HEADER SIGNALING PROTEIN, HYDROLASE 12-AUG-10 3OE8 TITLE CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A TITLE 2 SMALL MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: CXCR4 RESIDUES 2-229, LYSOZYME RESIDUES 1002-1161, CXCR4 COMPND 5 RESIDUES 230-319; COMPND 6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF- COMPND 7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN COMPND 8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, COMPND 9 ENDOLYSIN; COMPND 10 EC: 3.2.1.17; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 9606, 10665; SOURCE 4 GENE: CXCR4, CXCR4_HUMAN,E; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED KEYWDS 2 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G KEYWDS 3 PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE, KEYWDS 4 CANCER, HIV-1 CO-RECEPTOR, CHEMOTAXIS, CHEMOKINE, CXCL12, SDF1, KEYWDS 5 ISOTHIOUREA, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, KEYWDS 6 SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.WU,C.D.MOL,G.W.HAN,V.KATRITCH,E.Y.T.CHIEN,W.LIU,V.CHEREZOV, AUTHOR 2 R.C.STEVENS,ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE AUTHOR 3 (ATCG3D),GPCR NETWORK (GPCR) REVDAT 7 06-OCT-21 3OE8 1 REMARK SEQADV LINK REVDAT 6 13-JUN-18 3OE8 1 REMARK DBREF SEQADV REVDAT 5 26-JUL-17 3OE8 1 SOURCE REMARK REVDAT 4 02-MAY-12 3OE8 1 REMARK VERSN REVDAT 3 16-FEB-11 3OE8 1 HEADER REVDAT 2 05-JAN-11 3OE8 1 JRNL REVDAT 1 27-OCT-10 3OE8 0 JRNL AUTH B.WU,E.Y.CHIEN,C.D.MOL,G.FENALTI,W.LIU,V.KATRITCH,R.ABAGYAN, JRNL AUTH 2 A.BROOUN,P.WELLS,F.C.BI,D.J.HAMEL,P.KUHN,T.M.HANDEL, JRNL AUTH 3 V.CHEREZOV,R.C.STEVENS JRNL TITL STRUCTURES OF THE CXCR4 CHEMOKINE GPCR WITH SMALL-MOLECULE JRNL TITL 2 AND CYCLIC PEPTIDE ANTAGONISTS. JRNL REF SCIENCE V. 330 1066 2010 JRNL REFN ISSN 0036-8075 JRNL PMID 20929726 JRNL DOI 10.1126/SCIENCE.1194396 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 28647 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) : 0.253 REMARK 3 R VALUE (WORKING SET) : 0.250 REMARK 3 FREE R VALUE : 0.295 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 1441 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 14 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.22 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1954 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2584 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1871 REMARK 3 BIN R VALUE (WORKING SET) : 0.2558 REMARK 3 BIN FREE R VALUE : 0.3204 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.25 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 83 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10292 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 81 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 102.4 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 103.6 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.68450 REMARK 3 B22 (A**2) : 10.37890 REMARK 3 B33 (A**2) : -13.06340 REMARK 3 B12 (A**2) : -4.10050 REMARK 3 B13 (A**2) : -0.95230 REMARK 3 B23 (A**2) : 0.66120 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.838 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.854 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 10635 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 14450 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 3546 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 191 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1532 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 10545 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1410 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 12091 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.25 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.60 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|27 - A|229 } REMARK 3 ORIGIN FOR THE GROUP (A): -27.1542 1.6998 35.2206 REMARK 3 T TENSOR REMARK 3 T11: -0.2163 T22: -0.0339 REMARK 3 T33: -0.1883 T12: -0.0250 REMARK 3 T13: -0.0162 T23: 0.0751 REMARK 3 L TENSOR REMARK 3 L11: 2.7244 L22: 2.3650 REMARK 3 L33: 2.8683 L12: 0.1898 REMARK 3 L13: -0.9018 L23: -0.8128 REMARK 3 S TENSOR REMARK 3 S11: 0.0202 S12: 0.3570 S13: 0.3592 REMARK 3 S21: 0.2502 S22: 0.0887 S23: -0.0802 REMARK 3 S31: -0.1683 S32: -0.1644 S33: -0.1089 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|900 - A|901 } REMARK 3 ORIGIN FOR THE GROUP (A): -25.6706 -23.0882 68.2627 REMARK 3 T TENSOR REMARK 3 T11: 0.1129 T22: 0.0244 REMARK 3 T33: 0.0349 T12: 0.0310 REMARK 3 T13: -0.0106 T23: -0.0094 REMARK 3 L TENSOR REMARK 3 L11: 0.0242 L22: 0.0792 REMARK 3 L33: 0.0217 L12: -0.0276 REMARK 3 L13: -0.0036 L23: -0.0469 REMARK 3 S TENSOR REMARK 3 S11: -0.0013 S12: 0.0011 S13: 0.0033 REMARK 3 S21: -0.0007 S22: 0.0015 S23: -0.0034 REMARK 3 S31: -0.0019 S32: 0.0004 S33: -0.0003 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|1002 - A|1161 } REMARK 3 ORIGIN FOR THE GROUP (A): -16.3508 -18.8147 78.4237 REMARK 3 T TENSOR REMARK 3 T11: -0.0305 T22: 0.0520 REMARK 3 T33: -0.3362 T12: -0.0240 REMARK 3 T13: -0.1183 T23: 0.0277 REMARK 3 L TENSOR REMARK 3 L11: 3.5567 L22: 3.1571 REMARK 3 L33: 3.9214 L12: -1.3737 REMARK 3 L13: -1.0970 L23: 1.0632 REMARK 3 S TENSOR REMARK 3 S11: 0.0857 S12: 0.0031 S13: -0.0011 REMARK 3 S21: 0.0103 S22: -0.0253 S23: 0.0682 REMARK 3 S31: 0.0700 S32: -0.1052 S33: -0.0604 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { A|232 - A|305 } REMARK 3 ORIGIN FOR THE GROUP (A): -33.0890 -8.7081 31.7780 REMARK 3 T TENSOR REMARK 3 T11: -0.1402 T22: 0.2082 REMARK 3 T33: -0.2361 T12: -0.0808 REMARK 3 T13: -0.0474 T23: 0.0924 REMARK 3 L TENSOR REMARK 3 L11: 0.8254 L22: 2.5690 REMARK 3 L33: 2.5444 L12: 0.5971 REMARK 3 L13: 0.4843 L23: -0.2585 REMARK 3 S TENSOR REMARK 3 S11: 0.0388 S12: 0.1669 S13: -0.0763 REMARK 3 S21: 0.0711 S22: 0.0127 S23: 0.2861 REMARK 3 S31: -0.0167 S32: -0.1231 S33: -0.0515 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { B|27 - B|226 } REMARK 3 ORIGIN FOR THE GROUP (A): -66.4418 11.3855 33.3222 REMARK 3 T TENSOR REMARK 3 T11: -0.1584 T22: -0.1138 REMARK 3 T33: -0.1501 T12: -0.0178 REMARK 3 T13: 0.0916 T23: -0.0136 REMARK 3 L TENSOR REMARK 3 L11: 3.2433 L22: 1.4565 REMARK 3 L33: 5.6998 L12: 0.2012 REMARK 3 L13: 2.2949 L23: 0.4152 REMARK 3 S TENSOR REMARK 3 S11: -0.0651 S12: 0.0740 S13: -0.0540 REMARK 3 S21: 0.0867 S22: 0.0274 S23: 0.1679 REMARK 3 S31: -0.0486 S32: 0.0919 S33: 0.0377 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { B|1002 - B|1161 } REMARK 3 ORIGIN FOR THE GROUP (A): -45.5156 5.9077 79.2088 REMARK 3 T TENSOR REMARK 3 T11: -0.0330 T22: 0.1309 REMARK 3 T33: -0.2827 T12: 0.0274 REMARK 3 T13: 0.0013 T23: 0.1353 REMARK 3 L TENSOR REMARK 3 L11: 3.3042 L22: 2.4432 REMARK 3 L33: 2.7826 L12: 1.1038 REMARK 3 L13: 1.3717 L23: 0.8815 REMARK 3 S TENSOR REMARK 3 S11: 0.0005 S12: -0.3085 S13: 0.2501 REMARK 3 S21: 0.2325 S22: 0.1367 S23: -0.1800 REMARK 3 S31: -0.2166 S32: -0.3057 S33: -0.1372 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { B|1200 - B|1201 } REMARK 3 ORIGIN FOR THE GROUP (A): -53.8271 8.7772 62.3260 REMARK 3 T TENSOR REMARK 3 T11: 0.0217 T22: 0.0210 REMARK 3 T33: 0.0192 T12: 0.0018 REMARK 3 T13: -0.0146 T23: 0.0033 REMARK 3 L TENSOR REMARK 3 L11: 0.0333 L22: 0.0096 REMARK 3 L33: 0.0043 L12: -0.0172 REMARK 3 L13: 0.0156 L23: 0.0007 REMARK 3 S TENSOR REMARK 3 S11: -0.0002 S12: 0.0004 S13: -0.0021 REMARK 3 S21: 0.0026 S22: 0.0010 S23: 0.0007 REMARK 3 S31: 0.0010 S32: -0.0015 S33: -0.0008 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { B|230 - B|304 } REMARK 3 ORIGIN FOR THE GROUP (A): -56.5048 3.4250 32.0329 REMARK 3 T TENSOR REMARK 3 T11: -0.1229 T22: 0.0231 REMARK 3 T33: -0.1076 T12: 0.0958 REMARK 3 T13: 0.0012 T23: -0.0714 REMARK 3 L TENSOR REMARK 3 L11: 2.6490 L22: 1.3804 REMARK 3 L33: 3.3552 L12: -0.7468 REMARK 3 L13: 2.7982 L23: 0.2774 REMARK 3 S TENSOR REMARK 3 S11: 0.0082 S12: 0.1536 S13: -0.2049 REMARK 3 S21: 0.0997 S22: -0.0363 S23: 0.0215 REMARK 3 S31: 0.1160 S32: 0.0666 S33: 0.0281 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: { C|27 - C|227 } REMARK 3 ORIGIN FOR THE GROUP (A): -44.0917 38.4251 35.8887 REMARK 3 T TENSOR REMARK 3 T11: 0.0751 T22: -0.0266 REMARK 3 T33: -0.3247 T12: -0.0846 REMARK 3 T13: -0.0136 T23: -0.0334 REMARK 3 L TENSOR REMARK 3 L11: 2.3582 L22: 2.3521 REMARK 3 L33: 2.5424 L12: -0.0202 REMARK 3 L13: -0.1243 L23: 0.4788 REMARK 3 S TENSOR REMARK 3 S11: -0.1420 S12: 0.1478 S13: -0.1373 REMARK 3 S21: 0.2674 S22: 0.0842 S23: -0.2651 REMARK 3 S31: 0.3499 S32: 0.1778 S33: 0.0579 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: { C|1002 - C|1161 } REMARK 3 ORIGIN FOR THE GROUP (A): -67.2350 38.2804 82.7051 REMARK 3 T TENSOR REMARK 3 T11: 0.0274 T22: 0.1349 REMARK 3 T33: -0.3446 T12: 0.0845 REMARK 3 T13: -0.0790 T23: -0.0113 REMARK 3 L TENSOR REMARK 3 L11: 3.5721 L22: 2.8985 REMARK 3 L33: 2.6219 L12: 1.1157 REMARK 3 L13: 1.0930 L23: 0.0006 REMARK 3 S TENSOR REMARK 3 S11: 0.0168 S12: -0.1513 S13: -0.2523 REMARK 3 S21: 0.0510 S22: -0.0636 S23: 0.1092 REMARK 3 S31: 0.1179 S32: 0.1816 S33: 0.0469 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: { C|1200 - C|1201 } REMARK 3 ORIGIN FOR THE GROUP (A): -55.4766 45.8414 69.5709 REMARK 3 T TENSOR REMARK 3 T11: -0.0006 T22: 0.0094 REMARK 3 T33: 0.0172 T12: 0.0113 REMARK 3 T13: -0.0016 T23: -0.0083 REMARK 3 L TENSOR REMARK 3 L11: 0.0100 L22: 0.0172 REMARK 3 L33: -0.0018 L12: 0.0134 REMARK 3 L13: -0.0247 L23: 0.0189 REMARK 3 S TENSOR REMARK 3 S11: 0.0001 S12: 0.0017 S13: -0.0005 REMARK 3 S21: -0.0020 S22: 0.0022 S23: -0.0040 REMARK 3 S31: 0.0005 S32: 0.0010 S33: -0.0023 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: { C|230 - C|305 } REMARK 3 ORIGIN FOR THE GROUP (A): -55.0013 45.5716 33.9298 REMARK 3 T TENSOR REMARK 3 T11: 0.1383 T22: 0.0022 REMARK 3 T33: -0.3215 T12: -0.1271 REMARK 3 T13: 0.0051 T23: -0.0488 REMARK 3 L TENSOR REMARK 3 L11: 1.8993 L22: 2.2347 REMARK 3 L33: 1.7421 L12: 1.1578 REMARK 3 L13: -1.7420 L23: -2.7984 REMARK 3 S TENSOR REMARK 3 S11: -0.1496 S12: 0.2402 S13: 0.1150 REMARK 3 S21: 0.2885 S22: 0.1892 S23: -0.0232 REMARK 3 S31: 0.0477 S32: -0.0628 S33: -0.0396 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3OE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-10. REMARK 100 THE DEPOSITION ID IS D_1000061004. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 11 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28801 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.3 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 59.3 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.51000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN REMARK 280 AND CHOLESTEROL, 26% PEG400, 0.3M SODIUM MALONATE, 5MM STRONTIUM REMARK 280 CHLORIDE, 0.1M MES PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 46550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 67690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 ILE A 6 REMARK 465 TYR A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ASP A 10 REMARK 465 ASN A 11 REMARK 465 TYR A 12 REMARK 465 THR A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 465 MET A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 GLY A 19 REMARK 465 ASP A 20 REMARK 465 TYR A 21 REMARK 465 ASP A 22 REMARK 465 SER A 23 REMARK 465 MET A 24 REMARK 465 LYS A 25 REMARK 465 GLU A 26 REMARK 465 PHE A 29 REMARK 465 ARG A 30 REMARK 465 GLU A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 33 REMARK 465 ALA A 34 REMARK 465 GLY A 1200 REMARK 465 SER A 1201 REMARK 465 LYS A 230 REMARK 465 GLY A 231 REMARK 465 GLY A 306 REMARK 465 ALA A 307 REMARK 465 LYS A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 THR A 311 REMARK 465 SER A 312 REMARK 465 ALA A 313 REMARK 465 GLN A 314 REMARK 465 HIS A 315 REMARK 465 ALA A 316 REMARK 465 LEU A 317 REMARK 465 THR A 318 REMARK 465 SER A 319 REMARK 465 GLY A 320 REMARK 465 ARG A 321 REMARK 465 PRO A 322 REMARK 465 LEU A 323 REMARK 465 GLU A 324 REMARK 465 VAL A 325 REMARK 465 LEU A 326 REMARK 465 PHE A 327 REMARK 465 GLN A 328 REMARK 465 ASP B -9 REMARK 465 TYR B -8 REMARK 465 LYS B -7 REMARK 465 ASP B -6 REMARK 465 ASP B -5 REMARK 465 ASP B -4 REMARK 465 ASP B -3 REMARK 465 ALA B -2 REMARK 465 GLY B -1 REMARK 465 ALA B 0 REMARK 465 PRO B 1 REMARK 465 GLU B 2 REMARK 465 GLY B 3 REMARK 465 ILE B 4 REMARK 465 SER B 5 REMARK 465 ILE B 6 REMARK 465 TYR B 7 REMARK 465 THR B 8 REMARK 465 SER B 9 REMARK 465 ASP B 10 REMARK 465 ASN B 11 REMARK 465 TYR B 12 REMARK 465 THR B 13 REMARK 465 GLU B 14 REMARK 465 GLU B 15 REMARK 465 MET B 16 REMARK 465 GLY B 17 REMARK 465 SER B 18 REMARK 465 GLY B 19 REMARK 465 ASP B 20 REMARK 465 TYR B 21 REMARK 465 ASP B 22 REMARK 465 SER B 23 REMARK 465 MET B 24 REMARK 465 LYS B 25 REMARK 465 GLU B 26 REMARK 465 ARG B 30 REMARK 465 GLU B 31 REMARK 465 GLU B 32 REMARK 465 THR B 142 REMARK 465 ASN B 143 REMARK 465 SER B 144 REMARK 465 SER B 227 REMARK 465 HIS B 228 REMARK 465 SER B 229 REMARK 465 GLY B 900 REMARK 465 SER B 901 REMARK 465 LEU B 267 REMARK 465 GLU B 268 REMARK 465 ILE B 269 REMARK 465 ILE B 270 REMARK 465 LYS B 271 REMARK 465 LEU B 305 REMARK 465 GLY B 306 REMARK 465 ALA B 307 REMARK 465 LYS B 308 REMARK 465 PHE B 309 REMARK 465 LYS B 310 REMARK 465 THR B 311 REMARK 465 SER B 312 REMARK 465 ALA B 313 REMARK 465 GLN B 314 REMARK 465 HIS B 315 REMARK 465 ALA B 316 REMARK 465 LEU B 317 REMARK 465 THR B 318 REMARK 465 SER B 319 REMARK 465 GLY B 320 REMARK 465 ARG B 321 REMARK 465 PRO B 322 REMARK 465 LEU B 323 REMARK 465 GLU B 324 REMARK 465 VAL B 325 REMARK 465 LEU B 326 REMARK 465 PHE B 327 REMARK 465 GLN B 328 REMARK 465 ASP C -9 REMARK 465 TYR C -8 REMARK 465 LYS C -7 REMARK 465 ASP C -6 REMARK 465 ASP C -5 REMARK 465 ASP C -4 REMARK 465 ASP C -3 REMARK 465 ALA C -2 REMARK 465 GLY C -1 REMARK 465 ALA C 0 REMARK 465 PRO C 1 REMARK 465 GLU C 2 REMARK 465 GLY C 3 REMARK 465 ILE C 4 REMARK 465 SER C 5 REMARK 465 ILE C 6 REMARK 465 TYR C 7 REMARK 465 THR C 8 REMARK 465 SER C 9 REMARK 465 ASP C 10 REMARK 465 ASN C 11 REMARK 465 TYR C 12 REMARK 465 THR C 13 REMARK 465 GLU C 14 REMARK 465 GLU C 15 REMARK 465 MET C 16 REMARK 465 GLY C 17 REMARK 465 SER C 18 REMARK 465 GLY C 19 REMARK 465 ASP C 20 REMARK 465 TYR C 21 REMARK 465 ASP C 22 REMARK 465 SER C 23 REMARK 465 MET C 24 REMARK 465 LYS C 25 REMARK 465 GLU C 26 REMARK 465 ARG C 30 REMARK 465 GLU C 31 REMARK 465 GLU C 32 REMARK 465 ASN C 33 REMARK 465 ALA C 34 REMARK 465 ASN C 35 REMARK 465 THR C 142 REMARK 465 ASN C 143 REMARK 465 SER C 144 REMARK 465 ASP C 181 REMARK 465 ASP C 182 REMARK 465 HIS C 228 REMARK 465 SER C 229 REMARK 465 GLY C 900 REMARK 465 SER C 901 REMARK 465 GLY C 306 REMARK 465 ALA C 307 REMARK 465 LYS C 308 REMARK 465 PHE C 309 REMARK 465 LYS C 310 REMARK 465 THR C 311 REMARK 465 SER C 312 REMARK 465 ALA C 313 REMARK 465 GLN C 314 REMARK 465 HIS C 315 REMARK 465 ALA C 316 REMARK 465 LEU C 317 REMARK 465 THR C 318 REMARK 465 SER C 319 REMARK 465 GLY C 320 REMARK 465 ARG C 321 REMARK 465 PRO C 322 REMARK 465 LEU C 323 REMARK 465 GLU C 324 REMARK 465 VAL C 325 REMARK 465 LEU C 326 REMARK 465 PHE C 327 REMARK 465 GLN C 328 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LEU A 69 CG CD1 CD2 REMARK 470 VAL A 99 CG1 CG2 REMARK 470 ASP A 182 CG OD1 OD2 REMARK 470 ARG A 183 CD NE CZ NH1 NH2 REMARK 470 ILE A1003 CG1 CG2 CD1 REMARK 470 ILE A1009 CG1 CG2 CD1 REMARK 470 LYS A 234 CG CD CE NZ REMARK 470 LEU A 267 CG CD1 CD2 REMARK 470 LYS A 271 CG CD CE NZ REMARK 470 ASN B 33 CG OD1 ND2 REMARK 470 ASP B1020 CG OD1 OD2 REMARK 470 TYR B1025 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B1065 CD CE NZ REMARK 470 LYS B 234 CG CD CE NZ REMARK 470 ILE B 257 CG1 CG2 CD1 REMARK 470 SER B 260 OG REMARK 470 SER B 263 OG REMARK 470 GLU B 277 CG CD OE1 OE2 REMARK 470 LYS C 68 CG CD CE NZ REMARK 470 ARG C 70 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 145 CG CD OE1 NE2 REMARK 470 SER C1201 OG REMARK 470 LYS C 230 CG CD CE NZ REMARK 470 LYS C 234 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLY C1200 CA GLY C1200 C -0.102 REMARK 500 SER C1201 CA SER C1201 C -0.208 REMARK 500 SER C1201 C SER C1201 O 0.190 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 VAL A 99 CB - CA - C ANGL. DEV. = -15.7 DEGREES REMARK 500 ALA A 100 CB - CA - C ANGL. DEV. = -14.7 DEGREES REMARK 500 ALA A 100 N - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 ASN A 101 N - CA - CB ANGL. DEV. = -13.3 DEGREES REMARK 500 ALA A 137 CB - CA - C ANGL. DEV. = 13.6 DEGREES REMARK 500 VAL A 139 CB - CA - C ANGL. DEV. = 13.8 DEGREES REMARK 500 HIS A 140 N - CA - CB ANGL. DEV. = -15.1 DEGREES REMARK 500 ALA A 141 CB - CA - C ANGL. DEV. = -10.1 DEGREES REMARK 500 ILE A 173 CB - CA - C ANGL. DEV. = -18.9 DEGREES REMARK 500 ILE A 173 N - CA - C ANGL. DEV. = 16.8 DEGREES REMARK 500 ASP A 182 CB - CA - C ANGL. DEV. = -13.5 DEGREES REMARK 500 ARG A 183 N - CA - CB ANGL. DEV. = 13.0 DEGREES REMARK 500 SER A 229 CA - C - N ANGL. DEV. = 19.4 DEGREES REMARK 500 SER A 229 O - C - N ANGL. DEV. = -20.6 DEGREES REMARK 500 GLY A 900 C - N - CA ANGL. DEV. = 13.8 DEGREES REMARK 500 GLY A 900 N - CA - C ANGL. DEV. = 28.6 DEGREES REMARK 500 GLU A1005 CB - CA - C ANGL. DEV. = -19.6 DEGREES REMARK 500 MET A1006 N - CA - C ANGL. DEV. = -20.8 DEGREES REMARK 500 THR A1115 N - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 HIS A 232 N - CA - CB ANGL. DEV. = -22.8 DEGREES REMARK 500 HIS A 232 N - CA - C ANGL. DEV. = 30.0 DEGREES REMARK 500 LEU A 266 CB - CA - C ANGL. DEV. = -13.8 DEGREES REMARK 500 LEU B 208 N - CA - C ANGL. DEV. = 19.0 DEGREES REMARK 500 SER B1201 CB - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 SER B1201 N - CA - C ANGL. DEV. = 37.7 DEGREES REMARK 500 GLY B 231 N - CA - C ANGL. DEV. = -19.8 DEGREES REMARK 500 ILE B 257 CB - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 ILE B 259 CB - CA - C ANGL. DEV. = -12.4 DEGREES REMARK 500 SER B 260 CB - CA - C ANGL. DEV. = -14.8 DEGREES REMARK 500 ILE B 261 CB - CA - C ANGL. DEV. = -15.1 DEGREES REMARK 500 ALA C 100 CB - CA - C ANGL. DEV. = -14.7 DEGREES REMARK 500 ALA C 100 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 ASN C 101 N - CA - CB ANGL. DEV. = -20.8 DEGREES REMARK 500 GLY C1023 N - CA - C ANGL. DEV. = 27.4 DEGREES REMARK 500 SER C1201 C - N - CA ANGL. DEV. = 25.3 DEGREES REMARK 500 SER C1201 CB - CA - C ANGL. DEV. = -25.6 DEGREES REMARK 500 SER C1201 N - CA - C ANGL. DEV. = 35.5 DEGREES REMARK 500 SER C1201 CA - C - O ANGL. DEV. = -14.9 DEGREES REMARK 500 SER C1201 O - C - N ANGL. DEV. = -19.3 DEGREES REMARK 500 LYS C 230 C - N - CA ANGL. DEV. = 25.3 DEGREES REMARK 500 GLU C 268 N - CA - C ANGL. DEV. = 22.4 DEGREES REMARK 500 ILE C 269 N - CA - C ANGL. DEV. = 23.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 181 86.20 -66.45 REMARK 500 ASP A 182 9.03 96.26 REMARK 500 HIS A 228 40.95 -92.41 REMARK 500 SER A 229 -151.66 -129.65 REMARK 500 SER A 901 -2.82 -147.32 REMARK 500 ASN A1002 4.35 55.56 REMARK 500 CYS A 274 -37.60 -31.41 REMARK 500 SER C1201 42.18 -86.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY C 1200 SER C 1201 125.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLY C1200 11.51 REMARK 500 SER C1201 -42.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD A 1500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD B 1500 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD C 1500 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATCG3D_11 RELATED DB: TARGETDB REMARK 900 RELATED ID: 3ODU RELATED DB: PDB REMARK 900 SAME PROTEIN AT 2.5 A IN P21 SPACEGROUP REMARK 900 RELATED ID: 3OE0 RELATED DB: PDB REMARK 900 SAME PROTEIN IN COMPLEX WITH A CYCLIC PEPTIDE CVX15 REMARK 900 RELATED ID: 3OE6 RELATED DB: PDB REMARK 900 SAME PROTEIN IN I222 SPACEGROUP REMARK 900 RELATED ID: 3OE9 RELATED DB: PDB REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 2 MOLECULES PER ASYMMETRIC UNIT REMARK 900 RELATED ID: GPCR-34 RELATED DB: TARGETTRACK REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4 REMARK 999 LYSOZYME INSERTED BETWEEN SER229 AND LYS230 OF CXCR4, AS INDICATED REMARK 999 AS CXCR4-2 IN THE PUBLICATION. DBREF 3OE8 A 2 229 UNP P61073 CXCR4_HUMAN 2 229 DBREF 3OE8 A 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 3OE8 A 230 319 UNP P61073 CXCR4_HUMAN 230 319 DBREF 3OE8 B 2 229 UNP P61073 CXCR4_HUMAN 2 229 DBREF 3OE8 B 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 3OE8 B 230 319 UNP P61073 CXCR4_HUMAN 230 319 DBREF 3OE8 C 2 229 UNP P61073 CXCR4_HUMAN 2 229 DBREF 3OE8 C 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 3OE8 C 230 319 UNP P61073 CXCR4_HUMAN 230 319 SEQADV 3OE8 ASP A -9 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TYR A -8 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LYS A -7 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP A -6 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP A -5 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP A -4 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP A -3 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA A -2 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLY A -1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA A 0 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO A 1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TRP A 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 3OE8 GLY A 900 UNP P61073 LINKER SEQADV 3OE8 SER A 901 UNP P61073 LINKER SEQADV 3OE8 GLY A 1200 UNP P61073 LINKER SEQADV 3OE8 SER A 1201 UNP P61073 LINKER SEQADV 3OE8 THR A 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 3OE8 ALA A 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 3OE8 GLY A 320 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ARG A 321 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO A 322 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU A 323 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLU A 324 UNP P61073 EXPRESSION TAG SEQADV 3OE8 VAL A 325 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU A 326 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PHE A 327 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLN A 328 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP B -9 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TYR B -8 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LYS B -7 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP B -6 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP B -5 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP B -4 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP B -3 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA B -2 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLY B -1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA B 0 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO B 1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TRP B 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 3OE8 GLY B 900 UNP P61073 LINKER SEQADV 3OE8 SER B 901 UNP P61073 LINKER SEQADV 3OE8 GLY B 1200 UNP P61073 LINKER SEQADV 3OE8 SER B 1201 UNP P61073 LINKER SEQADV 3OE8 THR B 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 3OE8 ALA B 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 3OE8 GLY B 320 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ARG B 321 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO B 322 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU B 323 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLU B 324 UNP P61073 EXPRESSION TAG SEQADV 3OE8 VAL B 325 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU B 326 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PHE B 327 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLN B 328 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP C -9 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TYR C -8 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LYS C -7 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP C -6 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP C -5 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP C -4 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ASP C -3 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA C -2 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLY C -1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ALA C 0 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO C 1 UNP P61073 EXPRESSION TAG SEQADV 3OE8 TRP C 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 3OE8 GLY C 900 UNP P61073 LINKER SEQADV 3OE8 SER C 901 UNP P61073 LINKER SEQADV 3OE8 GLY C 1200 UNP P61073 LINKER SEQADV 3OE8 SER C 1201 UNP P61073 LINKER SEQADV 3OE8 THR C 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 3OE8 ALA C 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 3OE8 GLY C 320 UNP P61073 EXPRESSION TAG SEQADV 3OE8 ARG C 321 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PRO C 322 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU C 323 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLU C 324 UNP P61073 EXPRESSION TAG SEQADV 3OE8 VAL C 325 UNP P61073 EXPRESSION TAG SEQADV 3OE8 LEU C 326 UNP P61073 EXPRESSION TAG SEQADV 3OE8 PHE C 327 UNP P61073 EXPRESSION TAG SEQADV 3OE8 GLN C 328 UNP P61073 EXPRESSION TAG SEQRES 1 A 502 ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY SEQRES 2 A 502 ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET SEQRES 3 A 502 GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE SEQRES 4 A 502 ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO SEQRES 5 A 502 THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY SEQRES 6 A 502 ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS SEQRES 7 A 502 LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER SEQRES 8 A 502 VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP SEQRES 9 A 502 ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE SEQRES 10 A 502 LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU SEQRES 11 A 502 TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP SEQRES 12 A 502 ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG SEQRES 13 A 502 PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY SEQRES 14 A 502 VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE SEQRES 15 A 502 ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE SEQRES 16 A 502 CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL SEQRES 17 A 502 PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO SEQRES 18 A 502 GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER SEQRES 19 A 502 LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU SEQRES 20 A 502 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 21 A 502 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 22 A 502 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 23 A 502 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 24 A 502 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 25 A 502 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 26 A 502 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 27 A 502 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 28 A 502 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 29 A 502 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 30 A 502 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 31 A 502 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER SEQRES 32 A 502 LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL SEQRES 33 A 502 ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR SEQRES 34 A 502 TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU SEQRES 35 A 502 ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS SEQRES 36 A 502 LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS SEQRES 37 A 502 CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA SEQRES 38 A 502 LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY SEQRES 39 A 502 ARG PRO LEU GLU VAL LEU PHE GLN SEQRES 1 B 502 ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY SEQRES 2 B 502 ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET SEQRES 3 B 502 GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE SEQRES 4 B 502 ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO SEQRES 5 B 502 THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY SEQRES 6 B 502 ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS SEQRES 7 B 502 LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER SEQRES 8 B 502 VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP SEQRES 9 B 502 ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE SEQRES 10 B 502 LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU SEQRES 11 B 502 TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP SEQRES 12 B 502 ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG SEQRES 13 B 502 PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY SEQRES 14 B 502 VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE SEQRES 15 B 502 ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE SEQRES 16 B 502 CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL SEQRES 17 B 502 PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO SEQRES 18 B 502 GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER SEQRES 19 B 502 LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU SEQRES 20 B 502 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 21 B 502 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 22 B 502 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 23 B 502 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 24 B 502 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 25 B 502 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 26 B 502 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 27 B 502 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 28 B 502 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 29 B 502 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 30 B 502 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 31 B 502 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER SEQRES 32 B 502 LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL SEQRES 33 B 502 ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR SEQRES 34 B 502 TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU SEQRES 35 B 502 ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS SEQRES 36 B 502 LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS SEQRES 37 B 502 CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA SEQRES 38 B 502 LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY SEQRES 39 B 502 ARG PRO LEU GLU VAL LEU PHE GLN SEQRES 1 C 502 ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY SEQRES 2 C 502 ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET SEQRES 3 C 502 GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE SEQRES 4 C 502 ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO SEQRES 5 C 502 THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY SEQRES 6 C 502 ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS SEQRES 7 C 502 LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER SEQRES 8 C 502 VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP SEQRES 9 C 502 ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE SEQRES 10 C 502 LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU SEQRES 11 C 502 TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP SEQRES 12 C 502 ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG SEQRES 13 C 502 PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY SEQRES 14 C 502 VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE SEQRES 15 C 502 ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE SEQRES 16 C 502 CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL SEQRES 17 C 502 PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO SEQRES 18 C 502 GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER SEQRES 19 C 502 LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU SEQRES 20 C 502 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 21 C 502 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 22 C 502 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 23 C 502 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 24 C 502 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 25 C 502 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 26 C 502 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 27 C 502 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 28 C 502 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 29 C 502 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 30 C 502 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 31 C 502 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER SEQRES 32 C 502 LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL SEQRES 33 C 502 ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR SEQRES 34 C 502 TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU SEQRES 35 C 502 ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS SEQRES 36 C 502 LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS SEQRES 37 C 502 CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA SEQRES 38 C 502 LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY SEQRES 39 C 502 ARG PRO LEU GLU VAL LEU PHE GLN HET ITD A1500 27 HET ITD B1500 27 HET ITD C1500 27 HETNAM ITD (6,6-DIMETHYL-5,6-DIHYDROIMIDAZO[2,1-B][1,3]THIAZOL-3- HETNAM 2 ITD YL)METHYL N,N'-DICYCLOHEXYLIMIDOTHIOCARBAMATE FORMUL 4 ITD 3(C21 H34 N4 S2) HELIX 1 1 PHE A 36 GLN A 66 1 31 HELIX 2 2 SER A 71 ILE A 89 1 19 HELIX 3 3 THR A 90 ALA A 100 1 11 HELIX 4 4 GLY A 105 HIS A 140 1 36 HELIX 5 5 SER A 144 LYS A 154 1 11 HELIX 6 6 LYS A 154 VAL A 160 1 7 HELIX 7 7 VAL A 160 LEU A 167 1 8 HELIX 8 8 THR A 168 PHE A 174 1 7 HELIX 9 9 ASN A 192 LEU A 208 1 17 HELIX 10 10 LEU A 208 LEU A 226 1 19 HELIX 11 11 ILE A 1003 GLU A 1011 1 9 HELIX 12 12 SER A 1038 GLY A 1051 1 14 HELIX 13 13 THR A 1059 LEU A 1079 1 21 HELIX 14 14 LEU A 1084 SER A 1090 1 7 HELIX 15 15 ASP A 1092 MET A 1106 1 15 HELIX 16 16 GLY A 1107 ALA A 1112 1 6 HELIX 17 17 THR A 1115 GLN A 1123 1 9 HELIX 18 18 ARG A 1125 LYS A 1135 1 11 HELIX 19 19 SER A 1136 THR A 1142 1 7 HELIX 20 20 THR A 1142 GLY A 1156 1 15 HELIX 21 21 GLN A 233 GLU A 268 1 36 HELIX 22 22 GLY A 273 PHE A 292 1 20 HELIX 23 23 PHE A 293 LEU A 305 1 13 HELIX 24 24 PHE B 36 MET B 63 1 28 HELIX 25 25 SER B 71 ILE B 89 1 19 HELIX 26 26 THR B 90 ALA B 100 1 11 HELIX 27 27 PHE B 104 VAL B 139 1 36 HELIX 28 28 PRO B 147 LYS B 154 1 8 HELIX 29 29 LYS B 154 VAL B 160 1 7 HELIX 30 30 VAL B 160 LEU B 167 1 8 HELIX 31 31 THR B 168 PHE B 174 1 7 HELIX 32 32 ASN B 192 LEU B 208 1 17 HELIX 33 33 LEU B 208 LEU B 226 1 19 HELIX 34 34 ASN B 1002 GLU B 1011 1 10 HELIX 35 35 LEU B 1039 GLY B 1051 1 13 HELIX 36 36 THR B 1059 ASN B 1081 1 23 HELIX 37 37 LEU B 1084 LEU B 1091 1 8 HELIX 38 38 ASP B 1092 GLY B 1107 1 16 HELIX 39 39 GLY B 1107 GLY B 1113 1 7 HELIX 40 40 PHE B 1114 GLN B 1123 1 10 HELIX 41 41 ARG B 1125 SER B 1136 1 12 HELIX 42 42 SER B 1136 THR B 1142 1 7 HELIX 43 43 THR B 1142 GLY B 1156 1 15 HELIX 44 44 HIS B 232 SER B 263 1 32 HELIX 45 45 GLY B 273 PHE B 292 1 20 HELIX 46 46 PHE B 293 CYS B 295 5 3 HELIX 47 47 CYS B 296 ALA B 303 1 8 HELIX 48 48 PHE C 36 GLY C 64 1 29 HELIX 49 49 SER C 71 ILE C 89 1 19 HELIX 50 50 THR C 90 ALA C 100 1 11 HELIX 51 51 PHE C 104 VAL C 139 1 36 HELIX 52 52 ARG C 146 LYS C 154 1 9 HELIX 53 53 LYS C 154 VAL C 160 1 7 HELIX 54 54 VAL C 160 LEU C 167 1 8 HELIX 55 55 THR C 168 PHE C 174 1 7 HELIX 56 56 ASN C 192 LEU C 208 1 17 HELIX 57 57 LEU C 208 LYS C 225 1 18 HELIX 58 58 ASN C 1002 GLU C 1011 1 10 HELIX 59 59 ALA C 1041 GLY C 1051 1 11 HELIX 60 60 THR C 1059 ASN C 1081 1 23 HELIX 61 61 LYS C 1083 LEU C 1091 1 9 HELIX 62 62 ASP C 1092 MET C 1106 1 15 HELIX 63 63 GLY C 1107 ALA C 1112 1 6 HELIX 64 64 PHE C 1114 GLN C 1123 1 10 HELIX 65 65 ARG C 1125 LYS C 1135 1 11 HELIX 66 66 SER C 1136 THR C 1142 1 7 HELIX 67 67 THR C 1142 GLY C 1156 1 15 HELIX 68 68 THR C 1157 TYR C 1161 5 5 HELIX 69 69 HIS C 232 LEU C 267 1 36 HELIX 70 70 GLY C 273 PHE C 292 1 20 HELIX 71 71 PHE C 293 LEU C 305 1 13 SHEET 1 A 2 ALA A 175 ALA A 180 0 SHEET 2 A 2 ARG A 183 ARG A 188 -1 O ILE A 185 N SER A 178 SHEET 1 B 3 ARG A1014 LYS A1019 0 SHEET 2 B 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 B 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SHEET 1 C 2 ALA B 175 GLU B 179 0 SHEET 2 C 2 TYR B 184 ARG B 188 -1 O ILE B 185 N SER B 178 SHEET 1 D 3 ARG B1014 LYS B1019 0 SHEET 2 D 3 TYR B1025 GLY B1028 -1 O THR B1026 N TYR B1018 SHEET 3 D 3 HIS B1031 LEU B1032 -1 O HIS B1031 N ILE B1027 SHEET 1 E 2 ALA C 175 SER C 178 0 SHEET 2 E 2 ILE C 185 ARG C 188 -1 O ILE C 185 N SER C 178 SHEET 1 F 3 TYR C1018 LYS C1019 0 SHEET 2 F 3 TYR C1025 ILE C1027 -1 O THR C1026 N TYR C1018 SHEET 3 F 3 HIS C1031 LEU C1032 -1 O HIS C1031 N ILE C1027 SSBOND 1 CYS A 28 CYS A 274 1555 1555 1.98 SSBOND 2 CYS A 109 CYS A 186 1555 1555 2.03 SSBOND 3 CYS B 28 CYS B 274 1555 1555 2.04 SSBOND 4 CYS B 109 CYS B 186 1555 1555 2.04 SSBOND 5 CYS C 28 CYS C 274 1555 1555 2.04 SSBOND 6 CYS C 109 CYS C 186 1555 1555 2.03 LINK C SER A 229 N GLY A 900 1555 1555 1.28 LINK C SER A 901 N ASN A1002 1555 1555 1.33 LINK N LYS B 230 C SER B1201 1555 1555 1.33 LINK C TYR B1161 N GLY B1200 1555 1555 1.38 LINK N LYS C 230 C SER C1201 1555 1555 1.40 LINK C TYR C1161 N GLY C1200 1555 1555 1.31 SITE 1 AC1 8 TRP A 94 ASP A 97 TRP A 102 VAL A 112 SITE 2 AC1 8 TYR A 116 CYS A 186 ASP A 187 GLU A 288 SITE 1 AC2 9 TRP B 94 ASP B 97 TYR B 116 ARG B 183 SITE 2 AC2 9 ILE B 185 CYS B 186 ASP B 187 ARG B 188 SITE 3 AC2 9 GLU B 288 SITE 1 AC3 7 TRP C 94 ASP C 97 TYR C 116 ARG C 183 SITE 2 AC3 7 CYS C 186 ASP C 187 GLU C 288 CRYST1 69.369 76.602 91.719 96.00 97.78 97.38 P 1 3 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014416 0.001867 0.002218 0.00000 SCALE2 0.000000 0.013164 0.001646 0.00000 SCALE3 0.000000 0.000000 0.011090 0.00000 ATOM 1 N PRO A 27 -25.974 -7.973 4.062 1.00127.64 N ANISOU 1 N PRO A 27 15707 23199 9592 -2134 729 -426 N ATOM 2 CA PRO A 27 -27.054 -7.090 3.590 1.00128.42 C ANISOU 2 CA PRO A 27 15629 23694 9471 -2211 476 -124 C ATOM 3 C PRO A 27 -28.318 -7.215 4.442 1.00130.42 C ANISOU 3 C PRO A 27 15768 23898 9889 -2321 212 -116 C ATOM 4 O PRO A 27 -28.633 -6.283 5.186 1.00127.66 O ANISOU 4 O PRO A 27 15213 23463 9831 -2189 107 197 O ATOM 5 CB PRO A 27 -27.256 -7.519 2.130 1.00134.75 C ANISOU 5 CB PRO A 27 16579 24928 9694 -2395 481 -277 C ATOM 6 CG PRO A 27 -25.953 -8.158 1.737 1.00140.45 C ANISOU 6 CG PRO A 27 17516 25482 10367 -2321 809 -532 C ATOM 7 CD PRO A 27 -25.467 -8.842 2.983 1.00132.87 C ANISOU 7 CD PRO A 27 16611 24000 9873 -2232 916 -739 C ATOM 8 N CYS A 28 -29.016 -8.372 4.346 1.00128.28 N ANISOU 8 N CYS A 28 15635 23665 9440 -2566 122 -467 N ATOM 9 CA CYS A 28 -30.227 -8.756 5.084 1.00127.20 C ANISOU 9 CA CYS A 28 15416 23488 9425 -2721 -106 -531 C ATOM 10 C CYS A 28 -31.235 -7.631 5.327 1.00130.26 C ANISOU 10 C CYS A 28 15508 24102 9882 -2674 -348 -123 C ATOM 11 O CYS A 28 -31.830 -7.123 4.379 1.00132.70 O ANISOU 11 O CYS A 28 15715 24860 9846 -2750 -495 62 O ATOM 12 CB CYS A 28 -29.864 -9.478 6.379 1.00124.49 C ANISOU 12 CB CYS A 28 15161 22626 9513 -2661 0 -739 C ATOM 13 SG CYS A 28 -31.119 -10.653 6.964 1.00128.87 S ANISOU 13 SG CYS A 28 15770 23101 10093 -2952 -179 -1038 S ATOM 14 N ASN A 35 -43.730 -2.132 12.753 1.00129.42 N ANISOU 14 N ASN A 35 12536 24743 11896 -2148 -1960 2500 N ATOM 15 CA ASN A 35 -44.940 -1.339 12.543 1.00131.86 C ANISOU 15 CA ASN A 35 12474 25425 12201 -2044 -2111 2893 C ATOM 16 C ASN A 35 -45.777 -1.202 13.818 1.00134.02 C ANISOU 16 C ASN A 35 12575 25514 12834 -1937 -2061 2980 C ATOM 17 O ASN A 35 -46.244 -0.101 14.112 1.00134.25 O ANISOU 17 O ASN A 35 12395 25564 13051 -1654 -2031 3346 O ATOM 18 CB ASN A 35 -45.778 -1.900 11.384 1.00137.46 C ANISOU 18 CB ASN A 35 13007 26717 12505 -2341 -2375 2883 C ATOM 19 CG ASN A 35 -46.954 -1.033 10.981 1.00166.96 C ANISOU 19 CG ASN A 35 16336 30906 16194 -2220 -2552 3333 C ATOM 20 OD1 ASN A 35 -48.109 -1.476 10.973 1.00167.37 O ANISOU 20 OD1 ASN A 35 16124 31279 16189 -2407 -2732 3355 O ATOM 21 ND2 ASN A 35 -46.688 0.216 10.611 1.00157.87 N ANISOU 21 ND2 ASN A 35 15115 29801 15069 -1908 -2506 3716 N ATOM 22 N PHE A 36 -45.984 -2.314 14.560 1.00128.47 N ANISOU 22 N PHE A 36 11960 24630 12224 -2158 -2039 2653 N ATOM 23 CA PHE A 36 -46.738 -2.304 15.819 1.00126.58 C ANISOU 23 CA PHE A 36 11582 24203 12311 -2079 -1968 2703 C ATOM 24 C PHE A 36 -45.855 -1.795 16.962 1.00123.99 C ANISOU 24 C PHE A 36 11475 23321 12314 -1804 -1720 2678 C ATOM 25 O PHE A 36 -46.374 -1.208 17.912 1.00122.35 O ANISOU 25 O PHE A 36 11139 22965 12384 -1600 -1629 2854 O ATOM 26 CB PHE A 36 -47.341 -3.687 16.141 1.00129.33 C ANISOU 26 CB PHE A 36 11931 24587 12620 -2437 -2040 2388 C ATOM 27 CG PHE A 36 -48.210 -3.724 17.380 1.00130.34 C ANISOU 27 CG PHE A 36 11892 24574 13057 -2379 -1967 2456 C ATOM 28 CD1 PHE A 36 -49.536 -3.308 17.335 1.00136.20 C ANISOU 28 CD1 PHE A 36 12230 25687 13832 -2352 -2088 2753 C ATOM 29 CD2 PHE A 36 -47.700 -4.173 18.595 1.00129.33 C ANISOU 29 CD2 PHE A 36 12002 23957 13180 -2342 -1773 2237 C ATOM 30 CE1 PHE A 36 -50.334 -3.337 18.482 1.00136.60 C ANISOU 30 CE1 PHE A 36 12121 25613 14167 -2289 -1995 2821 C ATOM 31 CE2 PHE A 36 -48.500 -4.198 19.741 1.00131.57 C ANISOU 31 CE2 PHE A 36 12142 24121 13727 -2285 -1690 2306 C ATOM 32 CZ PHE A 36 -49.810 -3.783 19.675 1.00132.41 C ANISOU 32 CZ PHE A 36 11851 24592 13867 -2259 -1792 2592 C ATOM 33 N ASN A 37 -44.526 -1.988 16.847 1.00117.22 N ANISOU 33 N ASN A 37 10940 22178 11420 -1797 -1611 2466 N ATOM 34 CA ASN A 37 -43.535 -1.519 17.819 1.00113.15 C ANISOU 34 CA ASN A 37 10646 21162 11182 -1565 -1399 2426 C ATOM 35 C ASN A 37 -43.517 0.015 17.908 1.00116.38 C ANISOU 35 C ASN A 37 10940 21526 11754 -1221 -1328 2805 C ATOM 36 O ASN A 37 -43.135 0.560 18.944 1.00113.05 O ANISOU 36 O ASN A 37 10617 20722 11613 -1016 -1167 2831 O ATOM 37 CB ASN A 37 -42.139 -2.057 17.475 1.00111.60 C ANISOU 37 CB ASN A 37 10772 20752 10879 -1646 -1322 2148 C ATOM 38 CG ASN A 37 -41.918 -3.520 17.792 1.00132.51 C ANISOU 38 CG ASN A 37 13614 23248 13486 -1911 -1308 1750 C ATOM 39 OD1 ASN A 37 -42.845 -4.280 18.099 1.00130.29 O ANISOU 39 OD1 ASN A 37 13234 23067 13203 -2102 -1382 1651 O ATOM 40 ND2 ASN A 37 -40.670 -3.951 17.711 1.00121.75 N ANISOU 40 ND2 ASN A 37 12528 21633 12097 -1927 -1203 1521 N ATOM 41 N LYS A 38 -43.970 0.703 16.832 1.00115.95 N ANISOU 41 N LYS A 38 10677 21863 11517 -1163 -1449 3103 N ATOM 42 CA LYS A 38 -44.082 2.164 16.748 1.00116.42 C ANISOU 42 CA LYS A 38 10602 21921 11710 -840 -1391 3505 C ATOM 43 C LYS A 38 -45.058 2.718 17.798 1.00120.89 C ANISOU 43 C LYS A 38 10974 22384 12574 -644 -1323 3696 C ATOM 44 O LYS A 38 -44.923 3.874 18.192 1.00120.57 O ANISOU 44 O LYS A 38 10926 22132 12752 -347 -1191 3937 O ATOM 45 CB LYS A 38 -44.514 2.589 15.343 1.00122.06 C ANISOU 45 CB LYS A 38 11112 23135 12131 -852 -1562 3786 C ATOM 46 CG LYS A 38 -43.389 2.661 14.323 1.00133.03 C ANISOU 46 CG LYS A 38 12699 24563 13283 -897 -1554 3740 C ATOM 47 CD LYS A 38 -43.904 3.142 12.973 1.00143.85 C ANISOU 47 CD LYS A 38 13855 26452 14347 -893 -1724 4056 C ATOM 48 CE LYS A 38 -42.799 3.448 11.999 1.00151.80 C ANISOU 48 CE LYS A 38 15047 27487 15144 -879 -1679 4084 C ATOM 49 NZ LYS A 38 -43.330 4.012 10.729 1.00163.55 N ANISOU 49 NZ LYS A 38 16325 29485 16330 -847 -1840 4438 N ATOM 50 N ILE A 39 -46.040 1.893 18.233 1.00117.92 N ANISOU 50 N ILE A 39 10445 22153 12204 -814 -1399 3586 N ATOM 51 CA ILE A 39 -47.017 2.201 19.285 1.00117.87 C ANISOU 51 CA ILE A 39 10253 22067 12467 -665 -1320 3720 C ATOM 52 C ILE A 39 -46.588 1.450 20.557 1.00118.30 C ANISOU 52 C ILE A 39 10553 21697 12701 -745 -1176 3382 C ATOM 53 O ILE A 39 -46.568 2.047 21.629 1.00116.80 O ANISOU 53 O ILE A 39 10417 21183 12780 -521 -1003 3438 O ATOM 54 CB ILE A 39 -48.478 1.843 18.872 1.00124.81 C ANISOU 54 CB ILE A 39 10746 23443 13232 -800 -1504 3876 C ATOM 55 CG1 ILE A 39 -48.946 2.675 17.657 1.00129.10 C ANISOU 55 CG1 ILE A 39 11023 24429 13600 -686 -1655 4262 C ATOM 56 CG2 ILE A 39 -49.455 1.994 20.059 1.00125.70 C ANISOU 56 CG2 ILE A 39 10676 23452 13632 -669 -1391 3971 C ATOM 57 CD1 ILE A 39 -50.180 2.098 16.890 1.00138.59 C ANISOU 57 CD1 ILE A 39 11863 26224 14572 -921 -1913 4362 C ATOM 58 N PHE A 40 -46.229 0.151 20.421 1.00113.48 N ANISOU 58 N PHE A 40 10101 21083 11932 -1058 -1244 3033 N ATOM 59 CA PHE A 40 -45.812 -0.744 21.508 1.00110.36 C ANISOU 59 CA PHE A 40 9942 20322 11667 -1169 -1131 2709 C ATOM 60 C PHE A 40 -44.592 -0.288 22.318 1.00109.48 C ANISOU 60 C PHE A 40 10133 19723 11742 -976 -946 2613 C ATOM 61 O PHE A 40 -44.619 -0.412 23.543 1.00107.70 O ANISOU 61 O PHE A 40 10001 19200 11720 -912 -818 2521 O ATOM 62 CB PHE A 40 -45.630 -2.184 21.001 1.00112.72 C ANISOU 62 CB PHE A 40 10358 20726 11743 -1535 -1241 2380 C ATOM 63 CG PHE A 40 -45.467 -3.228 22.081 1.00112.66 C ANISOU 63 CG PHE A 40 10542 20400 11865 -1673 -1142 2084 C ATOM 64 CD1 PHE A 40 -44.252 -3.875 22.267 1.00113.65 C ANISOU 64 CD1 PHE A 40 11001 20204 11978 -1740 -1064 1797 C ATOM 65 CD2 PHE A 40 -46.533 -3.575 22.905 1.00115.78 C ANISOU 65 CD2 PHE A 40 10773 20823 12396 -1730 -1121 2111 C ATOM 66 CE1 PHE A 40 -44.107 -4.858 23.253 1.00113.11 C ANISOU 66 CE1 PHE A 40 11107 19844 12024 -1856 -975 1550 C ATOM 67 CE2 PHE A 40 -46.382 -4.543 23.904 1.00117.10 C ANISOU 67 CE2 PHE A 40 11125 20693 12674 -1856 -1022 1860 C ATOM 68 CZ PHE A 40 -45.171 -5.179 24.069 1.00112.96 C ANISOU 68 CZ PHE A 40 10940 19849 12130 -1915 -954 1586 C ATOM 69 N LEU A 41 -43.524 0.203 21.655 1.00103.98 N ANISOU 69 N LEU A 41 9586 18955 10968 -901 -934 2629 N ATOM 70 CA LEU A 41 -42.320 0.678 22.355 1.00100.42 C ANISOU 70 CA LEU A 41 9398 18067 10690 -739 -776 2548 C ATOM 71 C LEU A 41 -42.547 1.995 23.124 1.00102.27 C ANISOU 71 C LEU A 41 9578 18102 11179 -431 -646 2795 C ATOM 72 O LEU A 41 -42.253 2.002 24.323 1.00100.58 O ANISOU 72 O LEU A 41 9517 17541 11155 -356 -519 2674 O ATOM 73 CB LEU A 41 -41.059 0.737 21.465 1.00 99.90 C ANISOU 73 CB LEU A 41 9504 17972 10481 -771 -785 2476 C ATOM 74 CG LEU A 41 -40.531 -0.593 20.905 1.00104.47 C ANISOU 74 CG LEU A 41 10229 18621 10844 -1045 -851 2164 C ATOM 75 CD1 LEU A 41 -39.597 -0.349 19.740 1.00105.39 C ANISOU 75 CD1 LEU A 41 10425 18845 10773 -1054 -869 2185 C ATOM 76 CD2 LEU A 41 -39.823 -1.423 21.978 1.00103.67 C ANISOU 76 CD2 LEU A 41 10370 18137 10882 -1102 -750 1866 C ATOM 77 N PRO A 42 -43.122 3.087 22.537 1.00 98.49 N ANISOU 77 N PRO A 42 8888 17822 10711 -246 -665 3139 N ATOM 78 CA PRO A 42 -43.377 4.289 23.351 1.00 97.36 C ANISOU 78 CA PRO A 42 8718 17442 10832 52 -512 3350 C ATOM 79 C PRO A 42 -44.422 4.056 24.448 1.00 98.71 C ANISOU 79 C PRO A 42 8779 17570 11156 93 -443 3337 C ATOM 80 O PRO A 42 -44.421 4.793 25.432 1.00 96.94 O ANISOU 80 O PRO A 42 8632 17045 11155 304 -278 3387 O ATOM 81 CB PRO A 42 -43.835 5.327 22.324 1.00102.01 C ANISOU 81 CB PRO A 42 9087 18301 11371 218 -562 3729 C ATOM 82 CG PRO A 42 -44.401 4.537 21.228 1.00108.61 C ANISOU 82 CG PRO A 42 9732 19611 11923 -4 -767 3740 C ATOM 83 CD PRO A 42 -43.559 3.300 21.141 1.00102.43 C ANISOU 83 CD PRO A 42 9176 18758 10984 -286 -817 3359 C ATOM 84 N THR A 43 -45.281 3.015 24.297 1.00 95.34 N ANISOU 84 N THR A 43 8186 17433 10606 -122 -559 3256 N ATOM 85 CA THR A 43 -46.273 2.624 25.305 1.00 95.18 C ANISOU 85 CA THR A 43 8051 17400 10714 -128 -492 3229 C ATOM 86 C THR A 43 -45.530 2.158 26.558 1.00 94.55 C ANISOU 86 C THR A 43 8280 16892 10754 -154 -356 2941 C ATOM 87 O THR A 43 -45.780 2.691 27.639 1.00 93.80 O ANISOU 87 O THR A 43 8223 16563 10853 33 -193 2985 O ATOM 88 CB THR A 43 -47.255 1.559 24.759 1.00106.05 C ANISOU 88 CB THR A 43 9186 19187 11920 -402 -662 3194 C ATOM 89 OG1 THR A 43 -47.991 2.117 23.672 1.00110.72 O ANISOU 89 OG1 THR A 43 9469 20195 12403 -348 -795 3498 O ATOM 90 CG2 THR A 43 -48.241 1.060 25.813 1.00103.60 C ANISOU 90 CG2 THR A 43 8757 18861 11746 -439 -582 3157 C ATOM 91 N ILE A 44 -44.589 1.202 26.389 1.00 88.04 N ANISOU 91 N ILE A 44 7679 15967 9805 -372 -416 2657 N ATOM 92 CA ILE A 44 -43.746 0.640 27.447 1.00 84.77 C ANISOU 92 CA ILE A 44 7561 15176 9471 -417 -317 2384 C ATOM 93 C ILE A 44 -42.915 1.760 28.091 1.00 86.75 C ANISOU 93 C ILE A 44 7996 15077 9888 -169 -180 2432 C ATOM 94 O ILE A 44 -42.884 1.867 29.322 1.00 84.74 O ANISOU 94 O ILE A 44 7871 14552 9777 -78 -51 2356 O ATOM 95 CB ILE A 44 -42.872 -0.526 26.888 1.00 86.65 C ANISOU 95 CB ILE A 44 7972 15414 9537 -673 -415 2115 C ATOM 96 CG1 ILE A 44 -43.743 -1.747 26.519 1.00 88.36 C ANISOU 96 CG1 ILE A 44 8053 15903 9616 -949 -525 2013 C ATOM 97 CG2 ILE A 44 -41.743 -0.926 27.859 1.00 84.90 C ANISOU 97 CG2 ILE A 44 8064 14793 9403 -670 -319 1876 C ATOM 98 CD1 ILE A 44 -43.019 -2.837 25.807 1.00 94.14 C ANISOU 98 CD1 ILE A 44 8940 16662 10167 -1194 -613 1763 C ATOM 99 N TYR A 45 -42.288 2.615 27.247 1.00 83.46 N ANISOU 99 N TYR A 45 7587 14678 9445 -70 -206 2566 N ATOM 100 CA TYR A 45 -41.469 3.744 27.692 1.00 82.14 C ANISOU 100 CA TYR A 45 7584 14190 9434 137 -87 2622 C ATOM 101 C TYR A 45 -42.236 4.750 28.544 1.00 86.22 C ANISOU 101 C TYR A 45 8038 14572 10150 383 61 2797 C ATOM 102 O TYR A 45 -41.642 5.326 29.453 1.00 85.29 O ANISOU 102 O TYR A 45 8124 14107 10175 500 185 2724 O ATOM 103 CB TYR A 45 -40.798 4.456 26.512 1.00 84.09 C ANISOU 103 CB TYR A 45 7817 14522 9613 182 -138 2772 C ATOM 104 CG TYR A 45 -39.782 3.632 25.750 1.00 85.41 C ANISOU 104 CG TYR A 45 8100 14749 9602 -22 -236 2584 C ATOM 105 CD1 TYR A 45 -39.002 2.676 26.397 1.00 85.43 C ANISOU 105 CD1 TYR A 45 8310 14548 9601 -159 -226 2285 C ATOM 106 CD2 TYR A 45 -39.544 3.862 24.397 1.00 87.66 C ANISOU 106 CD2 TYR A 45 8298 15282 9728 -55 -321 2717 C ATOM 107 CE1 TYR A 45 -38.045 1.935 25.705 1.00 85.99 C ANISOU 107 CE1 TYR A 45 8489 14657 9528 -318 -289 2117 C ATOM 108 CE2 TYR A 45 -38.586 3.130 23.696 1.00 87.81 C ANISOU 108 CE2 TYR A 45 8435 15349 9581 -226 -382 2539 C ATOM 109 CZ TYR A 45 -37.836 2.170 24.355 1.00 93.79 C ANISOU 109 CZ TYR A 45 9391 15891 10355 -351 -359 2236 C ATOM 110 OH TYR A 45 -36.895 1.442 23.669 1.00 94.50 O ANISOU 110 OH TYR A 45 9593 16017 10296 -496 -396 2064 O ATOM 111 N SER A 46 -43.539 4.960 28.264 1.00 83.64 N ANISOU 111 N SER A 46 7429 14521 9831 460 52 3021 N ATOM 112 CA SER A 46 -44.376 5.887 29.027 1.00 84.18 C ANISOU 112 CA SER A 46 7409 14483 10092 716 214 3204 C ATOM 113 C SER A 46 -44.702 5.320 30.403 1.00 85.71 C ANISOU 113 C SER A 46 7705 14497 10362 691 328 3015 C ATOM 114 O SER A 46 -44.713 6.072 31.377 1.00 84.95 O ANISOU 114 O SER A 46 7732 14119 10426 886 504 3023 O ATOM 115 CB SER A 46 -45.653 6.221 28.266 1.00 90.87 C ANISOU 115 CB SER A 46 7891 15712 10922 810 163 3519 C ATOM 116 OG SER A 46 -45.349 6.797 27.005 1.00100.52 O ANISOU 116 OG SER A 46 9029 17107 12059 848 62 3720 O ATOM 117 N ILE A 47 -44.932 3.988 30.484 1.00 81.02 N ANISOU 117 N ILE A 47 7083 14053 9646 444 234 2837 N ATOM 118 CA ILE A 47 -45.218 3.260 31.727 1.00 79.85 C ANISOU 118 CA ILE A 47 7036 13763 9541 381 330 2658 C ATOM 119 C ILE A 47 -44.005 3.377 32.663 1.00 82.68 C ANISOU 119 C ILE A 47 7755 13711 9950 410 412 2439 C ATOM 120 O ILE A 47 -44.175 3.663 33.848 1.00 82.31 O ANISOU 120 O ILE A 47 7826 13444 10004 530 568 2392 O ATOM 121 CB ILE A 47 -45.611 1.773 31.447 1.00 82.63 C ANISOU 121 CB ILE A 47 7296 14350 9748 81 200 2519 C ATOM 122 CG1 ILE A 47 -46.894 1.674 30.587 1.00 85.85 C ANISOU 122 CG1 ILE A 47 7322 15193 10104 30 104 2736 C ATOM 123 CG2 ILE A 47 -45.764 0.972 32.754 1.00 81.62 C ANISOU 123 CG2 ILE A 47 7310 14039 9663 5 307 2334 C ATOM 124 CD1 ILE A 47 -47.101 0.356 29.800 1.00 92.55 C ANISOU 124 CD1 ILE A 47 8075 16322 10767 -307 -81 2609 C ATOM 125 N ILE A 48 -42.789 3.184 32.112 1.00 78.20 N ANISOU 125 N ILE A 48 7350 13060 9303 304 308 2313 N ATOM 126 CA ILE A 48 -41.535 3.268 32.859 1.00 75.95 C ANISOU 126 CA ILE A 48 7374 12428 9055 309 350 2117 C ATOM 127 C ILE A 48 -41.238 4.710 33.259 1.00 80.31 C ANISOU 127 C ILE A 48 8024 12734 9757 542 476 2220 C ATOM 128 O ILE A 48 -40.887 4.943 34.413 1.00 79.50 O ANISOU 128 O ILE A 48 8129 12352 9725 605 580 2095 O ATOM 129 CB ILE A 48 -40.363 2.540 32.142 1.00 77.52 C ANISOU 129 CB ILE A 48 7685 12635 9135 123 212 1960 C ATOM 130 CG1 ILE A 48 -40.725 1.056 31.923 1.00 78.18 C ANISOU 130 CG1 ILE A 48 7713 12906 9086 -109 121 1826 C ATOM 131 CG2 ILE A 48 -39.056 2.644 32.952 1.00 76.08 C ANISOU 131 CG2 ILE A 48 7788 12115 9003 133 245 1778 C ATOM 132 CD1 ILE A 48 -40.007 0.366 30.822 1.00 88.03 C ANISOU 132 CD1 ILE A 48 8976 14279 10193 -281 -11 1733 C ATOM 133 N PHE A 49 -41.443 5.674 32.339 1.00 78.39 N ANISOU 133 N PHE A 49 7634 12593 9557 670 473 2453 N ATOM 134 CA PHE A 49 -41.226 7.098 32.604 1.00 79.32 C ANISOU 134 CA PHE A 49 7839 12463 9836 894 606 2575 C ATOM 135 C PHE A 49 -42.077 7.595 33.778 1.00 84.74 C ANISOU 135 C PHE A 49 8551 12996 10651 1077 796 2600 C ATOM 136 O PHE A 49 -41.521 8.127 34.732 1.00 83.60 O ANISOU 136 O PHE A 49 8651 12522 10589 1148 907 2473 O ATOM 137 CB PHE A 49 -41.445 7.960 31.341 1.00 82.95 C ANISOU 137 CB PHE A 49 8110 13092 10316 1005 573 2863 C ATOM 138 CG PHE A 49 -41.389 9.447 31.600 1.00 86.21 C ANISOU 138 CG PHE A 49 8600 13235 10919 1252 735 3019 C ATOM 139 CD1 PHE A 49 -42.556 10.198 31.692 1.00 92.02 C ANISOU 139 CD1 PHE A 49 9164 14023 11775 1488 865 3260 C ATOM 140 CD2 PHE A 49 -40.172 10.091 31.798 1.00 87.79 C ANISOU 140 CD2 PHE A 49 9047 13116 11195 1248 770 2921 C ATOM 141 CE1 PHE A 49 -42.505 11.570 31.964 1.00 94.65 C ANISOU 141 CE1 PHE A 49 9597 14065 12302 1727 1040 3395 C ATOM 142 CE2 PHE A 49 -40.121 11.463 32.064 1.00 92.31 C ANISOU 142 CE2 PHE A 49 9715 13403 11955 1456 931 3048 C ATOM 143 CZ PHE A 49 -41.287 12.193 32.145 1.00 92.94 C ANISOU 143 CZ PHE A 49 9648 13511 12154 1700 1073 3280 C ATOM 144 N LEU A 50 -43.407 7.393 33.717 1.00 83.73 N ANISOU 144 N LEU A 50 8170 13115 10528 1142 834 2754 N ATOM 145 CA LEU A 50 -44.345 7.815 34.761 1.00 85.33 C ANISOU 145 CA LEU A 50 8355 13217 10848 1331 1037 2802 C ATOM 146 C LEU A 50 -44.067 7.158 36.120 1.00 88.24 C ANISOU 146 C LEU A 50 8965 13380 11181 1244 1110 2531 C ATOM 147 O LEU A 50 -43.884 7.871 37.106 1.00 88.53 O ANISOU 147 O LEU A 50 9212 13119 11306 1387 1276 2456 O ATOM 148 CB LEU A 50 -45.800 7.587 34.315 1.00 87.59 C ANISOU 148 CB LEU A 50 8273 13868 11140 1387 1040 3034 C ATOM 149 CG LEU A 50 -46.584 8.832 33.891 1.00 95.28 C ANISOU 149 CG LEU A 50 9045 14892 12265 1681 1157 3358 C ATOM 150 CD1 LEU A 50 -46.184 9.304 32.492 1.00 95.69 C ANISOU 150 CD1 LEU A 50 8988 15091 12280 1683 1010 3549 C ATOM 151 CD2 LEU A 50 -48.079 8.558 33.921 1.00101.07 C ANISOU 151 CD2 LEU A 50 9433 15940 13030 1755 1208 3550 C ATOM 152 N THR A 51 -43.983 5.817 36.157 1.00 83.27 N ANISOU 152 N THR A 51 8326 12897 10415 1007 987 2380 N ATOM 153 CA THR A 51 -43.706 5.043 37.371 1.00 81.80 C ANISOU 153 CA THR A 51 8357 12549 10173 907 1034 2146 C ATOM 154 C THR A 51 -42.324 5.389 37.959 1.00 83.30 C ANISOU 154 C THR A 51 8886 12405 10361 893 1026 1948 C ATOM 155 O THR A 51 -42.195 5.519 39.178 1.00 82.82 O ANISOU 155 O THR A 51 9036 12124 10306 947 1145 1818 O ATOM 156 CB THR A 51 -43.875 3.543 37.077 1.00 91.29 C ANISOU 156 CB THR A 51 9465 13976 11244 651 895 2057 C ATOM 157 OG1 THR A 51 -45.105 3.338 36.374 1.00 93.08 O ANISOU 157 OG1 THR A 51 9354 14538 11475 640 873 2251 O ATOM 158 CG2 THR A 51 -43.831 2.675 38.334 1.00 89.98 C ANISOU 158 CG2 THR A 51 9484 13679 11027 561 963 1870 C ATOM 159 N GLY A 52 -41.332 5.557 37.084 1.00 77.98 N ANISOU 159 N GLY A 52 8247 11713 9669 820 889 1937 N ATOM 160 CA GLY A 52 -39.959 5.884 37.450 1.00 76.02 C ANISOU 160 CA GLY A 52 8268 11191 9427 783 852 1773 C ATOM 161 C GLY A 52 -39.749 7.288 37.973 1.00 80.75 C ANISOU 161 C GLY A 52 9017 11507 10156 967 994 1800 C ATOM 162 O GLY A 52 -39.159 7.453 39.037 1.00 79.46 O ANISOU 162 O GLY A 52 9105 11097 9989 961 1043 1622 O ATOM 163 N ILE A 53 -40.214 8.313 37.232 1.00 79.77 N ANISOU 163 N ILE A 53 8751 11412 10145 1128 1060 2022 N ATOM 164 CA ILE A 53 -40.061 9.728 37.604 1.00 81.37 C ANISOU 164 CA ILE A 53 9097 11320 10499 1313 1216 2068 C ATOM 165 C ILE A 53 -40.632 10.047 39.000 1.00 86.08 C ANISOU 165 C ILE A 53 9855 11719 11133 1444 1417 1967 C ATOM 166 O ILE A 53 -39.944 10.669 39.810 1.00 85.63 O ANISOU 166 O ILE A 53 10072 11354 11111 1460 1486 1808 O ATOM 167 CB ILE A 53 -40.534 10.696 36.463 1.00 86.43 C ANISOU 167 CB ILE A 53 9535 12047 11259 1477 1254 2367 C ATOM 168 CG1 ILE A 53 -39.719 12.025 36.375 1.00 87.65 C ANISOU 168 CG1 ILE A 53 9871 11875 11558 1565 1329 2396 C ATOM 169 CG2 ILE A 53 -42.066 10.861 36.354 1.00 89.52 C ANISOU 169 CG2 ILE A 53 9669 12637 11706 1670 1376 2595 C ATOM 170 CD1 ILE A 53 -39.979 13.159 37.447 1.00 95.86 C ANISOU 170 CD1 ILE A 53 11124 12551 12749 1763 1570 2351 C ATOM 171 N VAL A 54 -41.853 9.564 39.289 1.00 83.50 N ANISOU 171 N VAL A 54 9360 11582 10783 1516 1506 2046 N ATOM 172 CA VAL A 54 -42.533 9.766 40.570 1.00 84.69 C ANISOU 172 CA VAL A 54 9632 11595 10951 1649 1720 1970 C ATOM 173 C VAL A 54 -41.872 8.903 41.659 1.00 86.97 C ANISOU 173 C VAL A 54 10171 11786 11089 1475 1668 1692 C ATOM 174 O VAL A 54 -41.518 9.415 42.724 1.00 86.66 O ANISOU 174 O VAL A 54 10408 11478 11041 1526 1782 1530 O ATOM 175 CB VAL A 54 -44.052 9.472 40.451 1.00 90.22 C ANISOU 175 CB VAL A 54 10029 12568 11681 1770 1829 2170 C ATOM 176 CG1 VAL A 54 -44.771 9.747 41.767 1.00 91.67 C ANISOU 176 CG1 VAL A 54 10335 12608 11889 1931 2087 2104 C ATOM 177 CG2 VAL A 54 -44.687 10.268 39.312 1.00 91.93 C ANISOU 177 CG2 VAL A 54 9970 12925 12035 1944 1850 2475 C ATOM 178 N GLY A 55 -41.726 7.610 41.361 1.00 82.24 N ANISOU 178 N GLY A 55 9474 11406 10367 1273 1496 1647 N ATOM 179 CA GLY A 55 -41.149 6.604 42.244 1.00 80.60 C ANISOU 179 CA GLY A 55 9457 11152 10013 1105 1425 1430 C ATOM 180 C GLY A 55 -39.745 6.916 42.708 1.00 83.80 C ANISOU 180 C GLY A 55 10153 11304 10384 1026 1340 1235 C ATOM 181 O GLY A 55 -39.486 6.938 43.913 1.00 84.06 O ANISOU 181 O GLY A 55 10428 11167 10342 1027 1407 1072 O ATOM 182 N ASN A 56 -38.824 7.143 41.758 1.00 79.42 N ANISOU 182 N ASN A 56 9568 10739 9871 948 1188 1255 N ATOM 183 CA ASN A 56 -37.431 7.467 42.066 1.00 78.30 C ANISOU 183 CA ASN A 56 9654 10380 9715 855 1089 1092 C ATOM 184 C ASN A 56 -37.282 8.896 42.596 1.00 83.84 C ANISOU 184 C ASN A 56 10542 10792 10520 986 1231 1057 C ATOM 185 O ASN A 56 -36.360 9.164 43.364 1.00 83.59 O ANISOU 185 O ASN A 56 10755 10556 10450 912 1193 874 O ATOM 186 CB ASN A 56 -36.499 7.164 40.889 1.00 