH2 ARG A 883 18.781 15.904 40.345 1.00 43.16 N ANISOU 2116 NH2 ARG A 883 5405 6178 4813 -41 836 384 N ATOM 2117 N ASN A 884 21.191 9.071 40.774 1.00 32.68 N ANISOU 2117 N ASN A 884 3763 4943 3712 137 720 -235 N ATOM 2118 CA ASN A 884 22.429 8.327 41.040 1.00 32.89 C ANISOU 2118 CA ASN A 884 3681 4972 3842 189 809 -239 C ATOM 2119 C ASN A 884 22.149 7.225 42.056 1.00 32.25 C ANISOU 2119 C ASN A 884 3595 4776 3882 182 693 -325 C ATOM 2120 O ASN A 884 22.550 7.329 43.230 1.00 28.21 O ANISOU 2120 O ASN A 884 2989 4229 3501 141 651 -267 O ATOM 2121 CB ASN A 884 23.531 9.255 41.553 1.00 34.24 C ANISOU 2121 CB ASN A 884 3673 5179 4159 112 906 -109 C ATOM 2122 CG ASN A 884 24.850 8.511 41.799 1.00 39.09 C ANISOU 2122 CG ASN A 884 4131 5830 4893 194 979 -135 C ATOM 2123 OD1 ASN A 884 25.263 7.667 41.003 1.00 44.69 O ANISOU 2123 OD1 ASN A 884 4881 6579 5520 334 1077 -189 O ATOM 2124 ND2 ASN A 884 25.506 8.825 42.910 1.00 44.50 N ANISOU 2124 ND2 ASN A 884 4634 6511 5761 133 912 -118 N ATOM 2125 N PRO A 885 21.438 6.166 41.619 1.00 33.43 N ANISOU 2125 N PRO A 885 3858 4853 3989 239 645 -472 N ATOM 2126 CA PRO A 885 21.010 5.137 42.562 1.00 32.31 C ANISOU 2126 CA PRO A 885 3741 4545 3990 222 588 -529 C ATOM 2127 C PRO A 885 22.176 4.417 43.246 1.00 31.19 C ANISOU 2127 C PRO A 885 3545 4372 3932 328 651 -481 C ATOM 2128 O PRO A 885 21.985 3.867 44.317 1.00 33.03 O ANISOU 2128 O PRO A 885 3807 4476 4266 337 626 -450 O ATOM 2129 CB PRO A 885 20.206 4.167 41.687 1.00 34.60 C ANISOU 2129 CB PRO A 885 4137 4753 4255 259 552 -734 C ATOM 2130 CG PRO A 885 20.705 4.414 40.293 1.00 38.28 C ANISOU 2130 CG PRO A 885 4646 5380 4517 382 602 -785 C ATOM 2131 CD PRO A 885 20.978 5.876 40.246 1.00 35.97 C ANISOU 2131 CD PRO A 885 4298 5228 4139 335 644 -607 C ATOM 2132 N GLY A 886 23.370 4.431 42.652 1.00 31.92 N ANISOU 2132 N GLY A 886 3562 4586 3981 433 746 -466 N ATOM 2133 CA GLY A 886 24.523 3.839 43.331 1.00 31.69 C ANISOU 2133 CA GLY A 886 3441 4561 4038 561 779 -431 C ATOM 2134 C GLY A 886 24.813 4.468 44.699 1.00 31.29 C ANISOU 2134 C GLY A 886 3281 4532 4077 522 685 -331 C ATOM 2135 O GLY A 886 25.370 3.828 45.589 1.00 33.31 O ANISOU 2135 O GLY A 886 3518 4755 4383 658 649 -314 O ATOM 2136 N SER A 887 24.450 5.727 44.866 1.00 27.96 N ANISOU 2136 N SER A 887 2802 4166 3655 370 636 -274 N ATOM 2137 CA SER A 887 24.681 6.414 46.126 1.00 31.36 C ANISOU 2137 CA SER A 887 3138 4620 4156 339 522 -221 C ATOM 2138 C SER A 887 23.881 5.768 47.247 1.00 32.04 C ANISOU 2138 C SER A 887 3380 4568 4225 394 446 -198 C ATOM 2139 O SER A 887 24.261 5.878 48.416 1.00 37.62 O ANISOU 2139 O SER A 887 4056 5295 4943 485 350 -167 O ATOM 2140 CB SER A 887 24.257 7.864 45.999 1.00 31.41 C ANISOU 2140 CB SER A 887 3099 4666 4168 160 501 -177 C ATOM 2141 OG SER A 887 22.857 7.910 45.791 1.00 41.21 O ANISOU 2141 OG SER A 887 4508 5819 5330 81 482 -173 O ATOM 2142 N LEU A 888 22.772 5.100 46.895 1.00 28.81 N ANISOU 2142 N LEU A 888 3133 4017 3796 353 497 -223 N ATOM 2143 CA LEU A 888 21.975 4.378 47.886 1.00 29.66 C ANISOU 2143 CA LEU A 888 3390 3949 3932 397 504 -181 C ATOM 2144 C LEU A 888 22.632 3.107 48.436 1.00 31.60 C ANISOU 2144 C LEU A 888 3715 4096 4194 615 559 -156 C ATOM 2145 O LEU A 888 22.141 2.537 49.423 1.00 31.42 O ANISOU 2145 O LEU A 888 3839 3917 4184 698 604 -75 O ATOM 2146 CB LEU A 888 20.561 4.083 47.352 1.00 28.44 C ANISOU 2146 CB LEU A 888 3328 3652 3825 258 551 -242 C ATOM 2147 CG LEU A 888 19.714 5.322 47.027 1.00 26.69 C ANISOU 2147 CG LEU A 888 3057 3514 3570 91 482 -248 C ATOM 2148 CD1 LEU A 888 