76.95 C ANISOU 186 CB ASN A 56 9377 10307 9554 722 898 1128 C ATOM 187 CG ASN A 56 -36.422 5.688 40.554 1.00 90.03 C ANISOU 187 CG ASN A 56 10929 12186 11094 570 762 1094 C ATOM 188 OD1 ASN A 56 -35.774 4.889 41.250 1.00 81.69 O ANISOU 188 OD1 ASN A 56 10011 11084 9941 461 684 939 O ATOM 189 ND2 ASN A 56 -37.092 5.290 39.481 1.00 76.83 N ANISOU 189 ND2 ASN A 56 9014 10756 9423 559 731 1242 N ATOM 190 N GLY A 57 -38.224 9.770 42.236 1.00 82.03 N ANISOU 190 N GLY A 57 10201 10548 10419 1179 1397 1230 N ATOM 191 CA GLY A 57 -38.279 11.141 42.728 1.00 84.18 C ANISOU 191 CA GLY A 57 10651 10522 10810 1334 1579 1211 C ATOM 192 C GLY A 57 -38.627 11.179 44.205 1.00 89.50 C ANISOU 192 C GLY A 57 11561 11048 11398 1391 1735 1033 C ATOM 193 O GLY A 57 -38.022 11.940 44.962 1.00 89.77 O ANISOU 193 O GLY A 57 11873 10799 11437 1385 1791 863 O ATOM 194 N LEU A 58 -39.586 10.329 44.629 1.00 86.83 N ANISOU 194 N LEU A 58 11118 10906 10968 1428 1803 1064 N ATOM 195 CA LEU A 58 -40.006 10.207 46.025 1.00 88.25 C ANISOU 195 CA LEU A 58 11502 10995 11034 1479 1963 913 C ATOM 196 C LEU A 58 -38.879 9.630 46.883 1.00 91.34 C ANISOU 196 C LEU A 58 12153 11304 11248 1279 1807 668 C ATOM 197 O LEU A 58 -38.611 10.165 47.956 1.00 92.83 O ANISOU 197 O LEU A 58 12629 11277 11364 1300 1901 488 O ATOM 198 CB LEU A 58 -41.271 9.340 46.163 1.00 88.70 C ANISOU 198 CB LEU A 58 11346 11312 11043 1540 2062 1035 C ATOM 199 CG LEU A 58 -42.606 9.958 45.744 1.00 96.07 C ANISOU 199 CG LEU A 58 12044 12327 12132 1781 2277 1266 C ATOM 200 CD1 LEU A 58 -43.727 8.934 45.825 1.00 96.39 C ANISOU 200 CD1 LEU A 58 11841 12664 12117 1778 2327 1380 C ATOM 201 CD2 LEU A 58 -42.954 11.187 46.586 1.00102.30 C ANISOU 201 CD2 LEU A 58 13047 12828 12993 2005 2557 1206 C ATOM 202 N VAL A 59 -38.205 8.563 46.396 1.00 85.33 N ANISOU 202 N VAL A 59 11293 10714 10413 1090 1570 662 N ATOM 203 CA VAL A 59 -37.095 7.899 47.092 1.00 84.24 C ANISOU 203 CA VAL A 59 11353 10536 10117 908 1397 471 C ATOM 204 C VAL A 59 -35.916 8.876 47.299 1.00 89.44 C ANISOU 204 C VAL A 59 12229 10944 10810 846 1323 326 C ATOM 205 O VAL A 59 -35.295 8.874 48.362 1.00 89.46 O ANISOU 205 O VAL A 59 12483 10831 10676 768 1283 135 O ATOM 206 CB VAL A 59 -36.700 6.551 46.413 1.00 85.83 C ANISOU 206 CB VAL A 59 11380 10966 10266 751 1188 522 C ATOM 207 CG1 VAL A 59 -35.434 5.948 47.026 1.00 84.81 C ANISOU 207 CG1 VAL A 59 11431 10787 10006 587 1000 355 C ATOM 208 CG2 VAL A 59 -37.847 5.544 46.485 1.00 85.43 C ANISOU 208 CG2 VAL A 59 11172 11129 10161 774 1269 620 C ATOM 209 N ILE A 60 -35.657 9.809 46.314 1.00 87.20 N ANISOU 209 N ILE A 60 11856 10569 10709 882 1320 422 N ATOM 210 CA ILE A 60 -34.642 10.868 46.436 1.00 88.65 C ANISOU 210 CA ILE A 60 12229 10490 10962 819 1280 303 C ATOM 211 C ILE A 60 -35.045 11.960 47.448 1.00 97.59 C ANISOU 211 C ILE A 60 13630 11349 12102 937 1500 176 C ATOM 212 O ILE A 60 -34.232 12.364 48.272 1.00 98.08 O ANISOU 212 O ILE A 60 13954 11225 12088 827 1450 -35 O ATOM 213 CB ILE A 60 -34.318 11.507 45.072 1.00 91.27 C ANISOU 213 CB ILE A 60 12385 10804 11489 826 1236 469 C ATOM 214 CG1 ILE A 60 -33.685 10.469 44.140 1.00 88.75 C ANISOU 214 CG1 ILE A 60 11855 10729 11137 683 1014 544 C ATOM 215 CG2 ILE A 60 -33.356 12.696 45.236 1.00 93.54 C ANISOU 215 CG2 ILE A 60 12876 10790 11876 756 1229 355 C ATOM 216 CD1 ILE A 60 -33.526 10.906 42.708 1.00 94.46 C ANISOU 216 CD1 ILE A 60 12372 11507 12012 699 981 737 C ATOM 217 N LEU A 61 -36.288 12.423 47.365 1.00 97.92 N ANISOU 217 N LEU A 61 13598 11374 12233 1158 1741 304 N ATOM 218 CA LEU A 61 -36.767 13.490 48.237 1.00101.87 C ANISOU 218 CA LEU A 61 14345 11600 12760 1306 1994 196 C ATOM 219 C LEU A 61 -36.950 13.021 49.678 1.00109.32 C ANISOU 219 C LEU A 61 15525 12541 13470 1284 2060 -10 C ATOM 220 O LEU A 61 -36.502 13.680 50.616 1.00111.28 O ANISOU 220 O LEU A 61 16092 12550 13639 1243 2116 -235 O ATOM 221 CB LEU A 61 -38.080 14.067 47.703 1.00103.47 C ANISOU 221 CB LEU A 61 14368 11810 13138 1579 2246 423 C ATOM 222 CG LEU A 61 -38.221 15.590 47.753 1.00111.10 C ANISOU 222 CG LEU A 61 15504 12423 14287 1741 2469 413 C ATOM 223 CD1 LEU A 61 -39.654 15.987 48.073 1.00113.64 C ANISOU 223 CD1 LEU A 61 15776 12724 14679 2039 2792 527 C ATOM 224 CD2 LEU A 61 -37.256 16.186 48.766 1.00114.76 C ANISOU 224 CD2 LEU A 61 16363 12580 14661 1596 2454 100 C ATOM 225 N VAL A 62 -37.613 11.882 49.845 1.00106.36 N ANISOU 225 N VAL A 62 15001 12434 12977 1300 2056 69 N ATOM 226 CA VAL A 62 -37.896 11.346 51.173 1.00107.99 C ANISOU 226 CA VAL A 62 15408 12671 12952 1292 2137 -83 C ATOM 227 C VAL A 62 -36.623 11.035 51.956 1.00114.10 C ANISOU 227 C VAL A 62 16434 13390 13528 1069 1918 -313 C ATOM 228 O VAL A 62 -36.423 11.542 53.060 1.00115.91 O ANISOU 228 O VAL A 62 16977 13449 13615 1058 2000 -524 O ATOM 229 CB VAL A 62 -38.759 10.072 51.093 1.00110.42 C ANISOU 229 CB VAL A 62 15481 13286 13187 1315 2148 69 C ATOM 230 CG1 VAL A 62 -38.807 9.379 52.446 1.00110.90 C ANISOU 230 CG1 VAL A 62 15761 13390 12985 1262 2185 -80 C ATOM 231 CG2 VAL A 62 -40.161 10.412 50.611 1.00111.51 C ANISOU 231 CG2 VAL A 62 15387 13494 13486 1546 2396 280 C ATOM 232 N MET A 63 -35.768 10.196 51.380 1.00110.44 N ANISOU 232 N MET A 63 15830 13083 13050 896 1641 -270 N ATOM 233 CA MET A 63 -34.552 9.774 52.042 1.00111.29 C ANISOU 233 CA MET A 63 16116 13188 12982 693 1410 -445 C ATOM 234 C MET A 63 -33.573 10.897 51.951 1.00119.18 C ANISOU 234 C MET A 63 17267 13948 14068 599 1333 -578 C ATOM 235 O MET A 63 -33.113 11.428 52.964 1.00121.41 O ANISOU 235 O MET A 63 17845 14071 14215 528 1334 -796 O ATOM 236 CB MET A 63 -33.944 8.560 51.359 1.00111.13 C ANISOU 236 CB MET A 63 15877 13393 12955 562 1161 -339 C ATOM 237 CG MET A 63 -34.705 7.296 51.579 1.00114.39 C ANISOU 237 CG MET A 63 16179 14026 13257 596 1198 -239 C ATOM 238 SD MET A 63 -33.522 5.975 51.795 1.00117.51 S ANISOU 238 SD MET A 63 16578 14568 13503 403 900 -276 S ATOM 239 CE MET A 63 -33.736 5.066 50.267 1.00111.68 C ANISOU 239 CE MET A 63 15477 14024 12934 388 820 -65 C ATOM 240 N GLY A 64 -33.269 11.271 50.713 1.00116.46 N ANISOU 240 N GLY A 64 16720 13583 13947 589 1269 -445 N ATOM 241 CA GLY A 64 -32.245 12.261 50.445 1.00118.15 C ANISOU 241 CA GLY A 64 17031 13584 14277 470 1176 -537 C ATOM 242 C GLY A 64 -32.235 13.314 51.516 1.00127.66 C ANISOU 242 C GLY A 64 18582 14508 15416 474 1316 -764 C ATOM 243 O GLY A 64 -31.183 13.647 52.053 1.00128.39 O ANISOU 243 O GLY A 64 18864 14487 15430 284 1164 -956 O ATOM 244 N TYR A 65 -33.404 13.806 51.864 1.00127.76 N ANISOU 244 N TYR A 65 18678 14417 15448 684 1607 -750 N ATOM 245 CA TYR A 65 -33.457 14.902 52.797 1.00131.81 C ANISOU 245 CA TYR A 65 19537 14627 15917 709 1782 -974 C ATOM 246 C TYR A 65 -33.959 14.697 54.213 1.00139.31 C ANISOU 246 C TYR A 65 20759 15575 16596 756 1919 -1161 C ATOM 247 O TYR A 65 -33.243 14.947 55.183 1.00140.68 O ANISOU 247 O TYR A 65 21229 15643 16581 596 1833 -1416 O ATOM 248 CB TYR A 65 -34.225 15.998 52.129 1.00134.80 C ANISOU 248 CB TYR A 65 19871 14786 16559 920 2045 -848 C ATOM 249 CG TYR A 65 -33.485 16.463 50.922 1.00136.03 C ANISOU 249 CG TYR A 65 19860 14874 16953 830 1908 -720 C ATOM 250 CD1 TYR A 65 -33.212 15.616 49.888 1.00134.97 C ANISOU 250 CD1 TYR A 65 19399 15010 16872 774 1710 -515 C ATOM 251 CD2 TYR A 65 -33.009 17.736 50.844 1.00139.41 C ANISOU 251 CD2 TYR A 65 20474 14957 17537 786 1979 -816 C ATOM 252 CE1 TYR A 65 -32.521 16.045 48.826 1.00135.20 C ANISOU 252 CE1 TYR A 65 19291 14986 17095 692 1600 -402 C ATOM 253 CE2 TYR A 65 -32.327 18.153 49.790 1.00139.75 C ANISOU 253 CE2 TYR A 65 20372 14939 17788 697 1867 -691 C ATOM 254 CZ TYR A 65 -32.086 17.329 48.791 1.00144.52 C ANISOU 254 CZ TYR A 65 20653 15828 18432 655 1682 -483 C ATOM 255 OH TYR A 65 -31.393 17.827 47.748 1.00145.99 O ANISOU 255 OH TYR A 65 20711 15940 18817 570 1594 -358 O ATOM 256 N GLN A 66 -35.179 14.251 54.359 1.00137.28 N ANISOU 256 N GLN A 66 20404 15449 16307 963 2131 -1036 N ATOM 257 CA GLN A 66 -35.674 14.086 55.682 1.00139.99 C ANISOU 257 CA GLN A 66 21005 15794 16392 1015 2288 -1200 C ATOM 258 C GLN A 66 -34.997 13.054 56.518 1.00144.36 C ANISOU 258 C GLN A 66 21661 16547 16643 825 2056 -1312 C ATOM 259 O GLN A 66 -34.756 13.297 57.672 1.00146.58 O ANISOU 259 O GLN A 66 22267 16742 16685 760 2085 -1546 O ATOM 260 CB GLN A 66 -37.127 13.715 55.625 1.00141.67 C ANISOU 260 CB GLN A 66 21044 16142 16642 1268 2560 -1012 C ATOM 261 CG GLN A 66 -37.974 14.744 54.978 1.00164.89 C ANISOU 261 CG GLN A 66 23895 18899 19859 1507 2834 -886 C ATOM 262 CD GLN A 66 -39.419 14.317 54.872 1.00188.55 C ANISOU 262 CD GLN A 66 26660 22076 22904 1751 3083 -671 C ATOM 263 OE1 GLN A 66 -40.176 14.338 55.844 1.00187.24 O ANISOU 263 OE1 GLN A 66 26652 21896 22596 1882 3335 -751 O ATOM 264 NE2 GLN A 66 -39.805 13.930 53.687 1.00179.03 N ANISOU 264 NE2 GLN A 66 25074 21055 21893 1806 3015 -396 N ATOM 265 N LYS A 67 -34.705 11.890 55.952 1.00138.35 N ANISOU 265 N LYS A 67 20633 16053 15882 743 1833 -1144 N ATOM 266 CA LYS A 67 -34.291 10.740 56.753 1.00137.73 C ANISOU 266 CA LYS A 67 20619 16188 15523 617 1656 -1190 C ATOM 267 C LYS A 67 -32.957 10.827 57.541 1.00142.86 C ANISOU 267 C LYS A 67 21517 16799 15963 385 1396 -1416 C ATOM 268 O LYS A 67 -31.902 11.044 56.981 1.00141.58 O ANISOU 268 O LYS A 67 21285 16598 15911 228 1163 -1436 O ATOM 269 CB LYS A 67 -34.330 9.465 55.903 1.00137.06 C ANISOU 269 CB LYS A 67 20192 16369 15514 596 1503 -952 C ATOM 270 CG LYS A 67 -35.575 8.652 56.003 1.00152.08 C ANISOU 270 CG LYS A 67 21957 18445 17380 743 1694 -792 C ATOM 271 CD LYS A 67 -35.306 7.189 55.672 1.00162.01 C ANISOU 271 CD LYS A 67 23012 19951 18592 645 1491 -648 C ATOM 272 CE LYS A 67 -36.491 6.494 54.886 1.00175.84 C ANISOU 272 CE LYS A 67 24452 21871 20489 760 1630 -411 C ATOM 273 NZ LYS A 67 -36.376 5.044 54.414 1.00183.92 N ANISOU 273 NZ LYS A 67 25265 23112 21505 664 1467 -265 N ATOM 274 N LYS A 68 -33.042 10.589 58.851 1.00141.27 N ANISOU 274 N LYS A 68 21589 16640 15446 362 1435 -1567 N ATOM 275 CA LYS A 68 -31.887 10.643 59.738 1.00142.40 C ANISOU 275 CA LYS A 68 21979 16785 15341 146 1190 -1780 C ATOM 276 C LYS A 68 -31.408 9.283 60.271 1.00144.22 C ANISOU 276 C LYS A 68 22169 17299 15328 53 960 -1705 C ATOM 277 O LYS A 68 -30.228 9.087 60.528 1.00143.95 O ANISOU 277 O LYS A 68 22177 17333 15183 -138 659 -1780 O ATOM 278 CB LYS A 68 -32.101 11.648 60.867 1.00148.93 C ANISOU 278 CB LYS A 68 23212 17409 15965 150 1375 -2061 C ATOM 279 CG LYS A 68 -30.969 12.643 61.055 1.00166.58 C ANISOU 279 CG LYS A 68 25653 19448 18192 -69 1196 -2307 C ATOM 280 CD LYS A 68 -31.001 13.735 60.029 1.00175.42 C ANISOU 280 CD LYS A 68 26682 20296 19674 -31 1303 -2291 C ATOM 281 CE LYS A 68 -29.850 14.685 60.216 1.00186.15 C ANISOU 281 CE LYS A 68 28238 21453 21036 -280 1122 -2532 C ATOM 282 NZ LYS A 68 -30.071 15.970 59.491 1.00195.03 N ANISOU 282 NZ LYS A 68 29389 22234 22480 -218 1320 -2560 N ATOM 283 N LEU A 69 -32.308 8.316 60.380 1.00138.77 N ANISOU 283 N LEU A 69 21372 16776 14578 187 1095 -1533 N ATOM 284 CA LEU A 69 -31.882 6.966 60.730 1.00136.74 C ANISOU 284 CA LEU A 69 21048 16765 14143 115 891 -1418 C ATOM 285 C LEU A 69 -31.841 6.103 59.473 1.00134.80 C ANISOU 285 C LEU A 69 20427 16634 14158 132 788 -1174 C ATOM 286 O LEU A 69 -32.851 5.499 59.110 1.00133.24 O ANISOU 286 O LEU A 69 20066 16516 14045 258 964 -1005 O ATOM 287 CB LEU A 69 -32.829 6.353 61.763 1.00138.27 C ANISOU 287 CB LEU A 69 21394 17070 14073 224 1101 -1387 C ATOM 288 N ARG A 70 -30.687 5.980 58.826 1.00127.56 N ANISOU 288 N ARG A 70 19368 15741 13358 -3 505 -1154 N ATOM 289 CA ARG A 70 -30.612 5.161 57.610 1.00122.90 C ANISOU 289 CA ARG A 70 18441 15255 12999 12 419 -943 C ATOM 290 C ARG A 70 -29.677 3.949 57.712 1.00121.59 C ANISOU 290 C ARG A 70 18192 15265 12742 -84 150 -853 C ATOM 291 O ARG A 70 -28.580 4.050 58.259 1.00122.46 O ANISOU 291 O ARG A 70 18411 15398 12719 -211 -78 -951 O ATOM 292 CB ARG A 70 -30.211 6.026 56.412 1.00122.79 C ANISOU 292 CB ARG A 70 18261 15115 13278 -19 376 -941 C ATOM 293 CG ARG A 70 -31.384 6.508 55.574 1.00133.42 C ANISOU 293 CG ARG A 70 19465 16386 14843 138 637 -841 C ATOM 294 CD ARG A 70 -30.970 6.745 54.130 1.00141.33 C ANISOU 294 CD ARG A 70 20202 17369 16128 111 546 -733 C ATOM 295 NE ARG A 70 -29.749 7.540 54.035 1.00149.45 N ANISOU 295 NE ARG A 70 21299 18277 17209 -35 366 -857 N ATOM 296 CZ ARG A 70 -29.650 8.679 53.358 1.00163.62 C ANISOU 296 CZ ARG A 70 23068 19894 19206 -34 427 -878 C ATOM 297 NH1 ARG A 70 -30.702 9.162 52.711 1.00151.81 N ANISOU 297 NH1 ARG A 70 21476 18330 17873 127 657 -773 N ATOM 298 NH2 ARG A 70 -28.499 9.336 53.326 1.00149.21 N ANISOU 298 NH2 ARG A 70 21302 17964 17425 -195 256 -990 N ATOM 299 N SER A 71 -30.112 2.808 57.172 1.00112.62 N ANISOU 299 N SER A 71 16857 14249 11685 -25 178 -663 N ATOM 300 CA SER A 71 -29.243 1.626 57.084 1.00109.80 C ANISOU 300 CA SER A 71 16394 14027 11297 -90 -51 -555 C ATOM 301 C SER A 71 -28.361 1.692 55.829 1.00107.89 C ANISOU 301 C SER A 71 15910 13778 11307 -152 -219 -509 C ATOM 302 O SER A 71 -28.733 2.357 54.865 1.00106.39 O ANISOU 302 O SER A 71 15589 13507 11327 -123 -118 -501 O ATOM 303 CB SER A 71 -30.072 0.346 57.090 1.00112.58 C ANISOU 303 CB SER A 71 16669 14483 11624 -14 67 -384 C ATOM 304 OG SER A 71 -30.975 0.294 55.997 1.00119.76 O ANISOU 304 OG SER A 71 17363 15377 12761 50 230 -289 O ATOM 305 N MET A 72 -27.188 1.030 55.847 1.00101.42 N ANISOU 305 N MET A 72 15026 13046 10462 -228 -466 -468 N ATOM 306 CA MET A 72 -26.244 1.027 54.717 1.00 98.35 C ANISOU 306 CA MET A 72 14405 12666 10296 -286 -622 -421 C ATOM 307 C MET A 72 -26.908 0.682 53.383 1.00 97.19 C ANISOU 307 C MET A 72 14030 12519 10378 -218 -489 -302 C ATOM 308 O MET A 72 -26.601 1.315 52.369 1.00 95.66 O ANISOU 308 O MET A 72 13690 12278 10378 -246 -506 -305 O ATOM 309 CB MET A 72 -25.032 0.118 54.992 1.00100.74 C ANISOU 309 CB MET A 72 14653 13089 10534 -336 -872 -356 C ATOM 310 CG MET A 72 -24.161 0.596 56.139 1.00106.42 C ANISOU 310 CG MET A 72 15551 13840 11044 -436 -1063 -473 C ATOM 311 SD MET A 72 -23.332 2.164 55.796 1.00111.21 S ANISOU 311 SD MET A 72 16145 14336 11772 -585 -1171 -644 S ATOM 312 CE MET A 72 -23.110 2.757 57.434 1.00111.26 C ANISOU 312 CE MET A 72 16479 14352 11444 -683 -1267 -829 C ATOM 313 N THR A 73 -27.863 -0.275 53.406 1.00 90.99 N ANISOU 313 N THR A 73 13223 11789 9559 -142 -351 -199 N ATOM 314 CA THR A 73 -28.647 -0.701 52.243 1.00 87.94 C ANISOU 314 CA THR A 73 12635 11427 9351 -96 -223 -94 C ATOM 315 C THR A 73 -29.425 0.496 51.694 1.00 88.64 C ANISOU 315 C THR A 73 12684 11440 9558 -55 -65 -130 C ATOM 316 O THR A 73 -29.392 0.721 50.485 1.00 86.88 O ANISOU 316 O THR A 73 12270 11222 9517 -58 -65 -79 O ATOM 317 CB THR A 73 -29.568 -1.883 52.599 1.00 97.95 C ANISOU 317 CB THR A 73 13921 12758 10536 -50 -100 5 C ATOM 318 OG1 THR A 73 -28.868 -2.816 53.428 1.00 99.02 O ANISOU 318 OG1 THR A 73 14162 12937 10525 -68 -229 38 O ATOM 319 CG2 THR A 73 -30.113 -2.594 51.364 1.00 95.80 C ANISOU 319 CG2 THR A 73 13429 12536 10437 -47 -32 108 C ATOM 320 N ASP A 74 -30.064 1.295 52.590 1.00 84.46 N ANISOU 320 N ASP A 74 12340 10834 8916 -9 71 -216 N ATOM 321 CA ASP A 74 -30.816 2.499 52.222 1.00 83.66 C ANISOU 321 CA ASP A 74 12229 10632 8925 59 243 -246 C ATOM 322 C ASP A 74 -29.937 3.532 51.521 1.00 85.54 C ANISOU 322 C ASP A 74 12416 10769 9315 0 139 -301 C ATOM 323 O ASP A 74 -30.430 4.221 50.628 1.00 84.91 O ANISOU 323 O ASP A 74 12215 10642 9407 56 246 -247 O ATOM 324 CB ASP A 74 -31.515 3.119 53.429 1.00 87.53 C ANISOU 324 CB ASP A 74 12963 11042 9252 124 414 -348 C ATOM 325 CG ASP A 74 -32.820 2.466 53.806 1.00 99.35 C ANISOU 325 CG ASP A 74 14450 12620 10677 220 622 -258 C ATOM 326 OD1 ASP A 74 -33.747 2.354 53.002 1.00 98.87 O ANISOU 326 OD1 ASP A 74 14194 12610 10762 288 755 -140 O ATOM 327 OD2 ASP A 74 -33.053 2.045 54.973 1.00108.21 O ANISOU 327 OD2 ASP A 74 15760 13772 11581 231 676 -294 O ATOM 328 N LYS A 75 -28.639 3.621 51.896 1.00 80.95 N ANISOU 328 N LYS A 75 11911 10170 8677 -115 -73 -390 N ATOM 329 CA LYS A 75 -27.689 4.545 51.271 1.00 80.14 C ANISOU 329 CA LYS A 75 11751 9978 8722 -201 -185 -438 C ATOM 330 C LYS A 75 -27.380 4.131 49.832 1.00 79.88 C ANISOU 330 C LYS A 75 11440 10026 8884 -207 -240 -301 C ATOM 331 O LYS A 75 -27.370 4.989 48.940 1.00 79.08 O ANISOU 331 O LYS A 75 11242 9850 8954 -205 -191 -271 O ATOM 332 CB LYS A 75 -26.396 4.684 52.098 1.00 84.44 C ANISOU 332 CB LYS A 75 12424 10512 9146 -340 -408 -562 C ATOM 333 CG LYS A 75 -26.493 5.654 53.290 1.00106.38 C ANISOU 333 CG LYS A 75 15496 13157 11767 -378 -363 -750 C ATOM 334 CD LYS A 75 -26.680 7.144 52.895 1.00119.95 C ANISOU 334 CD LYS A 75 17273 14659 13644 -385 -237 -834 C ATOM 335 CE LYS A 75 -25.407 7.855 52.494 1.00129.13 C ANISOU 335 CE LYS A 75 18384 15747 14931 -552 -420 -895 C ATOM 336 NZ LYS A 75 -25.696 9.196 51.916 1.00138.01 N ANISOU 336 NZ LYS A 75 19539 16647 16251 -539 -266 -928 N ATOM 337 N TYR A 76 -27.166 2.812 49.599 1.00 73.23 N ANISOU 337 N TYR A 76 10483 9330 8012 -209 -324 -213 N ATOM 338 CA TYR A 76 -26.908 2.281 48.256 1.00 70.17 C ANISOU 338 CA TYR A 76 9853 9030 7778 -213 -360 -99 C ATOM 339 C TYR A 76 -28.162 2.372 47.403 1.00 72.55 C ANISOU 339 C TYR A 76 10039 9358 8169 -128 -177 -6 C ATOM 340 O TYR A 76 -28.060 2.571 46.196 1.00 71.66 O ANISOU 340 O TYR A 76 9750 9280 8196 -132 -175 68 O ATOM 341 CB TYR A 76 -26.441 0.826 48.304 1.00 69.71 C ANISOU 341 CB TYR A 76 9735 9089 7661 -225 -466 -45 C ATOM 342 CG TYR A 76 -25.058 0.610 48.874 1.00 71.17 C ANISOU 342 CG TYR A 76 9956 9293 7794 -298 -675 -88 C ATOM 343 CD1 TYR A 76 -23.923 1.008 48.174 1.00 72.71 C ANISOU 343 CD1 TYR A 76 10013 9492 8120 -367 -800 -85 C ATOM 344 CD2 TYR A 76 -24.877 -0.077 50.069 1.00 72.74 C ANISOU 344 CD2 TYR A 76 10299 9526 7811 -294 -749 -106 C ATOM 345 CE1 TYR A 76 -22.645 0.796 48.688 1.00 74.36 C ANISOU 345 CE1 TYR A 76 10217 9745 8292 -434 -1000 -107 C ATOM 346 CE2 TYR A 76 -23.604 -0.299 50.591 1.00 74.45 C ANISOU 346 CE2 TYR A 76 10523 9789 7975 -354 -959 -122 C ATOM 347 CZ TYR A 76 -22.489 0.129 49.892 1.00 80.34 C ANISOU 347 CZ TYR A 76 11113 10547 8865 -424 -1088 -122 C ATOM 348 OH TYR A 76 -21.232 -0.101 50.397 1.00 81.61 O ANISOU 348 OH TYR A 76 11245 10778 8985 -482 -1301 -122 O ATOM 349 N ARG A 77 -29.348 2.244 48.036 1.00 68.79 N ANISOU 349 N ARG A 77 9651 8883 7605 -51 -23 -1 N ATOM 350 CA ARG A 77 -30.643 2.337 47.364 1.00 67.51 C ANISOU 350 CA ARG A 77 9364 8770 7517 33 151 98 C ATOM 351 C ARG A 77 -30.951 3.762 46.907 1.00 72.59 C ANISOU 351 C ARG A 77 9988 9307 8286 93 251 110 C ATOM 352 O ARG A 77 -31.755 3.931 45.992 1.00 72.64 O ANISOU 352 O ARG A 77 9827 9379 8394 157 349 226 O ATOM 353 CB ARG A 77 -31.768 1.721 48.206 1.00 65.87 C ANISOU 353 CB ARG A 77 9232 8608 7188 92 290 114 C ATOM 354 CG ARG A 77 -31.773 0.189 48.160 1.00 69.07 C ANISOU 354 CG ARG A 77 9578 9132 7533 41 233 167 C ATOM 355 CD ARG A 77 -32.814 -0.440 49.074 1.00 74.03 C ANISOU 355 CD ARG A 77 10292 9797 8040 79 373 191 C ATOM 356 NE ARG A 77 -34.083 -0.692 48.386 1.00 75.76 N ANISOU 356 NE ARG A 77 10331 10117 8339 109 516 298 N ATOM 357 CZ ARG A 77 -35.143 -1.277 48.938 1.00 88.89 C ANISOU 357 CZ ARG A 77 12001 11837 9936 130 659 350 C ATOM 358 NH1 ARG A 77 -35.105 -1.683 50.201 1.00 79.54 N ANISOU 358 NH1 ARG A 77 11015 10614 8592 135 693 310 N ATOM 359 NH2 ARG A 77 -36.249 -1.460 48.232 1.00 75.27 N ANISOU 359 NH2 ARG A 77 10077 10225 8298 139 767 451 N ATOM 360 N LEU A 78 -30.275 4.778 47.501 1.00 69.87 N ANISOU 360 N LEU A 78 9810 8800 7939 64 220 -5 N ATOM 361 CA LEU A 78 -30.405 6.183 47.106 1.00 70.68 C ANISOU 361 CA LEU A 78 9926 8750 8179 111 315 -1 C ATOM 362 C LEU A 78 -29.575 6.416 45.830 1.00 75.46 C ANISOU 362 C LEU A 78 10352 9381 8939 44 205 79 C ATOM 363 O LEU A 78 -30.080 7.016 44.877 1.00 75.45 O ANISOU 363 O LEU A 78 10221 9375 9072 114 300 200 O ATOM 364 CB LEU A 78 -29.965 7.136 48.238 1.00 72.48 C ANISOU 364 CB LEU A 78 10423 8775 8340 76 325 -176 C ATOM 365 CG LEU A 78 -29.875 8.635 47.892 1.00 77.95 C ANISOU 365 CG LEU A 78 11171 9254 9192 96 414 -196 C ATOM 366 CD1 LEU A 78 -31.254 9.275 47.782 1.00 78.88 C ANISOU 366 CD1 LEU A 78 11286 9302 9383 284 673 -115 C ATOM 367 CD2 LEU A 78 -29.046 9.377 48.904 1.00 81.73 C ANISOU 367 CD2 LEU A 78 11907 9548 9599 -17 347 -401 C ATOM 368 N HIS A 79 -28.309 5.921 45.811 1.00 71.92 N ANISOU 368 N HIS A 79 9886 8974 8468 -84 10 29 N ATOM 369 CA HIS A 79 -27.393 5.998 44.659 1.00 70.64 C ANISOU 369 CA HIS A 79 9548 8857 8435 -156 -94 101 C ATOM 370 C HIS A 79 -28.062 5.387 43.436 1.00 73.62 C ANISOU 370 C HIS A 79 9711 9401 8861 -94 -37 253 C ATOM 371 O HIS A 79 -28.060 5.989 42.361 1.00 73.65 O ANISOU 371 O HIS A 79 9585 9411 8985 -79 -1 357 O ATOM 372 CB HIS A 79 -26.095 5.230 44.952 1.00 70.60 C ANISOU 372 CB HIS A 79 9533 8917 8374 -271 -294 38 C ATOM 373 CG HIS A 79 -25.095 6.028 45.710 1.00 75.35 C ANISOU 373 CG HIS A 79 10270 9386 8974 -381 -401 -86 C ATOM 374 ND1 HIS A 79 -24.217 6.867 45.063 1.00 77.71 N ANISOU 374 ND1 HIS A 79 10491 9613 9421 -471 -455 -71 N ATOM 375 CD2 HIS A 79 -24.873 6.103 47.041 1.00 78.58 C ANISOU 375 CD2 HIS A 79 10884 9732 9242 -428 -464 -225 C ATOM 376 CE1 HIS A 79 -23.477 7.411 46.010 1.00 78.78 C ANISOU 376 CE1 HIS A 79 10777 9642 9514 -584 -557 -209 C ATOM 377 NE2 HIS A 79 -23.833 6.982 47.216 1.00 79.77 N ANISOU 377 NE2 HIS A 79 11079 9776 9453 -562 -573 -310 N ATOM 378 N LEU A 80 -28.684 4.207 43.642 1.00 69.01 N ANISOU 378 N LEU A 80 9101 8948 8172 -66 -25 266 N ATOM 379 CA LEU A 80 -29.404 3.433 42.648 1.00 67.75 C ANISOU 379 CA LEU A 80 8760 8960 8022 -38 17 378 C ATOM 380 C LEU A 80 -30.596 4.222 42.113 1.00 73.46 C ANISOU 380 C LEU A 80 9401 9697 8815 65 169 490 C ATOM 381 O LEU A 80 -30.889 4.127 40.926 1.00 72.81 O ANISOU 381 O LEU A 80 9137 9744 8782 72 176 606 O ATOM 382 CB LEU A 80 -29.846 2.101 43.281 1.00 66.98 C ANISOU 382 CB LEU A 80 8702 8947 7799 -47 13 345 C ATOM 383 CG LEU A 80 -30.500 1.044 42.394 1.00 69.94 C ANISOU 383 CG LEU A 80 8917 9494 8164 -62 35 423 C ATOM 384 CD1 LEU A 80 -29.685 0.765 41.154 1.00 69.19 C ANISOU 384 CD1 LEU A 80 8682 9481 8127 -121 -54 455 C ATOM 385 CD2 LEU A 80 -30.699 -0.233 43.162 1.00 70.82 C ANISOU 385 CD2 LEU A 80 9107 9633 8169 -91 25 379 C ATOM 386 N SER A 81 -31.247 5.028 42.976 1.00 71.63 N ANISOU 386 N SER A 81 9301 9334 8581 150 291 460 N ATOM 387 CA SER A 81 -32.386 5.864 42.598 1.00 72.55 C ANISOU 387 CA SER A 81 9343 9442 8780 281 455 579 C ATOM 388 C SER A 81 -31.936 7.064 41.758 1.00 76.81 C ANISOU 388 C SER A 81 9835 9882 9468 303 464 659 C ATOM 389 O SER A 81 -32.696 7.521 40.902 1.00 76.48 O ANISOU 389 O SER A 81 9643 9910 9507 398 551 821 O ATOM 390 CB SER A 81 -33.138 6.331 43.839 1.00 77.84 C ANISOU 390 CB SER A 81 10188 9983 9405 379 605 510 C ATOM 391 OG SER A 81 -34.390 6.897 43.496 1.00 87.93 O ANISOU 391 OG SER A 81 11357 11291 10760 529 779 647 O ATOM 392 N VAL A 82 -30.700 7.562 41.987 1.00 73.72 N ANISOU 392 N VAL A 82 9559 9339 9112 208 372 560 N ATOM 393 CA VAL A 82 -30.123 8.686 41.229 1.00 74.07 C ANISOU 393 CA VAL A 82 9571 9265 9306 198 379 632 C ATOM 394 C VAL A 82 -29.817 8.247 39.783 1.00 75.75 C ANISOU 394 C VAL A 82 9554 9675 9552 159 304 776 C ATOM 395 O VAL A 82 -30.122 8.992 38.847 1.00 75.28 O ANISOU 395 O VAL A 82 9387 9622 9593 225 374 936 O ATOM 396 CB VAL A 82 -28.904 9.339 41.946 1.00 78.54 C ANISOU 396 CB VAL A 82 10320 9618 9905 79 300 477 C ATOM 397 CG1 VAL A 82 -28.301 10.470 41.119 1.00 79.10 C ANISOU 397 CG1 VAL A 82 10350 9559 10148 48 318 565 C ATOM 398 CG2 VAL A 82 -29.299 9.857 43.325 1.00 79.96 C ANISOU 398 CG2 VAL A 82 10748 9606 10028 120 392 326 C ATOM 399 N ALA A 83 -29.260 7.024 39.614 1.00 70.83 N ANISOU 399 N ALA A 83 8865 9212 8835 62 174 723 N ATOM 400 CA ALA A 83 -28.940 6.429 38.314 1.00 69.93 C ANISOU 400 CA ALA A 83 8560 9293 8716 16 110 820 C ATOM 401 C ALA A 83 -30.215 6.233 37.483 1.00 75.76 C ANISOU 401 C ALA A 83 9143 10216 9428 104 189 970 C ATOM 402 O ALA A 83 -30.270 6.682 36.336 1.00 75.56 O ANISOU 402 O ALA A 83 8982 10278 9450 126 206 1118 O ATOM 403 CB ALA A 83 -28.229 5.099 38.510 1.00 69.20 C ANISOU 403 CB ALA A 83 8464 9300 8528 -78 -12 712 C ATOM 404 N ASP A 84 -31.252 5.618 38.098 1.00 73.93 N ANISOU 404 N ASP A 84 8926 10047 9119 150 238 942 N ATOM 405 CA ASP A 84 -32.562 5.332 37.512 1.00 74.73 C ANISOU 405 CA ASP A 84 8867 10340 9187 216 303 1071 C ATOM 406 C ASP A 84 -33.358 6.590 37.137 1.00 81.26 C ANISOU 406 C ASP A 84 9624 11131 10118 362 424 1244 C ATOM 407 O ASP A 84 -34.005 6.584 36.091 1.00 81.55 O ANISOU 407 O ASP A 84 9471 11366 10149 396 429 1407 O ATOM 408 CB ASP A 84 -33.380 4.409 38.435 1.00 76.74 C ANISOU 408 CB ASP A 84 9166 10640 9350 216 337 992 C ATOM 409 CG ASP A 84 -32.789 3.023 38.690 1.00 89.01 C ANISOU 409 CG ASP A 84 10769 12248 10804 89 232 860 C ATOM 410 OD1 ASP A 84 -31.720 2.709 38.109 1.00 88.95 O ANISOU 410 OD1 ASP A 84 10747 12257 10795 7 131 823 O ATOM 411 OD2 ASP A 84 -33.380 2.262 39.496 1.00 95.98 O ANISOU 411 OD2 ASP A 84 11706 13146 11616 79 265 803 O ATOM 412 N LEU A 85 -33.309 7.661 37.967 1.00 79.33 N ANISOU 412 N LEU A 85 9538 10638 9967 447 522 1212 N ATOM 413 CA LEU A 85 -34.010 8.919 37.671 1.00 81.07 C ANISOU 413 CA LEU A 85 9717 10773 10314 609 663 1380 C ATOM 414 C LEU A 85 -33.378 9.616 36.472 1.00 85.45 C ANISOU 414 C LEU A 85 10181 11333 10953 596 627 1525 C ATOM 415 O LEU A 85 -34.094 10.162 35.630 1.00 86.22 O ANISOU 415 O LEU A 85 10127 11528 11106 712 691 1742 O ATOM 416 CB LEU A 85 -34.049 9.870 38.885 1.00 82.60 C ANISOU 416 CB LEU A 85 10138 10661 10583 695 794 1278 C ATOM 417 CG LEU A 85 -34.879 11.161 38.708 1.00 89.69 C ANISOU 417 CG LEU A 85 11016 11430 11630 897 980 1448 C ATOM 418 CD1 LEU A 85 -36.366 10.916 38.943 1.00 90.69 C ANISOU 418 CD1 LEU A 85 11022 11701 11736 1054 1106 1549 C ATOM 419 CD2 LEU A 85 -34.381 12.263 39.616 1.00 93.71 C ANISOU 419 CD2 LEU A 85 11793 11577 12237 924 1081 1318 C ATOM 420 N LEU A 86 -32.035 9.580 36.391 1.00 81.56 N ANISOU 420 N LEU A 86 9768 10752 10468 457 525 1422 N ATOM 421 CA LEU A 86 -31.276 10.180 35.297 1.00 81.80 C ANISOU 421 CA LEU A 86 9723 10784 10574 419 495 1550 C ATOM 422 C LEU A 86 -31.566 9.477 33.986 1.00 84.82 C ANISOU 422 C LEU A 86 9885 11487 10857 399 430 1691 C ATOM 423 O LEU A 86 -31.655 10.139 32.960 1.00 85.17 O ANISOU 423 O LEU A 86 9817 11594 10948 453 462 1893 O ATOM 424 CB LEU A 86 -29.776 10.179 35.609 1.00 81.38 C ANISOU 424 CB LEU A 86 9784 10588 10548 262 400 1396 C ATOM 425 CG LEU A 86 -29.156 11.537 35.976 1.00 88.16 C ANISOU 425 CG LEU A 86 10789 11135 11571 255 466 1387 C ATOM 426 CD1 LEU A 86 -29.771 12.130 37.264 1.00 89.55 C ANISOU 426 CD1 LEU A 86 11166 11073 11786 341 576 1275 C ATOM 427 CD2 LEU A 86 -27.654 11.415 36.130 1.00 90.41 C ANISOU 427 CD2 LEU A 86 11127 11348 11877 73 346 1257 C ATOM 428 N PHE A 87 -31.776 8.152 34.023 1.00 80.25 N ANISOU 428 N PHE A 87 9250 11107 10133 323 346 1590 N ATOM 429 CA PHE A 87 -32.114 7.402 32.821 1.00 79.76 C ANISOU 429 CA PHE A 87 9000 11353 9953 282 282 1687 C ATOM 430 C PHE A 87 -33.540 7.731 32.352 1.00 84.22 C ANISOU 430 C PHE A 87 9406 12084 10509 410 346 1888 C ATOM 431 O PHE A 87 -33.718 8.084 31.186 1.00 84.45 O ANISOU 431 O PHE A 87 9290 12282 10516 439 335 2079 O ATOM 432 CB PHE A 87 -31.913 5.887 33.019 1.00 80.22 C ANISOU 432 CB PHE A 87 9067 11538 9875 154 188 1508 C ATOM 433 CG PHE A 87 -32.372 5.050 31.843 1.00 82.17 C ANISOU 433 CG PHE A 87 9145 12093 9983 92 129 1571 C ATOM 434 CD1 PHE A 87 -33.562 4.332 31.901 1.00 85.89 C ANISOU 434 CD1 PHE A 87 9527 12738 10369 86 126 1577 C ATOM 435 CD2 PHE A 87 -31.638 5.017 30.664 1.00 84.65 C ANISOU 435 CD2 PHE A 87 9389 12531 10245 31 83 1626 C ATOM 436 CE1 PHE A 87 -34.001 3.584 30.803 1.00 87.22 C ANISOU 436 CE1 PHE A 87 9547 13197 10398 1 60 1620 C ATOM 437 CE2 PHE A 87 -32.084 4.277 29.566 1.00 87.94 C ANISOU 437 CE2 PHE A 87 9669 13238 10506 -36 31 1669 C ATOM 438 CZ PHE A 87 -33.257 3.561 29.644 1.00 86.27 C ANISOU 438 CZ PHE A 87 9379 13194 10207 -59 11 1657 C ATOM 439 N VAL A 88 -34.544 7.629 33.263 1.00 80.78 N ANISOU 439 N VAL A 88 8990 11616 10088 490 416 1859 N ATOM 440 CA VAL A 88 -35.962 7.890 32.965 1.00 81.66 C ANISOU 440 CA VAL A 88 8925 11896 10205 621 483 2051 C ATOM 441 C VAL A 88 -36.233 9.264 32.348 1.00 86.77 C ANISOU 441 C VAL A 88 9501 12491 10978 789 572 2304 C ATOM 442 O VAL A 88 -37.050 9.358 31.437 1.00 87.62 O ANISOU 442 O VAL A 88 9395 12847 11047 855 558 2520 O ATOM 443 CB VAL A 88 -36.987 7.496 34.074 1.00 85.46 C ANISOU 443 CB VAL A 88 9423 12362 10686 679 562 1981 C ATOM 444 CG1 VAL A 88 -36.862 6.025 34.459 1.00 83.50 C ANISOU 444 CG1 VAL A 88 9209 12215 10303 507 470 1784 C ATOM 445 CG2 VAL A 88 -36.889 8.394 35.302 1.00 85.81 C ANISOU 445 CG2 VAL A 88 9673 12075 10855 798 703 1908 C ATOM 446 N ILE A 89 -35.493 10.309 32.792 1.00 83.44 N ANISOU 446 N ILE A 89 9255 11748 10700 844 654 2282 N ATOM 447 CA ILE A 89 -35.615 11.678 32.277 1.00 85.28 C ANISOU 447 CA ILE A 89 9463 11857 11081 1001 760 2517 C ATOM 448 C ILE A 89 -35.227 11.791 30.773 1.00 87.84 C ANISOU 448 C ILE A 89 9635 12393 11349 958 677 2716 C ATOM 449 O ILE A 89 -35.468 12.824 30.146 1.00 89.27 O ANISOU 449 O ILE A 89 9752 12538 11629 1096 755 2967 O ATOM 450 CB ILE A 89 -34.932 12.710 33.231 1.00 89.51 C ANISOU 450 CB ILE A 89 10255 11968 11786 1038 875 2406 C ATOM 451 CG1 ILE A 89 -35.587 14.107 33.146 1.00 93.42 C ANISOU 451 CG1 ILE A 89 10752 12275 12466 1267 1056 2632 C ATOM 452 CG2 ILE A 89 -33.402 12.763 33.075 1.00 88.93 C ANISOU 452 CG2 ILE A 89 10304 11760 11726 858 787 2282 C ATOM 453 CD1 ILE A 89 -35.403 15.009 34.414 1.00105.13 C ANISOU 453 CD1 ILE A 89 12509 13332 14103 1336 1214 2479 C ATOM 454 N THR A 90 -34.664 10.701 30.202 1.00 81.41 N ANISOU 454 N THR A 90 8766 11799 10365 775 531 2608 N ATOM 455 CA THR A 90 -34.280 10.606 28.790 1.00 80.71 C ANISOU 455 CA THR A 90 8545 11949 10171 712 452 2757 C ATOM 456 C THR A 90 -35.241 9.705 27.998 1.00 84.09 C ANISOU 456 C THR A 90 8760 12785 10407 680 355 2835 C ATOM 457 O THR A 90 -35.161 9.669 26.768 1.00 84.69 O ANISOU 457 O THR A 90 8711 13106 10363 646 291 2986 O ATOM 458 CB THR A 90 -32.791 10.236 28.598 1.00 80.37 C ANISOU 458 CB THR A 90 8609 11832 10095 539 387 2594 C ATOM 459 OG1 THR A 90 -32.579 8.843 28.846 1.00 75.41 O ANISOU 459 OG1 THR A 90 7996 11334 9324 392 286 2360 O ATOM 460 CG2 THR A 90 -31.844 11.108 29.424 1.00 76.69 C ANISOU 460 CG2 THR A 90 8338 10982 9818 536 461 2507 C ATOM 461 N LEU A 91 -36.172 9.009 28.695 1.00 79.09 N ANISOU 461 N LEU A 91 8084 12229 9737 683 346 2739 N ATOM 462 CA LEU A 91 -37.167 8.146 28.052 1.00 79.17 C ANISOU 462 CA LEU A 91 7886 12617 9578 626 251 2798 C ATOM 463 C LEU A 91 -38.120 8.865 27.087 1.00 85.68 C ANISOU 463 C LEU A 91 8479 13688 10386 767 251 3135 C ATOM 464 O LEU A 91 -38.467 8.242 26.086 1.00 85.29 O ANISOU 464 O LEU A 91 8267 13991 10148 667 129 3198 O ATOM 465 CB LEU A 91 -37.915 7.240 29.035 1.00 78.41 C ANISOU 465 CB LEU A 91 7791 12539 9463 579 252 2629 C ATOM 466 CG LEU A 91 -37.130 6.052 29.621 1.00 80.75 C ANISOU 466 CG LEU A 91 8251 12744 9684 390 193 2318 C ATOM 467 CD1 LEU A 91 -37.882 5.431 30.761 1.00 80.55 C ANISOU 467 CD1 LEU A 91 8254 12671 9680 384 236 2194 C ATOM 468 CD2 LEU A 91 -36.833 4.979 28.565 1.00 82.40 C ANISOU 468 CD2 LEU A 91 8391 13223 9695 200 59 2244 C ATOM 469 N PRO A 92 -38.513 10.161 27.278 1.00 85.05 N ANISOU 469 N PRO A 92 8382 13444 10490 995 382 3362 N ATOM 470 CA PRO A 92 -39.349 10.824 26.256 1.00 87.87 C ANISOU 470 CA PRO A 92 8504 14058 10824 1142 371 3718 C ATOM 471 C PRO A 92 -38.624 10.938 24.907 1.00 93.11 C ANISOU 471 C PRO A 92 9132 14900 11346 1061 281 3845 C ATOM 472 O PRO A 92 -39.267 10.836 23.864 1.00 94.23 O ANISOU 472 O PRO A 92 9059 15412 11333 1068 184 4058 O ATOM 473 CB PRO A 92 -39.621 12.211 26.859 1.00 91.19 C ANISOU 473 CB PRO A 92 8987 14158 11503 1405 562 3895 C ATOM 474 CG PRO A 92 -39.378 12.051 28.319 1.00 93.85 C ANISOU 474 CG PRO A 92 9541 14160 11957 1388 660 3610 C ATOM 475 CD PRO A 92 -38.239 11.089 28.396 1.00 86.71 C ANISOU 475 CD PRO A 92 8788 13230 10928 1134 547 3312 C ATOM 476 N PHE A 93 -37.274 11.104 24.936 1.00 89.34 N ANISOU 476 N PHE A 93 8859 14180 10907 972 309 3709 N ATOM 477 CA PHE A 93 -36.407 11.187 23.747 1.00 89.82 C ANISOU 477 CA PHE A 93 8915 14373 10840 883 253 3799 C ATOM 478 C PHE A 93 -36.394 9.855 23.010 1.00 92.22 C ANISOU 478 C PHE A 93 9138 15042 10861 675 95 3654 C ATOM 479 O PHE A 93 -36.474 9.848 21.783 1.00 93.18 O ANISOU 479 O PHE A 93 9136 15471 10798 646 22 3828 O ATOM 480 CB PHE A 93 -34.975 11.603 24.118 1.00 90.68 C ANISOU 480 CB PHE A 93 9248 14126 11082 823 330 3661 C ATOM 481 CG PHE A 93 -34.867 12.947 24.790 1.00 93.74 C ANISOU 481 CG PHE A 93 9750 14123 11745 992 489 3778 C ATOM 482 CD1 PHE A 93 -34.752 14.111 24.039 1.00 99.19 C ANISOU 482 CD1 PHE A 93 10407 14758 12522 1118 570 4090 C ATOM 483 CD2 PHE A 93 -34.865 13.050 26.177 1.00 95.37 C ANISOU 483 CD2 PHE A 93 10113 14005 12116 1020 566 3571 C ATOM 484 CE1 PHE A 93 -34.648 15.358 24.663 1.00101.49 C ANISOU 484 CE1 PHE A 93 10829 14650 13083 1265 733 4185 C ATOM 485 CE2 PHE A 93 -34.759 14.297 26.801 1.00 99.60 C ANISOU 485 CE2 PHE A 93 10784 14162 12898 1163 722 3650 C ATOM 486 CZ PHE A 93 -34.647 15.443 26.039 1.00 99.91 C ANISOU 486 CZ PHE A 93 10795 14124 13042 1281 809 3950 C ATOM 487 N TRP A 94 -36.312 8.734 23.770 1.00 86.15 N ANISOU 487 N TRP A 94 8449 14231 10053 532 50 3337 N ATOM 488 CA TRP A 94 -36.373 7.353 23.282 1.00 85.16 C ANISOU 488 CA TRP A 94 8280 14390 9687 326 -80 3147 C ATOM 489 C TRP A 94 -37.768 7.114 22.674 1.00 91.49 C ANISOU 489 C TRP A 94 8837 15580 10344 335 -177 3319 C ATOM 490 O TRP A 94 -37.879 6.502 21.606 1.00 92.29 O ANISOU 490 O TRP A 94 8846 16021 10201 200 -294 3327 O ATOM 491 CB TRP A 94 -36.209 6.378 24.461 1.00 81.60 C ANISOU 491 CB TRP A 94 7964 13750 9288 221 -77 2823 C ATOM 492 CG TRP A 94 -34.808 6.080 24.894 1.00 80.44 C ANISOU 492 CG TRP A 94 8027 13341 9195 136 -44 2594 C ATOM 493 CD1 TRP A 94 -33.975 6.898 25.596 1.00 82.79 C ANISOU 493 CD1 TRP A 94 8469 13299 9690 215 48 2580 C ATOM 494 CD2 TRP A 94 -34.144 4.812 24.804 1.00 78.81 C ANISOU 494 CD2 TRP A 94 7907 13179 8860 -44 -104 2331 C ATOM 495 NE1 TRP A 94 -32.798 6.243 25.881 1.00 80.66 N ANISOU 495 NE1 TRP A 94 8340 12894 9412 94 33 2346 N ATOM 496 CE2 TRP A 94 -32.878 4.958 25.408 1.00 81.45 C ANISOU 496 CE2 TRP A 94 8410 13216 9321 -50 -49 2197 C ATOM 497 CE3 TRP A 94 -34.480 3.573 24.231 1.00 80.01 C ANISOU 497 CE3 TRP A 94 8010 13588 8802 -206 -194 2198 C ATOM 498 CZ2 TRP A 94 -31.948 3.913 25.455 1.00 79.37 C ANISOU 498 CZ2 TRP A 94 8249 12915 8991 -182 -76 1959 C ATOM 499 CZ3 TRP A 94 -33.557 2.542 24.274 1.00 79.97 C ANISOU 499 CZ3 TRP A 94 8137 13513 8734 -340 -205 1944 C ATOM 500 CH2 TRP A 94 -32.308 2.716 24.878 1.00 79.23 C ANISOU 500 CH2 TRP A 94 8194 13131 8779 -313 -144 1839 C ATOM 501 N ALA A 95 -38.826 7.607 23.377 1.00 88.69 N ANISOU 501 N ALA A 95 8377 15179 10140 491 -123 3452 N ATOM 502 CA ALA A 95 -40.234 7.481 23.006 1.00 90.48 C ANISOU 502 CA ALA A 95 8338 15756 10284 526 -202 3638 C ATOM 503 C ALA A 95 -40.574 8.150 21.686 1.00 97.08 C ANISOU 503 C ALA A 95 8985 16909 10993 607 -272 3978 C ATOM 504 O ALA A 95 -41.252 7.531 20.871 1.00 98.86 O ANISOU 504 O ALA A 95 9023 17545 10993 487 -423 4030 O ATOM 505 CB ALA A 95 -41.129 8.015 24.114 1.00 91.58 C ANISOU 505 CB ALA A 95 8422 15724 10652 717 -85 3721 C ATOM 506 N VAL A 96 -40.123 9.403 21.472 1.00 93.71 N ANISOU 506 N VAL A 96 8606 16298 10701 800 -165 4213 N ATOM 507 CA VAL A 96 -40.390 10.150 20.233 1.00 96.00 C ANISOU 507 CA VAL A 96 8730 16863 10881 906 -213 4581 C ATOM 508 C VAL A 96 -39.669 9.486 19.051 1.00 98.91 C ANISOU 508 C VAL A 96 9131 17503 10946 692 -337 4499 C ATOM 509 O VAL A 96 -40.294 9.241 18.015 1.00100.38 O ANISOU 509 O VAL A 96 9126 18128 10887 637 -480 4660 O ATOM 510 CB VAL A 96 -40.069 11.671 20.366 1.00101.04 C ANISOU 510 CB VAL A 96 9438 17184 11770 1167 -41 4856 C ATOM 511 CG1 VAL A 96 -40.174 12.396 19.023 1.00103.79 C ANISOU 511 CG1 VAL A 96 9644 17805 11987 1264 -86 5244 C ATOM 512 CG2 VAL A 96 -40.973 12.340 21.400 1.00101.66 C ANISOU 512 CG2 VAL A 96 9461 17048 12118 1401 89 4965 C ATOM 513 N ASP A 97 -38.373 9.157 19.244 1.00 92.87 N ANISOU 513 N ASP A 97 8605 16489 10193 569 -281 4238 N ATOM 514 CA ASP A 97 -37.476 8.515 18.277 1.00 92.31 C ANISOU 514 CA ASP A 97 8612 16592 9870 378 -346 4111 C ATOM 515 C ASP A 97 -38.038 7.214 17.693 1.00 96.93 C ANISOU 515 C ASP A 97 9103 17575 10151 158 -515 3940 C ATOM 516 O ASP A 97 -37.784 6.913 16.527 1.00 97.77 O ANISOU 516 O ASP A 97 9186 17983 9980 46 -595 3970 O ATOM 517 CB ASP A 97 -36.094 8.302 18.913 1.00 91.29 C ANISOU 517 CB ASP A 97 8733 16082 9870 303 -241 3831 C ATOM 518 CG ASP A 97 -35.192 7.310 18.213 1.00101.05 C ANISOU 518 CG ASP A 97 10066 17456 10873 94 -288 3599 C ATOM 519 OD1 ASP A 97 -35.160 6.136 18.644 1.00 99.60 O ANISOU 519 OD1 ASP A 97 9949 17268 10627 -61 -337 3286 O ATOM 520 OD2 ASP A 97 -34.503 7.710 17.247 1.00109.30 O ANISOU 520 OD2 ASP A 97 11126 18599 11803 92 -260 3734 O ATOM 521 N ALA A 98 -38.803 6.473 18.488 1.00 92.97 N ANISOU 521 N ALA A 98 8554 17072 9698 89 -562 3764 N ATOM 522 CA ALA A 98 -39.463 5.269 18.000 1.00 93.61 C ANISOU 522 CA ALA A 98 8536 17513 9519 -136 -722 3606 C ATOM 523 C ALA A 98 -40.431 5.640 16.882 1.00101.24 C ANISOU 523 C ALA A 98 9242 18952 10274 -109 -860 3925 C ATOM 524 O ALA A 98 -40.339 5.124 15.769 1.00102.99 O ANISOU 524 O ALA A 98 9440 19511 10181 -274 -979 3894 O ATOM 525 CB ALA A 98 -40.196 4.569 19.131 1.00 93.08 C ANISOU 525 CB ALA A 98 8445 17338 9585 -193 -726 3417 C ATOM 526 N VAL A 99 -41.360 6.540 17.187 1.00 99.39 N ANISOU 526 N VAL A 99 8813 18745 10206 108 -842 4234 N ATOM 527 CA VAL A 99 -42.347 6.984 16.210 1.00103.06 C ANISOU 527 CA VAL A 99 8995 19662 10500 173 -977 4589 C ATOM 528 C VAL A 99 -42.128 8.080 15.172 1.00109.19 C ANISOU 528 C VAL A 99 9706 20590 11189 343 -972 4975 C ATOM 529 O VAL A 99 -42.556 7.957 14.024 1.00111.23 O ANISOU 529 O VAL A 99 9805 21311 11145 266 -1134 5143 O ATOM 530 CB VAL A 99 -43.553 7.657 16.891 1.00108.45 C ANISOU 530 CB VAL A 99 9444 20343 11418 398 -944 4851 C ATOM 531 N ALA A 100 -41.458 9.152 15.583 1.00105.49 N ANISOU 531 N ALA A 100 9370 19732 10981 563 -786 5116 N ATOM 532 CA ALA A 100 -41.181 10.271 14.691 1.00108.17 C ANISOU 532 CA ALA A 100 9673 20142 11284 739 -746 5500 C ATOM 533 C ALA A 100 -39.677 10.241 14.938 1.00111.47 C ANISOU 533 C ALA A 100 10397 20174 11783 663 -604 5254 C ATOM 534 O ALA A 100 -39.204 9.584 15.865 1.00109.78 O ANISOU 534 O ALA A 100 10347 19675 11691 553 -550 4893 O ATOM 535 CB ALA A 100 -41.399 11.648 15.299 1.00109.61 C ANISOU 535 CB ALA A 100 9832 19995 11821 1066 -573 5812 C ATOM 536 N ASN A 101 -38.930 10.958 14.104 1.00108.89 N ANISOU 536 N ASN A 101 10134 19851 11389 725 -543 5467 N ATOM 537 CA ASN A 101 -37.479 11.014 14.231 1.00106.69 C ANISOU 537 CA ASN A 101 10108 19240 11188 655 -405 5280 C ATOM 538 C ASN A 101 -36.692 12.007 15.079 1.00109.16 C ANISOU 538 C ASN A 101 10587 19016 11874 804 -200 5314 C ATOM 539 O ASN A 101 -37.267 12.760 15.864 1.00109.42 O ANISOU 539 O ASN A 101 10583 18810 12181 996 -121 5453 O ATOM 540 CB ASN A 101 -37.163 11.222 12.748 1.00109.31 C ANISOU 540 CB ASN A 101 10396 19930 11207 620 -455 5514 C ATOM 541 CG ASN A 101 -36.940 12.680 12.399 1.00123.30 C ANISOU 541 CG ASN A 101 12157 21556 13138 852 -324 5945 C ATOM 542 OD1 ASN A 101 -37.527 13.574 13.011 1.00114.31 O ANISOU 542 OD1 ASN A 101 10952 20201 12281 1074 -251 6168 O ATOM 543 ND2 ASN A 101 -36.089 12.929 11.411 1.00114.48 N ANISOU 543 ND2 ASN A 101 11111 20543 11844 806 -278 6067 N ATOM 544 N TRP A 102 -35.373 12.003 14.914 1.00103.90 N ANISOU 544 N TRP A 102 10101 18162 11214 707 -109 5182 N ATOM 545 CA TRP A 102 -34.504 12.902 15.664 1.00102.60 C ANISOU 545 CA TRP A 102 10098 17499 11386 797 71 5190 C ATOM 546 C TRP A 102 -34.798 14.361 15.331 1.00110.11 C ANISOU 546 C TRP A 102 10990 18349 12496 1032 175 5639 C ATOM 547 O TRP A 102 -34.758 14.762 14.168 1.00113.02 O ANISOU 547 O TRP A 102 11281 18977 12683 1066 161 5938 O ATOM 548 CB TRP A 102 -33.034 12.584 15.384 1.00 99.95 C ANISOU 548 CB TRP A 102 9921 17056 11000 633 136 4996 C ATOM 549 CG TRP A 102 -32.178 12.574 16.612 1.00 98.07 C ANISOU 549 CG TRP A 102 9857 16357 11047 588 232 4715 C ATOM 550 CD1 TRP A 102 -30.983 13.210 16.784 1.00100.57 C ANISOU 550 CD1 TRP A 102 10302 16358 11552 568 364 4716 C ATOM 551 CD2 TRP A 102 -32.450 11.894 17.844 1.00 95.43 C ANISOU 551 CD2 TRP A 102 9583 15845 10832 546 196 4400 C ATOM 552 NE1 TRP A 102 -30.494 12.968 18.045 1.00 97.41 N ANISOU 552 NE1 TRP A 102 10031 15610 11370 513 395 4416 N ATOM 553 CE2 TRP A 102 -31.377 12.163 18.716 1.00 97.60 C ANISOU 553 CE2 TRP A 102 10024 15709 11349 507 297 4223 C ATOM 554 CE3 TRP A 102 -33.498 11.085 18.294 1.00 96.13 C ANISOU 554 CE3 TRP A 102 9593 16089 10842 528 87 4260 C ATOM 555 CZ2 TRP A 102 -31.320 11.652 20.011 1.00 94.56 C ANISOU 555 CZ2 TRP A 102 9741 15080 11109 463 288 3918 C ATOM 556 CZ3 TRP A 102 -33.440 10.578 19.580 1.00 95.13 C ANISOU 556 CZ3 TRP A 102 9571 15701 10872 486 98 3962 C ATOM 557 CH2 TRP A 102 -32.359 10.864 20.423 1.00 94.01 C ANISOU 557 CH2 TRP A 102 9605 15163 10950 460 194 3798 C ATOM 558 N TYR A 103 -35.092 15.150 16.359 1.00106.48 N ANISOU 558 N TYR A 103 10580 17505 12373 1196 288 5687 N ATOM 559 CA TYR A 103 -35.393 16.577 16.176 1.00109.48 C ANISOU 559 CA TYR A 103 10929 17710 12957 1442 417 6103 C ATOM 560 C TYR A 103 -34.430 17.243 17.170 1.00112.03 C ANISOU 560 C TYR A 103 11485 17459 13622 1439 594 5948 C ATOM 561 O TYR A 103 -34.099 18.421 17.029 1.00113.29 O ANISOU 561 O TYR A 103 11712 17349 13982 1562 742 6209 O ATOM 562 CB TYR A 103 -36.821 17.119 16.415 1.00113.02 C ANISOU 562 CB TYR A 103 11205 18225 13514 1695 416 6377 C ATOM 563 CG TYR A 103 -37.909 16.427 15.618 1.00116.43 C ANISOU 563 CG TYR A 103 11377 19232 13632 1686 216 6508 C ATOM 564 CD1 TYR A 103 -38.665 15.400 16.175 1.00116.60 C ANISOU 564 CD1 TYR A 103 11302 19430 13570 1595 92 6249 C ATOM 565 CD2 TYR A 103 -38.197 16.816 14.312 1.00120.89 C ANISOU 565 CD2 TYR A 103 11786 20169 13978 1760 148 6902 C ATOM 566 CE1 TYR A 103 -39.671 14.764 15.448 1.00118.86 C ANISOU 566 CE1 TYR A 103 11339 20249 13572 1555 -103 6361 C ATOM 567 CE2 TYR A 103 -39.201 16.187 13.575 1.00123.80 C ANISOU 567 CE2 TYR A 103 11907 21092 14039 1730 -58 7018 C ATOM 568 CZ TYR A 103 -39.934 15.159 14.146 1.00129.41 C ANISOU 568 CZ TYR A 103 12520 21968 14681 1617 -187 6738 C ATOM 569 OH TYR A 103 -40.928 14.540 13.421 1.00132.45 O ANISOU 569 OH TYR A 103 12652 22906 14768 1558 -400 6845 O ATOM 570 N PHE A 104 -34.001 16.479 18.175 1.00106.15 N ANISOU 570 N PHE A 104 10863 16532 12938 1290 573 5529 N ATOM 571 CA PHE A 104 -33.174 16.876 19.321 1.00104.39 C ANISOU 571 CA PHE A 104 10854 15804 13005 1250 695 5300 C ATOM 572 C PHE A 104 -31.732 17.333 19.063 1.00108.83 C ANISOU 572 C PHE A 104 11555 16139 13657 1124 786 5284 C ATOM 573 O PHE A 104 -31.168 18.058 19.890 1.00108.71 O ANISOU 573 O PHE A 104 11700 15683 13920 1128 906 5207 O ATOM 574 CB PHE A 104 -33.270 15.818 20.438 1.00102.85 C ANISOU 574 CB PHE A 104 10720 15554 12802 1135 619 4883 C ATOM 575 CG PHE A 104 -34.630 15.161 20.501 1.00104.11 C ANISOU 575 CG PHE A 104 10711 16021 12825 1205 513 4893 C ATOM 576 CD1 PHE A 104 -34.816 13.867 20.033 1.00105.75 C ANISOU 576 CD1 PHE A 104 10821 16615 12743 1043 352 4728 C ATOM 577 CD2 PHE A 104 -35.745 15.872 20.931 1.00107.82 C ANISOU 577 CD2 PHE A 104 11105 16409 13453 1436 584 5095 C ATOM 578 CE1 PHE A 104 -36.080 13.275 20.052 1.00107.11 C ANISOU 578 CE1 PHE A 104 10820 17082 12793 1079 248 4748 C ATOM 579 CE2 PHE A 104 -37.011 15.282 20.940 1.00111.08 C ANISOU 579 CE2 PHE A 104 11323 17136 13745 1494 486 5132 C ATOM 580 CZ PHE A 104 -37.168 13.986 20.508 1.00107.91 C ANISOU 580 CZ PHE A 104 10823 17117 13061 1302 311 4956 C ATOM 581 N GLY A 105 -31.158 16.926 17.934 1.00105.52 N ANISOU 581 N GLY A 105 11072 16020 12999 1009 735 5353 N ATOM 582 CA GLY A 105 -29.800 17.306 17.562 1.00105.33 C ANISOU 582 CA GLY A 105 11142 15840 13040 886 828 5367 C ATOM 583 C GLY A 105 -28.729 16.286 17.887 1.00106.10 C ANISOU 583 C GLY A 105 11309 15935 13070 661 776 4984 C ATOM 584 O GLY A 105 -29.029 15.185 18.361 1.00102.95 O ANISOU 584 O GLY A 105 10899 15665 12551 593 663 4696 O ATOM 585 N ASN A 106 -27.460 16.671 17.635 1.00103.31 N ANISOU 585 N ASN A 106 11020 15424 12808 549 871 4998 N ATOM 586 CA ASN A 106 -26.265 15.847 17.828 1.00100.93 C ANISOU 586 CA ASN A 106 10763 15114 12472 351 849 4693 C ATOM 587 C ASN A 106 -25.740 15.773 19.264 1.00101.77 C ANISOU 587 C ASN A 106 10995 14847 12828 273 844 4381 C ATOM 588 O ASN A 106 -25.272 14.706 19.672 1.00 98.78 O ANISOU 588 O ASN A 106 10629 14535 12369 156 764 4074 O ATOM 589 CB ASN A 106 -25.163 16.259 16.860 1.00103.59 C ANISOU 589 CB ASN A 106 11077 15498 12784 266 955 4868 C ATOM 590 CG ASN A 106 -24.192 15.151 16.553 1.00130.51 C ANISOU 590 CG ASN A 106 14463 19100 16023 102 925 4622 C ATOM 591 OD1 ASN A 106 -24.565 14.068 16.085 1.00124.70 O ANISOU 591 OD1 ASN A 106 13676 18704 15002 81 832 4496 O ATOM 592 ND2 ASN A 106 -22.915 15.407 16.788 1.00124.72 N ANISOU 592 ND2 ASN A 106 13764 18156 15469 -19 1009 4551 N ATOM 593 N PHE A 107 -25.791 16.894 20.021 1.00 98.90 N ANISOU 593 N PHE A 107 10731 14088 12757 335 932 4456 N ATOM 594 CA PHE A 107 -25.333 16.935 21.414 1.00 97.04 C ANISOU 594 CA PHE A 107 10632 13496 12742 255 923 4166 C ATOM 595 C PHE A 107 -26.188 16.039 22.298 1.00 98.79 C ANISOU 595 C PHE A 107 10873 13782 12880 300 813 3916 C ATOM 596 O PHE A 107 -25.657 15.355 23.176 1.00 96.32 O ANISOU 596 O PHE A 107 10626 13380 12590 187 745 3609 O ATOM 597 CB PHE A 107 -25.314 18.373 21.967 1.00100.77 C ANISOU 597 CB PHE A 107 11230 13532 13526 313 1054 4301 C ATOM 598 CG PHE A 107 -24.927 18.465 23.428 1.00101.22 C ANISOU 598 CG PHE A 107 11445 13231 13781 226 1038 3994 C ATOM 599 CD1 PHE A 107 -25.888 18.690 24.407 1.00104.02 C ANISOU 599 CD1 PHE A 107 11901 13400 14220 354 1049 3906 C ATOM 600 CD2 PHE A 107 -23.605 18.286 23.829 1.00102.85 C ANISOU 600 CD2 PHE A 107 11691 13314 14074 15 1008 3791 C ATOM 601 CE1 PHE A 107 -25.533 18.751 25.758 1.00104.21 C ANISOU 601 CE1 PHE A 107 12087 13118 14389 266 1031 3612 C ATOM 602 CE2 PHE A 107 -23.252 18.350 25.180 1.00104.89 C ANISOU 602 CE2 PHE A 107 12093 13277 14483 -77 970 3507 C ATOM 603 CZ PHE A 107 -24.218 18.585 26.134 1.00102.83 C ANISOU 603 CZ PHE A 107 11956 12834 14282 46 981 3415 C ATOM 604 N LEU A 108 -27.509 16.053 22.064 1.00 95.88 N ANISOU 604 N LEU A 108 10436 13577 12416 466 797 4067 N ATOM 605 CA LEU A 108 -28.471 15.248 22.810 1.00 93.77 C ANISOU 605 CA LEU A 108 10162 13398 12067 517 708 3877 C ATOM 606 C LEU A 108 -28.421 13.776 22.408 1.00 94.31 C ANISOU 606 C LEU A 108 10146 13824 11863 404 577 3690 C ATOM 607 O LEU A 108 -28.766 12.925 23.221 1.00 91.87 O ANISOU 607 O LEU A 108 9869 13522 11514 372 503 3444 O ATOM 608 CB LEU A 108 -29.883 15.842 22.676 1.00 95.70 C ANISOU 608 CB LEU A 108 10333 13698 12330 734 747 4130 C ATOM 609 CG LEU A 108 -30.438 16.616 23.889 1.00101.14 C ANISOU 609 CG LEU A 108 11146 14016 13266 864 843 4090 C ATOM 610 CD1 LEU A 108 -29.463 17.676 24.414 1.00102.18 C ANISOU 610 CD1 LEU A 108 11457 13702 13664 814 963 4066 C ATOM 611 CD2 LEU A 108 -31.738 17.291 23.539 1.00106.70 C ANISOU 611 CD2 LEU A 108 11744 14797 14002 1105 907 4404 C ATOM 612 N CYS A 109 -27.939 13.476 21.180 1.00 90.67 N ANISOU 612 N CYS A 109 9596 13638 11218 336 563 3798 N ATOM 613 CA CYS A 109 -27.763 12.116 20.660 1.00 88.77 C ANISOU 613 CA CYS A 109 9298 13719 10713 220 465 3616 C ATOM 614 C CYS A 109 -26.722 11.370 21.500 1.00 89.95 C ANISOU 614 C CYS A 109 9544 13698 10935 84 442 3286 C ATOM 615 O CYS A 109 -26.956 10.229 21.907 1.00 88.25 O ANISOU 615 O CYS A 109 9340 13580 10609 30 357 3047 O ATOM 616 CB CYS A 109 -27.371 12.154 19.185 1.00 90.46 C ANISOU 616 CB CYS A 109 9423 14221 10727 187 491 3815 C ATOM 617 SG CYS A 109 -27.032 10.530 18.461 1.00 93.41 S ANISOU 617 SG CYS A 109 9761 14959 10771 39 407 3572 S ATOM 618 N LYS A 110 -25.581 12.043 21.762 1.00 85.54 N ANISOU 618 N LYS A 110 9046 12883 10571 27 516 3290 N ATOM 619 CA LYS A 110 -24.468 11.562 22.576 1.00 82.98 C ANISOU 619 CA LYS A 110 8793 12383 10354 -95 494 3026 C ATOM 620 C LYS A 110 -24.896 11.518 24.049 1.00 85.44 C ANISOU 620 C LYS A 110 9216 12445 10802 -71 445 2833 C ATOM 621 O LYS A 110 -24.586 10.548 24.747 1.00 83.22 O ANISOU 621 O LYS A 110 8975 12157 10487 -138 371 2578 O ATOM 622 CB LYS A 110 -23.251 12.494 22.415 1.00 85.75 C ANISOU 622 CB LYS A 110 9152 12537 10892 -168 586 3132 C ATOM 623 CG LYS A 110 -22.648 12.472 21.023 1.00 90.33 C ANISOU 623 CG LYS A 110 9627 13359 11336 -206 654 3306 C ATOM 624 CD LYS A 110 -21.639 13.590 20.794 1.00 92.43 C ANISOU 624 CD LYS A 110 9888 13425 11806 -269 767 3479 C ATOM 625 CE LYS A 110 -21.052 13.569 19.401 1.00 93.14 C ANISOU 625 CE LYS A 110 9873 13771 11746 -301 855 3668 C ATOM 626 NZ LYS A 110 -20.284 12.325 19.118 1.00 94.08 N ANISOU 626 NZ LYS A 110 9936 14104 11708 -384 830 3458 N ATOM 627 N ALA A 111 -25.628 12.570 24.506 1.00 82.65 N ANISOU 627 N ALA A 111 8919 11888 10597 38 500 2965 N ATOM 628 CA ALA A 111 -26.108 12.720 25.882 1.00 81.21 C ANISOU 628 CA ALA A 111 8860 11456 10542 79 487 2807 C ATOM 629 C ALA A 111 -26.991 11.561 26.327 1.00 81.92 C ANISOU 629 C ALA A 111 8934 11718 10473 106 400 2640 C ATOM 630 O ALA A 111 -26.789 11.062 27.431 1.00 79.89 O ANISOU 630 O ALA A 111 8776 11327 10253 57 353 2405 O ATOM 631 CB ALA A 111 -26.828 14.047 26.059 1.00 83.90 C ANISOU 631 CB ALA A 111 9251 11578 11048 219 595 3010 C ATOM 632 N VAL A 112 -27.931 11.105 25.468 1.00 78.00 N ANISOU 632 N VAL A 112 8314 11530 9794 168 374 2763 N ATOM 633 CA VAL A 112 -28.801 9.968 25.793 1.00 76.17 C ANISOU 633 CA VAL A 112 8052 11478 9411 166 293 2614 C ATOM 634 C VAL A 112 -28.038 8.638 25.787 1.00 78.98 C ANISOU 634 C VAL A 112 8424 11944 9640 23 214 2372 C ATOM 635 O VAL A 112 -28.389 7.736 26.543 1.00 77.09 O ANISOU 635 O VAL A 112 8229 11704 9355 -6 160 2179 O ATOM 636 CB VAL A 112 -30.137 9.900 25.005 1.00 80.60 C ANISOU 636 CB VAL A 112 8466 12332 9827 258 273 2808 C ATOM 637 CG1 VAL A 112 -30.958 11.172 25.187 1.00 81.81 C ANISOU 637 CG1 VAL A 112 8602 12348 10135 436 364 3047 C ATOM 638 CG2 VAL A 112 -29.912 9.596 23.526 1.00 81.50 C ANISOU 638 CG2 VAL A 112 8462 12765 9738 202 239 2935 C ATOM 639 N HIS A 113 -26.987 8.527 24.947 1.00 76.23 N ANISOU 639 N HIS A 113 8041 11678 9243 -56 225 2393 N ATOM 640 CA HIS A 113 -26.166 7.321 24.857 1.00 75.01 C ANISOU 640 CA HIS A 113 7898 11614 8987 -167 180 2182 C ATOM 641 C HIS A 113 -25.264 7.189 26.073 1.00 78.67 C ANISOU 641 C HIS A 113 8468 11813 9612 -216 160 1989 C ATOM 642 O HIS A 113 -25.124 6.085 26.592 1.00 77.14 O ANISOU 642 O HIS A 113 8316 11635 9360 -261 104 1785 O ATOM 643 CB HIS A 113 -25.354 7.294 23.557 1.00 76.66 C ANISOU 643 CB HIS A 113 8029 12005 9092 -218 223 2279 C ATOM 644 CG HIS A 113 -26.084 6.652 22.421 1.00 80.77 C ANISOU 644 CG HIS A 113 8469 12867 9351 -226 198 2332 C ATOM 645 ND1 HIS A 113 -26.863 7.395 21.550 1.00 84.31 N ANISOU 645 ND1 HIS A 113 8831 13487 9717 -158 214 2593 N ATOM 646 CD2 HIS A 113 -26.145 5.349 22.059 1.00 81.95 C ANISOU 646 CD2 HIS A 113 8620 13209 9309 -300 156 2152 C ATOM 647 CE1 HIS A 113 -27.358 6.526 20.684 1.00 84.22 C ANISOU 647 CE1 HIS A 113 8764 13789 9445 -208 164 2557 C ATOM 648 NE2 HIS A 113 -26.953 5.283 20.947 1.00 83.23 N ANISOU 648 NE2 HIS A 113 8699 13675 9250 -301 134 2283 N ATOM 649 N VAL A 114 -24.689 8.318 26.551 1.00 76.42 N ANISOU 649 N VAL A 114 8230 11281 9526 -212 202 2056 N ATOM 650 CA VAL A 114 -23.823 8.335 27.734 1.00 75.70 C ANISOU 650 CA VAL A 114 8234 10947 9581 -275 164 1884 C ATOM 651 C VAL A 114 -24.581 8.089 29.040 1.00 77.64 C ANISOU 651 C VAL A 114 8596 11058 9845 -235 119 1738 C ATOM 652 O VAL A 114 -24.071 7.361 29.887 1.00 75.76 O ANISOU 652 O VAL A 114 8419 10758 9607 -288 51 1549 O ATOM 653 CB VAL A 114 -22.809 9.509 27.817 1.00 81.46 C ANISOU 653 CB VAL A 114 8978 11465 10508 -332 210 1967 C ATOM 654 CG1 VAL A 114 -21.858 9.504 26.630 1.00 82.19 C ANISOU 654 CG1 VAL A 114 8947 11706 10574 -392 257 2079 C ATOM 655 CG2 VAL A 114 -23.503 10.859 27.937 1.00 82.96 C ANISOU 655 CG2 VAL A 114 9226 11472 10824 -256 288 2132 C ATOM 656 N ILE A 115 -25.804 8.660 29.188 1.00 74.76 N ANISOU 656 N ILE A 115 8252 10664 9487 -130 165 1839 N ATOM 657 CA ILE A 115 -26.660 8.469 30.373 1.00 74.11 C ANISOU 657 CA ILE A 115 8273 10475 9412 -75 153 1722 C ATOM 658 C ILE A 115 -27.136 7.009 30.458 1.00 76.71 C ANISOU 658 C ILE A 115 8574 10998 9574 -100 87 1590 C ATOM 659 O ILE A 115 -27.048 6.411 31.530 1.00 74.69 O ANISOU 659 O ILE A 115 8417 10646 9314 -126 44 1415 O ATOM 660 CB ILE A 115 -27.822 9.507 30.476 1.00 78.49 C ANISOU 660 CB ILE A 115 8839 10945 10038 63 246 1883 C ATOM 661 CG1 ILE A 115 -27.269 10.944 30.708 1.00 80.53 C ANISOU 661 CG1 ILE A 115 9186 10915 10496 75 324 1964 C ATOM 662 CG2 ILE A 115 -28.808 9.121 31.594 1.00 78.12 C ANISOU 662 CG2 ILE A 115 8871 10846 9965 126 251 1765 C ATOM 663 CD1 ILE A 115 -28.288 12.128 30.544 1.00 88.16 C ANISOU 663 CD1 ILE A 115 10155 11778 11565 238 450 2177 C ATOM 664 N TYR A 116 -27.599 6.435 29.323 1.00 74.36 N ANISOU 664 N TYR A 116 8152 10970 9132 -104 78 1671 N ATOM 665 CA TYR A 116 -28.044 5.038 29.229 1.00 73.89 C ANISOU 665 CA TYR A 116 8067 11093 8913 -153 24 1545 C ATOM 666 C TYR A 116 -26.920 4.087 29.646 1.00 77.62 C ANISOU 666 C TYR A 116 8608 11503 9380 -239 -24 1350 C ATOM 667 O TYR A 116 -27.181 3.148 30.399 1.00 76.45 O ANISOU 667 O TYR A 116 8527 11332 9190 -260 -60 1203 O ATOM 668 CB TYR A 116 -28.555 4.707 27.808 1.00 76.12 C ANISOU 668 CB TYR A 116 8212 11677 9031 -171 18 1659 C ATOM 669 CG TYR A 116 -28.629 3.229 27.467 1.00 77.80 C ANISOU 669 CG TYR A 116 8417 12065 9077 -267 -32 1500 C ATOM 670 CD1 TYR A 116 -29.736 2.464 27.824 1.00 79.51 C ANISOU 670 CD1 TYR A 116 8627 12368 9215 -287 -63 1432 C ATOM 671 CD2 TYR A 116 -27.618 2.609 26.740 1.00 78.90 C ANISOU 671 CD2 TYR A 116 8554 12282 9144 -339 -32 1424 C ATOM 672 CE1 TYR A 116 -29.822 1.111 27.491 1.00 79.54 C ANISOU 672 CE1 TYR A 116 8640 12505 9077 -393 -99 1279 C ATOM 673 CE2 TYR A 116 -27.692 1.256 26.402 1.00 79.67 C ANISOU 673 CE2 TYR A 116 8667 12509 9094 -422 -57 1265 C ATOM 674 CZ TYR A 116 -28.798 0.511 26.777 1.00 85.05 C ANISOU 674 CZ TYR A 116 9358 13252 9704 -457 -94 1189 C ATOM 675 OH TYR A 116 -28.874 -0.822 26.448 1.00 84.09 O ANISOU 675 OH TYR A 116 9271 13229 9451 -558 -110 1024 O ATOM 676 N THR A 117 -25.680 4.345 29.160 1.00 74.49 N ANISOU 676 N THR A 117 8186 11083 9036 -279 -17 1368 N ATOM 677 CA THR A 117 -24.475 3.560 29.447 1.00 73.53 C ANISOU 677 CA THR A 117 8092 10914 8933 -340 -54 1221 C ATOM 678 C THR A 117 -24.066 3.682 30.914 1.00 76.30 C ANISOU 678 C THR A 117 8555 11036 9398 -344 -105 1108 C ATOM 679 O THR A 117 -23.649 2.686 31.507 1.00 74.68 O ANISOU 679 O THR A 117 8397 10809 9168 -365 -155 968 O ATOM 680 CB THR A 117 -23.359 3.931 28.466 1.00 84.24 C ANISOU 680 CB THR A 117 9358 12331 10320 -374 -14 1305 C ATOM 681 OG1 THR A 117 -23.866 3.814 27.134 1.00 85.37 O ANISOU 681 OG1 THR A 117 9415 12705 10315 -369 32 1411 O ATOM 682 CG2 THR A 117 -22.117 3.061 28.619 1.00 83.24 C ANISOU 682 CG2 THR A 117 9222 12191 10215 -416 -36 1176 C ATOM 683 N VAL A 118 -24.192 4.894 31.495 1.00 73.59 N ANISOU 683 N VAL A 118 8266 10523 9174 -321 -90 1170 N ATOM 684 CA VAL A 118 -23.892 5.149 32.909 1.00 73.06 C ANISOU 684 CA VAL A 118 8327 10244 9190 -336 -140 1056 C ATOM 685 C VAL A 118 -24.853 4.325 33.785 1.00 76.82 C ANISOU 685 C VAL A 118 8894 10725 9571 -295 -158 951 C ATOM 686 O VAL A 118 -24.381 3.528 34.585 1.00 75.72 O ANISOU 686 O VAL A 118 8819 10546 9405 -324 -224 823 O ATOM 687 CB VAL A 118 -23.841 6.667 33.259 1.00 77.77 C ANISOU 687 CB VAL A 118 8983 10638 9928 -332 -99 1129 C ATOM 688 CG1 VAL A 118 -24.084 6.924 34.744 1.00 77.66 C ANISOU 688 CG1 VAL A 118 9137 10428 9941 -326 -127 1000 C ATOM 689 CG2 VAL A 118 -22.512 7.278 32.828 1.00 78.48 C ANISOU 689 CG2 VAL A 118 9009 10674 10136 -421 -112 1175 C ATOM 690 N ASN A 119 -26.184 4.444 33.560 1.00 74.54 N ANISOU 690 N ASN A 119 8589 10507 9227 -228 -96 1025 N ATOM 691 CA ASN A 119 -27.217 3.680 34.281 1.00 74.05 C ANISOU 691 CA ASN A 119 8585 10472 9078 -197 -92 952 C ATOM 692 C ASN A 119 -27.033 2.159 34.104 1.00 77.64 C ANISOU 692 C ASN A 119 9022 11050 9427 -254 -140 850 C ATOM 693 O ASN A 119 -27.332 1.395 35.019 1.00 77.06 O ANISOU 693 O ASN A 119 9038 10932 9310 -257 -158 751 O ATOM 694 CB ASN A 119 -28.632 4.113 33.841 1.00 74.36 C ANISOU 694 CB ASN A 119 8552 10609 9092 -120 -16 1083 C ATOM 695 CG ASN A 119 -29.770 3.310 34.445 1.00 95.20 C ANISOU 695 CG ASN A 119 11211 13311 11648 -102 2 1031 C ATOM 696 OD1 ASN A 119 -30.508 2.612 33.743 1.00 89.38 O ANISOU 696 OD1 ASN A 119 10369 12772 10820 -127 -1 1067 O ATOM 697 ND2 ASN A 119 -29.931 3.375 35.763 1.00 88.22 N ANISOU 697 ND2 ASN A 119 10466 12267 10786 -73 20 941 N ATOM 698 N LEU A 120 -26.519 1.740 32.935 1.00 74.30 N ANISOU 698 N LEU A 120 8498 10769 8963 -295 -146 876 N ATOM 699 CA LEU A 120 -26.265 0.349 32.568 1.00 73.54 C ANISOU 699 CA LEU A 120 8392 10775 8777 -345 -167 777 C ATOM 700 C LEU A 120 -25.249 -0.284 33.520 1.00 76.93 C ANISOU 700 C LEU A 120 8910 11068 9251 -354 -221 658 C ATOM 701 O LEU A 120 -25.607 -1.183 34.280 1.00 75.56 O ANISOU 701 O LEU A 120 8822 10854 9034 -355 -235 572 O ATOM 702 CB LEU A 120 -25.755 0.319 31.112 1.00 74.10 C ANISOU 702 CB LEU A 120 8350 11005 8802 -375 -142 834 C ATOM 703 CG LEU A 120 -25.957 -0.919 30.251 1.00 78.74 C ANISOU 703 CG LEU A 120 8910 11755 9251 -428 -127 759 C ATOM 704 CD1 LEU A 120 -27.416 -1.383 30.246 1.00 78.94 C ANISOU 704 CD1 LEU A 120 8933 11884 9176 -457 -127 752 C ATOM 705 CD2 LEU A 120 -25.508 -0.636 28.820 1.00 81.64 C ANISOU 705 CD2 LEU A 120 9175 12288 9557 -447 -88 837 C ATOM 706 N TYR A 121 -24.016 0.242 33.533 1.00 74.62 N ANISOU 706 N TYR A 121 8591 10708 9052 -360 -251 671 N ATOM 707 CA TYR A 121 -22.914 -0.253 34.360 1.00 74.55 C ANISOU 707 CA TYR A 121 8628 10602 9096 -365 -321 589 C ATOM 708 C TYR A 121 -22.985 0.098 35.859 1.00 76.10 C ANISOU 708 C TYR A 121 8951 10644 9319 -357 -385 539 C ATOM 709 O TYR A 121 -22.515 -0.689 36.676 1.00 