18.561 4.979 46.067 1.00 29.77 C ANISOU 2148 CD1 LEU A 888 3480 3832 3999 -6 488 -380 C ATOM 2149 CD2 LEU A 888 19.168 5.996 48.302 1.00 24.99 C ANISOU 2149 CD2 LEU A 888 2865 3271 3357 62 444 -142 C ATOM 2150 N LYS A 889 23.731 2.673 47.808 1.00 29.90 N ANISOU 2150 N LYS A 889 3419 3965 3975 732 583 -210 N ATOM 2151 CA LYS A 889 24.406 1.442 48.204 1.00 33.16 C ANISOU 2151 CA LYS A 889 3914 4287 4399 974 638 -193 C ATOM 2152 C LYS A 889 25.271 1.617 49.449 1.00 32.59 C ANISOU 2152 C LYS A 889 3791 4320 4271 1185 529 -116 C ATOM 2153 O LYS A 889 25.730 0.636 50.028 1.00 35.68 O ANISOU 2153 O LYS A 889 4291 4630 4634 1440 560 -68 O ATOM 2154 CB LYS A 889 25.243 0.885 47.047 1.00 36.52 C ANISOU 2154 CB LYS A 889 4270 4771 4833 1053 709 -292 C ATOM 2155 CG LYS A 889 24.449 0.662 45.755 1.00 41.02 C ANISOU 2155 CG LYS A 889 4911 5263 5411 905 782 -412 C ATOM 2156 CD LYS A 889 25.257 -0.220 44.800 1.00 48.50 C ANISOU 2156 CD LYS A 889 5866 6219 6343 1063 873 -512 C ATOM 2157 CE LYS A 889 24.655 -0.259 43.388 1.00 55.23 C ANISOU 2157 CE LYS A 889 6774 7068 7142 965 907 -666 C ATOM 2158 NZ LYS A 889 25.396 0.580 42.390 1.00 54.85 N ANISOU 2158 NZ LYS A 889 6592 7269 6978 975 947 -671 N ATOM 2159 N ILE A 890 25.491 2.865 49.853 1.00 30.85 N ANISOU 2159 N ILE A 890 3415 4275 4032 1100 390 -118 N ATOM 2160 CA ILE A 890 26.266 3.153 51.056 1.00 34.45 C ANISOU 2160 CA ILE A 890 3803 4857 4430 1303 226 -104 C ATOM 2161 C ILE A 890 25.261 3.045 52.196 1.00 31.77 C ANISOU 2161 C ILE A 890 3709 4375 3988 1365 229 10 C ATOM 2162 O ILE A 890 24.310 3.799 52.230 1.00 27.95 O ANISOU 2162 O ILE A 890 3258 3854 3509 1159 235 29 O ATOM 2163 CB ILE A 890 26.865 4.573 51.025 1.00 34.80 C ANISOU 2163 CB ILE A 890 3570 5112 4540 1162 77 -192 C ATOM 2164 CG1 ILE A 890 27.799 4.754 49.809 1.00 39.23 C ANISOU 2164 CG1 ILE A 890 3882 5793 5230 1076 153 -273 C ATOM 2165 CG2 ILE A 890 27.603 4.874 52.345 1.00 38.62 C ANISOU 2165 CG2 ILE A 890 3973 5732 4968 1387 -150 -240 C ATOM 2166 CD1 ILE A 890 27.951 6.258 49.385 1.00 39.72 C ANISOU 2166 CD1 ILE A 890 3723 5958 5410 816 129 -320 C ATOM 2167 N ILE A 891 25.463 2.088 53.096 1.00 35.10 N ANISOU 2167 N ILE A 891 4317 4710 4310 1672 254 99 N ATOM 2168 CA ILE A 891 24.457 1.797 54.128 1.00 39.30 C ANISOU 2168 CA ILE A 891 5131 5060 4741 1762 349 251 C ATOM 2169 C ILE A 891 24.960 2.266 55.490 1.00 41.58 C ANISOU 2169 C ILE A 891 5462 5507 4831 2048 152 274 C ATOM 2170 O ILE A 891 26.157 2.239 55.743 1.00 41.37 O ANISOU 2170 O ILE A 891 5302 5669 4749 2280 -32 188 O ATOM 2171 CB ILE A 891 24.163 0.273 54.185 1.00 42.28 C ANISOU 2171 CB ILE A 891 5768 5153 5143 1930 591 373 C ATOM 2172 CG1 ILE A 891 23.820 -0.275 52.792 1.00 41.55 C ANISOU 2172 CG1 ILE A 891 5620 4919 5248 1685 736 281 C ATOM 2173 CG2 ILE A 891 23.048 -0.048 55.177 1.00 45.99 C ANISOU 2173 CG2 ILE A 891 6527 5391 5557 1994 776 559 C ATOM 2174 CD1 ILE A 891 22.546 0.294 52.187 1.00 39.65 C ANISOU 2174 CD1 ILE A 891 5340 4599 5127 1323 798 234 C ATOM 2175 N THR A 892 24.052 2.693 56.366 1.00 43.28 N ANISOU 2175 N THR A 892 5852 5658 4935 2055 181 370 N ATOM 2176 CA THR A 892 24.415 2.995 57.761 1.00 50.19 C ANISOU 2176 CA THR A 892 6848 6663 5558 2401 7 397 C ATOM 2177 C THR A 892 24.804 1.683 58.481 1.00 55.91 C ANISOU 2177 C THR A 892 7848 7282 6114 2846 111 553 C ATOM 2178 O THR A 892 24.384 0.599 58.064 1.00 58.46 O ANISOU 2178 O THR A 892 8330 7343 6539 2826 393 685 O ATOM 2179 CB THR A 892 23.256 3.709 58.525 1.00 47.58 C ANISOU 2179 CB THR A 892 6685 6270 5123 2334 64 483 C ATOM 2180 OG1 THR A 892 22.494 4.526 57.628 1.00 45.75 O ANISOU 2180 OG1 THR A 892 6285 6010 5090 1900 108 414 O ATOM 2181 CG2 THR A 892 23.809 4.584 59.636 1.00 51.55 C ANISOU 2181 CG2 THR A 892 7181 7008 5397 2587 -239 379 C ATOM 2182 N SER A 893 25.617 1.765 59.537 1.00 62.64 N ANISOU 2182 N SER A 893 8760 8327 6714 3265 -121 523 N ATOM 2183 CA SER A 893 26.050 0.560 60.270 1.00 67.49 C ANISOU 2183 CA SER A 893 9666 8859 7117 3766 -38 687 C ATOM 2184 C SER A 893 25.233 0.265 61.542 1.00 70.76 C ANISOU 2184 C SER A 893 10522 9121 7244 4083 146 938 C ATOM 2185 O SER A 893 24.429 1.093 62.002 1.00 69.40 O ANISOU 2185 O SER A 893 10406 8961 7001 3955 153 954 O ATOM 2186 CB SER A 893 27.542 0.631 60.609 1.00 71.70 C ANISOU 2186 CB SER A 893 10006 9710 7526 4127 -408 500 C ATOM 2187 OG SER A 893 27.785 1.518 61.689 1.00 74.52 O ANISOU 2187 OG SER A 893 10363 10313 7639 4362 -724 381 O ATOM 2188 N SER A 899 14.968 -1.195 68.528 1.00 58.52 N ANISOU 2188 N SER A 899 8721 4864 8650 -1000 -1971 38 N ATOM 2189 CA SER A 899 14.007 -0.663 69.501 1.00 55.75 C ANISOU 2189 CA SER A 899 7798 5053 8333 -1535 -1824 746 C ATOM 2190 C SER A 899 14.707 0.099 70.645 1.00 49.52 C ANISOU 2190 C SER A 899 6750 4929 7137 -1219 -1353 1202 C ATOM 2191 O SER A 899 14.287 0.058 71.801 1.00 53.37 O ANISOU 2191 O SER A 899 6995 5693 7589 -1526 -1161 1853 O ATOM 2192 CB SER A 899 13.079 -1.773 70.029 1.00 64.50 C ANISOU 2192 CB SER A 899 8856 5496 10155 -2286 -2109 1290 C ATOM 2193 OG SER A 899 12.074 -2.136 69.089 1.00 70.17 O ANISOU 2193 OG SER A 899 9542 5865 11254 -2842 -2646 874 O ATOM 2194 N ASN A 900 15.779 0.794 70.288 1.00 43.52 N ANISOU 2194 N ASN A 900 6041 4486 6009 -667 -1176 834 N ATOM 2195 CA ASN A 900 16.536 1.636 71.206 1.00 38.44 C ANISOU 2195 CA ASN A 900 5154 4448 5003 -439 -911 1059 C ATOM 2196 C ASN A 900 16.856 2.951 70.496 1.00 32.15 C ANISOU 2196 C ASN A 900 4213 4108 3895 -263 -711 642 C ATOM 2197 O ASN A 900 17.184 2.927 69.294 1.00 30.60 O ANISOU 2197 O ASN A 900 4193 3786 3649 -75 -707 264 O ATOM 2198 CB ASN A 900 17.838 0.947 71.545 1.00 44.88 C ANISOU 2198 CB ASN A 900 6072 4996 5985 8 -1033 1194 C ATOM 2199 CG ASN A 900 18.792 1.851 72.250 1.00 46.38 C ANISOU 2199 CG ASN A 900 5943 5843 5834 202 -952 1269 C ATOM 2200 OD1 ASN A 900 19.866 2.184 71.728 1.00 43.84 O ANISOU 2200 OD1 ASN A 900 5400 5668 5589 557 -875 973 O ATOM 2201 ND2 ASN A 900 18.409 2.277 73.442 1.00 53.27 N ANISOU 2201 ND2 ASN A 900 6753 7189 6296 -77 -948 1622 N ATOM 2202 N LEU A 901 16.786 4.079 71.213 1.00 25.61 N ANISOU 2202 N LEU A 901 3145 3762 2822 -330 -537 704 N ATOM 2203 CA LEU A 901 17.005 5.386 70.555 1.00 22.84 C ANISOU 2203 CA LEU A 901 2718 3596 2364 -255 -414 442 C ATOM 2204 C LEU A 901 18.490 5.724 70.561 1.00 24.75 C ANISOU 2204 C LEU A 901 2849 3970 2586 -103 -343 380 C ATOM 2205 O LEU A 901 19.210 5.310 71.460 1.00 25.78 O ANISOU 2205 O LEU A 901 2851 4220 2724 -30 -464 507 O ATOM 2206 CB LEU A 901 16.206 6.502 71.235 1.00 21.91 C ANISOU 2206 CB LEU A 901 2429 3698 2199 -338 -297 389 C ATOM 2207 CG LEU A 901 14.691 6.284 71.281 1.00 22.55 C ANISOU 2207 CG LEU A 901 2301 3830 2436 -451 -275 490 C ATOM 2208 CD1 LEU A 901 14.016 7.417 72.044 1.00 22.61 C ANISOU 2208 CD1 LEU A 901 2054 4096 2441 -306 -8 300 C ATOM 2209 CD2 LEU A 901 14.066 6.143 69.844 1.00 22.17 C ANISOU 2209 CD2 LEU A 901 2282 3561 2581 -481 -582 473 C ATOM 2210 N LEU A 902 18.928 6.510 69.580 1.00 23.96 N ANISOU 2210 N LEU A 902 2726 3913 2465 -105 -181 295 N ATOM 2211 CA LEU A 902 20.341 6.890 69.465 1.00 29.01 C ANISOU 2211 CA LEU A 