75.31 O ANISOU 709 O TYR A 121 8912 10497 9203 -349 -446 468 O ATOM 710 CB TYR A 121 -21.554 0.149 33.752 1.00 77.32 C ANISOU 710 CB TYR A 121 8868 10972 9537 -388 -332 631 C ATOM 711 CG TYR A 121 -21.293 -0.414 32.368 1.00 81.05 C ANISOU 711 CG TYR A 121 9236 11601 9959 -389 -259 656 C ATOM 712 CD1 TYR A 121 -21.121 -1.781 32.169 1.00 83.31 C ANISOU 712 CD1 TYR A 121 9537 11935 10182 -369 -237 567 C ATOM 713 CD2 TYR A 121 -21.181 0.423 31.263 1.00 83.17 C ANISOU 713 CD2 TYR A 121 9404 11959 10239 -408 -200 768 C ATOM 714 CE1 TYR A 121 -20.872 -2.305 30.900 1.00 85.39 C ANISOU 714 CE1 TYR A 121 9728 12333 10381 -373 -154 563 C ATOM 715 CE2 TYR A 121 -20.909 -0.087 29.992 1.00 84.98 C ANISOU 715 CE2 TYR A 121 9550 12346 10391 -411 -125 783 C ATOM 716 CZ TYR A 121 -20.758 -1.453 29.814 1.00 93.33 C ANISOU 716 CZ TYR A 121 10635 13451 11374 -395 -100 668 C ATOM 717 OH TYR A 121 -20.496 -1.961 28.563 1.00 95.65 O ANISOU 717 OH TYR A 121 10871 13894 11577 -401 -11 660 O ATOM 718 N SER A 122 -23.555 1.264 36.219 1.00 71.82 N ANISOU 718 N SER A 122 8456 10022 8810 -351 -365 579 N ATOM 719 CA SER A 122 -23.644 1.702 37.615 1.00 71.20 C ANISOU 719 CA SER A 122 8520 9796 8737 -349 -409 516 C ATOM 720 C SER A 122 -24.671 0.933 38.441 1.00 74.58 C ANISOU 720 C SER A 122 9058 10218 9059 -309 -385 462 C ATOM 721 O SER A 122 -24.348 0.535 39.561 1.00 74.51 O ANISOU 721 O SER A 122 9160 10141 9011 -313 -450 387 O ATOM 722 CB SER A 122 -23.874 3.208 37.720 1.00 74.08 C ANISOU 722 CB SER A 122 8920 10045 9181 -351 -369 562 C ATOM 723 OG SER A 122 -25.153 3.577 37.231 1.00 79.67 O ANISOU 723 OG SER A 122 9608 10793 9869 -287 -262 644 O ATOM 724 N SER A 123 -25.899 0.727 37.902 1.00 70.35 N ANISOU 724 N SER A 123 8484 9770 8474 -278 -296 510 N ATOM 725 CA SER A 123 -26.984 0.016 38.595 1.00 69.57 C ANISOU 725 CA SER A 123 8464 9681 8287 -253 -253 477 C ATOM 726 C SER A 123 -26.568 -1.376 39.057 1.00 71.52 C ANISOU 726 C SER A 123 8767 9932 8476 -276 -303 404 C ATOM 727 O SER A 123 -26.750 -1.704 40.231 1.00 70.97 O ANISOU 727 O SER A 123 8825 9788 8354 -261 -316 358 O ATOM 728 CB SER A 123 -28.234 -0.068 37.725 1.00 73.58 C ANISOU 728 CB SER A 123 8868 10324 8763 -241 -169 554 C ATOM 729 OG SER A 123 -27.975 -0.786 36.528 1.00 83.22 O ANISOU 729 OG SER A 123 9979 11683 9960 -289 -183 565 O ATOM 730 N VAL A 124 -25.971 -2.172 38.146 1.00 67.06 N ANISOU 730 N VAL A 124 8116 9446 7919 -304 -321 398 N ATOM 731 CA VAL A 124 -25.511 -3.525 38.449 1.00 66.38 C ANISOU 731 CA VAL A 124 8079 9341 7801 -308 -348 340 C ATOM 732 C VAL A 124 -24.406 -3.559 39.519 1.00 70.19 C ANISOU 732 C VAL A 124 8638 9723 8307 -282 -447 312 C ATOM 733 O VAL A 124 -24.479 -4.392 40.428 1.00 70.43 O ANISOU 733 O VAL A 124 8775 9701 8285 -262 -465 287 O ATOM 734 CB VAL A 124 -25.225 -4.384 37.184 1.00 69.82 C ANISOU 734 CB VAL A 124 8423 9871 8236 -334 -314 325 C ATOM 735 CG1 VAL A 124 -23.922 -3.987 36.484 1.00 69.75 C ANISOU 735 CG1 VAL A 124 8314 9887 8301 -324 -348 345 C ATOM 736 CG2 VAL A 124 -25.257 -5.873 37.504 1.00 69.63 C ANISOU 736 CG2 VAL A 124 8480 9802 8175 -337 -295 265 C ATOM 737 N TRP A 125 -23.429 -2.628 39.449 1.00 65.94 N ANISOU 737 N TRP A 125 8044 9167 7843 -292 -514 328 N ATOM 738 CA TRP A 125 -22.350 -2.582 40.432 1.00 66.12 C ANISOU 738 CA TRP A 125 8112 9127 7883 -289 -633 305 C ATOM 739 C TRP A 125 -22.745 -2.028 41.793 1.00 69.10 C ANISOU 739 C TRP A 125 8646 9419 8190 -294 -675 268 C ATOM 740 O TRP A 125 -22.125 -2.404 42.787 1.00 68.75 O ANISOU 740 O TRP A 125 8674 9346 8100 -287 -775 247 O ATOM 741 CB TRP A 125 -21.051 -2.024 39.855 1.00 65.64 C ANISOU 741 CB TRP A 125 7914 9093 7931 -318 -697 332 C ATOM 742 CG TRP A 125 -20.415 -2.985 38.892 1.00 66.80 C ANISOU 742 CG TRP A 125 7943 9318 8120 -285 -663 353 C ATOM 743 CD1 TRP A 125 -20.614 -3.043 37.544 1.00 69.63 C ANISOU 743 CD1 TRP A 125 8202 9759 8496 -290 -564 376 C ATOM 744 CD2 TRP A 125 -19.566 -4.096 39.220 1.00 67.36 C ANISOU 744 CD2 TRP A 125 7999 9389 8206 -228 -711 351 C ATOM 745 NE1 TRP A 125 -19.910 -4.096 37.004 1.00 69.51 N ANISOU 745 NE1 TRP A 125 8123 9785 8504 -247 -537 367 N ATOM 746 CE2 TRP A 125 -19.245 -4.750 38.009 1.00 71.52 C ANISOU 746 CE2 TRP A 125 8421 9981 8774 -198 -620 359 C ATOM 747 CE3 TRP A 125 -19.003 -4.574 40.415 1.00 69.43 C ANISOU 747 CE3 TRP A 125 8325 9609 8449 -192 -821 354 C ATOM 748 CZ2 TRP A 125 -18.392 -5.860 37.960 1.00 71.55 C ANISOU 748 CZ2 TRP A 125 8384 9983 8819 -120 -617 364 C ATOM 749 CZ3 TRP A 125 -18.166 -5.678 40.365 1.00 71.48 C ANISOU 749 CZ3 TRP A 125 8528 9880 8750 -111 -834 383 C ATOM 750 CH2 TRP A 125 -17.870 -6.310 39.150 1.00 72.20 C ANISOU 750 CH2 TRP A 125 8517 10012 8903 -69 -723 386 C ATOM 751 N ILE A 126 -23.831 -1.212 41.856 1.00 65.15 N ANISOU 751 N ILE A 126 8201 8887 7666 -295 -588 266 N ATOM 752 CA ILE A 126 -24.407 -0.704 43.114 1.00 65.33 C ANISOU 752 CA ILE A 126 8392 8824 7604 -286 -581 219 C ATOM 753 C ILE A 126 -25.004 -1.918 43.847 1.00 68.50 C ANISOU 753 C ILE A 126 8892 9241 7893 -249 -555 213 C ATOM 754 O ILE A 126 -24.784 -2.080 45.046 1.00 68.09 O ANISOU 754 O ILE A 126 8978 9147 7747 -244 -616 178 O ATOM 755 CB ILE A 126 -25.435 0.448 42.878 1.00 68.51 C ANISOU 755 CB ILE A 126 8811 9183 8035 -267 -463 234 C ATOM 756 CG1 ILE A 126 -24.709 1.796 42.689 1.00 69.82 C ANISOU 756 CG1 ILE A 126 8961 9266 8301 -312 -503 224 C ATOM 757 CG2 ILE A 126 -26.445 0.551 44.029 1.00 69.51 C ANISOU 757 CG2 ILE A 126 9104 9251 8054 -224 -387 194 C ATOM 758 CD1 ILE A 126 -25.443 2.831 41.833 1.00 77.45 C ANISOU 758 CD1 ILE A 126 9863 10209 9355 -280 -382 295 C ATOM 759 N LEU A 127 -25.684 -2.805 43.092 1.00 65.10 N ANISOU 759 N LEU A 127 8390 8875 7468 -238 -470 251 N ATOM 760 CA LEU A 127 -26.244 -4.062 43.597 1.00 65.20 C ANISOU 760 CA LEU A 127 8480 8890 7401 -223 -427 257 C ATOM 761 C LEU A 127 -25.124 -4.995 44.092 1.00 69.85 C ANISOU 761 C LEU A 127 9108 9453 7977 -204 -533 259 C ATOM 762 O LEU A 127 -25.313 -5.679 45.101 1.00 70.15 O ANISOU 762 O LEU A 127 9275 9454 7926 -181 -537 270 O ATOM 763 CB LEU A 127 -27.089 -4.761 42.520 1.00 64.50 C ANISOU 763 CB LEU A 127 8293 8876 7339 -249 -327 282 C ATOM 764 CG LEU A 127 -28.343 -4.020 42.062 1.00 68.76 C ANISOU 764 CG LEU A 127 8769 9474 7882 -257 -226 312 C ATOM 765 CD1 LEU A 127 -28.735 -4.455 40.706 1.00 68.32 C ANISOU 765 CD1 LEU A 127 8572 9529 7859 -303 -185 333 C ATOM 766 CD2 LEU A 127 -29.493 -4.234 43.014 1.00 71.72 C ANISOU 766 CD2 LEU A 127 9241 9832 8179 -243 -136 322 C ATOM 767 N ALA A 128 -23.950 -4.990 43.397 1.00 65.96 N ANISOU 767 N ALA A 128 8499 8986 7577 -205 -611 265 N ATOM 768 CA ALA A 128 -22.761 -5.758 43.774 1.00 66.03 C ANISOU 768 CA ALA A 128 8502 8984 7602 -165 -715 288 C ATOM 769 C ALA A 128 -22.194 -5.204 45.091 1.00 71.59 C ANISOU 769 C ALA A 128 9302 9667 8230 -167 -849 280 C ATOM 770 O ALA A 128 -21.675 -5.969 45.907 1.00 71.99 O ANISOU 770 O ALA A 128 9415 9711 8226 -122 -927 318 O ATOM 771 CB ALA A 128 -21.716 -5.676 42.677 1.00 66.42 C ANISOU 771 CB ALA A 128 8379 9083 7775 -164 -745 300 C ATOM 772 N PHE A 129 -22.326 -3.874 45.301 1.00 68.27 N ANISOU 772 N PHE A 129 8906 9233 7801 -221 -871 232 N ATOM 773 CA PHE A 129 -21.903 -3.188 46.519 1.00 69.13 C ANISOU 773 CA PHE A 129 9132 9318 7818 -255 -990 189 C ATOM 774 C PHE A 129 -22.883 -3.475 47.655 1.00 73.92 C ANISOU 774 C PHE A 129 9938 9891 8257 -227 -931 173 C ATOM 775 O PHE A 129 -22.455 -3.542 48.808 1.00 75.32 O ANISOU 775 O PHE A 129 10234 10075 8308 -230 -1040 161 O ATOM 776 CB PHE A 129 -21.722 -1.682 46.271 1.00 71.30 C ANISOU 776 CB PHE A 129 9380 9555 8155 -331 -1007 129 C ATOM 777 CG PHE A 129 -20.287 -1.255 46.045 1.00 74.04 C ANISOU 777 CG PHE A 129 9596 9937 8600 -394 -1160 133 C ATOM 778 CD1 PHE A 129 -19.603 -1.629 44.893 1.00 76.36 C ANISOU 778 CD1 PHE A 129 9690 10291 9035 -379 -1154 197 C ATOM 779 CD2 PHE A 129 -19.619 -0.477 46.985 1.00 78.03 C ANISOU 779 CD2 PHE A 129 10176 10423 9050 -479 -1304 68 C ATOM 780 CE1 PHE A 129 -18.277 -1.245 44.694 1.00 78.22 C ANISOU 780 CE1 PHE A 129 9780 10571 9371 -437 -1282 215 C ATOM 781 CE2 PHE A 129 -18.295 -0.083 46.778 1.00 81.68 C ANISOU 781 CE2 PHE A 129 10491 10931 9613 -560 -1452 78 C ATOM 782 CZ PHE A 129 -17.636 -0.467 45.633 1.00 79.13 C ANISOU 782 CZ PHE A 129 9948 10671 9445 -534 -1435 161 C ATOM 783 N ILE A 130 -24.193 -3.682 47.327 1.00 69.35 N ANISOU 783 N ILE A 130 9386 9294 7668 -202 -759 182 N ATOM 784 CA ILE A 130 -25.241 -4.061 48.293 1.00 69.23 C ANISOU 784 CA ILE A 130 9536 9258 7511 -173 -663 186 C ATOM 785 C ILE A 130 -24.949 -5.508 48.722 1.00 74.74 C ANISOU 785 C ILE A 130 10274 9967 8156 -133 -698 260 C ATOM 786 O ILE A 130 -25.034 -5.830 49.906 1.00 76.28 O ANISOU 786 O ILE A 130 10626 10157 8201 -112 -723 279 O ATOM 787 CB ILE A 130 -26.695 -3.902 47.742 1.00 70.95 C ANISOU 787 CB ILE A 130 9724 9475 7759 -165 -473 195 C ATOM 788 CG1 ILE A 130 -27.003 -2.444 47.352 1.00 70.90 C ANISOU 788 CG1 ILE A 130 9683 9441 7814 -175 -425 147 C ATOM 789 CG2 ILE A 130 -27.706 -4.372 48.777 1.00 72.23 C ANISOU 789 CG2 ILE A 130 10038 9626 7780 -137 -365 213 C ATOM 790 CD1 ILE A 130 -28.373 -2.174 46.666 1.00 74.66 C ANISOU 790 CD1 ILE A 130 10080 9944 8343 -150 -252 185 C ATOM 791 N SER A 131 -24.565 -6.354 47.747 1.00 70.77 N ANISOU 791 N SER A 131 9639 9475 7774 -119 -694 305 N ATOM 792 CA SER A 131 -24.191 -7.754 47.932 1.00 71.36 C ANISOU 792 CA SER A 131 9737 9527 7848 -68 -708 381 C ATOM 793 C SER A 131 -22.934 -7.884 48.811 1.00 75.54 C ANISOU 793 C SER A 131 10300 10080 8322 -24 -888 426 C ATOM 794 O SER A 131 -22.830 -8.835 49.590 1.00 75.99 O ANISOU 794 O SER A 131 10455 10116 8300 33 -907 509 O ATOM 795 CB SER A 131 -23.961 -8.412 46.574 1.00 75.54 C ANISOU 795 CB SER A 131 10120 10053 8530 -65 -655 387 C ATOM 796 OG SER A 131 -23.673 -9.793 46.715 1.00 89.22 O ANISOU 796 OG SER A 131 11893 11727 10279 -8 -637 454 O ATOM 797 N LEU A 132 -21.990 -6.924 48.684 1.00 71.84 N ANISOU 797 N LEU A 132 9740 9660 7895 -57 -1024 384 N ATOM 798 CA LEU A 132 -20.753 -6.862 49.469 1.00 73.04 C ANISOU 798 CA LEU A 132 9884 9869 7997 -43 -1224 421 C ATOM 799 C LEU A 132 -21.039 -6.474 50.919 1.00 77.42 C ANISOU 799 C LEU A 132 10641 10443 8334 -68 -1291 397 C ATOM 800 O LEU A 132 -20.388 -6.999 51.825 1.00 78.42 O ANISOU 800 O LEU A 132 10821 10622 8354 -27 -1425 474 O ATOM 801 CB LEU A 132 -19.763 -5.851 48.855 1.00 73.21 C ANISOU 801 CB LEU A 132 9740 9940 8136 -108 -1336 372 C ATOM 802 CG LEU A 132 -18.380 -6.366 48.400 1.00 78.87 C ANISOU 802 CG LEU A 132 10263 10721 8983 -58 -1452 454 C ATOM 803 CD1 LEU A 132 -17.608 -7.052 49.538 1.00 80.89 C ANISOU 803 CD1 LEU A 132 10560 11039 9137 7 -1616 553 C ATOM 804 CD2 LEU A 132 -18.475 -7.242 47.144 1.00 80.36 C ANISOU 804 CD2 LEU A 132 10336 10872 9323 13 -1305 492 C ATOM 805 N ASP A 133 -22.015 -5.555 51.128 1.00 72.56 N ANISOU 805 N ASP A 133 10136 9789 7646 -125 -1191 298 N ATOM 806 CA ASP A 133 -22.448 -5.047 52.432 1.00 73.11 C ANISOU 806 CA ASP A 133 10420 9863 7496 -152 -1207 242 C ATOM 807 C ASP A 133 -23.028 -6.171 53.284 1.00 75.87 C ANISOU 807 C ASP A 133 10916 10215 7695 -80 -1141 341 C ATOM 808 O ASP A 133 -22.651 -6.299 54.448 1.00 76.44 O ANISOU 808 O ASP A 133 11123 10344 7575 -73 -1256 368 O ATOM 809 CB ASP A 133 -23.472 -3.910 52.250 1.00 74.28 C ANISOU 809 CB ASP A 133 10632 9944 7646 -196 -1057 127 C ATOM 810 CG ASP A 133 -23.716 -3.067 53.488 1.00 85.79 C ANISOU 810 CG ASP A 133 12310 11392 8894 -236 -1075 24 C ATOM 811 OD1 ASP A 133 -24.829 -3.150 54.055 1.00 86.63 O ANISOU 811 OD1 ASP A 133 12564 11471 8879 -197 -912 16 O ATOM 812 OD2 ASP A 133 -22.811 -2.291 53.866 1.00 91.86 O ANISOU 812 OD2 ASP A 133 13101 12179 9621 -315 -1242 -57 O ATOM 813 N ARG A 134 -23.903 -7.013 52.684 1.00 70.73 N ANISOU 813 N ARG A 134 10234 9510 7131 -38 -963 401 N ATOM 814 CA ARG A 134 -24.552 -8.162 53.342 1.00 70.86 C ANISOU 814 CA ARG A 134 10376 9502 7044 15 -864 509 C ATOM 815 C ARG A 134 -23.566 -9.208 53.834 1.00 75.59 C ANISOU 815 C ARG A 134 10986 10125 7609 88 -1000 644 C ATOM 816 O ARG A 134 -23.859 -9.918 54.791 1.00 75.76 O ANISOU 816 O ARG A 134 11161 10146 7480 131 -972 743 O ATOM 817 CB ARG A 134 -25.641 -8.798 52.452 1.00 68.05 C ANISOU 817 CB ARG A 134 9957 9080 6818 9 -656 530 C ATOM 818 CG ARG A 134 -26.873 -7.925 52.232 1.00 72.50 C ANISOU 818 CG ARG A 134 10528 9641 7377 -37 -497 445 C ATOM 819 CD ARG A 134 -27.692 -7.726 53.497 1.00 81.83 C ANISOU 819 CD ARG A 134 11907 10833 8352 -26 -404 448 C ATOM 820 NE ARG A 134 -27.274 -6.538 54.243 1.00 90.10 N ANISOU 820 NE ARG A 134 13059 11909 9264 -37 -499 346 N ATOM 821 CZ ARG A 134 -27.880 -6.086 55.335 1.00107.62 C ANISOU 821 CZ ARG A 134 15467 14141 11283 -29 -420 307 C ATOM 822 NH1 ARG A 134 -27.437 -4.993 55.942 1.00 91.77 N ANISOU 822 NH1 ARG A 134 13568 12144 9156 -56 -510 188 N ATOM 823 NH2 ARG A 134 -28.941 -6.717 55.825 1.00101.52 N ANISOU 823 NH2 ARG A 134 14782 13366 10426 -2 -240 381 N ATOM 824 N TYR A 135 -22.401 -9.293 53.183 1.00 72.82 N ANISOU 824 N TYR A 135 10466 9798 7402 110 -1136 664 N ATOM 825 CA TYR A 135 -21.322 -10.183 53.571 1.00 74.57 C ANISOU 825 CA TYR A 135 10656 10054 7622 202 -1279 806 C ATOM 826 C TYR A 135 -20.690 -9.587 54.842 1.00 80.74 C ANISOU 826 C TYR A 135 11535 10960 8183 180 -1484 810 C ATOM 827 O TYR A 135 -20.672 -10.237 55.887 1.00 81.69 O ANISOU 827 O TYR A 135 11794 11115 8129 239 -1528 930 O ATOM 828 CB TYR A 135 -20.298 -10.320 52.416 1.00 75.12 C ANISOU 828 CB TYR A 135 10492 10127 7925 234 -1341 814 C ATOM 829 CG TYR A 135 -19.033 -11.054 52.805 1.00 79.05 C ANISOU 829 CG TYR A 135 10912 10682 8441 344 -1505 966 C ATOM 830 CD1 TYR A 135 -18.961 -12.441 52.740 1.00 82.09 C ANISOU 830 CD1 TYR A 135 11316 10978 8898 473 -1425 1113 C ATOM 831 CD2 TYR A 135 -17.910 -10.362 53.252 1.00 81.04 C ANISOU 831 CD2 TYR A 135 11071 11076 8646 319 -1741 970 C ATOM 832 CE1 TYR A 135 -17.812 -13.125 53.133 1.00 85.91 C ANISOU 832 CE1 TYR A 135 11723 11513 9408 604 -1567 1280 C ATOM 833 CE2 TYR A 135 -16.753 -11.034 53.640 1.00 84.10 C ANISOU 833 CE2 TYR A 135 11359 11544 9051 430 -1903 1133 C ATOM 834 CZ TYR A 135 -16.708 -12.418 53.580 1.00 93.97 C ANISOU 834 CZ TYR A 135 12623 12704 10376 588 -1812 1298 C ATOM 835 OH TYR A 135 -15.572 -13.095 53.960 1.00 98.36 O ANISOU 835 OH TYR A 135 13070 13337 10964 727 -1962 1485 O ATOM 836 N LEU A 136 -20.214 -8.351 54.745 1.00 77.49 N ANISOU 836 N LEU A 136 11061 10611 7769 83 -1604 680 N ATOM 837 CA LEU A 136 -19.610 -7.668 55.884 1.00 79.37 C ANISOU 837 CA LEU A 136 11395 10970 7793 23 -1811 644 C ATOM 838 C LEU A 136 -20.532 -7.634 57.103 1.00 85.35 C ANISOU 838 C LEU A 136 12426 11735 8270 14 -1737 627 C ATOM 839 O LEU A 136 -20.121 -7.992 58.207 1.00 87.28 O ANISOU 839 O LEU A 136 12783 12083 8298 42 -1876 716 O ATOM 840 CB LEU A 136 -19.201 -6.245 55.498 1.00 78.69 C ANISOU 840 CB LEU A 136 11230 10902 7769 -112 -1897 471 C ATOM 841 CG LEU A 136 -18.052 -6.118 54.495 1.00 81.51 C ANISOU 841 CG LEU A 136 11311 11294 8364 -125 -2012 495 C ATOM 842 CD1 LEU A 136 -17.976 -4.704 53.940 1.00 80.24 C ANISOU 842 CD1 LEU A 136 11093 11098 8294 -265 -2018 326 C ATOM 843 CD2 LEU A 136 -16.732 -6.518 55.138 1.00 85.56 C ANISOU 843 CD2 LEU A 136 11729 11961 8818 -100 -2273 614 C ATOM 844 N ALA A 137 -21.773 -7.200 56.903 1.00 81.19 N ANISOU 844 N ALA A 137 11997 11112 7739 -17 -1517 524 N ATOM 845 CA ALA A 137 -22.702 -7.069 57.987 1.00 82.18 C ANISOU 845 CA ALA A 137 12370 11243 7611 -22 -1410 496 C ATOM 846 C ALA A 137 -22.985 -8.372 58.664 1.00 87.06 C ANISOU 846 C ALA A 137 13093 11875 8110 74 -1357 685 C ATOM 847 O ALA A 137 -23.193 -8.409 59.850 1.00 89.51 O ANISOU 847 O ALA A 137 13606 12254 8150 79 -1374 712 O ATOM 848 CB ALA A 137 -23.763 -6.067 57.630 1.00 81.64 C ANISOU 848 CB ALA A 137 12350 11089 7582 -75 -1216 335 C ATOM 849 N ILE A 138 -22.993 -9.454 57.915 1.00 81.37 N ANISOU 849 N ILE A 138 12249 11081 7587 148 -1283 816 N ATOM 850 CA ILE A 138 -23.080 -10.747 58.545 1.00 82.41 C ANISOU 850 CA ILE A 138 12477 11202 7633 242 -1248 1018 C ATOM 851 C ILE A 138 -21.912 -11.629 58.815 1.00 89.77 C ANISOU 851 C ILE A 138 13348 12188 8574 342 -1433 1202 C ATOM 852 O ILE A 138 -21.773 -12.189 59.878 1.00 91.86 O ANISOU 852 O ILE A 138 13753 12517 8631 402 -1494 1350 O ATOM 853 CB ILE A 138 -23.909 -11.453 57.521 1.00 83.01 C ANISOU 853 CB ILE A 138 12472 11131 7938 256 -1022 1041 C ATOM 854 CG1 ILE A 138 -25.197 -10.697 57.256 1.00 81.98 C ANISOU 854 CG1 ILE A 138 12379 10961 7807 175 -821 898 C ATOM 855 CG2 ILE A 138 -24.262 -12.814 58.018 1.00 84.13 C ANISOU 855 CG2 ILE A 138 12723 11205 8037 333 -918 1238 C ATOM 856 CD1 ILE A 138 -26.324 -11.595 56.832 1.00 86.07 C ANISOU 856 CD1 ILE A 138 12901 11372 8429 173 -583 966 C ATOM 857 N VAL A 139 -21.056 -11.765 57.835 1.00 86.46 N ANISOU 857 N VAL A 139 12710 11748 8395 371 -1516 1209 N ATOM 858 CA VAL A 139 -19.924 -12.617 58.022 1.00 88.44 C ANISOU 858 CA VAL A 139 12871 12046 8685 491 -1676 1399 C ATOM 859 C VAL A 139 -19.094 -12.017 59.118 1.00 95.62 C ANISOU 859 C VAL A 139 13824 13157 9351 464 -1944 1417 C ATOM 860 O VAL A 139 -18.425 -12.712 59.853 1.00 97.38 O ANISOU 860 O VAL A 139 14064 13468 9467 565 -2085 1613 O ATOM 861 CB VAL A 139 -19.403 -13.070 56.700 1.00 91.03 C ANISOU 861 CB VAL A 139 12976 12281 9330 548 -1634 1410 C ATOM 862 CG1 VAL A 139 -18.303 -14.044 56.901 1.00 92.84 C ANISOU 862 CG1 VAL A 139 13115 12539 9621 705 -1760 1626 C ATOM 863 CG2 VAL A 139 -20.509 -13.681 55.911 1.00 89.10 C ANISOU 863 CG2 VAL A 139 12772 11852 9231 540 -1360 1377 C ATOM 864 N HIS A 140 -19.124 -10.708 59.218 1.00 92.82 N ANISOU 864 N HIS A 140 13487 12875 8907 323 -2019 1213 N ATOM 865 CA HIS A 140 -18.316 -10.042 60.203 1.00 95.67 C ANISOU 865 CA HIS A 140 13890 13429 9032 257 -2287 1189 C ATOM 866 C HIS A 140 -19.100 -9.105 61.041 1.00101.10 C ANISOU 866 C HIS A 140 14821 14146 9447 138 -2242 1017 C ATOM 867 O HIS A 140 -18.809 -7.936 61.118 1.00100.97 O ANISOU 867 O HIS A 140 14806 14183 9374 3 -2353 829 O ATOM 868 CB HIS A 140 -17.483 -9.266 59.206 1.00 95.47 C ANISOU 868 CB HIS A 140 13614 13418 9241 180 -2397 1071 C ATOM 869 CG HIS A 140 -16.534 -10.121 58.442 1.00 98.93 C ANISOU 869 CG HIS A 140 13800 13857 9932 305 -2458 1238 C ATOM 870 ND1 HIS A 140 -15.706 -11.029 59.053 1.00103.22 N ANISOU 870 ND1 HIS A 140 14293 14509 10416 436 -2617 1470 N ATOM 871 CD2 HIS A 140 -16.297 -10.228 57.118 1.00 98.77 C ANISOU 871 CD2 HIS A 140 13568 13740 10220 333 -2364 1214 C ATOM 872 CE1 HIS A 140 -14.992 -11.656 58.139 1.00102.21 C ANISOU 872 CE1 HIS A 140 13930 14339 10566 549 -2608 1577 C ATOM 873 NE2 HIS A 140 -15.331 -11.187 56.956 1.00 99.81 N ANISOU 873 NE2 HIS A 140 13531 13913 10479 484 -2453 1416 N ATOM 874 N ALA A 141 -20.124 -9.643 61.665 1.00 99.07 N ANISOU 874 N ALA A 141 14776 13839 9027 190 -2056 1083 N ATOM 875 CA ALA A 141 -21.058 -8.845 62.418 1.00 99.97 C ANISOU 875 CA ALA A 141 15134 13958 8892 104 -1942 924 C ATOM 876 C ALA A 141 -20.699 -7.767 63.426 1.00107.11 C ANISOU 876 C ALA A 141 16201 15007 9490 -18 -2120 763 C ATOM 877 O ALA A 141 -21.238 -6.680 63.401 1.00106.47 O ANISOU 877 O ALA A 141 16217 14868 9370 -118 -2025 538 O ATOM 878 CB ALA A 141 -21.892 -9.739 63.279 1.00102.01 C ANISOU 878 CB ALA A 141 15603 14211 8947 189 -1783 1081 C ATOM 879 N THR A 142 -19.789 -8.087 64.325 1.00106.94 N ANISOU 879 N THR A 142 16213 15174 9246 -8 -2379 883 N ATOM 880 CA THR A 142 -19.414 -7.213 65.426 1.00109.96 C ANISOU 880 CA THR A 142 16777 15724 9278 -136 -2574 743 C ATOM 881 C THR A 142 -18.436 -6.191 64.875 1.00114.56 C ANISOU 881 C THR A 142 17177 16341 10008 -283 -2792 569 C ATOM 882 O THR A 142 -18.614 -4.988 65.029 1.00114.70 O ANISOU 882 O THR A 142 17313 16328 9941 -434 -2788 310 O ATOM 883 CB THR A 142 -18.641 -7.997 66.426 1.00119.13 C ANISOU 883 CB THR A 142 17976 17104 10182 -74 -2815 968 C ATOM 884 OG1 THR A 142 -17.409 -8.371 65.820 1.00119.89 O ANISOU 884 OG1 THR A 142 17768 17273 10511 -35 -3047 1104 O ATOM 885 CG2 THR A 142 -19.397 -9.250 66.787 1.00115.88 C ANISOU 885 CG2 THR A 142 17683 16641 9705 94 -2613 1215 C ATOM 886 N ASN A 143 -17.381 -6.688 64.257 1.00111.28 N ANISOU 886 N ASN A 143 16476 15986 9819 -236 -2973 718 N ATOM 887 CA ASN A 143 -16.255 -5.870 63.860 1.00111.94 C ANISOU 887 CA ASN A 143 16354 16152 10024 -376 -3222 609 C ATOM 888 C ASN A 143 -16.387 -5.160 62.537 1.00113.18 C ANISOU 888 C ASN A 143 16343 16125 10534 -436 -3084 455 C ATOM 889 O ASN A 143 -15.390 -4.781 61.949 1.00112.84 O ANISOU 889 O ASN A 143 16060 16134 10680 -512 -3257 438 O ATOM 890 CB ASN A 143 -15.032 -6.752 63.820 1.00114.52 C ANISOU 890 CB ASN A 143 16427 16648 10436 -279 -3469 865 C ATOM 891 CG ASN A 143 -15.306 -8.053 63.122 1.00138.17 C ANISOU 891 CG ASN A 143 19306 19521 13673 -56 -3281 1100 C ATOM 892 OD1 ASN A 143 -14.487 -8.552 62.352 1.00133.62 O ANISOU 892 OD1 ASN A 143 18450 18954 13366 30 -3352 1236 O ATOM 893 ND2 ASN A 143 -16.477 -8.612 63.380 1.00128.31 N ANISOU 893 ND2 ASN A 143 18272 18146 12332 34 -3024 1144 N ATOM 894 N SER A 144 -17.601 -4.985 62.049 1.00107.45 N ANISOU 894 N SER A 144 15727 15201 9900 -402 -2774 361 N ATOM 895 CA SER A 144 -17.761 -4.450 60.702 1.00104.49 C ANISOU 895 CA SER A 144 15174 14662 9866 -431 -2635 263 C ATOM 896 C SER A 144 -18.570 -3.166 60.553 1.00107.83 C ANISOU 896 C SER A 144 15746 14940 10286 -545 -2470 10 C ATOM 897 O SER A 144 -19.099 -2.875 59.481 1.00104.45 O ANISOU 897 O SER A 144 15217 14358 10109 -525 -2280 -36 O ATOM 898 CB SER A 144 -18.473 -5.604 59.993 1.00105.60 C ANISOU 898 CB SER A 144 15246 14692 10186 -255 -2403 431 C ATOM 899 OG SER A 144 -19.813 -5.263 59.682 1.00111.80 O ANISOU 899 OG SER A 144 16159 15319 11003 -249 -2114 322 O ATOM 900 N GLN A 145 -18.665 -2.405 61.639 1.00107.60 N ANISOU 900 N GLN A 145 15963 14958 9961 -658 -2541 -150 N ATOM 901 CA GLN A 145 -19.399 -1.146 61.631 1.00107.34 C ANISOU 901 CA GLN A 145 16106 14771 9909 -755 -2376 -397 C ATOM 902 C GLN A 145 -18.755 -0.133 60.693 1.00109.95 C ANISOU 902 C GLN A 145 16257 15012 10506 -887 -2447 -521 C ATOM 903 O GLN A 145 -19.404 0.807 60.236 1.00108.74 O ANISOU 903 O GLN A 145 16171 14679 10466 -925 -2261 -675 O ATOM 904 CB GLN A 145 -19.489 -0.572 63.046 1.00112.16 C ANISOU 904 CB GLN A 145 17035 15456 10124 -858 -2453 -558 C ATOM 905 CG GLN A 145 -18.305 -0.918 63.933 1.00131.70 C ANISOU 905 CG GLN A 145 19498 18178 12364 -939 -2807 -489 C ATOM 906 CD GLN A 145 -17.294 0.209 64.021 1.00153.52 C ANISOU 906 CD GLN A 145 22227 20980 15122 -1175 -3057 -686 C ATOM 907 OE1 GLN A 145 -17.106 0.965 63.068 1.00146.74 O ANISOU 907 OE1 GLN A 145 21223 19977 14554 -1254 -3015 -785 O ATOM 908 NE2 GLN A 145 -16.637 0.326 65.169 1.00149.61 N ANISOU 908 NE2 GLN A 145 21867 20687 14289 -1300 -3323 -737 N ATOM 909 N ARG A 146 -17.472 -0.331 60.409 1.00106.59 N ANISOU 909 N ARG A 146 15594 14715 10189 -950 -2709 -437 N ATOM 910 CA ARG A 146 -16.735 0.569 59.530 1.00105.72 C ANISOU 910 CA ARG A 146 15289 14542 10336 -1089 -2790 -527 C ATOM 911 C ARG A 146 -16.505 0.098 58.097 1.00105.27 C ANISOU 911 C ARG A 146 14920 14440 10640 -992 -2710 -377 C ATOM 912 O ARG A 146 -16.658 0.867 57.149 1.00103.83 O ANISOU 912 O ARG A 146 14652 14113 10684 -1042 -2591 -456 O ATOM 913 CB ARG A 146 -15.321 0.803 60.066 1.00110.26 C ANISOU 913 CB ARG A 146 15760 15310 10825 -1258 -3149 -540 C ATOM 914 CG ARG A 146 -14.959 2.268 60.245 1.00127.81 C ANISOU 914 CG ARG A 146 18077 17452 13032 -1510 -3238 -795 C ATOM 915 CD ARG A 146 -13.496 2.433 60.623 1.00147.51 C ANISOU 915 CD ARG A 146 20402 20161 15486 -1698 -3609 -786 C ATOM 916 NE ARG A 146 -13.210 3.772 61.129 1.00163.43 N ANISOU 916 NE ARG A 146 22587 22113 17396 -1973 -3718 -1059 N ATOM 917 CZ ARG A 146 -12.782 4.029 62.361 1.00183.61 C ANISOU 917 CZ ARG A 146 25321 24825 19615 -2139 -3958 -1180 C ATOM 918 NH1 ARG A 146 -12.588 3.036 63.219 1.00172.11 N ANISOU 918 NH1 ARG A 146 23888 23616 17892 -2041 -4119 -1026 N ATOM 919 NH2 ARG A 146 -12.546 5.279 62.736 1.00174.90 N ANISOU 919 NH2 ARG A 146 24384 23630 18438 -2408 -4037 -1455 N ATOM 920 N PRO A 147 -16.135 -1.170 57.949 1.00 99.79 N ANISOU 920 N PRO A 147 14066 13862 9987 -848 -2767 -159 N ATOM 921 CA PRO A 147 -15.875 -1.748 56.626 1.00 96.25 C ANISOU 921 CA PRO A 147 13336 13380 9853 -745 -2685 -21 C ATOM 922 C PRO A 147 -16.991 -1.330 55.674 1.00 94.07 C ANISOU 922 C PRO A 147 13094 12907 9739 -709 -2392 -95 C ATOM 923 O PRO A 147 -16.744 -1.136 54.484 1.00 91.31 O ANISOU 923 O PRO A 147 12540 12506 9649 -710 -2331 -73 O ATOM 924 CB PRO A 147 -15.984 -3.242 56.941 1.00 98.16 C ANISOU 924 CB PRO A 147 13572 13700 10023 -557 -2671 188 C ATOM 925 CG PRO A 147 -16.801 -3.302 58.183 1.00104.41 C ANISOU 925 CG PRO A 147 14674 14502 10496 -549 -2630 141 C ATOM 926 CD PRO A 147 -16.421 -2.088 58.979 1.00102.58 C ANISOU 926 CD PRO A 147 14577 14318 10080 -746 -2797 -53 C ATOM 927 N ARG A 148 -18.205 -1.194 56.199 1.00 88.70 N ANISOU 927 N ARG A 148 12663 12138 8902 -672 -2212 -171 N ATOM 928 CA ARG A 148 -19.351 -0.803 55.387 1.00 85.69 C ANISOU 928 CA ARG A 148 12307 11594 8656 -626 -1939 -224 C ATOM 929 C ARG A 148 -19.403 0.709 55.194 1.00 89.40 C ANISOU 929 C ARG A 148 12836 11942 9188 -760 -1907 -406 C ATOM 930 O ARG A 148 -19.469 1.199 54.067 1.00 87.64 O ANISOU 930 O ARG A 148 12468 11631 9201 -770 -1811 -408 O ATOM 931 CB ARG A 148 -20.652 -1.297 56.023 1.00 84.63 C ANISOU 931 CB ARG A 148 12387 11422 8347 -522 -1742 -210 C ATOM 932 CG ARG A 148 -20.757 -2.810 56.125 1.00 89.03 C ANISOU 932 CG ARG A 148 12902 12053 8873 -390 -1726 -21 C ATOM 933 CD ARG A 148 -21.704 -3.223 57.239 1.00 94.85 C ANISOU 933 CD ARG A 148 13890 12799 9350 -334 -1613 -8 C ATOM 934 NE ARG A 148 -23.074 -3.385 56.761 1.00 98.85 N ANISOU 934 NE ARG A 148 14426 13202 9932 -262 -1330 1 N ATOM 935 CZ ARG A 148 -24.139 -3.456 57.553 1.00115.87 C ANISOU 935 CZ ARG A 148 16783 15337 11903 -223 -1162 -14 C ATOM 936 NH1 ARG A 148 -23.995 -3.381 58.869 1.00105.28 N ANISOU 936 NH1 ARG A 148 15661 14069 10270 -244 -1242 -48 N ATOM 937 NH2 ARG A 148 -25.348 -3.603 57.030 1.00104.78 N ANISOU 937 NH2 ARG A 148 15356 13859 10597 -166 -915 8 N ATOM 938 N LYS A 149 -19.373 1.443 56.302 1.00 87.59 N ANISOU 938 N LYS A 149 12836 11704 8739 -865 -1982 -560 N ATOM 939 CA LYS A 149 -19.422 2.899 56.258 1.00 87.91 C ANISOU 939 CA LYS A 149 12981 11596 8826 -1001 -1943 -752 C ATOM 940 C LYS A 149 -18.534 3.451 55.147 1.00 89.94 C ANISOU 940 C LYS A 149 12987 11819 9368 -1098 -2024 -734 C ATOM 941 O LYS A 149 -19.018 4.092 54.214 1.00 88.82 O ANISOU 941 O LYS A 149 12791 11530 9427 -1080 -1849 -748 O ATOM 942 CB LYS A 149 -19.004 3.490 57.606 1.00 93.69 C ANISOU 942 CB LYS A 149 13955 12366 9279 -1150 -2109 -924 C ATOM 943 CG LYS A 149 -19.274 4.979 57.742 1.00107.42 C ANISOU 943 CG LYS A 149 15883 13903 11028 -1280 -2018 -1156 C ATOM 944 CD LYS A 149 -18.085 5.702 58.355 1.00119.31 C ANISOU 944 CD LYS A 149 17433 15457 12442 -1526 -2295 -1306 C ATOM 945 CE LYS A 149 -18.504 7.023 58.979 1.00130.34 C ANISOU 945 CE LYS A 149 19144 16651 13727 -1653 -2196 -1577 C ATOM 946 NZ LYS A 149 -17.330 7.875 59.317 1.00141.28 N ANISOU 946 NZ LYS A 149 20543 18043 15093 -1934 -2454 -1739 N ATOM 947 N LEU A 150 -17.234 3.199 55.254 1.00 86.04 N ANISOU 947 N LEU A 150 12330 11474 8889 -1196 -2287 -685 N ATOM 948 CA LEU A 150 -16.276 3.677 54.263 1.00 85.01 C ANISOU 948 CA LEU A 150 11942 11338 9022 -1299 -2372 -653 C ATOM 949 C LEU A 150 -16.600 3.202 52.850 1.00 84.74 C ANISOU 949 C LEU A 150 11690 11268 9238 -1158 -2194 -504 C ATOM 950 O LEU A 150 -16.497 3.997 51.921 1.00 83.31 O ANISOU 950 O LEU A 150 11405 10982 9266 -1219 -2115 -522 O ATOM 951 CB LEU A 150 -14.845 3.282 54.665 1.00 87.03 C ANISOU 951 CB LEU A 150 12021 11803 9244 -1400 -2684 -589 C ATOM 952 CG LEU A 150 -13.757 4.357 54.530 1.00 93.52 C ANISOU 952 CG LEU A 150 12730 12618 10184 -1645 -2860 -685 C ATOM 953 CD1 LEU A 150 -13.955 5.502 55.532 1.00 96.26 C ANISOU 953 CD1 LEU A 150 13377 12854 10342 -1839 -2908 -933 C ATOM 954 CD2 LEU A 150 -12.402 3.752 54.747 1.00 96.86 C ANISOU 954 CD2 LEU A 150 12903 13288 10613 -1700 -3149 -564 C ATOM 955 N LEU A 151 -17.006 1.929 52.687 1.00 79.75 N ANISOU 955 N LEU A 151 11004 10718 8579 -980 -2125 -362 N ATOM 956 CA LEU A 151 -17.367 1.342 51.387 1.00 76.82 C ANISOU 956 CA LEU A 151 10451 10329 8409 -851 -1958 -236 C ATOM 957 C LEU A 151 -18.589 2.028 50.755 1.00 78.83 C ANISOU 957 C LEU A 151 10792 10423 8738 -814 -1708 -289 C ATOM 958 O LEU A 151 -18.639 2.173 49.530 1.00 77.22 O ANISOU 958 O LEU A 151 10422 10189 8731 -790 -1607 -227 O ATOM 959 CB LEU A 151 -17.611 -0.172 51.520 1.00 76.13 C ANISOU 959 CB LEU A 151 10341 10335 8252 -688 -1933 -99 C ATOM 960 CG LEU A 151 -17.547 -0.993 50.233 1.00 79.72 C ANISOU 960 CG LEU A 151 10577 10809 8904 -581 -1831 30 C ATOM 961 CD1 LEU A 151 -16.124 -1.429 49.924 1.00 81.21 C ANISOU 961 CD1 LEU A 151 10529 11121 9207 -587 -2002 126 C ATOM 962 CD2 LEU A 151 -18.436 -2.212 50.325 1.00 82.01 C ANISOU 962 CD2 LEU A 151 10946 11095 9120 -436 -1698 108 C ATOM 963 N ALA A 152 -19.559 2.455 51.599 1.00 75.39 N ANISOU 963 N ALA A 152 10609 9897 8137 -803 -1607 -394 N ATOM 964 CA ALA A 152 -20.791 3.124 51.183 1.00 73.85 C ANISOU 964 CA ALA A 152 10505 9558 7996 -746 -1367 -435 C ATOM 965 C ALA A 152 -20.599 4.610 50.938 1.00 78.41 C ANISOU 965 C ALA A 152 11124 9981 8686 -862 -1342 -545 C ATOM 966 O ALA A 152 -21.184 5.142 49.994 1.00 77.03 O ANISOU 966 O ALA A 152 10883 9711 8673 -814 -1176 -506 O ATOM 967 CB ALA A 152 -21.884 2.906 52.219 1.00 75.01 C ANISOU 967 CB ALA A 152 10894 9679 7926 -668 -1248 -488 C ATOM 968 N GLU A 153 -19.805 5.280 51.791 1.00 77.13 N ANISOU 968 N GLU A 153 11077 9793 8435 -1019 -1507 -678 N ATOM 969 CA GLU A 153 -19.568 6.722 51.710 1.00 78.58 C ANISOU 969 CA GLU A 153 11341 9797 8718 -1159 -1489 -808 C ATOM 970 C GLU A 153 -18.414 7.145 50.801 1.00 83.91 C ANISOU 970 C GLU A 153 11780 10482 9620 -1291 -1607 -755 C ATOM 971 O GLU A 153 -18.446 8.265 50.292 1.00 84.64 O ANISOU 971 O GLU A 153 11890 10401 9870 -1365 -1517 -799 O ATOM 972 CB GLU A 153 -19.375 7.321 53.108 1.00 82.75 C ANISOU 972 CB GLU A 153 12145 10271 9024 -1292 -1591 -1012 C ATOM 973 CG GLU A 153 -20.637 7.337 53.955 1.00 94.20 C ANISOU 973 CG GLU A 153 13873 11647 10272 -1172 -1404 -1098 C ATOM 974 CD GLU A 153 -20.419 7.356 55.457 1.00122.42 C ANISOU 974 CD GLU A 153 17707 15271 13537 -1266 -1534 -1261 C ATOM 975 OE1 GLU A 153 -19.384 7.896 55.912 1.00122.33 O ANISOU 975 OE1 GLU A 153 17732 15270 13478 -1472 -1749 -1382 O ATOM 976 OE2 GLU A 153 -21.304 6.851 56.186 1.00117.82 O ANISOU 976 OE2 GLU A 153 17294 14724 12748 -1142 -1418 -1267 O ATOM 977 N LYS A 154 -17.389 6.284 50.617 1.00 80.25 N ANISOU 977 N LYS A 154 11098 10215 9180 -1316 -1796 -651 N ATOM 978 CA LYS A 154 -16.206 6.625 49.815 1.00 80.15 C ANISOU 978 CA LYS A 154 10836 10240 9376 -1444 -1910 -590 C ATOM 979 C LYS A 154 -15.988 5.745 48.569 1.00 81.20 C ANISOU 979 C LYS A 154 10686 10496 9670 -1318 -1855 -396 C ATOM 980 O LYS A 154 -15.963 6.269 47.457 1.00 79.92 O ANISOU 980 O LYS A 154 10395 10267 9703 -1328 -1742 -332 O ATOM 981 CB LYS A 154 -14.929 6.654 50.687 1.00 84.95 C ANISOU 981 CB LYS A 154 11406 10972 9900 -1629 -2201 -654 C ATOM 982 CG LYS A 154 -15.068 7.339 52.047 1.00100.62 C ANISOU 982 CG LYS A 154 13690 12879 11664 -1766 -2290 -865 C ATOM 983 CD LYS A 154 -14.580 8.781 52.036 1.00115.65 C ANISOU 983 CD LYS A 154 15657 14604 13679 -2008 -2324 -1014 C ATOM 984 CE LYS A 154 -14.547 9.360 53.431 1.00132.69 C ANISOU 984 CE LYS A 154 18111 16712 15592 -2170 -2446 -1245 C ATOM 985 NZ LYS A 154 -13.935 10.715 53.457 1.00145.59 N ANISOU 985 NZ LYS A 154 19807 18170 17341 -2444 -2505 -1406 N ATOM 986 N VAL A 155 -15.812 4.422 48.766 1.00 77.27 N ANISOU 986 N VAL A 155 10105 10169 9084 -1201 -1927 -303 N ATOM 987 CA VAL A 155 -15.531 3.410 47.729 1.00 75.81 C ANISOU 987 CA VAL A 155 9679 10104 9022 -1076 -1882 -141 C ATOM 988 C VAL A 155 -16.599 3.340 46.600 1.00 78.59 C ANISOU 988 C VAL A 155 10014 10384 9461 -952 -1635 -81 C ATOM 989 O VAL A 155 -16.246 2.996 45.470 1.00 77.52 O ANISOU 989 O VAL A 155 9674 10312 9468 -909 -1581 23 O ATOM 990 CB VAL A 155 -15.188 2.011 48.349 1.00 79.76 C ANISOU 990 CB VAL A 155 10144 10763 9399 -968 -2000 -64 C ATOM 991 CG1 VAL A 155 -14.646 1.032 47.306 1.00 78.42 C ANISOU 991 CG1 VAL A 155 9721 10699 9375 -856 -1964 85 C ATOM 992 CG2 VAL A 155 -14.197 2.142 49.504 1.00 82.19 C ANISOU 992 CG2 VAL A 155 10467 11168 9593 -1091 -2261 -109 C ATOM 993 N VAL A 156 -17.873 3.699 46.887 1.00 74.95 N ANISOU 993 N VAL A 156 9759 9806 8914 -899 -1487 -144 N ATOM 994 CA VAL A 156 -18.937 3.678 45.873 1.00 73.29 C ANISOU 994 CA VAL A 156 9519 9554 8774 -790 -1273 -78 C ATOM 995 C VAL A 156 -18.740 4.719 44.736 1.00 77.70 C ANISOU 995 C VAL A 156 9957 10040 9525 -849 -1193 -34 C ATOM 996 O VAL A 156 -19.204 4.502 43.617 1.00 75.82 O ANISOU 996 O VAL A 156 9605 9840 9363 -768 -1064 64 O ATOM 997 CB VAL A 156 -20.367 3.665 46.487 1.00 76.80 C ANISOU 997 CB VAL A 156 10174 9924 9082 -699 -1132 -129 C ATOM 998 CG1 VAL A 156 -20.891 5.077 46.747 1.00 77.71 C ANISOU 998 CG1 VAL A 156 10444 9860 9221 -747 -1039 -219 C ATOM 999 CG2 VAL A 156 -21.338 2.871 45.614 1.00 74.56 C ANISOU 999 CG2 VAL A 156 9809 9702 8819 -568 -977 -29 C ATOM 1000 N TYR A 157 -18.035 5.824 45.021 1.00 76.57 N ANISOU 1000 N TYR A 157 9842 9798 9452 -999 -1271 -102 N ATOM 1001 CA TYR A 157 -17.785 6.867 44.029 1.00 77.02 C ANISOU 1001 CA TYR A 157 9801 9764 9699 -1069 -1193 -48 C ATOM 1002 C TYR A 157 -16.608 6.507 43.135 1.00 81.85 C ANISOU 1002 C TYR A 157 10145 10513 10442 -1118 -1266 60 C ATOM 1003 O TYR A 157 -16.711 6.613 41.913 1.00 81.07 O ANISOU 1003 O TYR A 157 9909 10439 10454 -1074 -1146 174 O ATOM 1004 CB TYR A 157 -17.585 8.229 44.712 1.00 80.13 C ANISOU 1004 CB TYR A 157 10360 9958 10127 -1224 -1222 -174 C ATOM 1005 CG TYR A 157 -18.815 8.707 45.454 1.00 82.13 C ANISOU 1005 CG TYR A 157 10881 10053 10270 -1151 -1095 -275 C ATOM 1006 CD1 TYR A 157 -18.969 8.465 46.816 1.00 85.13 C ANISOU 1006 CD1 TYR A 157 11463 10429 10452 -1170 -1179 -419 C ATOM 1007 CD2 TYR A 157 -19.840 9.375 44.789 1.00 82.47 C ANISOU 1007 CD2 TYR A 157 10968 9967 10400 -1049 -881 -213 C ATOM 1008 CE1 TYR A 157 -20.106 8.892 47.502 1.00 86.99 C ANISOU 1008 CE1 TYR A 157 11946 10525 10582 -1091 -1035 -513 C ATOM 1009 CE2 TYR A 157 -20.979 9.810 45.464 1.00 83.97 C ANISOU 1009 CE2 TYR A 157 11385 10017 10504 -960 -743 -295 C ATOM 1010 CZ TYR A 157 -21.103 9.576 46.824 1.00 94.22 C ANISOU 1010 CZ TYR A 157 12889 11303 11609 -983 -812 -452 C ATOM 1011 OH TYR A 157 -22.223 10.008 47.492 1.00 97.46 O ANISOU 1011 OH TYR A 157 13523 11578 11931 -885 -651 -534 O ATOM 1012 N VAL A 158 -15.501 6.032 43.735 1.00 79.68 N ANISOU 1012 N VAL A 158 9786 10347 10144 -1197 -1459 34 N ATOM 1013 CA VAL A 158 -14.254 5.628 43.085 1.00 79.97 C ANISOU 1013 CA VAL A 158 9552 10530 10303 -1237 -1543 133 C ATOM 1014 C VAL A 158 -14.428 4.325 42.277 1.00 81.64 C ANISOU 1014 C VAL A 158 9632 10887 10501 -1058 -1457 241 C ATOM 1015 O VAL A 158 -13.939 4.241 41.151 1.00 80.76 O ANISOU 1015 O VAL A 158 9324 10847 10513 -1044 -1386 342 O ATOM 1016 CB VAL A 158 -13.115 5.517 44.145 1.00 86.27 C ANISOU 1016 CB VAL A 158 10306 11411 11063 -1365 -1789 76 C ATOM 1017 CG1 VAL A 158 -12.941 4.087 44.655 1.00 85.76 C ANISOU 1017 CG1 VAL A 158 10202 11508 10875 -1228 -1882 116 C ATOM 1018 CG2 VAL A 158 -11.793 6.058 43.602 1.00 87.86 C ANISOU 1018 CG2 VAL A 158 10260 11669 11455 -1521 -1872 139 C ATOM 1019 N GLY A 159 -15.128 3.347 42.879 1.00 77.44 N ANISOU 1019 N GLY A 159 9224 10386 9814 -935 -1455 211 N ATOM 1020 CA GLY A 159 -15.319 2.014 42.310 1.00 76.01 C ANISOU 1020 CA GLY A 159 8961 10313 9606 -780 -1383 285 C ATOM 1021 C GLY A 159 -16.529 1.761 41.432 1.00 78.39 C ANISOU 1021 C GLY A 159 9310 10594 9882 -679 -1188 312 C ATOM 1022 O GLY A 159 -16.542 0.763 40.701 1.00 76.90 O ANISOU 1022 O GLY A 159 9030 10493 9697 -584 -1118 366 O ATOM 1023 N VAL A 160 -17.570 2.621 41.514 1.00 74.59 N ANISOU 1023 N VAL A 160 8972 9999 9369 -696 -1098 274 N ATOM 1024 CA VAL A 160 -18.792 2.457 40.706 1.00 72.54 C ANISOU 1024 CA VAL A 160 8737 9745 9081 -606 -929 314 C ATOM 1025 C VAL A 160 -19.015 3.642 39.770 1.00 76.18 C ANISOU 1025 C VAL A 160 9145 10152 9649 -645 -828 375 C ATOM 1026 O VAL A 160 -19.138 3.434 38.563 1.00 75.09 O ANISOU 1026 O VAL A 160 8883 10103 9547 -606 -736 462 O ATOM 1027 CB VAL A 160 -20.072 2.115 41.534 1.00 75.48 C ANISOU 1027 CB VAL A 160 9300 10068 9312 -538 -878 257 C ATOM 1028 CG1 VAL A 160 -21.248 1.740 40.635 1.00 73.75 C ANISOU 1028 CG1 VAL A 160 9053 9900 9067 -457 -726 313 C ATOM 1029 CG2 VAL A 160 -19.807 1.005 42.538 1.00 75.47 C ANISOU 1029 CG2 VAL A 160 9367 10106 9202 -504 -977 217 C ATOM 1030 N TRP A 161 -19.079 4.870 40.320 1.00 73.71 N ANISOU 1030 N TRP A 161 8938 9689 9378 -721 -838 331 N ATOM 1031 CA TRP A 161 -19.346 6.084 39.550 1.00 74.32 C ANISOU 1031 CA TRP A 161 8995 9673 9570 -748 -729 403 C ATOM 1032 C TRP A 161 -18.253 6.500 38.577 1.00 79.90 C ANISOU 1032 C TRP A 161 9514 10422 10421 -832 -738 495 C ATOM 1033 O TRP A 161 -18.577 6.838 37.437 1.00 80.08 O ANISOU 1033 O TRP A 161 9452 10478 10496 -795 -619 614 O ATOM 1034 CB TRP A 161 -19.786 7.236 40.454 1.00 74.42 C ANISOU 1034 CB TRP A 161 9206 9478 9594 -793 -710 318 C ATOM 1035 CG TRP A 161 -21.109 6.981 41.107 1.00 74.64 C ANISOU 1035 CG TRP A 161 9396 9471 9494 -679 -630 268 C ATOM 1036 CD1 TRP A 161 -21.324 6.589 42.394 1.00 77.83 C ANISOU 1036 CD1 TRP A 161 9963 9846 9763 -674 -693 144 C ATOM 1037 CD2 TRP A 161 -22.397 7.015 40.477 1.00 73.59 C ANISOU 1037 CD2 TRP A 161 9255 9360 9347 -550 -472 358 C ATOM 1038 NE1 TRP A 161 -22.666 6.400 42.613 1.00 76.43 N ANISOU 1038 NE1 TRP A 161 9881 9658 9499 -553 -566 149 N ATOM 1039 CE2 TRP A 161 -23.350 6.653 41.453 1.00 77.09 C ANISOU 1039 CE2 TRP A 161 9852 9778 9663 -476 -436 280 C ATOM 1040 CE3 TRP A 161 -22.840 7.327 39.179 1.00 74.53 C ANISOU 1040 CE3 TRP A 161 9242 9535 9541 -493 -362 509 C ATOM 1041 CZ2 TRP A 161 -24.720 6.595 41.178 1.00 75.80 C ANISOU 1041 CZ2 TRP A 161 9692 9643 9465 -351 -293 347 C ATOM 1042 CZ3 TRP A 161 -24.199 7.270 38.906 1.00 75.32 C ANISOU 1042 CZ3 TRP A 161 9350 9674 9592 -368 -239 578 C ATOM 1043 CH2 TRP A 161 -25.123 6.915 39.900 1.00 75.89 C ANISOU 1043 CH2 TRP A 161 9556 9720 9559 -300 -204 497 C ATOM 1044 N ILE A 162 -16.970 6.468 39.009 1.00 76.81 N ANISOU 1044 N ILE A 162 9047 10049 10087 -945 -878 455 N ATOM 1045 CA ILE A 162 -15.816 6.792 38.160 1.00 77.18 C ANISOU 1045 CA ILE A 162 8889 10155 10280 -1035 -887 548 C ATOM 1046 C ILE A 162 -15.631 5.783 36.995 1.00 80.14 C ANISOU 1046 C ILE A 162 9084 10725 10640 -934 -812 648 C ATOM 1047 O ILE A 162 -15.585 6.241 35.852 1.00 79.60 O ANISOU 1047 O ILE A 162 8914 10689 10642 -938 -698 763 O ATOM 1048 CB ILE A 162 -14.530 7.131 38.983 1.00 81.97 C ANISOU 1048 CB ILE A 162 9444 10738 10964 -1201 -1063 482 C ATOM 1049 CG1 ILE A 162 -14.349 8.650 39.128 1.00 84.65 C ANISOU 1049 CG1 ILE A 162 9856 10877 11429 -1365 -1052 463 C ATOM 1050 CG2 ILE A 162 -13.251 6.491 38.426 1.00 82.57 C ANISOU 1050 CG2 ILE A 162 9259 10993 11122 -1223 -1120 563 C ATOM 1051 CD1 ILE A 162 -15.279 9.332 40.142 1.00 94.59 C ANISOU 1051 CD1 ILE A 162 11396 11932 12612 -1375 -1041 331 C ATOM 1052 N PRO A 163 -15.603 4.437 37.213 1.00 76.09 N ANISOU 1052 N PRO A 163 8550 10332 10027 -838 -853 610 N ATOM 1053 CA PRO A 163 -15.462 3.522 36.069 1.00 75.31 C ANISOU 1053 CA PRO A 163 8312 10391 9912 -747 -758 681 C ATOM 1054 C PRO A 163 -16.662 3.556 35.122 1.00 78.03 C ANISOU 1054 C PRO A 163 8704 10765 10179 -674 -608 731 C ATOM 1055 O PRO A 163 -16.483 3.335 33.921 1.00 78.23 O ANISOU 1055 O PRO A 163 8609 10908 10207 -646 -510 810 O ATOM 1056 CB PRO A 163 -15.273 2.149 36.728 1.00 76.72 C ANISOU 1056 CB PRO A 163 8507 10633 10009 -663 -833 615 C ATOM 1057 CG PRO A 163 -14.888 2.447 38.149 1.00 81.89 C ANISOU 1057 CG PRO A 163 9246 11207 10663 -734 -1000 541 C ATOM 1058 CD PRO A 163 -15.663 3.674 38.474 1.00 77.46 C ANISOU 1058 CD PRO A 163 8834 10498 10098 -807 -976 507 C ATOM 1059 N ALA A 164 -17.869 3.889 35.649 1.00 73.33 N ANISOU 1059 N ALA A 164 8274 10075 9512 -645 -589 693 N ATOM 1060 CA ALA A 164 -19.105 4.011 34.862 1.00 72.20 C ANISOU 1060 CA ALA A 164 8162 9972 9299 -578 -467 755 C ATOM 1061 C ALA A 164 -18.948 5.091 33.794 1.00 76.91 C ANISOU 1061 C ALA A 164 8667 10573 9984 -613 -380 893 C ATOM 1062 O ALA A 164 -19.357 4.879 32.653 1.00 76.26 O ANISOU 1062 O ALA A 164 8509 10624 9841 -567 -289 980 O ATOM 1063 CB ALA A 164 -20.285 4.334 35.765 1.00 72.44 C ANISOU 1063 CB ALA A 164 8364 9889 9271 -542 -462 702 C ATOM 1064 N LEU A 165 -18.298 6.215 34.157 1.00 74.56 N ANISOU 1064 N LEU A 165 8376 10132 9823 -707 -410 913 N ATOM 1065 CA LEU A 165 -18.015 7.334 33.265 1.00 75.34 C ANISOU 1065 CA LEU A 165 8397 10193 10034 -758 -325 1056 C ATOM 1066 C LEU A 165 -16.895 7.003 32.268 1.00 79.89 C ANISOU 1066 C LEU A 165 8778 10923 10655 -797 -297 1137 C ATOM 1067 O LEU A 165 -16.937 7.469 31.129 1.00 79.56 O ANISOU 1067 O LEU A 165 8655 10948 10628 -790 -188 1283 O ATOM 1068 CB LEU A 165 -17.657 8.573 34.085 1.00 76.71 C ANISOU 1068 CB LEU A 165 8663 10135 10349 -869 -365 1026 C ATOM 1069 CG LEU A 165 -18.773 9.583 34.259 1.00 81.80 C ANISOU 1069 CG LEU A 165 9457 10606 11015 -819 -276 1064 C ATOM 1070 CD1 LEU A 165 -19.555 9.321 35.522 1.00 81.35 C ANISOU 1070 CD1 LEU A 165 9583 10458 10868 -769 -325 911 C ATOM 1071 CD2 LEU A 165 -18.217 10.980 34.309 1.00 87.00 C ANISOU 1071 CD2 LEU A 165 10149 11052 11854 -939 -245 1114 C ATOM 1072 N LEU A 166 -15.899 6.198 32.695 1.00 77.30 N ANISOU 1072 N LEU A 166 8370 10657 10341 -827 -388 1054 N ATOM 1073 CA LEU A 166 -14.776 5.787 31.842 1.00 78.27 C ANISOU 1073 CA LEU A 166 8296 10930 10514 -844 -349 1122 C ATOM 1074 C LEU A 166 -15.255 4.913 30.685 1.00 82.14 C ANISOU 1074 C LEU A 166 8744 11603 10862 -734 -232 1161 C ATOM 1075 O LEU A 166 -14.706 4.995 29.582 1.00 82.67 O ANISOU 1075 O LEU A 166 8677 11789 10945 -741 -129 1265 O ATOM 1076 CB LEU A 166 -13.686 5.055 32.647 1.00 78.79 C ANISOU 1076 CB LEU A 166 8281 11026 10630 -870 -475 1034 C ATOM 1077 CG LEU A 166 -12.965 5.860 33.727 1.00 85.19 C ANISOU 1077 CG LEU A 166 9096 11703 11570 -1013 -616 990 C ATOM 1078 CD1 LEU A 166 -12.244 4.951 34.695 1.00 85.83 C ANISOU 1078 CD1 LEU A 166 9133 11838 11640 -1001 -768 899 C ATOM 1079 CD2 LEU A 166 -12.003 6.874 33.129 1.00 89.72 C ANISOU 1079 CD2 LEU A 166 9512 12262 12316 -1151 -576 1107 C ATOM 1080 N LEU A 167 -16.288 4.090 30.935 1.00 77.69 N ANISOU 1080 N LEU A 167 8299 11065 10154 -646 -242 1073 N ATOM 1081 CA LEU A 167 -16.879 3.220 29.917 1.00 77.35 C ANISOU 1081 CA LEU A 167 8246 11189 9956 -568 -147 1078 C ATOM 1082 C LEU A 167 -17.846 3.991 29.011 1.00 82.44 C ANISOU 1082 C LEU A 167 8907 11885 10532 -559 -60 1203 C ATOM 1083 O LEU A 167 -18.259 3.475 27.973 1.00 82.21 O ANISOU 1083 O LEU A 167 8848 12024 10364 -521 18 1231 O ATOM 1084 CB LEU A 167 -17.581 2.007 30.560 1.00 76.08 C ANISOU 1084 CB LEU A 167 8197 11028 9680 -502 -194 937 C ATOM 1085 CG LEU A 167 -16.705 1.029 31.357 1.00 80.76 C ANISOU 1085 CG LEU A 167 8777 11592 10316 -477 -268 836 C ATOM 1086 CD1 LEU A 167 -17.552 -0.024 32.019 1.00 79.85 C ANISOU 1086 CD1 LEU A 167 8799 11446 10093 -421 -302 724 C ATOM 1087 CD2 LEU A 167 -15.642 0.361 30.482 1.00 84.02 C ANISOU 1087 CD2 LEU A 167 9046 12128 10751 -444 -189 854 C ATOM 1088 N THR A 168 -18.184 5.233 29.398 1.00 80.12 N ANISOU 1088 N THR A 168 8663 11445 10333 -593 -72 1280 N ATOM 1089 CA THR A 168 -19.098 6.107 28.672 1.00 80.63 C ANISOU 1089 CA THR A 168 8741 11529 10364 -564 6 1431 C ATOM 1090 C THR A 168 -18.417 6.945 27.562 1.00 85.52 C ANISOU 1090 C THR A 168 9244 12204 11048 -606 103 1615 C ATOM 1091 O THR A 168 -19.114 7.565 26.762 1.00 85.88 O ANISOU 1091 O THR A 168 9282 12307 11043 -568 176 1773 O ATOM 1092 CB THR A 168 -20.036 6.823 29.666 1.00 93.29 C ANISOU 1092 CB THR A 168 10482 12945 12018 -539 -29 1412 C ATOM 1093 OG1 THR A 168 -21.385 6.681 29.233 1.00 95.90 O ANISOU 1093 OG1 THR A 168 10839 13379 12220 -453 11 1469 O ATOM 1094 CG2 THR A 168 -19.701 8.292 29.885 1.00 94.06 C ANISOU 1094 CG2 THR A 168 10606 12838 12293 -595 0 1511 C ATOM 1095 N ILE A 169 -17.064 6.938 27.500 1.00 82.45 N ANISOU 1095 N ILE A 169 8750 11811 10767 -681 106 1611 N ATOM 1096 CA ILE A 169 -16.268 7.642 26.479 1.00 83.59 C ANISOU 1096 CA ILE A 169 8766 12014 10980 -735 211 1786 C ATOM 1097 C ILE A 169 -16.558 7.101 25.052 1.00 88.84 C ANISOU 1097 C ILE A 169 9367 12941 11449 -671 322 1874 C ATOM 1098 O ILE A 169 -16.899 7.926 24.206 1.00 89.33 O ANISOU 1098 O ILE A 169 9409 13046 11485 -665 407 2065 O ATOM 1099 CB ILE A 169 -14.747 7.754 26.844 1.00 87.24 C ANISOU 1099 CB ILE A 169 9107 12421 11621 -842 184 1761 C ATOM 1100 CG1 ILE A 169 -14.545 8.575 28.136 1.00 87.82 C ANISOU 1100 CG1 ILE A 169 9259 12238 11872 -940 72 1697 C ATOM 1101 CG2 ILE A 169 -13.926 8.371 25.706 1.00 89.32 C ANISOU 1101 CG2 ILE A 169 9220 12772 11947 -899 318 1952 C ATOM 1102 CD1 ILE A 169 -13.444 8.084 29.060 1.00 93.24 C ANISOU 1102 CD1 ILE A 169 9873 12899 12656 -1013 -50 1565 C ATOM 1103 N PRO A 170 -16.536 5.763 24.754 1.00 85.81 N ANISOU 1103 N PRO A 170 8969 12725 10908 -619 327 1744 N ATOM 1104 CA PRO A 170 -16.870 5.308 23.384 1.00 86.80 C ANISOU 1104 CA PRO A 170 9062 13099 10819 -577 432 1807 C ATOM 1105 C PRO A 170 -18.300 5.640 22.922 1.00 92.95 C ANISOU 1105 C PRO A 170 9912 13960 11445 -534 425 1900 C ATOM 1106 O PRO A 170 -18.678 5.324 21.796 1.00 93.26 O ANISOU 1106 O PRO A 170 9930 14226 11280 -513 489 1958 O ATOM 1107 CB PRO A 170 -16.616 3.793 23.437 1.00 87.45 C ANISOU 1107 CB PRO A 170 9157 13275 10795 -539 428 1604 C ATOM 1108 CG PRO A 170 -15.724 3.597 24.601 1.00 91.14 C ANISOU 1108 CG PRO A 170 9600 13574 11456 -558 349 1502 C ATOM 1109 CD PRO A 170 -16.168 4.610 25.600 1.00 86.15 C ANISOU 1109 CD PRO A 170 9037 12738 10959 -599 248 1539 C ATOM 1110 N ASP A 171 -19.088 6.288 23.789 1.00 90.26 N ANISOU 1110 N ASP A 171 9651 13447 11196 -519 349 1917 N ATOM 1111 CA ASP A 171 -20.437 6.744 23.482 1.00 90.78 C ANISOU 1111 CA ASP A 171 9758 13571 11162 -461 342 2034 C ATOM 1112 C ASP A 171 -20.413 8.258 23.294 1.00 95.46 C ANISOU 1112 C ASP A 171 10334 14036 11901 -458 401 2269 C ATOM 1113 O ASP A 171 -21.316 8.802 22.661 1.00 95.78 O ANISOU 1113 O ASP A 171 10365 14168 11860 -395 431 2448 O ATOM 1114 CB ASP A 171 -21.425 6.325 24.581 1.00 91.97 C ANISOU 1114 CB ASP A 171 10011 13622 11313 -424 245 1890 C ATOM 1115 CG ASP A 171 -21.731 4.839 24.610 1.00107.71 C ANISOU 1115 CG ASP A 171 12031 15752 13141 -426 201 1694 C ATOM 1116 OD1 ASP A 171 -22.929 4.483 24.662 1.00108.72 O ANISOU 1116 OD1 ASP A 171 12194 15961 13154 -397 161 1671 O ATOM 1117 OD2 ASP A 171 -20.769 4.028 24.607 1.00115.10 O ANISOU 1117 OD2 ASP A 171 12951 16704 14077 -457 212 1567 O ATOM 1118 N PHE A 172 -19.368 8.910 23.778 1.00 92.40 N ANISOU 1118 N PHE A 172 9933 13450 11725 -528 419 2278 N ATOM 1119 CA PHE A 172 -19.235 10.334 23.566 1.00 93.72 C ANISOU 1119 CA PHE A 172 10095 13465 12050 -546 492 2496 C ATOM 1120 C PHE A 172 -18.883 10.555 22.126 1.00 97.36 C ANISOU 1120 C PHE A 172 10450 14134 12408 -548 607 2707 C ATOM 1121 O PHE A 172 -19.142 11.603 21.560 1.00 98.48 O ANISOU 1121 O PHE A 172 10585 14240 12595 -524 686 2949 O ATOM 1122 CB PHE A 172 -18.136 10.889 24.434 1.00 96.29 C ANISOU 1122 CB PHE A 172 10428 13538 12621 -659 472 2429 C ATOM 1123 CG PHE A 172 -18.596 11.293 25.775 1.00 97.76 C ANISOU 1123 CG PHE A 172 10751 13460 12933 -659 392 2307 C ATOM 1124 CD1 PHE A 172 -17.927 10.879 26.897 1.00100.95 C ANISOU 1124 CD1 PHE A 172 11187 13747 13422 -738 289 2095 C ATOM 1125 CD2 PHE A 172 -19.696 12.085 25.918 1.00100.48 C ANISOU 1125 CD2 PHE A 172 11190 13684 13302 -572 425 2411 C ATOM 1126 CE1 PHE A 172 -18.347 11.253 28.136 1.00101.61 C ANISOU 1126 CE1 PHE A 172 11414 13601 13591 -744 221 1973 C ATOM 1127 CE2 PHE A 172 -20.120 12.457 27.150 1.00103.21 C ANISOU 1127 CE2 PHE A 172 11676 13786 13754 -565 375 2287 C ATOM 1128 CZ PHE A 172 -19.445 12.041 28.263 1.00100.76 C ANISOU 1128 CZ PHE A 172 11416 13365 13505 -657 273 2060 C ATOM 1129 N ILE A 173 -18.291 9.534 21.538 1.00 92.31 N ANISOU 1129 N ILE A 173 9737 13712 11623 -570 627 2615 N ATOM 1130 CA ILE A 173 -17.873 9.566 20.160 1.00 93.16 C ANISOU 1130 CA ILE A 173 9751 14052 11592 -575 748 2781 C ATOM 1131 C ILE A 173 -18.598 9.012 18.961 1.00 96.47 C ANISOU 1131 C ILE A 173 10159 14795 11701 -515 782 2847 C ATOM 1132 O ILE A 173 -18.821 9.690 17.980 1.00 98.38 O ANISOU 1132 O ILE A 173 10365 15163 11853 -492 861 3092 O ATOM 1133 CB ILE A 173 -16.716 8.646 19.972 1.00 96.09 C ANISOU 1133 CB ILE A 173 10044 14528 11940 -623 791 2638 C ATOM 1134 CG1 ILE A 173 -15.441 9.243 20.527 1.00 97.36 C ANISOU 1134 CG1 ILE A 173 10127 14491 12375 -720 815 2656 C ATOM 1135 CG2 ILE A 173 -16.576 8.324 18.532 1.00 97.89 C ANISOU 1135 CG2 ILE A 173 10210 15051 11931 -603 914 2745 C ATOM 1136 CD1 ILE A 173 -14.494 8.192 21.004 1.00104.72 C ANISOU 1136 CD1 ILE A 173 10996 15447 13346 -742 786 2443 C ATOM 1137 N PHE A 174 -18.961 7.745 19.070 1.00 89.84 N ANISOU 1137 N PHE A 174 9355 14086 10692 -499 717 2622 N ATOM 1138 CA PHE A 174 -19.499 6.955 17.975 1.00 89.44 C ANISOU 1138 CA PHE A 174 9304 14355 10325 -478 738 2606 C ATOM 1139 C PHE A 174 -20.983 7.221 17.883 1.00 92.46 C ANISOU 1139 C PHE A 174 9722 14824 10587 -424 650 2703 C ATOM 1140 O PHE A 174 -21.660 6.645 17.046 1.00 93.28 O ANISOU 1140 O PHE A 174 9825 15203 10416 -422 631 2698 O ATOM 1141 CB PHE A 174 -19.295 5.471 18.188 1.00 89.72 C ANISOU 1141 CB PHE A 174 9380 14457 10251 -496 711 2310 C ATOM 1142 CG PHE A 174 -17.880 5.052 18.108 1.00 91.33 C ANISOU 1142 CG PHE A 174 9527 14635 10538 -522 812 2225 C ATOM 1143 CD1 PHE A 174 -17.361 4.184 19.018 1.00 92.78 C ANISOU 1143 CD1 PHE A 174 9733 14683 10836 -522 770 1997 C ATOM 1144 CD2 PHE A 174 -17.066 5.533 17.116 1.00 94.65 C ANISOU 1144 CD2 PHE A 174 9860 15177 10923 -538 957 2393 C ATOM 1145 CE1 PHE A 174 -16.065 3.812 18.934 1.00 93.96 C ANISOU 1145 CE1 PHE A 174 9804 14823 11073 -527 865 1943 C ATOM 1146 CE2 PHE A 174 -15.779 5.153 17.031 1.00 97.47 C ANISOU 1146 CE2 PHE A 174 10141 15527 11367 -553 1063 2329 C ATOM 1147 CZ PHE A 174 -15.278 4.298 17.938 1.00 94.30 C ANISOU 1147 CZ PHE A 174 9747 14995 11090 -542 1015 2105 C ATOM 1148 N ALA A 175 -21.506 8.073 18.738 1.00 86.96 N ANISOU 1148 N ALA A 175 9051 13901 10087 -383 598 2785 N ATOM 1149 CA ALA A 175 -22.914 8.355 18.682 1.00 86.28 C ANISOU 1149 CA ALA A 175 8973 13898 9912 -311 528 2896 C ATOM 1150 C ALA A 175 -23.110 9.596 17.866 1.00 91.93 C ANISOU 1150 C ALA A 175 9635 14662 10632 -253 601 3241 C ATOM 1151 O ALA A 175 -22.606 10.650 18.208 1.00 92.23 O ANISOU 1151 O ALA A 175 9683 14453 10908 -244 668 3377 O ATOM 1152 CB ALA A 175 -23.438 8.562 20.037 1.00 85.30 C ANISOU 1152 CB ALA A 175 8915 13508 9986 -275 455 2799 C ATOM 1153 N ASN A 176 -23.846 9.475 16.776 1.00 89.52 N ANISOU 1153 N ASN A 176 9277 14678 10060 -222 586 3389 N ATOM 1154 CA ASN A 176 -24.086 10.629 15.900 1.00 91.64 C ANISOU 1154 CA ASN A 176 9488 15029 10303 -150 654 3759 C ATOM 1155 C ASN A 176 -25.409 10.507 15.148 1.00 97.16 C ANISOU 1155 C ASN A 176 10124 16058 10735 -84 566 3910 C ATOM 1156 O ASN A 176 -25.892 9.397 14.927 1.00 95.97 O ANISOU 1156 O ASN A 176 9967 16148 10348 -140 473 3718 O ATOM 1157 CB ASN A 176 -22.945 10.786 14.876 1.00 92.87 C ANISOU 1157 CB ASN A 176 9611 15304 10372 -210 786 3871 C ATOM 1158 CG ASN A 176 -21.601 11.132 15.461 1.00110.02 C ANISOU 1158 CG ASN A 176 11801 17180 12823 -279 882 3802 C ATOM 1159 OD1 ASN A 176 -21.388 12.220 16.006 1.00103.40 O ANISOU 1159 OD1 ASN A 176 10979 16047 12262 -262 927 3942 O ATOM 1160 ND2 ASN A 176 -20.661 10.208 15.359 1.00100.23 N ANISOU 1160 ND2 ASN A 176 10553 16010 11519 -362 918 3583 N ATOM 1161 N VAL A 177 -25.973 11.650 14.722 1.00 96.43 N ANISOU 1161 N VAL A 177 9979 15980 10681 30 597 4265 N ATOM 1162 CA VAL A 177 -27.209 11.698 13.938 1.00 98.31 C ANISOU 1162 CA VAL A 177 10123 16557 10674 108 508 4478 C ATOM 1163 C VAL A 177 -26.817 11.534 12.466 1.00106.58 C ANISOU 1163 C VAL A 177 11131 17970 11396 55 547 4623 C ATOM 1164 O VAL A 177 -25.865 12.174 12.011 1.00106.95 O ANISOU 1164 O VAL A 177 11195 17934 11507 47 685 4782 O ATOM 1165 CB VAL A 177 -28.011 13.006 14.177 1.00103.23 C ANISOU 1165 CB VAL A 177 10702 17023 11498 285 532 4818 C ATOM 1166 CG1 VAL A 177 -29.403 12.926 13.555 1.00104.62 C ANISOU 1166 CG1 VAL A 177 10749 17563 11439 375 409 5015 C ATOM 1167 CG2 VAL A 177 -28.115 13.324 15.663 1.00101.04 C ANISOU 1167 CG2 VAL A 177 10502 16319 11569 332 548 4665 C ATOM 1168 N SER A 178 -27.536 10.665 11.735 1.00106.31 N ANISOU 1168 N SER A 178 11048 18339 11004 4 428 4558 N ATOM 1169 CA SER A 178 -27.286 10.401 10.316 1.00109.67 C ANISOU 1169 CA SER A 178 11452 19160 11057 -56 450 4663 C ATOM 1170 C SER A 178 -28.586 10.271 9.522 1.00117.53 C ANISOU 1170 C SER A 178 12343 20585 11728 -31 293 4834 C ATOM 1171 O SER A 178 -29.562 9.737 10.040 1.00115.86 O ANISOU 1171 O SER A 178 12087 20430 11505 -42 148 4696 O ATOM 1172 CB SER A 178 -26.438 9.144 10.142 1.00112.50 C ANISOU 1172 CB SER A 178 11899 19594 11252 -211 486 4288 C ATOM 1173 OG SER A 178 -27.236 7.975 10.045 1.00121.76 O ANISOU 1173 OG SER A 178 13077 21017 12171 -302 339 4037 O ATOM 1174 N GLU A 179 -28.633 10.801 8.325 1.00119.09 N ANISOU 1174 N GLU A 179 12489 21082 11679 6 317 5152 N ATOM 1175 CA GLU A 179 -29.879 10.741 7.583 1.00122.31 C ANISOU 1175 CA GLU A 179 12775 21920 11776 32 146 5345 C ATOM 1176 C GLU A 179 -30.066 9.347 7.059 1.00127.91 C ANISOU 1176 C GLU A 179 13520 22979 12102 -158 32 5010 C ATOM 1177 O GLU A 179 -29.110 8.608 6.882 1.00126.37 O ANISOU 1177 O GLU A 179 13448 22754 11815 -280 128 4729 O ATOM 1178 CB GLU A 179 -29.945 11.755 6.435 1.00127.54 C ANISOU 1178 CB GLU A 179 13368 22829 12262 138 190 5824 C ATOM 1179 CG GLU A 179 -30.796 13.009 6.767 1.00141.64 C ANISOU 1179 CG GLU A 179 15035 24482 14300 360 171 6242 C ATOM 1180 CD GLU A 179 -30.647 14.179 5.777 1.00170.74 C ANISOU 1180 CD GLU A 179 18678 28289 17907 492 266 6754 C ATOM 1181 OE1 GLU A 179 -29.540 14.386 5.242 1.00167.63 O ANISOU 1181 OE1 GLU A 179 18375 27849 17466 437 429 6798 O ATOM 1182 OE2 GLU A 179 -31.639 14.909 5.548 1.00166.58 O ANISOU 1182 OE2 GLU A 179 18016 27898 17377 661 187 7131 O ATOM 1183 N ALA A 180 -31.322 9.003 6.825 1.00127.13 N ANISOU 1183 N ALA A 180 13306 23204 11791 -182 -169 5046 N ATOM 1184 CA ALA A 180 -31.672 7.726 6.248 1.00128.15 C ANISOU 1184 CA ALA A 180 13464 23698 11529 -383 -300 4749 C ATOM 1185 C ALA A 180 -32.925 7.873 5.408 1.00136.51 C ANISOU 1185 C ALA A 180 14353 25252 12260 -384 -507 5011 C ATOM 1186 O ALA A 180 -33.380 8.971 5.122 1.00138.01 O ANISOU 1186 O ALA A 180 14412 25528 12497 -210 -524 5451 O ATOM 1187 CB ALA A 180 -31.889 6.708 7.328 1.00125.72 C ANISOU 1187 CB ALA A 180 13209 23168 11391 -487 -357 4332 C ATOM 1188 N ASP A 181 -33.485 6.745 5.020 1.00134.64 N ANISOU 1188 N ASP A 181 14120 25343 11695 -584 -666 4739 N ATOM 1189 CA ASP A 181 -34.690 6.735 4.229 1.00138.00 C ANISOU 1189 CA ASP A 181 14372 26283 11779 -629 -895 4943 C ATOM 1190 C ASP A 181 -35.885 7.273 4.996 1.00141.15 C ANISOU 1190 C ASP A 181 14553 26635 12444 -489 -1025 5167 C ATOM 1191 O ASP A 181 -36.640 6.511 5.586 1.00140.36 O ANISOU 1191 O ASP A 181 14391 26554 12385 -602 -1156 4930 O ATOM 1192 CB ASP A 181 -34.965 5.305 3.823 1.00140.71 C ANISOU 1192 CB ASP A 181 14791 26913 11760 -913 -1027 4523 C ATOM 1193 CG ASP A 181 -33.861 4.388 4.236 1.00148.96 C ANISOU 1193 CG ASP A 181 16076 27630 12892 -1030 -856 4065 C ATOM 1194 OD1 ASP A 181 -32.695 4.706 3.926 1.00149.14 O ANISOU 1194 OD1 ASP A 181 16227 27506 12933 -967 -652 4094 O ATOM 1195 OD2 ASP A 181 -34.154 3.369 4.890 1.00153.05 O ANISOU 1195 OD2 ASP A 181 16644 28029 13477 -1176 -917 3695 O ATOM 1196 N ASP A 182 -36.073 8.581 4.981 1.00137.26 N ANISOU 1196 N ASP A 182 13940 26075 12136 -241 -976 5632 N ATOM 1197 CA ASP A 182 -37.284 9.132 5.553 1.00136.67 C ANISOU 1197 CA ASP A 182 13638 26015 12274 -84 -1091 5888 C ATOM 1198 C ASP A 182 -37.194 9.627 6.980 1.00134.60 C ANISOU 1198 C ASP A 182 13401 25192 12548 81 -952 5852 C ATOM 1199 O ASP A 182 -38.216 9.922 7.580 1.00134.50 O ANISOU 1199 O ASP A 182 13212 25167 12723 200 -1030 5994 O ATOM 1200 CB ASP A 182 -38.321 8.062 5.798 1.00138.52 C ANISOU 1200 CB ASP A 182 13758 26501 12373 -271 -1307 5625 C ATOM 1201 N ARG A 183 -35.991 9.694 7.540 1.00125.83 N ANISOU 1201 N ARG A 183 12501 23632 11676 84 -748 5655 N ATOM 1202 CA ARG A 183 -35.868 10.084 8.939 1.00121.53 C ANISOU 1202 CA ARG A 183 12005 22562 11611 209 -628 5572 C ATOM 1203 C ARG A 183 -34.400 10.210 9.314 1.00121.53 C ANISOU 1203 C ARG A 183 12226 22141 11808 188 -419 5393 C ATOM 1204 O ARG A 183 -33.527 9.723 8.604 1.00120.71 O ANISOU 1204 O ARG A 183 12237 22154 11475 52 -373 5251 O ATOM 1205 CB ARG A 183 -36.653 9.432 10.067 1.00118.34 C ANISOU 1205 CB ARG A 183 11547 22028 11387 168 -709 5315 C ATOM 1206 CG ARG A 183 -36.347 7.973 10.307 1.00122.06 C ANISOU 1206 CG ARG A 183 12144 22513 11721 -91 -760 4818 C ATOM 1207 N TYR A 184 -34.134 10.850 10.445 1.00115.38 N ANISOU 1207 N TYR A 184 11505 20882 11452 318 -293 5393 N ATOM 1208 CA TYR A 184 -32.743 11.005 10.851 1.00112.54 C ANISOU 1208 CA TYR A 184 11332 20133 11296 286 -113 5232 C ATOM 1209 C TYR A 184 -32.582 9.786 11.753 1.00111.07 C ANISOU 1209 C TYR A 184 11238 19802 11162 131 -153 4756 C ATOM 1210 O TYR A 184 -33.557 9.278 12.307 1.00109.79 O ANISOU 1210 O TYR A 184 11002 19702 11013 115 -270 4641 O ATOM 1211 CB TYR A 184 -32.394 12.279 11.622 1.00113.50 C ANISOU 1211 CB TYR A 184 11499 19791 11836 467 45 5434 C ATOM 1212 CG TYR A 184 -32.095 13.468 10.737 1.00118.82 C ANISOU 1212 CG TYR A 184 12145 20502 12500 593 148 5871 C ATOM 1213 CD1 TYR A 184 -30.807 13.710 10.278 1.00121.29 C ANISOU 1213 CD1 TYR A 184 12569 20705 12810 524 292 5882 C ATOM 1214 CD2 TYR A 184 -33.101 14.348 10.360 1.00122.55 C ANISOU 1214 CD2 TYR A 184 12471 21120 12975 787 109 6292 C ATOM 1215 CE1 TYR A 184 -30.529 14.795 9.468 1.00125.27 C ANISOU 1215 CE1 TYR A 184 13052 21233 13310 630 400 6297 C ATOM 1216 CE2 TYR A 184 -32.832 15.436 9.551 1.00126.46 C ANISOU 1216 CE2 TYR A 184 12949 21634 13466 912 212 6717 C ATOM 1217 CZ TYR A 184 -31.545 15.654 9.108 1.00134.67 C ANISOU 1217 CZ TYR A 184 14115 22554 14499 825 359 6716 