902 3043 4765 3214 -93 -21 319 C ATOM 2212 C LEU A 902 20.529 8.359 69.806 1.00 29.72 C ANISOU 2212 C LEU A 902 3004 4840 3446 -442 -56 343 C ATOM 2213 O LEU A 902 19.758 9.204 69.329 1.00 31.88 O ANISOU 2213 O LEU A 902 3522 4868 3725 -550 -37 397 O ATOM 2214 CB LEU A 902 20.818 6.690 68.043 1.00 30.65 C ANISOU 2214 CB LEU A 902 3295 5095 3254 62 341 295 C ATOM 2215 CG LEU A 902 21.076 5.307 67.470 1.00 40.54 C ANISOU 2215 CG LEU A 902 4686 6290 4428 514 466 23 C ATOM 2216 CD1 LEU A 902 21.884 5.491 66.189 1.00 44.54 C ANISOU 2216 CD1 LEU A 902 5110 7217 4598 671 1048 -67 C ATOM 2217 CD2 LEU A 902 21.814 4.375 68.469 1.00 44.06 C ANISOU 2217 CD2 LEU A 902 4801 6619 5321 846 279 39 C ATOM 2218 N LEU A 903 21.564 8.668 70.587 1.00 33.09 N ANISOU 2218 N LEU A 903 3046 5448 4078 -615 -213 302 N ATOM 2219 CA LEU A 903 21.798 10.054 70.969 1.00 35.57 C ANISOU 2219 CA LEU A 903 3308 5558 4651 -1053 -371 186 C ATOM 2220 C LEU A 903 22.505 10.762 69.828 1.00 41.66 C ANISOU 2220 C LEU A 903 3846 6254 5729 -1374 -53 534 C ATOM 2221 O LEU A 903 23.620 10.402 69.468 1.00 45.71 O ANISOU 2221 O LEU A 903 3790 7180 6397 -1425 172 726 O ATOM 2222 CB LEU A 903 22.605 10.164 72.267 1.00 41.53 C ANISOU 2222 CB LEU A 903 3762 6564 5452 -1260 -843 -62 C ATOM 2223 CG LEU A 903 22.931 11.581 72.772 1.00 44.41 C ANISOU 2223 CG LEU A 903 4143 6583 6149 -1814 -1174 -408 C ATOM 2224 CD1 LEU A 903 21.666 12.429 72.904 1.00 45.41 C ANISOU 2224 CD1 LEU A 903 4912 6120 6222 -1710 -1097 -763 C ATOM 2225 CD2 LEU A 903 23.673 11.551 74.098 1.00 50.74 C ANISOU 2225 CD2 LEU A 903 4724 7779 6775 -2030 -1831 -768 C ATOM 2226 N ASP A 904 21.851 11.776 69.267 1.00 43.14 N ANISOU 2226 N ASP A 904 4419 5938 6034 -1559 -2 703 N ATOM 2227 CA ASP A 904 22.434 12.577 68.211 1.00 51.54 C ANISOU 2227 CA ASP A 904 5380 6876 7328 -1985 303 1269 C ATOM 2228 C ASP A 904 23.119 13.818 68.758 1.00 59.03 C ANISOU 2228 C ASP A 904 6115 7295 9017 -2678 23 1273 C ATOM 2229 O ASP A 904 22.470 14.658 69.375 1.00 60.78 O ANISOU 2229 O ASP A 904 6767 6771 9556 -2726 -376 925 O ATOM 2230 CB ASP A 904 21.355 12.983 67.227 1.00 53.67 C ANISOU 2230 CB ASP A 904 6248 6805 7339 -1809 360 1653 C ATOM 2231 CG ASP A 904 20.812 11.816 66.465 1.00 55.18 C ANISOU 2231 CG ASP A 904 6644 7522 6800 -1322 543 1630 C ATOM 2232 OD1 ASP A 904 20.908 10.666 66.951 1.00 55.43 O ANISOU 2232 OD1 ASP A 904 6503 7894 6662 -1012 546 1195 O ATOM 2233 OD2 ASP A 904 20.276 12.054 65.366 1.00 68.91 O ANISOU 2233 OD2 ASP A 904 8779 9270 8134 -1273 590 2069 O TER 2234 ASP A 904 HETATM 2235 O HOH A 1 -4.990 17.451 44.126 1.00 16.89 O HETATM 2236 O HOH A 2 12.020 23.423 57.212 1.00 20.58 O HETATM 2237 O HOH A 3 13.609 10.744 66.022 1.00 20.32 O HETATM 2238 O HOH A 4 2.669 17.366 60.447 1.00 19.06 O HETATM 2239 O HOH A 5 9.108 12.657 66.730 1.00 20.53 O HETATM 2240 O HOH A 6 7.752 24.818 64.117 1.00 21.06 O HETATM 2241 O HOH A 7 13.839 25.265 58.207 1.00 25.35 O HETATM 2242 O HOH A 8 -3.859 13.864 42.771 1.00 18.20 O HETATM 2243 O HOH A 9 -15.251 15.980 39.435 1.00 24.32 O HETATM 2244 O HOH A 10 -5.895 17.322 41.485 1.00 22.26 O HETATM 2245 O HOH A 11 4.099 3.422 60.724 1.00 24.16 O HETATM 2246 O HOH A 12 3.589 23.047 55.472 1.00 18.64 O HETATM 2247 O HOH A 13 10.309 24.466 49.995 1.00 20.97 O HETATM 2248 O HOH A 14 -9.481 4.975 48.065 1.00 26.08 O HETATM 2249 O HOH A 15 20.955 13.564 47.549 1.00 26.44 O HETATM 2250 O HOH A 16 -0.908 -2.238 42.731 1.00 24.13 O HETATM 2251 O HOH A 17 1.474 6.541 60.484 1.00 20.37 O HETATM 2252 O HOH A 18 5.620 20.301 44.403 1.00 22.45 O HETATM 2253 O HOH A 19 23.341 6.222 51.065 1.00 26.35 O HETATM 2254 O HOH A 20 7.557 25.240 50.152 1.00 21.70 O HETATM 2255 O HOH A 21 -22.707 15.160 31.082 1.00 26.77 O HETATM 2256 O HOH A 22 -21.960 12.967 33.150 1.00 28.89 O HETATM 2257 O HOH A 23 -6.920 18.138 46.269 1.00 23.52 O HETATM 2258 O HOH A 24 4.873 8.831 44.902 1.00 19.36 O HETATM 2259 O HOH A 25 10.075 16.668 72.555 1.00 24.67 O HETATM 2260 O HOH A 26 -22.053 15.481 38.519 1.00 22.64 O HETATM 2261 O HOH A 27 -10.217 5.602 37.692 1.00 24.82 O HETATM 2262 O HOH A 28 9.464 23.854 53.340 1.00 21.00 O HETATM 2263 O HOH A 29 -9.656 11.227 40.717 1.00 29.77 O HETATM 2264 O HOH A 30 -17.761 9.162 56.320 1.00 27.47 O HETATM 2265 O HOH A 31 -17.529 16.053 37.809 1.00 22.73 O HETATM 2266 O HOH A 32 8.010 4.345 43.683 1.00 24.83 O HETATM 2267 O HOH A 33 9.888 24.497 56.013 1.00 24.34 O HETATM 2268 O HOH A 34 1.552 9.630 69.202 1.00 31.48 O HETATM 2269 O HOH A 35 15.649 18.016 70.371 1.00 35.73 O HETATM 2270 O HOH A 36 -21.365 3.894 30.389 1.00 25.96 O HETATM 2271 O HOH A 37 -9.951 8.569 40.975 1.00 25.58 O HETATM 2272 O HOH A 38 3.445 20.579 61.769 1.00 24.39 O HETATM 2273 O HOH A 39 -8.783 18.698 44.255 1.00 28.17 O HETATM 2274 O HOH A 40 2.649 29.704 67.085 1.00 30.43 O HETATM 2275 O HOH A 41 7.838 14.038 68.799 1.00 24.08 O HETATM 2276 O HOH A 42 4.559 27.617 54.424 1.00 27.43 O HETATM 2277 O HOH A 43 -19.723 14.433 37.449 1.00 27.58 O HETATM 2278 O HOH A 44 6.012 6.083 43.958 1.00 24.96 O HETATM 2279 O HOH A 45 -13.806 10.573 49.973 1.00 27.12 O HETATM 2280 O HOH A 46 6.836 -3.912 58.908 1.00 28.57 O HETATM 2281 O HOH A 47 -14.237 15.037 56.015 1.00 37.92 O HETATM 2282 O HOH A 48 -9.319 9.332 48.704 1.00 26.27 O HETATM 2283 O HOH A 49 4.849 18.565 63.440 1.00 22.23 O HETATM 2284 O HOH A 50 17.009 -2.470 47.001 1.00 34.27 O HETATM 2285 O HOH A 51 4.955 10.622 42.544 1.00 25.98 O HETATM 2286 O HOH A 52 21.067 13.105 52.687 1.00 31.35 O HETATM 2287 O HOH A 53 9.964 -4.852 43.962 1.00 24.10 O HETATM 2288 O HOH A 54 -1.307 -3.957 57.315 1.00 27.48 O HETATM 2289 O HOH A 55 18.158 17.484 42.449 1.00 33.10 O HETATM 2290 O HOH A 56 9.198 19.041 73.394 1.00 29.42 O HETATM 2291 O HOH A 57 13.213 0.428 61.999 1.00 26.50 O HETATM 2292 O HOH A 58 -11.389 6.127 33.215 1.00 28.96 O HETATM 2293 O HOH A 59 18.223 10.050 79.538 1.00 29.22 O HETATM 2294 O HOH A 60 -4.179 24.388 43.856 1.00 26.08 O HETATM 2295 O HOH A 61 -6.813 11.274 40.134 1.00 29.94 O HETATM 2296 O HOH A 62 -3.178 -0.336 52.767 1.00 29.20 O HETATM 2297 O HOH A 63 -6.489 27.343 45.697 1.00 27.68 O HETATM 2298 O HOH A 64 -4.762 7.911 41.712 1.00 31.63 O HETATM 2299 O HOH A 65 7.659 17.681 40.550 1.00 55.22 O HETATM 2300 O HOH A 66 10.863 22.875 72.155 1.00 34.91 O HETATM 2301 O HOH A 67 -5.605 3.328 42.587 1.00 21.97 O HETATM 2302 O HOH A 68 -29.389 15.596 61.138 1.00 33.69 O HETATM 2303 O HOH A 69 -21.326 6.167 37.956 1.00 28.65 O HETATM 2304 O HOH A 70 8.026 19.247 43.647 1.00 27.06 O HETATM 2305 O HOH A 71 4.907 -8.260 55.769 1.00 30.61 O HETATM 2306 O HOH A 72 14.026 -1.634 60.465 1.00 29.07 O HETATM 2307 O HOH A 73 13.049 20.642 44.313 1.00 28.57 O HETATM 2308 O HOH A 74 -3.364 2.915 58.451 1.00 29.77 O HETATM 2309 O HOH A 75 7.007 32.158 65.045 1.00 45.52 O HETATM 2310 O HOH A 76 -26.127 17.561 44.184 1.00 26.82 O HETATM 2311 O HOH A 77 27.821 0.279 52.933 1.00 42.59 O HETATM 2312 O HOH A 78 -12.027 15.133 37.459 1.00 34.09 O HETATM 2313 O HOH A 79 -2.518 18.450 39.399 1.00 33.87 O HETATM 2314 O HOH A 80 2.472 17.071 64.048 1.00 31.34 O HETATM 2315 O HOH A 81 -32.153 13.193 50.048 1.00 37.03 O HETATM 2316 O HOH A 82 13.743 -2.634 51.170 1.00 35.07 O HETATM 2317 O HOH A 83 8.103 9.971 42.813 1.00 27.83 O HETATM 2318 O HOH A 84 19.721 18.725 66.542 1.00 36.48 O HETATM 2319 O HOH A 85 8.958 14.362 71.136 1.00 27.35 O HETATM 2320 O HOH A 86 5.097 16.340 41.524 1.00 39.66 O HETATM 2321 O HOH A 87 -3.260 3.955 40.033 1.00 32.43 O HETATM 2322 O HOH A 88 -20.640 1.818 33.383 1.00 31.36 O HETATM 2323 O HOH A 89 19.494 20.551 56.626 1.00 45.32 O HETATM 2324 O HOH A 90 21.152 10.352 78.355 1.00 39.72 O HETATM 2325 O HOH A 91 13.964 18.705 42.433 1.00 35.83 O HETATM 2326 O HOH A 92 10.444 -3.357 66.422 1.00 59.92 O HETATM 2327 O HOH A 93 20.285 28.806 61.028 1.00 58.37 O HETATM 2328 O HOH A 94 7.611 0.274 40.951 1.00 30.89 O HETATM 2329 O HOH A 95 2.586 5.197 79.691 1.00 42.99 O HETATM 2330 O HOH A 96 13.143 -0.683 41.445 1.00 34.74 O HETATM 2331 O HOH A 97 10.029 27.701 60.896 1.00 47.85 O HETATM 2332 O HOH A 98 22.497 12.571 41.130 1.00 46.40 O HETATM 2333 O HOH A 99 -28.342 16.276 44.981 1.00 33.07 O HETATM 2334 O HOH A 100 13.856 22.926 42.952 1.00 44.68 O HETATM 2335 O HOH A 101 -26.000 7.912 44.343 1.00 50.25 O HETATM 2336 O HOH A 102 13.072 21.880 68.699 1.00 35.84 O HETATM 2337 O HOH A 103 18.313 29.498 64.408 1.00 53.87 O HETATM 2338 O HOH A 104 -5.155 9.314 60.778 1.00 37.65 O HETATM 2339 O HOH A 105 -0.750 6.879 38.828 1.00 41.60 O HETATM 2340 O HOH A 106 -20.592 23.057 41.377 1.00 49.59 O HETATM 2341 O HOH A 107 -23.591 20.840 66.616 1.00 46.55 O HETATM 2342 O HOH A 108 6.100 -1.071 65.300 1.00 33.97 O HETATM 2343 O HOH A 109 5.099 -5.951 58.871 1.00 28.92 O HETATM 2344 O HOH A 110 1.839 27.957 65.232 1.00 34.69 O HETATM 2345 O HOH A 111 -5.503 1.592 37.526 1.00 52.66 O HETATM 2346 O HOH A 112 -4.985 5.236 58.057 1.00 34.11 O HETATM 2347 O HOH A 113 3.595 18.757 39.981 1.00 36.65 O HETATM 2348 O HOH A 114 18.822 20.487 48.290 1.00 45.42 O HETATM 2349 O HOH A 115 -5.853 1.491 54.166 1.00 30.74 O HETATM 2350 O HOH A 116 -10.162 13.355 37.452 1.00 36.85 O HETATM 2351 O HOH A 117 -1.286 6.789 67.267 1.00 50.17 O HETATM 2352 O HOH A 118 0.165 5.137 62.587 1.00 37.64 O HETATM 2353 O HOH A 119 14.050 20.122 71.137 1.00 36.28 O HETATM 2354 O HOH A 120 19.714 21.971 65.582 1.00 32.00 O HETATM 2355 O HOH A 121 -10.686 -1.252 46.932 1.00 47.71 O HETATM 2356 O HOH A 122 15.779 0.555 55.237 1.00 32.39 O HETATM 2357 O HOH A 123 -14.381 19.536 43.548 1.00 34.73 O HETATM 2358 O HOH A 124 -2.957 -3.195 41.378 1.00 37.34 O HETATM 2359 O HOH A 125 21.228 1.204 44.239 1.00 45.83 O HETATM 2360 O HOH A 126 -19.122 -0.839 36.982 1.00 49.69 O HETATM 2361 O HOH A 127 -2.963 -3.257 48.813 1.00 33.65 O HETATM 2362 O HOH A 128 8.334 4.312 78.023 1.00 36.46 O HETATM 2363 O HOH A 129 4.578 13.855 41.280 1.00 47.74 O HETATM 2364 O HOH A 130 -25.815 6.853 59.521 1.00 44.88 O HETATM 2365 O HOH A 131 -32.589 16.651 47.338 1.00 34.12 O HETATM 2366 O HOH A 132 8.779 -11.869 52.263 1.00 28.07 O HETATM 2367 O HOH A 133 -4.420 15.100 40.554 1.00 23.06 O HETATM 2368 O HOH A 134 10.263 20.979 44.559 1.00 28.49 O HETATM 2369 O HOH A 135 -16.804 10.178 27.494 1.00177.77 O HETATM 2370 O HOH A 136 -25.757 12.946 55.392 1.00 35.66 O HETATM 2371 O HOH A 137 -6.867 2.014 40.811 1.00 33.79 O HETATM 2372 O HOH A 138 7.641 -10.007 54.129 1.00 27.34 O HETATM 2373 O HOH A 139 -5.658 13.404 38.845 1.00 31.75 O HETATM 2374 O HOH A 140 -6.736 29.002 48.121 1.00 31.85 O HETATM 2375 O HOH A 141 16.102 18.256 81.255 1.00 29.52 O HETATM 2376 O HOH A 142 1.794 23.217 74.661 1.00 40.39 O HETATM 