C ATOM 1218 OH TYR A 184 -31.273 16.736 8.302 1.00139.91 O ANISOU 1218 OH TYR A 184 14767 23230 15164 939 475 7153 O ATOM 1219 N ILE A 185 -31.345 9.320 11.896 1.00104.30 N ANISOU 1219 N ILE A 185 10535 18754 10341 23 -49 4496 N ATOM 1220 CA ILE A 185 -31.055 8.159 12.728 1.00100.57 C ANISOU 1220 CA ILE A 185 10163 18123 9924 -110 -70 4062 C ATOM 1221 C ILE A 185 -29.887 8.430 13.670 1.00101.81 C ANISOU 1221 C ILE A 185 10450 17823 10412 -90 72 3923 C ATOM 1222 O ILE A 185 -28.758 8.645 13.228 1.00102.28 O ANISOU 1222 O ILE A 185 10570 17820 10471 -117 190 3943 O ATOM 1223 CB ILE A 185 -30.737 6.918 11.874 1.00104.01 C ANISOU 1223 CB ILE A 185 10657 18862 10002 -299 -113 3806 C ATOM 1224 CG1 ILE A 185 -32.027 6.287 11.347 1.00106.20 C ANISOU 1224 CG1 ILE A 185 10823 19546 9981 -383 -300 3798 C ATOM 1225 CG2 ILE A 185 -29.936 5.907 12.681 1.00101.75 C ANISOU 1225 CG2 ILE A 185 10513 18310 9836 -404 -59 3397 C ATOM 1226 CD1 ILE A 185 -31.823 5.392 10.145 1.00117.35 C ANISOU 1226 CD1 ILE A 185 12284 21335 10969 -556 -341 3652 C ATOM 1227 N CYS A 186 -30.165 8.418 14.969 1.00 95.25 N ANISOU 1227 N CYS A 186 9651 16688 9851 -49 60 3786 N ATOM 1228 CA CYS A 186 -29.136 8.658 15.977 1.00 92.42 C ANISOU 1228 CA CYS A 186 9410 15907 9797 -43 166 3640 C ATOM 1229 C CYS A 186 -28.749 7.337 16.614 1.00 93.06 C ANISOU 1229 C CYS A 186 9583 15917 9859 -171 130 3243 C ATOM 1230 O CYS A 186 -29.598 6.685 17.228 1.00 91.91 O ANISOU 1230 O CYS A 186 9429 15789 9703 -194 39 3092 O ATOM 1231 CB CYS A 186 -29.600 9.678 17.019 1.00 92.02 C ANISOU 1231 CB CYS A 186 9361 15537 10064 100 198 3773 C ATOM 1232 SG CYS A 186 -28.788 9.525 18.640 1.00 92.90 S ANISOU 1232 SG CYS A 186 9623 15176 10496 66 247 3469 S ATOM 1233 N ASP A 187 -27.472 6.940 16.442 1.00 87.99 N ANISOU 1233 N ASP A 187 9018 15199 9215 -249 212 3091 N ATOM 1234 CA ASP A 187 -26.858 5.743 17.018 1.00 85.55 C ANISOU 1234 CA ASP A 187 8802 14785 8919 -347 209 2739 C ATOM 1235 C ASP A 187 -25.341 5.717 16.875 1.00 88.10 C ANISOU 1235 C ASP A 187 9171 14982 9320 -381 329 2670 C ATOM 1236 O ASP A 187 -24.770 6.570 16.195 1.00 88.99 O ANISOU 1236 O ASP A 187 9243 15125 9444 -352 419 2890 O ATOM 1237 CB ASP A 187 -27.547 4.420 16.601 1.00 87.80 C ANISOU 1237 CB ASP A 187 9097 15337 8926 -454 118 2529 C ATOM 1238 CG ASP A 187 -26.985 3.687 15.408 1.00102.68 C ANISOU 1238 CG ASP A 187 11010 17479 10523 -549 164 2435 C ATOM 1239 OD1 ASP A 187 -27.389 4.009 14.270 1.00106.70 O ANISOU 1239 OD1 ASP A 187 11455 18298 10788 -556 146 2623 O ATOM 1240 OD2 ASP A 187 -26.221 2.721 15.617 1.00108.04 O ANISOU 1240 OD2 ASP A 187 11781 18065 11203 -613 215 2167 O ATOM 1241 N ARG A 188 -24.689 4.764 17.559 1.00 82.58 N ANISOU 1241 N ARG A 188 8547 14134 8694 -436 336 2383 N ATOM 1242 CA ARG A 188 -23.238 4.600 17.564 1.00 81.54 C ANISOU 1242 CA ARG A 188 8436 13883 8662 -461 443 2296 C ATOM 1243 C ARG A 188 -22.781 3.911 16.291 1.00 86.01 C ANISOU 1243 C ARG A 188 9001 14726 8954 -514 523 2245 C ATOM 1244 O ARG A 188 -23.146 2.757 16.047 1.00 85.25 O ANISOU 1244 O ARG A 188 8961 14768 8660 -571 490 2033 O ATOM 1245 CB ARG A 188 -22.780 3.833 18.817 1.00 79.24 C ANISOU 1245 CB ARG A 188 8215 13341 8552 -477 411 2032 C ATOM 1246 CG ARG A 188 -23.161 4.523 20.126 1.00 89.71 C ANISOU 1246 CG ARG A 188 9565 14392 10131 -431 342 2063 C ATOM 1247 CD ARG A 188 -22.928 3.644 21.341 1.00101.84 C ANISOU 1247 CD ARG A 188 11179 15733 11782 -449 289 1808 C ATOM 1248 NE ARG A 188 -23.813 2.476 21.360 1.00112.53 N ANISOU 1248 NE ARG A 188 12583 17209 12965 -482 226 1636 N ATOM 1249 CZ ARG A 188 -23.714 1.468 22.222 1.00127.28 C ANISOU 1249 CZ ARG A 188 14530 18952 14880 -502 190 1414 C ATOM 1250 NH1 ARG A 188 -24.562 0.451 22.160 1.00115.42 N ANISOU 1250 NH1 ARG A 188 13074 17556 13226 -550 145 1273 N ATOM 1251 NH2 ARG A 188 -22.764 1.467 23.148 1.00114.86 N ANISOU 1251 NH2 ARG A 188 12986 17153 13504 -482 196 1339 N ATOM 1252 N PHE A 189 -22.017 4.639 15.459 1.00 83.99 N ANISOU 1252 N PHE A 189 8689 14547 8678 -500 641 2443 N ATOM 1253 CA PHE A 189 -21.482 4.127 14.203 1.00 85.50 C ANISOU 1253 CA PHE A 189 8882 15004 8602 -539 751 2421 C ATOM 1254 C PHE A 189 -20.021 3.766 14.390 1.00 89.44 C ANISOU 1254 C PHE A 189 9375 15362 9246 -543 885 2297 C ATOM 1255 O PHE A 189 -19.163 4.646 14.474 1.00 88.88 O ANISOU 1255 O PHE A 189 9231 15166 9374 -525 970 2465 O ATOM 1256 CB PHE A 189 -21.686 5.127 13.051 1.00 89.60 C ANISOU 1256 CB PHE A 189 9335 15750 8957 -517 802 2749 C ATOM 1257 CG PHE A 189 -23.129 5.479 12.782 1.00 91.48 C ANISOU 1257 CG PHE A 189 9550 16169 9040 -496 665 2904 C ATOM 1258 CD1 PHE A 189 -23.988 4.560 12.189 1.00 95.45 C ANISOU 1258 CD1 PHE A 189 10084 16963 9218 -561 574 2769 C ATOM 1259 CD2 PHE A 189 -23.628 6.733 13.108 1.00 93.51 C ANISOU 1259 CD2 PHE A 189 9747 16305 9479 -413 630 3190 C ATOM 1260 CE1 PHE A 189 -25.327 4.883 11.947 1.00 97.36 C ANISOU 1260 CE1 PHE A 189 10269 17401 9322 -546 433 2928 C ATOM 1261 CE2 PHE A 189 -24.967 7.056 12.863 1.00 97.46 C ANISOU 1261 CE2 PHE A 189 10198 16984 9849 -370 509 3356 C ATOM 1262 CZ PHE A 189 -25.809 6.126 12.292 1.00 96.39 C ANISOU 1262 CZ PHE A 189 10066 17166 9394 -438 402 3231 C ATOM 1263 N TYR A 190 -19.760 2.457 14.509 1.00 86.77 N ANISOU 1263 N TYR A 190 9108 15032 8829 -568 904 2003 N ATOM 1264 CA TYR A 190 -18.434 1.881 14.727 1.00 87.11 C ANISOU 1264 CA TYR A 190 9138 14955 9003 -550 1030 1858 C ATOM 1265 C TYR A 190 -17.680 1.591 13.410 1.00 94.29 C ANISOU 1265 C TYR A 190 10036 16103 9688 -554 1220 1871 C ATOM 1266 O TYR A 190 -18.325 1.330 12.393 1.00 95.37 O ANISOU 1266 O TYR A 190 10231 16510 9497 -590 1229 1870 O ATOM 1267 CB TYR A 190 -18.550 0.604 15.572 1.00 86.86 C ANISOU 1267 CB TYR A 190 9200 14783 9020 -551 970 1551 C ATOM 1268 CG TYR A 190 -19.104 0.820 16.963 1.00 87.07 C ANISOU 1268 CG TYR A 190 9243 14563 9278 -542 810 1525 C ATOM 1269 CD1 TYR A 190 -20.314 0.251 17.348 1.00 88.35 C ANISOU 1269 CD1 TYR A 190 9490 14735 9344 -573 683 1403 C ATOM 1270 CD2 TYR A 190 -18.409 1.576 17.905 1.00 87.13 C ANISOU 1270 CD2 TYR A 190 9181 14334 9591 -513 791 1614 C ATOM 1271 CE1 TYR A 190 -20.829 0.441 18.629 1.00 87.48 C ANISOU 1271 CE1 TYR A 190 9399 14408 9431 -558 558 1382 C ATOM 1272 CE2 TYR A 190 -18.922 1.786 19.184 1.00 86.33 C ANISOU 1272 CE2 TYR A 190 9114 14015 9672 -506 653 1579 C ATOM 1273 CZ TYR A 190 -20.129 1.207 19.545 1.00 93.91 C ANISOU 1273 CZ TYR A 190 10164 14991 10528 -519 547 1465 C ATOM 1274 OH TYR A 190 -20.634 1.389 20.809 1.00 94.80 O ANISOU 1274 OH TYR A 190 10316 14899 10807 -505 433 1430 O ATOM 1275 N PRO A 191 -16.321 1.611 13.419 1.00 92.01 N ANISOU 1275 N PRO A 191 9666 15733 9560 -519 1373 1879 N ATOM 1276 CA PRO A 191 -15.556 1.358 12.179 1.00 94.74 C ANISOU 1276 CA PRO A 191 9995 16305 9699 -509 1586 1899 C ATOM 1277 C PRO A 191 -15.926 0.099 11.386 1.00100.47 C ANISOU 1277 C PRO A 191 10864 17232 10080 -525 1647 1649 C ATOM 1278 O PRO A 191 -15.987 0.164 10.156 1.00102.39 O ANISOU 1278 O PRO A 191 11137 17751 10017 -548 1754 1716 O ATOM 1279 CB PRO A 191 -14.107 1.324 12.663 1.00 96.45 C ANISOU 1279 CB PRO A 191 10090 16353 10205 -460 1713 1886 C ATOM 1280 CG PRO A 191 -14.107 2.167 13.874 1.00 98.70 C ANISOU 1280 CG PRO A 191 10300 16376 10826 -475 1564 1995 C ATOM 1281 CD PRO A 191 -15.414 1.924 14.542 1.00 92.21 C ANISOU 1281 CD PRO A 191 9597 15479 9959 -493 1360 1889 C ATOM 1282 N ASN A 192 -16.171 -1.034 12.083 1.00 95.78 N ANISOU 1282 N ASN A 192 10370 16494 9527 -520 1583 1362 N ATOM 1283 CA ASN A 192 -16.570 -2.311 11.476 1.00 96.80 C ANISOU 1283 CA ASN A 192 10664 16752 9362 -555 1633 1083 C ATOM 1284 C ASN A 192 -17.311 -3.224 12.466 1.00 98.33 C ANISOU 1284 C ASN A 192 10967 16755 9640 -582 1481 845 C ATOM 1285 O ASN A 192 -17.609 -2.793 13.584 1.00 95.51 O ANISOU 1285 O ASN A 192 10555 16197 9536 -570 1328 916 O ATOM 1286 CB ASN A 192 -15.389 -3.018 10.788 1.00100.59 C ANISOU 1286 CB ASN A 192 11162 17285 9771 -489 1896 956 C ATOM 1287 CG ASN A 192 -14.292 -3.424 11.720 1.00126.38 C ANISOU 1287 CG ASN A 192 14351 20283 13384 -382 1972 878 C ATOM 1288 OD1 ASN A 192 -14.335 -4.494 12.329 1.00122.35 O ANISOU 1288 OD1 ASN A 192 13938 19603 12945 -351 1957 637 O ATOM 1289 ND2 ASN A 192 -13.276 -2.585 11.838 1.00119.55 N ANISOU 1289 ND2 ASN A 192 13302 19379 12740 -329 2056 1093 N ATOM 1290 N ASP A 193 -17.637 -4.468 12.037 1.00 96.04 N ANISOU 1290 N ASP A 193 10842 16523 9126 -629 1530 563 N ATOM 1291 CA ASP A 193 -18.370 -5.476 12.815 1.00 94.51 C ANISOU 1291 CA ASP A 193 10775 16162 8973 -676 1415 322 C ATOM 1292 C ASP A 193 -17.729 -5.806 14.172 1.00 95.16 C ANISOU 1292 C ASP A 193 10824 15906 9428 -575 1402 267 C ATOM 1293 O ASP A 193 -18.448 -5.908 15.171 1.00 91.87 O ANISOU 1293 O ASP A 193 10430 15334 9144 -605 1236 237 O ATOM 1294 CB ASP A 193 -18.583 -6.761 11.991 1.00 98.88 C ANISOU 1294 CB ASP A 193 11524 16816 9229 -748 1522 20 C ATOM 1295 CG ASP A 193 -19.372 -6.564 10.709 1.00113.45 C ANISOU 1295 CG ASP A 193 13424 19021 10661 -879 1493 40 C ATOM 1296 OD1 ASP A 193 -18.746 -6.539 9.623 1.00117.78 O ANISOU 1296 OD1 ASP A 193 13996 19762 10993 -860 1674 43 O ATOM 1297 OD2 ASP A 193 -20.620 -6.472 10.785 1.00117.32 O ANISOU 1297 OD2 ASP A 193 13929 19615 11031 -1001 1292 52 O ATOM 1298 N LEU A 194 -16.379 -5.954 14.202 1.00 92.22 N ANISOU 1298 N LEU A 194 10383 15438 9217 -454 1579 268 N ATOM 1299 CA LEU A 194 -15.586 -6.277 15.397 1.00 90.28 C ANISOU 1299 CA LEU A 194 10079 14910 9311 -344 1577 238 C ATOM 1300 C LEU A 194 -15.864 -5.377 16.597 1.00 90.38 C ANISOU 1300 C LEU A 194 9988 14775 9576 -352 1373 408 C ATOM 1301 O LEU A 194 -15.942 -5.879 17.716 1.00 88.66 O ANISOU 1301 O LEU A 194 9808 14341 9540 -320 1281 320 O ATOM 1302 CB LEU A 194 -14.084 -6.288 15.079 1.00 91.92 C ANISOU 1302 CB LEU A 194 10167 15116 9644 -217 1792 288 C ATOM 1303 CG LEU A 194 -13.484 -7.647 14.750 1.00 98.57 C ANISOU 1303 CG LEU A 194 11122 15892 10439 -124 2000 45 C ATOM 1304 CD1 LEU A 194 -13.580 -7.949 13.254 1.00101.51 C ANISOU 1304 CD1 LEU A 194 11606 16511 10454 -167 2186 -56 C ATOM 1305 CD2 LEU A 194 -12.039 -7.721 15.207 1.00101.19 C ANISOU 1305 CD2 LEU A 194 11285 16101 11061 40 2130 115 C ATOM 1306 N TRP A 195 -16.025 -4.058 16.361 1.00 85.34 N ANISOU 1306 N TRP A 195 9235 14247 8942 -392 1311 651 N ATOM 1307 CA TRP A 195 -16.315 -3.055 17.391 1.00 82.56 C ANISOU 1307 CA TRP A 195 8801 13757 8810 -406 1138 816 C ATOM 1308 C TRP A 195 -17.691 -3.274 18.016 1.00 83.66 C ANISOU 1308 C TRP A 195 9049 13841 8897 -469 960 740 C ATOM 1309 O TRP A 195 -17.863 -3.031 19.208 1.00 81.27 O ANISOU 1309 O TRP A 195 8735 13344 8799 -455 836 760 O ATOM 1310 CB TRP A 195 -16.223 -1.644 16.813 1.00 82.13 C ANISOU 1310 CB TRP A 195 8627 13829 8750 -435 1149 1089 C ATOM 1311 CG TRP A 195 -14.847 -1.227 16.402 1.00 84.78 C ANISOU 1311 CG TRP A 195 8821 14191 9199 -389 1311 1207 C ATOM 1312 CD1 TRP A 195 -14.157 -1.644 15.302 1.00 89.93 C ANISOU 1312 CD1 TRP A 195 9459 15016 9693 -358 1516 1179 C ATOM 1313 CD2 TRP A 195 -14.017 -0.257 17.054 1.00 84.28 C ANISOU 1313 CD2 TRP A 195 8606 13990 9428 -383 1289 1380 C ATOM 1314 NE1 TRP A 195 -12.930 -1.027 15.250 1.00 90.59 N ANISOU 1314 NE1 TRP A 195 9371 15081 9968 -323 1629 1334 N ATOM 1315 CE2 TRP A 195 -12.820 -0.162 16.308 1.00 90.45 C ANISOU 1315 CE2 TRP A 195 9263 14875 10230 -350 1484 1460 C ATOM 1316 CE3 TRP A 195 -14.163 0.536 18.206 1.00 83.87 C ANISOU 1316 CE3 TRP A 195 8515 13735 9616 -411 1128 1465 C ATOM 1317 CZ2 TRP A 195 -11.774 0.695 16.674 1.00 90.13 C ANISOU 1317 CZ2 TRP A 195 9041 14748 10456 -362 1510 1629 C ATOM 1318 CZ3 TRP A 195 -13.128 1.385 18.567 1.00 85.83 C ANISOU 1318 CZ3 TRP A 195 8609 13889 10113 -428 1148 1613 C ATOM 1319 CH2 TRP A 195 -11.949 1.457 17.808 1.00 88.55 C ANISOU 1319 CH2 TRP A 195 8812 14345 10487 -411 1331 1698 C ATOM 1320 N VAL A 196 -18.662 -3.741 17.213 1.00 80.54 N ANISOU 1320 N VAL A 196 8754 13628 8220 -546 951 652 N ATOM 1321 CA VAL A 196 -20.022 -4.043 17.675 1.00 78.69 C ANISOU 1321 CA VAL A 196 8603 13381 7915 -622 794 577 C ATOM 1322 C VAL A 196 -19.975 -5.326 18.527 1.00 80.43 C ANISOU 1322 C VAL A 196 8941 13389 8231 -608 791 336 C ATOM 1323 O VAL A 196 -20.607 -5.378 19.576 1.00 77.78 O ANISOU 1323 O VAL A 196 8631 12904 8017 -620 666 321 O ATOM 1324 CB VAL A 196 -21.040 -4.142 16.501 1.00 83.79 C ANISOU 1324 CB VAL A 196 9295 14320 8221 -729 771 567 C ATOM 1325 CG1 VAL A 196 -22.477 -4.099 17.010 1.00 82.25 C ANISOU 1325 CG1 VAL A 196 9116 14141 7993 -806 592 573 C ATOM 1326 CG2 VAL A 196 -20.808 -3.035 15.473 1.00 85.10 C ANISOU 1326 CG2 VAL A 196 9356 14711 8266 -718 823 809 C ATOM 1327 N VAL A 197 -19.180 -6.324 18.092 1.00 78.07 N ANISOU 1327 N VAL A 197 8712 13064 7886 -570 947 164 N ATOM 1328 CA VAL A 197 -18.973 -7.600 18.781 1.00 77.55 C ANISOU 1328 CA VAL A 197 8766 12780 7919 -533 985 -52 C ATOM 1329 C VAL A 197 -18.265 -7.373 20.119 1.00 79.52 C ANISOU 1329 C VAL A 197 8937 12790 8485 -424 929 29 C ATOM 1330 O VAL A 197 -18.761 -7.848 21.141 1.00 78.16 O ANISOU 1330 O VAL A 197 8838 12447 8413 -430 831 -40 O ATOM 1331 CB VAL A 197 -18.203 -8.614 17.891 1.00 83.96 C ANISOU 1331 CB VAL A 197 9668 13619 8613 -490 1199 -235 C ATOM 1332 CG1 VAL A 197 -17.828 -9.878 18.665 1.00 83.79 C ANISOU 1332 CG1 VAL A 197 9761 13331 8746 -414 1260 -422 C ATOM 1333 CG2 VAL A 197 -18.999 -8.967 16.640 1.00 85.63 C ANISOU 1333 CG2 VAL A 197 9994 14066 8475 -627 1236 -359 C ATOM 1334 N VAL A 198 -17.119 -6.651 20.113 1.00 76.19 N ANISOU 1334 N VAL A 198 8366 12370 8213 -336 987 177 N ATOM 1335 CA VAL A 198 -16.343 -6.376 21.331 1.00 74.98 C ANISOU 1335 CA VAL A 198 8119 12023 8346 -251 920 257 C ATOM 1336 C VAL A 198 -17.112 -5.620 22.413 1.00 77.55 C ANISOU 1336 C VAL A 198 8440 12254 8774 -300 724 351 C ATOM 1337 O VAL A 198 -17.057 -6.037 23.566 1.00 76.07 O ANISOU 1337 O VAL A 198 8290 11883 8729 -261 644 302 O ATOM 1338 CB VAL A 198 -14.890 -5.855 21.135 1.00 79.75 C ANISOU 1338 CB VAL A 198 8546 12652 9105 -166 1022 385 C ATOM 1339 CG1 VAL A 198 -14.045 -6.823 20.312 1.00 81.53 C ANISOU 1339 CG1 VAL A 198 8784 12924 9270 -76 1240 268 C ATOM 1340 CG2 VAL A 198 -14.859 -4.450 20.544 1.00 79.88 C ANISOU 1340 CG2 VAL A 198 8439 12817 9096 -229 1011 593 C ATOM 1341 N PHE A 199 -17.853 -4.546 22.045 1.00 74.48 N ANISOU 1341 N PHE A 199 8012 11986 8302 -376 657 487 N ATOM 1342 CA PHE A 199 -18.641 -3.772 23.006 1.00 73.30 C ANISOU 1342 CA PHE A 199 7865 11744 8243 -409 499 575 C ATOM 1343 C PHE A 199 -19.879 -4.527 23.496 1.00 77.61 C ANISOU 1343 C PHE A 199 8543 12244 8700 -456 419 448 C ATOM 1344 O PHE A 199 -20.379 -4.221 24.584 1.00 76.16 O ANISOU 1344 O PHE A 199 8383 11931 8622 -456 309 475 O ATOM 1345 CB PHE A 199 -18.968 -2.355 22.505 1.00 75.64 C ANISOU 1345 CB PHE A 199 8072 12152 8516 -447 474 782 C ATOM 1346 CG PHE A 199 -17.794 -1.399 22.461 1.00 78.46 C ANISOU 1346 CG PHE A 199 8296 12477 9037 -420 519 935 C ATOM 1347 CD1 PHE A 199 -16.959 -1.241 23.562 1.00 81.61 C ANISOU 1347 CD1 PHE A 199 8649 12691 9668 -390 464 934 C ATOM 1348 CD2 PHE A 199 -17.552 -0.621 21.335 1.00 82.38 C ANISOU 1348 CD2 PHE A 199 8708 13138 9454 -440 610 1091 C ATOM 1349 CE1 PHE A 199 -15.870 -0.357 23.517 1.00 83.48 C ANISOU 1349 CE1 PHE A 199 8748 12906 10065 -396 497 1071 C ATOM 1350 CE2 PHE A 199 -16.471 0.270 21.296 1.00 86.06 C ANISOU 1350 CE2 PHE A 199 9045 13567 10088 -437 661 1240 C ATOM 1351 CZ PHE A 199 -15.640 0.398 22.387 1.00 83.66 C ANISOU 1351 CZ PHE A 199 8687 13076 10025 -424 601 1223 C ATOM 1352 N GLN A 200 -20.356 -5.530 22.710 1.00 75.46 N ANISOU 1352 N GLN A 200 8362 12076 8235 -506 484 300 N ATOM 1353 CA GLN A 200 -21.464 -6.403 23.106 1.00 74.91 C ANISOU 1353 CA GLN A 200 8415 11961 8087 -576 424 162 C ATOM 1354 C GLN A 200 -20.889 -7.451 24.050 1.00 80.02 C ANISOU 1354 C GLN A 200 9149 12376 8878 -509 450 31 C ATOM 1355 O GLN A 200 -21.528 -7.764 25.056 1.00 78.47 O ANISOU 1355 O GLN A 200 9021 12049 8745 -526 367 -2 O ATOM 1356 CB GLN A 200 -22.158 -7.058 21.904 1.00 77.44 C ANISOU 1356 CB GLN A 200 8803 12476 8144 -684 475 44 C ATOM 1357 CG GLN A 200 -23.247 -6.171 21.293 1.00 86.90 C ANISOU 1357 CG GLN A 200 9927 13904 9187 -767 387 180 C ATOM 1358 CD GLN A 200 -23.965 -6.760 20.093 1.00105.02 C ANISOU 1358 CD GLN A 200 12275 16435 11193 -896 405 72 C ATOM 1359 OE1 GLN A 200 -25.164 -6.530 19.890 1.00 98.04 O ANISOU 1359 OE1 GLN A 200 11358 15708 10184 -992 300 121 O ATOM 1360 NE2 GLN A 200 -23.254 -7.487 19.234 1.00100.02 N ANISOU 1360 NE2 GLN A 200 11717 15851 10436 -904 539 -72 N ATOM 1361 N PHE A 201 -19.647 -7.932 23.767 1.00 78.73 N ANISOU 1361 N PHE A 201 8971 12165 8777 -418 571 -17 N ATOM 1362 CA PHE A 201 -18.917 -8.875 24.626 1.00 79.05 C ANISOU 1362 CA PHE A 201 9069 11991 8977 -318 605 -100 C ATOM 1363 C PHE A 201 -18.383 -8.189 25.896 1.00 82.97 C ANISOU 1363 C PHE A 201 9477 12362 9687 -247 489 33 C ATOM 1364 O PHE A 201 -18.137 -8.865 26.897 1.00 83.08 O ANISOU 1364 O PHE A 201 9548 12203 9816 -181 457 -6 O ATOM 1365 CB PHE A 201 -17.801 -9.623 23.866 1.00 82.66 C ANISOU 1365 CB PHE A 201 9524 12449 9434 -225 787 -186 C ATOM 1366 CG PHE A 201 -18.251 -10.806 23.031 1.00 85.96 C ANISOU 1366 CG PHE A 201 10108 12878 9675 -280 913 -397 C ATOM 1367 CD1 PHE A 201 -19.487 -11.414 23.255 1.00 88.77 C ANISOU 1367 CD1 PHE A 201 10610 13187 9931 -403 848 -514 C ATOM 1368 CD2 PHE A 201 -17.426 -11.335 22.044 1.00 90.25 C ANISOU 1368 CD2 PHE A 201 10668 13470 10155 -215 1107 -487 C ATOM 1369 CE1 PHE A 201 -19.895 -12.512 22.490 1.00 91.29 C ANISOU 1369 CE1 PHE A 201 11094 13504 10089 -484 960 -728 C ATOM 1370 CE2 PHE A 201 -17.838 -12.434 21.279 1.00 94.71 C ANISOU 1370 CE2 PHE A 201 11415 14026 10545 -278 1232 -710 C ATOM 1371 CZ PHE A 201 -19.072 -13.007 21.503 1.00 92.49 C ANISOU 1371 CZ PHE A 201 11283 13694 10166 -424 1149 -834 C ATOM 1372 N GLN A 202 -18.231 -6.853 25.858 1.00 78.86 N ANISOU 1372 N GLN A 202 8829 11925 9209 -267 425 192 N ATOM 1373 CA GLN A 202 -17.813 -6.041 26.995 1.00 77.90 C ANISOU 1373 CA GLN A 202 8636 11698 9263 -237 305 304 C ATOM 1374 C GLN A 202 -19.033 -5.878 27.909 1.00 81.13 C ANISOU 1374 C GLN A 202 9146 12032 9649 -292 185 296 C ATOM 1375 O GLN A 202 -18.905 -5.950 29.133 1.00 79.35 O ANISOU 1375 O GLN A 202 8957 11665 9530 -259 96 298 O ATOM 1376 CB GLN A 202 -17.332 -4.661 26.512 1.00 79.59 C ANISOU 1376 CB GLN A 202 8704 12012 9524 -264 302 463 C ATOM 1377 CG GLN A 202 -16.449 -3.912 27.503 1.00 97.26 C ANISOU 1377 CG GLN A 202 10847 14145 11964 -242 208 558 C ATOM 1378 CD GLN A 202 -16.498 -2.426 27.261 1.00116.81 C ANISOU 1378 CD GLN A 202 13239 16665 14480 -310 177 706 C ATOM 1379 OE1 GLN A 202 -17.424 -1.729 27.698 1.00111.92 O ANISOU 1379 OE1 GLN A 202 12681 16000 13842 -355 98 743 O ATOM 1380 NE2 GLN A 202 -15.503 -1.906 26.558 1.00108.39 N ANISOU 1380 NE2 GLN A 202 12029 15678 13477 -312 254 802 N ATOM 1381 N HIS A 203 -20.215 -5.675 27.295 1.00 79.20 N ANISOU 1381 N HIS A 203 8938 11900 9253 -374 186 292 N ATOM 1382 CA HIS A 203 -21.498 -5.488 27.969 1.00 78.77 C ANISOU 1382 CA HIS A 203 8953 11814 9163 -426 99 298 C ATOM 1383 C HIS A 203 -21.922 -6.730 28.754 1.00 82.47 C ANISOU 1383 C HIS A 203 9554 12152 9629 -428 90 168 C ATOM 1384 O HIS A 203 -22.376 -6.585 29.887 1.00 81.36 O ANISOU 1384 O HIS A 203 9463 11902 9547 -421 13 188 O ATOM 1385 CB HIS A 203 -22.569 -5.041 26.962 1.00 80.33 C ANISOU 1385 CB HIS A 203 9119 12204 9200 -506 108 344 C ATOM 1386 CG HIS A 203 -23.869 -4.600 27.562 1.00 83.51 C ANISOU 1386 CG HIS A 203 9541 12605 9585 -543 29 394 C ATOM 1387 ND1 HIS A 203 -24.995 -4.420 26.773 1.00 86.10 N ANISOU 1387 ND1 HIS A 203 9832 13118 9765 -613 21 433 N ATOM 1388 CD2 HIS A 203 -24.191 -4.316 28.848 1.00 84.72 C ANISOU 1388 CD2 HIS A 203 9739 12609 9843 -513 -36 415 C ATOM 1389 CE1 HIS A 203 -25.956 -4.049 27.601 1.00 85.10 C ANISOU 1389 CE1 HIS A 203 9713 12942 9678 -613 -38 483 C ATOM 1390 NE2 HIS A 203 -25.524 -3.993 28.862 1.00 84.57 N ANISOU 1390 NE2 HIS A 203 9709 12669 9755 -554 -65 465 N ATOM 1391 N ILE A 204 -21.742 -7.941 28.180 1.00 79.80 N ANISOU 1391 N ILE A 204 9285 11810 9226 -435 181 36 N ATOM 1392 CA ILE A 204 -22.054 -9.209 28.860 1.00 79.61 C ANISOU 1392 CA ILE A 204 9401 11631 9217 -437 197 -83 C ATOM 1393 C ILE A 204 -21.079 -9.393 30.043 1.00 83.03 C ANISOU 1393 C ILE A 204 9843 11887 9818 -316 160 -43 C ATOM 1394 O ILE A 204 -21.510 -9.734 31.139 1.00 81.58 O ANISOU 1394 O ILE A 204 9744 11578 9673 -310 103 -44 O ATOM 1395 CB ILE A 204 -22.014 -10.426 27.878 1.00 84.31 C ANISOU 1395 CB ILE A 204 10085 12240 9711 -475 325 -245 C ATOM 1396 CG1 ILE A 204 -22.895 -10.227 26.611 1.00 85.84 C ANISOU 1396 CG1 ILE A 204 10260 12652 9701 -611 344 -288 C ATOM 1397 CG2 ILE A 204 -22.283 -11.771 28.580 1.00 84.94 C ANISOU 1397 CG2 ILE A 204 10325 12118 9831 -477 360 -362 C ATOM 1398 CD1 ILE A 204 -24.421 -10.451 26.731 1.00 94.30 C ANISOU 1398 CD1 ILE A 204 11383 13779 10669 -758 278 -328 C ATOM 1399 N MET A 205 -19.777 -9.138 29.817 1.00 80.74 N ANISOU 1399 N MET A 205 9451 11606 9620 -223 189 6 N ATOM 1400 CA MET A 205 -18.736 -9.296 30.832 1.00 80.98 C ANISOU 1400 CA MET A 205 9452 11511 9805 -109 139 59 C ATOM 1401 C MET A 205 -18.870 -8.321 32.007 1.00 83.13 C ANISOU 1401 C MET A 205 9700 11747 10138 -123 -13 158 C ATOM 1402 O MET A 205 -19.118 -8.767 33.125 1.00 82.36 O ANISOU 1402 O MET A 205 9699 11532 10063 -98 -76 153 O ATOM 1403 CB MET A 205 -17.335 -9.246 30.198 1.00 84.80 C ANISOU 1403 CB MET A 205 9798 12046 10375 -17 215 95 C ATOM 1404 CG MET A 205 -16.295 -10.049 30.958 1.00 89.96 C ANISOU 1404 CG MET A 205 10438 12575 11169 124 216 112 C ATOM 1405 SD MET A 205 -16.565 -11.839 30.880 1.00 95.84 S ANISOU 1405 SD MET A 205 11369 13156 11889 192 355 -28 S ATOM 1406 CE MET A 205 -15.347 -12.404 32.085 1.00 93.69 C ANISOU 1406 CE MET A 205 11041 12750 11806 380 300 76 C ATOM 1407 N VAL A 206 -18.744 -7.004 31.746 1.00 78.72 N ANISOU 1407 N VAL A 206 9032 11281 9595 -167 -59 245 N ATOM 1408 CA VAL A 206 -18.815 -5.935 32.756 1.00 77.38 C ANISOU 1408 CA VAL A 206 8851 11066 9483 -192 -187 322 C ATOM 1409 C VAL A 206 -20.226 -5.757 33.371 1.00 79.28 C ANISOU 1409 C VAL A 206 9214 11269 9641 -247 -226 303 C ATOM 1410 O VAL A 206 -20.334 -5.492 34.571 1.00 78.51 O ANISOU 1410 O VAL A 206 9180 11080 9571 -238 -315 317 O ATOM 1411 CB VAL A 206 -18.202 -4.597 32.237 1.00 81.39 C ANISOU 1411 CB VAL A 206 9216 11652 10055 -228 -201 419 C ATOM 1412 CG1 VAL A 206 -18.141 -3.537 33.336 1.00 80.81 C ANISOU 1412 CG1 VAL A 206 9153 11498 10054 -263 -327 471 C ATOM 1413 CG2 VAL A 206 -16.810 -4.819 31.649 1.00 82.35 C ANISOU 1413 CG2 VAL A 206 9196 11826 10266 -175 -147 448 C ATOM 1414 N GLY A 207 -21.271 -5.919 32.562 1.00 74.89 N ANISOU 1414 N GLY A 207 8682 10796 8976 -303 -159 272 N ATOM 1415 CA GLY A 207 -22.650 -5.753 33.010 1.00 74.11 C ANISOU 1415 CA GLY A 207 8659 10692 8805 -353 -179 270 C ATOM 1416 C GLY A 207 -23.347 -6.961 33.612 1.00 78.26 C ANISOU 1416 C GLY A 207 9313 11139 9285 -366 -161 189 C ATOM 1417 O GLY A 207 -24.228 -6.789 34.460 1.00 77.62 O ANISOU 1417 O GLY A 207 9296 11014 9181 -385 -191 204 O ATOM 1418 N LEU A 208 -22.996 -8.192 33.170 1.00 74.95 N ANISOU 1418 N LEU A 208 8936 10691 8851 -359 -94 103 N ATOM 1419 CA LEU A 208 -23.656 -9.418 33.648 1.00 74.52 C ANISOU 1419 CA LEU A 208 9014 10537 8763 -387 -58 25 C ATOM 1420 C LEU A 208 -22.770 -10.456 34.380 1.00 77.81 C ANISOU 1420 C LEU A 208 9516 10787 9261 -292 -45 2 C ATOM 1421 O LEU A 208 -23.117 -10.848 35.495 1.00 77.08 O ANISOU 1421 O LEU A 208 9524 10585 9180 -276 -77 22 O ATOM 1422 CB LEU A 208 -24.489 -10.058 32.510 1.00 75.14 C ANISOU 1422 CB LEU A 208 9108 10709 8732 -499 22 -68 C ATOM 1423 CG LEU A 208 -24.967 -11.507 32.676 1.00 80.69 C ANISOU 1423 CG LEU A 208 9952 11293 9413 -554 91 -178 C ATOM 1424 CD1 LEU A 208 -26.216 -11.589 33.533 1.00 80.53 C ANISOU 1424 CD1 LEU A 208 9986 11243 9366 -630 62 -154 C ATOM 1425 CD2 LEU A 208 -25.239 -12.132 31.338 1.00 84.28 C ANISOU 1425 CD2 LEU A 208 10417 11837 9767 -656 173 -301 C ATOM 1426 N ILE A 209 -21.675 -10.931 33.736 1.00 74.54 N ANISOU 1426 N ILE A 209 9061 10361 8900 -219 14 -27 N ATOM 1427 CA ILE A 209 -20.772 -11.974 34.256 1.00 74.81 C ANISOU 1427 CA ILE A 209 9154 10244 9026 -101 46 -33 C ATOM 1428 C ILE A 209 -19.957 -11.535 35.481 1.00 78.14 C ANISOU 1428 C ILE A 209 9536 10619 9536 -1 -77 82 C ATOM 1429 O ILE A 209 -20.054 -12.181 36.525 1.00 77.75 O ANISOU 1429 O ILE A 209 9592 10447 9502 45 -107 111 O ATOM 1430 CB ILE A 209 -19.930 -12.660 33.121 1.00 78.90 C ANISOU 1430 CB ILE A 209 9640 10764 9573 -41 178 -106 C ATOM 1431 CG1 ILE A 209 -20.851 -13.331 32.072 1.00 79.62 C ANISOU 1431 CG1 ILE A 209 9826 10879 9547 -163 294 -251 C ATOM 1432 CG2 ILE A 209 -18.914 -13.667 33.684 1.00 80.77 C ANISOU 1432 CG2 ILE A 209 9914 10840 9933 120 221 -81 C ATOM 1433 CD1 ILE A 209 -20.151 -13.905 30.845 1.00 88.50 C ANISOU 1433 CD1 ILE A 209 10943 12024 10658 -124 442 -351 C ATOM 1434 N LEU A 210 -19.161 -10.453 35.351 1.00 74.82 N ANISOU 1434 N LEU A 210 8966 10299 9164 18 -149 149 N ATOM 1435 CA LEU A 210 -18.321 -9.915 36.432 1.00 75.07 C ANISOU 1435 CA LEU A 210 8939 10315 9267 79 -287 245 C ATOM 1436 C LEU A 210 -19.097 -9.520 37.712 1.00 78.50 C ANISOU 1436 C LEU A 210 9486 10702 9637 34 -393 271 C ATOM 1437 O LEU A 210 -18.676 -9.968 38.782 1.00 79.24 O ANISOU 1437 O LEU A 210 9634 10726 9749 105 -468 321 O ATOM 1438 CB LEU A 210 -17.366 -8.800 35.954 1.00 75.36 C ANISOU 1438 CB LEU A 210 8790 10466 9375 71 -335 301 C ATOM 1439 CG LEU A 210 -16.340 -9.191 34.878 1.00 81.60 C ANISOU 1439 CG LEU A 210 9450 11312 10244 143 -229 301 C ATOM 1440 CD1 LEU A 210 -15.832 -7.971 34.136 1.00 81.81 C ANISOU 1440 CD1 LEU A 210 9311 11468 10306 84 -237 350 C ATOM 1441 CD2 LEU A 210 -15.187 -9.988 35.461 1.00 86.37 C ANISOU 1441 CD2 LEU A 210 9998 11859 10960 288 -252 359 C ATOM 1442 N PRO A 211 -20.225 -8.750 37.672 1.00 73.15 N ANISOU 1442 N PRO A 211 8851 10064 8880 -67 -392 248 N ATOM 1443 CA PRO A 211 -20.958 -8.493 38.926 1.00 71.99 C ANISOU 1443 CA PRO A 211 8824 9862 8667 -90 -460 266 C ATOM 1444 C PRO A 211 -21.751 -9.730 39.377 1.00 75.31 C ANISOU 1444 C PRO A 211 9392 10188 9034 -83 -391 241 C ATOM 1445 O PRO A 211 -21.934 -9.932 40.580 1.00 75.65 O ANISOU 1445 O PRO A 211 9543 10165 9035 -57 -443 278 O ATOM 1446 CB PRO A 211 -21.861 -7.296 38.601 1.00 72.77 C ANISOU 1446 CB PRO A 211 8898 10030 8721 -175 -449 259 C ATOM 1447 CG PRO A 211 -21.763 -7.091 37.132 1.00 77.52 C ANISOU 1447 CG PRO A 211 9380 10729 9346 -206 -377 245 C ATOM 1448 CD PRO A 211 -20.921 -8.151 36.514 1.00 74.00 C ANISOU 1448 CD PRO A 211 8900 10272 8944 -150 -321 217 C ATOM 1449 N GLY A 212 -22.156 -10.569 38.415 1.00 70.70 N ANISOU 1449 N GLY A 212 8819 9597 8448 -113 -274 179 N ATOM 1450 CA GLY A 212 -22.863 -11.824 38.663 1.00 70.57 C ANISOU 1450 CA GLY A 212 8940 9470 8403 -132 -189 145 C ATOM 1451 C GLY A 212 -22.064 -12.775 39.533 1.00 73.99 C ANISOU 1451 C GLY A 212 9454 9768 8890 -14 -207 201 C ATOM 1452 O GLY A 212 -22.625 -13.385 40.449 1.00 73.26 O ANISOU 1452 O GLY A 212 9496 9580 8761 -15 -195 234 O ATOM 1453 N ILE A 213 -20.726 -12.862 39.276 1.00 70.52 N ANISOU 1453 N ILE A 213 8919 9332 8542 97 -235 233 N ATOM 1454 CA ILE A 213 -19.760 -13.663 40.046 1.00 71.06 C ANISOU 1454 CA ILE A 213 9017 9301 8680 244 -269 320 C ATOM 1455 C ILE A 213 -19.642 -13.056 41.454 1.00 71.57 C ANISOU 1455 C ILE A 213 9110 9395 8687 263 -428 417 C ATOM 1456 O ILE A 213 -19.840 -13.768 42.436 1.00 71.09 O ANISOU 1456 O ILE A 213 9180 9240 8592 312 -438 483 O ATOM 1457 CB ILE A 213 -18.376 -13.770 39.326 1.00 75.49 C ANISOU 1457 CB ILE A 213 9425 9897 9362 359 -254 339 C ATOM 1458 CG1 ILE A 213 -18.476 -14.645 38.062 1.00 77.04 C ANISOU 1458 CG1 ILE A 213 9647 10029 9594 361 -68 231 C ATOM 1459 CG2 ILE A 213 -17.284 -14.314 40.269 1.00 77.91 C ANISOU 1459 CG2 ILE A 213 9708 10150 9746 526 -334 472 C ATOM 1460 CD1 ILE A 213 -17.331 -14.432 37.035 1.00 89.46 C ANISOU 1460 CD1 ILE A 213 11048 11687 11255 439 -18 221 C ATOM 1461 N VAL A 214 -19.351 -11.737 41.531 1.00 66.26 N ANISOU 1461 N VAL A 214 8331 8848 7997 214 -542 420 N ATOM 1462 CA VAL A 214 -19.220 -10.942 42.758 1.00 66.16 C ANISOU 1462 CA VAL A 214 8348 8878 7911 201 -697 474 C ATOM 1463 C VAL A 214 -20.436 -11.156 43.683 1.00 71.06 C ANISOU 1463 C VAL A 214 9157 9437 8405 156 -668 473 C ATOM 1464 O VAL A 214 -20.249 -11.395 44.880 1.00 71.82 O ANISOU 1464 O VAL A 214 9346 9510 8431 205 -752 546 O ATOM 1465 CB VAL A 214 -18.970 -9.442 42.418 1.00 68.88 C ANISOU 1465 CB VAL A 214 8571 9333 8267 117 -775 440 C ATOM 1466 CG1 VAL A 214 -19.205 -8.526 43.616 1.00 68.66 C ANISOU 1466 CG1 VAL A 214 8628 9324 8136 63 -899 445 C ATOM 1467 CG2 VAL A 214 -17.570 -9.233 41.859 1.00 69.43 C ANISOU 1467 CG2 VAL A 214 8448 9473 8460 166 -832 478 C ATOM 1468 N ILE A 215 -21.668 -11.110 43.114 1.00 66.76 N ANISOU 1468 N ILE A 215 8657 8882 7826 64 -546 401 N ATOM 1469 CA ILE A 215 -22.923 -11.310 43.851 1.00 66.26 C ANISOU 1469 CA ILE A 215 8743 8775 7659 11 -487 402 C ATOM 1470 C ILE A 215 -23.057 -12.756 44.346 1.00 71.82 C ANISOU 1470 C ILE A 215 9576 9351 8362 63 -419 458 C ATOM 1471 O ILE A 215 -23.159 -12.961 45.555 1.00 71.47 O ANISOU 1471 O ILE A 215 9651 9272 8233 99 -461 534 O ATOM 1472 CB ILE A 215 -24.179 -10.783 43.080 1.00 67.90 C ANISOU 1472 CB ILE A 215 8919 9038 7843 -102 -388 330 C ATOM 1473 CG1 ILE A 215 -24.114 -9.247 42.910 1.00 67.55 C ANISOU 1473 CG1 ILE A 215 8784 9091 7792 -132 -454 309 C ATOM 1474 CG2 ILE A 215 -25.484 -11.191 43.788 1.00 68.02 C ANISOU 1474 CG2 ILE A 215 9063 9011 7772 -153 -302 344 C ATOM 1475 CD1 ILE A 215 -24.870 -8.656 41.714 1.00 72.15 C ANISOU 1475 CD1 ILE A 215 9262 9757 8396 -207 -378 265 C ATOM 1476 N LEU A 216 -23.043 -13.748 43.418 1.00 70.68 N ANISOU 1476 N LEU A 216 9421 9128 8305 64 -307 420 N ATOM 1477 CA LEU A 216 -23.173 -15.176 43.743 1.00 72.70 C ANISOU 1477 CA LEU A 216 9812 9221 8591 106 -214 465 C ATOM 1478 C LEU A 216 -22.196 -15.617 44.813 1.00 79.15 C ANISOU 1478 C LEU A 216 10679 9982 9411 257 -305 603 C ATOM 1479 O LEU A 216 -22.614 -16.268 45.772 1.00 80.68 O ANISOU 1479 O LEU A 216 11021 10087 9547 277 -279 690 O ATOM 1480 CB LEU A 216 -23.066 -16.088 42.504 1.00 73.50 C ANISOU 1480 CB LEU A 216 9898 9234 8796 93 -83 379 C ATOM 1481 CG LEU A 216 -24.304 -16.183 41.599 1.00 78.16 C ANISOU 1481 CG LEU A 216 10497 9843 9357 -81 29 256 C ATOM 1482 CD1 LEU A 216 -23.985 -16.949 40.320 1.00 79.29 C ANISOU 1482 CD1 LEU A 216 10626 9920 9579 -95 138 146 C ATOM 1483 CD2 LEU A 216 -25.495 -16.823 42.324 1.00 80.63 C ANISOU 1483 CD2 LEU A 216 10954 10063 9619 -174 106 285 C ATOM 1484 N SER A 217 -20.915 -15.209 44.682 1.00 75.42 N ANISOU 1484 N SER A 217 10073 9583 8999 358 -419 638 N ATOM 1485 CA SER A 217 -19.859 -15.525 45.642 1.00 76.39 C ANISOU 1485 CA SER A 217 10196 9703 9127 506 -540 784 C ATOM 1486 C SER A 217 -20.252 -15.121 47.074 1.00 80.02 C ANISOU 1486 C SER A 217 10773 10212 9419 484 -648 861 C ATOM 1487 O SER A 217 -20.200 -15.968 47.967 1.00 80.94 O ANISOU 1487 O SER A 217 11012 10248 9494 570 -649 989 O ATOM 1488 CB SER A 217 -18.533 -14.896 45.220 1.00 79.33 C ANISOU 1488 CB SER A 217 10362 10195 9585 574 -658 797 C ATOM 1489 OG SER A 217 -18.141 -15.385 43.946 1.00 86.01 O ANISOU 1489 OG SER A 217 11117 10991 10573 615 -532 736 O ATOM 1490 N CYS A 218 -20.726 -13.865 47.265 1.00 75.06 N ANISOU 1490 N CYS A 218 10128 9702 8689 372 -715 783 N ATOM 1491 CA CYS A 218 -21.176 -13.339 48.556 1.00 75.28 C ANISOU 1491 CA CYS A 218 10282 9782 8537 338 -795 818 C ATOM 1492 C CYS A 218 -22.294 -14.203 49.130 1.00 80.51 C ANISOU 1492 C CYS A 218 11131 10338 9123 321 -656 867 C ATOM 1493 O CYS A 218 -22.097 -14.833 50.167 1.00 81.51 O ANISOU 1493 O CYS A 218 11375 10431 9165 398 -694 997 O ATOM 1494 CB CYS A 218 -21.609 -11.879 48.439 1.00 74.30 C ANISOU 1494 CB CYS A 218 10118 9761 8352 224 -834 700 C ATOM 1495 SG CYS A 218 -20.266 -10.727 48.058 1.00 78.11 S ANISOU 1495 SG CYS A 218 10406 10366 8906 216 -1015 662 S ATOM 1496 N TYR A 219 -23.442 -14.278 48.428 1.00 76.79 N ANISOU 1496 N TYR A 219 10673 9819 8683 216 -496 777 N ATOM 1497 CA TYR A 219 -24.600 -15.055 48.870 1.00 77.31 C ANISOU 1497 CA TYR A 219 10889 9790 8696 165 -348 815 C ATOM 1498 C TYR A 219 -24.349 -16.515 49.109 1.00 83.32 C ANISOU 1498 C TYR A 219 11752 10390 9517 244 -278 931 C ATOM 1499 O TYR A 219 -24.892 -17.051 50.068 1.00 84.19 O ANISOU 1499 O TYR A 219 12014 10440 9534 247 -223 1033 O ATOM 1500 CB TYR A 219 -25.825 -14.811 48.003 1.00 77.27 C ANISOU 1500 CB TYR A 219 10837 9797 8724 25 -212 701 C ATOM 1501 CG TYR A 219 -26.363 -13.414 48.201 1.00 78.24 C ANISOU 1501 CG TYR A 219 10917 10055 8755 -32 -249 637 C ATOM 1502 CD1 TYR A 219 -26.023 -12.386 47.328 1.00 78.73 C ANISOU 1502 CD1 TYR A 219 10830 10209 8875 -54 -311 546 C ATOM 1503 CD2 TYR A 219 -27.144 -13.097 49.310 1.00 79.70 C ANISOU 1503 CD2 TYR A 219 11222 10266 8792 -48 -213 676 C ATOM 1504 CE1 TYR A 219 -26.493 -11.090 47.520 1.00 78.19 C ANISOU 1504 CE1 TYR A 219 10737 10232 8740 -91 -330 495 C ATOM 1505 CE2 TYR A 219 -27.614 -11.801 49.516 1.00 79.98 C ANISOU 1505 CE2 TYR A 219 11235 10402 8752 -79 -225 611 C ATOM 1506 CZ TYR A 219 -27.290 -10.803 48.613 1.00 85.20 C ANISOU 1506 CZ TYR A 219 11752 11130 9492 -99 -284 521 C ATOM 1507 OH TYR A 219 -27.738 -9.526 48.807 1.00 86.07 O ANISOU 1507 OH TYR A 219 11852 11305 9546 -118 -281 464 O ATOM 1508 N CYS A 220 -23.474 -17.140 48.304 1.00 80.72 N ANISOU 1508 N CYS A 220 11346 9983 9341 322 -273 928 N ATOM 1509 CA CYS A 220 -23.095 -18.537 48.488 1.00 82.99 C ANISOU 1509 CA CYS A 220 11733 10085 9715 429 -196 1045 C ATOM 1510 C CYS A 220 -22.342 -18.720 49.817 1.00 85.61 C ANISOU 1510 C CYS A 220 12134 10442 9952 577 -326 1240 C ATOM 1511 O CYS A 220 -22.503 -19.754 50.457 1.00 87.06 O ANISOU 1511 O CYS A 220 12465 10483 10130 640 -250 1381 O ATOM 1512 CB CYS A 220 -22.278 -19.043 47.306 1.00 84.82 C ANISOU 1512 CB CYS A 220 11862 10237 10129 498 -148 984 C ATOM 1513 SG CYS A 220 -22.026 -20.833 47.298 1.00 92.02 S ANISOU 1513 SG CYS A 220 12921 10856 11185 616 15 1090 S ATOM 1514 N ILE A 221 -21.556 -17.703 50.240 1.00 79.26 N ANISOU 1514 N ILE A 221 11227 9824 9064 619 -525 1251 N ATOM 1515 CA ILE A 221 -20.817 -17.699 51.504 1.00 79.79 C ANISOU 1515 CA ILE A 221 11340 9973 9003 735 -692 1422 C ATOM 1516 C ILE A 221 -21.789 -17.358 52.645 1.00 82.42 C ANISOU 1516 C ILE A 221 11847 10359 9109 652 -684 1449 C ATOM 1517 O ILE A 221 -21.783 -18.050 53.663 1.00 83.58 O ANISOU 1517 O ILE A 221 12137 10469 9153 731 -690 1622 O ATOM 1518 CB ILE A 221 -19.559 -16.774 51.436 1.00 82.74 C ANISOU 1518 CB ILE A 221 11523 10530 9386 782 -912 1407 C ATOM 1519 CG1 ILE A 221 -18.472 -17.392 50.521 1.00 83.85 C ANISOU 1519 CG1 ILE A 221 11499 10610 9748 916 -900 1446 C ATOM 1520 CG2 ILE A 221 -18.982 -16.490 52.829 1.00 84.88 C ANISOU 1520 CG2 ILE A 221 11844 10944 9463 841 -1120 1547 C ATOM 1521 CD1 ILE A 221 -17.497 -16.403 49.877 1.00 87.90 C ANISOU 1521 CD1 ILE A 221 11777 11283 10338 903 -1037 1366 C ATOM 1522 N ILE A 222 -22.634 -16.315 52.461 1.00 76.64 N ANISOU 1522 N ILE A 222 11107 9711 8303 506 -654 1289 N ATOM 1523 CA ILE A 222 -23.649 -15.881 53.437 1.00 76.32 C ANISOU 1523 CA ILE A 222 11221 9723 8056 428 -610 1288 C ATOM 1524 C ILE A 222 -24.600 -17.045 53.766 1.00 82.85 C ANISOU 1524 C ILE A 222 12204 10398 8879 416 -414 1393 C ATOM 1525 O ILE A 222 -24.814 -17.326 54.945 1.00 84.15 O ANISOU 1525 O ILE A 222 12527 10577 8870 452 -414 1526 O ATOM 1526 CB ILE A 222 -24.406 -14.586 53.000 1.00 76.77 C ANISOU 1526 CB ILE A 222 11217 9869 8083 297 -578 1100 C ATOM 1527 CG1 ILE A 222 -23.461 -13.369 52.917 1.00 76.54 C ANISOU 1527 CG1 ILE A 222 11072 9977 8033 296 -774 1013 C ATOM 1528 CG2 ILE A 222 -25.593 -14.283 53.926 1.00 76.98 C ANISOU 1528 CG2 ILE A 222 11402 9925 7922 234 -472 1102 C ATOM 1529 CD1 ILE A 222 -23.890 -12.294 51.864 1.00 80.48 C ANISOU 1529 CD1 ILE A 222 11441 10510 8628 195 -728 840 C ATOM 1530 N ILE A 223 -25.118 -17.753 52.740 1.00 80.02 N ANISOU 1530 N ILE A 223 11806 9893 8703 358 -251 1339 N ATOM 1531 CA ILE A 223 -26.005 -18.893 52.988 1.00 81.58 C ANISOU 1531 CA ILE A 223 12147 9926 8924 316 -60 1431 C ATOM 1532 C ILE A 223 -25.274 -20.236 53.245 1.00 89.24 C ANISOU 1532 C ILE A 223 13206 10717 9982 455 -39 1613 C ATOM 1533 O ILE A 223 -25.891 -21.301 53.179 1.00 90.87 O ANISOU 1533 O ILE A 223 13522 10733 10272 413 136 1674 O ATOM 1534 CB ILE A 223 -27.294 -18.968 52.116 1.00 83.14 C ANISOU 1534 CB ILE A 223 12308 10070 9213 138 123 1298 C ATOM 1535 CG1 ILE A 223 -26.990 -19.199 50.628 1.00 82.34 C ANISOU 1535 CG1 ILE A 223 12071 9901 9315 100 148 1161 C ATOM 1536 CG2 ILE A 223 -28.185 -17.740 52.367 1.00 82.50 C ANISOU 1536 CG2 ILE A 223 12187 10162 8997 42 128 1204 C ATOM 1537 CD1 ILE A 223 -28.203 -19.187 49.679 1.00 90.31 C ANISOU 1537 CD1 ILE A 223 13017 10903 10394 -91 290 1020 C ATOM 1538 N SER A 224 -23.965 -20.161 53.580 1.00 86.20 N ANISOU 1538 N SER A 224 12771 10397 9584 620 -219 1710 N ATOM 1539 CA SER A 224 -23.117 -21.292 53.961 1.00 88.24 C ANISOU 1539 CA SER A 224 13092 10521 9913 800 -231 1920 C ATOM 1540 C SER A 224 -22.726 -21.074 55.416 1.00 94.70 C ANISOU 1540 C SER A 224 14002 11485 10494 895 -387 2108 C ATOM 1541 O SER A 224 -22.864 -21.995 56.219 1.00 96.61 O ANISOU 1541 O SER A 224 14404 11620 10683 972 -320 2317 O ATOM 1542 CB SER A 224 -21.872 -21.378 53.079 1.00 91.09 C ANISOU 1542 CB SER A 224 13279 10869 10461 925 -316 1891 C ATOM 1543 OG SER A 224 -20.993 -22.416 53.493 1.00101.08 O ANISOU 1543 OG SER A 224 14586 12018 11803 1132 -330 2115 O ATOM 1544 N LYS A 225 -22.277 -19.841 55.762 1.00 90.87 N ANISOU 1544 N LYS A 225 13428 11241 9856 875 -591 2031 N ATOM 1545 CA LYS A 225 -21.919 -19.422 57.119 1.00 92.32 C ANISOU 1545 CA LYS A 225 13699 11609 9771 927 -767 2158 C ATOM 1546 C LYS A 225 -23.126 -19.651 58.022 1.00 97.88 C ANISOU 1546 C LYS A 225 14624 12282 10284 852 -616 2222 C ATOM 1547 O LYS A 225 -22.998 -20.329 59.034 1.00100.58 O ANISOU 1547 O LYS A 225 15110 12617 10489 948 -630 2448 O ATOM 1548 CB LYS A 225 -21.461 -17.940 57.134 1.00 93.46 C ANISOU 1548 CB LYS A 225 13723 11985 9805 854 -971 1989 C ATOM 1549 CG LYS A 225 -21.575 -17.196 58.482 1.00107.12 C ANISOU 1549 CG LYS A 225 15590 13908 11204 816 -1104 2013 C ATOM 1550 CD LYS A 225 -20.528 -17.612 59.532 1.00119.89 C ANISOU 1550 CD LYS A 225 17241 15649 12664 959 -1317 2245 C ATOM 1551 CE LYS A 225 -19.337 -16.683 59.571 1.00126.81 C ANISOU 1551 CE LYS A 225 17948 16736 13499 955 -1604 2181 C ATOM 1552 NZ LYS A 225 -18.429 -16.996 60.705 1.00135.46 N ANISOU 1552 NZ LYS A 225 19076 17999 14393 1070 -1834 2407 N ATOM 1553 N LEU A 226 -24.304 -19.166 57.593 1.00 93.11 N ANISOU 1553 N LEU A 226 14032 11654 9690 689 -456 2045 N ATOM 1554 CA LEU A 226 -25.601 -19.297 58.265 1.00 93.78 C ANISOU 1554 CA LEU A 226 14287 11714 9631 596 -271 2077 C ATOM 1555 C LEU A 226 -25.983 -20.755 58.523 1.00101.04 C ANISOU 1555 C LEU A 226 15344 12423 10624 635 -94 2285 C ATOM 1556 O LEU A 226 -26.605 -21.056 59.541 1.00101.94 O ANISOU 1556 O LEU A 226 15632 12547 10556 626 -2 2426 O ATOM 1557 CB LEU A 226 -26.681 -18.632 57.389 1.00 91.27 C ANISOU 1557 CB LEU A 226 13880 11391 9406 430 -128 1852 C ATOM 1558 CG LEU A 226 -27.123 -17.204 57.731 1.00 94.77 C ANISOU 1558 CG LEU A 226 14316 12022 9672 355 -172 1695 C ATOM 1559 CD1 LEU A 226 -25.964 -16.318 58.086 1.00 94.95 C ANISOU 1559 CD1 LEU A 226 14297 12203 9579 421 -429 1652 C ATOM 1560 CD2 LEU A 226 -27.883 -16.588 56.581 1.00 94.90 C ANISOU 1560 CD2 LEU A 226 14183 12027 9848 233 -69 1496 C ATOM 1561 N SER A 227 -25.614 -21.650 57.588 1.00 99.69 N ANISOU 1561 N SER A 227 15105 12052 10720 676 -32 2300 N ATOM 1562 CA SER A 227 -25.908 -23.081 57.632 1.00102.43 C ANISOU 1562 CA SER A 227 15580 12141 11196 706 153 2473 C ATOM 1563 C SER A 227 -25.052 -23.831 58.643 1.00113.02 C ANISOU 1563 C SER A 227 17039 13454 12448 908 66 2769 C ATOM 1564 O SER A 227 -25.611 -24.519 59.500 1.00114.84 O ANISOU 1564 O SER A 227 17453 13602 12577 911 191 2964 O ATOM 1565 CB SER A 227 -25.754 -23.698 56.248 1.00104.52 C ANISOU 1565 CB SER A 227 15747 12198 11769 680 250 2354 C ATOM 1566 OG SER A 227 -26.577 -23.043 55.296 1.00110.47 O ANISOU 1566 OG SER A 227 16388 12996 12589 490 321 2100 O ATOM 1567 N HIS A 228 -23.731 -23.693 58.547 1.00113.02 N ANISOU 1567 N HIS A 228 16923 13535 12485 1074 -141 2819 N ATOM 1568 CA HIS A 228 -22.801 -24.456 59.379 1.00117.52 C ANISOU 1568 CA HIS A 228 17562 14087 13004 1293 -241 3122 C ATOM 1569 C HIS A 228 -22.386 -23.757 60.676 1.00124.66 C ANISOU 1569 C HIS A 228 18512 15285 13567 1349 -468 3243 C ATOM 1570 O HIS A 228 -21.222 -23.809 61.073 1.00126.08 O ANISOU 1570 O HIS A 228 18619 15584 13701 1520 -682 3401 O ATOM 1571 CB HIS A 228 -21.556 -24.835 58.572 1.00119.14 C ANISOU 1571 CB HIS A 228 17597 14215 13455 1464 -329 3145 C ATOM 1572 CG HIS A 228 -20.551 -23.731 58.459 1.00122.02 C ANISOU 1572 CG HIS A 228 17752 14857 13754 1502 -603 3045 C ATOM 1573 ND1 HIS A 228 -20.903 -22.399 58.476 1.00121.89 N ANISOU 1573 ND1 HIS A 228 17676 15062 13575 1336 -706 2822 N ATOM 1574 CD2 HIS A 228 -19.203 -23.762 58.326 1.00125.20 C ANISOU 1574 CD2 HIS A 228 17983 15345 14243 1683 -788 3144 C ATOM 1575 CE1 HIS A 228 -19.817 -21.656 58.360 1.00121.21 C ANISOU 1575 CE1 HIS A 228 17403 15174 13477 1393 -945 2780 C ATOM 1576 NE2 HIS A 228 -18.772 -22.459 58.267 1.00123.53 N ANISOU 1576 NE2 HIS A 228 17612 15404 13919 1599 -1004 2975 N ATOM 1577 N SER A 229 -23.344 -23.114 61.333 1.00122.33 N ANISOU 1577 N SER A 229 18336 15114 13029 1203 -419 3168 N ATOM 1578 CA SER A 229 -23.131 -22.527 62.626 1.00124.78 C ANISOU 1578 CA SER A 229 18747 15684 12981 1232 -592 3267 C ATOM 1579 C SER A 229 -24.214 -22.961 63.593 1.00133.13 C ANISOU 1579 C SER A 229 20046 16703 13832 1179 -398 3410 C ATOM 1580 O SER A 229 -24.959 -23.891 63.318 1.00132.74 O ANISOU 1580 O SER A 229 20079 16410 13947 1144 -150 3489 O ATOM 1581 CB SER A 229 -23.138 -21.015 62.489 1.00125.52 C ANISOU 1581 CB SER A 229 18741 16006 12944 1103 -735 2982 C ATOM 1582 OG SER A 229 -24.430 -20.554 62.172 1.00129.72 O ANISOU 1582 OG SER A 229 19318 16488 13482 929 -525 2786 O ATOM 1583 N GLY A 900 -24.767 -22.457 64.634 1.00110.20 N ANISOU 1583 N GLY A 900 14513 13626 13730 309 -102 -92 N ATOM 1584 CA GLY A 900 -25.843 -22.833 65.533 1.00110.97 C ANISOU 1584 CA GLY A 900 14611 13725 13828 309 -104 -93 C ATOM 1585 C GLY A 900 -26.095 -23.336 66.940 1.00116.84 C ANISOU 1585 C GLY A 900 15353 14468 14571 309 -105 -93 C ATOM 1586 O GLY A 900 -26.645 -24.421 67.132 1.00117.06 O ANISOU 1586 O GLY A 900 15382 14497 14599 310 -105 -94 O ATOM 1587 N SER A 901 -25.677 -22.555 67.929 1.00113.63 N ANISOU 1587 N SER A 901 14946 14061 14166 310 -105 -94 N ATOM 1588 CA SER A 901 -25.848 -22.937 69.325 1.00113.38 C ANISOU 1588 CA SER A 901 14915 14029 14134 311 -106 -95 C ATOM 1589 C SER A 901 -26.066 -21.703 70.189 1.00116.68 C ANISOU 1589 C SER A 901 15335 14447 14553 311 -107 -95 C ATOM 1590 O SER A 901 -26.285 -21.805 71.396 1.00116.56 O ANISOU 1590 O SER A 901 15320 14430 14536 313 -107 -96 O ATOM 1591 CB SER A 901 -24.631 -23.719 69.821 1.00116.61 C ANISOU 1591 CB SER A 901 15324 14439 14544 310 -106 -95 C ATOM 1592 OG SER A 901 -24.849 -25.116 69.728 1.00124.47 O ANISOU 1592 OG SER A 901 16319 15436 15539 311 -106 -96 O ATOM 1593 N ASN A1002 -26.005 -20.536 69.558 1.00112.18 N ANISOU 1593 N ASN A1002 14020 17044 11559 138 -2138 -547 N ATOM 1594 CA ASN A1002 -26.197 -19.276 70.260 1.00110.57 C ANISOU 1594 CA ASN A1002 13816 16829 11366 261 -2048 -370 C ATOM 1595 C ASN A1002 -25.239 -19.119 71.434 1.00110.44 C ANISOU 1595 C ASN A1002 13951 16559 11450 147 -1855 -218 C ATOM 1596 O ASN A1002 -25.321 -18.145 72.183 1.00109.87 O ANISOU 1596 O ASN A1002 13893 16444 11410 213 -1763 -98 O ATOM 1597 CB ASN A1002 -27.628 -19.173 70.792 1.00112.63 C ANISOU 1597 CB ASN A1002 13801 17249 11746 228 -2088 -470 C ATOM 1598 CG ASN A1002 -28.531 -18.363 69.883 1.00134.63 C ANISOU 1598 CG ASN A1002 16457 20310 14386 505 -2253 -505 C ATOM 1599 OD1 ASN A1002 -28.847 -18.782 68.769 1.00131.69 O ANISOU 1599 OD1 ASN A1002 16016 20129 13892 581 -2435 -654 O ATOM 1600 ND2 ASN A1002 -28.951 -17.195 70.354 1.00126.66 N ANISOU 1600 ND2 ASN A1002 15422 19327 13376 681 -2196 -376 N ATOM 1601 N ILE A1003 -24.330 -20.077 71.595 1.00104.20 N ANISOU 1601 N ILE A1003 13275 15613 10705 -6 -1804 -237 N ATOM 1602 CA ILE A1003 -23.380 -20.014 72.679 1.00101.16 C ANISOU 1602 CA ILE A1003 13018 15027 10392 -92 -1655 -113 C ATOM 1603 C ILE A1003 -22.053 -20.185 72.024 1.00102.02 C ANISOU 1603 C ILE A1003 13303 15051 10411 -44 -1640 -69 C ATOM 1604 O ILE A1003 -21.035 -19.832 72.576 1.00 99.77 O ANISOU 1604 O ILE A1003 13128 14641 10139 -48 -1540 38 O ATOM 1605 CB ILE A1003 -23.551 -21.122 73.705 1.00104.07 C ANISOU 1605 CB ILE A1003 13347 15283 10911 -311 -1586 -164 C ATOM 1606 N PHE A1004 -22.069 -20.723 70.820 1.00 98.39 N ANISOU 1606 N PHE A1004 12852 14678 9852 6 -1743 -172 N ATOM 1607 CA PHE A1004 -20.816 -21.029 70.140 1.00 96.69 C ANISOU 1607 CA PHE A1004 12794 14397 9548 52 -1714 -149 C ATOM 1608 C PHE A1004 -20.075 -19.755 69.750 1.00 96.96 C ANISOU 1608 C PHE A1004 12938 14433 9469 215 -1634 18 C ATOM 1609 O PHE A1004 -18.990 -19.475 70.260 1.00 95.70 O ANISOU 1609 O PHE A1004 12861 14143 9356 183 -1515 115 O ATOM 1610 CB PHE A1004 -21.075 -21.888 68.901 1.00100.35 C ANISOU 1610 CB PHE A1004 13249 14971 9908 84 -1843 -323 C ATOM 1611 CG PHE A1004 -19.904 -22.737 68.496 1.00101.68 C ANISOU 1611 CG PHE A1004 13553 15034 10047 66 -1801 -362 C ATOM 1612 CD1 PHE A1004 -19.342 -23.635 69.387 1.00103.86 C ANISOU 1612 CD1 PHE A1004 13867 15118 10476 -79 -1726 -371 C ATOM 1613 CD2 PHE A1004 -19.366 -22.637 67.224 1.00104.56 C ANISOU 1613 CD2 PHE A1004 14014 15499 10216 223 -1826 -381 C ATOM 1614 CE1 PHE A1004 -18.264 -24.418 69.017 1.00104.76 C ANISOU 1614 CE1 PHE A1004 14098 15139 10566 -60 -1689 -410 C ATOM 1615 CE2 PHE A1004 -18.288 -23.417 66.848 1.00107.21 C ANISOU 1615 CE2 PHE A1004 14461 15749 10525 224 -1774 -428 C ATOM 1616 CZ PHE A1004 -17.737 -24.308 67.746 1.00104.43 C ANISOU 1616 CZ PHE A1004 14131 15203 10346 87 -1710 -448 C ATOM 1617 N GLU A1005 -20.667 -18.987 68.841 1.00 91.68 N ANISOU 1617 N GLU A1005 12266 13912 8656 393 -1696 48 N ATOM 1618 CA GLU A1005 -20.065 -17.742 68.381 1.00 90.59 C ANISOU 1618 CA GLU A1005 12260 13748 8412 555 -1591 228 C ATOM 1619 C GLU A1005 -20.190 -16.496 69.270 1.00 91.79 C ANISOU 1619 C GLU A1005 12419 13796 8661 574 -1486 365 C ATOM 1620 O GLU A1005 -19.916 -15.382 68.823 1.00 92.76 O ANISOU 1620 O GLU A1005 12656 13880 8708 718 -1395 513 O ATOM 1621 CB GLU A1005 -20.939 -17.090 67.307 1.00 94.03 C ANISOU 1621 CB GLU A1005 12701 14372 8655 791 -1689 257 C ATOM 1622 CG GLU A1005 -21.981 -18.019 66.707 1.00105.88 C ANISOU 1622 CG GLU A1005 14060 16085 10085 805 -1900 47 C ATOM 1623 CD GLU A1005 -21.405 -18.928 65.639 1.00122.56 C ANISOU 1623 CD GLU A1005 16253 18267 12048 825 -1955 -65 C ATOM 1624 OE1 GLU A1005 -20.707 -18.420 64.736 1.00116.91 O ANISOU 1624 OE1 GLU A1005 15702 17577 11139 994 -1884 55 O ATOM 1625 OE2 GLU A1005 -21.649 -20.151 65.703 1.00108.87 O ANISOU 1625 OE2 GLU A1005 14427 16546 10392 671 -2050 -274 O ATOM 1626 N MET A1006 -20.606 -16.686 70.522 1.00 84.82 N ANISOU 1626 N MET A1006 11432 12857 7940 434 -1482 316 N ATOM 1627 CA MET A1006 -20.777 -15.597 71.432 1.00 83.13 C ANISOU 1627 CA MET A1006 11221 12551 7814 450 -1391 403 C ATOM 1628 C MET A1006 -19.364 -15.730 71.866 1.00 84.36 C ANISOU 1628 C MET A1006 11465 12555 8032 329 -1281 434 C ATOM 1629 O MET A1006 -18.701 -14.756 72.120 1.00 83.87 O ANISOU 1629 O MET A1006 11484 12375 8010 341 -1162 522 O ATOM 1630 CB MET A1006 -21.670 -16.035 72.563 1.00 84.89 C ANISOU 1630 CB MET A1006 11295 12802 8157 335 -1426 314 C ATOM 1631 CG MET A1006 -20.992 -15.994 73.887 1.00 86.88 C ANISOU 1631 CG MET A1006 11577 12909 8524 196 -1322 331 C ATOM 1632 SD MET A1006 -22.068 -15.410 75.177 1.00 90.98 S ANISOU 1632 SD MET A1006 11993 13444 9131 189 -1281 315 S ATOM 1633 CE MET A1006 -22.095 -13.692 74.808 1.00 88.80 C ANISOU 1633 CE MET A1006 11811 13105 8824 389 -1215 420 C ATOM 1634 N LEU A1007 -18.873 -16.955 71.903 1.00 79.59 N ANISOU 1634 N LEU A1007 10842 11954 7444 217 -1320 350 N ATOM 1635 CA LEU A1007 -17.484 -17.151 72.294 1.00 78.08 C ANISOU 1635 CA LEU A1007 10708 11653 7307 131 -1233 368 C ATOM 1636 C LEU A1007 -16.539 -17.165 71.115 1.00 80.90 C ANISOU 1636 C LEU A1007 11150 12021 7567 201 -1182 404 C ATOM 1637 O LEU A1007 -15.364 -16.848 71.290 1.00 80.37 O ANISOU 1637 O LEU A1007 11114 11874 7548 160 -1074 443 O ATOM 1638 CB LEU A1007 -17.313 -18.360 73.219 1.00 77.40 C ANISOU 1638 CB LEU A1007 10575 11531 7301 0 -1271 286 C ATOM 1639 CG LEU A1007 -17.650 -18.042 74.669 1.00 81.44 C ANISOU 1639 CG LEU A1007 11043 11997 7902 -73 -1242 294 C ATOM 1640 CD1 LEU A1007 -18.616 -19.033 75.257 1.00 81.70 C ANISOU 1640 CD1 LEU A1007 11011 12055 7976 -154 -1292 235 C ATOM 1641 CD2 LEU A1007 -16.404 -17.826 75.497 1.00 83.16 C ANISOU 1641 CD2 LEU A1007 11292 12138 8168 -120 -1179 308 C ATOM 1642 N ARG A1008 -17.058 -17.468 69.902 1.00 76.97 N ANISOU 1642 N ARG A1008 10679 11641 6924 314 -1256 381 N ATOM 1643 CA ARG A1008 -16.278 -17.441 68.663 1.00 77.03 C ANISOU 1643 CA ARG A1008 10786 11689 6791 415 -1195 424 C ATOM 1644 C ARG A1008 -15.853 -15.993 68.391 1.00 81.12 C ANISOU 1644 C ARG A1008 11398 12135 7288 495 -1034 596 C ATOM 1645 O ARG A1008 -14.730 -15.764 67.950 1.00 80.89 O ANISOU 1645 O ARG A1008 11434 12057 7244 490 -889 659 O ATOM 1646 CB ARG A1008 -17.090 -18.003 67.486 1.00 77.97 C ANISOU 1646 CB ARG A1008 10917 11981 6728 541 -1332 343 C ATOM 1647 CG ARG A1008 -16.227 -18.364 66.283 1.00 89.50 C ANISOU 1647 CG ARG A1008 12481 13502 8024 634 -1278 340 C ATOM 1648 CD ARG A1008 -17.038 -18.688 65.042 1.00100.52 C ANISOU 1648 CD ARG A1008 13907 15098 9189 798 -1420 258 C ATOM 1649 NE ARG A1008 -16.202 -18.668 63.838 1.00110.04 N ANISOU 1649 NE ARG A1008 15251 16373 10187 937 -1323 306 N ATOM 1650 CZ ARG A1008 -16.561 -19.167 62.659 1.00124.78 C ANISOU 1650 CZ ARG A1008 17170 18428 11813 1087 -1434 201 C ATOM 1651 NH1 ARG A1008 -17.746 -19.746 62.509 1.00114.88 N ANISOU 1651 NH1 ARG A1008 15819 17312 10519 1100 -1662 18 N ATOM 1652 NH2 ARG A1008 -15.735 -19.100 61.624 1.00109.83 N ANISOU 1652 NH2 ARG A1008 15415 16598 9716 1221 -1312 261 N ATOM 1653 N ILE A1009 -16.744 -15.025 68.698 1.00 78.16 N ANISOU 1653 N ILE A1009 11028 11738 6931 562 -1041 668 N ATOM 1654 CA ILE A1009 -16.517 -13.583 68.558 1.00 78.83 C ANISOU 1654 CA ILE A1009 11226 11699 7026 640 -878 835 C ATOM 1655 C ILE A1009 -15.552 -13.078 69.652 1.00 82.25 C ANISOU 1655 C ILE A1009 11635 11947 7671 457 -740 831 C ATOM 1656 O ILE A1009 -14.584 -12.386 69.336 1.00 82.91 O ANISOU 1656 O ILE A1009 11796 11914 7791 428 -557 920 O ATOM 1657 CB ILE A1009 -17.878 -12.819 68.579 1.00 82.66 C ANISOU 1657 CB ILE A1009 11715 12224 7466 803 -952 888 C ATOM 1658 N ASP A1010 -15.837 -13.420 70.930 1.00 77.25 N ANISOU 1658 N ASP A1010 10887 11297 7166 335 -823 720 N ATOM 1659 CA ASP A1010 -15.098 -12.988 72.120 1.00 76.27 C ANISOU 1659 CA ASP A1010 10721 11043 7216 180 -745 673 C ATOM 1660 C ASP A1010 -13.709 -13.611 72.307 1.00 79.87 C ANISOU 1660 C ASP A1010 11119 11494 7733 52 -704 607 C ATOM 1661 O ASP A1010 -12.733 -12.876 72.463 1.00 79.52 O ANISOU 1661 O ASP A1010 11075 11345 7792 -31 -566 617 O ATOM 1662 CB ASP A1010 -15.967 -13.159 73.381 1.00 77.05 C ANISOU 1662 CB ASP A1010 10736 11162 7379 135 -848 586 C ATOM 1663 CG ASP A1010 -17.201 -12.269 73.430 1.00 87.85 C ANISOU 1663 CG ASP A1010 12132 12515 8732 260 -853 638 C ATOM 1664 OD1 ASP A1010 -17.152 -11.144 72.871 1.00 90.78 O ANISOU 1664 OD1 ASP A1010 12615 12779 9099 357 -740 747 O ATOM 1665 OD2 ASP A1010 -18.198 -12.675 74.060 1.00 90.73 O ANISOU 1665 OD2 ASP A1010 12409 12966 9099 265 -951 575 O ATOM 1666 N GLU A1011 -13.625 -14.954 72.317 1.00 76.65 N ANISOU 1666 N GLU A1011 10652 11192 7277 37 -820 527 N ATOM 1667 CA GLU A1011 -12.368 -15.687 72.477 1.00 76.68 C ANISOU 1667 CA GLU A1011 10594 11214 7325 -35 -803 461 C ATOM 1668 C GLU A1011 -11.672 -15.865 71.123 1.00 82.02 C ANISOU 1668 C GLU A1011 11319 11933 7913 32 -711 508 C ATOM 1669 O GLU A1011 -10.566 -15.359 70.928 1.00 82.90 O ANISOU 1669 O GLU A1011 11405 12005 8088 -19 -565 529 O ATOM 1670 CB GLU A1011 -12.602 -17.053 73.156 1.00 77.24 C ANISOU 1670 CB GLU A1011 10614 11342 7390 -56 -947 370 C ATOM 1671 CG GLU A1011 -12.718 -16.996 74.669 1.00 90.47 C ANISOU 1671 CG GLU A1011 12236 12990 9149 -131 -996 322 C ATOM 1672 CD GLU A1011 -11.549 -17.564 75.456 1.00117.75 C ANISOU 1672 CD GLU A1011 15622 16463 12653 -170 -1018 253 C ATOM 1673 OE1 GLU A1011 -10.389 -17.433 74.998 1.00118.03 O ANISOU 1673 OE1 GLU A1011 15610 16515 12722 -176 -950 235 O ATOM 1674 OE2 GLU A1011 -11.795 -18.114 76.555 1.00110.02 O ANISOU 1674 OE2 GLU A1011 14632 15496 11674 -182 -1096 221 O ATOM 1675 N GLY A1012 -12.335 -16.562 70.205 1.00 78.63 N ANISOU 1675 N GLY A1012 10947 11592 7334 139 -790 509 N ATOM 1676 CA GLY A1012 -11.804 -16.847 68.882 1.00 79.67 C ANISOU 1676 CA GLY A1012 11144 11795 7333 232 -717 537 C ATOM 1677 C GLY A1012 -11.640 -18.332 68.636 1.00 83.37 C ANISOU 1677 C GLY A1012 11589 12339 7748 256 -824 412 C ATOM 1678 O GLY A1012 -11.208 -19.072 69.528 1.00 82.21 O ANISOU 1678 O GLY A1012 11366 12159 7710 181 -878 329 O ATOM 1679 N LEU A1013 -11.985 -18.770 67.414 1.00 80.46 N ANISOU 1679 N LEU A1013 11302 12070 7198 378 -856 393 N ATOM 1680 CA LEU A1013 -11.892 -20.162 66.985 1.00 80.11 C ANISOU 1680 CA LEU A1013 11265 12082 7092 413 -949 249 C ATOM 1681 C LEU A1013 -10.595 -20.391 66.214 1.00 84.48 C ANISOU 1681 C LEU A1013 11840 12675 7583 478 -805 248 C ATOM 1682 O LEU A1013 -10.309 -19.657 65.266 1.00 85.66 O ANISOU 1682 O LEU A1013 12061 12884 7602 563 -668 349 O ATOM 1683 CB LEU A1013 -13.110 -20.510 66.113 1.00 81.13 C ANISOU 1683 CB LEU A1013 11453 12320 7052 507 -1091 179 C ATOM 1684 CG LEU A1013 -13.248 -21.957 65.659 1.00 86.45 C ANISOU 1684 CG LEU A1013 12143 13028 7676 523 -1206 -13 C ATOM 1685 CD1 LEU A1013 -14.101 -22.757 66.630 1.00 85.85 C ANISOU 1685 CD1 LEU A1013 11997 12867 7755 390 -1344 -120 C ATOM 1686 CD2 LEU A1013 -13.859 -22.022 64.278 1.00 90.79 C ANISOU 1686 CD2 LEU A1013 12771 13746 7979 672 -1280 -80 C ATOM 1687 N ARG A1014 -9.808 -21.396 66.636 1.00 80.12 N ANISOU 1687 N ARG A1014 11230 12090 7122 452 -819 145 N ATOM 1688 CA ARG A1014 -8.552 -21.787 65.987 1.00 80.78 C ANISOU 1688 CA ARG A1014 11301 12226 7165 528 -688 111 C ATOM 1689 C ARG A1014 -8.622 -23.282 65.685 1.00 85.14 C ANISOU 1689 C ARG A1014 11901 12776 7670 601 -799 -57 C ATOM 1690 O ARG A1014 -8.541 -24.108 66.599 1.00 84.07 O ANISOU 1690 O ARG A1014 11727 12544 7670 557 -887 -127 O ATOM 1691 CB ARG A1014 -7.320 -21.404 66.828 1.00 79.30 C ANISOU 1691 CB ARG A1014 10968 12005 7158 449 -575 145 C ATOM 1692 CG ARG A1014 -7.034 -19.902 66.818 1.00 90.45 C ANISOU 1692 CG ARG A1014 12346 13403 8618 370 -408 286 C ATOM 1693 CD ARG A1014 -5.747 -19.525 67.537 1.00106.65 C ANISOU 1693 CD ARG A1014 14217 15446 10858 273 -295 270 C ATOM 1694 NE ARG A1014 -4.547 -19.929 66.794 1.00121.46 N ANISOU 1694 NE ARG A1014 16020 17420 12709 344 -144 229 N ATOM 1695 CZ ARG A1014 -3.937 -19.183 65.876 1.00138.83 C ANISOU 1695 CZ ARG A1014 18223 19661 14866 341 100 317 C ATOM 1696 NH1 ARG A1014 -2.857 -19.637 65.254 1.00127.33 N ANISOU 1696 NH1 ARG A1014 16679 18311 13388 411 245 265 N ATOM 1697 NH2 ARG A1014 -4.407 -17.979 65.567 1.00126.97 N ANISOU 1697 NH2 ARG A1014 16818 18086 13339 281 220 466 N ATOM 1698 N LEU A1015 -8.847 -23.614 64.395 1.00 82.84 N ANISOU 1698 N LEU A1015 11717 12584 7174 723 -795 -125 N ATOM 1699 CA LEU A1015 -9.031 -24.974 63.867 1.00 83.52 C ANISOU 1699 CA LEU A1015 11878 12665 7190 798 -896 -322 C ATOM 1700 C LEU A1015 -7.755 -25.832 63.766 1.00 88.62 C ANISOU 1700 C LEU A1015 12503 13290 7877 887 -801 -407 C ATOM 1701 O LEU A1015 -7.835 -27.023 63.446 1.00 89.19 O ANISOU 1701 O LEU A1015 12651 13311 7924 953 -875 -582 O ATOM 1702 CB LEU A1015 -9.798 -24.929 62.537 1.00 85.17 C ANISOU 1702 CB LEU A1015 12203 13019 7138 908 -950 -391 C ATOM 1703 CG LEU A1015 -11.178 -24.289 62.610 1.00 89.04 C ANISOU 1703 CG LEU A1015 12696 13552 7584 859 -1087 -348 C ATOM 1704 CD1 LEU A1015 -11.371 -23.279 61.505 1.00 90.64 C ANISOU 1704 CD1 LEU A1015 12983 13928 7528 1004 -1018 -231 C ATOM 1705 CD2 LEU A1015 -12.257 -25.326 62.601 1.00 91.31 C ANISOU 1705 CD2 LEU A1015 12991 13814 7888 808 -1298 -565 C ATOM 1706 N LYS A1016 -6.592 -25.228 64.059 1.00 85.14 N ANISOU 1706 N LYS A1016 11950 12884 7517 888 -638 -299 N ATOM 1707 CA LYS A1016 -5.292 -25.893 64.090 1.00 85.96 C ANISOU 1707 CA LYS A1016 11976 13000 7684 985 -540 -367 C ATOM 1708 C LYS A1016 -4.707 -25.714 65.501 1.00 88.13 C ANISOU 1708 C LYS A1016 12091 13206 8187 898 -561 -307 C ATOM 1709 O LYS A1016 -5.077 -24.754 66.183 1.00 86.48 O ANISOU 1709 O LYS A1016 11826 12977 8055 762 -577 -195 O ATOM 1710 CB LYS A1016 -4.354 -25.308 63.023 1.00 90.54 C ANISOU 1710 CB LYS A1016 12526 13741 8135 1076 -307 -319 C ATOM 1711 CG LYS A1016 -3.217 -26.247 62.629 1.00109.48 C ANISOU 1711 CG LYS A1016 14878 16192 10529 1235 -212 -446 C ATOM 1712 CD LYS A1016 -2.000 -25.492 62.100 1.00122.09 C ANISOU 1712 CD LYS A1016 16338 17941 12110 1265 62 -365 C ATOM 1713 CE LYS A1016 -0.825 -26.402 61.826 1.00134.22 C ANISOU 1713 CE LYS A1016 17781 19549 13667 1436 160 -498 C ATOM 1714 NZ LYS A1016 -0.992 -27.167 60.561 1.00144.03 N ANISOU 1714 NZ LYS A1016 19207 20854 14663 1620 196 -628 N ATOM 1715 N ILE A1017 -3.828 -26.645 65.951 1.00 85.17 N ANISOU 1715 N ILE A1017 11651 12802 7908 1000 -573 -391 N ATOM 1716 CA ILE A1017 -3.194 -26.604 67.278 1.00 84.33 C ANISOU 1716 CA ILE A1017 11390 12671 7980 972 -620 -355 C ATOM 1717 C ILE A1017 -2.370 -25.329 67.442 1.00 87.96 C ANISOU 1717 C ILE A1017 11646 13262 8513 880 -481 -275 C ATOM 1718 O ILE A1017 -1.677 -24.929 66.506 1.00 88.89 O ANISOU 1718 O ILE A1017 11702 13496 8576 913 -296 -273 O ATOM 1719 CB ILE A1017 -2.358 -27.892 67.576 1.00 89.11 C ANISOU 1719 CB ILE A1017 11977 13238 8642 1163 -657 -457 C ATOM 1720 CG1 ILE A1017 -3.275 -29.117 67.816 1.00 89.40 C ANISOU 1720 CG1 ILE A1017 12229 13064 8676 1201 -800 -518 C ATOM 1721 CG2 ILE A1017 -1.390 -27.693 68.769 1.00 90.65 C ANISOU 1721 CG2 ILE A1017 11961 13501 8982 1189 -688 -426 C ATOM 1722 CD1 ILE A1017 -2.551 -30.494 67.974 1.00 98.09 C ANISOU 1722 CD1 ILE A1017 13379 14066 9822 1423 -820 -613 C ATOM 1723 N TYR A1018 -2.459 -24.698 68.630 1.00 83.43 N ANISOU 1723 N TYR A1018 10973 12663 8064 755 -556 -220 N ATOM 1724 CA TYR A1018 -1.725 -23.480 68.987 1.00 83.61 C ANISOU 1724 CA TYR A1018 10792 12777 8199 629 -446 -181 C ATOM 1725 C TYR A1018 -1.294 -23.493 70.466 1.00 86.22 C ANISOU 1725 C TYR A1018 10967 13127 8667 606 -583 -220 C ATOM 1726 O TYR A1018 -1.703 -24.378 71.217 1.00 84.82 O ANISOU 1726 O TYR A1018 10879 12875 8473 691 -750 -232 O ATOM 1727 CB TYR A1018 -2.554 -22.216 68.646 1.00 84.27 C ANISOU 1727 CB TYR A1018 10960 12807 8250 467 -366 -66 C ATOM 1728 CG TYR A1018 -3.739 -21.964 69.555 1.00 84.52 C ANISOU 1728 CG TYR A1018 11089 12726 8299 375 -528 -20 C ATOM 1729 CD1 TYR A1018 -3.674 -21.016 70.572 1.00 85.89 C ANISOU 1729 CD1 TYR A1018 11155 12881 8598 237 -545 -1 C ATOM 1730 CD2 TYR A1018 -4.936 -22.653 69.382 1.00 84.57 C ANISOU 1730 CD2 TYR A1018 11281 12651 8202 419 -654 -16 C ATOM 1731 CE1 TYR A1018 -4.763 -20.776 71.410 1.00 84.80 C ANISOU 1731 CE1 TYR A1018 11104 12652 8462 169 -674 36 C ATOM 1732 CE2 TYR A1018 -6.032 -22.422 70.214 1.00 84.06 C ANISOU 1732 CE2 TYR A1018 11279 12500 8161 332 -778 24 C ATOM 1733 CZ TYR A1018 -5.943 -21.477 71.222 1.00 89.49 C ANISOU 1733 CZ TYR A1018 11869 13177 8954 218 -781 58 C ATOM 1734 OH TYR A1018 -7.018 -21.249 72.043 1.00 87.84 O ANISOU 1734 OH TYR A1018 11722 12896 8757 149 -884 92 O ATOM 1735 N LYS A1019 -0.464 -22.513 70.871 1.00 83.20 N ANISOU 1735 N LYS A1019 10356 12843 8412 490 -503 -245 N ATOM 1736 CA LYS A1019 0.010 -22.342 72.246 1.00 82.62 C ANISOU 1736 CA LYS A1019 10107 12835 8450 463 -640 -313 C ATOM 1737 C LYS A1019 -0.709 -21.137 72.845 1.00 85.60 C ANISOU 1737 C LYS A1019 10515 13132 8878 254 -651 -267 C ATOM 1738 O LYS A1019 -0.746 -20.068 72.226 1.00 84.71 O ANISOU 1738 O LYS A1019 10391 12983 8813 102 -477 -223 O ATOM 1739 CB LYS A1019 1.536 -22.136 72.293 1.00 86.89 C ANISOU 1739 CB LYS A1019 10322 13573 9120 479 -559 -435 C ATOM 1740 CG LYS A1019 2.361 -23.384 72.002 1.00 98.31 C ANISOU 1740 CG LYS A1019 11698 15125 10531 735 -584 -504 C ATOM 1741 CD LYS A1019 3.847 -23.085 72.148 1.00111.67 C ANISOU 1741 CD LYS A1019 13011 17050 12370 744 -514 -643 C ATOM 1742 CE LYS A1019 4.728 -24.280 71.879 1.00125.79 C ANISOU 1742 CE LYS A1019 14702 18962 14131 1032 -534 -720 C ATOM 1743 NZ LYS A1019 6.149 -24.002 72.221 1.00137.02 N ANISOU 1743 NZ LYS A1019 15702 20651 15707 1055 -510 -879 N ATOM 1744 N ASP A1020 -1.295 -21.309 74.040 1.00 82.42 N ANISOU 1744 N ASP A1020 10171 12689 8456 261 -838 -268 N ATOM 1745 CA ASP A1020 -2.034 -20.245 74.718 1.00 81.80 C ANISOU 1745 CA ASP A1020 10132 12535 8414 92 -861 -243 C ATOM 1746 C ASP A1020 -1.107 -19.249 75.444 1.00 87.95 C ANISOU 1746 C ASP A1020 10659 13417 9342 -40 -846 -371 C ATOM 1747 O ASP A1020 0.116 -19.335 75.311 1.00 89.32 O ANISOU 1747 O ASP A1020 10599 13737 9602 -17 -804 -477 O ATOM 1748 CB ASP A1020 -3.065 -20.843 75.697 1.00 82.44 C ANISOU 1748 CB ASP A1020 10381 12543 8401 155 -1039 -196 C ATOM 1749 CG ASP A1020 -2.497 -21.620 76.875 1.00 98.33 C ANISOU 1749 CG ASP A1020 12317 14659 10386 297 -1209 -258 C ATOM 1750 OD1 ASP A1020 -1.256 -21.761 76.957 1.00100.88 O ANISOU 1750 OD1 ASP A1020 12430 15136 10765 372 -1223 -361 O ATOM 1751 OD2 ASP A1020 -3.296 -22.089 77.715 1.00106.29 O ANISOU 1751 OD2 ASP A1020 13473 15604 11309 348 -1322 -200 O ATOM 1752 N THR A1021 -1.699 -18.305 76.203 1.00 84.63 N ANISOU 1752 N THR A1021 10272 12924 8959 -179 -880 -384 N ATOM 1753 CA THR A1021 -0.990 -17.284 76.983 1.00 86.41 C ANISOU 1753 CA THR A1021 10282 13218 9331 -333 -883 -542 C ATOM 1754 C THR A1021 0.091 -17.881 77.895 1.00 91.85 C ANISOU 1754 C THR A1021 10732 14137 10030 -221 -1057 -708 C ATOM 1755 O THR A1021 1.202 -17.350 77.950 1.00 93.83 O ANISOU 1755 O THR A1021 10702 14516 10434 -321 -1010 -871 O ATOM 1756 CB THR A1021 -1.983 -16.424 77.783 1.00 96.18 C ANISOU 1756 CB THR A1021 11649 14334 10562 -442 -930 -538 C ATOM 1757 OG1 THR A1021 -2.796 -17.273 78.603 1.00 95.02 O ANISOU 1757 OG1 THR A1021 11652 14201 10250 -293 -1115 -483 O ATOM 1758 CG2 THR A1021 -2.850 -15.537 76.890 1.00 94.05 C ANISOU 1758 CG2 THR A1021 11558 13855 10320 -555 -743 -401 C ATOM 1759 N GLU A1022 -0.232 -18.994 78.585 1.00 87.20 N ANISOU 1759 N GLU A1022 10252 13601 9281 -7 -1249 -664 N ATOM 1760 CA GLU A1022 0.705 -19.688 79.475 1.00 88.54 C ANISOU 1760 CA GLU A1022 10240 13994 9408 175 -1438 -785 C ATOM 1761 C GLU A1022 1.740 -20.564 78.749 1.00 91.69 C ANISOU 1761 C GLU A1022 10489 14514 9833 341 -1403 -807 C ATOM 1762 O GLU A1022 2.790 -20.850 79.321 1.00 93.61 O ANISOU 1762 O GLU A1022 10487 14986 10096 469 -1529 -949 O ATOM 1763 CB GLU A1022 0.001 -20.432 80.635 1.00 89.42 C ANISOU 1763 CB GLU A1022 10543 14105 9328 352 -1637 -713 C ATOM 1764 CG GLU A1022 -1.337 -21.069 80.295 1.00100.11 C ANISOU 1764 CG GLU A1022 12229 15236 10572 389 -1590 -504 C ATOM 1765 CD GLU A1022 -2.556 -20.269 80.712 1.00123.69 C ANISOU 1765 CD GLU A1022 15373 18089 13533 232 -1565 -453 C ATOM 1766 OE1 GLU A1022 -2.694 -19.985 81.925 1.00123.33 O ANISOU 1766 OE1 GLU A1022 15324 18122 13415 248 -1686 -513 O ATOM 1767 OE2 GLU A1022 -3.397 -19.963 79.835 1.00113.70 O ANISOU 1767 OE2 GLU A1022 14241 16658 12301 120 -1432 -355 O ATOM 1768 N GLY A1023 1.414 -21.033 77.552 1.00 85.59 N ANISOU 1768 N GLY A1023 9867 13611 9042 370 -1252 -679 N ATOM 1769 CA GLY A1023 2.348 -21.816 76.766 1.00 85.96 C ANISOU 1769 CA GLY A1023 9790 13761 9111 530 -1187 -708 C ATOM 1770 C GLY A1023 1.900 -23.219 76.435 1.00 86.89 C ANISOU 1770 C GLY A1023 10151 13773 9089 770 -1235 -590 C ATOM 1771 O GLY A1023 2.544 -23.944 75.711 1.00 86.87 O ANISOU 1771 O GLY A1023 10096 13821 9088 925 -1171 -610 O ATOM 1772 N TYR A1024 0.749 -23.619 76.939 1.00 81.41 N ANISOU 1772 N TYR A1024 9733 12916 8283 793 -1329 -474 N ATOM 1773 CA TYR A1024 0.307 -24.978 76.703 1.00 81.05 C ANISOU 1773 CA TYR A1024 9924 12737 8136 994 -1365 -379 C ATOM 1774 C TYR A1024 -0.434 -25.123 75.421 1.00 83.42 C ANISOU 1774 C TYR A1024 10406 12872 8417 915 -1220 -314 C ATOM 1775 O TYR A1024 -0.957 -24.170 74.902 1.00 82.06 O ANISOU 1775 O TYR A1024 10250 12659 8271 715 -1118 -290 O ATOM 1776 CB TYR A1024 -0.597 -25.447 77.813 1.00 81.76 C ANISOU 1776 CB TYR A1024 10226 12715 8123 1047 -1504 -281 C ATOM 1777 CG TYR A1024 0.038 -25.346 79.151 1.00 85.80 C ANISOU 1777 CG TYR A1024 10598 13407 8596 1161 -1669 -337 C ATOM 1778 CD1 TYR A1024 -0.449 -24.476 80.097 1.00 87.13 C ANISOU 1778 CD1 TYR A1024 10758 13611 8735 1022 -1737 -350 C ATOM 1779 CD2 TYR A1024 1.125 -26.116 79.472 1.00 89.04 C ANISOU 1779 CD2 TYR A1024 10883 13968 8981 1432 -1767 -390 C ATOM 1780 CE1 TYR A1024 0.126 -24.378 81.316 1.00 89.36 C ANISOU 1780 CE1 TYR A1024 10917 14086 8949 1141 -1904 -424 C ATOM 1781 CE2 TYR A1024 1.706 -26.020 80.689 1.00 91.70 C ANISOU 1781 CE2 TYR A1024 11084 14508 9250 1566 -1945 -452 C ATOM 1782 CZ TYR A1024 1.202 -25.150 81.610 1.00 98.57 C ANISOU 1782 CZ TYR A1024 11955 15422 10076 1415 -2018 -475 C ATOM 1783 OH TYR A1024 1.776 -25.047 82.844 1.00102.21 O ANISOU 1783 OH TYR A1024 12285 16113 10436 1564 -2213 -560 O ATOM 1784 N TYR A1025 -0.491 -26.349 74.936 1.00 79.79 N ANISOU 1784 N TYR A1025 10098 12315 7904 1094 -1220 -293 N ATOM 1785 CA TYR A1025 -1.135 -26.673 73.665 1.00 78.50 C ANISOU 1785 CA TYR A1025 10109 12019 7700 1057 -1108 -273 C ATOM 1786 C TYR A1025 -2.659 -26.644 73.733 1.00 80.41 C ANISOU 1786 C TYR A1025 10583 12078 7893 916 -1141 -190 C ATOM 1787 O TYR A1025 -3.271 -27.337 74.543 1.00 79.17 O ANISOU 1787 O TYR A1025 10571 11796 7714 958 -1239 -136 O ATOM 1788 CB TYR A1025 -0.604 -27.989 73.084 1.00 81.22 C ANISOU 1788 CB TYR A1025 10524 12318 8016 1296 -1092 -324 C ATOM 1789 CG TYR A1025 0.824 -27.916 72.582 1.00 84.56 C ANISOU 1789 CG TYR A1025 10697 12946 8486 1423 -1003 -423 C ATOM 1790 CD1 TYR A1025 1.835 -28.653 73.188 1.00 88.70 C ANISOU 1790 CD1 TYR A1025 11099 13566 9037 1674 -1085 -473 C ATOM 1791 CD2 TYR A1025 1.158 -27.133 71.479 1.00 85.18 C ANISOU 1791 CD2 TYR A1025 10661 13128 8575 1310 -822 -459 C ATOM 1792 CE1 TYR A1025 3.148 -28.601 72.722 1.00 91.87 C ANISOU 1792 CE1 TYR A1025 11229 14181 9495 1797 -998 -582 C ATOM 1793 CE2 TYR A1025 2.468 -27.070 71.006 1.00 88.02 C ANISOU 1793 CE2 TYR A1025 10770 13684 8991 1411 -705 -551 C ATOM 1794 CZ TYR A1025 3.459 -27.815 71.624 1.00 97.25 C ANISOU 1794 CZ TYR A1025 11781 14963 10205 1650 -796 -625 C ATOM 1795 OH TYR A1025 4.750 -27.764 71.158 1.00100.46 O ANISOU 1795 OH TYR A1025 11901 15590 10679 1756 -677 -732 O ATOM 1796 N THR A1026 -3.257 -25.822 72.865 1.00 77.05 N ANISOU 1796 N THR A1026 10182 11646 7447 758 -1048 -174 N ATOM 1797 CA THR A1026 -4.690 -25.550 72.794 1.00 75.82 C ANISOU 1797 CA THR A1026 10185 11372 7250 619 -1073 -113 C ATOM 1798 C THR A1026 -5.221 -25.682 71.335 1.00 81.12 C ANISOU 1798 C THR A1026 10968 12016 7838 612 -997 -139 C ATOM 1799 O THR A1026 -4.429 -25.750 70.391 1.00 82.35 O ANISOU 1799 O THR A1026 11076 12254 7960 695 -896 -188 O ATOM 1800 CB THR A1026 -4.938 -24.145 73.411 1.00 84.29 C ANISOU 1800 CB THR A1026 11161 12498 8366 455 -1063 -65 C ATOM 1801 OG1 THR A1026 -4.018 -23.895 74.480 1.00 85.97 O ANISOU 1801 OG1 THR A1026 11211 12810 8643 482 -1114 -99 O ATOM 1802 CG2 THR A1026 -6.335 -23.964 73.933 1.00 81.71 C ANISOU 1802 CG2 THR A1026 10960 12068 8017 352 -1128 -3 C ATOM 1803 N ILE A1027 -6.565 -25.733 71.176 1.00 77.22 N ANISOU 1803 N ILE A1027 10611 11429 7302 524 -1050 -118 N ATOM 1804 CA ILE A1027 -7.320 -25.847 69.917 1.00 77.63 C ANISOU 1804 CA ILE A1027 10769 11476 7248 518 -1032 -162 C ATOM 1805 C ILE A1027 -8.790 -25.399 70.154 1.00 81.10 C ANISOU 1805 C ILE A1027 11264 11872 7678 387 -1106 -121 C ATOM 1806 O ILE A1027 -9.237 -25.377 71.302 1.00 79.13 O ANISOU 1806 O ILE A1027 11002 11555 7507 313 -1164 -73 O ATOM 1807 CB ILE A1027 -7.199 -27.285 69.303 1.00 82.28 C ANISOU 1807 CB ILE A1027 11473 11985 7805 638 -1056 -285 C ATOM 1808 CG1 ILE A1027 -7.551 -27.305 67.798 1.00 83.66 C ANISOU 1808 CG1 ILE A1027 11726 12231 7831 677 -1021 -370 C ATOM 1809 CG2 ILE A1027 -7.976 -28.347 70.109 1.00 83.21 C ANISOU 1809 CG2 ILE A1027 11703 11912 8002 600 -1157 -308 C ATOM 1810 CD1 ILE A1027 -6.744 -28.244 66.974 1.00 90.97 C ANISOU 1810 CD1 ILE A1027 12702 13162 8700 839 -967 -494 C ATOM 1811 N GLY A1028 -9.505 -25.051 69.079 1.00 79.30 N ANISOU 1811 N GLY A1028 11087 11704 7339 383 -1103 -143 N ATOM 1812 CA GLY A1028 -10.896 -24.607 69.125 1.00 79.08 C ANISOU 1812 CA GLY A1028 11080 11676 7289 295 -1179 -123 C ATOM 1813 C GLY A1028 -11.072 -23.349 69.951 1.00 83.30 C ANISOU 1813 C GLY A1028 11540 12225 7883 218 -1148 2 C ATOM 1814 O GLY A1028 -10.276 -22.410 69.825 1.00 83.19 O ANISOU 1814 O GLY A1028 11479 12261 7869 232 -1043 74 O ATOM 1815 N ILE A1029 -12.101 -23.329 70.822 1.00 79.43 N ANISOU 1815 N ILE A1029 11039 11683 7457 127 -1223 16 N ATOM 1816 CA ILE A1029 -12.338 -22.194 71.720 1.00 78.45 C ANISOU 1816 CA ILE A1029 10857 11561 7391 64 -1198 110 C ATOM 1817 C ILE A1029 -11.767 -22.535 73.113 1.00 82.29 C ANISOU 1817 C ILE A1029 11309 11985 7974 27 -1207 123 C ATOM 1818 O ILE A1029 -12.463 -23.094 73.976 1.00 81.53 O ANISOU 1818 O ILE A1029 11235 11827 7917 -24 -1258 123 O ATOM 1819 CB ILE A1029 -13.807 -21.656 71.723 1.00 81.36 C ANISOU 1819 CB ILE A1029 11217 11956 7740 24 -1252 127 C ATOM 1820 CG1 ILE A1029 -14.268 -21.264 70.294 1.00 82.47 C ANISOU 1820 CG1 ILE A1029 11394 12197 7744 114 -1263 120 C ATOM 1821 CG2 ILE A1029 -13.959 -20.464 72.697 1.00 81.58 C ANISOU 1821 CG2 ILE A1029 11198 11967 7830 -22 -1209 210 C ATOM 1822 CD1 ILE A1029 -15.773 -20.995 70.125 1.00 88.83 C ANISOU 1822 CD1 ILE A1029 12165 13071 8514 115 -1356 98 C ATOM 1823 N GLY A1030 -10.474 -22.249 73.263 1.00 79.28 N ANISOU 1823 N GLY A1030 10870 11635 7618 63 -1151 129 N ATOM 1824 CA GLY A1030 -9.702 -22.468 74.481 1.00 79.22 C ANISOU 1824 CA GLY A1030 10808 11623 7670 72 -1177 125 C ATOM 1825 C GLY A1030 -9.659 -23.884 75.025 1.00 83.88 C ANISOU 1825 C GLY A1030 11469 12142 8262 136 -1242 110 C ATOM 1826 O GLY A1030 -9.481 -24.062 76.233 1.00 84.68 O ANISOU 1826 O GLY A1030 11564 12234 8376 153 -1283 138 O ATOM 1827 N HIS A1031 -9.791 -24.902 74.157 1.00 80.17 N ANISOU 1827 N HIS A1031 11081 11612 7769 186 -1246 63 N ATOM 1828 CA HIS A1031 -9.747 -26.293 74.603 1.00 80.70 C ANISOU 1828 CA HIS A1031 11249 11554 7858 251 -1281 52 C ATOM 1829 C HIS A1031 -8.312 -26.766 74.773 1.00 83.83 C ANISOU 1829 C HIS A1031 11608 11985 8258 410 -1279 36 C ATOM 1830 O HIS A1031 -7.625 -27.023 73.782 1.00 84.45 O ANISOU 1830 O HIS A1031 11668 12101 8320 492 -1240 -32 O ATOM 1831 CB HIS A1031 -10.533 -27.225 73.662 1.00 82.53 C ANISOU 1831 CB HIS A1031 11590 11680 8088 224 -1288 -28 C ATOM 1832 CG HIS A1031 -10.545 -28.655 74.105 1.00 87.28 C ANISOU 1832 CG HIS A1031 12325 12094 8744 271 -1294 -38 C ATOM 1833 ND1 HIS A1031 -11.558 -29.153 74.907 1.00 89.30 N ANISOU 1833 ND1 HIS A1031 12661 12210 9059 164 -1290 9 N ATOM 1834 CD2 HIS A1031 -9.660 -29.648 73.849 1.00 90.50 C ANISOU 1834 CD2 HIS A1031 12807 12418 9160 420 -1281 -82 C ATOM 1835 CE1 HIS A1031 -11.260 -30.426 75.110 1.00 90.39 C ANISOU 1835 CE1 HIS A1031 12941 12160 9244 241 -1267 6 C ATOM 1836 NE2 HIS A1031 -10.122 -30.767 74.503 1.00 91.45 N ANISOU 1836 NE2 HIS A1031 13079 12318 9348 410 -1271 -50 N ATOM 1837 N LEU A1032 -7.867 -26.894 76.032 1.00 79.34 N ANISOU 1837 N LEU A1032 11023 11427 7695 473 -1322 92 N ATOM 1838 CA LEU A1032 -6.526 -27.370 76.376 1.00 79.82 C ANISOU 1838 CA LEU A1032 11025 11553 7752 660 -1351 75 C ATOM 1839 C LEU A1032 -6.432 -28.853 76.026 1.00 84.05 C ANISOU 1839 C LEU A1032 11719 11921 8295 799 -1343 63 C ATOM 1840 O LEU A1032 -7.366 -29.617 76.308 1.00 84.13 O ANISOU 1840 O LEU A1032 11904 11742 8321 752 -1337 111 O ATOM 1841 CB LEU A1032 -6.266 -27.166 77.882 1.00 80.14 C ANISOU 1841 CB LEU A1032 11032 11660 7759 714 -1427 137 C ATOM 1842 CG LEU A1032 -4.813 -27.127 78.349 1.00 85.99 C ANISOU 1842 CG LEU A1032 11613 12574 8486 890 -1491 88 C ATOM 1843 CD1 LEU A1032 -4.652 -26.165 79.498 1.00 86.30 C ANISOU 1843 CD1 LEU A1032 11532 12767 8490 846 -1564 79 C ATOM 1844 CD2 LEU A1032 -4.332 -28.497 78.777 1.00 90.12 C ANISOU 1844 CD2 LEU A1032 12257 13015 8968 1137 -1537 139 C ATOM 1845 N LEU A1033 -5.315 -29.252 75.399 1.00 80.28 N ANISOU 1845 N LEU A1033 11178 11503 7821 962 -1325 -8 N ATOM 1846 CA LEU A1033 -5.081 -30.644 75.022 1.00 80.79 C ANISOU 1846 CA LEU A1033 11397 11400 7900 1128 -1309 -40 C ATOM 1847 C LEU A1033 -4.197 -31.337 76.054 1.00 83.82 C ANISOU 1847 C LEU A1033 11798 11780 8270 1373 -1368 25 C ATOM 1848 O LEU A1033 -4.596 -32.356 76.616 1.00 84.37 O ANISOU 1848 O LEU A1033 12080 11632 8345 1454 -1372 106 O ATOM 1849 CB LEU A1033 -4.481 -30.752 73.608 1.00 81.43 C ANISOU 1849 CB LEU A1033 11423 11542 7974 1191 -1240 -169 C ATOM 1850 CG LEU A1033 -5.408 -30.408 72.448 1.00 85.10 C ANISOU 1850 CG LEU A1033 11938 11986 8409 1018 -1192 -238 C ATOM 1851 CD1 LEU A1033 -4.615 -30.182 71.184 1.00 86.21 C ANISOU 1851 CD1 LEU A1033 11988 12269 8498 1097 -1108 -338 C ATOM 1852 CD2 LEU A1033 -6.457 -31.483 72.235 1.00 88.01 C ANISOU 1852 CD2 LEU A1033 12527 12106 8806 965 -1206 -283 C ATOM 1853 N THR A1034 -3.012 -30.767 76.316 1.00 79.42 N ANISOU 1853 N THR A1034 11012 11465 7697 1492 -1411 -10 N ATOM 1854 CA THR A1034 -2.055 -31.280 77.290 1.00 80.72 C ANISOU 1854 CA THR A1034 11137 11708 7825 1761 -1501 31 C ATOM 1855 C THR A1034 -1.182 -30.168 77.876 1.00 82.71 C ANISOU 1855 C THR A1034 11088 12275 8065 1758 -1579 -24 C ATOM 1856 O THR A1034 -0.815 -29.218 77.170 1.00 81.39 O ANISOU 1856 O THR A1034 10708 12261 7954 1613 -1520 -125 O ATOM 1857 CB THR A1034 -1.244 -32.473 76.721 1.00 93.27 C ANISOU 1857 CB THR A1034 12790 13215 9435 2042 -1473 -17 C ATOM 1858 OG1 THR A1034 -0.572 -33.135 77.791 1.00 97.62 O ANISOU 1858 OG1 THR A1034 13374 13789 9930 2340 -1572 65 O ATOM 1859 CG2 THR A1034 -0.239 -32.069 75.641 1.00 91.62 C ANISOU 1859 CG2 THR A1034 12336 13209 9265 2082 -1411 -168 C ATOM 1860 N LYS A1035 -0.846 -30.296 79.171 1.00 78.90 N ANISOU 1860 N LYS A1035 10592 11883 7502 1919 -1706 37 N ATOM 1861 CA LYS A1035 0.050 -29.355 79.840 1.00 78.68 C ANISOU 1861 CA LYS A1035 10265 12171 7460 1937 -1814 -58 C ATOM 1862 C LYS A1035 1.518 -29.798 79.640 1.00 84.27 C ANISOU 1862 C LYS A1035 10750 13078 8193 2218 -1866 -162 C ATOM 1863 O LYS A1035 2.449 -29.071 79.993 1.00 84.92 O ANISOU 1863 O LYS A1035 10515 13453 8299 2233 -1949 -293 O ATOM 1864 CB LYS A1035 -0.336 -29.151 81.312 1.00 80.81 C ANISOU 1864 CB LYS A1035 10609 12493 7601 1971 -1940 27 C ATOM 1865 CG LYS A1035 -1.225 -27.928 81.521 1.00 84.95 C ANISOU 1865 CG LYS A1035 11109 13025 8141 1650 -1907 10 C ATOM 1866 CD LYS A1035 -1.861 -27.913 82.904 1.00 92.20 C ANISOU 1866 CD LYS A1035 12180 13943 8910 1688 -1992 115 C ATOM 1867 CE LYS A1035 -2.178 -26.526 83.411 1.00101.49 C ANISOU 1867 CE LYS A1035 13220 15256 10086 1461 -2020 23 C ATOM 1868 NZ LYS A1035 -3.388 -25.951 82.769 1.00112.64 N ANISOU 1868 NZ LYS A1035 14732 16484 11583 1173 -1878 60 N ATOM 1869 N SER A1036 1.700 -30.977 79.000 1.00 81.20 N ANISOU 1869 N SER A1036 10512 12524 7814 2426 -1806 -129 N ATOM 1870 CA SER A1036 2.977 -31.583 78.624 1.00 83.23 C ANISOU 1870 CA SER A1036 10598 12924 8102 2726 -1822 -222 C ATOM 1871 C SER A1036 3.659 -30.702 77.554 1.00 85.63 C ANISOU 1871 C SER A1036 10580 13430 8527 2556 -1706 -393 C ATOM 1872 O SER A1036 2.952 -30.020 76.804 1.00 83.20 O ANISOU 1872 O SER A1036 10318 13031 8264 2254 -1579 -397 O ATOM 1873 CB SER A1036 2.740 -32.981 78.065 1.00 87.75 C ANISOU 1873 CB SER A1036 11473 13196 8673 2931 -1743 -150 C ATOM 1874 OG SER A1036 1.857 -33.710 78.902 1.00 95.81 O ANISOU 1874 OG SER A1036 12839 13951 9612 2992 -1781 31 O ATOM 1875 N PRO A1037 5.010 -30.677 77.447 1.00 83.28 N ANISOU 1875 N PRO A1037 9951 13412 8281 2746 -1734 -529 N ATOM 1876 CA PRO A1037 5.639 -29.797 76.450 1.00 82.80 C ANISOU 1876 CA PRO A1037 9583 13532 8344 2553 -1578 -676 C ATOM 1877 C PRO A1037 5.841 -30.426 75.069 1.00 87.20 C ANISOU 1877 C PRO A1037 10209 13992 8931 2636 -1390 -710 C ATOM 1878 O PRO A1037 6.661 -29.924 74.295 1.00 88.90 O ANISOU 1878 O PRO A1037 10141 14404 9234 2581 -1251 -831 O ATOM 1879 CB PRO A1037 6.961 -29.415 77.115 1.00 87.13 C ANISOU 1879 CB PRO A1037 9702 14456 8947 2689 -1700 -828 C ATOM 1880 CG PRO A1037 7.274 -30.558 78.021 1.00 93.93 C ANISOU 1880 CG PRO A1037 10669 15329 9691 3108 -1896 -766 C ATOM 1881 CD PRO A1037 6.032 -31.387 78.238 1.00 87.79 C ANISOU 1881 CD PRO A1037 10389 14169 8800 3146 -1899 -557 C ATOM 1882 N SER A1038 5.079 -31.493 74.743 1.00 81.56 N ANISOU 1882 N SER A1038 9870 12973 8147 2750 -1368 -617 N ATOM 1883 CA SER A1038 5.190 -32.195 73.466 1.00 81.18 C ANISOU 1883 CA SER A1038 9931 12812 8102 2851 -1208 -674 C ATOM 1884 C SER A1038 3.990 -31.979 72.560 1.00 80.63 C ANISOU 1884 C SER A1038 10119 12520 7997 2578 -1089 -638 C ATOM 1885 O SER A1038 2.853 -32.192 72.984 1.00 77.88 O ANISOU 1885 O SER A1038 10042 11937 7611 2465 -1157 -536 O ATOM 1886 CB SER A1038 5.433 -33.684 73.698 1.00 87.09 C ANISOU 1886 CB SER A1038 10885 13391 8817 3238 -1272 -650 C ATOM 1887 OG SER A1038 5.340 -34.467 72.518 1.00 95.94 O ANISOU 1887 OG SER A1038 12185 14338 9931 3329 -1127 -720 O ATOM 1888 N LEU A1039 4.256 -31.563 71.302 1.00 77.24 N ANISOU 1888 N LEU A1039 9593 12183 7570 2487 -906 -724 N ATOM 1889 CA LEU A1039 3.247 -31.359 70.253 1.00 75.14 C ANISOU 1889 CA LEU A1039 9548 11768 7235 2282 -795 -714 C ATOM 1890 C LEU A1039 2.735 -32.722 69.762 1.00 80.26 C ANISOU 1890 C LEU A1039 10517 12149 7828 2452 -803 -755 C ATOM 1891 O LEU A1039 1.553 -32.849 69.435 1.00 78.41 O ANISOU 1891 O LEU A1039 10532 11715 7545 2291 -816 -734 O ATOM 1892 CB LEU A1039 3.830 -30.522 69.095 1.00 75.57 C ANISOU 1892 CB LEU A1039 9405 12029 7277 2183 -583 -779 C ATOM 1893 CG LEU A1039 3.016 -30.378 67.799 1.00 78.82 C ANISOU 1893 CG LEU A1039 10029 12352 7566 2060 -453 -786 C ATOM 1894 CD1 LEU A1039 1.746 -29.589 68.019 1.00 76.01 C ANISOU 1894 CD1 LEU A1039 9815 11885 7179 1782 -516 -677 C ATOM 1895 CD2 LEU A1039 3.835 -29.713 66.730 1.00 82.88 C ANISOU 1895 CD2 LEU A1039 10352 13087 8051 2042 -215 -832 C ATOM 1896 N ASN A1040 3.623 -33.742 69.754 1.00 79.69 N ANISOU 1896 N ASN A1040 10429 12073 7778 2780 -800 -828 N ATOM 1897 CA ASN A1040 3.296 -35.120 69.380 1.00 81.29 C ANISOU 1897 CA ASN A1040 10939 11989 7959 2976 -799 -887 C ATOM 1898 C ASN A1040 2.398 -35.763 70.456 1.00 84.73 C ANISOU 1898 C ASN A1040 11643 12124 8427 2958 -941 -763 C ATOM 1899 O ASN A1040 1.637 -36.682 70.146 1.00 84.95 O ANISOU 1899 O ASN A1040 11977 11842 8459 2961 -930 -797 O ATOM 1900 CB ASN A1040 4.565 -35.950 69.155 1.00 87.17 C ANISOU 1900 CB ASN A1040 11578 12816 8728 3362 -748 -991 C ATOM 1901 CG ASN A1040 5.576 -35.319 68.221 1.00123.54 C ANISOU 1901 CG ASN A1040 15874 17750 13317 3393 -580 -1104 C ATOM 1902 OD1 ASN A1040 5.274 -34.957 67.077 1.00121.51 O ANISOU 1902 OD1 ASN A1040 15662 17528 12977 3249 -435 -1172 O ATOM 1903 ND2 ASN A1040 6.811 -35.193 68.685 1.00119.67 N ANISOU 1903 ND2 ASN A1040 15054 17519 12895 3595 -589 -1129 N ATOM 1904 N ALA A1041 2.483 -35.271 71.710 1.00 80.71 N ANISOU 1904 N ALA A1041 11018 11709 7940 2929 -1061 -629 N ATOM 1905 CA ALA A1041 1.640 -35.725 72.820 1.00 80.33 C ANISOU 1905 CA ALA A1041 11209 11416 7898 2900 -1170 -480 C ATOM 1906 C ALA A1041 0.297 -34.992 72.766 1.00 82.04 C ANISOU 1906 C ALA A1041 11519 11550 8102 2515 -1168 -430 C ATOM 1907 O ALA A1041 -0.718 -35.542 73.199 1.00 81.65 O ANISOU 1907 O ALA A1041 11728 11225 8070 2426 -1192 -351 O ATOM 1908 CB ALA A1041 2.323 -35.458 74.150 1.00 81.72 C ANISOU 1908 CB ALA A1041 11216 11775 8060 3057 -1303 -374 C ATOM 1909 N ALA A1042 0.299 -33.750 72.229 1.00 76.62 N ANISOU 1909 N ALA A1042 10618 11100 7396 2296 -1123 -472 N ATOM 1910 CA ALA A1042 -0.894 -32.922 72.061 1.00 73.95 C ANISOU 1910 CA ALA A1042 10334 10727 7037 1968 -1117 -432 C ATOM 1911 C ALA A1042 -1.742 -33.473 70.917 1.00 79.63 C ANISOU 1911 C ALA A1042 11265 11262 7728 1885 -1054 -530 C ATOM 1912 O ALA A1042 -2.971 -33.504 71.026 1.00 78.02 O ANISOU 1912 O ALA A1042 11217 10897 7530 1689 -1088 -500 O ATOM 1913 CB ALA A1042 -0.498 -31.483 71.783 1.00 73.24 C ANISOU 1913 CB ALA A1042 9973 10918 6937 1810 -1067 -442 C ATOM 1914 N LYS A1043 -1.076 -33.939 69.834 1.00 79.23 N ANISOU 1914 N LYS A1043 11208 11252 7643 2044 -964 -668 N ATOM 1915 CA LYS A1043 -1.718 -34.538 68.661 1.00 80.16 C ANISOU 1915 CA LYS A1043 11519 11229 7708 2010 -914 -813 C ATOM 1916 C LYS A1043 -2.360 -35.885 69.006 1.00 87.40 C ANISOU 1916 C LYS A1043 12721 11785 8702 2059 -961 -846 C ATOM 1917 O LYS A1043 -3.448 -36.177 68.511 1.00 86.88 O ANISOU 1917 O LYS A1043 12818 11559 8633 1888 -975 -933 O ATOM 1918 CB LYS A1043 -0.730 -34.676 67.495 1.00 83.82 C ANISOU 1918 CB LYS A1043 11899 11851 8096 2198 -791 -955 C ATOM 1919 CG LYS A1043 -0.437 -33.362 66.790 1.00 91.62 C ANISOU 1919 CG LYS A1043 12679 13139 8993 2079 -691 -936 C ATOM 1920 CD LYS A1043 0.305 -33.574 65.489 1.00102.45 C ANISOU 1920 CD LYS A1043 14022 14648 10257 2243 -538 -1079 C ATOM 1921 CE LYS A1043 0.593 -32.263 64.808 1.00114.08 C ANISOU 1921 CE LYS A1043 15316 16393 11637 2122 -400 -1023 C ATOM 1922 NZ LYS A1043 1.041 -32.460 63.406 1.00130.48 N ANISOU 1922 NZ LYS A1043 17426 18594 13555 2260 -233 -1153 N ATOM 1923 N SER A1044 -1.702 -36.683 69.880 1.00 86.99 N ANISOU 1923 N SER A1044 12723 11604 8724 2292 -983 -774 N ATOM 1924 CA SER A1044 -2.203 -37.977 70.359 1.00 89.38 C ANISOU 1924 CA SER A1044 13321 11519 9120 2361 -993 -760 C ATOM 1925 C SER A1044 -3.458 -37.795 71.225 1.00 93.50 C ANISOU 1925 C SER A1044 13950 11882 9693 2091 -1044 -626 C ATOM 1926 O SER A1044 -4.363 -38.631 71.171 1.00 94.11 O ANISOU 1926 O SER A1044 14265 11639 9855 1978 -1019 -673 O ATOM 1927 CB SER A1044 -1.125 -38.715 71.145 1.00 95.29 C ANISOU 1927 CB SER A1044 14093 12208 9904 2719 -1003 -672 C ATOM 1928 OG SER A1044 -0.006 -39.001 70.324 1.00106.09 O ANISOU 1928 OG SER A1044 15360 13708 11241 2986 -941 -815 O ATOM 1929 N GLU A1045 -3.511 -36.693 72.008 1.00 89.09 N ANISOU 1929 N GLU A1045 13208 11549 9095 1976 -1101 -477 N ATOM 1930 CA GLU A1045 -4.654 -36.346 72.856 1.00 87.88 C ANISOU 1930 CA GLU A1045 13115 11306 8971 1730 -1137 -348 C ATOM 1931 C GLU A1045 -5.812 -35.790 72.033 1.00 91.44 C ANISOU 1931 C GLU A1045 13545 11786 9413 1427 -1134 -453 C ATOM 1932 O GLU A1045 -6.969 -35.969 72.415 1.00 90.74 O ANISOU 1932 O GLU A1045 13565 11526 9387 1222 -1136 -419 O ATOM 1933 CB GLU A1045 -4.255 -35.373 73.980 1.00 87.78 C ANISOU 1933 CB GLU A1045 12918 11529 8904 1744 -1203 -183 C ATOM 1934 CG GLU A1045 -3.672 -36.059 75.208 1.00 99.97 C ANISOU 1934 CG GLU A1045 14559 12980 10443 1998 -1238 -31 C ATOM 1935 CD GLU A1045 -4.556 -37.093 75.885 1.00119.90 C ANISOU 1935 CD GLU A1045 17396 15132 13029 1967 -1188 87 C ATOM 1936 OE1 GLU A1045 -5.709 -36.756 76.239 1.00113.78 O ANISOU 1936 OE1 GLU A1045 16668 14287 12276 1697 -1169 146 O ATOM 1937 OE2 GLU A1045 -4.090 -38.243 76.064 1.00112.90 O ANISOU 1937 OE2 GLU A1045 16707 14015 12175 2220 -1152 125 O ATOM 1938 N LEU A1046 -5.502 -35.125 70.904 1.00 88.63 N ANISOU 1938 N LEU A1046 13047 11657 8973 1414 -1121 -577 N ATOM 1939 CA LEU A1046 -6.500 -34.575 69.984 1.00 88.12 C ANISOU 1939 CA LEU A1046 12961 11664 8856 1193 -1133 -682 C ATOM 1940 C LEU A1046 -7.181 -35.726 69.232 1.00 95.83 C ANISOU 1940 C LEU A1046 14139 12392 9878 1152 -1127 -875 C ATOM 1941 O LEU A1046 -8.413 -35.781 69.199 1.00 95.24 O ANISOU 1941 O LEU A1046 14116 12220 9850 928 -1165 -926 O ATOM 1942 CB LEU A1046 -5.852 -33.561 69.013 1.00 87.34 C ANISOU 1942 CB LEU A1046 12685 11874 8627 1235 -1095 -726 C ATOM 1943 CG LEU A1046 -6.762 -32.835 68.010 1.00 90.95 C ANISOU 1943 CG LEU A1046 13120 12460 8979 1069 -1111 -804 C ATOM 1944 CD1 LEU A1046 -7.780 -31.941 68.707 1.00 88.97 C ANISOU 1944 CD1 LEU A1046 12805 12244 8755 854 -1170 -679 C ATOM 1945 CD2 LEU A1046 -5.945 -31.997 67.061 1.00 93.31 C ANISOU 1945 CD2 LEU A1046 13293 13022 9141 1160 -1026 -816 C ATOM 1946 N ASP A1047 -6.374 -36.667 68.682 1.00 95.69 N ANISOU 1946 N ASP A1047 14226 12268 9863 1371 -1077 -1000 N ATOM 1947 CA ASP A1047 -6.838 -37.857 67.964 1.00 98.21 C ANISOU 1947 CA ASP A1047 14753 12321 10239 1362 -1062 -1223 C ATOM 1948 C ASP A1047 -7.684 -38.754 68.870 1.00102.46 C ANISOU 1948 C ASP A1047 15482 12486 10964 1226 -1053 -1172 C ATOM 1949 O ASP A1047 -8.672 -39.313 68.403 1.00103.37 O ANISOU 1949 O ASP A1047 15704 12417 11155 1036 -1064 -1351 O ATOM 1950 CB ASP A1047 -5.649 -38.644 67.383 1.00102.84 C ANISOU 1950 CB ASP A1047 15414 12862 10800 1671 -992 -1340 C ATOM 1951 CG ASP A1047 -4.885 -37.943 66.269 1.00115.53 C ANISOU 1951 CG ASP A1047 16863 14811 12224 1793 -956 -1434 C ATOM 1952 OD1 ASP A1047 -5.481 -37.075 65.591 1.00115.02 O ANISOU 1952 OD1 ASP A1047 16706 14960 12036 1631 -989 -1476 O ATOM 1953 OD2 ASP A1047 -3.698 -38.283 66.056 1.00123.52 O ANISOU 1953 OD2 ASP A1047 17847 15875 13211 2067 -883 -1462 O ATOM 1954 N LYS A1048 -7.307 -38.866 70.166 1.00 98.21 N ANISOU 1954 N LYS A1048 14976 11848 10490 1318 -1027 -931 N ATOM 1955 CA LYS A1048 -8.020 -39.649 71.181 1.00 99.00 C ANISOU 1955 CA LYS A1048 15271 11597 10746 1212 -978 -814 C ATOM 1956 C LYS A1048 -9.403 -39.050 71.474 1.00100.40 C ANISOU 1956 C LYS A1048 15371 11812 10966 863 -1005 -786 C ATOM 1957 O LYS A1048 -10.382 -39.796 71.547 1.00101.54 O ANISOU 1957 O LYS A1048 15655 11665 11261 659 -954 -860 O ATOM 1958 CB LYS A1048 -7.199 -39.736 72.483 1.00101.84 C ANISOU 1958 CB LYS A1048 15668 11931 11094 1446 -958 -542 C ATOM 1959 CG LYS A1048 -6.429 -41.040 72.654 1.00121.62 C ANISOU 1959 CG LYS A1048 18415 14124 13672 1744 -886 -528 C ATOM 1960 CD LYS A1048 -5.664 -41.065 73.977 1.00132.31 C ANISOU 1960 CD LYS A1048 19795 15502 14973 2006 -895 -250 C ATOM 1961 CE LYS A1048 -5.106 -42.428 74.323 1.00145.60 C ANISOU 1961 CE LYS A1048 21772 16816 16734 2312 -813 -184 C ATOM 1962 NZ LYS A1048 -6.122 -43.304 74.969 1.00155.39 N ANISOU 1962 NZ LYS A1048 23321 17600 18121 2147 -688 -70 N ATOM 1963 N ALA A1049 -9.475 -37.708 71.634 1.00 93.39 N ANISOU 1963 N ALA A1049 14253 11272 9961 793 -1074 -690 N ATOM 1964 CA ALA A1049 -10.703 -36.960 71.930 1.00 91.21 C ANISOU 1964 CA ALA A1049 13866 11088 9702 509 -1105 -652 C ATOM 1965 C ALA A1049 -11.709 -36.984 70.780 1.00 95.32 C ANISOU 1965 C ALA A1049 14342 11636 10238 303 -1156 -907 C ATOM 1966 O ALA A1049 -12.899 -37.192 71.025 1.00 95.51 O ANISOU 1966 O ALA A1049 14370 11539 10379 57 -1146 -948 O ATOM 1967 CB ALA A1049 -10.368 -35.524 72.303 1.00 88.99 C ANISOU 1967 CB ALA A1049 13370 11152 9291 535 -1159 -506 C ATOM 1968 N ILE A1050 -11.230 -36.774 69.533 1.00 91.52 N ANISOU 1968 N ILE A1050 13809 11336 9629 413 -1206 -1083 N ATOM 1969 CA ILE A1050 -12.052 -36.767 68.320 1.00 91.82 C ANISOU 1969 CA ILE A1050 13807 11463 9619 280 -1283 -1346 C ATOM 1970 C ILE A1050 -12.377 -38.198 67.875 1.00 99.22 C ANISOU 1970 C ILE A1050 14933 12069 10698 223 -1256 -1593 C ATOM 1971 O ILE A1050 -13.549 -38.575 67.862 1.00100.49 O ANISOU 1971 O ILE A1050 15092 12100 10989 -30 -1281 -1730 O ATOM 1972 CB ILE A1050 -11.420 -35.892 67.185 1.00 93.62 C ANISOU 1972 CB ILE A1050 13923 12036 9612 437 -1329 -1409 C ATOM 1973 CG1 ILE A1050 -11.140 -34.420 67.630 1.00 90.74 C ANISOU 1973 CG1 ILE A1050 13380 11955 9143 459 -1332 -1171 C ATOM 1974 CG2 ILE A1050 -12.210 -35.965 65.866 1.00 95.49 C ANISOU 1974 CG2 ILE A1050 14146 12389 9745 358 -1426 -1694 C ATOM 1975 CD1 ILE A1050 -12.339 -33.569 68.187 1.00 94.21 C ANISOU 1975 CD1 ILE A1050 13696 12485 9614 244 -1390 -1076 C ATOM 1976 N GLY A1051 -11.345 -38.967 67.523 1.00 97.22 N ANISOU 1976 N GLY A1051 14827 11678 10432 453 -1200 -1662 N ATOM 1977 CA GLY A1051 -11.478 -40.344 67.054 1.00100.47 C ANISOU 1977 CA GLY A1051 15451 11744 10979 441 -1158 -1913 C ATOM 1978 C GLY A1051 -10.584 -40.673 65.870 1.00105.36 C ANISOU 1978 C GLY A1051 16132 12446 11454 685 -1164 -2129 C ATOM 1979 O GLY A1051 -9.972 -41.745 65.837 1.00107.71 O ANISOU 1979 O GLY A1051 16631 12451 11845 846 -1081 -2211 O ATOM 1980 N ARG A1052 -10.504 -39.749 64.891 1.00 99.83 N ANISOU 1980 N ARG A1052 15275 12140 10515 734 -1245 -2212 N ATOM 1981 CA ARG A1052 -9.698 -39.881 63.671 1.00100.70 C ANISOU 1981 CA ARG A1052 15422 12407 10433 968 -1235 -2409 C ATOM 1982 C ARG A1052 -8.286 -39.270 63.798 1.00103.99 C ANISOU 1982 C ARG A1052 15751 13038 10724 1250 -1147 -2193 C ATOM 1983 O ARG A1052 -8.028 -38.500 64.727 1.00101.09 O ANISOU 1983 O ARG A1052 15256 12770 10384 1237 -1131 -1908 O ATOM 1984 CB ARG A1052 -10.448 -39.273 62.465 1.00 99.08 C ANISOU 1984 CB ARG A1052 15119 12514 10012 877 -1358 -2625 C ATOM 1985 CG ARG A1052 -10.732 -37.774 62.575 1.00 99.78 C ANISOU 1985 CG ARG A1052 14996 12966 9950 818 -1410 -2400 C ATOM 1986 CD ARG A1052 -11.155 -37.178 61.251 1.00102.93 C ANISOU 1986 CD ARG A1052 15337 13702 10069 849 -1509 -2579 C ATOM 1987 NE ARG A1052 -11.278 -35.721 61.325 1.00105.85 N ANISOU 1987 NE ARG A1052 15540 14387 10290 843 -1525 -2332 N ATOM 1988 CZ ARG A1052 -10.290 -34.870 61.063 1.00118.65 C ANISOU 1988 CZ ARG A1052 17109 16229 11744 1026 -1418 -2145 C ATOM 1989 NH1 ARG A1052 -9.095 -35.319 60.704 1.00107.43 N ANISOU 1989 NH1 ARG A1052 15758 14789 10272 1239 -1293 -2180 N ATOM 1990 NH2 ARG A1052 -10.491 -33.562 61.159 1.00102.48 N ANISOU 1990 NH2 ARG A1052 14933 14412 9592 996 -1421 -1927 N ATOM 1991 N ASN A1053 -7.381 -39.608 62.854 1.00103.25 N ANISOU 1991 N ASN A1053 15710 13026 10494 1497 -1086 -2352 N ATOM 1992 CA ASN A1053 -6.023 -39.058 62.809 1.00102.80 C ANISOU 1992 CA ASN A1053 15533 13203 10323 1755 -983 -2197 C ATOM 1993 C ASN A1053 -6.110 -37.686 62.132 1.00104.42 C ANISOU 1993 C ASN A1053 15558 13821 10297 1705 -994 -2125 C ATOM 1994 O ASN A1053 -6.314 -37.588 60.920 1.00105.19 O ANISOU 1994 O ASN A1053 15690 14090 10188 1742 -1006 -2319 O ATOM 1995 CB ASN A1053 -5.058 -40.001 62.075 1.00110.07 C ANISOU 1995 CB ASN A1053 16578 14044 11200 2046 -887 -2400 C ATOM 1996 CG ASN A1053 -3.624 -39.520 62.053 1.00139.66 C ANISOU 1996 CG ASN A1053 20165 18037 14861 2313 -764 -2260 C ATOM 1997 OD1 ASN A1053 -2.938 -39.469 63.084 1.00136.07 O ANISOU 1997 OD1 ASN A1053 19624 17541 14534 2410 -735 -2048 O ATOM 1998 ND2 ASN A1053 -3.135 -39.182 60.866 1.00130.89 N ANISOU 1998 ND2 ASN A1053 19006 17202 13526 2446 -686 -2388 N ATOM 1999 N THR A1054 -5.991 -36.634 62.942 1.00 98.29 N ANISOU 1999 N THR A1054 14609 13186 9549 1625 -989 -1847 N ATOM 2000 CA THR A1054 -6.151 -35.237 62.542 1.00 96.36 C ANISOU 2000 CA THR A1054 14209 13268 9134 1550 -984 -1722 C ATOM 2001 C THR A1054 -4.884 -34.519 62.073 1.00100.36 C ANISOU 2001 C THR A1054 14582 14039 9509 1732 -829 -1626 C ATOM 2002 O THR A1054 -4.985 -33.621 61.229 1.00 99.55 O ANISOU 2002 O THR A1054 14432 14186 9206 1723 -784 -1600 O ATOM 2003 CB THR A1054 -6.816 -34.456 63.683 1.00102.39 C ANISOU 2003 CB THR A1054 14869 14013 10020 1339 -1053 -1498 C ATOM 2004 OG1 THR A1054 -5.947 -34.465 64.816 1.00103.26 O ANISOU 2004 OG1 THR A1054 14904 14054 10276 1412 -1001 -1319 O ATOM 2005 CG2 THR A1054 -8.191 -35.010 64.060 1.00100.33 C ANISOU 2005 CG2 THR A1054 14704 13538 9881 1125 -1179 -1588 C ATOM 2006 N ASN A1055 -3.710 -34.872 62.653 1.00 97.64 N ANISOU 2006 N ASN A1055 14168 13650 9281 1898 -741 -1560 N ATOM 2007 CA ASN A1055 -2.397 -34.248 62.396 1.00 97.93 C ANISOU 2007 CA ASN A1055 14021 13933 9256 2053 -578 -1475 C ATOM 2008 C ASN A1055 -2.389 -32.759 62.816 1.00 99.05 C ANISOU 2008 C ASN A1055 13969 14270 9397 1888 -545 -1246 C ATOM 2009 O ASN A1055 -1.708 -31.930 62.200 1.00 98.81 O ANISOU 2009 O ASN A1055 13811 14472 9260 1927 -390 -1186 O ATOM 2010 CB ASN A1055 -1.907 -34.456 60.939 1.00101.85 C ANISOU 2010 CB ASN A1055 14572 14592 9534 2233 -446 -1650 C ATOM 2011 CG ASN A1055 -1.850 -35.892 60.466 1.00129.11 C ANISOU 2011 CG ASN A1055 18222 17848 12985 2410 -465 -1911 C ATOM 2012 OD1 ASN A1055 -1.792 -36.847 61.252 1.00126.76 O ANISOU 2012 OD1 ASN A1055 18005 17277 12880 2464 -529 -1943 O ATOM 2013 ND2 ASN A1055 -1.838 -36.073 59.155 1.00120.89 N ANISOU 2013 ND2 ASN A1055 17281 16936 11714 2522 -397 -2102 N ATOM 2014 N GLY A1056 -3.154 -32.458 63.868 1.00 93.24 N ANISOU 2014 N GLY A1056 13223 13416 8787 1704 -673 -1124 N ATOM 2015 CA GLY A1056 -3.287 -31.124 64.440 1.00 90.76 C ANISOU 2015 CA GLY A1056 12755 13226 8503 1536 -665 -928 C ATOM 2016 C GLY A1056 -4.332 -30.219 63.817 1.00 93.33 C ANISOU 2016 C GLY A1056 13130 13641 8690 1385 -687 -885 C ATOM 2017 O GLY A1056 -4.431 -29.053 64.205 1.00 90.61 O ANISOU 2017 O GLY A1056 12677 13382 8369 1261 -659 -724 O ATOM 2018 N VAL A1057 -5.111 -30.739 62.845 1.00 91.87 N ANISOU 2018 N VAL A1057 13108 13441 8358 1408 -745 -1042 N ATOM 2019 CA VAL A1057 -6.152 -29.982 62.134 1.00 91.56 C ANISOU 2019 CA VAL A1057 13121 13519 8147 1319 -796 -1026 C ATOM 2020 C VAL A1057 -7.520 -30.628 62.356 1.00 95.61 C ANISOU 2020 C VAL A1057 13735 13883 8710 1194 -993 -1153 C ATOM 2021 O VAL A1057 -7.697 -31.814 62.077 1.00 96.77 O ANISOU 2021 O VAL A1057 13996 13894 8877 1237 -1053 -1363 O ATOM 2022 CB VAL A1057 -5.823 -29.796 60.622 1.00 97.74 C ANISOU 2022 CB VAL A1057 13975 14512 8651 1478 -681 -1103 C ATOM 2023 CG1 VAL A1057 -6.962 -29.099 59.880 1.00 97.82 C ANISOU 2023 CG1 VAL A1057 14061 14657 8450 1436 -766 -1090 C ATOM 2024 CG2 VAL A1057 -4.516 -29.031 60.423 1.00 97.99 C ANISOU 2024 CG2 VAL A1057 13882 14695 8657 1561 -443 -955 C ATOM 2025 N ILE A1058 -8.485 -29.838 62.846 1.00 91.08 N ANISOU 2025 N ILE A1058 13109 13326 8169 1035 -1079 -1038 N ATOM 2026 CA ILE A1058 -9.853 -30.299 63.105 1.00 91.15 C ANISOU 2026 CA ILE A1058 13160 13227 8246 888 -1250 -1148 C ATOM 2027 C ILE A1058 -10.907 -29.422 62.412 1.00 95.51 C ANISOU 2027 C ILE A1058 13693 13974 8621 854 -1337 -1143 C ATOM 2028 O ILE A1058 -10.646 -28.250 62.131 1.00 94.59 O ANISOU 2028 O ILE A1058 13537 14021 8382 910 -1254 -968 O ATOM 2029 CB ILE A1058 -10.148 -30.468 64.626 1.00 92.69 C ANISOU 2029 CB ILE A1058 13304 13220 8694 734 -1286 -1037 C ATOM 2030 CG1 ILE A1058 -9.850 -29.189 65.429 1.00 90.84 C ANISOU 2030 CG1 ILE A1058 12944 13071 8501 688 -1224 -789 C ATOM 2031 CG2 ILE A1058 -9.437 -31.681 65.217 1.00 94.53 C ANISOU 2031 CG2 ILE A1058 13610 13225 9081 792 -1249 -1091 C ATOM 2032 CD1 ILE A1058 -11.038 -28.452 65.868 1.00 95.79 C ANISOU 2032 CD1 ILE A1058 13516 13727 9153 541 -1308 -715 C ATOM 2033 N THR A1059 -12.100 -29.989 62.159 1.00 93.19 N ANISOU 2033 N THR A1059 13424 13658 8327 764 -1501 -1337 N ATOM 2034 CA THR A1059 -13.214 -29.258 61.545 1.00 93.42 C ANISOU 2034 CA THR A1059 13411 13894 8190 756 -1626 -1361 C ATOM 2035 C THR A1059 -13.981 -28.490 62.634 1.00 95.09 C ANISOU 2035 C THR A1059 13501 14068 8562 602 -1663 -1186 C ATOM 2036 O THR A1059 -13.755 -28.731 63.822 1.00 93.39 O ANISOU 2036 O THR A1059 13251 13657 8574 485 -1611 -1093 O ATOM 2037 CB THR A1059 -14.104 -30.177 60.675 1.00103.00 C ANISOU 2037 CB THR A1059 14666 15156 9315 742 -1800 -1695 C ATOM 2038 OG1 THR A1059 -14.973 -30.965 61.491 1.00102.54 O ANISOU 2038 OG1 THR A1059 14550 14892 9519 518 -1894 -1822 O ATOM 2039 CG2 THR A1059 -13.305 -31.058 59.712 1.00103.65 C ANISOU 2039 CG2 THR A1059 14887 15238 9258 895 -1754 -1901 C ATOM 2040 N LYS A1060 -14.868 -27.561 62.231 1.00 91.48 N ANISOU 2040 N LYS A1060 12986 13807 7965 632 -1750 -1137 N ATOM 2041 CA LYS A1060 -15.655 -26.724 63.141 1.00 89.37 C ANISOU 2041 CA LYS A1060 12603 13535 7820 523 -1780 -982 C ATOM 2042 C LYS A1060 -16.596 -27.522 64.061 1.00 92.19 C ANISOU 2042 C LYS A1060 12869 13738 8421 306 -1873 -1106 C ATOM 2043 O LYS A1060 -16.705 -27.191 65.240 1.00 89.67 O ANISOU 2043 O LYS A1060 12488 13305 8278 195 -1816 -954 O ATOM 2044 CB LYS A1060 -16.414 -25.653 62.352 1.00 92.80 C ANISOU 2044 CB LYS A1060 13011 14221 8028 656 -1861 -925 C ATOM 2045 CG LYS A1060 -16.887 -24.493 63.202 1.00101.83 C ANISOU 2045 CG LYS A1060 14066 15359 9265 614 -1831 -707 C ATOM 2046 CD LYS A1060 -18.109 -23.860 62.595 1.00112.67 C ANISOU 2046 CD LYS A1060 15375 16957 10479 718 -1985 -739 C ATOM 2047 CE LYS A1060 -18.809 -23.007 63.608 1.00123.17 C ANISOU 2047 CE LYS A1060 16591 18249 11961 645 -1980 -592 C ATOM 2048 NZ LYS A1060 -19.800 -22.118 62.972 1.00134.72 N ANISOU 2048 NZ LYS A1060 18007 19940 13241 821 -2098 -559 N ATOM 2049 N ASP A1061 -17.262 -28.567 63.527 1.00 90.80 N ANISOU 2049 N ASP A1061 12689 13554 8256 239 -1999 -1388 N ATOM 2050 CA ASP A1061 -18.166 -29.435 64.292 1.00 90.91 C ANISOU 2050 CA ASP A1061 12621 13399 8522 3 -2054 -1528 C ATOM 2051 C ASP A1061 -17.386 -30.179 65.375 1.00 91.82 C ANISOU 2051 C ASP A1061 12828 13203 8857 -89 -1907 -1431 C ATOM 2052 O ASP A1061 -17.916 -30.409 66.464 1.00 90.99 O ANISOU 2052 O ASP A1061 12667 12944 8961 -262 -1871 -1371 O ATOM 2053 CB ASP A1061 -18.878 -30.440 63.366 1.00 96.17 C ANISOU 2053 CB ASP A1061 13273 14104 9162 -57 -2206 -1891 C ATOM 2054 CG ASP A1061 -19.953 -29.827 62.496 1.00109.68 C ANISOU 2054 CG ASP A1061 14845 16143 10685 9 -2399 -2025 C ATOM 2055 OD1 ASP A1061 -21.027 -29.483 63.034 1.00110.73 O ANISOU 2055 OD1 ASP A1061 14797 16340 10937 -116 -2467 -2020 O ATOM 2056 OD2 ASP A1061 -19.731 -29.713 61.273 1.00117.49 O ANISOU 2056 OD2 ASP A1061 15904 17341 11395 204 -2483 -2139 O ATOM 2057 N GLU A1062 -16.119 -30.533 65.071 1.00 86.72 N ANISOU 2057 N GLU A1062 12319 12482 8147 51 -1816 -1406 N ATOM 2058 CA GLU A1062 -15.203 -31.213 65.986 1.00 85.26 C ANISOU 2058 CA GLU A1062 12230 12040 8126 42 -1690 -1306 C ATOM 2059 C GLU A1062 -14.801 -30.256 67.119 1.00 85.62 C ANISOU 2059 C GLU A1062 12213 12096 8223 45 -1605 -1017 C ATOM 2060 O GLU A1062 -14.701 -30.682 68.270 1.00 84.50 O ANISOU 2060 O GLU A1062 12096 11763 8246 -33 -1545 -920 O ATOM 2061 CB GLU A1062 -13.979 -31.752 65.230 1.00 87.48 C ANISOU 2061 CB GLU A1062 12638 12298 8304 230 -1628 -1381 C ATOM 2062 CG GLU A1062 -14.331 -32.832 64.217 1.00 98.58 C ANISOU 2062 CG GLU A1062 14131 13652 9673 226 -1706 -1701 C ATOM 2063 CD GLU A1062 -13.208 -33.374 63.353 1.00112.32 C ANISOU 2063 CD GLU A1062 15999 15391 11285 433 -1642 -1811 C ATOM 2064 OE1 GLU A1062 -12.242 -32.627 63.077 1.00 90.58 O ANISOU 2064 OE1 GLU A1062 13232 12802 8384 604 -1552 -1656 O ATOM 2065 OE2 GLU A1062 -13.321 -34.540 62.907 1.00109.04 O ANISOU 2065 OE2 GLU A1062 15694 14812 10923 417 -1671 -2070 O ATOM 2066 N ALA A1063 -14.636 -28.953 66.790 1.00 80.34 N ANISOU 2066 N ALA A1063 11474 11646 7406 135 -1598 -887 N ATOM 2067 CA ALA A1063 -14.322 -27.875 67.734 1.00 77.51 C ANISOU 2067 CA ALA A1063 11048 11317 7086 129 -1527 -653 C ATOM 2068 C ALA A1063 -15.514 -27.609 68.650 1.00 79.42 C ANISOU 2068 C ALA A1063 11201 11529 7445 -29 -1572 -609 C ATOM 2069 O ALA A1063 -15.307 -27.258 69.812 1.00 78.19 O ANISOU 2069 O ALA A1063 11021 11304 7382 -73 -1511 -460 O ATOM 2070 CB ALA A1063 -13.945 -26.603 66.986 1.00 77.87 C ANISOU 2070 CB ALA A1063 11066 11563 6956 252 -1488 -550 C ATOM 2071 N GLU A1064 -16.755 -27.781 68.127 1.00 75.82 N ANISOU 2071 N GLU A1064 10682 11148 6977 -105 -1680 -757 N ATOM 2072 CA GLU A1064 -17.997 -27.631 68.888 1.00 75.10 C ANISOU 2072 CA GLU A1064 10473 11052 7009 -261 -1714 -753 C ATOM 2073 C GLU A1064 -18.067 -28.720 69.969 1.00 78.61 C ANISOU 2073 C GLU A1064 10966 11242 7659 -416 -1640 -754 C ATOM 2074 O GLU A1064 -18.406 -28.413 71.115 1.00 77.48 O ANISOU 2074 O GLU A1064 10779 11049 7610 -498 -1577 -619 O ATOM 2075 CB GLU A1064 -19.219 -27.714 67.967 1.00 78.39 C ANISOU 2075 CB GLU A1064 10781 11632 7372 -298 -1860 -958 C ATOM 2076 CG GLU A1064 -19.894 -26.381 67.704 1.00 89.81 C ANISOU 2076 CG GLU A1064 12111 13317 8697 -203 -1924 -875 C ATOM 2077 CD GLU A1064 -20.844 -26.390 66.522 1.00120.19 C ANISOU 2077 CD GLU A1064 15862 17393 12410 -146 -2099 -1081 C ATOM 2078 OE1 GLU A1064 -20.363 -26.421 65.364 1.00112.58 O ANISOU 2078 OE1 GLU A1064 14992 16542 11244 11 -2153 -1154 O ATOM 2079 OE2 GLU A1064 -22.075 -26.357 66.755 1.00120.83 O ANISOU 2079 OE2 GLU A1064 15766 17566 12580 -247 -2185 -1177 O ATOM 2080 N LYS A1065 -17.701 -29.978 69.612 1.00 75.58 N ANISOU 2080 N LYS A1065 10698 10686 7332 -437 -1631 -894 N ATOM 2081 CA LYS A1065 -17.687 -31.114 70.537 1.00 75.88 C ANISOU 2081 CA LYS A1065 10836 10435 7560 -556 -1537 -878 C ATOM 2082 C LYS A1065 -16.736 -30.842 71.706 1.00 77.81 C ANISOU 2082 C LYS A1065 11154 10600 7810 -464 -1434 -630 C ATOM 2083 O LYS A1065 -17.115 -31.048 72.862 1.00 77.37 O ANISOU 2083 O LYS A1065 11114 10421 7863 -563 -1355 -514 O ATOM 2084 CB LYS A1065 -17.312 -32.416 69.809 1.00 80.37 C ANISOU 2084 CB LYS A1065 11545 10820 8173 -546 -1540 -1077 C ATOM 2085 CG LYS A1065 -17.688 -33.681 70.585 1.00 96.65 C ANISOU 2085 CG LYS A1065 13716 12545 10464 -714 -1439 -1103 C ATOM 2086 CD LYS A1065 -17.293 -34.959 69.853 1.00107.45 C ANISOU 2086 CD LYS A1065 15246 13689 11891 -693 -1431 -1314 C ATOM 2087 CE LYS A1065 -15.983 -35.548 70.321 1.00111.78 C ANISOU 2087 CE LYS A1065 15996 14032 12443 -501 -1330 -1172 C ATOM 2088 NZ LYS A1065 -16.111 -36.222 71.642 1.00119.00 N ANISOU 2088 NZ LYS A1065 17035 14649 13530 -583 -1187 -993 N ATOM 2089 N LEU A1066 -15.527 -30.333 71.407 1.00 72.96 N ANISOU 2089 N LEU A1066 10568 10083 7070 -275 -1432 -557 N ATOM 2090 CA LEU A1066 -14.525 -29.997 72.421 1.00 71.35 C ANISOU 2090 CA LEU A1066 10394 9859 6857 -172 -1367 -365 C ATOM 2091 C LEU A1066 -15.017 -28.872 73.340 1.00 75.20 C ANISOU 2091 C LEU A1066 10775 10460 7339 -235 -1357 -224 C ATOM 2092 O LEU A1066 -14.777 -28.929 74.547 1.00 74.74 O ANISOU 2092 O LEU A1066 10752 10330 7315 -230 -1305 -93 O ATOM 2093 CB LEU A1066 -13.175 -29.625 71.777 1.00 70.40 C ANISOU 2093 CB LEU A1066 10273 9851 6625 15 -1362 -357 C ATOM 2094 CG LEU A1066 -12.458 -30.716 70.975 1.00 76.00 C ANISOU 2094 CG LEU A1066 11094 10457 7326 128 -1351 -488 C ATOM 2095 CD1 LEU A1066 -11.267 -30.151 70.252 1.00 75.60 C ANISOU 2095 CD1 LEU A1066 10996 10573 7157 295 -1324 -482 C ATOM 2096 CD2 LEU A1066 -12.030 -31.895 71.856 1.00 79.04 C ANISOU 2096 CD2 LEU A1066 11616 10592 7824 176 -1300 -441 C ATOM 2097 N PHE A1067 -15.742 -27.881 72.766 1.00 71.83 N ANISOU 2097 N PHE A1067 10230 10209 6852 -273 -1407 -256 N ATOM 2098 CA PHE A1067 -16.318 -26.734 73.475 1.00 70.71 C ANISOU 2098 CA PHE A1067 9988 10175 6704 -316 -1398 -151 C ATOM 2099 C PHE A1067 -17.431 -27.158 74.434 1.00 76.83 C ANISOU 2099 C PHE A1067 10737 10864 7592 -468 -1360 -134 C ATOM 2100 O PHE A1067 -17.467 -26.680 75.569 1.00 76.21 O ANISOU 2100 O PHE A1067 10647 10787 7522 -479 -1305 -11 O ATOM 2101 CB PHE A1067 -16.856 -25.690 72.478 1.00 71.94 C ANISOU 2101 CB PHE A1067 10050 10520 6765 -278 -1459 -192 C ATOM 2102 CG PHE A1067 -17.630 -24.559 73.117 1.00 72.02 C ANISOU 2102 CG PHE A1067 9961 10620 6783 -309 -1449 -107 C ATOM 2103 CD1 PHE A1067 -16.970 -23.452 73.642 1.00 73.26 C ANISOU 2103 CD1 PHE A1067 10116 10812 6907 -244 -1397 14 C ATOM 2104 CD2 PHE A1067 -19.016 -24.606 73.208 1.00 74.17 C ANISOU 2104 CD2 PHE A1067 10129 10941 7110 -405 -1486 -170 C ATOM 2105 CE1 PHE A1067 -17.683 -22.414 74.236 1.00 73.31 C ANISOU 2105 CE1 PHE A1067 10050 10879 6925 -258 -1380 74 C ATOM 2106 CE2 PHE A1067 -19.726 -23.571 73.808 1.00 76.17 C ANISOU 2106 CE2 PHE A1067 10288 11281 7371 -405 -1467 -99 C ATOM 2107 CZ PHE A1067 -19.055 -22.482 74.314 1.00 72.94 C ANISOU 2107 CZ PHE A1067 9911 10884 6919 -323 -1414 24 C ATOM 2108 N ASN A1068 -18.364 -28.003 73.959 1.00 75.43 N ANISOU 2108 N ASN A1068 10537 10623 7498 -593 -1383 -273 N ATOM 2109 CA ASN A1068 -19.484 -28.492 74.754 1.00 76.67 C ANISOU 2109 CA ASN A1068 10649 10692 7792 -773 -1316 -275 C ATOM 2110 C ASN A1068 -19.001 -29.312 75.946 1.00 82.83 C ANISOU 2110 C ASN A1068 11586 11251 8636 -790 -1189 -138 C ATOM 2111 O ASN A1068 -19.690 -29.360 76.963 1.00 83.45 O ANISOU 2111 O ASN A1068 11647 11284 8779 -894 -1089 -49 O ATOM 2112 CB ASN A1068 -20.457 -29.282 73.883 1.00 78.67 C ANISOU 2112 CB ASN A1068 10828 10920 8144 -921 -1370 -495 C ATOM 2113 CG ASN A1068 -21.311 -28.437 72.963 1.00 96.54 C ANISOU 2113 CG ASN A1068 12901 13444 10337 -905 -1501 -620 C ATOM 2114 OD1 ASN A1068 -21.382 -27.203 73.065 1.00 85.31 O ANISOU 2114 OD1 ASN A1068 11401 12199 8815 -799 -1527 -520 O ATOM 2115 ND2 ASN A1068 -22.014 -29.096 72.057 1.00 90.71 N ANISOU 2115 ND2 ASN A1068 12084 12731 9650 -1003 -1590 -853 N ATOM 2116 N GLN A1069 -17.806 -29.928 75.832 1.00 80.37 N ANISOU 2116 N GLN A1069 11429 10818 8289 -661 -1186 -109 N ATOM 2117 CA GLN A1069 -17.164 -30.683 76.906 1.00 81.37 C ANISOU 2117 CA GLN A1069 11728 10753 8436 -601 -1088 41 C ATOM 2118 C GLN A1069 -16.671 -29.684 77.957 1.00 84.95 C ANISOU 2118 C GLN A1069 12152 11350 8773 -492 -1082 206 C ATOM 2119 O GLN A1069 -16.851 -29.915 79.156 1.00 85.55 O ANISOU 2119 O GLN A1069 12307 11353 8847 -503 -989 345 O ATOM 2120 CB GLN A1069 -15.976 -31.495 76.364 1.00 83.38 C ANISOU 2120 CB GLN A1069 12124 10886 8672 -444 -1112 3 C ATOM 2121 CG GLN A1069 -16.364 -32.795 75.658 1.00102.18 C ANISOU 2121 CG GLN A1069 14607 13029 11186 -543 -1081 -150 C ATOM 2122 CD GLN A1069 -15.187 -33.531 75.051 1.00123.46 C ANISOU 2122 CD GLN A1069 17439 15616 13854 -358 -1102 -207 C ATOM 2123 OE1 GLN A1069 -15.333 -34.263 74.067 1.00120.96 O ANISOU 2123 OE1 GLN A1069 17169 15191 13599 -399 -1123 -400 O ATOM 2124 NE2 GLN A1069 -13.997 -33.389 75.627 1.00115.11 N ANISOU 2124 NE2 GLN A1069 16438 14593 12704 -140 -1101 -63 N ATOM 2125 N ASP A1070 -16.070 -28.560 77.491 1.00 79.96 N ANISOU 2125 N ASP A1070 11415 10921 8044 -393 -1170 182 N ATOM 2126 CA ASP A1070 -15.549 -27.477 78.326 1.00 78.57 C ANISOU 2126 CA ASP A1070 11188 10890 7775 -308 -1181 280 C ATOM 2127 C ASP A1070 -16.658 -26.734 79.054 1.00 81.38 C ANISOU 2127 C ASP A1070 11463 11322 8136 -413 -1137 321 C ATOM 2128 O ASP A1070 -16.458 -26.349 80.202 1.00 81.24 O ANISOU 2128 O ASP A1070 11469 11344 8054 -367 -1104 417 O ATOM 2129 CB ASP A1070 -14.696 -26.498 77.501 1.00 79.69 C ANISOU 2129 CB ASP A1070 11240 11185 7854 -217 -1252 226 C ATOM 2130 CG ASP A1070 -13.395 -27.074 76.961 1.00 95.96 C ANISOU 2130 CG ASP A1070 13352 13215 9893 -82 -1276 195 C ATOM 2131 OD1 ASP A1070 -12.836 -27.996 77.606 1.00 98.92 O ANISOU 2131 OD1 ASP A1070 13833 13479 10272 4 -1260 249 O ATOM 2132 OD2 ASP A1070 -12.911 -26.571 75.921 1.00101.90 O ANISOU 2132 OD2 ASP A1070 14041 14061 10614 -40 -1301 128 O ATOM 2133 N VAL A1071 -17.821 -26.538 78.398 1.00 77.09 N ANISOU 2133 N VAL A1071 10814 10820 7658 -536 -1143 235 N ATOM 2134 CA VAL A1071 -18.987 -25.876 78.995 1.00 76.36 C ANISOU 2134 CA VAL A1071 10614 10813 7587 -626 -1093 255 C ATOM 2135 C VAL A1071 -19.594 -26.751 80.090 1.00 82.18 C ANISOU 2135 C VAL A1071 11423 11421 8381 -727 -959 339 C ATOM 2136 O VAL A1071 -19.910 -26.236 81.163 1.00 81.81 O ANISOU 2136 O VAL A1071 11367 11434 8284 -721 -885 427 O ATOM 2137 CB VAL A1071 -20.012 -25.372 77.938 1.00 79.48 C ANISOU 2137 CB VAL A1071 10847 11328 8022 -687 -1158 130 C ATOM 2138 CG1 VAL A1071 -21.433 -25.297 78.489 1.00 80.06 C ANISOU 2138 CG1 VAL A1071 10794 11449 8177 -816 -1086 117 C ATOM 2139 CG2 VAL A1071 -19.590 -24.016 77.405 1.00 77.74 C ANISOU 2139 CG2 VAL A1071 10574 11256 7709 -560 -1231 133 C ATOM 2140 N ASP A1072 -19.707 -28.072 79.841 1.00 80.47 N ANISOU 2140 N ASP A1072 11299 11011 8263 -813 -909 315 N ATOM 2141 CA ASP A1072 -20.224 -29.015 80.830 1.00 82.47 C ANISOU 2141 CA ASP A1072 11660 11089 8586 -918 -740 420 C ATOM 2142 C ASP A1072 -19.311 -29.007 82.050 1.00 85.44 C ANISOU 2142 C ASP A1072 12206 11442 8817 -751 -692 607 C ATOM 2143 O ASP A1072 -19.806 -28.999 83.175 1.00 85.73 O ANISOU 2143 O ASP A1072 12285 11475 8813 -779 -559 731 O ATOM 2144 CB ASP A1072 -20.376 -30.421 80.230 1.00 86.91 C ANISOU 2144 CB ASP A1072 12318 11403 9302 -1036 -691 345 C ATOM 2145 CG ASP A1072 -21.553 -30.594 79.270 1.00105.34 C ANISOU 2145 CG ASP A1072 14466 13764 11795 -1247 -718 137 C ATOM 2146 OD1 ASP A1072 -22.124 -29.564 78.823 1.00105.11 O ANISOU 2146 OD1 ASP A1072 14229 13977 11732 -1250 -815 48 O ATOM 2147 OD2 ASP A1072 -21.892 -31.756 78.951 1.00116.80 O ANISOU 2147 OD2 ASP A1072 15980 14993 13405 -1398 -648 51 O ATOM 2148 N ALA A1073 -17.981 -28.900 81.811 1.00 80.47 N ANISOU 2148 N ALA A1073 11645 10840 8091 -563 -808 612 N ATOM 2149 CA ALA A1073 -16.944 -28.799 82.833 1.00 79.88 C ANISOU 2149 CA ALA A1073 11687 10804 7859 -367 -822 743 C ATOM 2150 C ALA A1073 -17.074 -27.460 83.557 1.00 83.58 C ANISOU 2150 C ALA A1073 12047 11497 8215 -336 -850 752 C ATOM 2151 O ALA A1073 -16.951 -27.428 84.777 1.00 84.31 O ANISOU 2151 O ALA A1073 12230 11624 8179 -251 -796 868 O ATOM 2152 CB ALA A1073 -15.571 -28.921 82.195 1.00 79.77 C ANISOU 2152 CB ALA A1073 11696 10806 7807 -199 -950 693 C ATOM 2153 N ALA A1074 -17.367 -26.364 82.809 1.00 79.53 N ANISOU 2153 N ALA A1074 11356 11125 7738 -391 -925 629 N ATOM 2154 CA ALA A1074 -17.565 -25.011 83.353 1.00 78.79 C ANISOU 2154 CA ALA A1074 11161 11207 7570 -370 -942 608 C ATOM 2155 C ALA A1074 -18.828 -24.951 84.205 1.00 85.07 C ANISOU 2155 C ALA A1074 11939 12017 8366 -465 -805 664 C ATOM 2156 O ALA A1074 -18.855 -24.221 85.192 1.00 85.48 O ANISOU 2156 O ALA A1074 11993 12178 8306 -404 -778 693 O ATOM 2157 CB ALA A1074 -17.643 -23.986 82.232 1.00 78.01 C ANISOU 2157 CB ALA A1074 10914 11200 7525 -394 -1027 489 C ATOM 2158 N VAL A1075 -19.863 -25.727 83.828 1.00 82.68 N ANISOU 2158 N VAL A1075 11608 11611 8195 -619 -712 659 N ATOM 2159 CA VAL A1075 -21.120 -25.846 84.563 1.00 84.02 C ANISOU 2159 CA VAL A1075 11735 11787 8403 -740 -545 708 C ATOM 2160 C VAL A1075 -20.844 -26.662 85.842 1.00 90.45 C ANISOU 2160 C VAL A1075 12760 12497 9110 -687 -403 889 C ATOM 2161 O VAL A1075 -21.157 -26.185 86.935 1.00 91.06 O ANISOU 2161 O VAL A1075 12859 12677 9064 -642 -309 962 O ATOM 2162 CB VAL A1075 -22.241 -26.426 83.659 1.00 88.94 C ANISOU 2162 CB VAL A1075 12221 12344 9226 -941 -502 609 C ATOM 2163 CG1 VAL A1075 -23.362 -27.072 84.467 1.00 91.07 C ANISOU 2163 CG1 VAL A1075 12481 12544 9578 -1104 -277 682 C ATOM 2164 CG2 VAL A1075 -22.800 -25.344 82.739 1.00 87.70 C ANISOU 2164 CG2 VAL A1075 11843 12367 9111 -944 -622 460 C ATOM 2165 N ARG A1076 -20.178 -27.841 85.709 1.00 87.61 N ANISOU 2165 N ARG A1076 12576 11941 8770 -655 -392 963 N ATOM 2166 CA ARG A1076 -19.775 -28.706 86.825 1.00 88.96 C ANISOU 2166 CA ARG A1076 12993 11989 8820 -551 -268 1164 C ATOM 2167 C ARG A1076 -18.564 -28.051 87.512 1.00 92.32 C ANISOU 2167 C ARG A1076 13484 12584 9011 -296 -410 1197 C ATOM 2168 O ARG A1076 -17.450 -28.584 87.494 1.00 92.60 O ANISOU 2168 O ARG A1076 13645 12563 8977 -129 -502 1242 O ATOM 2169 CB ARG A1076 -19.420 -30.124 86.330 1.00 89.64 C ANISOU 2169 CB ARG A1076 13247 11791 9022 -572 -224 1215 C ATOM 2170 CG ARG A1076 -20.589 -30.939 85.788 1.00101.58 C ANISOU 2170 CG ARG A1076 14714 13102 10780 -847 -66 1166 C ATOM 2171 CD ARG A1076 -20.210 -32.403 85.663 1.00114.14 C ANISOU 2171 CD ARG A1076 16546 14359 12464 -846 31 1254 C ATOM 2172 NE ARG A1076 -20.727 -33.026 84.443 1.00122.93 N ANISOU 2172 NE ARG A1076 17568 15309 13830 -1062 22 1065 N ATOM 2173 CZ ARG A1076 -19.997 -33.275 83.359 1.00136.27 C ANISOU 2173 CZ ARG A1076 19260 16951 15565 -994 -145 922 C ATOM 2174 NH1 ARG A1076 -18.712 -32.943 83.324 1.00119.68 N ANISOU 2174 NH1 ARG A1076 17223 14953 13297 -728 -305 954 N ATOM 2175 NH2 ARG A1076 -20.547 -33.854 82.300 1.00125.38 N ANISOU 2175 NH2 ARG A1076 17805 15439 14396 -1192 -152 727 N ATOM 2176 N GLY A1077 -18.808 -26.871 88.070 1.00 87.75 N ANISOU 2176 N GLY A1077 12798 12220 8325 -269 -435 1145 N ATOM 2177 CA GLY A1077 -17.821 -26.032 88.735 1.00 86.67 C ANISOU 2177 CA GLY A1077 12671 12275 7986 -73 -576 1112 C ATOM 2178 C GLY A1077 -18.497 -24.834 89.359 1.00 89.04 C ANISOU 2178 C GLY A1077 12865 12756 8211 -99 -538 1042 C ATOM 2179 O GLY A1077 -18.273 -24.543 90.538 1.00 89.90 O ANISOU 2179 O GLY A1077 13065 12990 8103 35 -522 1089 O ATOM 2180 N ILE A1078 -19.356 -24.149 88.571 1.00 83.25 N ANISOU 2180 N ILE A1078 11945 12042 7644 -250 -526 926 N ATOM 2181 CA ILE A1078 -20.167 -23.013 89.012 1.00 82.30 C ANISOU 2181 CA ILE A1078 11710 12065 7494 -274 -472 850 C ATOM 2182 C ILE A1078 -21.126 -23.553 90.095 1.00 88.79 C ANISOU 2182 C ILE A1078 12617 12886 8234 -308 -241 989 C ATOM 2183 O ILE A1078 -21.283 -22.929 91.152 1.00 89.73 O ANISOU 2183 O ILE A1078 12772 13146 8176 -216 -182 991 O ATOM 2184 CB ILE A1078 -20.909 -22.362 87.802 1.00 83.37 C ANISOU 2184 CB ILE A1078 11640 12206 7833 -395 -509 723 C ATOM 2185 CG1 ILE A1078 -19.913 -21.596 86.893 1.00 81.84 C ANISOU 2185 CG1 ILE A1078 11390 12030 7674 -336 -700 606 C ATOM 2186 CG2 ILE A1078 -22.030 -21.432 88.270 1.00 83.96 C ANISOU 2186 CG2 ILE A1078 11596 12401 7904 -415 -406 672 C ATOM 2187 CD1 ILE A1078 -20.395 -21.296 85.464 1.00 88.80 C ANISOU 2187 CD1 ILE A1078 12127 12886 8727 -418 -755 524 C ATOM 2188 N LEU A1079 -21.687 -24.762 89.847 1.00 85.62 N ANISOU 2188 N LEU A1079 12263 12314 7954 -440 -98 1102 N ATOM 2189 CA LEU A1079 -22.594 -25.479 90.743 1.00 87.41 C ANISOU 2189 CA LEU A1079 12577 12486 8147 -514 171 1260 C ATOM 2190 C LEU A1079 -21.923 -25.878 92.066 1.00 92.44 C ANISOU 2190 C LEU A1079 13482 13145 8498 -318 238 1440 C ATOM 2191 O LEU A1079 -22.612 -26.018 93.077 1.00 94.08 O ANISOU 2191 O LEU A1079 13769 13393 8584 -318 462 1564 O ATOM 2192 CB LEU A1079 -23.196 -26.709 90.037 1.00 88.46 C ANISOU 2192 CB LEU A1079 12703 12387 8520 -726 298 1311 C ATOM 2193 CG LEU A1079 -24.016 -26.452 88.762 1.00 91.65 C ANISOU 2193 CG LEU A1079 12834 12800 9190 -919 236 1123 C ATOM 2194 CD1 LEU A1079 -24.203 -27.727 87.985 1.00 92.85 C ANISOU 2194 CD1 LEU A1079 13013 12710 9554 -1097 288 1126 C ATOM 2195 CD2 LEU A1079 -25.368 -25.816 89.073 1.00 94.90 C ANISOU 2195 CD2 LEU A1079 13030 13365 9664 -1027 385 1066 C ATOM 2196 N ARG A1080 -20.588 -26.054 92.058 1.00 88.03 N ANISOU 2196 N ARG A1080 13050 12580 7816 -135 45 1452 N ATOM 2197 CA ARG A1080 -19.806 -26.383 93.255 1.00 89.40 C ANISOU 2197 CA ARG A1080 13465 12820 7683 108 45 1602 C ATOM 2198 C ARG A1080 -19.477 -25.103 94.012 1.00 92.74 C ANISOU 2198 C ARG A1080 13830 13523 7884 256 -78 1465 C ATOM 2199 O ARG A1080 -19.420 -25.124 95.244 1.00 94.96 O ANISOU 2199 O ARG A1080 14274 13929 7879 420 -2 1566 O ATOM 2200 CB ARG A1080 -18.500 -27.105 92.894 1.00 88.49 C ANISOU 2200 CB ARG A1080 13471 12609 7541 264 -130 1644 C ATOM 2201 CG ARG A1080 -18.686 -28.521 92.382 1.00 98.17 C ANISOU 2201 CG ARG A1080 14837 13527 8938 174 8 1800 C ATOM 2202 CD ARG A1080 -17.431 -29.354 92.570 1.00109.72 C ANISOU 2202 CD ARG A1080 16509 14913 10267 429 -103 1918 C ATOM 2203 NE ARG A1080 -16.269 -28.805 91.866 1.00116.52 N ANISOU 2203 NE ARG A1080 17222 15902 11149 535 -396 1727 N ATOM 2204 CZ ARG A1080 -15.950 -29.085 90.606 1.00129.77 C ANISOU 2204 CZ ARG A1080 18801 17449 13057 444 -485 1620 C ATOM 2205 NH1 ARG A1080 -16.712 -29.899 89.885 1.00117.27 N ANISOU 2205 NH1 ARG A1080 17248 15605 11704 243 -334 1656 N ATOM 2206 NH2 ARG A1080 -14.870 -28.549 90.055 1.00115.57 N ANISOU 2206 NH2 ARG A1080 16866 15786 11259 546 -717 1461 N ATOM 2207 N ASN A1081 -19.246 -23.994 93.271 1.00 86.38 N ANISOU 2207 N ASN A1081 12810 12808 7203 203 -260 1231 N ATOM 2208 CA ASN A1081 -18.924 -22.678 93.824 1.00 85.62 C ANISOU 2208 CA ASN A1081 12639 12932 6960 303 -382 1050 C ATOM 2209 C ASN A1081 -20.100 -22.117 94.630 1.00 90.59 C ANISOU 2209 C ASN A1081 13253 13664 7502 272 -183 1049 C ATOM 2210 O ASN A1081 -21.196 -21.930 94.088 1.00 89.69 O ANISOU 2210 O ASN A1081 12997 13491 7590 103 -52 1028 O ATOM 2211 CB ASN A1081 -18.492 -21.706 92.721 1.00 83.02 C ANISOU 2211 CB ASN A1081 12106 12604 6833 224 -567 832 C ATOM 2212 CG ASN A1081 -17.797 -20.471 93.240 1.00 99.28 C ANISOU 2212 CG ASN A1081 14114 14840 8766 327 -721 629 C ATOM 2213 OD1 ASN A1081 -18.422 -19.550 93.781 1.00 92.07 O ANISOU 2213 OD1 ASN A1081 13164 14022 7796 327 -655 529 O ATOM 2214 ND2 ASN A1081 -16.483 -20.422 93.079 1.00 89.22 N ANISOU 2214 ND2 ASN A1081 12825 13613 7462 413 -923 543 N ATOM 2215 N ALA A1082 -19.855 -21.868 95.935 1.00 88.67 N ANISOU 2215 N ALA A1082 13149 13599 6942 457 -167 1061 N ATOM 2216 CA ALA A1082 -20.819 -21.347 96.907 1.00 89.93 C ANISOU 2216 CA ALA A1082 13331 13894 6944 484 29 1057 C ATOM 2217 C ALA A1082 -21.428 -19.985 96.530 1.00 91.40 C ANISOU 2217 C ALA A1082 13304 14142 7282 399 8 822 C ATOM 2218 O ALA A1082 -22.605 -19.750 96.808 1.00 92.05 O ANISOU 2218 O ALA A1082 13325 14260 7391 339 223 840 O ATOM 2219 CB ALA A1082 -20.171 -21.270 98.282 1.00 93.18 C ANISOU 2219 CB ALA A1082 