2377 O HOH A 143 24.245 5.137 40.134 1.00 40.19 O HETATM 2378 O HOH A 144 -6.461 23.854 39.421 1.00 34.09 O HETATM 2379 O HOH A 145 15.883 12.372 39.465 1.00 35.69 O HETATM 2380 O HOH A 146 -4.329 18.089 58.227 1.00 35.56 O HETATM 2381 O HOH A 147 -15.956 9.920 58.076 1.00 38.72 O HETATM 2382 O HOH A 148 -14.916 19.550 39.778 1.00 58.22 O HETATM 2383 O HOH A 149 10.762 -9.917 52.343 1.00 35.12 O HETATM 2384 O HOH A 150 22.900 12.216 46.288 1.00 34.61 O HETATM 2385 O HOH A 151 6.412 8.344 82.095 1.00 51.62 O HETATM 2386 O HOH A 152 -9.526 7.011 50.142 1.00 31.74 O HETATM 2387 O HOH A 153 -24.596 10.622 31.148 1.00 37.28 O HETATM 2388 O HOH A 154 2.494 4.295 74.438 1.00 45.51 O HETATM 2389 O HOH A 155 5.905 28.306 58.051 1.00 26.73 O HETATM 2390 O HOH A 156 19.730 16.298 66.564 1.00 34.79 O HETATM 2391 O HOH A 157 20.571 23.159 67.864 1.00 42.07 O HETATM 2392 O HOH A 158 7.250 24.227 42.631 1.00 37.32 O HETATM 2393 O HOH A 159 -7.916 4.660 50.747 1.00 48.87 O HETATM 2394 O HOH A 160 -3.132 -2.572 38.890 1.00 38.90 O HETATM 2395 O HOH A 161 -3.769 -3.855 45.007 1.00 34.00 O HETATM 2396 O HOH A 162 8.756 27.778 47.196 1.00 35.89 O HETATM 2397 O HOH A 163 11.836 1.232 40.126 1.00 43.62 O HETATM 2398 O HOH A 164 5.122 4.581 40.105 1.00 43.94 O HETATM 2399 O HOH A 165 23.032 6.730 71.988 1.00 41.06 O HETATM 2400 O HOH A 166 -12.524 0.048 47.888 1.00 48.63 O HETATM 2401 O HOH A 167 12.018 -6.414 45.247 1.00 38.91 O HETATM 2402 O HOH A 168 -11.883 3.885 48.332 1.00 43.33 O HETATM 2403 O HOH A 169 13.040 12.195 40.224 1.00 40.26 O HETATM 2404 O HOH A 170 6.013 -3.348 62.004 1.00 46.64 O HETATM 2405 O HOH A 171 19.928 24.129 48.794 1.00 47.67 O HETATM 2406 O HOH A 172 -6.651 9.181 54.327 1.00 41.41 O HETATM 2407 O HOH A 173 20.292 15.370 53.828 1.00 39.33 O HETATM 2408 O HOH A 174 -13.380 2.599 37.475 1.00 43.72 O HETATM 2409 O HOH A 175 6.756 13.136 42.475 1.00 40.12 O HETATM 2410 O HOH A 176 -20.451 1.217 40.031 1.00 58.75 O HETATM 2411 O HOH A 177 12.975 24.853 66.833 1.00 36.96 O HETATM 2412 O HOH A 178 -21.475 17.200 67.440 1.00 40.65 O HETATM 2413 O HOH A 179 20.107 18.668 46.486 1.00 37.24 O HETATM 2414 O HOH A 180 -2.609 16.059 38.948 1.00 41.10 O HETATM 2415 O HOH A 181 5.743 30.095 60.096 1.00 34.68 O HETATM 2416 O HOH A 182 -23.985 6.774 37.847 1.00 60.50 O HETATM 2417 O HOH A 183 16.553 -4.999 45.611 1.00 57.66 O HETATM 2418 O HOH A 184 20.647 0.332 49.214 1.00 41.43 O HETATM 2419 O HOH A 185 -8.436 4.743 39.714 1.00 40.73 O HETATM 2420 O HOH A 186 1.762 4.058 71.868 1.00 38.63 O HETATM 2421 O HOH A 187 -24.954 2.949 43.727 1.00 38.67 O HETATM 2422 O HOH A 188 -12.887 13.532 30.990 1.00 44.27 O HETATM 2423 O HOH A 189 -26.912 12.503 48.556 1.00 47.67 O HETATM 2424 O HOH A 190 2.794 9.558 78.838 1.00 47.63 O HETATM 2425 O HOH A 191 -15.460 17.589 36.219 1.00 43.97 O HETATM 2426 O HOH A 192 -16.451 25.463 42.799 1.00 57.50 O HETATM 2427 O HOH A 193 9.898 -5.317 41.335 1.00 49.97 O HETATM 2428 O HOH A 194 -28.042 19.071 62.199 1.00 52.99 O HETATM 2429 O HOH A 195 -26.563 6.362 40.848 1.00 45.02 O HETATM 2430 O HOH A 196 -7.863 1.174 49.164 1.00 51.31 O HETATM 2431 O HOH A 197 16.570 22.864 46.329 1.00 47.70 O HETATM 2432 O HOH A 198 15.469 0.682 63.544 1.00 43.06 O HETATM 2433 O HOH A 199 18.358 0.500 68.060 1.00 45.95 O HETATM 2434 O HOH A 200 -12.948 4.378 50.239 1.00 39.40 O HETATM 2435 O HOH A 201 16.435 19.343 41.651 1.00 56.21 O HETATM 2436 O HOH A 202 -23.343 6.398 58.438 1.00 55.64 O HETATM 2437 O HOH A 203 27.884 3.959 46.238 1.00 40.75 O HETATM 2438 O HOH A 204 