13941 14514 6949 739 -18 1070 C ATOM 2220 N LYS A1083 -20.631 -19.097 95.908 1.00 84.90 N ANISOU 2220 N LYS A1083 12371 13323 6562 402 -230 610 N ATOM 2221 CA LYS A1083 -21.069 -17.755 95.524 1.00 83.12 C ANISOU 2221 CA LYS A1083 11985 13116 6481 352 -256 396 C ATOM 2222 C LYS A1083 -21.519 -17.602 94.061 1.00 84.21 C ANISOU 2222 C LYS A1083 11943 13096 6956 189 -274 380 C ATOM 2223 O LYS A1083 -22.021 -16.537 93.685 1.00 83.96 O ANISOU 2223 O LYS A1083 11790 13060 7049 169 -271 241 O ATOM 2224 CB LYS A1083 -20.009 -16.706 95.929 1.00 85.48 C ANISOU 2224 CB LYS A1083 12296 13517 6666 458 -463 155 C ATOM 2225 CG LYS A1083 -20.532 -15.591 96.847 1.00101.71 C ANISOU 2225 CG LYS A1083 14362 15702 8581 544 -391 -25 C ATOM 2226 CD LYS A1083 -21.276 -16.108 98.099 1.00114.95 C ANISOU 2226 CD LYS A1083 16178 17529 9969 655 -181 107 C ATOM 2227 CE LYS A1083 -21.433 -15.066 99.178 1.00126.70 C ANISOU 2227 CE LYS A1083 17718 19188 11233 793 -157 -107 C ATOM 2228 NZ LYS A1083 -20.289 -15.082 100.130 1.00136.42 N ANISOU 2228 NZ LYS A1083 19092 20597 12145 959 -341 -214 N ATOM 2229 N LEU A1084 -21.377 -18.662 93.247 1.00 78.10 N ANISOU 2229 N LEU A1084 11164 12194 6315 94 -289 519 N ATOM 2230 CA LEU A1084 -21.784 -18.603 91.840 1.00 74.87 C ANISOU 2230 CA LEU A1084 10595 11665 6187 -41 -323 496 C ATOM 2231 C LEU A1084 -23.065 -19.361 91.532 1.00 77.70 C ANISOU 2231 C LEU A1084 10869 11976 6677 -172 -140 608 C ATOM 2232 O LEU A1084 -23.830 -18.915 90.673 1.00 75.95 O ANISOU 2232 O LEU A1084 10473 11744 6641 -245 -138 538 O ATOM 2233 CB LEU A1084 -20.647 -19.003 90.887 1.00 72.96 C ANISOU 2233 CB LEU A1084 10364 11320 6036 -63 -504 493 C ATOM 2234 CG LEU A1084 -19.505 -17.990 90.726 1.00 76.21 C ANISOU 2234 CG LEU A1084 10758 11763 6435 3 -685 328 C ATOM 2235 CD1 LEU A1084 -18.439 -18.528 89.815 1.00 74.68 C ANISOU 2235 CD1 LEU A1084 10560 11487 6329 -19 -823 344 C ATOM 2236 CD2 LEU A1084 -20.001 -16.668 90.169 1.00 78.07 C ANISOU 2236 CD2 LEU A1084 10874 11980 6808 -25 -685 192 C ATOM 2237 N LYS A1085 -23.301 -20.497 92.234 1.00 75.17 N ANISOU 2237 N LYS A1085 10670 11628 6263 -199 18 779 N ATOM 2238 CA LYS A1085 -24.500 -21.329 92.083 1.00 75.81 C ANISOU 2238 CA LYS A1085 10671 11649 6485 -360 232 883 C ATOM 2239 C LYS A1085 -25.796 -20.516 92.284 1.00 80.78 C ANISOU 2239 C LYS A1085 11108 12411 7174 -389 375 797 C ATOM 2240 O LYS A1085 -26.638 -20.570 91.383 1.00 79.70 O ANISOU 2240 O LYS A1085 10762 12255 7265 -518 391 743 O ATOM 2241 CB LYS A1085 -24.450 -22.579 92.992 1.00 79.63 C ANISOU 2241 CB LYS A1085 11365 12057 6833 -366 419 1101 C ATOM 2242 CG LYS A1085 -25.703 -23.453 92.931 1.00 87.24 C ANISOU 2242 CG LYS A1085 12245 12934 7968 -573 687 1203 C ATOM 2243 CD LYS A1085 -25.568 -24.717 93.757 1.00 97.53 C ANISOU 2243 CD LYS A1085 13801 14103 9153 -580 896 1448 C ATOM 2244 CE LYS A1085 -26.825 -25.558 93.752 1.00113.52 C ANISOU 2244 CE LYS A1085 15735 16020 11378 -824 1203 1541 C ATOM 2245 NZ LYS A1085 -27.630 -25.376 94.994 1.00122.07 N ANISOU 2245 NZ LYS A1085 16850 17238 12295 -797 1503 1647 N ATOM 2246 N PRO A1086 -25.964 -19.718 93.382 1.00 79.19 N ANISOU 2246 N PRO A1086 10956 12360 6774 -252 459 758 N ATOM 2247 CA PRO A1086 -27.208 -18.941 93.542 1.00 80.49 C ANISOU 2247 CA PRO A1086 10926 12653 7005 -253 604 668 C ATOM 2248 C PRO A1086 -27.521 -18.003 92.374 1.00 84.43 C ANISOU 2248 C PRO A1086 11212 13153 7716 -252 448 504 C ATOM 2249 O PRO A1086 -28.684 -17.903 91.967 1.00 84.48 O ANISOU 2249 O PRO A1086 10991 13223 7886 -317 544 466 O ATOM 2250 CB PRO A1086 -26.970 -18.167 94.844 1.00 83.29 C ANISOU 2250 CB PRO A1086 11421 13149 7076 -66 659 618 C ATOM 2251 CG PRO A1086 -26.006 -18.987 95.592 1.00 88.21 C ANISOU 2251 CG PRO A1086 12304 13744 7468 -7 646 758 C ATOM 2252 CD PRO A1086 -25.075 -19.503 94.544 1.00 81.49 C ANISOU 2252 CD PRO A1086 11471 12732 6758 -75 427 776 C ATOM 2253 N VAL A1087 -26.474 -17.340 91.827 1.00 80.46 N ANISOU 2253 N VAL A1087 10777 12585 7207 -172 213 414 N ATOM 2254 CA VAL A1087 -26.566 -16.417 90.687 1.00 79.26 C ANISOU 2254 CA VAL A1087 10487 12403 7224 -141 64 293 C ATOM 2255 C VAL A1087 -27.009 -17.209 89.460 1.00 83.98 C ANISOU 2255 C VAL A1087 10939 12946 8025 -281 19 335 C ATOM 2256 O VAL A1087 -27.977 -16.821 88.805 1.00 84.20 O ANISOU 2256 O VAL A1087 10762 13040 8192 -279 24 272 O ATOM 2257 CB VAL A1087 -25.233 -15.657 90.431 1.00 81.14 C ANISOU 2257 CB VAL A1087 10855 12559 7414 -57 -134 209 C ATOM 2258 CG1 VAL A1087 -25.386 -14.628 89.313 1.00 79.64 C ANISOU 2258 CG1 VAL A1087 10559 12316 7383 -8 -239 117 C ATOM 2259 CG2 VAL A1087 -24.718 -14.989 91.705 1.00 82.04 C ANISOU 2259 CG2 VAL A1087 11112 12739 7321 61 -111 128 C ATOM 2260 N TYR A1088 -26.327 -18.344 89.192 1.00 80.42 N ANISOU 2260 N TYR A1088 10591 12386 7579 -386 -28 429 N ATOM 2261 CA TYR A1088 -26.588 -19.246 88.072 1.00 79.98 C ANISOU 2261 CA TYR A1088 10434 12256 7699 -529 -79 446 C ATOM 2262 C TYR A1088 -27.992 -19.861 88.120 1.00 86.04 C ANISOU 2262 C TYR A1088 11005 13088 8600 -673 98 452 C ATOM 2263 O TYR A1088 -28.590 -20.058 87.061 1.00 85.98 O ANISOU 2263 O TYR A1088 10809 13099 8762 -756 26 376 O ATOM 2264 CB TYR A1088 -25.507 -20.332 88.015 1.00 80.58 C ANISOU 2264 CB TYR A1088 10700 12185 7732 -583 -133 542 C ATOM 2265 CG TYR A1088 -25.565 -21.216 86.788 1.00 82.06 C ANISOU 2265 CG TYR A1088 10819 12271 8087 -713 -212 525 C ATOM 2266 CD1 TYR A1088 -24.998 -20.810 85.585 1.00 82.31 C ANISOU 2266 CD1 TYR A1088 10820 12283 8169 -666 -409 445 C ATOM 2267 CD2 TYR A1088 -26.142 -22.481 86.843 1.00 84.58 C ANISOU 2267 CD2 TYR A1088 11126 12502 8510 -886 -76 586 C ATOM 2268 CE1 TYR A1088 -25.028 -21.629 84.457 1.00 83.07 C ANISOU 2268 CE1 TYR A1088 10869 12306 8390 -767 -487 408 C ATOM 2269 CE2 TYR A1088 -26.184 -23.307 85.721 1.00 85.44 C ANISOU 2269 CE2 TYR A1088 11179 12509 8775 -1012 -155 531 C ATOM 2270 CZ TYR A1088 -25.632 -22.874 84.528 1.00 89.99 C ANISOU 2270 CZ TYR A1088 11721 13098 9372 -941 -372 434 C ATOM 2271 OH TYR A1088 -25.678 -23.681 83.417 1.00 88.71 O ANISOU 2271 OH TYR A1088 11513 12857 9337 -1048 -455 357 O ATOM 2272 N ASP A1089 -28.515 -20.153 89.337 1.00 84.00 N ANISOU 2272 N ASP A1089 10780 12878 8259 -702 331 533 N ATOM 2273 CA ASP A1089 -29.857 -20.714 89.538 1.00 85.99 C ANISOU 2273 CA ASP A1089 10827 13197 8647 -861 552 541 C ATOM 2274 C ASP A1089 -30.944 -19.705 89.161 1.00 90.39 C ANISOU 2274 C ASP A1089 11091 13946 9308 -791 540 394 C ATOM 2275 O ASP A1089 -31.821 -20.028 88.366 1.00 90.90 O ANISOU 2275 O ASP A1089 10897 14070 9572 -913 527 310 O ATOM 2276 CB ASP A1089 -30.045 -21.212 90.986 1.00 89.90 C ANISOU 2276 CB ASP A1089 11468 13698 8994 -883 836 691 C ATOM 2277 CG ASP A1089 -29.277 -22.474 91.357 1.00 99.63 C ANISOU 2277 CG ASP A1089 12966 14732 10155 -964 904 870 C ATOM 2278 OD1 ASP A1089 -28.695 -23.112 90.447 1.00 99.34 O ANISOU 2278 OD1 ASP A1089 12975 14541 10230 -1040 750 863 O ATOM 2279 OD2 ASP A1089 -29.265 -22.829 92.558 1.00105.25 O ANISOU 2279 OD2 ASP A1089 13855 15446 10690 -931 1121 1022 O ATOM 2280 N SER A1090 -30.848 -18.467 89.680 1.00 87.03 N ANISOU 2280 N SER A1090 10704 13616 8747 -580 523 345 N ATOM 2281 CA SER A1090 -31.788 -17.374 89.390 1.00 87.72 C ANISOU 2281 CA SER A1090 10553 13868 8908 -447 509 214 C ATOM 2282 C SER A1090 -31.680 -16.830 87.940 1.00 89.17 C ANISOU 2282 C SER A1090 10632 14042 9206 -369 247 120 C ATOM 2283 O SER A1090 -32.404 -15.900 87.558 1.00 89.84 O ANISOU 2283 O SER A1090 10537 14251 9347 -216 204 26 O ATOM 2284 CB SER A1090 -31.780 -16.356 90.534 1.00 92.40 C ANISOU 2284 CB SER A1090 11248 14537 9322 -256 621 190 C ATOM 2285 OG SER A1090 -30.556 -15.637 90.600 1.00 99.51 O ANISOU 2285 OG SER A1090 12395 15328 10086 -121 457 170 O ATOM 2286 N LEU A1091 -30.777 -17.421 87.142 1.00 82.93 N ANISOU 2286 N LEU A1091 9967 13109 8435 -450 82 156 N ATOM 2287 CA LEU A1091 -30.505 -16.989 85.776 1.00 81.13 C ANISOU 2287 CA LEU A1091 9696 12862 8268 -369 -152 94 C ATOM 2288 C LEU A1091 -31.078 -17.810 84.627 1.00 84.54 C ANISOU 2288 C LEU A1091 9925 13342 8852 -501 -249 31 C ATOM 2289 O LEU A1091 -31.173 -19.034 84.719 1.00 84.15 O ANISOU 2289 O LEU A1091 9860 13235 8879 -718 -173 52 O ATOM 2290 CB LEU A1091 -28.962 -16.954 85.727 1.00 78.80 C ANISOU 2290 CB LEU A1091 9693 12389 7860 -342 -262 158 C ATOM 2291 CG LEU A1091 -28.275 -15.641 85.316 1.00 81.96 C ANISOU 2291 CG LEU A1091 10201 12738 8204 -150 -389 126 C ATOM 2292 CD1 LEU A1091 -28.552 -14.509 86.305 1.00 82.95 C ANISOU 2292 CD1 LEU A1091 10354 12905 8257 0 -283 84 C ATOM 2293 CD2 LEU A1091 -26.781 -15.837 85.196 1.00 82.17 C ANISOU 2293 CD2 LEU A1091 10453 12610 8158 -178 -484 173 C ATOM 2294 N ASP A1092 -31.479 -17.118 83.558 1.00 81.34 N ANISOU 2294 N ASP A1092 9375 13042 8487 -357 -415 -53 N ATOM 2295 CA ASP A1092 -32.081 -17.700 82.357 1.00 82.44 C ANISOU 2295 CA ASP A1092 9299 13285 8740 -429 -556 -156 C ATOM 2296 C ASP A1092 -31.016 -18.201 81.374 1.00 86.15 C ANISOU 2296 C ASP A1092 9951 13614 9169 -468 -725 -137 C ATOM 2297 O ASP A1092 -29.851 -17.819 81.507 1.00 84.49 O ANISOU 2297 O ASP A1092 10002 13252 8847 -391 -750 -43 O ATOM 2298 CB ASP A1092 -33.003 -16.669 81.687 1.00 85.40 C ANISOU 2298 CB ASP A1092 9446 13872 9131 -196 -667 -246 C ATOM 2299 CG ASP A1092 -32.369 -15.301 81.531 1.00 92.75 C ANISOU 2299 CG ASP A1092 10576 14729 9935 83 -736 -175 C ATOM 2300 OD1 ASP A1092 -32.321 -14.552 82.535 1.00 92.12 O ANISOU 2300 OD1 ASP A1092 10585 14607 9810 176 -599 -135 O ATOM 2301 OD2 ASP A1092 -31.900 -14.988 80.412 1.00 98.93 O ANISOU 2301 OD2 ASP A1092 11442 15484 10663 203 -912 -162 O ATOM 2302 N ALA A1093 -31.425 -19.034 80.377 1.00 83.69 N ANISOU 2302 N ALA A1093 9484 13367 8947 -584 -843 -249 N ATOM 2303 CA ALA A1093 -30.573 -19.633 79.337 1.00 82.12 C ANISOU 2303 CA ALA A1093 9424 13065 8712 -622 -1000 -267 C ATOM 2304 C ALA A1093 -29.665 -18.635 78.613 1.00 84.94 C ANISOU 2304 C ALA A1093 9969 13387 8917 -383 -1136 -197 C ATOM 2305 O ALA A1093 -28.524 -18.980 78.291 1.00 83.32 O ANISOU 2305 O ALA A1093 9979 13029 8651 -408 -1176 -142 O ATOM 2306 CB ALA A1093 -31.423 -20.379 78.327 1.00 84.94 C ANISOU 2306 CB ALA A1093 9530 13567 9176 -729 -1127 -454 C ATOM 2307 N VAL A1094 -30.158 -17.405 78.364 1.00 81.89 N ANISOU 2307 N VAL A1094 9505 13131 8479 -147 -1187 -192 N ATOM 2308 CA VAL A1094 -29.378 -16.363 77.685 1.00 80.20 C ANISOU 2308 CA VAL A1094 9480 12856 8136 81 -1274 -105 C ATOM 2309 C VAL A1094 -28.328 -15.799 78.645 1.00 80.35 C ANISOU 2309 C VAL A1094 9743 12673 8115 85 -1146 12 C ATOM 2310 O VAL A1094 -27.142 -15.790 78.309 1.00 78.24 O ANISOU 2310 O VAL A1094 9679 12263 7787 81 -1174 76 O ATOM 2311 CB VAL A1094 -30.262 -15.246 77.054 1.00 86.04 C ANISOU 2311 CB VAL A1094 10085 13772 8832 361 -1365 -123 C ATOM 2312 CG1 VAL A1094 -29.424 -14.263 76.239 1.00 84.84 C ANISOU 2312 CG1 VAL A1094 10166 13519 8550 582 -1426 -7 C ATOM 2313 CG2 VAL A1094 -31.376 -15.837 76.194 1.00 88.32 C ANISOU 2313 CG2 VAL A1094 10081 14319 9158 360 -1516 -279 C ATOM 2314 N ARG A1095 -28.767 -15.362 79.839 1.00 76.24 N ANISOU 2314 N ARG A1095 9185 12160 7625 91 -1006 20 N ATOM 2315 CA ARG A1095 -27.905 -14.776 80.868 1.00 74.74 C ANISOU 2315 CA ARG A1095 9197 11816 7385 103 -897 86 C ATOM 2316 C ARG A1095 -26.902 -15.737 81.524 1.00 77.63 C ANISOU 2316 C ARG A1095 9711 12057 7727 -83 -848 126 C ATOM 2317 O ARG A1095 -25.844 -15.281 81.969 1.00 75.34 O ANISOU 2317 O ARG A1095 9603 11646 7377 -58 -829 163 O ATOM 2318 CB ARG A1095 -28.720 -13.978 81.886 1.00 74.92 C ANISOU 2318 CB ARG A1095 9140 11907 7420 200 -770 59 C ATOM 2319 CG ARG A1095 -29.186 -12.645 81.326 1.00 81.21 C ANISOU 2319 CG ARG A1095 9910 12734 8211 461 -814 53 C ATOM 2320 CD ARG A1095 -30.193 -11.994 82.239 1.00 87.51 C ANISOU 2320 CD ARG A1095 10582 13631 9035 573 -690 0 C ATOM 2321 NE ARG A1095 -30.646 -10.710 81.709 1.00 90.79 N ANISOU 2321 NE ARG A1095 10992 14053 9450 858 -727 3 N ATOM 2322 CZ ARG A1095 -31.909 -10.417 81.423 1.00103.52 C ANISOU 2322 CZ ARG A1095 12366 15865 11104 1029 -750 -47 C ATOM 2323 NH1 ARG A1095 -32.866 -11.320 81.606 1.00 90.00 N ANISOU 2323 NH1 ARG A1095 10369 14372 9456 905 -732 -125 N ATOM 2324 NH2 ARG A1095 -32.226 -9.222 80.949 1.00 91.64 N ANISOU 2324 NH2 ARG A1095 10898 14337 9584 1328 -782 -22 N ATOM 2325 N ARG A1096 -27.206 -17.059 81.547 1.00 75.54 N ANISOU 2325 N ARG A1096 9371 11815 7516 -261 -830 110 N ATOM 2326 CA ARG A1096 -26.299 -18.090 82.073 1.00 74.90 C ANISOU 2326 CA ARG A1096 9445 11603 7410 -404 -787 166 C ATOM 2327 C ARG A1096 -25.066 -18.190 81.169 1.00 78.45 C ANISOU 2327 C ARG A1096 10038 11949 7818 -375 -912 185 C ATOM 2328 O ARG A1096 -23.950 -18.333 81.669 1.00 77.06 O ANISOU 2328 O ARG A1096 10025 11671 7583 -385 -899 236 O ATOM 2329 CB ARG A1096 -26.993 -19.459 82.167 1.00 76.28 C ANISOU 2329 CB ARG A1096 9518 11784 7681 -599 -719 146 C ATOM 2330 CG ARG A1096 -27.839 -19.631 83.416 1.00 86.94 C ANISOU 2330 CG ARG A1096 10793 13186 9053 -672 -523 174 C ATOM 2331 CD ARG A1096 -28.516 -20.984 83.447 1.00 96.43 C ANISOU 2331 CD ARG A1096 11897 14356 10385 -897 -422 158 C ATOM 2332 NE ARG A1096 -29.465 -21.073 84.556 1.00104.23 N ANISOU 2332 NE ARG A1096 12780 15416 11405 -971 -200 188 N ATOM 2333 CZ ARG A1096 -30.033 -22.197 84.977 1.00119.76 C ANISOU 2333 CZ ARG A1096 14699 17322 13481 -1186 -24 215 C ATOM 2334 NH1 ARG A1096 -29.744 -23.355 84.392 1.00107.71 N ANISOU 2334 NH1 ARG A1096 13230 15639 12055 -1349 -56 202 N ATOM 2335 NH2 ARG A1096 -30.884 -22.178 85.992 1.00107.65 N ANISOU 2335 NH2 ARG A1096 13069 15869 11963 -1242 208 255 N ATOM 2336 N ALA A1097 -25.273 -18.072 79.841 1.00 75.74 N ANISOU 2336 N ALA A1097 9626 11660 7492 -320 -1034 138 N ATOM 2337 CA ALA A1097 -24.212 -18.103 78.841 1.00 74.41 C ANISOU 2337 CA ALA A1097 9579 11421 7273 -276 -1132 155 C ATOM 2338 C ALA A1097 -23.297 -16.888 78.954 1.00 77.52 C ANISOU 2338 C ALA A1097 10103 11743 7609 -154 -1115 214 C ATOM 2339 O ALA A1097 -22.106 -17.008 78.663 1.00 76.53 O ANISOU 2339 O ALA A1097 10099 11529 7452 -164 -1135 242 O ATOM 2340 CB ALA A1097 -24.808 -18.176 77.456 1.00 76.04 C ANISOU 2340 CB ALA A1097 9681 11738 7474 -216 -1255 88 C ATOM 2341 N ALA A1098 -23.842 -15.725 79.381 1.00 74.30 N ANISOU 2341 N ALA A1098 9665 11365 7203 -47 -1066 219 N ATOM 2342 CA ALA A1098 -23.055 -14.504 79.578 1.00 73.55 C ANISOU 2342 CA ALA A1098 9696 11164 7087 44 -1025 250 C ATOM 2343 C ALA A1098 -22.093 -14.704 80.764 1.00 76.14 C ANISOU 2343 C ALA A1098 10117 11414 7398 -51 -971 239 C ATOM 2344 O ALA A1098 -20.932 -14.300 80.686 1.00 74.25 O ANISOU 2344 O ALA A1098 9977 11081 7154 -57 -975 242 O ATOM 2345 CB ALA A1098 -23.973 -13.315 79.816 1.00 75.35 C ANISOU 2345 CB ALA A1098 9875 11422 7332 189 -977 241 C ATOM 2346 N LEU A1099 -22.572 -15.398 81.825 1.00 73.92 N ANISOU 2346 N LEU A1099 9795 11187 7102 -125 -919 226 N ATOM 2347 CA LEU A1099 -21.822 -15.752 83.035 1.00 73.59 C ANISOU 2347 CA LEU A1099 9843 11117 6999 -180 -880 225 C ATOM 2348 C LEU A1099 -20.765 -16.829 82.700 1.00 77.45 C ANISOU 2348 C LEU A1099 10401 11554 7471 -249 -943 259 C ATOM 2349 O LEU A1099 -19.659 -16.781 83.242 1.00 76.99 O ANISOU 2349 O LEU A1099 10425 11465 7363 -244 -964 247 O ATOM 2350 CB LEU A1099 -22.803 -16.244 84.119 1.00 74.55 C ANISOU 2350 CB LEU A1099 9914 11320 7090 -216 -778 235 C ATOM 2351 CG LEU A1099 -22.223 -16.597 85.487 1.00 79.73 C ANISOU 2351 CG LEU A1099 10681 11981 7631 -231 -724 251 C ATOM 2352 CD1 LEU A1099 -22.479 -15.490 86.501 1.00 81.01 C ANISOU 2352 CD1 LEU A1099 10860 12193 7726 -144 -657 181 C ATOM 2353 CD2 LEU A1099 -22.810 -17.889 85.994 1.00 82.96 C ANISOU 2353 CD2 LEU A1099 11086 12412 8023 -320 -633 332 C ATOM 2354 N ILE A1100 -21.113 -17.790 81.807 1.00 73.93 N ANISOU 2354 N ILE A1100 9911 11108 7069 -303 -980 280 N ATOM 2355 CA ILE A1100 -20.215 -18.858 81.342 1.00 73.09 C ANISOU 2355 CA ILE A1100 9873 10939 6960 -347 -1033 301 C ATOM 2356 C ILE A1100 -19.101 -18.241 80.478 1.00 77.46 C ANISOU 2356 C ILE A1100 10465 11457 7507 -289 -1094 286 C ATOM 2357 O ILE A1100 -17.943 -18.645 80.618 1.00 77.34 O ANISOU 2357 O ILE A1100 10512 11405 7468 -288 -1119 291 O ATOM 2358 CB ILE A1100 -20.987 -20.038 80.667 1.00 76.34 C ANISOU 2358 CB ILE A1100 10230 11343 7433 -434 -1044 290 C ATOM 2359 CG1 ILE A1100 -21.757 -20.857 81.735 1.00 77.81 C ANISOU 2359 CG1 ILE A1100 10409 11516 7639 -530 -936 327 C ATOM 2360 CG2 ILE A1100 -20.052 -20.955 79.848 1.00 75.88 C ANISOU 2360 CG2 ILE A1100 10248 11207 7377 -446 -1110 283 C ATOM 2361 CD1 ILE A1100 -22.924 -21.739 81.230 1.00 84.21 C ANISOU 2361 CD1 ILE A1100 11103 12333 8561 -658 -910 278 C ATOM 2362 N ASN A1101 -19.437 -17.216 79.651 1.00 73.91 N ANISOU 2362 N ASN A1101 9980 11024 7077 -226 -1101 278 N ATOM 2363 CA ASN A1101 -18.464 -16.491 78.819 1.00 73.45 C ANISOU 2363 CA ASN A1101 9971 10918 7019 -178 -1109 287 C ATOM 2364 C ASN A1101 -17.448 -15.799 79.726 1.00 77.55 C ANISOU 2364 C ASN A1101 10529 11386 7550 -195 -1072 257 C ATOM 2365 O ASN A1101 -16.269 -15.722 79.378 1.00 77.25 O ANISOU 2365 O ASN A1101 10512 11312 7526 -210 -1073 246 O ATOM 2366 CB ASN A1101 -19.162 -15.465 77.910 1.00 74.56 C ANISOU 2366 CB ASN A1101 10098 11070 7162 -79 -1099 315 C ATOM 2367 CG ASN A1101 -18.236 -14.673 77.007 1.00 96.67 C ANISOU 2367 CG ASN A1101 12975 13797 9960 -30 -1060 358 C ATOM 2368 OD1 ASN A1101 -17.450 -13.827 77.449 1.00 88.04 O ANISOU 2368 OD1 ASN A1101 11925 12611 8915 -54 -990 349 O ATOM 2369 ND2 ASN A1101 -18.367 -14.875 75.710 1.00 90.94 N ANISOU 2369 ND2 ASN A1101 12264 13112 9175 39 -1093 398 N ATOM 2370 N MET A1102 -17.917 -15.307 80.889 1.00 74.11 N ANISOU 2370 N MET A1102 10087 10964 7105 -193 -1037 222 N ATOM 2371 CA MET A1102 -17.092 -14.646 81.894 1.00 74.07 C ANISOU 2371 CA MET A1102 10109 10937 7096 -210 -1022 147 C ATOM 2372 C MET A1102 -16.123 -15.639 82.537 1.00 79.10 C ANISOU 2372 C MET A1102 10757 11624 7674 -237 -1081 130 C ATOM 2373 O MET A1102 -14.930 -15.346 82.616 1.00 79.34 O ANISOU 2373 O MET A1102 10774 11648 7724 -255 -1109 66 O ATOM 2374 CB MET A1102 -17.966 -13.948 82.946 1.00 76.77 C ANISOU 2374 CB MET A1102 10453 11302 7415 -176 -971 101 C ATOM 2375 CG MET A1102 -18.508 -12.634 82.470 1.00 80.35 C ANISOU 2375 CG MET A1102 10915 11675 7940 -116 -910 90 C ATOM 2376 SD MET A1102 -19.448 -11.773 83.737 1.00 85.12 S ANISOU 2376 SD MET A1102 11525 12300 8518 -52 -838 6 S ATOM 2377 CE MET A1102 -18.186 -10.803 84.490 1.00 82.29 C ANISOU 2377 CE MET A1102 11230 11849 8187 -102 -833 -148 C ATOM 2378 N VAL A1103 -16.626 -16.831 82.936 1.00 76.15 N ANISOU 2378 N VAL A1103 10402 11293 7238 -237 -1092 191 N ATOM 2379 CA VAL A1103 -15.841 -17.923 83.530 1.00 76.49 C ANISOU 2379 CA VAL A1103 10490 11366 7208 -220 -1140 213 C ATOM 2380 C VAL A1103 -14.782 -18.408 82.519 1.00 80.97 C ANISOU 2380 C VAL A1103 11042 11902 7821 -215 -1193 214 C ATOM 2381 O VAL A1103 -13.666 -18.754 82.907 1.00 81.00 O ANISOU 2381 O VAL A1103 11044 11944 7788 -173 -1249 185 O ATOM 2382 CB VAL A1103 -16.765 -19.055 84.068 1.00 80.90 C ANISOU 2382 CB VAL A1103 11100 11924 7715 -230 -1093 304 C ATOM 2383 CG1 VAL A1103 -15.989 -20.329 84.400 1.00 81.29 C ANISOU 2383 CG1 VAL A1103 11232 11953 7701 -186 -1128 366 C ATOM 2384 CG2 VAL A1103 -17.553 -18.581 85.289 1.00 81.49 C ANISOU 2384 CG2 VAL A1103 11190 12062 7711 -215 -1021 299 C ATOM 2385 N PHE A1104 -15.114 -18.357 81.221 1.00 77.53 N ANISOU 2385 N PHE A1104 10585 11420 7452 -238 -1176 235 N ATOM 2386 CA PHE A1104 -14.196 -18.721 80.144 1.00 77.10 C ANISOU 2386 CA PHE A1104 10521 11346 7428 -224 -1200 232 C ATOM 2387 C PHE A1104 -13.000 -17.754 80.067 1.00 80.66 C ANISOU 2387 C PHE A1104 10917 11810 7922 -231 -1188 168 C ATOM 2388 O PHE A1104 -11.871 -18.195 79.840 1.00 80.48 O ANISOU 2388 O PHE A1104 10858 11813 7907 -209 -1213 140 O ATOM 2389 CB PHE A1104 -14.952 -18.775 78.806 1.00 78.74 C ANISOU 2389 CB PHE A1104 10729 11530 7657 -228 -1185 260 C ATOM 2390 CG PHE A1104 -15.298 -20.171 78.353 1.00 80.53 C ANISOU 2390 CG PHE A1104 10990 11735 7873 -235 -1219 271 C ATOM 2391 CD1 PHE A1104 -16.328 -20.881 78.956 1.00 84.09 C ANISOU 2391 CD1 PHE A1104 11454 12168 8330 -283 -1211 288 C ATOM 2392 CD2 PHE A1104 -14.600 -20.775 77.315 1.00 83.22 C ANISOU 2392 CD2 PHE A1104 11351 12062 8208 -201 -1238 251 C ATOM 2393 CE1 PHE A1104 -16.638 -22.179 78.545 1.00 85.76 C ANISOU 2393 CE1 PHE A1104 11702 12318 8564 -318 -1224 278 C ATOM 2394 CE2 PHE A1104 -14.919 -22.069 76.897 1.00 86.61 C ANISOU 2394 CE2 PHE A1104 11825 12444 8640 -211 -1266 231 C ATOM 2395 CZ PHE A1104 -15.934 -22.763 77.517 1.00 85.03 C ANISOU 2395 CZ PHE A1104 11642 12197 8469 -280 -1260 240 C ATOM 2396 N GLN A1105 -13.250 -16.447 80.297 1.00 76.90 N ANISOU 2396 N GLN A1105 10425 11305 7488 -264 -1138 132 N ATOM 2397 CA GLN A1105 -12.234 -15.394 80.245 1.00 76.99 C ANISOU 2397 CA GLN A1105 10383 11289 7580 -313 -1095 53 C ATOM 2398 C GLN A1105 -11.394 -15.317 81.513 1.00 81.42 C ANISOU 2398 C GLN A1105 10882 11928 8127 -329 -1162 -69 C ATOM 2399 O GLN A1105 -10.165 -15.368 81.438 1.00 81.89 O ANISOU 2399 O GLN A1105 10848 12035 8230 -351 -1185 -144 O ATOM 2400 CB GLN A1105 -12.880 -14.027 79.971 1.00 78.31 C ANISOU 2400 CB GLN A1105 10588 11352 7813 -336 -1001 62 C ATOM 2401 CG GLN A1105 -11.864 -12.915 79.715 1.00 90.90 C ANISOU 2401 CG GLN A1105 12147 12860 9530 -418 -911 -7 C ATOM 2402 CD GLN A1105 -12.482 -11.550 79.553 1.00110.32 C ANISOU 2402 CD GLN A1105 14682 15170 12066 -425 -800 8 C ATOM 2403 OE1 GLN A1105 -13.705 -11.375 79.538 1.00106.18 O ANISOU 2403 OE1 GLN A1105 14225 14627 11492 -341 -799 75 O ATOM 2404 NE2 GLN A1105 -11.635 -10.542 79.410 1.00103.78 N ANISOU 2404 NE2 GLN A1105 13838 14221 11372 -524 -693 -57 N ATOM 2405 N MET A1106 -12.069 -15.148 82.662 1.00 77.33 N ANISOU 2405 N MET A1106 10402 11442 7537 -308 -1191 -102 N ATOM 2406 CA MET A1106 -11.473 -14.965 83.981 1.00 77.78 C ANISOU 2406 CA MET A1106 10422 11600 7533 -297 -1267 -234 C ATOM 2407 C MET A1106 -11.247 -16.262 84.749 1.00 81.46 C ANISOU 2407 C MET A1106 10915 12188 7847 -191 -1366 -189 C ATOM 2408 O MET A1106 -10.134 -16.519 85.201 1.00 82.37 O ANISOU 2408 O MET A1106 10956 12414 7927 -147 -1462 -276 O ATOM 2409 CB MET A1106 -12.346 -14.015 84.818 1.00 80.51 C ANISOU 2409 CB MET A1106 10818 11919 7853 -305 -1227 -299 C ATOM 2410 CG MET A1106 -12.379 -12.601 84.295 1.00 84.63 C ANISOU 2410 CG MET A1106 11331 12296 8528 -388 -1130 -369 C ATOM 2411 SD MET A1106 -13.861 -11.739 84.850 1.00 89.02 S ANISOU 2411 SD MET A1106 11979 12784 9059 -342 -1051 -371 S ATOM 2412 CE MET A1106 -14.877 -11.995 83.480 1.00 84.64 C ANISOU 2412 CE MET A1106 11462 12151 8547 -299 -980 -172 C ATOM 2413 N GLY A1107 -12.305 -17.047 84.908 1.00 76.93 N ANISOU 2413 N GLY A1107 10443 11592 7193 -147 -1335 -56 N ATOM 2414 CA GLY A1107 -12.293 -18.274 85.688 1.00 77.04 C ANISOU 2414 CA GLY A1107 10536 11671 7064 -45 -1382 28 C ATOM 2415 C GLY A1107 -13.174 -18.071 86.896 1.00 81.50 C ANISOU 2415 C GLY A1107 11179 12288 7501 -14 -1345 38 C ATOM 2416 O GLY A1107 -13.211 -16.961 87.439 1.00 81.06 O ANISOU 2416 O GLY A1107 11088 12275 7436 -36 -1346 -90 O ATOM 2417 N GLU A1108 -13.900 -19.134 87.320 1.00 79.33 N ANISOU 2417 N GLU A1108 11015 11995 7132 32 -1290 186 N ATOM 2418 CA GLU A1108 -14.827 -19.109 88.468 1.00 80.56 C ANISOU 2418 CA GLU A1108 11256 12203 7149 65 -1210 232 C ATOM 2419 C GLU A1108 -14.238 -18.538 89.752 1.00 85.42 C ANISOU 2419 C GLU A1108 11891 12982 7584 168 -1286 116 C ATOM 2420 O GLU A1108 -14.949 -17.872 90.504 1.00 85.32 O ANISOU 2420 O GLU A1108 11904 13022 7493 172 -1221 66 O ATOM 2421 CB GLU A1108 -15.507 -20.469 88.708 1.00 82.80 C ANISOU 2421 CB GLU A1108 11663 12421 7374 85 -1112 424 C ATOM 2422 CG GLU A1108 -14.592 -21.605 89.124 1.00 97.77 C ANISOU 2422 CG GLU A1108 13669 14327 9151 221 -1176 518 C ATOM 2423 CD GLU A1108 -15.338 -22.896 89.387 1.00128.26 C ANISOU 2423 CD GLU A1108 17687 18068 12980 222 -1036 720 C ATOM 2424 OE1 GLU A1108 -15.577 -23.215 90.575 1.00128.91 O ANISOU 2424 OE1 GLU A1108 17903 18208 12868 321 -965 822 O ATOM 2425 OE2 GLU A1108 -15.695 -23.582 88.403 1.00123.19 O ANISOU 2425 OE2 GLU A1108 17037 17266 12502 121 -985 770 O ATOM 2426 N THR A1109 -12.930 -18.765 89.970 1.00 83.17 N ANISOU 2426 N THR A1109 11575 12792 7233 260 -1432 49 N ATOM 2427 CA THR A1109 -12.160 -18.263 91.108 1.00 85.25 C ANISOU 2427 CA THR A1109 11822 13250 7319 370 -1558 -109 C ATOM 2428 C THR A1109 -12.087 -16.725 91.087 1.00 89.30 C ANISOU 2428 C THR A1109 12219 13772 7940 256 -1573 -347 C ATOM 2429 O THR A1109 -12.019 -16.098 92.147 1.00 90.41 O ANISOU 2429 O THR A1109 12374 14046 7932 312 -1623 -498 O ATOM 2430 CB THR A1109 -10.789 -18.971 91.190 1.00 96.30 C ANISOU 2430 CB THR A1109 13177 14763 8648 506 -1722 -127 C ATOM 2431 OG1 THR A1109 -10.061 -18.474 92.313 1.00 97.55 O ANISOU 2431 OG1 THR A1109 13293 15151 8619 622 -1873 -311 O ATOM 2432 CG2 THR A1109 -9.951 -18.830 89.904 1.00 94.43 C ANISOU 2432 CG2 THR A1109 12777 14453 8651 406 -1764 -198 C ATOM 2433 N GLY A1110 -12.127 -16.153 89.879 1.00 84.52 N ANISOU 2433 N GLY A1110 11521 13012 7580 108 -1519 -373 N ATOM 2434 CA GLY A1110 -12.092 -14.717 89.637 1.00 84.62 C ANISOU 2434 CA GLY A1110 11453 12956 7744 -12 -1492 -559 C ATOM 2435 C GLY A1110 -13.465 -14.098 89.470 1.00 88.61 C ANISOU 2435 C GLY A1110 12023 13339 8305 -55 -1343 -506 C ATOM 2436 O GLY A1110 -13.661 -12.946 89.864 1.00 89.09 O ANISOU 2436 O GLY A1110 12080 13371 8399 -87 -1313 -666 O ATOM 2437 N VAL A1111 -14.426 -14.845 88.877 1.00 84.64 N ANISOU 2437 N VAL A1111 11569 12764 7825 -54 -1251 -302 N ATOM 2438 CA VAL A1111 -15.812 -14.376 88.671 1.00 84.34 C ANISOU 2438 CA VAL A1111 11555 12649 7841 -74 -1119 -246 C ATOM 2439 C VAL A1111 -16.534 -14.226 90.028 1.00 91.45 C ANISOU 2439 C VAL A1111 12525 13659 8562 6 -1062 -282 C ATOM 2440 O VAL A1111 -17.320 -13.286 90.213 1.00 91.57 O ANISOU 2440 O VAL A1111 12539 13641 8612 12 -978 -355 O ATOM 2441 CB VAL A1111 -16.596 -15.242 87.642 1.00 86.40 C ANISOU 2441 CB VAL A1111 11807 12835 8184 -108 -1058 -62 C ATOM 2442 CG1 VAL A1111 -18.039 -14.767 87.488 1.00 85.93 C ANISOU 2442 CG1 VAL A1111 11728 12746 8176 -109 -943 -28 C ATOM 2443 CG2 VAL A1111 -15.895 -15.240 86.281 1.00 85.13 C ANISOU 2443 CG2 VAL A1111 11592 12582 8172 -165 -1103 -47 C ATOM 2444 N ALA A1112 -16.208 -15.119 90.995 1.00 89.81 N ANISOU 2444 N ALA A1112 12391 13585 8146 91 -1104 -232 N ATOM 2445 CA ALA A1112 -16.742 -15.086 92.356 1.00 91.81 C ANISOU 2445 CA ALA A1112 12736 13974 8172 192 -1045 -251 C ATOM 2446 C ALA A1112 -16.114 -13.925 93.162 1.00 98.99 C ANISOU 2446 C ALA A1112 13636 14973 9000 232 -1135 -518 C ATOM 2447 O ALA A1112 -16.533 -13.657 94.294 1.00100.86 O ANISOU 2447 O ALA A1112 13951 15335 9037 327 -1091 -588 O ATOM 2448 CB ALA A1112 -16.508 -16.421 93.044 1.00 93.44 C ANISOU 2448 CB ALA A1112 13054 14279 8168 293 -1054 -86 C ATOM 2449 N GLY A1113 -15.147 -13.232 92.547 1.00 95.82 N ANISOU 2449 N GLY A1113 13139 14502 8765 149 -1242 -677 N ATOM 2450 CA GLY A1113 -14.489 -12.048 93.095 1.00 97.51 C ANISOU 2450 CA GLY A1113 13315 14751 8985 129 -1324 -971 C ATOM 2451 C GLY A1113 -15.437 -10.862 93.122 1.00102.34 C ANISOU 2451 C GLY A1113 13955 15236 9693 102 -1191 -1071 C ATOM 2452 O GLY A1113 -15.334 -9.999 94.001 1.00103.92 O ANISOU 2452 O GLY A1113 14183 15488 9813 133 -1213 -1309 O ATOM 2453 N PHE A1114 -16.388 -10.837 92.194 1.00 97.98 N ANISOU 2453 N PHE A1114 13397 14533 9299 67 -1059 -903 N ATOM 2454 CA PHE A1114 -17.316 -9.714 92.078 1.00 98.88 C ANISOU 2454 CA PHE A1114 13531 14515 9522 78 -932 -974 C ATOM 2455 C PHE A1114 -18.631 -9.875 92.851 1.00 99.86 C ANISOU 2455 C PHE A1114 13707 14743 9492 193 -802 -910 C ATOM 2456 O PHE A1114 -19.578 -10.492 92.364 1.00 99.36 O ANISOU 2456 O PHE A1114 13611 14677 9463 204 -708 -709 O ATOM 2457 CB PHE A1114 -17.616 -9.425 90.604 1.00100.55 C ANISOU 2457 CB PHE A1114 13696 14525 9984 11 -871 -848 C ATOM 2458 CG PHE A1114 -16.501 -8.721 89.885 1.00104.11 C ANISOU 2458 CG PHE A1114 14115 14819 10624 -103 -921 -955 C ATOM 2459 CD1 PHE A1114 -16.257 -7.376 90.107 1.00110.51 C ANISOU 2459 CD1 PHE A1114 14958 15481 11550 -140 -882 -1171 C ATOM 2460 CD2 PHE A1114 -15.698 -9.404 88.987 1.00106.16 C ANISOU 2460 CD2 PHE A1114 14313 15067 10957 -181 -985 -847 C ATOM 2461 CE1 PHE A1114 -15.232 -6.725 89.447 1.00112.36 C ANISOU 2461 CE1 PHE A1114 15159 15549 11984 -277 -890 -1266 C ATOM 2462 CE2 PHE A1114 -14.672 -8.758 88.324 1.00109.93 C ANISOU 2462 CE2 PHE A1114 14746 15410 11614 -297 -996 -939 C ATOM 2463 CZ PHE A1114 -14.438 -7.417 88.554 1.00110.11 C ANISOU 2463 CZ PHE A1114 14796 15276 11766 -358 -940 -1143 C ATOM 2464 N THR A1115 -18.722 -9.201 93.994 1.00 94.68 N ANISOU 2464 N THR A1115 13115 14170 8689 273 -785 -1109 N ATOM 2465 CA THR A1115 -19.937 -9.204 94.810 1.00 94.04 C ANISOU 2465 CA THR A1115 13080 14200 8452 394 -633 -1079 C ATOM 2466 C THR A1115 -21.240 -8.413 94.585 1.00 94.24 C ANISOU 2466 C THR A1115 13080 14135 8593 461 -464 -1082 C ATOM 2467 O THR A1115 -22.332 -8.974 94.674 1.00 93.56 O ANISOU 2467 O THR A1115 12952 14140 8457 511 -330 -923 O ATOM 2468 CB THR A1115 -19.637 -8.762 96.258 1.00104.69 C ANISOU 2468 CB THR A1115 14524 15711 9541 495 -665 -1316 C ATOM 2469 OG1 THR A1115 -18.815 -9.744 96.900 1.00101.86 O ANISOU 2469 OG1 THR A1115 14209 15547 8946 526 -788 -1269 O ATOM 2470 CG2 THR A1115 -20.929 -8.596 97.043 1.00106.09 C ANISOU 2470 CG2 THR A1115 14747 15991 9571 628 -472 -1302 C ATOM 2471 N ASN A1116 -21.119 -7.113 94.315 1.00 88.85 N ANISOU 2471 N ASN A1116 12417 13270 8074 465 -460 -1269 N ATOM 2472 CA ASN A1116 -22.251 -6.192 94.351 1.00 88.89 C ANISOU 2472 CA ASN A1116 12425 13197 8153 586 -308 -1326 C ATOM 2473 C ASN A1116 -22.957 -6.496 93.041 1.00 89.99 C ANISOU 2473 C ASN A1116 12458 13248 8484 574 -265 -1089 C ATOM 2474 O ASN A1116 -24.185 -6.606 93.028 1.00 89.75 O ANISOU 2474 O ASN A1116 12352 13297 8451 674 -142 -997 O ATOM 2475 CB ASN A1116 -21.861 -4.718 94.446 1.00 88.85 C ANISOU 2475 CB ASN A1116 12505 12977 8277 602 -307 -1595 C ATOM 2476 CG ASN A1116 -21.458 -4.278 95.833 1.00103.92 C ANISOU 2476 CG ASN A1116 14509 14997 9980 648 -334 -1886 C ATOM 2477 OD1 ASN A1116 -21.798 -4.903 96.844 1.00 91.00 O ANISOU 2477 OD1 ASN A1116 12892 13616 8066 736 -306 -1878 O ATOM 2478 ND2 ASN A1116 -20.762 -3.157 95.911 1.00 98.98 N ANISOU 2478 ND2 ASN A1116 13951 14173 9483 595 -376 -2160 N ATOM 2479 N SER A1117 -22.175 -6.681 91.950 1.00 84.15 N ANISOU 2479 N SER A1117 11699 12377 7899 456 -368 -1000 N ATOM 2480 CA SER A1117 -22.682 -7.008 90.614 1.00 81.85 C ANISOU 2480 CA SER A1117 11318 12019 7761 447 -362 -792 C ATOM 2481 C SER A1117 -23.304 -8.401 90.565 1.00 82.77 C ANISOU 2481 C SER A1117 11333 12327 7788 417 -350 -603 C ATOM 2482 O SER A1117 -24.170 -8.638 89.730 1.00 81.43 O ANISOU 2482 O SER A1117 11057 12168 7713 447 -318 -476 O ATOM 2483 CB SER A1117 -21.580 -6.878 89.567 1.00 84.22 C ANISOU 2483 CB SER A1117 11644 12148 8208 331 -459 -759 C ATOM 2484 OG SER A1117 -21.058 -5.560 89.548 1.00 93.96 O ANISOU 2484 OG SER A1117 12971 13163 9566 331 -433 -926 O ATOM 2485 N LEU A1118 -22.875 -9.312 91.460 1.00 78.62 N ANISOU 2485 N LEU A1118 10842 11949 7081 364 -374 -592 N ATOM 2486 CA LEU A1118 -23.430 -10.658 91.547 1.00 78.14 C ANISOU 2486 CA LEU A1118 10719 12028 6942 321 -325 -413 C ATOM 2487 C LEU A1118 -24.700 -10.671 92.395 1.00 85.03 C ANISOU 2487 C LEU A1118 11543 13044 7719 408 -147 -408 C ATOM 2488 O LEU A1118 -25.547 -11.545 92.192 1.00 85.10 O ANISOU 2488 O LEU A1118 11446 13134 7754 361 -59 -265 O ATOM 2489 CB LEU A1118 -22.409 -11.682 92.067 1.00 77.79 C ANISOU 2489 CB LEU A1118 10760 12053 6745 255 -410 -362 C ATOM 2490 CG LEU A1118 -21.376 -12.214 91.064 1.00 80.67 C ANISOU 2490 CG LEU A1118 11116 12320 7214 155 -555 -295 C ATOM 2491 CD1 LEU A1118 -20.453 -13.211 91.724 1.00 80.86 C ANISOU 2491 CD1 LEU A1118 11222 12433 7067 144 -631 -249 C ATOM 2492 CD2 LEU A1118 -22.044 -12.900 89.880 1.00 83.22 C ANISOU 2492 CD2 LEU A1118 11338 12596 7686 91 -534 -136 C ATOM 2493 N ARG A1119 -24.844 -9.702 93.331 1.00 83.52 N ANISOU 2493 N ARG A1119 11420 12885 7428 525 -82 -580 N ATOM 2494 CA ARG A1119 -26.051 -9.582 94.153 1.00 85.45 C ANISOU 2494 CA ARG A1119 11614 13276 7576 632 111 -596 C ATOM 2495 C ARG A1119 -27.182 -8.995 93.297 1.00 89.30 C ANISOU 2495 C ARG A1119 11938 13720 8272 706 179 -581 C ATOM 2496 O ARG A1119 -28.334 -9.395 93.459 1.00 90.19 O ANISOU 2496 O ARG A1119 11905 13975 8388 733 328 -510 O ATOM 2497 CB ARG A1119 -25.809 -8.756 95.437 1.00 88.76 C ANISOU 2497 CB ARG A1119 12171 13756 7798 754 154 -809 C ATOM 2498 CG ARG A1119 -27.031 -8.704 96.369 1.00103.56 C ANISOU 2498 CG ARG A1119 14001 15810 9536 878 383 -821 C ATOM 2499 CD ARG A1119 -26.698 -8.784 97.848 1.00116.53 C ANISOU 2499 CD ARG A1119 15805 17620 10850 958 440 -920 C ATOM 2500 NE ARG A1119 -26.252 -7.498 98.380 1.00126.33 N ANISOU 2500 NE ARG A1119 17161 18802 12036 1070 381 -1215 N ATOM 2501 CZ ARG A1119 -24.985 -7.202 98.649 1.00141.15 C ANISOU 2501 CZ ARG A1119 19165 20628 13836 1035 192 -1380 C ATOM 2502 NH1 ARG A1119 -24.664 -6.009 99.126 1.00131.50 N ANISOU 2502 NH1 ARG A1119 18033 19335 12595 1114 154 -1681 N ATOM 2503 NH2 ARG A1119 -24.029 -8.104 98.452 1.00125.86 N ANISOU 2503 NH2 ARG A1119 17256 18715 11851 921 40 -1263 N ATOM 2504 N MET A1120 -26.844 -8.087 92.363 1.00 84.87 N ANISOU 2504 N MET A1120 11393 12969 7883 743 76 -638 N ATOM 2505 CA MET A1120 -27.814 -7.473 91.459 1.00 85.02 C ANISOU 2505 CA MET A1120 11281 12942 8079 861 109 -611 C ATOM 2506 C MET A1120 -28.314 -8.445 90.386 1.00 87.11 C ANISOU 2506 C MET A1120 11370 13278 8450 775 60 -436 C ATOM 2507 O MET A1120 -29.459 -8.321 89.954 1.00 87.17 O ANISOU 2507 O MET A1120 11196 13378 8546 874 115 -410 O ATOM 2508 CB MET A1120 -27.268 -6.178 90.853 1.00 87.52 C ANISOU 2508 CB MET A1120 11717 13009 8526 948 41 -706 C ATOM 2509 CG MET A1120 -27.440 -4.983 91.757 1.00 93.73 C ANISOU 2509 CG MET A1120 12612 13726 9275 1101 141 -910 C ATOM 2510 SD MET A1120 -26.049 -3.844 91.621 1.00 98.57 S ANISOU 2510 SD MET A1120 13450 14019 9983 1049 56 -1077 S ATOM 2511 CE MET A1120 -26.590 -2.536 92.721 1.00 98.58 C ANISOU 2511 CE MET A1120 13557 13955 9945 1251 200 -1340 C ATOM 2512 N LEU A1121 -27.480 -9.428 89.981 1.00 82.43 N ANISOU 2512 N LEU A1121 10815 12657 7845 600 -47 -336 N ATOM 2513 CA LEU A1121 -27.884 -10.448 89.004 1.00 81.80 C ANISOU 2513 CA LEU A1121 10586 12637 7858 498 -99 -202 C ATOM 2514 C LEU A1121 -28.793 -11.456 89.702 1.00 88.69 C ANISOU 2514 C LEU A1121 11327 13693 8680 418 48 -148 C ATOM 2515 O LEU A1121 -29.789 -11.896 89.117 1.00 89.29 O ANISOU 2515 O LEU A1121 11190 13871 8866 392 76 -109 O ATOM 2516 CB LEU A1121 -26.678 -11.149 88.342 1.00 79.54 C ANISOU 2516 CB LEU A1121 10398 12244 7581 354 -244 -129 C ATOM 2517 CG LEU A1121 -25.780 -10.290 87.437 1.00 82.62 C ANISOU 2517 CG LEU A1121 10891 12452 8050 395 -363 -155 C ATOM 2518 CD1 LEU A1121 -24.495 -11.001 87.118 1.00 80.62 C ANISOU 2518 CD1 LEU A1121 10730 12126 7774 255 -471 -109 C ATOM 2519 CD2 LEU A1121 -26.488 -9.864 86.164 1.00 84.96 C ANISOU 2519 CD2 LEU A1121 11082 12730 8467 499 -406 -106 C ATOM 2520 N GLN A1122 -28.468 -11.781 90.974 1.00 86.75 N ANISOU 2520 N GLN A1122 11203 13497 8260 387 150 -153 N ATOM 2521 CA GLN A1122 -29.263 -12.668 91.821 1.00 88.83 C ANISOU 2521 CA GLN A1122 11390 13914 8446 319 344 -81 C ATOM 2522 C GLN A1122 -30.620 -11.992 92.070 1.00 96.29 C ANISOU 2522 C GLN A1122 12142 14999 9445 447 502 -157 C ATOM 2523 O GLN A1122 -31.664 -12.619 91.864 1.00 97.39 O ANISOU 2523 O GLN A1122 12057 15260 9687 370 614 -106 O ATOM 2524 CB GLN A1122 -28.517 -12.961 93.145 1.00 90.86 C ANISOU 2524 CB GLN A1122 11869 14199 8453 323 409 -68 C ATOM 2525 CG GLN A1122 -29.394 -13.374 94.342 1.00111.45 C ANISOU 2525 CG GLN A1122 14453 16977 10915 338 672 -20 C ATOM 2526 CD GLN A1122 -29.879 -14.802 94.281 1.00133.30 C ANISOU 2526 CD GLN A1122 17146 19771 13733 154 807 162 C ATOM 2527 OE1 GLN A1122 -29.092 -15.749 94.223 1.00128.99 O ANISOU 2527 OE1 GLN A1122 16739 19132 13140 52 744 282 O ATOM 2528 NE2 GLN A1122 -31.191 -14.991 94.343 1.00126.61 N ANISOU 2528 NE2 GLN A1122 16074 19043 12989 110 1013 179 N ATOM 2529 N GLN A1123 -30.590 -10.695 92.447 1.00 94.20 N ANISOU 2529 N GLN A1123 11950 14708 9133 640 506 -297 N ATOM 2530 CA GLN A1123 -31.780 -9.890 92.726 1.00 96.64 C ANISOU 2530 CA GLN A1123 12100 15136 9482 818 651 -391 C ATOM 2531 C GLN A1123 -32.475 -9.328 91.479 1.00100.67 C ANISOU 2531 C GLN A1123 12412 15634 10204 929 555 -408 C ATOM 2532 O GLN A1123 -33.458 -8.595 91.601 1.00101.80 O ANISOU 2532 O GLN A1123 12409 15876 10396 1118 652 -489 O ATOM 2533 CB GLN A1123 -31.496 -8.818 93.789 1.00 99.46 C ANISOU 2533 CB GLN A1123 12641 15468 9683 990 721 -549 C ATOM 2534 CG GLN A1123 -31.333 -9.405 95.194 1.00120.29 C ANISOU 2534 CG GLN A1123 15401 18237 12065 944 878 -537 C ATOM 2535 CD GLN A1123 -30.624 -8.496 96.173 1.00146.01 C ANISOU 2535 CD GLN A1123 18896 21453 15128 1076 866 -718 C ATOM 2536 OE1 GLN A1123 -30.241 -7.360 95.866 1.00142.77 O ANISOU 2536 OE1 GLN A1123 18565 20882 14799 1184 758 -872 O ATOM 2537 NE2 GLN A1123 -30.414 -8.992 97.387 1.00140.34 N ANISOU 2537 NE2 GLN A1123 18308 20873 14141 1070 978 -709 N ATOM 2538 N LYS A1124 -31.992 -9.726 90.283 1.00 96.25 N ANISOU 2538 N LYS A1124 11843 14975 9752 831 366 -329 N ATOM 2539 CA LYS A1124 -32.534 -9.392 88.952 1.00 96.51 C ANISOU 2539 CA LYS A1124 11708 15015 9946 933 238 -317 C ATOM 2540 C LYS A1124 -32.572 -7.891 88.588 1.00101.55 C ANISOU 2540 C LYS A1124 12429 15530 10626 1209 191 -389 C ATOM 2541 O LYS A1124 -33.465 -7.451 87.860 1.00102.46 O ANISOU 2541 O LYS A1124 12363 15731 10838 1391 156 -395 O ATOM 2542 CB LYS A1124 -33.895 -10.099 88.684 1.00100.59 C ANISOU 2542 CB LYS A1124 11871 15780 10568 892 308 -310 C ATOM 2543 CG LYS A1124 -33.992 -11.555 89.166 1.00114.80 C ANISOU 2543 CG LYS A1124 13598 17665 12355 608 419 -241 C ATOM 2544 CD LYS A1124 -33.338 -12.562 88.223 1.00122.38 C ANISOU 2544 CD LYS A1124 14594 18532 13373 404 254 -160 C ATOM 2545 CE LYS A1124 -34.313 -13.186 87.255 1.00133.28 C ANISOU 2545 CE LYS A1124 15653 20067 14921 327 194 -190 C ATOM 2546 NZ LYS A1124 -35.144 -14.238 87.904 1.00143.28 N ANISOU 2546 NZ LYS A1124 16717 21468 16254 112 403 -184 N ATOM 2547 N ARG A1125 -31.586 -7.123 89.069 1.00 97.83 N ANISOU 2547 N ARG A1125 12231 14852 10086 1243 188 -447 N ATOM 2548 CA ARG A1125 -31.459 -5.694 88.793 1.00 98.98 C ANISOU 2548 CA ARG A1125 12515 14803 10289 1471 172 -516 C ATOM 2549 C ARG A1125 -30.322 -5.735 87.767 1.00101.49 C ANISOU 2549 C ARG A1125 12989 14917 10656 1365 10 -428 C ATOM 2550 O ARG A1125 -29.153 -5.918 88.122 1.00100.02 O ANISOU 2550 O ARG A1125 12978 14609 10417 1198 -24 -450 O ATOM 2551 CB ARG A1125 -31.216 -4.898 90.091 1.00101.61 C ANISOU 2551 CB ARG A1125 13019 15060 10530 1544 303 -680 C ATOM 2552 CG ARG A1125 -32.486 -4.306 90.702 1.00119.84 C ANISOU 2552 CG ARG A1125 15188 17512 12835 1782 467 -776 C ATOM 2553 CD ARG A1125 -33.118 -5.164 91.788 1.00135.00 C ANISOU 2553 CD ARG A1125 16960 19706 14628 1693 627 -795 C ATOM 2554 NE ARG A1125 -32.395 -5.082 93.061 1.00145.36 N ANISOU 2554 NE ARG A1125 18489 20986 15756 1628 704 -907 N ATOM 2555 CZ ARG A1125 -32.853 -5.555 94.218 1.00161.47 C ANISOU 2555 CZ ARG A1125 20483 23235 17631 1609 882 -941 C ATOM 2556 NH1 ARG A1125 -32.128 -5.436 95.322 1.00150.04 N ANISOU 2556 NH1 ARG A1125 19254 21772 15981 1583 920 -1050 N ATOM 2557 NH2 ARG A1125 -34.039 -6.151 94.279 1.00148.94 N ANISOU 2557 NH2 ARG A1125 18626 21890 16077 1617 1027 -871 N ATOM 2558 N TRP A1126 -30.691 -5.584 86.480 1.00 98.37 N ANISOU 2558 N TRP A1126 12513 14514 10349 1479 -89 -330 N ATOM 2559 CA TRP A1126 -29.788 -5.641 85.322 1.00 96.76 C ANISOU 2559 CA TRP A1126 12433 14152 10181 1414 -223 -222 C ATOM 2560 C TRP A1126 -29.091 -4.301 85.131 1.00102.92 C ANISOU 2560 C TRP A1126 13467 14620 11016 1536 -191 -240 C ATOM 2561 O TRP A1126 -27.865 -4.277 85.054 1.00101.50 O ANISOU 2561 O TRP A1126 13461 14260 10846 1372 -218 -238 O ATOM 2562 CB TRP A1126 -30.489 -6.068 84.024 1.00 95.43 C ANISOU 2562 CB TRP A1126 12084 14132 10045 1502 -344 -115 C ATOM 2563 CG TRP A1126 -31.505 -7.154 84.193 1.00 96.49 C ANISOU 2563 CG TRP A1126 11918 14569 10176 1419 -349 -139 C ATOM 2564 CD1 TRP A1126 -32.837 -7.078 83.914 1.00101.67 C ANISOU 2564 CD1 TRP A1126 12307 15449 10875 1596 -355 -167 C ATOM 2565 CD2 TRP A1126 -31.271 -8.473 84.696 1.00 95.00 C ANISOU 2565 CD2 TRP A1126 11660 14481 9957 1134 -332 -141 C ATOM 2566 NE1 TRP A1126 -33.448 -8.275 84.199 1.00101.25 N ANISOU 2566 NE1 TRP A1126 12003 15627 10840 1401 -333 -202 N ATOM 2567 CE2 TRP A1126 -32.510 -9.149 84.688 1.00100.49 C ANISOU 2567 CE2 TRP A1126 12045 15437 10698 1118 -307 -173 C ATOM 2568 CE3 TRP A1126 -30.130 -9.156 85.149 1.00 94.16 C ANISOU 2568 CE3 TRP A1126 11718 14264 9792 900 -332 -118 C ATOM 2569 CZ2 TRP A1126 -32.643 -10.471 85.126 1.00 99.36 C ANISOU 2569 CZ2 TRP A1126 11784 15407 10560 855 -253 -171 C ATOM 2570 CZ3 TRP A1126 -30.264 -10.463 85.589 1.00 95.13 C ANISOU 2570 CZ3 TRP A1126 11740 14510 9895 684 -295 -101 C ATOM 2571 CH2 TRP A1126 -31.505 -11.110 85.565 1.00 97.38 C ANISOU 2571 CH2 TRP A1126 11746 15012 10241 651 -244 -121 C ATOM 2572 N ASP A1127 -29.864 -3.193 85.048 1.00102.34 N ANISOU 2572 N ASP A1127 13413 14477 10996 1823 -122 -263 N ATOM 2573 CA ASP A1127 -29.338 -1.838 84.853 1.00103.55 C ANISOU 2573 CA ASP A1127 13827 14285 11231 1960 -55 -275 C ATOM 2574 C ASP A1127 -28.400 -1.435 85.991 1.00106.52 C ANISOU 2574 C ASP A1127 14382 14478 11613 1791 29 -452 C ATOM 2575 O ASP A1127 -27.377 -0.793 85.743 1.00105.62 O ANISOU 2575 O ASP A1127 14481 14071 11579 1710 49 -465 O ATOM 2576 CB ASP A1127 -30.483 -0.826 84.674 1.00108.69 C ANISOU 2576 CB ASP A1127 14453 14914 11930 2335 12 -271 C ATOM 2577 CG ASP A1127 -31.356 -1.088 83.457 1.00121.21 C ANISOU 2577 CG ASP A1127 15865 16691 13499 2545 -103 -111 C ATOM 2578 OD1 ASP A1127 -30.873 -0.884 82.323 1.00121.69 O ANISOU 2578 OD1 ASP A1127 16061 16611 13566 2593 -171 43 O ATOM 2579 OD2 ASP A1127 -32.529 -1.475 83.641 1.00128.67 O ANISOU 2579 OD2 ASP A1127 16531 17939 14417 2669 -121 -150 O ATOM 2580 N GLU A1128 -28.728 -1.869 87.226 1.00103.20 N ANISOU 2580 N GLU A1128 13865 14250 11099 1727 80 -591 N ATOM 2581 CA GLU A1128 -27.927 -1.639 88.429 1.00103.22 C ANISOU 2581 CA GLU A1128 14004 14166 11048 1584 131 -787 C ATOM 2582 C GLU A1128 -26.631 -2.454 88.373 1.00104.28 C ANISOU 2582 C GLU A1128 14183 14295 11143 1290 23 -765 C ATOM 2583 O GLU A1128 -25.591 -1.984 88.839 1.00103.72 O ANISOU 2583 O GLU A1128 14264 14052 11092 1168 21 -908 O ATOM 2584 CB GLU A1128 -28.739 -1.973 89.686 1.00105.79 C ANISOU 2584 CB GLU A1128 14211 14746 11238 1637 223 -907 C ATOM 2585 CG GLU A1128 -29.725 -0.881 90.069 1.00119.54 C ANISOU 2585 CG GLU A1128 15964 16436 13019 1930 358 -1018 C ATOM 2586 CD GLU A1128 -30.677 -1.221 91.199 1.00139.05 C ANISOU 2586 CD GLU A1128 18286 19193 15355 2010 481 -1115 C ATOM 2587 OE1 GLU A1128 -31.899 -1.013 91.018 1.00131.36 O ANISOU 2587 OE1 GLU A1128 17140 18351 14420 2239 556 -1083 O ATOM 2588 OE2 GLU A1128 -30.209 -1.682 92.265 1.00132.87 O ANISOU 2588 OE2 GLU A1128 17552 18516 14415 1861 507 -1221 O ATOM 2589 N ALA A1129 -26.697 -3.666 87.782 1.00 99.07 N ANISOU 2589 N ALA A1129 13379 13826 10439 1182 -70 -603 N ATOM 2590 CA ALA A1129 -25.546 -4.550 87.587 1.00 96.82 C ANISOU 2590 CA ALA A1129 13118 13552 10119 940 -175 -556 C ATOM 2591 C ALA A1129 -24.697 -4.051 86.413 1.00100.78 C ANISOU 2591 C ALA A1129 13732 13812 10747 903 -220 -475 C ATOM 2592 O ALA A1129 -23.489 -4.273 86.405 1.00 99.18 O ANISOU 2592 O ALA A1129 13596 13532 10556 719 -272 -507 O ATOM 2593 CB ALA A1129 -26.013 -5.972 87.321 1.00 96.01 C ANISOU 2593 CB ALA A1129 12838 13698 9944 858 -235 -421 C ATOM 2594 N ALA A1130 -25.331 -3.367 85.432 1.00 99.18 N ANISOU 2594 N ALA A1130 13549 13502 10631 1095 -189 -365 N ATOM 2595 CA ALA A1130 -24.672 -2.821 84.242 1.00 99.48 C ANISOU 2595 CA ALA A1130 13720 13306 10770 1103 -191 -247 C ATOM 2596 C ALA A1130 -23.675 -1.710 84.579 1.00105.30 C ANISOU 2596 C ALA A1130 14662 13718 11629 1022 -96 -375 C ATOM 2597 O ALA A1130 -22.544 -1.746 84.086 1.00104.30 O ANISOU 2597 O ALA A1130 14606 13458 11565 848 -106 -346 O ATOM 2598 CB ALA A1130 -25.704 -2.327 83.238 1.00101.67 C ANISOU 2598 CB ALA A1130 13985 13573 11070 1383 -179 -95 C ATOM 2599 N VAL A1131 -24.086 -0.739 85.420 1.00104.12 N ANISOU 2599 N VAL A1131 14595 13442 11523 1139 5 -534 N ATOM 2600 CA VAL A1131 -23.238 0.378 85.862 1.00105.89 C ANISOU 2600 CA VAL A1131 15010 13339 11886 1051 105 -713 C ATOM 2601 C VAL A1131 -22.110 -0.183 86.743 1.00108.03 C ANISOU 2601 C VAL A1131 15234 13705 12107 769 26 -903 C ATOM 2602 O VAL A1131 -20.955 0.227 86.599 1.00108.13 O ANISOU 2602 O VAL A1131 15330 13511 12244 580 46 -987 O ATOM 2603 CB VAL A1131 -24.068 1.483 86.590 1.00113.05 C ANISOU 2603 CB VAL A1131 16014 14104 12836 1272 227 -864 C ATOM 2604 CG1 VAL A1131 -23.180 2.613 87.115 1.00115.19 C ANISOU 2604 CG1 VAL A1131 16483 14016 13267 1151 331 -1099 C ATOM 2605 CG2 VAL A1131 -25.163 2.045 85.683 1.00114.40 C ANISOU 2605 CG2 VAL A1131 16223 14195 13051 1598 291 -666 C ATOM 2606 N ASN A1132 -22.456 -1.144 87.621 1.00103.04 N ANISOU 2606 N ASN A1132 14463 13397 11292 749 -58 -960 N ATOM 2607 CA ASN A1132 -21.538 -1.807 88.544 1.00102.17 C ANISOU 2607 CA ASN A1132 14304 13442 11072 550 -154 -1117 C ATOM 2608 C ASN A1132 -20.481 -2.677 87.833 1.00103.43 C ANISOU 2608 C ASN A1132 14401 13653 11246 357 -260 -1002 C ATOM 2609 O ASN A1132 -19.351 -2.780 88.322 1.00103.16 O ANISOU 2609 O ASN A1132 14361 13627 11210 184 -326 -1157 O ATOM 2610 CB ASN A1132 -22.317 -2.614 89.585 1.00103.95 C ANISOU 2610 CB ASN A1132 14431 13986 11081 624 -179 -1148 C ATOM 2611 CG ASN A1132 -21.979 -2.281 91.019 1.00134.71 C ANISOU 2611 CG ASN A1132 18383 17941 14858 600 -179 -1428 C ATOM 2612 OD1 ASN A1132 -22.863 -2.039 91.848 1.00133.25 O ANISOU 2612 OD1 ASN A1132 18206 17857 14567 752 -99 -1518 O ATOM 2613 ND2 ASN A1132 -20.696 -2.287 91.359 1.00127.55 N ANISOU 2613 ND2 ASN A1132 17503 17007 13954 421 -274 -1587 N ATOM 2614 N LEU A1133 -20.843 -3.294 86.689 1.00 97.73 N ANISOU 2614 N LEU A1133 13620 12981 10531 399 -282 -752 N ATOM 2615 CA LEU A1133 -19.904 -4.107 85.913 1.00 95.54 C ANISOU 2615 CA LEU A1133 13293 12744 10266 246 -364 -640 C ATOM 2616 C LEU A1133 -19.016 -3.234 85.015 1.00 99.82 C ANISOU 2616 C LEU A1133 13938 12997 10994 163 -287 -620 C ATOM 2617 O LEU A1133 -17.953 -3.685 84.587 1.00 98.33 O ANISOU 2617 O LEU A1133 13709 12814 10839 3 -330 -600 O ATOM 2618 CB LEU A1133 -20.623 -5.184 85.080 1.00 93.80 C ANISOU 2618 CB LEU A1133 12971 12706 9964 315 -423 -416 C ATOM 2619 CG LEU A1133 -20.960 -6.514 85.766 1.00 97.11 C ANISOU 2619 CG LEU A1133 13271 13403 10223 278 -504 -403 C ATOM 2620 CD1 LEU A1133 -21.826 -7.372 84.868 1.00 96.32 C ANISOU 2620 CD1 LEU A1133 13071 13433 10094 340 -540 -221 C ATOM 2621 CD2 LEU A1133 -19.707 -7.304 86.115 1.00 97.87 C ANISOU 2621 CD2 LEU A1133 13350 13569 10265 111 -597 -453 C ATOM 2622 N ALA A1134 -19.451 -1.989 84.736 1.00 98.38 N ANISOU 2622 N ALA A1134 13892 12552 10938 280 -153 -619 N ATOM 2623 CA ALA A1134 -18.710 -1.027 83.914 1.00 99.79 C ANISOU 2623 CA ALA A1134 14208 12399 11310 210 -23 -579 C ATOM 2624 C ALA A1134 -17.562 -0.370 84.698 1.00105.11 C ANISOU 2624 C ALA A1134 14910 12902 12124 -18 17 -856 C ATOM 2625 O ALA A1134 -16.612 0.134 84.093 1.00105.50 O ANISOU 2625 O ALA A1134 15015 12723 12347 -176 116 -851 O ATOM 2626 CB ALA A1134 -19.654 0.033 83.370 1.00102.56 C ANISOU 2626 CB ALA A1134 14720 12515 11735 451 115 -460 C ATOM 2627 N LYS A1135 -17.651 -0.383 86.042 1.00102.18 N ANISOU 2627 N LYS A1135 14493 12657 11673 -37 -55 -1109 N ATOM 2628 CA LYS A1135 -16.626 0.170 86.935 1.00103.81 C ANISOU 2628 CA LYS A1135 14696 12770 11978 -242 -64 -1433 C ATOM 2629 C LYS A1135 -15.435 -0.793 87.082 1.00106.61 C ANISOU 2629 C LYS A1135 14877 13353 12276 -445 -213 -1498 C ATOM 2630 O LYS A1135 -14.338 -0.358 87.446 1.00107.77 O ANISOU 2630 O LYS A1135 14978 13417 12553 -652 -222 -1741 O ATOM 2631 CB LYS A1135 -17.220 0.473 88.324 1.00107.12 C ANISOU 2631 CB LYS A1135 15138 13284 12279 -144 -100 -1684 C ATOM 2632 CG LYS A1135 -18.185 1.653 88.351 1.00121.78 C ANISOU 2632 CG LYS A1135 17169 14866 14234 44 63 -1709 C ATOM 2633 CD LYS A1135 -17.962 2.536 89.577 1.00134.21 C ANISOU 2633 CD LYS A1135 18816 16330 15849 -6 85 -2097 C ATOM 2634 CE LYS A1135 -18.829 2.160 90.757 1.00144.21 C ANISOU 2634 CE LYS A1135 20046 17892 16857 170 16 -2215 C ATOM 2635 NZ LYS A1135 -18.504 2.980 91.956 1.00155.24 N ANISOU 2635 NZ LYS A1135 21515 19209 18259 118 19 -2627 N ATOM 2636 N SER A1136 -15.672 -2.101 86.804 1.00100.47 N ANISOU 2636 N SER A1136 13995 12864 11316 -379 -329 -1297 N ATOM 2637 CA SER A1136 -14.722 -3.213 86.926 1.00 98.70 C ANISOU 2637 CA SER A1136 13616 12887 10997 -498 -480 -1311 C ATOM 2638 C SER A1136 -13.464 -3.096 86.075 1.00103.06 C ANISOU 2638 C SER A1136 14106 13320 11733 -692 -440 -1304 C ATOM 2639 O SER A1136 -13.479 -2.450 85.026 1.00103.34 O ANISOU 2639 O SER A1136 14232 13100 11933 -711 -280 -1164 O ATOM 2640 CB SER A1136 -15.417 -4.547 86.658 1.00 98.95 C ANISOU 2640 CB SER A1136 13594 13169 10832 -370 -565 -1071 C ATOM 2641 OG SER A1136 -15.704 -4.726 85.282 1.00103.73 O ANISOU 2641 OG SER A1136 14226 13687 11502 -327 -498 -815 O ATOM 2642 N ARG A1137 -12.383 -3.760 86.530 1.00 99.36 N ANISOU 2642 N ARG A1137 13479 13055 11220 -815 -579 -1445 N ATOM 2643 CA ARG A1137 -11.086 -3.810 85.858 1.00 99.59 C ANISOU 2643 CA ARG A1137 13388 13044 11409 -1003 -557 -1471 C ATOM 2644 C ARG A1137 -11.142 -4.701 84.618 1.00101.16 C ANISOU 2644 C ARG A1137 13575 13298 11564 -943 -531 -1161 C ATOM 2645 O ARG A1137 -10.334 -4.524 83.706 1.00101.27 O ANISOU 2645 O ARG A1137 13545 13202 11732 -1066 -427 -1106 O ATOM 2646 CB ARG A1137 -9.992 -4.276 86.837 1.00100.81 C ANISOU 2646 CB ARG A1137 13350 13452 11501 -1102 -744 -1741 C ATOM 2647 CG ARG A1137 -8.870 -3.260 87.060 1.00114.56 C ANISOU 2647 CG ARG A1137 14987 15048 13492 -1348 -695 -2054 C ATOM 2648 CD ARG A1137 -9.321 -1.995 87.781 1.00127.49 C ANISOU 2648 CD ARG A1137 16752 16463 15227 -1386 -618 -2290 C ATOM 2649 NE ARG A1137 -8.808 -0.792 87.118 1.00137.11 N ANISOU 2649 NE ARG A1137 18008 17301 16787 -1604 -394 -2368 N ATOM 2650 CZ ARG A1137 -9.391 0.403 87.161 1.00150.63 C ANISOU 2650 CZ ARG A1137 19915 18667 18652 -1614 -222 -2431 C ATOM 2651 NH1 ARG A1137 -10.525 0.574 87.832 1.00136.13 N ANISOU 2651 NH1 ARG A1137 18230 16842 16652 -1406 -256 -2439 N ATOM 2652 NH2 ARG A1137 -8.851 1.434 86.527 1.00138.69 N ANISOU 2652 NH2 ARG A1137 18452 16782 17463 -1825 7 -2478 N ATOM 2653 N TRP A1138 -12.107 -5.644 84.586 1.00 95.77 N ANISOU 2653 N TRP A1138 12930 12782 10676 -761 -612 -974 N ATOM 2654 CA TRP A1138 -12.376 -6.566 83.478 1.00 93.55 C ANISOU 2654 CA TRP A1138 12651 12569 10325 -681 -611 -708 C ATOM 2655 C TRP A1138 -12.823 -5.756 82.253 1.00 96.78 C ANISOU 2655 C TRP A1138 13191 12732 10850 -644 -431 -529 C ATOM 2656 O TRP A1138 -12.331 -5.986 81.143 1.00 95.39 O ANISOU 2656 O TRP A1138 13008 12522 10714 -675 -365 -388 O ATOM 2657 CB TRP A1138 -13.443 -7.592 83.917 1.00 90.73 C ANISOU 2657 CB TRP A1138 12306 12412 9754 -523 -722 -605 C ATOM 2658 CG TRP A1138 -14.218 -8.247 82.814 1.00 90.47 C ANISOU 2658 CG TRP A1138 12309 12401 9664 -419 -703 -361 C ATOM 2659 CD1 TRP A1138 -13.737 -9.105 81.869 1.00 92.43 C ANISOU 2659 CD1 TRP A1138 12515 12712 9893 -433 -729 -240 C ATOM 2660 CD2 TRP A1138 -15.632 -8.150 82.587 1.00 89.98 C ANISOU 2660 CD2 TRP A1138 12313 12329 9545 -274 -673 -241 C ATOM 2661 NE1 TRP A1138 -14.760 -9.530 81.051 1.00 91.10 N ANISOU 2661 NE1 TRP A1138 12391 12567 9654 -317 -724 -66 N ATOM 2662 CE2 TRP A1138 -15.934 -8.958 81.467 1.00 92.85 C ANISOU 2662 CE2 TRP A1138 12665 12757 9858 -220 -696 -64 C ATOM 2663 CE3 TRP A1138 -16.675 -7.443 83.210 1.00 92.05 C ANISOU 2663 CE3 TRP A1138 12629 12548 9796 -175 -628 -285 C ATOM 2664 CZ2 TRP A1138 -17.236 -9.092 80.970 1.00 91.77 C ANISOU 2664 CZ2 TRP A1138 12544 12661 9662 -82 -697 56 C ATOM 2665 CZ3 TRP A1138 -17.960 -7.560 82.704 1.00 93.11 C ANISOU 2665 CZ3 TRP A1138 12776 12721 9881 -27 -613 -147 C ATOM 2666 CH2 TRP A1138 -18.228 -8.364 81.589 1.00 92.66 C ANISOU 2666 CH2 TRP A1138 12684 12743 9779 14 -656 16 C ATOM 2667 N TYR A1139 -13.721 -4.777 82.486 1.00 94.23 N ANISOU 2667 N TYR A1139 12996 12238 10567 -557 -345 -539 N ATOM 2668 CA TYR A1139 -14.251 -3.855 81.484 1.00 94.94 C ANISOU 2668 CA TYR A1139 13246 12075 10751 -468 -173 -369 C ATOM 2669 C TYR A1139 -13.149 -2.901 81.032 1.00101.27 C ANISOU 2669 C TYR A1139 14091 12606 11779 -651 5 -421 C ATOM 2670 O TYR A1139 -13.080 -2.587 79.848 1.00101.67 O ANISOU 2670 O TYR A1139 14245 12505 11880 -618 152 -216 O ATOM 2671 CB TYR A1139 -15.465 -3.091 82.046 1.00 96.86 C ANISOU 2671 CB TYR A1139 13601 12223 10980 -302 -139 -398 C ATOM 2672 CG TYR A1139 -16.088 -2.089 81.097 1.00100.31 C ANISOU 2672 CG TYR A1139 14221 12395 11498 -152 30 -217 C ATOM 2673 CD1 TYR A1139 -17.048 -2.481 80.170 1.00101.43 C ANISOU 2673 CD1 TYR A1139 14394 12635 11509 67 2 23 C ATOM 2674 CD2 TYR A1139 -15.762 -0.738 81.168 1.00103.95 C ANISOU 2674 CD2 TYR A1139 14830 12505 12163 -211 213 -297 C ATOM 2675 CE1 TYR A1139 -17.639 -1.558 79.307 1.00104.14 C ANISOU 2675 CE1 TYR A1139 14915 12760 11892 258 140 203 C ATOM 2676 CE2 TYR A1139 -16.351 0.195 80.315 1.00106.72 C ANISOU 2676 CE2 TYR A1139 15385 12587 12576 -33 381 -102 C ATOM 2677 CZ TYR A1139 -17.286 -0.221 79.383 1.00113.01 C ANISOU 2677 CZ TYR A1139 16215 13515 13210 220 337 159 C ATOM 2678 OH TYR A1139 -17.863 0.695 78.539 1.00116.24 O ANISOU 2678 OH TYR A1139 16833 13684 13648 442 487 365 O ATOM 2679 N ASN A1140 -12.283 -2.455 81.964 1.00 99.31 N ANISOU 2679 N ASN A1140 13762 12308 11663 -848 -2 -702 N ATOM 2680 CA ASN A1140 -11.162 -1.560 81.657 1.00101.65 C ANISOU 2680 CA ASN A1140 14056 12349 12218 -1081 176 -805 C ATOM 2681 C ASN A1140 -10.109 -2.268 80.793 1.00104.72 C ANISOU 2681 C ASN A1140 14309 12853 12628 -1200 199 -709 C ATOM 2682 O ASN A1140 -9.532 -1.638 79.903 1.00106.43 O ANISOU 2682 O ASN A1140 14584 12837 13016 -1313 422 -614 O ATOM 2683 CB ASN A1140 -10.529 -1.016 82.941 1.00104.06 C ANISOU 2683 CB ASN A1140 14263 12630 12646 -1266 119 -1185 C ATOM 2684 CG ASN A1140 -9.580 0.135 82.711 1.00128.08 C ANISOU 2684 CG ASN A1140 17319 15339 16007 -1526 335 -1332 C ATOM 2685 OD1 ASN A1140 -8.425 -0.047 82.308 1.00121.76 O ANISOU 2685 OD1 ASN A1140 16358 14571 15335 -1732 385 -1379 O ATOM 2686 ND2 ASN A1140 -10.048 1.348 82.963 1.00122.55 N ANISOU 2686 ND2 ASN A1140 16806 14299 15457 -1526 485 -1414 N ATOM 2687 N GLN A1141 -9.874 -3.575 81.052 1.00 98.47 N ANISOU 2687 N GLN A1141 13350 12406 11661 -1161 -11 -724 N ATOM 2688 CA GLN A1141 -8.908 -4.409 80.328 1.00 97.45 C ANISOU 2688 CA GLN A1141 13074 12429 11522 -1233 -17 -654 C ATOM 2689 C GLN A1141 -9.426 -4.771 78.932 1.00 98.64 C ANISOU 2689 C GLN A1141 13355 12553 11569 -1081 79 -330 C ATOM 2690 O GLN A1141 -8.753 -4.479 77.944 1.00 98.98 O ANISOU 2690 O GLN A1141 13414 12478 11715 -1164 266 -223 O ATOM 2691 CB GLN A1141 -8.565 -5.670 81.145 1.00 97.35 C ANISOU 2691 CB GLN A1141 12876 12766 11348 -1199 -274 -777 C ATOM 2692 CG GLN A1141 -7.080 -6.048 81.125 1.00116.95 C ANISOU 2692 CG GLN A1141 15121 15385 13931 -1362 -299 -924 C ATOM 2693 CD GLN A1141 -6.547 -6.495 82.474 1.00134.94 C ANISOU 2693 CD GLN A1141 17218 17909 16142 -1385 -531 -1197 C ATOM 2694 OE1 GLN A1141 -5.432 -6.139 82.875 1.00132.22 O ANISOU 2694 OE1 GLN A1141 16678 17610 15952 -1562 -545 -1445 O ATOM 2695 NE2 GLN A1141 -7.312 -7.298 83.203 1.00124.55 N ANISOU 2695 NE2 GLN A1141 15958 16774 14592 -1203 -714 -1160 N ATOM 2696 N THR A1142 -10.621 -5.392 78.857 1.00 92.51 N ANISOU 2696 N THR A1142 12664 11899 10588 -862 -43 -187 N ATOM 2697 CA THR A1142 -11.272 -5.796 77.606 1.00 90.87 C ANISOU 2697 CA THR A1142 12567 11715 10244 -688 -5 81 C ATOM 2698 C THR A1142 -12.633 -5.078 77.473 1.00 93.93 C ANISOU 2698 C THR A1142 13137 11970 10583 -498 34 203 C ATOM 2699 O THR A1142 -13.656 -5.653 77.849 1.00 91.97 O ANISOU 2699 O THR A1142 12872 11881 10192 -357 -119 214 O ATOM 2700 CB THR A1142 -11.382 -7.341 77.491 1.00 93.84 C ANISOU 2700 CB THR A1142 12837 12387 10432 -608 -197 118 C ATOM 2701 OG1 THR A1142 -11.924 -7.881 78.701 1.00 92.78 O ANISOU 2701 OG1 THR A1142 12636 12399 10216 -575 -377 -7 O ATOM 2702 CG2 THR A1142 -10.054 -8.006 77.152 1.00 89.71 C ANISOU 2702 CG2 THR A1142 12169 11971 9944 -727 -189 71 C ATOM 2703 N PRO A1143 -12.679 -3.824 76.961 1.00 91.55 N ANISOU 2703 N PRO A1143 13006 11371 10406 -485 248 295 N ATOM 2704 CA PRO A1143 -13.971 -3.122 76.864 1.00 91.53 C ANISOU 2704 CA PRO A1143 13174 11248 10355 -259 276 409 C ATOM 2705 C PRO A1143 -14.934 -3.652 75.804 1.00 92.86 C ANISOU 2705 C PRO A1143 13407 11567 10311 -1 209 644 C ATOM 2706 O PRO A1143 -16.141 -3.657 76.047 1.00 91.99 O ANISOU 2706 O PRO A1143 13310 11535 10106 191 108 665 O ATOM 2707 CB PRO A1143 -13.577 -1.659 76.611 1.00 96.55 C ANISOU 2707 CB PRO A1143 13993 11489 11202 -323 544 443 C ATOM 2708 CG PRO A1143 -12.080 -1.597 76.769 1.00102.15 C ANISOU 2708 CG PRO A1143 14584 12129 12097 -635 644 294 C ATOM 2709 CD PRO A1143 -11.577 -2.970 76.482 1.00 95.44 C ANISOU 2709 CD PRO A1143 13549 11611 11104 -669 491 302 C ATOM 2710 N ASN A1144 -14.412 -4.084 74.639 1.00 88.12 N ANISOU 2710 N ASN A1144 12830 11021 9630 8 265 800 N ATOM 2711 CA ASN A1144 -15.239 -4.586 73.536 1.00 86.93 C ANISOU 2711 CA ASN A1144 12740 11033 9256 255 190 997 C ATOM 2712 C ASN A1144 -15.994 -5.870 73.881 1.00 86.78 C ANISOU 2712 C ASN A1144 12551 11334 9088 312 -71 909 C ATOM 2713 O ASN A1144 -17.201 -5.946 73.651 1.00 86.08 O ANISOU 2713 O ASN A1144 12473 11354 8878 522 -174 971 O ATOM 2714 CB ASN A1144 -14.418 -4.735 72.254 1.00 87.75 C ANISOU 2714 CB ASN A1144 12921 11128 9293 247 328 1160 C ATOM 2715 CG ASN A1144 -14.142 -3.444 71.526 1.00110.80 C ANISOU 2715 CG ASN A1144 16077 13735 12287 301 612 1354 C ATOM 2716 OD1 ASN A1144 -14.199 -2.340 72.083 1.00104.64 O ANISOU 2716 OD1 ASN A1144 15399 12672 11687 261 748 1327 O ATOM 2717 ND2 ASN A1144 -13.799 -3.562 70.256 1.00105.43 N ANISOU 2717 ND2 ASN A1144 15507 13084 11468 392 729 1554 N ATOM 2718 N ARG A1145 -15.289 -6.856 74.465 1.00 80.82 N ANISOU 2718 N ARG A1145 11634 10720 8355 127 -170 761 N ATOM 2719 CA ARG A1145 -15.850 -8.139 74.891 1.00 77.98 C ANISOU 2719 CA ARG A1145 11128 10613 7886 139 -381 677 C ATOM 2720 C ARG A1145 -16.809 -7.921 76.063 1.00 81.77 C ANISOU 2720 C ARG A1145 11562 11114 8395 172 -455 576 C ATOM 2721 O ARG A1145 -17.911 -8.473 76.044 1.00 81.49 O ANISOU 2721 O ARG A1145 11466 11237 8260 287 -573 589 O ATOM 2722 CB ARG A1145 -14.724 -9.121 75.267 1.00 74.77 C ANISOU 2722 CB ARG A1145 10598 10304 7506 -42 -434 564 C ATOM 2723 CG ARG A1145 -15.208 -10.456 75.813 1.00 76.34 C ANISOU 2723 CG ARG A1145 10681 10708 7615 -45 -619 487 C ATOM 2724 CD ARG A1145 -14.062 -11.374 76.172 1.00 76.05 C ANISOU 2724 CD ARG A1145 10549 10747 7599 -175 -665 396 C ATOM 2725 NE ARG A1145 -14.539 -12.679 76.631 1.00 75.50 N ANISOU 2725 NE ARG A1145 10411 10829 7446 -164 -812 354 N ATOM 2726 CZ ARG A1145 -13.831 -13.801 76.552 1.00 88.78 C ANISOU 2726 CZ ARG A1145 12041 12593 9097 -202 -873 323 C ATOM 2727 NH1 ARG A1145 -12.606 -13.787 76.043 1.00 77.02 N ANISOU 2727 NH1 ARG A1145 10530 11087 7647 -246 -809 315 N ATOM 2728 NH2 ARG A1145 -14.340 -14.946 76.989 1.00 75.45 N ANISOU 2728 NH2 ARG A1145 10325 10994 7350 -192 -979 300 N ATOM 2729 N ALA A1146 -16.395 -7.099 77.063 1.00 78.13 N ANISOU 2729 N ALA A1146 11118 10497 8071 68 -377 458 N ATOM 2730 CA ALA A1146 -17.186 -6.779 78.258 1.00 77.29 C ANISOU 2730 CA ALA A1146 10983 10400 7985 101 -418 341 C ATOM 2731 C ALA A1146 -18.502 -6.081 77.952 1.00 80.97 C ANISOU 2731 C ALA A1146 11522 10826 8418 328 -392 435 C ATOM 2732 O ALA A1146 -19.506 -6.454 78.550 1.00 80.21 O ANISOU 2732 O ALA A1146 11335 10879 8260 405 -479 386 O ATOM 2733 CB ALA A1146 -16.375 -5.965 79.247 1.00 79.01 C ANISOU 2733 CB ALA A1146 11220 10453 8346 -50 -339 171 C ATOM 2734 N LYS A1147 -18.517 -5.101 77.015 1.00 78.24 N ANISOU 2734 N LYS A1147 11334 10288 8107 450 -263 578 N ATOM 2735 CA LYS A1147 -19.747 -4.398 76.625 1.00 78.93 C ANISOU 2735 CA LYS A1147 11499 10342 8148 723 -245 687 C ATOM 2736 C LYS A1147 -20.782 -5.402 76.104 1.00 79.82 C ANISOU 2736 C LYS A1147 11475 10761 8093 866 -421 740 C ATOM 2737 O LYS A1147 -21.930 -5.360 76.546 1.00 79.87 O ANISOU 2737 O LYS A1147 11393 10881 8072 1005 -486 698 O ATOM 2738 CB LYS A1147 -19.473 -3.286 75.594 1.00 83.87 C ANISOU 2738 CB LYS A1147 12351 10704 8811 850 -68 874 C ATOM 2739 CG LYS A1147 -20.682 -2.384 75.343 1.00103.83 C ANISOU 2739 CG LYS A1147 14987 13159 11305 1170 -38 982 C ATOM 2740 CD LYS A1147 -20.481 -1.454 74.149 1.00119.08 C ANISOU 2740 CD LYS A1147 17171 14856 13219 1349 132 1226 C ATOM 2741 CE LYS A1147 -21.783 -0.923 73.582 1.00131.73 C ANISOU 2741 CE LYS A1147 18849 16505 14697 1749 90 1377 C ATOM 2742 NZ LYS A1147 -22.399 0.125 74.442 1.00140.79 N ANISOU 2742 NZ LYS A1147 20070 17442 15981 1875 175 1305 N ATOM 2743 N ARG A1148 -20.345 -6.342 75.229 1.00 73.38 N ANISOU 2743 N ARG A1148 10620 10084 7178 814 -494 801 N ATOM 2744 CA ARG A1148 -21.168 -7.404 74.641 1.00 71.61 C ANISOU 2744 CA ARG A1148 10261 10141 6808 903 -666 812 C ATOM 2745 C ARG A1148 -21.770 -8.286 75.720 1.00 74.12 C ANISOU 2745 C ARG A1148 10385 10628 7147 794 -773 658 C ATOM 2746 O ARG A1148 -22.952 -8.610 75.642 1.00 74.76 O ANISOU 2746 O ARG A1148 10338 10893 7175 912 -872 637 O ATOM 2747 CB ARG A1148 -20.350 -8.260 73.667 1.00 69.12 C ANISOU 2747 CB ARG A1148 9959 9902 6403 825 -701 860 C ATOM 2748 CG ARG A1148 -20.004 -7.563 72.368 1.00 76.43 C ANISOU 2748 CG ARG A1148 11069 10730 7241 983 -600 1044 C ATOM 2749 CD ARG A1148 -19.270 -8.477 71.398 1.00 77.60 C ANISOU 2749 CD ARG A1148 11221 10990 7273 926 -632 1074 C ATOM 2750 NE ARG A1148 -17.864 -8.108 71.200 1.00 84.74 N ANISOU 2750 NE ARG A1148 12236 11706 8255 783 -444 1130 N ATOM 2751 CZ ARG A1148 -17.444 -7.077 70.464 1.00108.33 C ANISOU 2751 CZ ARG A1148 15419 14507 11236 875 -251 1304 C ATOM 2752 NH1 ARG A1148 -18.317 -6.260 69.884 1.00 98.21 N ANISOU 2752 NH1 ARG A1148 14273 13187 9855 1144 -227 1456 N ATOM 2753 NH2 ARG A1148 -16.147 -6.840 70.326 1.00100.94 N ANISOU 2753 NH2 ARG A1148 14540 13416 10398 703 -66 1330 N ATOM 2754 N VAL A1149 -20.964 -8.649 76.738 1.00 68.80 N ANISOU 2754 N VAL A1149 9687 9903 6550 577 -745 552 N ATOM 2755 CA VAL A1149 -21.382 -9.482 77.872 1.00 67.15 C ANISOU 2755 CA VAL A1149 9339 9827 6346 469 -809 432 C ATOM 2756 C VAL A1149 -22.386 -8.729 78.772 1.00 72.33 C ANISOU 2756 C VAL A1149 9961 10481 7039 573 -763 376 C ATOM 2757 O VAL A1149 -23.455 -9.272 79.058 1.00 72.19 O ANISOU 2757 O VAL A1149 9798 10639 6990 612 -817 342 O ATOM 2758 CB VAL A1149 -20.161 -10.072 78.638 1.00 68.91 C ANISOU 2758 CB VAL A1149 9569 10014 6600 259 -803 353 C ATOM 2759 CG1 VAL A1149 -20.564 -10.677 79.981 1.00 68.08 C ANISOU 2759 CG1 VAL A1149 9377 10011 6480 183 -829 255 C ATOM 2760 CG2 VAL A1149 -19.441 -11.108 77.784 1.00 67.42 C ANISOU 2760 CG2 VAL A1149 9368 9885 6364 185 -866 394 C ATOM 2761 N ILE A1150 -22.052 -7.473 79.171 1.00 69.73 N ANISOU 2761 N ILE A1150 9759 9947 6787 616 -649 355 N ATOM 2762 CA ILE A1150 -22.889 -6.590 80.002 1.00 70.82 C ANISOU 2762 CA ILE A1150 9900 10042 6965 741 -582 287 C ATOM 2763 C ILE A1150 -24.246 -6.312 79.310 1.00 77.80 C ANISOU 2763 C ILE A1150 10715 11035 7808 998 -616 370 C ATOM 2764 O ILE A1150 -25.275 -6.268 79.996 1.00 78.63 O ANISOU 2764 O ILE A1150 10702 11262 7912 1087 -613 300 O ATOM 2765 CB ILE A1150 -22.119 -5.302 80.459 1.00 74.59 C ANISOU 2765 CB ILE A1150 10553 10232 7555 716 -449 224 C ATOM 2766 CG1 ILE A1150 -20.894 -5.663 81.334 1.00 73.64 C ANISOU 2766 CG1 ILE A1150 10433 10083 7463 468 -454 86 C ATOM 2767 CG2 ILE A1150 -23.029 -4.314 81.210 1.00 76.88 C ANISOU 2767 CG2 ILE A1150 10873 10453 7886 884 -369 146 C ATOM 2768 CD1 ILE A1150 -19.797 -4.604 81.401 1.00 80.08 C ANISOU 2768 CD1 ILE A1150 11390 10621 8415 368 -341 16 C ATOM 2769 N THR A1151 -24.250 -6.190 77.957 1.00 75.30 N ANISOU 2769 N THR A1151 10457 10711 7442 1128 -654 512 N ATOM 2770 CA THR A1151 -25.470 -5.979 77.167 1.00 77.19 C ANISOU 2770 CA THR A1151 10620 11099 7611 1404 -726 589 C ATOM 2771 C THR A1151 -26.374 -7.220 77.190 1.00 81.30 C ANISOU 2771 C THR A1151 10874 11942 8076 1356 -871 511 C ATOM 2772 O THR A1151 -27.589 -7.070 77.305 1.00 82.58 O ANISOU 2772 O THR A1151 10876 12267 8233 1526 -909 474 O ATOM 2773 CB THR A1151 -25.152 -5.366 75.786 1.00 86.23 C ANISOU 2773 CB THR A1151 11945 12133 8687 1587 -710 770 C ATOM 2774 OG1 THR A1151 -24.895 -3.973 75.968 1.00 87.74 O ANISOU 2774 OG1 THR A1151 12352 12018 8967 1705 -543 832 O ATOM 2775 CG2 THR A1151 -26.283 -5.521 74.779 1.00 86.12 C ANISOU 2775 CG2 THR A1151 11820 12364 8539 1865 -852 840 C ATOM 2776 N THR A1152 -25.781 -8.433 77.149 1.00 76.53 N ANISOU 2776 N THR A1152 10213 11416 7450 1119 -934 473 N ATOM 2777 CA THR A1152 -26.516 -9.703 77.221 1.00 76.49 C ANISOU 2777 CA THR A1152 9976 11658 7427 1015 -1041 387 C ATOM 2778 C THR A1152 -27.209 -9.827 78.590 1.00 81.91 C ANISOU 2778 C THR A1152 10528 12412 8182 944 -968 284 C ATOM 2779 O THR A1152 -28.327 -10.336 78.668 1.00 82.48 O ANISOU 2779 O THR A1152 10375 12695 8269 961 -1012 220 O ATOM 2780 CB THR A1152 -25.585 -10.901 76.962 1.00 83.69 C ANISOU 2780 CB THR A1152 10914 12567 8316 785 -1091 375 C ATOM 2781 OG1 THR A1152 -24.573 -10.555 76.014 1.00 82.73 O ANISOU 2781 OG1 THR A1152 10974 12317 8142 824 -1086 472 O ATOM 2782 CG2 THR A1152 -26.341 -12.135 76.490 1.00 82.86 C ANISOU 2782 CG2 THR A1152 10610 12683 8191 716 -1217 301 C ATOM 2783 N PHE A1153 -26.545 -9.335 79.657 1.00 78.85 N ANISOU 2783 N PHE A1153 10271 11858 7832 866 -849 257 N ATOM 2784 CA PHE A1153 -27.067 -9.327 81.022 1.00 79.28 C ANISOU 2784 CA PHE A1153 10246 11963 7912 823 -755 166 C ATOM 2785 C PHE A1153 -28.200 -8.323 81.181 1.00 86.86 C ANISOU 2785 C PHE A1153 11129 12974 8899 1068 -703 140 C ATOM 2786 O PHE A1153 -29.101 -8.546 81.992 1.00 88.17 O ANISOU 2786 O PHE A1153 11131 13290 9078 1071 -644 66 O ATOM 2787 CB PHE A1153 -25.956 -8.992 82.029 1.00 79.90 C ANISOU 2787 CB PHE A1153 10501 11865 7991 704 -671 120 C ATOM 2788 CG PHE A1153 -25.097 -10.153 82.460 1.00 79.42 C ANISOU 2788 CG PHE A1153 10458 11825 7892 476 -700 111 C ATOM 2789 CD1 PHE A1153 -25.673 -11.339 82.908 1.00 82.02 C ANISOU 2789 CD1 PHE A1153 10653 12316 8197 365 -700 102 C ATOM 2790 CD2 PHE A1153 -23.714 -10.039 82.486 1.00 80.25 C ANISOU 2790 CD2 PHE A1153 10713 11783 7996 377 -711 107 C ATOM 2791 CE1 PHE A1153 -24.877 -12.405 83.332 1.00 81.67 C ANISOU 2791 CE1 PHE A1153 10659 12262 8110 191 -715 115 C ATOM 2792 CE2 PHE A1153 -22.919 -11.103 82.915 1.00 81.69 C ANISOU 2792 CE2 PHE A1153 10907 11998 8132 212 -748 100 C ATOM 2793 CZ PHE A1153 -23.505 -12.279 83.337 1.00 79.57 C ANISOU 2793 CZ PHE A1153 10541 11870 7824 135 -750 115 C ATOM 2794 N ARG A1154 -28.136 -7.209 80.435 1.00 84.35 N ANISOU 2794 N ARG A1154 10940 12520 8589 1286 -705 210 N ATOM 2795 CA ARG A1154 -29.128 -6.144 80.494 1.00 86.68 C ANISOU 2795 CA ARG A1154 11199 12824 8909 1575 -656 202 C ATOM 2796 C ARG A1154 -30.351 -6.491 79.637 1.00 92.72 C ANISOU 2796 C ARG A1154 11720 13867 9644 1754 -780 221 C ATOM 2797 O ARG A1154 -31.449 -6.632 80.178 1.00 93.43 O ANISOU 2797 O ARG A1154 11576 14161 9762 1818 -759 132 O ATOM 2798 CB ARG A1154 -28.483 -4.803 80.093 1.00 87.59 C ANISOU 2798 CB ARG A1154 11593 12631 9056 1735 -582 282 C ATOM 2799 CG ARG A1154 -29.393 -3.574 80.151 1.00100.78 C ANISOU 2799 CG ARG A1154 13290 14240 10761 2073 -512 288 C ATOM 2800 CD ARG A1154 -28.658 -2.297 79.763 1.00112.55 C ANISOU 2800 CD ARG A1154 15099 15360 12307 2195 -405 380 C ATOM 2801 NE ARG A1154 -27.815 -2.465 78.575 1.00122.32 N ANISOU 2801 NE ARG A1154 16476 16502 13499 2142 -451 538 N ATOM 2802 CZ ARG A1154 -28.219 -2.281 77.321 1.00138.28 C ANISOU 2802 CZ ARG A1154 18524 18583 15431 2392 -525 701 C ATOM 2803 NH1 ARG A1154 -27.381 -2.466 76.312 1.00123.97 N ANISOU 2803 NH1 ARG A1154 16853 16691 13557 2330 -542 838 N ATOM 2804 NH2 ARG A1154 -29.470 -1.908 77.067 1.00127.02 N ANISOU 2804 NH2 ARG A1154 16980 17321 13963 2728 -583 724 N ATOM 2805 N THR A1155 -30.148 -6.653 78.316 1.00 90.05 N ANISOU 2805 N THR A1155 11419 13557 9238 1830 -908 321 N ATOM 2806 CA THR A1155 -31.194 -6.947 77.329 1.00 91.82 C ANISOU 2806 CA THR A1155 11423 14063 9401 2023 -1069 322 C ATOM 2807 C THR A1155 -31.863 -8.309 77.520 1.00 96.15 C ANISOU 2807 C THR A1155 11653 14898 9980 1808 -1152 187 C ATOM 2808 O THR A1155 -33.092 -8.394 77.476 1.00 98.08 O ANISOU 2808 O THR A1155 11612 15405 10250 1937 -1212 101 O ATOM 2809 CB THR A1155 -30.674 -6.762 75.883 1.00 98.82 C ANISOU 2809 CB THR A1155 12477 14903 10167 2165 -1176 463 C ATOM 2810 OG1 THR A1155 -29.656 -7.727 75.606 1.00 94.51 O ANISOU 2810 OG1 THR A1155 12006 14308 9596 1877 -1207 466 O ATOM 2811 CG2 THR A1155 -30.159 -5.349 75.613 1.00 98.64 C ANISOU 2811 CG2 THR A1155 12769 14579 10130 2399 -1060 620 C ATOM 2812 N GLY A1156 -31.054 -9.348 77.718 1.00 90.70 N ANISOU 2812 N GLY A1156 11011 14150 9302 1488 -1147 166 N ATOM 2813 CA GLY A1156 -31.530 -10.717 77.876 1.00 90.60 C ANISOU 2813 CA GLY A1156 10754 14333 9338 1245 -1196 52 C ATOM 2814 C GLY A1156 -31.671 -11.430 76.550 1.00 96.00 C ANISOU 2814 C GLY A1156 11340 15176 9959 1250 -1392 22 C ATOM 2815 O GLY A1156 -32.279 -12.501 76.480 1.00 96.16 O ANISOU 2815 O GLY A1156 11119 15379 10039 1077 -1456 -104 O ATOM 2816 N THR A1157 -31.112 -10.817 75.487 1.00 93.68 N ANISOU 2816 N THR A1157 11244 14807 9543 1448 -1475 133 N ATOM 2817 CA THR A1157 -31.101 -11.305 74.104 1.00 94.58 C ANISOU 2817 CA THR A1157 11332 15067 9536 1517 -1664 121 C ATOM 2818 C THR A1157 -29.657 -11.386 73.594 1.00 97.22 C ANISOU 2818 C THR A1157 11975 15174 9788 1433 -1631 239 C ATOM 2819 O THR A1157 -28.747 -10.844 74.223 1.00 95.36 O ANISOU 2819 O THR A1157 11956 14681 9595 1371 -1476 334 O ATOM 2820 CB THR A1157 -31.974 -10.409 73.203 1.00104.86 C ANISOU 2820 CB THR A1157 12562 16557 10722 1918 -1793 159 C ATOM 2821 OG1 THR A1157 -31.582 -9.047 73.359 1.00104.67 O ANISOU 2821 OG1 THR A1157 12798 16303 10670 2151 -1665 334 O ATOM 2822 CG2 THR A1157 -33.464 -10.565 73.477 1.00105.31 C ANISOU 2822 CG2 THR A1157 12231 16926 10857 1997 -1874 -3 C ATOM 2823 N TRP A1158 -29.452 -12.046 72.449 1.00 94.96 N ANISOU 2823 N TRP A1158 11694 15001 9386 1437 -1776 211 N ATOM 2824 CA TRP A1158 -28.126 -12.236 71.851 1.00 93.65 C ANISOU 2824 CA TRP A1158 11786 14665 9133 1365 -1742 306 C ATOM 2825 C TRP A1158 -27.798 -11.210 70.768 1.00 99.02 C ANISOU 2825 C TRP A1158 12682 15304 9635 1671 -1748 481 C ATOM 2826 O TRP A1158 -26.808 -11.376 70.047 1.00 97.88 O ANISOU 2826 O TRP A1158 12728 15071 9391 1645 -1723 558 O ATOM 2827 CB TRP A1158 -28.009 -13.650 71.274 1.00 92.30 C ANISOU 2827 CB TRP A1158 11520 14618 8933 1177 -1869 162 C ATOM 2828 CG TRP A1158 -28.381 -14.734 72.233 1.00 92.81 C ANISOU 2828 CG TRP A1158 11392 14698 9172 880 -1845 9 C ATOM 2829 CD1 TRP A1158 -29.639 -15.102 72.609 1.00 97.42 C ANISOU 2829 CD1 TRP A1158 11682 15476 9857 831 -1900 -137 C ATOM 2830 CD2 TRP A1158 -27.481 -15.596 72.935 1.00 90.50 C ANISOU 2830 CD2 TRP A1158 11193 14218 8975 600 -1741 0 C ATOM 2831 NE1 TRP A1158 -29.581 -16.181 73.457 1.00 96.23 N ANISOU 2831 NE1 TRP A1158 11457 15248 9859 518 -1818 -225 N ATOM 2832 CE2 TRP A1158 -28.267 -16.489 73.697 1.00 95.24 C ANISOU 2832 CE2 TRP A1158 11579 14885 9721 392 -1726 -133 C ATOM 2833 CE3 TRP A1158 -26.082 -15.696 73.004 1.00 89.54 C ANISOU 2833 CE3 TRP A1158 11306 13884 8830 516 -1653 95 C ATOM 2834 CZ2 TRP A1158 -27.701 -17.475 74.510 1.00 93.06 C ANISOU 2834 CZ2 TRP A1158 11359 14451 9547 128 -1624 -149 C ATOM 2835 CZ3 TRP A1158 -25.524 -16.667 73.815 1.00 89.60 C ANISOU 2835 CZ3 TRP A1158 11337 13768 8938 270 -1580 57 C ATOM 2836 CH2 TRP A1158 -26.329 -17.559 74.536 1.00 90.82 C ANISOU 2836 CH2 TRP A1158 11317 13974 9216 91 -1567 -52 C ATOM 2837 N ASP A1159 -28.617 -10.146 70.665 1.00 97.80 N ANISOU 2837 N ASP A1159 12511 15208 9442 1974 -1760 554 N ATOM 2838 CA ASP A1159 -28.495 -9.055 69.687 1.00 99.48 C ANISOU 2838 CA ASP A1159 12948 15372 9480 2323 -1746 754 C ATOM 2839 C ASP A1159 -27.108 -8.390 69.627 1.00101.94 C ANISOU 2839 C ASP A1159 13601 15334 9799 2266 -1529 945 C ATOM 2840 O ASP A1159 -26.729 -7.870 68.576 1.00102.89 O ANISOU 2840 O ASP A1159 13935 15413 9745 2478 -1502 1116 O ATOM 2841 CB ASP A1159 -29.619 -8.024 69.885 1.00103.83 C ANISOU 2841 CB ASP A1159 13419 15996 10036 2651 -1765 795 C ATOM 2842 CG ASP A1159 -31.020 -8.614 69.858 1.00114.81 C ANISOU 2842 CG ASP A1159 14427 17771 11426 2727 -1978 595 C ATOM 2843 OD1 ASP A1159 -31.287 -9.479 68.993 1.00116.02 O ANISOU 2843 OD1 ASP A1159 14440 18190 11454 2719 -2177 480 O ATOM 2844 OD2 ASP A1159 -31.857 -8.194 70.686 1.00120.87 O ANISOU 2844 OD2 ASP A1159 15024 18582 12321 2796 -1943 536 O ATOM 2845 N ALA A1160 -26.332 -8.473 70.729 1.00 96.40 N ANISOU 2845 N ALA A1160 12939 14402 9287 1972 -1376 906 N ATOM 2846 CA ALA A1160 -24.966 -7.952 70.841 1.00 95.25 C ANISOU 2846 CA ALA A1160 13049 13942 9199 1846 -1173 1026 C ATOM 2847 C ALA A1160 -23.952 -8.800 70.037 1.00 98.50 C ANISOU 2847 C ALA A1160 13531 14379 9513 1704 -1187 1038 C ATOM 2848 O ALA A1160 -22.770 -8.445 69.973 1.00 97.65 O ANISOU 2848 O ALA A1160 13606 14049 9447 1598 -1019 1132 O ATOM 2849 CB ALA A1160 -24.558 -7.901 72.307 1.00 93.95 C ANISOU 2849 CB ALA A1160 12849 13601 9245 1590 -1059 927 C ATOM 2850 N TYR A1161 -24.419 -9.911 69.427 1.00 94.88 N ANISOU 2850 N TYR A1161 12917 14194 8938 1698 -1379 923 N ATOM 2851 CA TYR A1161 -23.600 -10.839 68.646 1.00108.94 C ANISOU 2851 CA TYR A1161 14746 16031 10615 1588 -1413 896 C ATOM 2852 C TYR A1161 -24.245 -11.129 67.296 1.00137.48 C ANISOU 2852 C TYR A1161 18340 19917 13977 1833 -1592 888 C ATOM 2853 O TYR A1161 -23.550 -11.498 66.353 1.00 98.50 O ANISOU 2853 O TYR A1161 13525 15016 8884 1855 -1585 925 O ATOM 2854 CB TYR A1161 -23.387 -12.147 69.431 1.00107.35 C ANISOU 2854 CB TYR A1161 14378 15860 10550 1274 -1469 704 C ATOM 2855 CG TYR A1161 -22.710 -11.952 70.772 1.00106.42 C ANISOU 2855 CG TYR A1161 14280 15519 10635 1055 -1320 699 C ATOM 2856 CD1 TYR A1161 -21.322 -11.941 70.880 1.00107.11 C ANISOU 2856 CD1 TYR A1161 14501 15427 10771 912 -1185 749 C ATOM 2857 CD2 TYR A1161 -23.456 -11.797 71.937 1.00106.52 C ANISOU 2857 CD2 TYR A1161 14162 15530 10781 1000 -1318 627 C ATOM 2858 CE1 TYR A1161 -20.693 -11.753 72.109 1.00106.25 C ANISOU 2858 CE1 TYR A1161 14392 15151 10828 729 -1080 716 C ATOM 2859 CE2 TYR A1161 -22.839 -11.602 73.172 1.00105.68 C ANISOU 2859 CE2 TYR A1161 14086 15247 10821 826 -1197 608 C ATOM 2860 CZ TYR A1161 -21.456 -11.583 73.252 1.00111.44 C ANISOU 2860 CZ TYR A1161 14945 15812 11586 694 -1093 645 C ATOM 2861 OH TYR A1161 -20.839 -11.409 74.464 1.00111.51 O ANISOU 2861 OH TYR A1161 14963 15686 11719 536 -1006 597 O ATOM 2862 N HIS A 232 -33.239 -12.638 63.283 1.00152.47 N ANISOU 2862 N HIS A 232 23824 19538 14571 -3025 827 1534 N ATOM 2863 CA HIS A 232 -34.548 -12.127 62.741 1.00152.27 C ANISOU 2863 CA HIS A 232 23533 19661 14664 -2922 1175 1446 C ATOM 2864 C HIS A 232 -35.179 -10.878 62.213 1.00154.36 C ANISOU 2864 C HIS A 232 23603 20030 15016 -2755 1404 1350 C ATOM 2865 O HIS A 232 -36.227 -10.943 61.569 1.00154.12 O ANISOU 2865 O HIS A 232 23275 20136 15147 -2676 1614 1306 O ATOM 2866 CB HIS A 232 -35.137 -12.353 64.110 1.00156.04 C ANISOU 2866 CB HIS A 232 24373 20038 14875 -3109 1386 1462 C ATOM 2867 CG HIS A 232 -36.150 -13.456 64.137 1.00160.66 C ANISOU 2867 CG HIS A 232 24857 20682 15505 -3215 1555 1486 C ATOM 2868 ND1 HIS A 232 -36.841 -13.859 63.014 1.00161.27 N ANISOU 2868 ND1 HIS A 232 24516 20917 15843 -3120 1621 1463 N ATOM 2869 CD2 HIS A 232 -36.589 -14.239 65.150 1.00164.78 C ANISOU 2869 CD2 HIS A 232 25652 21124 15834 -3425 1666 1536 C ATOM 2870 CE1 HIS A 232 -37.661 -14.844 63.335 1.00162.19 C ANISOU 2870 CE1 HIS A 232 24644 21049 15933 -3272 1760 1499 C ATOM 2871 NE2 HIS A 232 -37.528 -15.093 64.625 1.00164.76 N ANISOU 2871 NE2 HIS A 232 25384 21234 15985 -3459 1797 1545 N ATOM 2872 N GLN A 233 -34.579 -9.727 62.503 1.00149.11 N ANISOU 2872 N GLN A 233 23115 19296 14243 -2705 1361 1320 N ATOM 2873 CA GLN A 233 -35.163 -8.430 62.049 1.00147.76 C ANISOU 2873 CA GLN A 233 22803 19197 14142 -2535 1574 1226 C ATOM 2874 C GLN A 233 -34.165 -8.081 60.944 1.00146.74 C ANISOU 2874 C GLN A 233 22457 19112 14185 -2415 1284 1240 C ATOM 2875 O GLN A 233 -34.585 -7.492 59.944 1.00145.05 O ANISOU 2875 O GLN A 233 21947 19011 14153 -2251 1361 1188 O ATOM 2876 CB GLN A 233 -35.217 -7.318 63.135 1.00151.10 C ANISOU 2876 CB GLN A 233 23606 19494 14309 -2564 1740 1174 C ATOM 2877 CG GLN A 233 -36.596 -7.187 63.792 1.00168.51 C ANISOU 2877 CG GLN A 233 25873 21727 16426 -2574 2159 1109 C ATOM 2878 CD GLN A 233 -37.592 -6.351 63.010 1.00185.81 C ANISOU 2878 CD GLN A 233 27747 24048 18805 -2360 2413 1019 C ATOM 2879 OE1 GLN A 233 -37.367 -5.950 61.857 1.00178.71 O ANISOU 2879 OE1 GLN A 233 26552 23231 18119 -2204 2280 1007 O ATOM 2880 NE2 GLN A 233 -38.729 -6.065 63.631 1.00178.78 N ANISOU 2880 NE2 GLN A 233 26913 23179 17835 -2345 2788 953 N ATOM 2881 N LYS A 234 -32.881 -8.472 61.089 1.00140.87 N ANISOU 2881 N LYS A 234 21842 18288 13393 -2495 955 1313 N ATOM 2882 CA LYS A 234 -31.809 -8.278 60.055 1.00137.68 C ANISOU 2882 CA LYS A 234 21222 17938 13153 -2401 666 1336 C ATOM 2883 C LYS A 234 -31.998 -9.237 58.907 1.00137.61 C ANISOU 2883 C LYS A 234 20839 18059 13388 -2325 600 1348 C ATOM 2884 O LYS A 234 -31.440 -9.001 57.830 1.00135.45 O ANISOU 2884 O LYS A 234 20317 17868 13279 -2214 451 1343 O ATOM 2885 CB LYS A 234 -30.464 -8.457 60.733 1.00140.66 C ANISOU 2885 CB LYS A 234 21862 18190 13393 -2522 360 1414 C ATOM 2886 N ARG A 235 -32.766 -10.329 59.122 1.00132.87 N ANISOU 2886 N ARG A 235 20211 17472 12801 -2397 708 1364 N ATOM 2887 CA ARG A 235 -33.088 -11.342 58.118 1.00130.50 C ANISOU 2887 CA ARG A 235 19595 17277 12711 -2349 662 1373 C ATOM 2888 C ARG A 235 -34.046 -10.769 57.070 1.00130.57 C ANISOU 2888 C ARG A 235 19272 17438 12902 -2202 854 1302 C ATOM 2889 O ARG A 235 -33.883 -11.055 55.882 1.00128.58 O ANISOU 2889 O ARG A 235 18732 17282 12841 -2106 739 1296 O ATOM 2890 CB ARG A 235 -33.692 -12.597 58.780 1.00132.53 C ANISOU 2890 CB ARG A 235 19969 17485 12901 -2500 732 1415 C ATOM 2891 CG ARG A 235 -32.663 -13.623 59.246 1.00143.50 C ANISOU 2891 CG ARG A 235 21553 18750 14219 -2605 443 1500 C ATOM 2892 CD ARG A 235 -32.140 -14.471 58.095 1.00151.77 C ANISOU 2892 CD ARG A 235 22329 19856 15481 -2516 221 1515 C ATOM 2893 NE ARG A 235 -32.094 -15.892 58.436 1.00160.55 N ANISOU 2893 NE ARG A 235 23554 20879 16571 -2628 105 1579 N ATOM 2894 CZ ARG A 235 -31.055 -16.501 58.999 1.00175.53 C ANISOU 2894 CZ ARG A 235 25665 22642 18387 -2687 -160 1651 C ATOM 2895 NH1 ARG A 235 -29.959 -15.815 59.303 1.00163.29 N ANISOU 2895 NH1 ARG A 235 24226 21044 16774 -2658 -338 1672 N ATOM 2896 NH2 ARG A 235 -31.106 -17.797 59.271 1.00163.12 N ANISOU 2896 NH2 ARG A 235 24202 20977 16799 -2781 -258 1707 N ATOM 2897 N LYS A 236 -35.025 -9.937 57.512 1.00125.88 N ANISOU 2897 N LYS A 236 18727 16860 12242 -2177 1143 1248 N ATOM 2898 CA LYS A 236 -36.004 -9.269 56.645 1.00123.85 C ANISOU 2898 CA LYS A 236 18174 16735 12149 -2026 1335 1184 C ATOM 2899 C LYS A 236 -35.312 -8.293 55.699 1.00121.97 C ANISOU 2899 C LYS A 236 17804 16532 12007 -1879 1189 1161 C ATOM 2900 O LYS A 236 -35.777 -8.101 54.577 1.00120.06 O ANISOU 2900 O LYS A 236 17257 16410 11951 -1755 1212 1133 O ATOM 2901 CB LYS A 236 -37.083 -8.550 57.471 1.00128.58 C ANISOU 2901 CB LYS A 236 18890 17324 12642 -2019 1671 1130 C ATOM 2902 CG LYS A 236 -38.171 -9.478 58.006 1.00145.10 C ANISOU 2902 CG LYS A 236 20961 19456 14716 -2136 1888 1142 C ATOM 2903 CD LYS A 236 -39.340 -8.709 58.619 1.00157.60 C ANISOU 2903 CD LYS A 236 22573 21067 16240 -2091 2256 1077 C ATOM 2904 CE LYS A 236 -39.234 -8.570 60.122 1.00170.76 C ANISOU 2904 CE LYS A 236 24667 22593 17619 -2228 2390 1076 C ATOM 2905 NZ LYS A 236 -40.353 -7.764 60.684 1.00180.90 N ANISOU 2905 NZ LYS A 236 25978 23908 18848 -2160 2771 999 N ATOM 2906 N ALA A 237 -34.187 -7.702 56.155 1.00115.96 N ANISOU 2906 N ALA A 237 17281 15666 11113 -1910 1026 1179 N ATOM 2907 CA ALA A 237 -33.347 -6.779 55.387 1.00113.06 C ANISOU 2907 CA ALA A 237 16837 15316 10804 -1812 863 1171 C ATOM 2908 C ALA A 237 -32.580 -7.540 54.303 1.00111.42 C ANISOU 2908 C ALA A 237 16385 15190 10758 -1785 618 1208 C ATOM 2909 O ALA A 237 -32.393 -7.011 53.208 1.00109.69 O ANISOU 2909 O ALA A 237 15951 15056 10669 -1674 558 1189 O ATOM 2910 CB ALA A 237 -32.376 -6.062 56.312 1.00114.52 C ANISOU 2910 CB ALA A 237 17364 15363 10787 -1893 753 1192 C ATOM 2911 N LEU A 238 -32.154 -8.784 54.610 1.00105.34 N ANISOU 2911 N LEU A 238 15662 14386 9975 -1884 483 1259 N ATOM 2912 CA LEU A 238 -31.447 -9.669 53.687 1.00102.58 C ANISOU 2912 CA LEU A 238 15107 14097 9770 -1854 264 1288 C ATOM 2913 C LEU A 238 -32.384 -10.164 52.568 1.00103.79 C ANISOU 2913 C LEU A 238 14947 14378 10110 -1771 360 1252 C ATOM 2914 O LEU A 238 -31.961 -10.208 51.415 1.00102.35 O ANISOU 2914 O LEU A 238 14542 14280 10065 -1682 239 1242 O ATOM 2915 CB LEU A 238 -30.800 -10.844 54.455 1.00103.08 C ANISOU 2915 CB LEU A 238 15350 14061 9756 -1974 99 1351 C ATOM 2916 CG LEU A 238 -30.108 -11.953 53.644 1.00106.48 C ANISOU 2916 CG LEU A 238 15602 14527 10327 -1937 -118 1377 C ATOM 2917 CD1 LEU A 238 -28.817 -11.465 53.002 1.00105.53 C ANISOU 2917 CD1 LEU A 238 15379 14447 10269 -1862 -329 1388 C ATOM 2918 CD2 LEU A 238 -29.830 -13.162 54.508 1.00109.74 C ANISOU 2918 CD2 LEU A 238 16215 14822 10659 -2052 -232 1437 C ATOM 2919 N LYS A 239 -33.647 -10.512 52.900 1.00 99.46 N ANISOU 2919 N LYS A 239 14381 13847 9563 -1808 576 1235 N ATOM 2920 CA LYS A 239 -34.632 -10.982 51.920 1.00 98.26 C ANISOU 2920 CA LYS A 239 13938 13815 9583 -1753 664 1209 C ATOM 2921 C LYS A 239 -35.109 -9.866 50.994 1.00100.48 C ANISOU 2921 C LYS A 239 14008 14198 9973 -1607 751 1161 C ATOM 2922 O LYS A 239 -35.368 -10.131 49.821 1.00 99.31 O ANISOU 2922 O LYS A 239 13603 14151 9981 -1537 702 1147 O ATOM 2923 CB LYS A 239 -35.813 -11.692 52.593 1.00102.49 C ANISOU 2923 CB LYS A 239 14506 14348 10088 -1857 863 1216 C ATOM 2924 CG LYS A 239 -36.267 -12.931 51.826 1.00121.16 C ANISOU 2924 CG LYS A 239 16669 16775 12592 -1891 807 1228 C ATOM 2925 CD LYS A 239 -37.341 -13.734 52.562 1.00135.79 C ANISOU 2925 CD LYS A 239 18574 18619 14402 -2034 984 1250 C ATOM 2926 CE LYS A 239 -38.717 -13.565 51.952 1.00147.31 C ANISOU 2926 CE LYS A 239 19750 20218 16003 -1995 1180 1219 C ATOM 2927 NZ LYS A 239 -39.697 -14.533 52.518 1.00156.70 N ANISOU 2927 NZ LYS A 239 20950 21414 17173 -2160 1324 1250 N ATOM 2928 N THR A 240 -35.186 -8.617 51.503 1.00 96.79 N ANISOU 2928 N THR A 240 13669 13691 9414 -1561 865 1136 N ATOM 2929 CA THR A 240 -35.569 -7.428 50.722 1.00 95.77 C ANISOU 2929 CA THR A 240 13389 13628 9370 -1415 934 1095 C ATOM 2930 C THR A 240 -34.474 -7.159 49.672 1.00 96.08 C ANISOU 2930 C THR A 240 13329 13702 9474 -1358 703 1107 C ATOM 2931 O THR A 240 -34.764 -6.751 48.545 1.00 94.82 O ANISOU 2931 O THR A 240 12952 13634 9443 -1253 691 1087 O ATOM 2932 CB THR A 240 -35.803 -6.223 51.662 1.00106.55 C ANISOU 2932 CB THR A 240 14981 14906 10597 -1389 1100 1065 C ATOM 2933 OG1 THR A 240 -36.737 -6.590 52.680 1.00108.40 O ANISOU 2933 OG1 THR A 240 15318 15113 10756 -1457 1324 1054 O ATOM 2934 CG2 THR A 240 -36.320 -4.989 50.931 1.00105.73 C ANISOU 2934 CG2 THR A 240 14743 14848 10580 -1227 1183 1023 C ATOM 2935 N THR A 241 -33.224 -7.444 50.048 1.00 90.81 N ANISOU 2935 N THR A 241 12816 12966 8720 -1434 518 1143 N ATOM 2936 CA THR A 241 -32.043 -7.308 49.208 1.00 88.43 C ANISOU 2936 CA THR A 241 12431 12701 8466 -1403 303 1160 C ATOM 2937 C THR A 241 -32.059 -8.378 48.106 1.00 88.65 C ANISOU 2937 C THR A 241 12211 12826 8645 -1371 211 1158 C ATOM 2938 O THR A 241 -31.878 -8.033 46.939 1.00 87.37 O ANISOU 2938 O THR A 241 11866 12751 8579 -1290 152 1142 O ATOM 2939 CB THR A 241 -30.780 -7.391 50.081 1.00 96.52 C ANISOU 2939 CB THR A 241 13685 13627 9360 -1501 140 1205 C ATOM 2940 OG1 THR A 241 -30.852 -6.426 51.132 1.00 96.91 O ANISOU 2940 OG1 THR A 241 13996 13574 9252 -1544 230 1203 O ATOM 2941 CG2 THR A 241 -29.528 -7.173 49.295 1.00 94.44 C ANISOU 2941 CG2 THR A 241 13322 13413 9146 -1475 -67 1226 C ATOM 2942 N VAL A 242 -32.278 -9.664 48.479 1.00 83.33 N ANISOU 2942 N VAL A 242 11557 12126 7979 -1443 198 1174 N ATOM 2943 CA VAL A 242 -32.312 -10.814 47.564 1.00 81.38 C ANISOU 2943 CA VAL A 242 11125 11939 7854 -1427 109 1168 C ATOM 2944 C VAL A 242 -33.312 -10.600 46.422 1.00 82.79 C ANISOU 2944 C VAL A 242 11058 12233 8165 -1347 199 1131 C ATOM 2945 O VAL A 242 -32.940 -10.796 45.264 1.00 81.09 O ANISOU 2945 O VAL A 242 10682 12090 8040 -1287 91 1115 O ATOM 2946 CB VAL A 242 -32.463 -12.182 48.302 1.00 85.83 C ANISOU 2946 CB VAL A 242 11802 12425 8384 -1533 87 1196 C ATOM 2947 CG1 VAL A 242 -32.725 -13.331 47.331 1.00 85.25 C ANISOU 2947 CG1 VAL A 242 11552 12402 8436 -1517 19 1181 C ATOM 2948 CG2 VAL A 242 -31.231 -12.487 49.149 1.00 85.81 C ANISOU 2948 CG2 VAL A 242 12011 12315 8277 -1591 -77 1241 C ATOM 2949 N ILE A 243 -34.546 -10.131 46.743 1.00 78.94 N ANISOU 2949 N ILE A 243 10544 11765 7684 -1340 396 1117 N ATOM 2950 CA ILE A 243 -35.594 -9.825 45.750 1.00 77.80 C ANISOU 2950 CA ILE A 243 10162 11729 7671 -1261 478 1090 C ATOM 2951 C ILE A 243 -35.086 -8.772 44.755 1.00 78.19 C ANISOU 2951 C ILE A 243 10122 11829 7757 -1151 398 1076 C ATOM 2952 O ILE A 243 -35.163 -9.003 43.552 1.00 77.31 O ANISOU 2952 O ILE A 243 9829 11800 7746 -1105 319 1064 O ATOM 2953 CB ILE A 243 -36.948 -9.404 46.400 1.00 82.21 C ANISOU 2953 CB ILE A 243 10702 12299 8235 -1259 713 1081 C ATOM 2954 CG1 ILE A 243 -37.525 -10.528 47.301 1.00 83.64 C ANISOU 2954 CG1 ILE A 243 10955 12445 8379 -1394 803 1101 C ATOM 2955 CG2 ILE A 243 -37.972 -8.969 45.325 1.00 82.69 C ANISOU 2955 CG2 ILE A 243 10496 12476 8447 -1158 768 1061 C ATOM 2956 CD1 ILE A 243 -38.452 -10.037 48.443 1.00 92.95 C ANISOU 2956 CD1 ILE A 243 12229 13600 9487 -1420 1054 1094 C ATOM 2957 N LEU A 244 -34.537 -7.648 45.268 1.00 72.80 N ANISOU 2957 N LEU A 244 9594 11089 6979 -1125 412 1079 N ATOM 2958 CA LEU A 244 -33.986 -6.538 44.483 1.00 71.34 C ANISOU 2958 CA LEU A 244 9374 10931 6800 -1046 339 1074 C ATOM 2959 C LEU A 244 -32.936 -6.985 43.457 1.00 73.17 C ANISOU 2959 C LEU A 244 9509 11221 7073 -1047 152 1081 C ATOM 2960 O LEU A 244 -33.001 -6.539 42.315 1.00 72.46 O ANISOU 2960 O LEU A 244 9278 11205 7047 -980 112 1071 O ATOM 2961 CB LEU A 244 -33.430 -5.440 45.418 1.00 71.82 C ANISOU 2961 CB LEU A 244 9672 10892 6725 -1060 365 1083 C ATOM 2962 CG LEU A 244 -32.777 -4.194 44.788 1.00 75.32 C ANISOU 2962 CG LEU A 244 10134 11337 7146 -1007 286 1087 C ATOM 2963 CD1 LEU A 244 -33.814 -3.255 44.175 1.00 75.65 C ANISOU 2963 CD1 LEU A 244 10077 11408 7259 -888 392 1065 C ATOM 2964 CD2 LEU A 244 -31.965 -3.441 45.820 1.00 77.12 C ANISOU 2964 CD2 LEU A 244 10629 11452 7222 -1070 261 1105 C ATOM 2965 N ILE A 245 -31.994 -7.865 43.851 1.00 69.08 N ANISOU 2965 N ILE A 245 9065 10668 6514 -1116 41 1098 N ATOM 2966 CA ILE A 245 -30.944 -8.381 42.959 1.00 67.98 C ANISOU 2966 CA ILE A 245 8829 10584 6416 -1105 -119 1098 C ATOM 2967 C ILE A 245 -31.516 -9.396 41.940 1.00 72.85 C ANISOU 2967 C ILE A 245 9265 11272 7142 -1076 -135 1069 C ATOM 2968 O ILE A 245 -31.284 -9.255 40.734 1.00 71.46 O ANISOU 2968 O ILE A 245 8955 11178 7019 -1024 -193 1050 O ATOM 2969 CB ILE A 245 -29.711 -8.930 43.740 1.00 70.76 C ANISOU 2969 CB ILE A 245 9312 10872 6702 -1168 -243 1127 C ATOM 2970 CG1 ILE A 245 -29.091 -7.841 44.640 1.00 71.35 C ANISOU 2970 CG1 ILE A 245 9570 10879 6661 -1212 -254 1159 C ATOM 2971 CG2 ILE A 245 -28.662 -9.511 42.778 1.00 70.83 C ANISOU 2971 CG2 ILE A 245 9191 10950 6772 -1132 -388 1119 C ATOM 2972 CD1 ILE A 245 -28.005 -8.313 45.621 1.00 79.33 C ANISOU 2972 CD1 ILE A 245 10734 11812 7596 -1289 -383 1201 C ATOM 2973 N LEU A 246 -32.256 -10.409 42.438 1.00 71.31 N ANISOU 2973 N LEU A 246 9086 11040 6968 -1125 -85 1068 N ATOM 2974 CA LEU A 246 -32.881 -11.479 41.651 1.00 71.68 C ANISOU 2974 CA LEU A 246 8999 11130 7106 -1128 -104 1044 C ATOM 2975 C LEU A 246 -33.855 -10.930 40.601 1.00 74.95 C ANISOU 2975 C LEU A 246 9237 11637 7601 -1072 -51 1026 C ATOM 2976 O LEU A 246 -33.830 -11.391 39.458 1.00 74.44 O ANISOU 2976 O LEU A 246 9055 11632 7596 -1047 -129 1001 O ATOM 2977 CB LEU A 246 -33.591 -12.476 42.594 1.00 73.15 C ANISOU 2977 CB LEU A 246 9267 11246 7281 -1220 -42 1060 C ATOM 2978 CG LEU A 246 -33.497 -13.971 42.266 1.00 78.73 C ANISOU 2978 CG LEU A 246 9961 11924 8028 -1263 -138 1049 C ATOM 2979 CD1 LEU A 246 -32.052 -14.461 42.254 1.00 78.76 C ANISOU 2979 CD1 LEU A 246 10045 11879 8002 -1233 -294 1048 C ATOM 2980 CD2 LEU A 246 -34.260 -14.784 43.281 1.00 82.76 C ANISOU 2980 CD2 LEU A 246 10575 12361 8510 -1376 -63 1076 C ATOM 2981 N ALA A 247 -34.679 -9.922 40.976 1.00 71.34 N ANISOU 2981 N ALA A 247 8773 11188 7144 -1045 76 1035 N ATOM 2982 CA ALA A 247 -35.640 -9.286 40.072 1.00 71.17 C ANISOU 2982 CA ALA A 247 8587 11247 7208 -978 117 1027 C ATOM 2983 C ALA A 247 -34.928 -8.514 38.974 1.00 74.91 C ANISOU 2983 C ALA A 247 9017 11769 7677 -910 17 1021 C ATOM 2984 O ALA A 247 -35.403 -8.511 37.842 1.00 74.31 O ANISOU 2984 O ALA A 247 8800 11764 7669 -875 -28 1012 O ATOM 2985 CB ALA A 247 -36.569 -8.362 40.837 1.00 72.71 C ANISOU 2985 CB ALA A 247 8800 11424 7403 -942 280 1036 C ATOM 2986 N PHE A 248 -33.779 -7.885 39.304 1.00 71.86 N ANISOU 2986 N PHE A 248 8758 11344 7203 -908 -26 1031 N ATOM 2987 CA PHE A 248 -32.956 -7.114 38.371 1.00 71.36 C ANISOU 2987 CA PHE A 248 8674 11325 7115 -870 -113 1033 C ATOM 2988 C PHE A 248 -32.419 -8.003 37.258 1.00 75.06 C ANISOU 2988 C PHE A 248 9042 11861 7615 -875 -221 1008 C ATOM 2989 O PHE A 248 -32.528 -7.634 36.089 1.00 73.92 O ANISOU 2989 O PHE A 248 8808 11784 7493 -840 -262 1001 O ATOM 2990 CB PHE A 248 -31.803 -6.414 39.110 1.00 73.06 C ANISOU 2990 CB PHE A 248 9046 11484 7229 -899 -141 1055 C ATOM 2991 CG PHE A 248 -30.947 -5.515 38.249 1.00 74.45 C ANISOU 2991 CG PHE A 248 9210 11707 7370 -885 -219 1066 C ATOM 2992 CD1 PHE A 248 -31.253 -4.168 38.104 1.00 77.87 C ANISOU 2992 CD1 PHE A 248 9693 12120 7776 -849 -185 1084 C ATOM 2993 CD2 PHE A 248 -29.802 -6.003 37.627 1.00 76.30 C ANISOU 2993 CD2 PHE A 248 9396 12000 7596 -909 -320 1061 C ATOM 2994 CE1 PHE A 248 -30.437 -3.329 37.338 1.00 78.51 C ANISOU 2994 CE1 PHE A 248 9784 12236 7809 -860 -260 1104 C ATOM 2995 CE2 PHE A 248 -28.990 -5.162 36.862 1.00 78.75 C ANISOU 2995 CE2 PHE A 248 9693 12363 7865 -917 -376 1077 C ATOM 2996 CZ PHE A 248 -29.312 -3.832 36.726 1.00 77.00 C ANISOU 2996 CZ PHE A 248 9533 12118 7606 -903 -349 1102 C ATOM 2997 N PHE A 249 -31.840 -9.166 37.618 1.00 72.27 N ANISOU 2997 N PHE A 249 8721 11481 7258 -916 -267 995 N ATOM 2998 CA PHE A 249 -31.295 -10.105 36.641 1.00 72.03 C ANISOU 2998 CA PHE A 249 8617 11498 7253 -906 -357 960 C ATOM 2999 C PHE A 249 -32.382 -10.798 35.821 1.00 76.28 C ANISOU 2999 C PHE A 249 9051 12069 7860 -907 -357 934 C ATOM 3000 O PHE A 249 -32.126 -11.173 34.673 1.00 75.79 O ANISOU 3000 O PHE A 249 8926 12061 7809 -887 -423 901 O ATOM 3001 CB PHE A 249 -30.317 -11.089 37.286 1.00 73.83 C ANISOU 3001 CB PHE A 249 8919 11670 7461 -928 -418 954 C ATOM 3002 CG PHE A 249 -28.971 -10.475 37.584 1.00 75.57 C ANISOU 3002 CG PHE A 249 9189 11897 7626 -923 -468 976 C ATOM 3003 CD1 PHE A 249 -27.960 -10.478 36.630 1.00 78.99 C ANISOU 3003 CD1 PHE A 249 9543 12409 8060 -888 -532 954 C ATOM 3004 CD2 PHE A 249 -28.712 -9.892 38.819 1.00 78.57 C ANISOU 3004 CD2 PHE A 249 9695 12209 7949 -965 -450 1019 C ATOM 3005 CE1 PHE A 249 -26.705 -9.918 36.913 1.00 80.17 C ANISOU 3005 CE1 PHE A 249 9712 12579 8169 -899 -580 982 C ATOM 3006 CE2 PHE A 249 -27.456 -9.334 39.102 1.00 81.33 C ANISOU 3006 CE2 PHE A 249 10086 12566 8249 -981 -517 1047 C ATOM 3007 CZ PHE A 249 -26.461 -9.355 38.149 1.00 79.25 C ANISOU 3007 CZ PHE A 249 9715 12393 8003 -950 -584 1032 C ATOM 3008 N ALA A 250 -33.607 -10.904 36.381 1.00 72.94 N ANISOU 3008 N ALA A 250 8610 11622 7482 -935 -281 950 N ATOM 3009 CA ALA A 250 -34.764 -11.464 35.685 1.00 73.16 C ANISOU 3009 CA ALA A 250 8523 11688 7586 -955 -285 939 C ATOM 3010 C ALA A 250 -35.151 -10.530 34.526 1.00 77.45 C ANISOU 3010 C ALA A 250 8965 12311 8153 -900 -313 942 C ATOM 3011 O ALA A 250 -35.431 -11.010 33.429 1.00 76.97 O ANISOU 3011 O ALA A 250 8831 12296 8119 -908 -388 920 O ATOM 3012 CB ALA A 250 -35.929 -11.623 36.645 1.00 74.59 C ANISOU 3012 CB ALA A 250 8689 11841 7812 -1002 -179 965 C ATOM 3013 N CYS A 251 -35.098 -9.201 34.764 1.00 74.64 N ANISOU 3013 N CYS A 251 8631 11958 7773 -848 -265 970 N ATOM 3014 CA CYS A 251 -35.386 -8.144 33.794 1.00 75.15 C ANISOU 3014 CA CYS A 251 8633 12074 7845 -791 -298 984 C ATOM 3015 C CYS A 251 -34.406 -8.197 32.623 1.00 79.00 C ANISOU 3015 C CYS A 251 9133 12610 8275 -792 -398 962 C ATOM 3016 O CYS A 251 -34.814 -8.166 31.456 1.00 79.20 O ANISOU 3016 O CYS A 251 9088 12688 8315 -784 -465 958 O ATOM 3017 CB CYS A 251 -35.342 -6.772 34.469 1.00 75.96 C ANISOU 3017 CB CYS A 251 8809 12137 7916 -739 -227 1015 C ATOM 3018 SG CYS A 251 -36.636 -6.494 35.705 1.00 81.27 S ANISOU 3018 SG CYS A 251 9462 12764 8654 -712 -76 1032 S ATOM 3019 N TRP A 252 -33.112 -8.285 32.949 1.00 74.51 N ANISOU 3019 N TRP A 252 8649 12025 7637 -806 -408 951 N ATOM 3020 CA TRP A 252 -32.020 -8.242 31.995 1.00 73.57 C ANISOU 3020 CA TRP A 252 8537 11960 7455 -806 -472 931 C ATOM 3021 C TRP A 252 -31.652 -9.494 31.218 1.00 77.57 C ANISOU 3021 C TRP A 252 9012 12497 7963 -817 -526 875 C ATOM 3022 O TRP A 252 -31.227 -9.358 30.071 1.00 77.09 O ANISOU 3022 O TRP A 252 8935 12500 7857 -812 -566 854 O ATOM 3023 CB TRP A 252 -30.796 -7.591 32.633 1.00 71.63 C ANISOU 3023 CB TRP A 252 8372 11700 7144 -816 -460 952 C ATOM 3024 CG TRP A 252 -30.934 -6.108 32.774 1.00 72.42 C ANISOU 3024 CG TRP A 252 8523 11785 7208 -806 -437 999 C ATOM 3025 CD1 TRP A 252 -31.124 -5.408 33.928 1.00 75.21 C ANISOU 3025 CD1 TRP A 252 8963 12062 7549 -804 -381 1030 C ATOM 3026 CD2 TRP A 252 -30.945 -5.147 31.712 1.00 72.30 C ANISOU 3026 CD2 TRP A 252 8500 11815 7155 -797 -472 1018 C ATOM 3027 NE1 TRP A 252 -31.213 -4.063 33.656 1.00 74.85 N ANISOU 3027 NE1 TRP A 252 8968 12005 7465 -786 -381 1064 N ATOM 3028 CE2 TRP A 252 -31.107 -3.874 32.301 1.00 76.56 C ANISOU 3028 CE2 TRP A 252 9127 12295 7667 -784 -442 1063 C ATOM 3029 CE3 TRP A 252 -30.808 -5.235 30.314 1.00 73.66 C ANISOU 3029 CE3 TRP A 252 8623 12064 7300 -804 -528 1003 C ATOM 3030 CZ2 TRP A 252 -31.142 -2.695 31.540 1.00 76.29 C ANISOU 3030 CZ2 TRP A 252 9131 12268 7587 -776 -477 1098 C ATOM 3031 CZ3 TRP A 252 -30.862 -4.072 29.561 1.00 75.30 C ANISOU 3031 CZ3 TRP A 252 8867 12289 7456 -805 -560 1041 C ATOM 3032 CH2 TRP A 252 -31.019 -2.820 30.172 1.00 76.20 C ANISOU 3032 CH2 TRP A 252 9066 12336 7551 -791 -539 1090 C ATOM 3033 N LEU A 253 -31.777 -10.695 31.817 1.00 74.57 N ANISOU 3033 N LEU A 253 8646 12065 7621 -835 -524 850 N ATOM 3034 CA LEU A 253 -31.408 -11.945 31.134 1.00 74.57 C ANISOU 3034 CA LEU A 253 8645 12068 7619 -834 -577 790 C ATOM 3035 C LEU A 253 -31.982 -12.170 29.720 1.00 76.69 C ANISOU 3035 C LEU A 253 8871 12388 7880 -842 -629 757 C ATOM 3036 O LEU A 253 -31.175 -12.474 28.845 1.00 75.60 O ANISOU 3036 O LEU A 253 8749 12288 7689 -820 -655 708 O ATOM 3037 CB LEU A 253 -31.485 -13.196 32.024 1.00 75.12 C ANISOU 3037 CB LEU A 253 8765 12049 7727 -857 -582 774 C ATOM 3038 CG LEU A 253 -30.442 -14.276 31.708 1.00 80.27 C ANISOU 3038 CG LEU A 253 9457 12680 8361 -820 -630 714 C ATOM 3039 CD1 LEU A 253 -29.115 -13.995 32.408 1.00 80.41 C ANISOU 3039 CD1 LEU A 253 9501 12694 8356 -781 -626 729 C ATOM 3040 CD2 LEU A 253 -30.950 -15.649 32.083 1.00 82.95 C ANISOU 3040 CD2 LEU A 253 9854 12924 8738 -854 -663 690 C ATOM 3041 N PRO A 254 -33.301 -11.960 29.424 1.00 73.24 N ANISOU 3041 N PRO A 254 8377 11960 7489 -871 -647 783 N ATOM 3042 CA PRO A 254 -33.776 -12.127 28.031 1.00 73.53 C ANISOU 3042 CA PRO A 254 8389 12044 7506 -889 -723 759 C ATOM 3043 C PRO A 254 -33.041 -11.235 27.021 1.00 76.43 C ANISOU 3043 C PRO A 254 8777 12481 7784 -863 -738 756 C ATOM 3044 O PRO A 254 -32.810 -11.665 25.889 1.00 76.41 O ANISOU 3044 O PRO A 254 8805 12509 7719 -875 -786 709 O ATOM 3045 CB PRO A 254 -35.264 -11.766 28.113 1.00 75.70 C ANISOU 3045 CB PRO A 254 8574 12326 7863 -916 -740 811 C ATOM 3046 CG PRO A 254 -35.630 -11.989 29.523 1.00 79.99 C ANISOU 3046 CG PRO A 254 9104 12815 8473 -928 -661 836 C ATOM 3047 CD PRO A 254 -34.422 -11.594 30.314 1.00 74.82 C ANISOU 3047 CD PRO A 254 8529 12134 7766 -889 -599 836 C ATOM 3048 N TYR A 255 -32.635 -10.018 27.448 1.00 71.56 N ANISOU 3048 N TYR A 255 8163 11880 7147 -837 -693 805 N ATOM 3049 CA TYR A 255 -31.884 -9.076 26.620 1.00 70.62 C ANISOU 3049 CA TYR A 255 8075 11822 6936 -833 -700 816 C ATOM 3050 C TYR A 255 -30.466 -9.570 26.408 1.00 72.95 C ANISOU 3050 C TYR A 255 8401 12151 7165 -827 -669 763 C ATOM 3051 O TYR A 255 -29.990 -9.525 25.276 1.00 73.66 O ANISOU 3051 O TYR A 255 8512 12303 7172 -839 -682 733 O ATOM 3052 CB TYR A 255 -31.894 -7.658 27.215 1.00 71.42 C ANISOU 3052 CB TYR A 255 8189 11910 7035 -819 -669 886 C ATOM 3053 CG TYR A 255 -31.000 -6.675 26.490 1.00 73.42 C ANISOU 3053 CG TYR A 255 8493 12217 7185 -837 -675 906 C ATOM 3054 CD1 TYR A 255 -31.385 -6.115 25.275 1.00 75.84 C ANISOU 3054 CD1 TYR A 255 8820 12560 7434 -855 -737 925 C ATOM 3055 CD2 TYR A 255 -29.768 -6.301 27.020 1.00 74.15 C ANISOU 3055 CD2 TYR A 255 8616 12324 7233 -852 -627 915 C ATOM 3056 CE1 TYR A 255 -30.568 -5.204 24.606 1.00 77.14 C ANISOU 3056 CE1 TYR A 255 9048 12773 7491 -892 -738 951 C ATOM 3057 CE2 TYR A 255 -28.940 -5.392 26.360 1.00 75.34 C ANISOU 3057 CE2 TYR A 255 8809 12532 7287 -893 -628 941 C ATOM 3058 CZ TYR A 255 -29.352 -4.832 25.161 1.00 84.36 C ANISOU 3058 CZ TYR A 255 9983 13706 8365 -916 -677 959 C ATOM 3059 OH TYR A 255 -28.534 -3.943 24.504 1.00 86.31 O ANISOU 3059 OH TYR A 255 10285 14006 8501 -975 -673 991 O ATOM 3060 N TYR A 256 -29.793 -10.047 27.474 1.00 67.43 N ANISOU 3060 N TYR A 256 7703 11415 6502 -807 -629 753 N ATOM 3061 CA TYR A 256 -28.428 -10.559 27.362 1.00 67.08 C ANISOU 3061 CA TYR A 256 7660 11407 6422 -782 -604 706 C ATOM 3062 C TYR A 256 -28.317 -11.797 26.478 1.00 72.01 C ANISOU 3062 C TYR A 256 8297 12036 7029 -757 -622 619 C ATOM 3063 O TYR A 256 -27.330 -11.942 25.762 1.00 72.07 O ANISOU 3063 O TYR A 256 8298 12109 6976 -732 -591 572 O ATOM 3064 CB TYR A 256 -27.741 -10.709 28.730 1.00 67.64 C ANISOU 3064 CB TYR A 256 7731 11430 6538 -765 -583 727 C ATOM 3065 CG TYR A 256 -27.385 -9.371 29.350 1.00 69.11 C ANISOU 3065 CG TYR A 256 7929 11629 6699 -796 -563 800 C ATOM 3066 CD1 TYR A 256 -26.577 -8.460 28.675 1.00 71.20 C ANISOU 3066 CD1 TYR A 256 8181 11979 6891 -823 -551 818 C ATOM 3067 CD2 TYR A 256 -27.864 -9.012 30.606 1.00 69.83 C ANISOU 3067 CD2 TYR A 256 8063 11643 6828 -809 -553 849 C ATOM 3068 CE1 TYR A 256 -26.262 -7.220 29.228 1.00 71.97 C ANISOU 3068 CE1 TYR A 256 8313 12073 6958 -867 -545 887 C ATOM 3069 CE2 TYR A 256 -27.549 -7.776 31.174 1.00 70.85 C ANISOU 3069 CE2 TYR A 256 8234 11764 6921 -840 -539 909 C ATOM 3070 CZ TYR A 256 -26.752 -6.879 30.477 1.00 79.64 C ANISOU 3070 CZ TYR A 256 9341 12954 7966 -871 -543 929 C ATOM 3071 OH TYR A 256 -26.429 -5.652 31.016 1.00 81.08 O ANISOU 3071 OH TYR A 256 9586 13117 8105 -917 -541 990 O ATOM 3072 N ILE A 257 -29.371 -12.633 26.460 1.00 69.63 N ANISOU 3072 N ILE A 257 8017 11669 6772 -771 -666 598 N ATOM 3073 CA ILE A 257 -29.473 -13.823 25.613 1.00 70.65 C ANISOU 3073 CA ILE A 257 8193 11776 6876 -762 -700 516 C ATOM 3074 C ILE A 257 -29.597 -13.372 24.149 1.00 77.03 C ANISOU 3074 C ILE A 257 9024 12658 7585 -790 -718 495 C ATOM 3075 O ILE A 257 -28.873 -13.890 23.291 1.00 77.86 O ANISOU 3075 O ILE A 257 9172 12794 7615 -762 -695 419 O ATOM 3076 CB ILE A 257 -30.629 -14.765 26.086 1.00 73.67 C ANISOU 3076 CB ILE A 257 8598 12062 7332 -801 -755 515 C ATOM 3077 CG1 ILE A 257 -30.372 -15.341 27.512 1.00 73.91 C ANISOU 3077 CG1 ILE A 257 8639 12009 7435 -782 -734 531 C ATOM 3078 CG2 ILE A 257 -30.934 -15.888 25.082 1.00 74.98 C ANISOU 3078 CG2 ILE A 257 8838 12193 7458 -817 -812 436 C ATOM 3079 CD1 ILE A 257 -28.969 -16.025 27.776 1.00 80.84 C ANISOU 3079 CD1 ILE A 257 9548 12864 8304 -698 -714 477 C ATOM 3080 N GLY A 258 -30.461 -12.377 23.905 1.00 73.81 N ANISOU 3080 N GLY A 258 8594 12276 7174 -838 -756 564 N ATOM 3081 CA GLY A 258 -30.682 -11.781 22.588 1.00 74.33 C ANISOU 3081 CA GLY A 258 8697 12403 7142 -876 -795 568 C ATOM 3082 C GLY A 258 -29.408 -11.213 22.001 1.00 78.54 C ANISOU 3082 C GLY A 258 9253 13021 7569 -866 -724 550 C ATOM 3083 O GLY A 258 -28.988 -11.609 20.910 1.00 78.62 O ANISOU 3083 O GLY A 258 9324 13072 7476 -874 -711 485 O ATOM 3084 N ILE A 259 -28.763 -10.331 22.757 1.00 75.13 N ANISOU 3084 N ILE A 259 8773 12615 7156 -856 -670 605 N ATOM 3085 CA ILE A 259 -27.480 -9.767 22.363 1.00 75.47 C ANISOU 3085 CA ILE A 259 8814 12749 7114 -863 -596 600 C ATOM 3086 C ILE A 259 -26.433 -10.851 22.108 1.00 79.80 C ANISOU 3086 C ILE A 259 9348 13330 7643 -808 -528 503 C ATOM 3087 O ILE A 259 -25.718 -10.801 21.107 1.00 80.78 O ANISOU 3087 O ILE A 259 9493 13539 7662 -819 -470 460 O ATOM 3088 CB ILE A 259 -26.943 -8.791 23.427 1.00 78.11 C ANISOU 3088 CB ILE A 259 9102 13089 7489 -871 -566 676 C ATOM 3089 CG1 ILE A 259 -27.737 -7.483 23.400 1.00 78.45 C ANISOU 3089 CG1 ILE A 259 9182 13111 7516 -917 -615 765 C ATOM 3090 CG2 ILE A 259 -25.462 -8.525 23.206 1.00 79.80 C ANISOU 3090 CG2 ILE A 259 9278 13401 7640 -883 -487 663 C ATOM 3091 CD1 ILE A 259 -27.786 -6.827 22.038 1.00 88.03 C ANISOU 3091 CD1 ILE A 259 10460 14383 8604 -975 -639 779 C ATOM 3092 N SER A 260 -26.337 -11.826 23.005 1.00 75.15 N ANISOU 3092 N SER A 260 8730 12672 7152 -745 -530 469 N ATOM 3093 CA SER A 260 -25.363 -12.903 22.847 1.00 75.34 C ANISOU 3093 CA SER A 260 8741 12706 7177 -664 -475 376 C ATOM 3094 C SER A 260 -25.439 -13.513 21.449 1.00 79.26 C ANISOU 3094 C SER A 260 9322 13226 7568 -660 -457 285 C ATOM 3095 O SER A 260 -24.422 -13.705 20.783 1.00 79.17 O ANISOU 3095 O SER A 260 9298 13293 7490 -619 -367 219 O ATOM 3096 CB SER A 260 -25.583 -13.985 23.906 1.00 78.74 C ANISOU 3096 CB SER A 260 9175 13022 7722 -605 -516 356 C ATOM 3097 OG SER A 260 -25.137 -13.550 25.179 1.00 87.81 O ANISOU 3097 OG SER A 260 10258 14159 8947 -598 -514 424 O ATOM 3098 N ILE A 261 -26.658 -13.801 21.005 1.00 75.81 N ANISOU 3098 N ILE A 261 8969 12723 7112 -709 -543 281 N ATOM 3099 CA ILE A 261 -26.879 -14.356 19.675 1.00 76.72 C ANISOU 3099 CA ILE A 261 9199 12842 7111 -727 -552 199 C ATOM 3100 C ILE A 261 -26.473 -13.360 18.592 1.00 82.37 C ANISOU 3100 C ILE A 261 9942 13672 7683 -786 -502 215 C ATOM 3101 O ILE A 261 -25.819 -13.724 17.616 1.00 83.97 O ANISOU 3101 O ILE A 261 10209 13927 7770 -769 -424 130 O ATOM 3102 CB ILE A 261 -28.351 -14.756 19.467 1.00 79.48 C ANISOU 3102 CB ILE A 261 9622 13100 7476 -793 -683 213 C ATOM 3103 CG1 ILE A 261 -28.632 -16.112 20.116 1.00 79.51 C ANISOU 3103 CG1 ILE A 261 9656 12985 7569 -750 -720 159 C ATOM 3104 CG2 ILE A 261 -28.690 -14.789 17.984 1.00 81.62 C ANISOU 3104 CG2 ILE A 261 10020 13396 7595 -856 -720 169 C ATOM 3105 CD1 ILE A 261 -29.952 -16.175 20.853 1.00 83.56 C ANISOU 3105 CD1 ILE A 261 10140 13423 8188 -816 -824 232 C ATOM 3106 N ASP A 262 -26.865 -12.102 18.772 1.00 78.31 N ANISOU 3106 N ASP A 262 9393 13192 7171 -855 -541 324 N ATOM 3107 CA ASP A 262 -26.531 -11.046 17.805 1.00 79.09 C ANISOU 3107 CA ASP A 262 9537 13386 7129 -930 -510 359 C ATOM 3108 C ASP A 262 -25.016 -11.022 17.560 1.00 83.61 C ANISOU 3108 C ASP A 262 10060 14068 7638 -900 -356 310 C ATOM 3109 O ASP A 262 -24.591 -10.924 16.408 1.00 84.05 O ANISOU 3109 O ASP A 262 10192 14199 7543 -941 -291 266 O ATOM 3110 CB ASP A 262 -27.005 -9.662 18.304 1.00 80.42 C ANISOU 3110 CB ASP A 262 9670 13555 7333 -987 -570 488 C ATOM 3111 CG ASP A 262 -27.135 -8.561 17.247 1.00 95.48 C ANISOU 3111 CG ASP A 262 11668 15514 9095 -1082 -599 546 C ATOM 3112 OD1 ASP A 262 -26.405 -8.614 16.224 1.00 97.10 O ANISOU 3112 OD1 ASP A 262 11940 15799 9152 -1120 -522 496 O ATOM 3113 OD2 ASP A 262 -27.930 -7.619 17.465 1.00103.43 O ANISOU 3113 OD2 ASP A 262 12685 16481 10133 -1115 -693 642 O ATOM 3114 N SER A 263 -24.214 -11.159 18.644 1.00 79.70 N ANISOU 3114 N SER A 263 9436 13585 7259 -833 -300 316 N ATOM 3115 CA SER A 263 -22.750 -11.171 18.613 1.00 80.12 C ANISOU 3115 CA SER A 263 9393 13752 7298 -794 -164 279 C ATOM 3116 C SER A 263 -22.203 -12.319 17.767 1.00 85.14 C ANISOU 3116 C SER A 263 10066 14412 7870 -711 -69 142 C ATOM 3117 O SER A 263 -21.401 -12.063 16.874 1.00 86.21 O ANISOU 3117 O SER A 263 10201 14667 7888 -735 52 105 O ATOM 3118 CB SER A 263 -22.178 -11.226 20.026 1.00 83.20 C ANISOU 3118 CB SER A 263 9646 14124 7841 -734 -167 318 C ATOM 3119 OG SER A 263 -22.793 -10.272 20.878 1.00 91.08 O ANISOU 3119 OG SER A 263 10641 15073 8893 -800 -253 431 O ATOM 3120 N PHE A 264 -22.659 -13.541 18.020 1.00 81.82 N ANISOU 3120 N PHE A 264 9694 13876 7517 -622 -118 67 N ATOM 3121 CA PHE A 264 -22.209 -14.701 17.259 1.00 83.45 C ANISOU 3121 CA PHE A 264 9968 14074 7665 -528 -36 -74 C ATOM 3122 C PHE A 264 -22.605 -14.634 15.783 1.00 88.50 C ANISOU 3122 C PHE A 264 10776 14739 8109 -605 -15 -127 C ATOM 3123 O PHE A 264 -21.846 -15.060 14.913 1.00 89.31 O ANISOU 3123 O PHE A 264 10921 14907 8107 -557 119 -231 O ATOM 3124 CB PHE A 264 -22.745 -15.991 17.886 1.00 85.14 C ANISOU 3124 CB PHE A 264 10234 14128 7987 -436 -121 -131 C ATOM 3125 CG PHE A 264 -22.077 -16.358 19.181 1.00 86.50 C ANISOU 3125 CG PHE A 264 10269 14272 8326 -331 -120 -113 C ATOM 3126 CD1 PHE A 264 -20.734 -16.694 19.212 1.00 91.10 C ANISOU 3126 CD1 PHE A 264 10739 14933 8942 -210 0 -174 C ATOM 3127 CD2 PHE A 264 -22.792 -16.367 20.366 1.00 87.60 C ANISOU 3127 CD2 PHE A 264 10390 14308 8586 -355 -239 -32 C ATOM 3128 CE1 PHE A 264 -20.117 -17.032 20.401 1.00 91.64 C ANISOU 3128 CE1 PHE A 264 10684 14970 9166 -115 -25 -148 C ATOM 3129 CE2 PHE A 264 -22.181 -16.704 21.559 1.00 90.18 C ANISOU 3129 CE2 PHE A 264 10616 14599 9048 -271 -251 -10 C ATOM 3130 CZ PHE A 264 -20.841 -17.037 21.576 1.00 89.23 C ANISOU 3130 CZ PHE A 264 10389 14550 8963 -151 -157 -64 C ATOM 3131 N ILE A 265 -23.798 -14.146 15.530 1.00 84.86 N ANISOU 3131 N ILE A 265 10413 14224 7605 -717 -148 -58 N ATOM 3132 CA ILE A 265 -24.243 -14.015 14.179 1.00 86.37 C ANISOU 3132 CA ILE A 265 10777 14430 7608 -807 -163 -89 C ATOM 3133 C ILE A 265 -23.153 -13.330 13.434 1.00 92.70 C ANISOU 3133 C ILE A 265 11561 15386 8276 -840 -1 -100 C ATOM 3134 O ILE A 265 -22.553 -13.905 12.560 1.00 94.60 O ANISOU 3134 O ILE A 265 11881 15669 8394 -803 123 -214 O ATOM 3135 CB ILE A 265 -25.388 -13.081 14.087 1.00 88.45 C ANISOU 3135 CB ILE A 265 11087 14665 7855 -931 -317 30 C ATOM 3136 CG1 ILE A 265 -26.654 -13.843 13.751 1.00 88.73 C ANISOU 3136 CG1 ILE A 265 11254 14576 7883 -962 -472 3 C ATOM 3137 CG2 ILE A 265 -25.088 -12.074 13.024 1.00 89.73 C ANISOU 3137 CG2 ILE A 265 11330 14931 7833 -1038 -270 66 C ATOM 3138 CD1 ILE A 265 -27.451 -14.213 14.935 1.00 88.60 C ANISOU 3138 CD1 ILE A 265 11147 14459 8058 -930 -581 50 C ATOM 3139 N LEU A 266 -22.909 -12.076 13.780 1.00 88.69 N ANISOU 3139 N LEU A 266 10957 14958 7782 -918 2 18 N ATOM 3140 CA LEU A 266 -21.885 -11.319 13.107 1.00 89.78 C ANISOU 3140 CA LEU A 266 11072 15250 7790 -982 152 27 C ATOM 3141 C LEU A 266 -20.475 -11.823 13.008 1.00 96.00 C ANISOU 3141 C LEU A 266 11743 16155 8578 -890 359 -68 C ATOM 3142 O LEU A 266 -19.799 -11.593 12.024 1.00 97.66 O ANISOU 3142 O LEU A 266 11995 16483 8627 -940 505 -110 O ATOM 3143 CB LEU A 266 -21.551 -10.023 13.895 1.00 88.48 C ANISOU 3143 CB LEU A 266 10775 15148 7697 -1055 136 167 C ATOM 3144 CG LEU A 266 -22.646 -9.029 14.272 1.00 91.33 C ANISOU 3144 CG LEU A 266 11187 15426 8087 -1145 -40 299 C ATOM 3145 CD1 LEU A 266 -22.645 -8.821 15.746 1.00 89.47 C ANISOU 3145 CD1 LEU A 266 10805 15144 8047 -1092 -92 366 C ATOM 3146 CD2 LEU A 266 -22.457 -7.703 13.610 1.00 94.42 C ANISOU 3146 CD2 LEU A 266 11649 15893 8332 -1293 -29 392 C ATOM 3147 N LEU A 267 -20.023 -12.529 14.028 1.00 92.46 N ANISOU 3147 N LEU A 267 11143 15676 8311 -751 373 -101 N ATOM 3148 CA LEU A 267 -18.706 -13.140 13.967 1.00 94.24 C ANISOU 3148 CA LEU A 267 11236 16005 8566 -629 558 -198 C ATOM 3149 C LEU A 267 -19.109 -14.335 13.193 1.00100.92 C ANISOU 3149 C LEU A 267 12259 16756 9329 -545 574 -341 C ATOM 3150 O LEU A 267 -18.284 -15.077 12.681 1.00102.32 O ANISOU 3150 O LEU A 267 12424 16985 9467 -431 736 -468 O ATOM 3151 CB LEU A 267 -18.231 -13.485 15.376 1.00 93.16 C ANISOU 3151 CB LEU A 267 10902 15839 8658 -511 519 -171 C ATOM 3152 N GLU A 268 -20.411 -14.530 13.104 1.00 97.80 N ANISOU 3152 N GLU A 268 12034 16217 8909 -600 403 -322 N ATOM 3153 CA GLU A 268 -20.979 -15.551 12.250 1.00 99.09 C ANISOU 3153 CA GLU A 268 12414 16275 8960 -569 382 -443 C ATOM 3154 C GLU A 268 -20.698 -17.028 12.378 1.00104.72 C ANISOU 3154 C GLU A 268 13166 16887 9735 -392 426 -589 C ATOM 3155 O GLU A 268 -20.473 -17.708 11.393 1.00106.16 O ANISOU 3155 O GLU A 268 13503 17059 9774 -348 526 -722 O ATOM 3156 CB GLU A 268 -20.770 -15.203 10.781 1.00102.10 C ANISOU 3156 CB GLU A 268 12955 16748 9090 -665 495 -494 C ATOM 3157 CG GLU A 268 -19.335 -14.954 10.395 1.00112.01 C ANISOU 3157 CG GLU A 268 14087 18185 10287 -622 743 -545 C ATOM 3158 CD GLU A 268 -19.217 -14.254 9.057 1.00128.23 C ANISOU 3158 CD GLU A 268 16296 20346 12081 -773 843 -547 C ATOM 3159 OE1 GLU A 268 -18.456 -14.721 8.192 1.00114.21 O ANISOU 3159 OE1 GLU A 268 14579 18648 10168 -721 1046 -674 O ATOM 3160 OE2 GLU A 268 -19.896 -13.235 8.864 1.00121.57 O ANISOU 3160 OE2 GLU A 268 15525 19502 11163 -940 718 -422 O ATOM 3161 N ILE A 269 -20.717 -17.499 13.617 1.00100.56 N ANISOU 3161 N ILE A 269 12518 16277 9415 -295 347 -562 N ATOM 3162 CA ILE A 269 -20.828 -18.907 13.944 1.00101.18 C ANISOU 3162 CA ILE A 269 12672 16198 9572 -150 309 -669 C ATOM 3163 C ILE A 269 -22.233 -19.457 13.762 1.00105.51 C ANISOU 3163 C ILE A 269 13433 16576 10081 -235 126 -672 C ATOM 3164 O ILE A 269 -22.418 -20.631 13.440 1.00106.43 O ANISOU 3164 O ILE A 269 13714 16560 10164 -161 109 -790 O ATOM 3165 CB ILE A 269 -20.357 -19.169 15.383 1.00103.18 C ANISOU 3165 CB ILE A 269 12732 16418 10054 -34 273 -621 C ATOM 3166 CG1 ILE A 269 -18.952 -18.602 15.596 1.00104.17 C ANISOU 3166 CG1 ILE A 269 12623 16724 10233 36 434 -605 C ATOM 3167 CG2 ILE A 269 -20.387 -20.659 15.690 1.00104.87 C ANISOU 3167 CG2 ILE A 269 13045 16459 10343 122 234 -732 C ATOM 3168 CD1 ILE A 269 -17.987 -19.581 16.227 1.00112.30 C ANISOU 3168 CD1 ILE A 269 13536 17720 11411 253 491 -683 C ATOM 3169 N ILE A 270 -23.223 -18.590 13.960 1.00100.98 N ANISOU 3169 N ILE A 270 12852 16003 9513 -391 -14 -541 N ATOM 3170 CA ILE A 270 -24.610 -18.946 13.685 1.00100.65 C ANISOU 3170 CA ILE A 270 12981 15831 9432 -499 -193 -526 C ATOM 3171 C ILE A 270 -24.963 -18.858 12.205 1.00107.64 C ANISOU 3171 C ILE A 270 14078 16733 10088 -600 -193 -581 C ATOM 3172 O ILE A 270 -24.972 -17.774 11.622 1.00107.40 O ANISOU 3172 O ILE A 270 14042 16815 9951 -705 -175 -513 O ATOM 3173 CB ILE A 270 -25.578 -18.058 14.488 1.00101.32 C ANISOU 3173 CB ILE A 270 12959 15911 9626 -611 -342 -364 C ATOM 3174 CG1 ILE A 270 -25.325 -18.214 15.989 1.00100.20 C ANISOU 3174 CG1 ILE A 270 12646 15732 9691 -526 -352 -311 C ATOM 3175 CG2 ILE A 270 -27.020 -18.399 14.148 1.00101.99 C ANISOU 3175 CG2 ILE A 270 13186 15883 9681 -727 -527 -343 C ATOM 3176 CD1 ILE A 270 -26.075 -17.215 16.842 1.00104.94 C ANISOU 3176 CD1 ILE A 270 13130 16348 10394 -616 -450 -160 C ATOM 3177 N LYS A 271 -25.254 -20.006 11.602 1.00106.49 N ANISOU 3177 N LYS A 271 14142 16463 9856 -575 -224 -704 N ATOM 3178 CA LYS A 271 -25.608 -20.061 10.189 1.00108.29 C ANISOU 3178 CA LYS A 271 14613 16685 9849 -676 -238 -769 C ATOM 3179 C LYS A 271 -27.123 -20.194 10.304 1.00112.14 C ANISOU 3179 C LYS A 271 15182 17054 10372 -817 -491 -689 C ATOM 3180 O LYS A 271 -27.640 -21.262 10.632 1.00112.55 O ANISOU 3180 O LYS A 271 15320 16955 10487 -798 -590 -738 O ATOM 3181 CB LYS A 271 -24.890 -21.224 9.501 1.00113.09 C ANISOU 3181 CB LYS A 271 15402 17228 10339 -551 -99 -960 C ATOM 3182 N GLN A 272 -27.830 -19.101 10.032 1.00107.91 N ANISOU 3182 N GLN A 272 14614 16586 9799 -960 -599 -562 N ATOM 3183 CA GLN A 272 -29.286 -19.093 10.103 1.00107.40 C ANISOU 3183 CA GLN A 272 14586 16438 9783 -1095 -841 -472 C ATOM 3184 C GLN A 272 -29.729 -18.098 9.036 1.00112.34 C ANISOU 3184 C GLN A 272 15307 17137 10239 -1237 -918 -403 C ATOM 3185 O GLN A 272 -29.064 -17.090 8.799 1.00112.50 O ANISOU 3185 O GLN A 272 15269 17283 10195 -1237 -807 -360 O ATOM 3186 CB GLN A 272 -29.953 -18.763 11.439 1.00106.66 C ANISOU 3186 CB GLN A 272 14268 16327 9929 -1096 -941 -343 C ATOM 3187 CG GLN A 272 -29.673 -19.775 12.539 1.00120.01 C ANISOU 3187 CG GLN A 272 15891 17924 11782 -982 -901 -394 C ATOM 3188 CD GLN A 272 -30.247 -21.144 12.231 1.00140.95 C ANISOU 3188 CD GLN A 272 18742 20416 14396 -1013 -1005 -488 C ATOM 3189 OE1 GLN A 272 -29.688 -22.167 12.627 1.00133.42 O ANISOU 3189 OE1 GLN A 272 17839 19370 13484 -900 -938 -586 O ATOM 3190 NE2 GLN A 272 -31.369 -21.169 11.522 1.00139.59 N ANISOU 3190 NE2 GLN A 272 18691 20202 14146 -1169 -1184 -455 N ATOM 3191 N GLY A 273 -30.857 -18.389 8.395 1.00109.49 N ANISOU 3191 N GLY A 273 15102 16695 9805 -1368 -1123 -386 N ATOM 3192 CA GLY A 273 -31.388 -17.525 7.357 1.00110.45 C ANISOU 3192 CA GLY A 273 15337 16864 9763 -1509 -1240 -313 C ATOM 3193 C GLY A 273 -31.926 -16.219 7.908 1.00112.84 C ANISOU 3193 C GLY A 273 15433 17241 10199 -1546 -1332 -138 C ATOM 3194 O GLY A 273 -32.420 -16.166 9.034 1.00111.41 O ANISOU 3194 O GLY A 273 15049 17039 10243 -1506 -1386 -64 O ATOM 3195 N CYS A 274 -31.829 -15.161 7.110 1.00109.15 N ANISOU 3195 N CYS A 274 15037 16852 9584 -1622 -1346 -74 N ATOM 3196 CA CYS A 274 -32.308 -13.846 7.519 1.00107.39 C ANISOU 3196 CA CYS A 274 14655 16684 9465 -1651 -1437 90 C ATOM 3197 C CYS A 274 -33.505 -13.997 8.454 1.00108.10 C ANISOU 3197 C CYS A 274 14568 16710 9795 -1646 -1612 175 C ATOM 3198 O CYS A 274 -33.656 -13.239 9.412 1.00106.57 O ANISOU 3198 O CYS A 274 14166 16548 9776 -1592 -1603 273 O ATOM 3199 CB CYS A 274 -32.630 -12.988 6.294 1.00109.64 C ANISOU 3199 CB CYS A 274 15118 16997 9542 -1781 -1556 157 C ATOM 3200 SG CYS A 274 -31.213 -12.094 5.615 1.00114.39 S ANISOU 3200 SG CYS A 274 15818 17722 9924 -1793 -1324 138 S ATOM 3201 N GLU A 275 -34.352 -14.981 8.168 1.00103.61 N ANISOU 3201 N GLU A 275 14089 16051 9227 -1712 -1765 136 N ATOM 3202 CA GLU A 275 -35.537 -15.234 8.984 1.00101.86 C ANISOU 3202 CA GLU A 275 13699 15777 9226 -1730 -1927 214 C ATOM 3203 C GLU A 275 -35.177 -15.145 10.472 1.00101.51 C ANISOU 3203 C GLU A 275 13416 15751 9402 -1606 -1784 236 C ATOM 3204 O GLU A 275 -35.760 -14.327 11.189 1.00100.13 O ANISOU 3204 O GLU A 275 13051 15607 9387 -1587 -1836 353 O ATOM 3205 CB GLU A 275 -36.151 -16.600 8.620 1.00104.74 C ANISOU 3205 CB GLU A 275 14205 16035 9557 -1812 -2050 133 C ATOM 3206 CG GLU A 275 -37.644 -16.716 8.886 1.00116.73 C ANISOU 3206 CG GLU A 275 15604 17517 11232 -1910 -2293 236 C ATOM 3207 CD GLU A 275 -38.537 -15.690 8.213 1.00139.29 C ANISOU 3207 CD GLU A 275 18438 20419 14067 -1998 -2501 368 C ATOM 3208 OE1 GLU A 275 -38.364 -15.443 6.997 1.00127.91 O ANISOU 3208 OE1 GLU A 275 17219 18981 12401 -2073 -2567 350 O ATOM 3209 OE2 GLU A 275 -39.424 -15.144 8.908 1.00137.66 O ANISOU 3209 OE2 GLU A 275 17995 20241 14068 -1988 -2598 489 O ATOM 3210 N PHE A 276 -34.143 -15.861 10.895 1.00 95.65 N ANISOU 3210 N PHE A 276 12694 14995 8655 -1512 -1599 126 N ATOM 3211 CA PHE A 276 -33.653 -15.763 12.270 1.00 92.81 C ANISOU 3211 CA PHE A 276 12135 14651 8477 -1398 -1465 146 C ATOM 3212 C PHE A 276 -33.260 -14.348 12.745 1.00 94.83 C ANISOU 3212 C PHE A 276 12245 15001 8784 -1352 -1389 246 C ATOM 3213 O PHE A 276 -33.593 -13.963 13.866 1.00 93.63 O ANISOU 3213 O PHE A 276 11916 14849 8810 -1310 -1388 322 O ATOM 3214 CB PHE A 276 -32.479 -16.723 12.481 1.00 94.41 C ANISOU 3214 CB PHE A 276 12401 14826 8645 -1296 -1289 10 C ATOM 3215 CG PHE A 276 -32.155 -16.975 13.926 1.00 94.23 C ANISOU 3215 CG PHE A 276 12206 14782 8814 -1196 -1203 23 C ATOM 3216 CD1 PHE A 276 -33.080 -16.693 14.917 1.00 96.18 C ANISOU 3216 CD1 PHE A 276 12294 15009 9240 -1221 -1290 128 C ATOM 3217 CD2 PHE A 276 -30.925 -17.495 14.293 1.00 96.38 C ANISOU 3217 CD2 PHE A 276 12477 15055 9087 -1076 -1036 -68 C ATOM 3218 CE1 PHE A 276 -32.784 -16.924 16.247 1.00 95.88 C ANISOU 3218 CE1 PHE A 276 12127 14945 9357 -1142 -1212 142 C ATOM 3219 CE2 PHE A 276 -30.623 -17.729 15.622 1.00 98.05 C ANISOU 