7.741 2.756 41.629 1.00 42.37 O HETATM 2439 O HOH A 205 12.163 30.760 68.142 1.00 47.61 O HETATM 2440 O HOH A 206 -2.016 3.564 61.700 1.00 37.42 O HETATM 2441 O HOH A 207 15.556 -0.661 52.319 1.00 40.27 O HETATM 2442 O HOH A 208 -25.142 12.989 65.487 1.00 41.17 O HETATM 2443 O HOH A 209 12.344 -6.591 57.849 1.00 57.55 O HETATM 2444 O HOH A 210 21.431 8.940 65.438 1.00 47.04 O HETATM 2445 O HOH A 211 -26.594 3.425 41.440 1.00 51.11 O HETATM 2446 O HOH A 212 7.985 31.038 61.445 1.00 40.69 O HETATM 2447 O HOH A 213 -12.299 12.458 28.402 1.00 44.57 O HETATM 2448 O HOH A 214 16.455 10.864 37.296 1.00 42.45 O HETATM 2449 O HOH A 215 19.374 -0.935 51.634 1.00 48.75 O HETATM 2450 O HOH A 216 -22.195 4.908 51.708 1.00 49.03 O HETATM 2451 O HOH A 217 9.719 -8.597 45.278 1.00 49.37 O HETATM 2452 O HOH A 218 -24.564 15.245 34.582 1.00 42.98 O HETATM 2453 O HOH A 219 -17.483 17.150 64.758 1.00 47.25 O HETATM 2454 O HOH A 220 -0.434 11.409 40.406 1.00 43.98 O HETATM 2455 O HOH A 221 24.397 10.792 48.474 1.00 38.31 O HETATM 2456 O HOH A 222 11.507 5.631 41.982 1.00 47.21 O HETATM 2457 O HOH A 223 16.856 25.487 55.384 1.00 61.57 O HETATM 2458 O HOH A 224 1.539 7.226 76.799 1.00 48.93 O HETATM 2459 O HOH A 225 25.275 -1.824 49.691 1.00 54.78 O HETATM 2460 O HOH A 226 9.560 27.239 55.964 1.00 44.81 O HETATM 2461 O HOH A 227 26.210 12.246 56.205 1.00 38.33 O HETATM 2462 O HOH A 228 13.460 -1.934 57.222 1.00 38.70 O HETATM 2463 O HOH A 229 -8.763 11.124 51.299 1.00 42.32 O HETATM 2464 O HOH A 230 19.247 22.895 54.938 1.00 53.25 O HETATM 2465 O HOH A 231 11.217 26.570 48.434 1.00 41.08 O HETATM 2466 O HOH A 232 -27.946 20.340 57.178 1.00 53.95 O HETATM 2467 O HOH A 233 -7.814 31.155 47.073 1.00 43.33 O HETATM 2468 O HOH A 234 -5.315 1.214 57.078 1.00 51.71 O HETATM 2469 O HOH A 235 2.137 3.649 63.524 1.00 40.57 O HETATM 2470 O HOH A 236 -28.166 14.745 42.709 1.00 42.00 O HETATM 2471 O HOH A 237 -10.650 10.370 53.082 1.00 51.40 O HETATM 2472 O HOH A 238 9.574 23.119 42.972 1.00 43.93 O HETATM 2473 O HOH A 239 9.678 19.568 76.005 1.00 45.78 O HETATM 2474 O HOH A 240 13.209 -0.014 64.887 1.00 54.75 O HETATM 2475 O HOH A 241 -27.200 18.915 42.299 1.00 47.31 O HETATM 2476 O HOH A 242 22.043 16.850 51.197 1.00 36.05 O HETATM 2477 O HOH A 243 -0.649 1.452 69.151 1.00 53.56 O HETATM 2478 O HOH A 244 -11.739 6.321 51.467 1.00 52.47 O HETATM 2479 O HOH A 245 11.192 -2.791 59.935 1.00 51.90 O HETATM 2480 O HOH A 246 -3.545 1.068 60.122 1.00 57.53 O HETATM 2481 O HOH A 247 -19.960 5.437 51.795 1.00 27.41 O HETATM 2482 O HOH A 248 -6.755 9.812 57.285 1.00 57.90 O HETATM 2483 O HOH A 249 -13.852 3.500 34.996 1.00 42.82 O HETATM 2484 O HOH A 250 -20.711 1.462 37.529 1.00 63.39 O HETATM 2485 O HOH A 251 2.650 -1.143 67.591 1.00 45.02 O HETATM 2486 O HOH A 252 -23.535 23.018 59.570 1.00 51.88 O HETATM 2487 O HOH A 253 16.941 0.036 44.345 1.00 30.82 O HETATM 2488 O HOH A 254 -18.897 17.073 66.999 1.00 53.65 O HETATM 2489 O HOH A 255 -6.736 -4.207 45.728 1.00 59.76 O HETATM 2490 O HOH A 256 1.285 0.140 69.110 1.00 71.07 O HETATM 2491 O HOH A 257 4.617 0.806 39.963 1.00 51.80 O HETATM 2492 O HOH A 258 -30.104 12.509 43.374 1.00 62.68 O HETATM 2493 O HOH A 259 -13.841 18.281 38.198 1.00 45.54 O HETATM 2494 O HOH A 260 10.486 8.126 41.241 1.00 46.14 O HETATM 2495 O HOH A 261 20.053 20.900 50.325 1.00 51.44 O HETATM 2496 O HOH A 262 -8.790 8.248 36.990 1.00 43.79 O HETATM 2497 O HOH A 263 -9.260 20.523 63.193 1.00 64.62 O HETATM 2498 O HOH A 264 -9.117 2.376 39.288 1.00 59.36 O MASTER 629 0 0 13 9 0 0 6 2497 1 0 29 END