3219 CE2 PHE A 276 12549 15240 9467 -991 -980 -48 C ATOM 3220 CZ PHE A 276 -31.554 -17.442 16.600 1.00 94.87 C ANISOU 3220 CZ PHE A 276 12016 14810 9220 -1032 -1067 57 C ATOM 3221 N GLU A 277 -32.563 -13.602 11.895 1.00 90.57 N ANISOU 3221 N GLU A 277 11799 14535 8078 -1371 -1325 244 N ATOM 3222 CA GLU A 277 -32.124 -12.255 12.239 1.00 88.93 C ANISOU 3222 CA GLU A 277 11491 14406 7892 -1349 -1260 337 C ATOM 3223 C GLU A 277 -33.233 -11.327 12.724 1.00 90.86 C ANISOU 3223 C GLU A 277 11616 14636 8272 -1369 -1406 476 C ATOM 3224 O GLU A 277 -33.191 -10.828 13.849 1.00 89.33 O ANISOU 3224 O GLU A 277 11265 14447 8229 -1303 -1354 533 O ATOM 3225 CB GLU A 277 -31.466 -11.581 11.033 1.00 91.75 C ANISOU 3225 CB GLU A 277 12004 14834 8023 -1412 -1212 330 C ATOM 3226 CG GLU A 277 -30.081 -11.022 11.314 1.00104.56 C ANISOU 3226 CG GLU A 277 13570 16549 9609 -1363 -1005 317 C ATOM 3227 CD GLU A 277 -29.074 -11.397 10.244 1.00127.65 C ANISOU 3227 CD GLU A 277 16649 19535 12317 -1386 -862 208 C ATOM 3228 OE1 GLU A 277 -28.455 -10.481 9.661 1.00116.28 O ANISOU 3228 OE1 GLU A 277 15263 18180 10738 -1446 -789 246 O ATOM 3229 OE2 GLU A 277 -28.900 -12.606 9.986 1.00125.01 O ANISOU 3229 OE2 GLU A 277 16391 19160 11947 -1345 -817 84 O ATOM 3230 N ASN A 278 -34.223 -11.098 11.867 1.00 87.92 N ANISOU 3230 N ASN A 278 11323 14242 7841 -1455 -1593 529 N ATOM 3231 CA ASN A 278 -35.336 -10.213 12.195 1.00 87.33 C ANISOU 3231 CA ASN A 278 11130 14154 7897 -1459 -1745 660 C ATOM 3232 C ASN A 278 -35.983 -10.613 13.518 1.00 87.81 C ANISOU 3232 C ASN A 278 10988 14180 8195 -1397 -1740 682 C ATOM 3233 O ASN A 278 -36.483 -9.764 14.255 1.00 86.63 O ANISOU 3233 O ASN A 278 10697 14034 8184 -1347 -1760 774 O ATOM 3234 CB ASN A 278 -36.376 -10.241 11.073 1.00 93.51 C ANISOU 3234 CB ASN A 278 12019 14911 8600 -1562 -1974 701 C ATOM 3235 CG ASN A 278 -36.965 -8.873 10.791 1.00120.29 C ANISOU 3235 CG ASN A 278 15387 18313 12003 -1570 -2108 836 C ATOM 3236 OD1 ASN A 278 -37.820 -8.387 11.532 1.00114.95 O ANISOU 3236 OD1 ASN A 278 14532 17623 11519 -1514 -2182 923 O ATOM 3237 ND2 ASN A 278 -36.510 -8.243 9.714 1.00111.44 N ANISOU 3237 ND2 ASN A 278 14455 17213 10672 -1635 -2135 852 N ATOM 3238 N THR A 279 -35.972 -11.909 13.812 1.00 82.93 N ANISOU 3238 N THR A 279 10374 13520 7613 -1401 -1709 594 N ATOM 3239 CA THR A 279 -36.584 -12.423 15.042 1.00 80.97 C ANISOU 3239 CA THR A 279 9959 13235 7571 -1366 -1700 611 C ATOM 3240 C THR A 279 -35.674 -11.970 16.186 1.00 80.47 C ANISOU 3240 C THR A 279 9804 13192 7578 -1264 -1518 614 C ATOM 3241 O THR A 279 -36.180 -11.528 17.208 1.00 79.05 O ANISOU 3241 O THR A 279 9476 13007 7553 -1222 -1504 682 O ATOM 3242 CB THR A 279 -36.697 -13.958 14.980 1.00 89.57 C ANISOU 3242 CB THR A 279 11122 14258 8651 -1411 -1721 515 C ATOM 3243 OG1 THR A 279 -37.378 -14.343 13.781 1.00 92.89 O ANISOU 3243 OG1 THR A 279 11672 14657 8965 -1522 -1894 504 O ATOM 3244 CG2 THR A 279 -37.402 -14.547 16.196 1.00 86.76 C ANISOU 3244 CG2 THR A 279 10613 13859 8492 -1405 -1722 540 C ATOM 3245 N VAL A 280 -34.338 -12.052 15.989 1.00 75.44 N ANISOU 3245 N VAL A 280 9255 12584 6825 -1228 -1378 541 N ATOM 3246 CA VAL A 280 -33.308 -11.647 16.952 1.00 73.83 C ANISOU 3246 CA VAL A 280 8977 12407 6666 -1146 -1218 541 C ATOM 3247 C VAL A 280 -33.406 -10.142 17.203 1.00 78.06 C ANISOU 3247 C VAL A 280 9453 12979 7226 -1134 -1222 649 C ATOM 3248 O VAL A 280 -33.413 -9.724 18.357 1.00 77.33 O ANISOU 3248 O VAL A 280 9254 12874 7255 -1081 -1168 694 O ATOM 3249 CB VAL A 280 -31.879 -12.060 16.499 1.00 77.86 C ANISOU 3249 CB VAL A 280 9579 12958 7046 -1117 -1081 443 C ATOM 3250 CG1 VAL A 280 -30.828 -11.694 17.541 1.00 76.29 C ANISOU 3250 CG1 VAL A 280 9283 12792 6913 -1042 -939 451 C ATOM 3251 CG2 VAL A 280 -31.806 -13.548 16.181 1.00 78.61 C ANISOU 3251 CG2 VAL A 280 9764 12996 7110 -1112 -1081 327 C ATOM 3252 N HIS A 281 -33.505 -9.341 16.126 1.00 76.18 N ANISOU 3252 N HIS A 281 9307 12775 6864 -1187 -1294 690 N ATOM 3253 CA HIS A 281 -33.609 -7.880 16.184 1.00 76.48 C ANISOU 3253 CA HIS A 281 9331 12829 6900 -1182 -1321 794 C ATOM 3254 C HIS A 281 -34.877 -7.435 16.912 1.00 79.44 C ANISOU 3254 C HIS A 281 9578 13156 7450 -1141 -1417 879 C ATOM 3255 O HIS A 281 -34.804 -6.523 17.737 1.00 78.26 O ANISOU 3255 O HIS A 281 9367 12994 7373 -1086 -1368 938 O ATOM 3256 CB HIS A 281 -33.549 -7.280 14.768 1.00 79.20 C ANISOU 3256 CB HIS A 281 9830 13202 7059 -1262 -1403 819 C ATOM 3257 CG HIS A 281 -33.649 -5.783 14.734 1.00 83.19 C ANISOU 3257 CG HIS A 281 10355 13705 7548 -1263 -1449 930 C ATOM 3258 ND1 HIS A 281 -32.520 -4.988 14.653 1.00 85.08 N ANISOU 3258 ND1 HIS A 281 10662 13989 7677 -1288 -1340 944 N ATOM 3259 CD2 HIS A 281 -34.746 -4.985 14.743 1.00 85.63 C ANISOU 3259 CD2 HIS A 281 10629 13967 7937 -1241 -1598 1028 C ATOM 3260 CE1 HIS A 281 -32.963 -3.740 14.633 1.00 84.87 C ANISOU 3260 CE1 HIS A 281 10664 13925 7658 -1287 -1429 1051 C ATOM 3261 NE2 HIS A 281 -34.295 -3.689 14.696 1.00 85.56 N ANISOU 3261 NE2 HIS A 281 10690 13956 7864 -1245 -1583 1102 N ATOM 3262 N LYS A 282 -36.034 -8.058 16.586 1.00 76.15 N ANISOU 3262 N LYS A 282 9123 12713 7095 -1171 -1553 884 N ATOM 3263 CA LYS A 282 -37.329 -7.754 17.199 1.00 75.81 C ANISOU 3263 CA LYS A 282 8929 12643 7232 -1133 -1642 961 C ATOM 3264 C LYS A 282 -37.342 -8.139 18.674 1.00 77.74 C ANISOU 3264 C LYS A 282 9041 12866 7629 -1072 -1515 945 C ATOM 3265 O LYS A 282 -37.947 -7.430 19.477 1.00 76.68 O ANISOU 3265 O LYS A 282 8795 12717 7623 -1008 -1502 1010 O ATOM 3266 CB LYS A 282 -38.473 -8.456 16.457 1.00 79.73 C ANISOU 3266 CB LYS A 282 9405 13132 7755 -1204 -1820 969 C ATOM 3267 CG LYS A 282 -39.096 -7.608 15.357 1.00 95.60 C ANISOU 3267 CG LYS A 282 11473 15148 9703 -1236 -2004 1049 C ATOM 3268 CD LYS A 282 -40.239 -8.330 14.648 1.00106.19 C ANISOU 3268 CD LYS A 282 12787 16484 11077 -1320 -2203 1063 C ATOM 3269 CE LYS A 282 -41.607 -7.901 15.126 1.00121.12 C ANISOU 3269 CE LYS A 282 14463 18378 13181 -1273 -2317 1160 C ATOM 3270 NZ LYS A 282 -41.927 -8.411 16.490 1.00131.12 N ANISOU 3270 NZ LYS A 282 15541 19645 14632 -1224 -2187 1143 N ATOM 3271 N TRP A 283 -36.660 -9.254 19.025 1.00 73.38 N ANISOU 3271 N TRP A 283 8518 12305 7056 -1088 -1421 857 N ATOM 3272 CA TRP A 283 -36.536 -9.760 20.391 1.00 72.07 C ANISOU 3272 CA TRP A 283 8265 12110 7007 -1046 -1307 837 C ATOM 3273 C TRP A 283 -35.775 -8.719 21.210 1.00 74.36 C ANISOU 3273 C TRP A 283 8548 12404 7301 -978 -1191 870 C ATOM 3274 O TRP A 283 -36.316 -8.234 22.206 1.00 74.40 O ANISOU 3274 O TRP A 283 8461 12385 7422 -931 -1154 920 O ATOM 3275 CB TRP A 283 -35.833 -11.135 20.394 1.00 70.96 C ANISOU 3275 CB TRP A 283 8196 11947 6818 -1071 -1255 736 C ATOM 3276 CG TRP A 283 -35.506 -11.699 21.748 1.00 71.38 C ANISOU 3276 CG TRP A 283 8198 11959 6963 -1033 -1146 715 C ATOM 3277 CD1 TRP A 283 -34.393 -11.441 22.498 1.00 73.38 C ANISOU 3277 CD1 TRP A 283 8465 12214 7201 -977 -1027 701 C ATOM 3278 CD2 TRP A 283 -36.248 -12.697 22.461 1.00 71.44 C ANISOU 3278 CD2 TRP A 283 8151 11916 7079 -1066 -1159 706 C ATOM 3279 NE1 TRP A 283 -34.419 -12.184 23.654 1.00 72.34 N ANISOU 3279 NE1 TRP A 283 8299 12028 7159 -965 -973 687 N ATOM 3280 CE2 TRP A 283 -35.538 -12.977 23.651 1.00 74.53 C ANISOU 3280 CE2 TRP A 283 8540 12271 7507 -1021 -1045 688 C ATOM 3281 CE3 TRP A 283 -37.435 -13.400 22.200 1.00 74.04 C ANISOU 3281 CE3 TRP A 283 8436 12225 7470 -1144 -1265 716 C ATOM 3282 CZ2 TRP A 283 -35.994 -13.903 24.594 1.00 73.95 C ANISOU 3282 CZ2 TRP A 283 8439 12136 7523 -1051 -1026 683 C ATOM 3283 CZ3 TRP A 283 -37.892 -14.313 23.140 1.00 75.47 C ANISOU 3283 CZ3 TRP A 283 8573 12354 7747 -1181 -1239 711 C ATOM 3284 CH2 TRP A 283 -37.176 -14.556 24.321 1.00 75.37 C ANISOU 3284 CH2 TRP A 283 8577 12300 7761 -1134 -1117 695 C ATOM 3285 N ILE A 284 -34.565 -8.321 20.735 1.00 68.80 N ANISOU 3285 N ILE A 284 7944 11733 6464 -982 -1137 846 N ATOM 3286 CA ILE A 284 -33.691 -7.311 21.343 1.00 66.88 C ANISOU 3286 CA ILE A 284 7717 11499 6197 -947 -1044 880 C ATOM 3287 C ILE A 284 -34.424 -5.985 21.595 1.00 70.75 C ANISOU 3287 C ILE A 284 8181 11961 6739 -911 -1088 974 C ATOM 3288 O ILE A 284 -34.196 -5.375 22.635 1.00 69.93 O ANISOU 3288 O ILE A 284 8057 11826 6685 -868 -1013 1003 O ATOM 3289 CB ILE A 284 -32.369 -7.133 20.547 1.00 69.57 C ANISOU 3289 CB ILE A 284 8155 11899 6379 -983 -993 845 C ATOM 3290 CG1 ILE A 284 -31.499 -8.407 20.615 1.00 69.42 C ANISOU 3290 CG1 ILE A 284 8142 11898 6338 -977 -915 746 C ATOM 3291 CG2 ILE A 284 -31.575 -5.899 21.017 1.00 69.53 C ANISOU 3291 CG2 ILE A 284 8172 11906 6340 -978 -929 900 C ATOM 3292 CD1 ILE A 284 -30.474 -8.518 19.517 1.00 76.18 C ANISOU 3292 CD1 ILE A 284 9083 12825 7039 -1011 -870 691 C ATOM 3293 N SER A 285 -35.315 -5.559 20.678 1.00 67.92 N ANISOU 3293 N SER A 285 7831 11604 6370 -924 -1217 1020 N ATOM 3294 CA SER A 285 -36.075 -4.320 20.858 1.00 68.24 C ANISOU 3294 CA SER A 285 7848 11607 6474 -867 -1274 1108 C ATOM 3295 C SER A 285 -37.098 -4.455 21.993 1.00 71.38 C ANISOU 3295 C SER A 285 8098 11968 7053 -795 -1242 1126 C ATOM 3296 O SER A 285 -37.119 -3.606 22.887 1.00 70.67 O ANISOU 3296 O SER A 285 7999 11835 7016 -726 -1173 1161 O ATOM 3297 CB SER A 285 -36.736 -3.882 19.554 1.00 74.35 C ANISOU 3297 CB SER A 285 8670 12388 7191 -896 -1440 1157 C ATOM 3298 OG SER A 285 -37.730 -4.798 19.120 1.00 86.55 O ANISOU 3298 OG SER A 285 10134 13948 8803 -923 -1545 1143 O ATOM 3299 N ILE A 286 -37.896 -5.550 21.985 1.00 68.05 N ANISOU 3299 N ILE A 286 7575 11563 6718 -821 -1281 1099 N ATOM 3300 CA ILE A 286 -38.918 -5.862 23.002 1.00 67.96 C ANISOU 3300 CA ILE A 286 7408 11535 6877 -779 -1240 1114 C ATOM 3301 C ILE A 286 -38.268 -6.095 24.381 1.00 70.33 C ANISOU 3301 C ILE A 286 7718 11805 7200 -756 -1073 1079 C ATOM 3302 O ILE A 286 -38.682 -5.472 25.360 1.00 69.67 O ANISOU 3302 O ILE A 286 7582 11690 7201 -687 -994 1111 O ATOM 3303 CB ILE A 286 -39.846 -7.059 22.577 1.00 71.93 C ANISOU 3303 CB ILE A 286 7814 12067 7449 -850 -1333 1096 C ATOM 3304 CG1 ILE A 286 -40.618 -6.769 21.265 1.00 74.21 C ANISOU 3304 CG1 ILE A 286 8090 12381 7724 -877 -1526 1143 C ATOM 3305 CG2 ILE A 286 -40.825 -7.440 23.693 1.00 72.66 C ANISOU 3305 CG2 ILE A 286 7740 12156 7713 -829 -1265 1112 C ATOM 3306 CD1 ILE A 286 -41.106 -8.036 20.484 1.00 84.69 C ANISOU 3306 CD1 ILE A 286 9407 13732 9041 -992 -1647 1110 C ATOM 3307 N THR A 287 -37.255 -6.979 24.440 1.00 66.04 N ANISOU 3307 N THR A 287 7249 11267 6576 -810 -1023 1014 N ATOM 3308 CA THR A 287 -36.546 -7.354 25.665 1.00 65.08 C ANISOU 3308 CA THR A 287 7150 11113 6465 -802 -895 983 C ATOM 3309 C THR A 287 -35.763 -6.227 26.338 1.00 70.22 C ANISOU 3309 C THR A 287 7872 11737 7072 -756 -816 1010 C ATOM 3310 O THR A 287 -35.658 -6.231 27.563 1.00 69.62 O ANISOU 3310 O THR A 287 7796 11620 7037 -735 -722 1011 O ATOM 3311 CB THR A 287 -35.715 -8.619 25.473 1.00 70.98 C ANISOU 3311 CB THR A 287 7952 11866 7153 -854 -886 909 C ATOM 3312 OG1 THR A 287 -34.769 -8.407 24.422 1.00 71.34 O ANISOU 3312 OG1 THR A 287 8085 11951 7069 -871 -917 884 O ATOM 3313 CG2 THR A 287 -36.578 -9.843 25.196 1.00 67.82 C ANISOU 3313 CG2 THR A 287 7499 11461 6811 -909 -949 881 C ATOM 3314 N GLU A 288 -35.220 -5.270 25.566 1.00 68.08 N ANISOU 3314 N GLU A 288 7678 11483 6706 -755 -858 1036 N ATOM 3315 CA GLU A 288 -34.501 -4.129 26.138 1.00 67.98 C ANISOU 3315 CA GLU A 288 7750 11437 6643 -732 -802 1070 C ATOM 3316 C GLU A 288 -35.507 -3.216 26.821 1.00 72.97 C ANISOU 3316 C GLU A 288 8352 12008 7365 -652 -783 1121 C ATOM 3317 O GLU A 288 -35.238 -2.725 27.916 1.00 71.42 O ANISOU 3317 O GLU A 288 8204 11757 7175 -624 -696 1129 O ATOM 3318 CB GLU A 288 -33.758 -3.352 25.049 1.00 69.78 C ANISOU 3318 CB GLU A 288 8073 11698 6742 -772 -858 1092 C ATOM 3319 CG GLU A 288 -32.739 -2.363 25.583 1.00 81.66 C ANISOU 3319 CG GLU A 288 9677 13177 8173 -788 -804 1121 C ATOM 3320 CD GLU A 288 -31.983 -1.563 24.538 1.00113.12 C ANISOU 3320 CD GLU A 288 13760 17197 12023 -851 -850 1152 C ATOM 3321 OE1 GLU A 288 -31.012 -0.874 24.924 1.00118.99 O ANISOU 3321 OE1 GLU A 288 14579 17933 12698 -894 -809 1175 O ATOM 3322 OE2 GLU A 288 -32.350 -1.617 23.340 1.00108.81 O ANISOU 3322 OE2 GLU A 288 13226 16687 11431 -873 -931 1158 O ATOM 3323 N ALA A 289 -36.672 -3.006 26.164 1.00 71.92 N ANISOU 3323 N ALA A 289 8142 11884 7302 -612 -868 1153 N ATOM 3324 CA ALA A 289 -37.772 -2.174 26.640 1.00 72.77 C ANISOU 3324 CA ALA A 289 8188 11943 7517 -510 -858 1199 C ATOM 3325 C ALA A 289 -38.329 -2.717 27.952 1.00 77.50 C ANISOU 3325 C ALA A 289 8698 12524 8225 -480 -733 1176 C ATOM 3326 O ALA A 289 -38.450 -1.956 28.913 1.00 77.57 O ANISOU 3326 O ALA A 289 8746 12470 8258 -409 -639 1189 O ATOM 3327 CB ALA A 289 -38.862 -2.097 25.587 1.00 74.62 C ANISOU 3327 CB ALA A 289 8326 12209 7817 -483 -996 1237 C ATOM 3328 N LEU A 290 -38.609 -4.035 28.011 1.00 74.29 N ANISOU 3328 N LEU A 290 8198 12163 7866 -543 -727 1140 N ATOM 3329 CA LEU A 290 -39.132 -4.693 29.211 1.00 74.35 C ANISOU 3329 CA LEU A 290 8131 12157 7962 -544 -609 1122 C ATOM 3330 C LEU A 290 -38.104 -4.708 30.346 1.00 78.57 C ANISOU 3330 C LEU A 290 8795 12638 8421 -563 -495 1096 C ATOM 3331 O LEU A 290 -38.491 -4.577 31.509 1.00 78.67 O ANISOU 3331 O LEU A 290 8804 12609 8478 -532 -377 1097 O ATOM 3332 CB LEU A 290 -39.642 -6.113 28.900 1.00 74.44 C ANISOU 3332 CB LEU A 290 8036 12218 8028 -629 -654 1097 C ATOM 3333 CG LEU A 290 -40.796 -6.245 27.882 1.00 79.80 C ANISOU 3333 CG LEU A 290 8571 12954 8796 -633 -781 1128 C ATOM 3334 CD1 LEU A 290 -41.027 -7.689 27.520 1.00 79.99 C ANISOU 3334 CD1 LEU A 290 8547 13011 8834 -747 -840 1096 C ATOM 3335 CD2 LEU A 290 -42.094 -5.631 28.398 1.00 82.75 C ANISOU 3335 CD2 LEU A 290 8784 13338 9320 -546 -732 1174 C ATOM 3336 N ALA A 291 -36.797 -4.808 30.003 1.00 75.02 N ANISOU 3336 N ALA A 291 8459 12190 7854 -614 -531 1075 N ATOM 3337 CA ALA A 291 -35.681 -4.803 30.957 1.00 74.03 C ANISOU 3337 CA ALA A 291 8452 12022 7654 -642 -459 1058 C ATOM 3338 C ALA A 291 -35.568 -3.483 31.702 1.00 79.48 C ANISOU 3338 C ALA A 291 9241 12643 8314 -589 -397 1090 C ATOM 3339 O ALA A 291 -35.066 -3.475 32.819 1.00 78.85 O ANISOU 3339 O ALA A 291 9249 12511 8199 -607 -322 1083 O ATOM 3340 CB ALA A 291 -34.378 -5.084 30.239 1.00 73.91 C ANISOU 3340 CB ALA A 291 8498 12046 7539 -697 -520 1036 C ATOM 3341 N PHE A 292 -36.040 -2.378 31.089 1.00 78.21 N ANISOU 3341 N PHE A 292 9085 12471 8161 -525 -441 1127 N ATOM 3342 CA PHE A 292 -36.012 -1.027 31.656 1.00 79.08 C ANISOU 3342 CA PHE A 292 9311 12495 8238 -462 -397 1156 C ATOM 3343 C PHE A 292 -36.891 -0.840 32.897 1.00 84.84 C ANISOU 3343 C PHE A 292 10031 13164 9042 -387 -266 1148 C ATOM 3344 O PHE A 292 -36.719 0.159 33.603 1.00 84.17 O ANISOU 3344 O PHE A 292 10083 12988 8909 -343 -208 1158 O ATOM 3345 CB PHE A 292 -36.326 0.042 30.592 1.00 81.67 C ANISOU 3345 CB PHE A 292 9659 12815 8557 -407 -495 1199 C ATOM 3346 CG PHE A 292 -35.310 0.240 29.492 1.00 82.96 C ANISOU 3346 CG PHE A 292 9895 13019 8606 -489 -599 1215 C ATOM 3347 CD1 PHE A 292 -33.982 -0.145 29.665 1.00 85.61 C ANISOU 3347 CD1 PHE A 292 10298 13383 8846 -589 -584 1194 C ATOM 3348 CD2 PHE A 292 -35.664 0.866 28.304 1.00 85.98 C ANISOU 3348 CD2 PHE A 292 10282 13412 8975 -466 -711 1255 C ATOM 3349 CE1 PHE A 292 -33.040 0.054 28.649 1.00 86.45 C ANISOU 3349 CE1 PHE A 292 10456 13543 8848 -667 -655 1207 C ATOM 3350 CE2 PHE A 292 -34.720 1.070 27.295 1.00 88.79 C ANISOU 3350 CE2 PHE A 292 10720 13810 9207 -556 -789 1270 C ATOM 3351 CZ PHE A 292 -33.415 0.665 27.476 1.00 86.07 C ANISOU 3351 CZ PHE A 292 10425 13507 8771 -657 -749 1243 C ATOM 3352 N PHE A 293 -37.796 -1.810 33.191 1.00 83.29 N ANISOU 3352 N PHE A 293 9686 13011 8949 -385 -212 1130 N ATOM 3353 CA PHE A 293 -38.652 -1.780 34.383 1.00 84.39 C ANISOU 3353 CA PHE A 293 9798 13110 9154 -331 -60 1119 C ATOM 3354 C PHE A 293 -37.826 -1.959 35.665 1.00 87.36 C ANISOU 3354 C PHE A 293 10341 13419 9432 -394 35 1097 C ATOM 3355 O PHE A 293 -38.367 -1.815 36.762 1.00 88.41 O ANISOU 3355 O PHE A 293 10508 13503 9581 -359 175 1085 O ATOM 3356 CB PHE A 293 -39.791 -2.809 34.306 1.00 87.26 C ANISOU 3356 CB PHE A 293 9954 13553 9649 -343 -33 1114 C ATOM 3357 CG PHE A 293 -41.044 -2.393 35.049 1.00 91.15 C ANISOU 3357 CG PHE A 293 10348 14034 10250 -243 109 1117 C ATOM 3358 CD1 PHE A 293 -41.222 -2.724 36.391 1.00 94.69 C ANISOU 3358 CD1 PHE A 293 10844 14449 10685 -268 280 1094 C ATOM 3359 CD2 PHE A 293 -42.062 -1.700 34.398 1.00 95.55 C ANISOU 3359 CD2 PHE A 293 10761 14620 10924 -123 73 1146 C ATOM 3360 CE1 PHE A 293 -42.382 -2.341 37.077 1.00 97.44 C ANISOU 3360 CE1 PHE A 293 11094 14798 11131 -172 439 1091 C ATOM 3361 CE2 PHE A 293 -43.229 -1.327 35.083 1.00100.16 C ANISOU 3361 CE2 PHE A 293 11226 15205 11625 -13 218 1145 C ATOM 3362 CZ PHE A 293 -43.381 -1.652 36.417 1.00 98.37 C ANISOU 3362 CZ PHE A 293 11043 14953 11380 -38 413 1114 C ATOM 3363 N HIS A 294 -36.505 -2.198 35.528 1.00 82.16 N ANISOU 3363 N HIS A 294 9790 12758 8669 -483 -43 1094 N ATOM 3364 CA HIS A 294 -35.581 -2.296 36.654 1.00 81.74 C ANISOU 3364 CA HIS A 294 9901 12639 8517 -549 5 1085 C ATOM 3365 C HIS A 294 -35.544 -0.950 37.423 1.00 87.67 C ANISOU 3365 C HIS A 294 10825 13283 9202 -495 74 1094 C ATOM 3366 O HIS A 294 -35.374 -0.949 38.646 1.00 88.34 O ANISOU 3366 O HIS A 294 11043 13295 9226 -524 164 1083 O ATOM 3367 CB HIS A 294 -34.177 -2.756 36.192 1.00 81.14 C ANISOU 3367 CB HIS A 294 9866 12599 8365 -640 -109 1085 C ATOM 3368 CG HIS A 294 -33.360 -1.711 35.488 1.00 84.00 C ANISOU 3368 CG HIS A 294 10303 12959 8654 -645 -191 1111 C ATOM 3369 ND1 HIS A 294 -32.565 -0.825 36.190 1.00 85.64 N ANISOU 3369 ND1 HIS A 294 10686 13091 8764 -678 -186 1130 N ATOM 3370 CD2 HIS A 294 -33.206 -1.474 34.165 1.00 85.42 C ANISOU 3370 CD2 HIS A 294 10418 13204 8833 -641 -283 1123 C ATOM 3371 CE1 HIS A 294 -31.974 -0.072 35.278 1.00 84.93 C ANISOU 3371 CE1 HIS A 294 10622 13024 8625 -697 -271 1156 C ATOM 3372 NE2 HIS A 294 -32.328 -0.424 34.047 1.00 85.12 N ANISOU 3372 NE2 HIS A 294 10509 13134 8700 -675 -326 1153 N ATOM 3373 N CYS A 295 -35.779 0.179 36.694 1.00 84.01 N ANISOU 3373 N CYS A 295 10375 12800 8746 -416 30 1115 N ATOM 3374 CA CYS A 295 -35.851 1.551 37.210 1.00 84.42 C ANISOU 3374 CA CYS A 295 10600 12735 8742 -345 79 1123 C ATOM 3375 C CYS A 295 -36.946 1.689 38.258 1.00 88.46 C ANISOU 3375 C CYS A 295 11116 13189 9305 -250 251 1094 C ATOM 3376 O CYS A 295 -36.834 2.515 39.167 1.00 89.25 O ANISOU 3376 O CYS A 295 11413 13172 9326 -219 332 1082 O ATOM 3377 CB CYS A 295 -36.090 2.536 36.070 1.00 85.45 C ANISOU 3377 CB CYS A 295 10714 12859 8894 -268 -17 1155 C ATOM 3378 SG CYS A 295 -34.785 2.571 34.822 1.00 88.51 S ANISOU 3378 SG CYS A 295 11125 13311 9192 -389 -193 1191 S ATOM 3379 N CYS A 296 -38.021 0.900 38.101 1.00 84.08 N ANISOU 3379 N CYS A 296 10346 12718 8881 -208 309 1083 N ATOM 3380 CA CYS A 296 -39.204 0.910 38.950 1.00 84.56 C ANISOU 3380 CA CYS A 296 10347 12762 9019 -118 490 1058 C ATOM 3381 C CYS A 296 -39.173 -0.102 40.088 1.00 86.99 C ANISOU 3381 C CYS A 296 10688 13075 9290 -218 609 1034 C ATOM 3382 O CYS A 296 -39.970 0.036 41.010 1.00 87.88 O ANISOU 3382 O CYS A 296 10812 13155 9422 -162 788 1009 O ATOM 3383 CB CYS A 296 -40.464 0.767 38.101 1.00 85.71 C ANISOU 3383 CB CYS A 296 10224 13001 9339 -18 478 1071 C ATOM 3384 SG CYS A 296 -40.565 1.943 36.727 1.00 89.84 S ANISOU 3384 SG CYS A 296 10726 13507 9902 99 314 1111 S ATOM 3385 N LEU A 297 -38.245 -1.083 40.055 1.00 81.54 N ANISOU 3385 N LEU A 297 10026 12417 8539 -360 517 1041 N ATOM 3386 CA LEU A 297 -38.121 -2.113 41.096 1.00 81.14 C ANISOU 3386 CA LEU A 297 10030 12357 8443 -467 598 1028 C ATOM 3387 C LEU A 297 -37.856 -1.555 42.502 1.00 85.11 C ANISOU 3387 C LEU A 297 10783 12738 8815 -481 724 1011 C ATOM 3388 O LEU A 297 -38.578 -1.911 43.429 1.00 85.50 O ANISOU 3388 O LEU A 297 10844 12775 8866 -490 888 992 O ATOM 3389 CB LEU A 297 -37.070 -3.177 40.728 1.00 79.68 C ANISOU 3389 CB LEU A 297 9844 12210 8219 -593 450 1040 C ATOM 3390 CG LEU A 297 -37.388 -4.142 39.581 1.00 83.66 C ANISOU 3390 CG LEU A 297 10130 12825 8833 -613 352 1044 C ATOM 3391 CD1 LEU A 297 -36.179 -4.976 39.248 1.00 82.42 C ANISOU 3391 CD1 LEU A 297 10014 12682 8619 -706 216 1046 C ATOM 3392 CD2 LEU A 297 -38.545 -5.077 39.927 1.00 87.04 C ANISOU 3392 CD2 LEU A 297 10418 13299 9353 -640 455 1039 C ATOM 3393 N ASN A 298 -36.837 -0.680 42.652 1.00 81.13 N ANISOU 3393 N ASN A 298 10487 12146 8191 -495 648 1018 N ATOM 3394 CA ASN A 298 -36.447 -0.042 43.921 1.00 81.49 C ANISOU 3394 CA ASN A 298 10814 12060 8089 -523 733 1003 C ATOM 3395 C ASN A 298 -37.596 0.769 44.592 1.00 86.19 C ANISOU 3395 C ASN A 298 11463 12589 8696 -393 945 964 C ATOM 3396 O ASN A 298 -37.895 0.477 45.753 1.00 85.91 O ANISOU 3396 O ASN A 298 11546 12506 8591 -431 1097 940 O ATOM 3397 CB ASN A 298 -35.162 0.790 43.743 1.00 82.17 C ANISOU 3397 CB ASN A 298 11084 12076 8060 -573 582 1027 C ATOM 3398 CG ASN A 298 -34.562 1.352 45.011 1.00102.65 C ANISOU 3398 CG ASN A 298 13990 14529 10483 -640 620 1020 C ATOM 3399 OD1 ASN A 298 -34.298 0.631 45.974 1.00 99.75 O ANISOU 3399 OD1 ASN A 298 13725 14133 10041 -739 652 1019 O ATOM 3400 ND2 ASN A 298 -34.251 2.643 45.003 1.00 92.13 N ANISOU 3400 ND2 ASN A 298 12835 13096 9074 -604 593 1020 N ATOM 3401 N PRO A 299 -38.280 1.733 43.906 1.00 83.51 N ANISOU 3401 N PRO A 299 11038 12246 8444 -235 965 956 N ATOM 3402 CA PRO A 299 -39.391 2.456 44.562 1.00 85.29 C ANISOU 3402 CA PRO A 299 11298 12412 8698 -86 1180 912 C ATOM 3403 C PRO A 299 -40.606 1.581 44.879 1.00 89.65 C ANISOU 3403 C PRO A 299 11625 13068 9371 -61 1356 895 C ATOM 3404 O PRO A 299 -41.323 1.867 45.839 1.00 91.15 O ANISOU 3404 O PRO A 299 11886 13209 9537 5 1576 852 O ATOM 3405 CB PRO A 299 -39.770 3.527 43.539 1.00 87.56 C ANISOU 3405 CB PRO A 299 11506 12685 9079 77 1109 922 C ATOM 3406 CG PRO A 299 -38.630 3.607 42.601 1.00 90.21 C ANISOU 3406 CG PRO A 299 11875 13033 9368 -17 870 969 C ATOM 3407 CD PRO A 299 -38.084 2.232 42.531 1.00 84.23 C ANISOU 3407 CD PRO A 299 11015 12381 8609 -179 798 988 C ATOM 3408 N ILE A 300 -40.852 0.537 44.056 1.00 84.64 N ANISOU 3408 N ILE A 300 10725 12574 8862 -118 1263 927 N ATOM 3409 CA ILE A 300 -41.941 -0.426 44.245 1.00 84.95 C ANISOU 3409 CA ILE A 300 10533 12726 9021 -137 1396 924 C ATOM 3410 C ILE A 300 -41.650 -1.249 45.510 1.00 87.93 C ANISOU 3410 C ILE A 300 11077 13065 9267 -290 1509 912 C ATOM 3411 O ILE A 300 -42.540 -1.409 46.344 1.00 89.36 O ANISOU 3411 O ILE A 300 11232 13260 9461 -276 1731 888 O ATOM 3412 CB ILE A 300 -42.149 -1.293 42.953 1.00 87.13 C ANISOU 3412 CB ILE A 300 10524 13140 9442 -178 1228 964 C ATOM 3413 CG1 ILE A 300 -43.031 -0.588 41.874 1.00 88.52 C ANISOU 3413 CG1 ILE A 300 10471 13377 9786 -11 1182 977 C ATOM 3414 CG2 ILE A 300 -42.577 -2.742 43.225 1.00 87.94 C ANISOU 3414 CG2 ILE A 300 10489 13334 9590 -318 1275 975 C ATOM 3415 CD1 ILE A 300 -44.545 -0.275 42.222 1.00101.49 C ANISOU 3415 CD1 ILE A 300 11912 15072 11577 133 1390 959 C ATOM 3416 N LEU A 301 -40.384 -1.695 45.681 1.00 82.68 N ANISOU 3416 N LEU A 301 10596 12348 8472 -431 1359 932 N ATOM 3417 CA LEU A 301 -39.934 -2.486 46.831 1.00 82.64 C ANISOU 3417 CA LEU A 301 10782 12289 8329 -586 1413 934 C ATOM 3418 C LEU A 301 -39.974 -1.756 48.176 1.00 88.13 C ANISOU 3418 C LEU A 301 11762 12857 8866 -575 1596 897 C ATOM 3419 O LEU A 301 -39.971 -2.408 49.222 1.00 88.21 O ANISOU 3419 O LEU A 301 11913 12831 8770 -693 1696 896 O ATOM 3420 CB LEU A 301 -38.573 -3.141 46.571 1.00 80.79 C ANISOU 3420 CB LEU A 301 10638 12036 8021 -716 1183 969 C ATOM 3421 CG LEU A 301 -38.615 -4.420 45.739 1.00 84.47 C ANISOU 3421 CG LEU A 301 10884 12613 8600 -785 1063 995 C ATOM 3422 CD1 LEU A 301 -37.299 -4.656 45.033 1.00 82.85 C ANISOU 3422 CD1 LEU A 301 10709 12406 8365 -834 827 1018 C ATOM 3423 CD2 LEU A 301 -39.002 -5.624 46.588 1.00 87.61 C ANISOU 3423 CD2 LEU A 301 11304 13013 8970 -914 1156 1004 C ATOM 3424 N TYR A 302 -40.035 -0.414 48.148 1.00 85.35 N ANISOU 3424 N TYR A 302 11514 12427 8489 -436 1640 866 N ATOM 3425 CA TYR A 302 -40.156 0.414 49.346 1.00 86.48 C ANISOU 3425 CA TYR A 302 11943 12435 8479 -399 1825 819 C ATOM 3426 C TYR A 302 -41.623 0.515 49.745 1.00 92.77 C ANISOU 3426 C TYR A 302 12597 13283 9368 -279 2112 773 C ATOM 3427 O TYR A 302 -41.921 0.583 50.938 1.00 94.21 O ANISOU 3427 O TYR A 302 12974 13396 9424 -306 2323 734 O ATOM 3428 CB TYR A 302 -39.604 1.825 49.106 1.00 87.07 C ANISOU 3428 CB TYR A 302 12206 12389 8489 -298 1743 803 C ATOM 3429 CG TYR A 302 -38.138 1.992 49.429 1.00 86.82 C ANISOU 3429 CG TYR A 302 12458 12251 8279 -443 1553 831 C ATOM 3430 CD1 TYR A 302 -37.683 1.949 50.743 1.00 89.60 C ANISOU 3430 CD1 TYR A 302 13130 12485 8428 -560 1618 816 C ATOM 3431 CD2 TYR A 302 -37.216 2.285 48.430 1.00 85.68 C ANISOU 3431 CD2 TYR A 302 12271 12122 8161 -465 1310 874 C ATOM 3432 CE1 TYR A 302 -36.337 2.133 51.048 1.00 89.65 C ANISOU 3432 CE1 TYR A 302 13385 12398 8280 -699 1423 850 C ATOM 3433 CE2 TYR A 302 -35.868 2.480 48.724 1.00 85.55 C ANISOU 3433 CE2 TYR A 302 12488 12023 7994 -602 1136 905 C ATOM 3434 CZ TYR A 302 -35.432 2.401 50.035 1.00 93.13 C ANISOU 3434 CZ TYR A 302 13745 12870 8769 -718 1183 895 C ATOM 3435 OH TYR A 302 -34.108 2.600 50.334 1.00 92.03 O ANISOU 3435 OH TYR A 302 13822 12655 8492 -860 993 934 O ATOM 3436 N ALA A 303 -42.534 0.539 48.746 1.00 89.71 N ANISOU 3436 N ALA A 303 11868 13019 9198 -149 2118 781 N ATOM 3437 CA ALA A 303 -43.981 0.645 48.949 1.00 91.97 C ANISOU 3437 CA ALA A 303 11940 13385 9620 -16 2372 746 C ATOM 3438 C ALA A 303 -44.564 -0.590 49.640 1.00 97.27 C ANISOU 3438 C ALA A 303 12514 14151 10292 -165 2531 756 C ATOM 3439 O ALA A 303 -45.351 -0.450 50.578 1.00 98.81 O ANISOU 3439 O ALA A 303 12747 14343 10455 -128 2812 712 O ATOM 3440 CB ALA A 303 -44.684 0.889 47.622 1.00 92.52 C ANISOU 3440 CB ALA A 303 11661 13568 9926 134 2278 770 C ATOM 3441 N PHE A 304 -44.157 -1.789 49.191 1.00 92.75 N ANISOU 3441 N PHE A 304 11835 13655 9749 -335 2358 812 N ATOM 3442 CA PHE A 304 -44.643 -3.061 49.722 1.00 93.60 C ANISOU 3442 CA PHE A 304 11859 13845 9861 -502 2465 834 C ATOM 3443 C PHE A 304 -43.837 -3.605 50.911 1.00 98.00 C ANISOU 3443 C PHE A 304 12761 14290 10183 -689 2486 839 C ATOM 3444 O PHE A 304 -44.403 -4.323 51.738 1.00 99.50 O ANISOU 3444 O PHE A 304 12968 14510 10327 -805 2669 841 O ATOM 3445 CB PHE A 304 -44.754 -4.108 48.600 1.00 94.17 C ANISOU 3445 CB PHE A 304 11642 14047 10093 -582 2270 889 C ATOM 3446 CG PHE A 304 -45.556 -3.680 47.388 1.00 96.22 C ANISOU 3446 CG PHE A 304 11562 14420 10578 -423 2217 897 C ATOM 3447 CD1 PHE A 304 -44.971 -3.630 46.131 1.00 97.36 C ANISOU 3447 CD1 PHE A 304 11621 14582 10790 -395 1946 925 C ATOM 3448 CD2 PHE A 304 -46.899 -3.337 47.505 1.00101.09 C ANISOU 3448 CD2 PHE A 304 11942 15130 11340 -304 2436 878 C ATOM 3449 CE1 PHE A 304 -45.714 -3.245 45.012 1.00 98.79 C ANISOU 3449 CE1 PHE A 304 11511 14859 11164 -260 1878 939 C ATOM 3450 CE2 PHE A 304 -47.637 -2.944 46.386 1.00104.34 C ANISOU 3450 CE2 PHE A 304 12036 15642 11965 -155 2359 894 C ATOM 3451 CZ PHE A 304 -47.039 -2.901 45.147 1.00100.43 C ANISOU 3451 CZ PHE A 304 11487 15151 11520 -140 2072 927 C ATOM 3452 N LEU A 305 -42.532 -3.264 51.000 1.00 92.59 N ANISOU 3452 N LEU A 305 12349 13480 9352 -728 2296 846 N ATOM 3453 CA LEU A 305 -41.632 -3.723 52.069 1.00102.82 C ANISOU 3453 CA LEU A 305 13983 14657 10426 -902 2261 860 C ATOM 3454 C LEU A 305 -40.988 -2.547 52.808 1.00112.87 C ANISOU 3454 C LEU A 305 15604 15770 11513 -854 2289 822 C ATOM 3455 O LEU A 305 -41.681 -1.639 53.264 1.00 72.82 O ANISOU 3455 O LEU A 305 10595 10660 6416 -729 2511 763 O ATOM 3456 CB LEU A 305 -40.538 -4.657 51.508 1.00100.43 C ANISOU 3456 CB LEU A 305 13675 14360 10125 -1030 1962 919 C ATOM 3457 CG LEU A 305 -40.952 -6.077 51.094 1.00104.55 C ANISOU 3457 CG LEU A 305 13975 14989 10759 -1141 1916 960 C ATOM 3458 CD1 LEU A 305 -41.451 -6.123 49.660 1.00103.88 C ANISOU 3458 CD1 LEU A 305 13534 15037 10898 -1038 1824 966 C ATOM 3459 CD2 LEU A 305 -39.781 -7.018 51.196 1.00105.44 C ANISOU 3459 CD2 LEU A 305 14238 15040 10784 -1288 1686 1007 C TER 3460 LEU A 305 ATOM 3461 N PRO B 27 -57.654 11.878 -1.659 1.00179.49 N ANISOU 3461 N PRO B 27 19264 34197 14735 -2160 1106 -529 N ATOM 3462 CA PRO B 27 -57.820 10.521 -1.115 1.00176.95 C ANISOU 3462 CA PRO B 27 18937 33564 14734 -1558 1113 -1078 C ATOM 3463 C PRO B 27 -57.346 10.390 0.334 1.00177.57 C ANISOU 3463 C PRO B 27 19011 33236 15220 -1432 1162 -1119 C ATOM 3464 O PRO B 27 -56.846 11.368 0.895 1.00176.83 O ANISOU 3464 O PRO B 27 18898 33145 15145 -1814 1201 -738 O ATOM 3465 CB PRO B 27 -57.011 9.657 -2.087 1.00183.37 C ANISOU 3465 CB PRO B 27 19374 35278 15022 -1282 1244 -1511 C ATOM 3466 CG PRO B 27 -57.088 10.394 -3.378 1.00191.79 C ANISOU 3466 CG PRO B 27 20380 36925 15568 -1679 1243 -1223 C ATOM 3467 CD PRO B 27 -57.067 11.856 -3.012 1.00186.59 C ANISOU 3467 CD PRO B 27 19865 36068 14963 -2288 1206 -575 C ATOM 3468 N CYS B 28 -57.508 9.182 0.936 1.00172.14 N ANISOU 3468 N CYS B 28 18366 32188 14853 -910 1140 -1574 N ATOM 3469 CA CYS B 28 -57.164 8.845 2.329 1.00169.14 C ANISOU 3469 CA CYS B 28 18014 31369 14882 -709 1162 -1672 C ATOM 3470 C CYS B 28 -57.890 9.786 3.323 1.00168.84 C ANISOU 3470 C CYS B 28 18297 30559 15294 -1013 1069 -1243 C ATOM 3471 O CYS B 28 -57.260 10.405 4.191 1.00167.63 O ANISOU 3471 O CYS B 28 18093 30361 15239 -1213 1127 -1022 O ATOM 3472 CB CYS B 28 -55.648 8.809 2.549 1.00172.22 C ANISOU 3472 CB CYS B 28 17998 32466 14972 -689 1338 -1768 C ATOM 3473 SG CYS B 28 -55.120 7.845 3.995 1.00173.93 S ANISOU 3473 SG CYS B 28 18191 32299 15595 -216 1347 -2109 S ATOM 3474 N PHE B 29 -59.231 9.905 3.154 1.00163.10 N ANISOU 3474 N PHE B 29 17891 29258 14820 -1038 913 -1141 N ATOM 3475 CA PHE B 29 -60.109 10.761 3.959 1.00159.29 C ANISOU 3475 CA PHE B 29 17721 28056 14744 -1263 799 -783 C ATOM 3476 C PHE B 29 -60.430 10.135 5.310 1.00158.47 C ANISOU 3476 C PHE B 29 17760 27305 15148 -980 775 -953 C ATOM 3477 O PHE B 29 -60.813 10.839 6.242 1.00154.98 O ANISOU 3477 O PHE B 29 17502 26362 15020 -1140 726 -689 O ATOM 3478 CB PHE B 29 -61.411 11.097 3.202 1.00160.96 C ANISOU 3478 CB PHE B 29 18173 27991 14993 -1364 637 -635 C ATOM 3479 CG PHE B 29 -61.251 11.589 1.781 1.00166.57 C ANISOU 3479 CG PHE B 29 18781 29314 15195 -1615 633 -485 C ATOM 3480 CD1 PHE B 29 -60.826 12.887 1.519 1.00171.43 C ANISOU 3480 CD1 PHE B 29 19399 30172 15565 -2090 630 -25 C ATOM 3481 CD2 PHE B 29 -61.576 10.773 0.705 1.00170.91 C ANISOU 3481 CD2 PHE B 29 19263 30169 15505 -1398 607 -788 C ATOM 3482 CE1 PHE B 29 -60.691 13.345 0.203 1.00176.18 C ANISOU 3482 CE1 PHE B 29 19920 31351 15671 -2356 616 149 C ATOM 3483 CE2 PHE B 29 -61.449 11.234 -0.611 1.00177.35 C ANISOU 3483 CE2 PHE B 29 19984 31577 15822 -1637 602 -640 C ATOM 3484 CZ PHE B 29 -61.005 12.516 -0.853 1.00177.12 C ANISOU 3484 CZ PHE B 29 19947 31813 15539 -2122 611 -160 C ATOM 3485 N ASN B 33 -62.852 1.922 6.880 1.00131.23 N ANISOU 3485 N ASN B 33 15084 21723 13055 1307 162 -3285 N ATOM 3486 CA ASN B 33 -63.137 0.506 6.677 1.00132.88 C ANISOU 3486 CA ASN B 33 15473 21667 13348 1642 -25 -3705 C ATOM 3487 C ASN B 33 -62.378 -0.385 7.676 1.00137.38 C ANISOU 3487 C ASN B 33 16107 22003 14089 1968 -68 -3924 C ATOM 3488 O ASN B 33 -61.174 -0.617 7.526 1.00139.16 O ANISOU 3488 O ASN B 33 16129 22679 14067 2235 1 -4144 O ATOM 3489 CB ASN B 33 -62.876 0.096 5.223 1.00136.91 C ANISOU 3489 CB ASN B 33 15868 22705 13448 1825 -62 -4033 C ATOM 3490 N ALA B 34 -63.097 -0.850 8.718 1.00132.10 N ANISOU 3490 N ALA B 34 15708 20650 13832 1932 -185 -3845 N ATOM 3491 CA ALA B 34 -62.594 -1.725 9.785 1.00131.95 C ANISOU 3491 CA ALA B 34 15829 20276 14032 2198 -272 -3996 C ATOM 3492 C ALA B 34 -63.629 -2.823 10.082 1.00135.63 C ANISOU 3492 C ALA B 34 16664 20065 14806 2239 -522 -4125 C ATOM 3493 O ALA B 34 -64.737 -2.539 10.556 1.00132.97 O ANISOU 3493 O ALA B 34 16466 19329 14729 1924 -546 -3852 O ATOM 3494 CB ALA B 34 -62.285 -0.915 11.043 1.00129.38 C ANISOU 3494 CB ALA B 34 15436 19836 13888 2006 -123 -3641 C ATOM 3495 N ASN B 35 -63.268 -4.075 9.755 1.00134.54 N ANISOU 3495 N ASN B 35 16678 19825 14615 2626 -724 -4553 N ATOM 3496 CA ASN B 35 -64.121 -5.254 9.922 1.00134.92 C ANISOU 3496 CA ASN B 35 17111 19237 14916 2679 -1012 -4724 C ATOM 3497 C ASN B 35 -64.147 -5.753 11.377 1.00136.57 C ANISOU 3497 C ASN B 35 17556 18865 15471 2676 -1104 -4588 C ATOM 3498 O ASN B 35 -65.222 -6.015 11.919 1.00134.49 O ANISOU 3498 O ASN B 35 17530 18080 15489 2403 -1217 -4406 O ATOM 3499 CB ASN B 35 -63.658 -6.366 8.964 1.00138.07 C ANISOU 3499 CB ASN B 35 17611 19748 15102 3121 -1221 -5258 C ATOM 3500 CG ASN B 35 -64.682 -7.430 8.634 1.00151.86 C ANISOU 3500 CG ASN B 35 19736 20949 17013 3103 -1536 -5460 C ATOM 3501 OD1 ASN B 35 -65.829 -7.418 9.097 1.00140.25 O ANISOU 3501 OD1 ASN B 35 18451 19016 15823 2733 -1608 -5196 O ATOM 3502 ND2 ASN B 35 -64.282 -8.381 7.805 1.00146.85 N ANISOU 3502 ND2 ASN B 35 19218 20388 16191 3507 -1742 -5949 N ATOM 3503 N PHE B 36 -62.960 -5.876 11.996 1.00133.39 N ANISOU 3503 N PHE B 36 17066 18595 15020 2969 -1056 -4671 N ATOM 3504 CA PHE B 36 -62.778 -6.361 13.364 1.00132.31 C ANISOU 3504 CA PHE B 36 17140 17975 15159 3021 -1149 -4562 C ATOM 3505 C PHE B 36 -63.349 -5.434 14.438 1.00130.20 C ANISOU 3505 C PHE B 36 16827 17532 15113 2591 -973 -4075 C ATOM 3506 O PHE B 36 -63.919 -5.922 15.416 1.00129.05 O ANISOU 3506 O PHE B 36 16947 16842 15245 2460 -1096 -3926 O ATOM 3507 CB PHE B 36 -61.293 -6.682 13.629 1.00136.68 C ANISOU 3507 CB PHE B 36 17565 18808 15558 3486 -1147 -4807 C ATOM 3508 CG PHE B 36 -60.930 -6.963 15.070 1.00137.71 C ANISOU 3508 CG PHE B 36 17847 18553 15925 3540 -1203 -4651 C ATOM 3509 CD1 PHE B 36 -61.277 -8.170 15.671 1.00143.09 C ANISOU 3509 CD1 PHE B 36 18961 18561 16847 3667 -1514 -4751 C ATOM 3510 CD2 PHE B 36 -60.244 -6.021 15.828 1.00137.63 C ANISOU 3510 CD2 PHE B 36 17564 18843 15884 3443 -965 -4392 C ATOM 3511 CE1 PHE B 36 -60.949 -8.424 17.005 1.00143.44 C ANISOU 3511 CE1 PHE B 36 19155 18259 17087 3701 -1575 -4583 C ATOM 3512 CE2 PHE B 36 -59.916 -6.277 17.162 1.00139.81 C ANISOU 3512 CE2 PHE B 36 17979 18781 16360 3492 -1024 -4249 C ATOM 3513 CZ PHE B 36 -60.262 -7.481 17.736 1.00139.87 C ANISOU 3513 CZ PHE B 36 18409 18143 16592 3629 -1324 -4343 C ATOM 3514 N ASN B 37 -63.177 -4.110 14.275 1.00122.92 N ANISOU 3514 N ASN B 37 15582 17070 14054 2375 -700 -3831 N ATOM 3515 CA ASN B 37 -63.662 -3.122 15.244 1.00118.10 C ANISOU 3515 CA ASN B 37 14914 16334 13623 2009 -535 -3402 C ATOM 3516 C ASN B 37 -65.197 -3.038 15.357 1.00118.58 C ANISOU 3516 C ASN B 37 15137 16014 13902 1649 -590 -3190 C ATOM 3517 O ASN B 37 -65.700 -2.439 16.305 1.00115.46 O ANISOU 3517 O ASN B 37 14742 15440 13687 1391 -495 -2878 O ATOM 3518 CB ASN B 37 -63.010 -1.750 15.015 1.00116.29 C ANISOU 3518 CB ASN B 37 14339 16664 13183 1886 -274 -3216 C ATOM 3519 CG ASN B 37 -61.605 -1.617 15.572 1.00131.69 C ANISOU 3519 CG ASN B 37 16116 18903 15019 2106 -183 -3264 C ATOM 3520 OD1 ASN B 37 -60.816 -2.571 15.623 1.00126.33 O ANISOU 3520 OD1 ASN B 37 15484 18230 14287 2484 -306 -3563 O ATOM 3521 ND2 ASN B 37 -61.250 -0.408 15.977 1.00119.47 N ANISOU 3521 ND2 ASN B 37 14359 17611 13421 1881 16 -2980 N ATOM 3522 N LYS B 38 -65.933 -3.679 14.430 1.00115.82 N ANISOU 3522 N LYS B 38 14918 15557 13531 1646 -755 -3379 N ATOM 3523 CA LYS B 38 -67.396 -3.723 14.455 1.00114.14 C ANISOU 3523 CA LYS B 38 14836 15025 13507 1314 -835 -3216 C ATOM 3524 C LYS B 38 -67.902 -5.033 15.084 1.00116.86 C ANISOU 3524 C LYS B 38 15532 14785 14085 1310 -1091 -3299 C ATOM 3525 O LYS B 38 -69.059 -5.411 14.905 1.00116.91 O ANISOU 3525 O LYS B 38 15675 14530 14213 1068 -1224 -3259 O ATOM 3526 CB LYS B 38 -67.979 -3.461 13.051 1.00118.62 C ANISOU 3526 CB LYS B 38 15306 15868 13896 1241 -855 -3319 C ATOM 3527 CG LYS B 38 -68.344 -1.993 12.790 1.00136.81 C ANISOU 3527 CG LYS B 38 17352 18514 16117 990 -641 -3022 C ATOM 3528 CD LYS B 38 -67.135 -1.074 12.514 1.00148.09 C ANISOU 3528 CD LYS B 38 18526 20451 17290 1107 -440 -2987 C ATOM 3529 CE LYS B 38 -67.008 0.017 13.553 1.00155.91 C ANISOU 3529 CE LYS B 38 19409 21439 18391 924 -258 -2639 C ATOM 3530 NZ LYS B 38 -65.754 0.802 13.387 1.00164.76 N ANISOU 3530 NZ LYS B 38 20306 23023 19274 1004 -91 -2603 N ATOM 3531 N ILE B 39 -67.017 -5.711 15.832 1.00112.79 N ANISOU 3531 N ILE B 39 15162 14072 13621 1563 -1174 -3402 N ATOM 3532 CA ILE B 39 -67.297 -6.934 16.582 1.00113.93 C ANISOU 3532 CA ILE B 39 15678 13632 13979 1570 -1435 -3444 C ATOM 3533 C ILE B 39 -66.600 -6.865 17.946 1.00114.14 C ANISOU 3533 C ILE B 39 15734 13526 14110 1637 -1369 -3267 C ATOM 3534 O ILE B 39 -67.076 -7.464 18.906 1.00113.94 O ANISOU 3534 O ILE B 39 15962 13044 14287 1473 -1502 -3112 O ATOM 3535 CB ILE B 39 -67.021 -8.240 15.773 1.00121.78 C ANISOU 3535 CB ILE B 39 16947 14416 14908 1892 -1750 -3873 C ATOM 3536 CG1 ILE B 39 -68.076 -9.325 16.061 1.00124.65 C ANISOU 3536 CG1 ILE B 39 17710 14154 15496 1653 -2056 -3850 C ATOM 3537 CG2 ILE B 39 -65.596 -8.770 15.934 1.00124.67 C ANISOU 3537 CG2 ILE B 39 17357 14844 15168 2399 -1827 -4150 C ATOM 3538 CD1 ILE B 39 -69.188 -9.398 15.022 1.00132.31 C ANISOU 3538 CD1 ILE B 39 18691 15142 16441 1409 -2144 -3919 C ATOM 3539 N PHE B 40 -65.496 -6.103 18.027 1.00108.12 N ANISOU 3539 N PHE B 40 14700 13189 13191 1842 -1164 -3272 N ATOM 3540 CA PHE B 40 -64.747 -5.904 19.261 1.00106.28 C ANISOU 3540 CA PHE B 40 14446 12913 13024 1914 -1084 -3113 C ATOM 3541 C PHE B 40 -65.479 -4.865 20.123 1.00104.34 C ANISOU 3541 C PHE B 40 14076 12668 12901 1509 -872 -2706 C ATOM 3542 O PHE B 40 -66.036 -5.223 21.163 1.00103.66 O ANISOU 3542 O PHE B 40 14182 12203 13003 1320 -940 -2510 O ATOM 3543 CB PHE B 40 -63.297 -5.475 18.952 1.00108.82 C ANISOU 3543 CB PHE B 40 14496 13740 13112 2264 -956 -3288 C ATOM 3544 CG PHE B 40 -62.408 -5.275 20.159 1.00109.95 C ANISOU 3544 CG PHE B 40 14590 13890 13295 2369 -888 -3157 C ATOM 3545 CD1 PHE B 40 -62.329 -4.038 20.790 1.00110.11 C ANISOU 3545 CD1 PHE B 40 14376 14146 13314 2123 -633 -2852 C ATOM 3546 CD2 PHE B 40 -61.626 -6.315 20.647 1.00115.18 C ANISOU 3546 CD2 PHE B 40 15452 14322 13988 2733 -1101 -3354 C ATOM 3547 CE1 PHE B 40 -61.506 -3.854 21.905 1.00110.42 C ANISOU 3547 CE1 PHE B 40 14372 14203 13381 2211 -582 -2741 C ATOM 3548 CE2 PHE B 40 -60.787 -6.126 21.751 1.00117.46 C ANISOU 3548 CE2 PHE B 40 15684 14645 14300 2839 -1049 -3235 C ATOM 3549 CZ PHE B 40 -60.735 -4.897 22.373 1.00112.22 C ANISOU 3549 CZ PHE B 40 14774 14233 13631 2565 -784 -2929 C ATOM 3550 N LEU B 41 -65.505 -3.588 19.661 1.00 96.57 N ANISOU 3550 N LEU B 41 12783 12114 11794 1376 -633 -2584 N ATOM 3551 CA LEU B 41 -66.139 -2.446 20.336 1.00 92.13 C ANISOU 3551 CA LEU B 41 12082 11608 11316 1051 -437 -2242 C ATOM 3552 C LEU B 41 -67.564 -2.704 20.867 1.00 93.68 C ANISOU 3552 C LEU B 41 12431 11446 11717 731 -502 -2053 C ATOM 3553 O LEU B 41 -67.777 -2.449 22.053 1.00 91.71 O ANISOU 3553 O LEU B 41 12204 11057 11586 583 -432 -1827 O ATOM 3554 CB LEU B 41 -66.100 -1.148 19.499 1.00 90.48 C ANISOU 3554 CB LEU B 41 11588 11852 10939 959 -246 -2172 C ATOM 3555 CG LEU B 41 -64.764 -0.690 18.904 1.00 95.64 C ANISOU 3555 CG LEU B 41 12027 12968 11345 1179 -147 -2305 C ATOM 3556 CD1 LEU B 41 -64.977 0.462 17.952 1.00 94.97 C ANISOU 3556 CD1 LEU B 41 11729 13260 11095 1014 -13 -2206 C ATOM 3557 CD2 LEU B 41 -63.775 -0.285 19.973 1.00 96.75 C ANISOU 3557 CD2 LEU B 41 12086 13185 11488 1246 -45 -2195 C ATOM 3558 N PRO B 42 -68.543 -3.231 20.077 1.00 90.26 N ANISOU 3558 N PRO B 42 12093 10885 11318 608 -638 -2140 N ATOM 3559 CA PRO B 42 -69.885 -3.466 20.647 1.00 89.24 C ANISOU 3559 CA PRO B 42 12063 10478 11366 269 -693 -1944 C ATOM 3560 C PRO B 42 -69.910 -4.489 21.788 1.00 92.38 C ANISOU 3560 C PRO B 42 12737 10450 11914 212 -843 -1870 C ATOM 3561 O PRO B 42 -70.741 -4.360 22.683 1.00 91.12 O ANISOU 3561 O PRO B 42 12582 10171 11868 -77 -797 -1624 O ATOM 3562 CB PRO B 42 -70.707 -3.933 19.442 1.00 92.83 C ANISOU 3562 CB PRO B 42 12565 10913 11794 188 -842 -2103 C ATOM 3563 CG PRO B 42 -69.703 -4.510 18.508 1.00 99.65 C ANISOU 3563 CG PRO B 42 13500 11855 12507 538 -955 -2434 C ATOM 3564 CD PRO B 42 -68.506 -3.623 18.651 1.00 93.68 C ANISOU 3564 CD PRO B 42 12529 11454 11611 751 -749 -2417 C ATOM 3565 N THR B 43 -68.992 -5.482 21.761 1.00 89.57 N ANISOU 3565 N THR B 43 12606 9886 11539 499 -1028 -2083 N ATOM 3566 CA THR B 43 -68.895 -6.517 22.794 1.00 90.39 C ANISOU 3566 CA THR B 43 13026 9546 11772 479 -1219 -2017 C ATOM 3567 C THR B 43 -68.341 -5.908 24.070 1.00 90.53 C ANISOU 3567 C THR B 43 12949 9642 11806 484 -1046 -1795 C ATOM 3568 O THR B 43 -68.898 -6.139 25.144 1.00 90.07 O ANISOU 3568 O THR B 43 13012 9353 11856 230 -1066 -1554 O ATOM 3569 CB THR B 43 -68.053 -7.707 22.310 1.00100.19 C ANISOU 3569 CB THR B 43 14546 10542 12980 847 -1500 -2343 C ATOM 3570 OG1 THR B 43 -68.453 -8.068 20.989 1.00101.44 O ANISOU 3570 OG1 THR B 43 14737 10728 13078 887 -1626 -2593 O ATOM 3571 CG2 THR B 43 -68.167 -8.915 23.229 1.00100.85 C ANISOU 3571 CG2 THR B 43 15040 10067 13210 783 -1778 -2269 C ATOM 3572 N ILE B 44 -67.264 -5.108 23.942 1.00 84.46 N ANISOU 3572 N ILE B 44 11952 9228 10909 743 -875 -1868 N ATOM 3573 CA ILE B 44 -66.611 -4.422 25.055 1.00 81.91 C ANISOU 3573 CA ILE B 44 11514 9031 10577 770 -710 -1690 C ATOM 3574 C ILE B 44 -67.564 -3.422 25.728 1.00 82.70 C ANISOU 3574 C ILE B 44 11453 9234 10735 419 -505 -1392 C ATOM 3575 O ILE B 44 -67.662 -3.428 26.958 1.00 82.21 O ANISOU 3575 O ILE B 44 11458 9040 10737 297 -475 -1191 O ATOM 3576 CB ILE B 44 -65.219 -3.848 24.644 1.00 84.34 C ANISOU 3576 CB ILE B 44 11605 9724 10717 1103 -602 -1857 C ATOM 3577 CG1 ILE B 44 -64.108 -4.909 24.804 1.00 87.57 C ANISOU 3577 CG1 ILE B 44 12197 9980 11097 1486 -808 -2078 C ATOM 3578 CG2 ILE B 44 -64.848 -2.594 25.426 1.00 82.04 C ANISOU 3578 CG2 ILE B 44 11081 9703 10389 1009 -360 -1645 C ATOM 3579 CD1 ILE B 44 -63.981 -5.933 23.674 1.00 98.25 C ANISOU 3579 CD1 ILE B 44 13706 11224 12401 1744 -1037 -2417 C ATOM 3580 N TYR B 45 -68.312 -2.624 24.930 1.00 76.98 N ANISOU 3580 N TYR B 45 10531 8739 9979 270 -387 -1372 N ATOM 3581 CA TYR B 45 -69.285 -1.673 25.475 1.00 74.28 C ANISOU 3581 CA TYR B 45 10030 8508 9685 -9 -218 -1133 C ATOM 3582 C TYR B 45 -70.372 -2.397 26.261 1.00 79.65 C ANISOU 3582 C TYR B 45 10862 8911 10488 -294 -308 -973 C ATOM 3583 O TYR B 45 -70.616 -2.036 27.410 1.00 78.77 O ANISOU 3583 O TYR B 45 10714 8806 10408 -432 -203 -771 O ATOM 3584 CB TYR B 45 -69.909 -0.781 24.382 1.00 73.91 C ANISOU 3584 CB TYR B 45 9773 8731 9579 -80 -128 -1159 C ATOM 3585 CG TYR B 45 -68.931 0.100 23.632 1.00 74.21 C ANISOU 3585 CG TYR B 45 9640 9088 9466 117 -23 -1254 C ATOM 3586 CD1 TYR B 45 -67.808 0.631 24.266 1.00 75.08 C ANISOU 3586 CD1 TYR B 45 9687 9323 9516 251 79 -1217 C ATOM 3587 CD2 TYR B 45 -69.153 0.447 22.303 1.00 74.95 C ANISOU 3587 CD2 TYR B 45 9628 9388 9462 133 -28 -1360 C ATOM 3588 CE1 TYR B 45 -66.904 1.438 23.579 1.00 74.66 C ANISOU 3588 CE1 TYR B 45 9466 9597 9306 373 169 -1280 C ATOM 3589 CE2 TYR B 45 -68.254 1.251 21.605 1.00 75.07 C ANISOU 3589 CE2 TYR B 45 9487 9729 9308 264 65 -1416 C ATOM 3590 CZ TYR B 45 -67.134 1.748 22.250 1.00 80.59 C ANISOU 3590 CZ TYR B 45 10119 10553 9948 368 165 -1369 C ATOM 3591 OH TYR B 45 -66.261 2.559 21.573 1.00 81.62 O ANISOU 3591 OH TYR B 45 10082 11034 9895 437 253 -1397 O ATOM 3592 N SER B 46 -70.968 -3.458 25.667 1.00 78.15 N ANISOU 3592 N SER B 46 10853 8487 10352 -390 -513 -1065 N ATOM 3593 CA SER B 46 -72.024 -4.270 26.279 1.00 79.60 C ANISOU 3593 CA SER B 46 11197 8409 10637 -721 -635 -908 C ATOM 3594 C SER B 46 -71.574 -4.920 27.582 1.00 84.48 C ANISOU 3594 C SER B 46 12038 8764 11295 -748 -709 -764 C ATOM 3595 O SER B 46 -72.364 -4.997 28.526 1.00 84.70 O ANISOU 3595 O SER B 46 12072 8751 11359 -1056 -673 -528 O ATOM 3596 CB SER B 46 -72.525 -5.328 25.304 1.00 85.46 C ANISOU 3596 CB SER B 46 12135 8918 11419 -794 -886 -1068 C ATOM 3597 OG SER B 46 -72.963 -4.726 24.097 1.00 92.66 O ANISOU 3597 OG SER B 46 12838 10095 12275 -775 -825 -1193 O ATOM 3598 N ILE B 47 -70.302 -5.360 27.640 1.00 81.20 N ANISOU 3598 N ILE B 47 11787 8212 10854 -418 -810 -906 N ATOM 3599 CA ILE B 47 -69.700 -5.970 28.825 1.00 82.11 C ANISOU 3599 CA ILE B 47 12130 8075 10993 -375 -907 -788 C ATOM 3600 C ILE B 47 -69.592 -4.933 29.956 1.00 83.48 C ANISOU 3600 C ILE B 47 12092 8504 11123 -446 -653 -573 C ATOM 3601 O ILE B 47 -70.067 -5.195 31.061 1.00 84.13 O ANISOU 3601 O ILE B 47 12270 8471 11227 -693 -658 -339 O ATOM 3602 CB ILE B 47 -68.363 -6.694 28.469 1.00 86.87 C ANISOU 3602 CB ILE B 47 12933 8505 11568 57 -1102 -1041 C ATOM 3603 CG1 ILE B 47 -68.658 -8.107 27.910 1.00 91.34 C ANISOU 3603 CG1 ILE B 47 13871 8627 12208 50 -1450 -1181 C ATOM 3604 CG2 ILE B 47 -67.399 -6.766 29.668 1.00 87.31 C ANISOU 3604 CG2 ILE B 47 13078 8493 11604 220 -1108 -939 C ATOM 3605 CD1 ILE B 47 -67.565 -8.737 27.013 1.00101.68 C ANISOU 3605 CD1 ILE B 47 15315 9851 13468 531 -1647 -1551 C ATOM 3606 N ILE B 48 -69.023 -3.747 29.655 1.00 77.22 N ANISOU 3606 N ILE B 48 11019 8066 10255 -260 -441 -648 N ATOM 3607 CA ILE B 48 -68.869 -2.637 30.603 1.00 74.60 C ANISOU 3607 CA ILE B 48 10488 7980 9875 -298 -213 -489 C ATOM 3608 C ILE B 48 -70.247 -2.119 31.038 1.00 77.99 C ANISOU 3608 C ILE B 48 10778 8529 10328 -635 -81 -297 C ATOM 3609 O ILE B 48 -70.428 -1.793 32.209 1.00 77.23 O ANISOU 3609 O ILE B 48 10646 8492 10206 -756 21 -118 O ATOM 3610 CB ILE B 48 -67.910 -1.545 30.036 1.00 75.33 C ANISOU 3610 CB ILE B 48 10353 8389 9880 -45 -67 -623 C ATOM 3611 CG1 ILE B 48 -66.460 -2.070 30.050 1.00 76.92 C ANISOU 3611 CG1 ILE B 48 10656 8539 10030 282 -177 -773 C ATOM 3612 CG2 ILE B 48 -68.000 -0.215 30.811 1.00 73.13 C ANISOU 3612 CG2 ILE B 48 9866 8359 9559 -129 156 -474 C ATOM 3613 CD1 ILE B 48 -65.567 -1.544 28.967 1.00 83.70 C ANISOU 3613 CD1 ILE B 48 11335 9682 10786 525 -125 -981 C ATOM 3614 N PHE B 49 -71.222 -2.121 30.113 1.00 74.78 N ANISOU 3614 N PHE B 49 10289 8171 9954 -778 -99 -345 N ATOM 3615 CA PHE B 49 -72.601 -1.707 30.367 1.00 74.69 C ANISOU 3615 CA PHE B 49 10107 8317 9955 -1076 4 -199 C ATOM 3616 C PHE B 49 -73.265 -2.568 31.470 1.00 81.02 C ANISOU 3616 C PHE B 49 11053 8956 10775 -1385 -66 14 C ATOM 3617 O PHE B 49 -73.762 -2.004 32.443 1.00 79.74 O ANISOU 3617 O PHE B 49 10742 8991 10563 -1528 90 175 O ATOM 3618 CB PHE B 49 -73.417 -1.715 29.056 1.00 76.90 C ANISOU 3618 CB PHE B 49 10292 8665 10262 -1147 -51 -314 C ATOM 3619 CG PHE B 49 -74.916 -1.663 29.216 1.00 79.62 C ANISOU 3619 CG PHE B 49 10484 9141 10625 -1475 -14 -184 C ATOM 3620 CD1 PHE B 49 -75.689 -2.805 29.043 1.00 86.12 C ANISOU 3620 CD1 PHE B 49 11453 9771 11499 -1757 -196 -142 C ATOM 3621 CD2 PHE B 49 -75.557 -0.472 29.534 1.00 80.16 C ANISOU 3621 CD2 PHE B 49 10263 9541 10654 -1500 183 -113 C ATOM 3622 CE1 PHE B 49 -77.079 -2.757 29.189 1.00 88.48 C ANISOU 3622 CE1 PHE B 49 11564 10259 11795 -2086 -158 -18 C ATOM 3623 CE2 PHE B 49 -76.946 -0.424 29.680 1.00 84.53 C ANISOU 3623 CE2 PHE B 49 10630 10284 11205 -1772 218 -15 C ATOM 3624 CZ PHE B 49 -77.697 -1.567 29.508 1.00 85.72 C ANISOU 3624 CZ PHE B 49 10883 10292 11393 -2077 58 38 C ATOM 3625 N LEU B 50 -73.237 -3.916 31.331 1.00 80.35 N ANISOU 3625 N LEU B 50 11270 8515 10744 -1485 -312 12 N ATOM 3626 CA LEU B 50 -73.825 -4.843 32.307 1.00 82.65 C ANISOU 3626 CA LEU B 50 11752 8610 11041 -1828 -424 243 C ATOM 3627 C LEU B 50 -73.116 -4.757 33.649 1.00 85.58 C ANISOU 3627 C LEU B 50 12206 8960 11350 -1768 -363 395 C ATOM 3628 O LEU B 50 -73.774 -4.539 34.663 1.00 85.78 O ANISOU 3628 O LEU B 50 12128 9157 11306 -2029 -243 611 O ATOM 3629 CB LEU B 50 -73.821 -6.300 31.797 1.00 86.12 C ANISOU 3629 CB LEU B 50 12564 8598 11559 -1921 -755 192 C ATOM 3630 CG LEU B 50 -74.635 -6.628 30.540 1.00 92.38 C ANISOU 3630 CG LEU B 50 13333 9360 12407 -2053 -871 57 C ATOM 3631 CD1 LEU B 50 -74.240 -7.983 29.992 1.00 95.86 C ANISOU 3631 CD1 LEU B 50 14193 9308 12919 -2001 -1224 -73 C ATOM 3632 CD2 LEU B 50 -76.138 -6.603 30.813 1.00 96.79 C ANISOU 3632 CD2 LEU B 50 13710 10114 12950 -2534 -810 260 C ATOM 3633 N THR B 51 -71.773 -4.891 33.642 1.00 81.14 N ANISOU 3633 N THR B 51 11799 8237 10792 -1412 -440 269 N ATOM 3634 CA THR B 51 -70.902 -4.836 34.825 1.00 80.65 C ANISOU 3634 CA THR B 51 11830 8145 10669 -1293 -415 378 C ATOM 3635 C THR B 51 -70.991 -3.472 35.536 1.00 82.62 C ANISOU 3635 C THR B 51 11762 8801 10829 -1285 -117 450 C ATOM 3636 O THR B 51 -70.973 -3.423 36.764 1.00 82.44 O ANISOU 3636 O THR B 51 11767 8828 10728 -1395 -60 635 O ATOM 3637 CB THR B 51 -69.458 -5.211 34.442 1.00 85.96 C ANISOU 3637 CB THR B 51 12675 8626 11361 -873 -567 175 C ATOM 3638 OG1 THR B 51 -69.473 -6.261 33.475 1.00 87.74 O ANISOU 3638 OG1 THR B 51 13140 8532 11666 -816 -826 21 O ATOM 3639 CG2 THR B 51 -68.617 -5.624 35.638 1.00 84.65 C ANISOU 3639 CG2 THR B 51 12711 8305 11148 -777 -656 301 C ATOM 3640 N GLY B 52 -71.106 -2.398 34.755 1.00 77.39 N ANISOU 3640 N GLY B 52 10826 8410 10170 -1159 46 305 N ATOM 3641 CA GLY B 52 -71.246 -1.035 35.252 1.00 75.07 C ANISOU 3641 CA GLY B 52 10257 8463 9806 -1125 291 333 C ATOM 3642 C GLY B 52 -72.585 -0.806 35.919 1.00 80.90 C ANISOU 3642 C GLY B 52 10840 9404 10494 -1435 410 499 C ATOM 3643 O GLY B 52 -72.627 -0.468 37.102 1.00 81.12 O ANISOU 3643 O GLY B 52 10821 9573 10428 -1499 519 628 O ATOM 3644 N ILE B 53 -73.693 -1.037 35.179 1.00 78.29 N ANISOU 3644 N ILE B 53 10417 9120 10208 -1632 383 491 N ATOM 3645 CA ILE B 53 -75.063 -0.863 35.673 1.00 79.13 C ANISOU 3645 CA ILE B 53 10320 9492 10256 -1935 492 629 C ATOM 3646 C ILE B 53 -75.396 -1.744 36.904 1.00 84.41 C ANISOU 3646 C ILE B 53 11126 10105 10842 -2253 449 878 C ATOM 3647 O ILE B 53 -76.114 -1.290 37.797 1.00 84.56 O ANISOU 3647 O ILE B 53 10942 10447 10740 -2413 609 998 O ATOM 3648 CB ILE B 53 -76.107 -0.922 34.512 1.00 83.05 C ANISOU 3648 CB ILE B 53 10670 10071 10816 -2063 451 550 C ATOM 3649 CG1 ILE B 53 -77.305 0.036 34.728 1.00 83.54 C ANISOU 3649 CG1 ILE B 53 10364 10571 10807 -2154 638 573 C ATOM 3650 CG2 ILE B 53 -76.501 -2.357 34.086 1.00 87.20 C ANISOU 3650 CG2 ILE B 53 11425 10301 11404 -2344 219 614 C ATOM 3651 CD1 ILE B 53 -78.530 -0.496 35.561 1.00 95.76 C ANISOU 3651 CD1 ILE B 53 11783 12342 12259 -2566 676 776 C ATOM 3652 N VAL B 54 -74.842 -2.971 36.968 1.00 81.88 N ANISOU 3652 N VAL B 54 11157 9387 10568 -2325 222 951 N ATOM 3653 CA VAL B 54 -75.050 -3.869 38.109 1.00 84.33 C ANISOU 3653 CA VAL B 54 11663 9585 10792 -2640 137 1218 C ATOM 3654 C VAL B 54 -74.122 -3.428 39.246 1.00 86.96 C ANISOU 3654 C VAL B 54 12038 9976 11025 -2448 229 1275 C ATOM 3655 O VAL B 54 -74.599 -3.126 40.341 1.00 87.76 O ANISOU 3655 O VAL B 54 12010 10357 10976 -2633 374 1443 O ATOM 3656 CB VAL B 54 -74.884 -5.372 37.736 1.00 90.69 C ANISOU 3656 CB VAL B 54 12878 9892 11690 -2799 -191 1281 C ATOM 3657 CG1 VAL B 54 -74.816 -6.261 38.974 1.00 93.30 C ANISOU 3657 CG1 VAL B 54 13485 10039 11925 -3076 -317 1576 C ATOM 3658 CG2 VAL B 54 -76.003 -5.834 36.807 1.00 92.28 C ANISOU 3658 CG2 VAL B 54 13025 10080 11959 -3093 -282 1266 C ATOM 3659 N GLY B 55 -72.821 -3.376 38.957 1.00 81.10 N ANISOU 3659 N GLY B 55 11451 9015 10349 -2078 146 1122 N ATOM 3660 CA GLY B 55 -71.778 -2.996 39.902 1.00 79.65 C ANISOU 3660 CA GLY B 55 11320 8860 10085 -1861 196 1145 C ATOM 3661 C GLY B 55 -72.038 -1.685 40.607 1.00 81.73 C ANISOU 3661 C GLY B 55 11274 9550 10228 -1823 469 1142 C ATOM 3662 O GLY B 55 -72.209 -1.670 41.828 1.00 82.09 O ANISOU 3662 O GLY B 55 11320 9742 10129 -1973 539 1317 O ATOM 3663 N ASN B 56 -72.079 -0.598 39.843 1.00 76.71 N ANISOU 3663 N ASN B 56 10398 9107 9641 -1625 604 943 N ATOM 3664 CA ASN B 56 -72.341 0.724 40.397 1.00 75.41 C ANISOU 3664 CA ASN B 56 9968 9305 9379 -1546 827 898 C ATOM 3665 C ASN B 56 -73.717 0.817 41.046 1.00 81.95 C ANISOU 3665 C ASN B 56 10602 10444 10090 -1836 957 1030 C ATOM 3666 O ASN B 56 -73.846 1.278 42.180 1.00 81.86 O ANISOU 3666 O ASN B 56 10501 10679 9924 -1867 1085 1102 O ATOM 3667 CB ASN B 56 -72.196 1.796 39.315 1.00 73.04 C ANISOU 3667 CB ASN B 56 9495 9093 9164 -1305 895 677 C ATOM 3668 CG ASN B 56 -70.755 2.012 38.897 1.00 94.99 C ANISOU 3668 CG ASN B 56 12387 11712 11995 -1018 824 549 C ATOM 3669 OD1 ASN B 56 -69.947 2.540 39.662 1.00 90.25 O ANISOU 3669 OD1 ASN B 56 11799 11169 11323 -888 869 545 O ATOM 3670 ND2 ASN B 56 -70.424 1.602 37.678 1.00 84.77 N ANISOU 3670 ND2 ASN B 56 11156 10247 10805 -925 710 435 N ATOM 3671 N GLY B 57 -74.745 0.378 40.325 1.00 80.44 N ANISOU 3671 N GLY B 57 10328 10280 9955 -2048 923 1051 N ATOM 3672 CA GLY B 57 -76.126 0.426 40.857 1.00 82.78 C ANISOU 3672 CA GLY B 57 10383 10945 10125 -2346 1047 1171 C ATOM 3673 C GLY B 57 -76.185 -0.197 42.238 1.00 89.18 C ANISOU 3673 C GLY B 57 11295 11830 10759 -2606 1059 1417 C ATOM 3674 O GLY B 57 -76.864 0.299 43.121 1.00 89.35 O ANISOU 3674 O GLY B 57 11086 12264 10600 -2708 1233 1476 O ATOM 3675 N LEU B 58 -75.458 -1.292 42.432 1.00 87.46 N ANISOU 3675 N LEU B 58 11431 11221 10579 -2698 861 1557 N ATOM 3676 CA LEU B 58 -75.307 -1.864 43.758 1.00 90.13 C ANISOU 3676 CA LEU B 58 11924 11578 10743 -2912 840 1807 C ATOM 3677 C LEU B 58 -74.679 -0.855 44.697 1.00 95.71 C ANISOU 3677 C LEU B 58 12528 12518 11318 -2650 1003 1736 C ATOM 3678 O LEU B 58 -75.200 -0.605 45.775 1.00 96.51 O ANISOU 3678 O LEU B 58 12485 12982 11204 -2811 1148 1857 O ATOM 3679 CB LEU B 58 -74.429 -3.099 43.731 1.00 90.94 C ANISOU 3679 CB LEU B 58 12468 11155 10932 -2945 557 1928 C ATOM 3680 CG LEU B 58 -75.091 -4.412 43.410 1.00 97.90 C ANISOU 3680 CG LEU B 58 13566 11774 11859 -3348 343 2122 C ATOM 3681 CD1 LEU B 58 -73.975 -5.475 43.181 1.00 98.42 C ANISOU 3681 CD1 LEU B 58 14104 11238 12052 -3206 22 2139 C ATOM 3682 CD2 LEU B 58 -76.083 -4.770 44.518 1.00103.33 C ANISOU 3682 CD2 LEU B 58 14173 12772 12316 -3839 420 2436 C ATOM 3683 N VAL B 59 -73.545 -0.282 44.311 1.00 92.59 N ANISOU 3683 N VAL B 59 12205 11942 11034 -2262 975 1539 N ATOM 3684 CA VAL B 59 -72.932 0.704 45.187 1.00 92.72 C ANISOU 3684 CA VAL B 59 12137 12163 10927 -2034 1107 1463 C ATOM 3685 C VAL B 59 -73.980 1.729 45.582 1.00102.03 C ANISOU 3685 C VAL B 59 12970 13828 11968 -2062 1340 1392 C ATOM 3686 O VAL B 59 -74.215 1.925 46.759 1.00103.52 O ANISOU 3686 O VAL B 59 13086 14306 11942 -2152 1449 1485 O ATOM 3687 CB VAL B 59 -71.710 1.417 44.563 1.00 93.18 C ANISOU 3687 CB VAL B 59 12240 12044 11119 -1640 1069 1235 C ATOM 3688 CG1 VAL B 59 -71.224 2.547 45.497 1.00 91.87 C ANISOU 3688 CG1 VAL B 59 11970 12119 10817 -1450 1203 1151 C ATOM 3689 CG2 VAL B 59 -70.595 0.422 44.299 1.00 93.07 C ANISOU 3689 CG2 VAL B 59 12536 11621 11205 -1554 842 1276 C ATOM 3690 N ILE B 60 -74.635 2.332 44.595 1.00101.14 N ANISOU 3690 N ILE B 60 12647 13819 11965 -1978 1400 1225 N ATOM 3691 CA ILE B 60 -75.628 3.390 44.842 1.00103.12 C ANISOU 3691 CA ILE B 60 12557 14522 12101 -1921 1594 1105 C ATOM 3692 C ILE B 60 -76.744 2.940 45.808 1.00114.83 C ANISOU 3692 C ILE B 60 13868 16411 13352 -2260 1706 1292 C ATOM 3693 O ILE B 60 -77.097 3.674 46.723 1.00115.38 O ANISOU 3693 O ILE B 60 13742 16876 13220 -2188 1866 1236 O ATOM 3694 CB ILE B 60 -76.246 3.910 43.530 1.00104.97 C ANISOU 3694 CB ILE B 60 12615 14773 12494 -1807 1596 930 C ATOM 3695 CG1 ILE B 60 -75.170 4.583 42.671 1.00101.94 C ANISOU 3695 CG1 ILE B 60 12359 14091 12284 -1477 1518 746 C ATOM 3696 CG2 ILE B 60 -77.372 4.918 43.813 1.00106.77 C ANISOU 3696 CG2 ILE B 60 12488 15483 12596 -1727 1768 803 C ATOM 3697 CD1 ILE B 60 -75.596 4.934 41.270 1.00106.54 C ANISOU 3697 CD1 ILE B 60 12837 14617 13025 -1384 1478 609 C ATOM 3698 N LEU B 61 -77.259 1.728 45.644 1.00116.98 N ANISOU 3698 N LEU B 61 14221 16594 13630 -2640 1612 1513 N ATOM 3699 CA LEU B 61 -78.350 1.249 46.487 1.00122.18 C ANISOU 3699 CA LEU B 61 14700 17673 14051 -3036 1711 1723 C ATOM 3700 C LEU B 61 -77.877 0.825 47.881 1.00130.45 C ANISOU 3700 C LEU B 61 15913 18781 14872 -3189 1722 1941 C ATOM 3701 O LEU B 61 -78.539 1.104 48.880 1.00132.63 O ANISOU 3701 O LEU B 61 15955 19565 14872 -3324 1894 2006 O ATOM 3702 CB LEU B 61 -79.091 0.093 45.809 1.00124.74 C ANISOU 3702 CB LEU B 61 15072 17868 14455 -3450 1579 1906 C ATOM 3703 CG LEU B 61 -79.814 0.438 44.494 1.00128.88 C ANISOU 3703 CG LEU B 61 15378 18437 15153 -3371 1577 1718 C ATOM 3704 CD1 LEU B 61 -80.091 -0.841 43.657 1.00130.85 C ANISOU 3704 CD1 LEU B 61 15830 18340 15548 -3725 1359 1873 C ATOM 3705 CD2 LEU B 61 -81.100 1.257 44.702 1.00133.04 C ANISOU 3705 CD2 LEU B 61 15416 19620 15514 -3382 1792 1617 C ATOM 3706 N VAL B 62 -76.738 0.154 47.954 1.00128.05 N ANISOU 3706 N VAL B 62 15999 17991 14664 -3153 1534 2045 N ATOM 3707 CA VAL B 62 -76.260 -0.403 49.226 1.00131.02 C ANISOU 3707 CA VAL B 62 16582 18368 14831 -3322 1494 2288 C ATOM 3708 C VAL B 62 -75.701 0.653 50.168 1.00137.32 C ANISOU 3708 C VAL B 62 17284 19427 15464 -3016 1643 2145 C ATOM 3709 O VAL B 62 -75.856 0.547 51.378 1.00139.64 O ANISOU 3709 O VAL B 62 17553 20024 15478 -3188 1723 2308 O ATOM 3710 CB VAL B 62 -75.191 -1.470 48.974 1.00134.02 C ANISOU 3710 CB VAL B 62 17422 18126 15374 -3328 1208 2424 C ATOM 3711 CG1 VAL B 62 -74.371 -1.756 50.251 1.00134.86 C ANISOU 3711 CG1 VAL B 62 17759 18191 15290 -3337 1151 2605 C ATOM 3712 CG2 VAL B 62 -75.859 -2.722 48.406 1.00136.50 C ANISOU 3712 CG2 VAL B 62 17892 18200 15770 -3742 1030 2640 C ATOM 3713 N MET B 63 -75.030 1.654 49.615 1.00132.83 N ANISOU 3713 N MET B 63 16677 18736 15057 -2586 1665 1849 N ATOM 3714 CA MET B 63 -74.533 2.755 50.412 1.00132.78 C ANISOU 3714 CA MET B 63 16585 18952 14913 -2293 1784 1678 C ATOM 3715 C MET B 63 -75.593 3.806 50.444 1.00138.32 C ANISOU 3715 C MET B 63 16906 20142 15507 -2192 1993 1477 C ATOM 3716 O MET B 63 -76.094 4.176 51.508 1.00139.74 O ANISOU 3716 O MET B 63 16907 20784 15404 -2237 2147 1482 O ATOM 3717 CB MET B 63 -73.284 3.363 49.796 1.00131.96 C ANISOU 3717 CB MET B 63 16631 18484 15024 -1912 1684 1465 C ATOM 3718 CG MET B 63 -72.069 2.505 49.917 1.00136.04 C ANISOU 3718 CG MET B 63 17489 18587 15612 -1905 1482 1604 C ATOM 3719 SD MET B 63 -70.678 3.570 50.261 1.00138.58 S ANISOU 3719 SD MET B 63 17870 18843 15943 -1511 1468 1388 S ATOM 3720 CE MET B 63 -69.783 3.480 48.712 1.00132.30 C ANISOU 3720 CE MET B 63 17188 17606 15475 -1294 1309 1243 C ATOM 3721 N GLY B 64 -75.947 4.276 49.253 1.00134.58 N ANISOU 3721 N GLY B 64 16308 19579 15248 -2039 1988 1290 N ATOM 3722 CA GLY B 64 -76.871 5.383 49.112 1.00135.42 C ANISOU 3722 CA GLY B 64 16074 20084 15296 -1849 2143 1053 C ATOM 3723 C GLY B 64 -77.922 5.333 50.185 1.00144.68 C ANISOU 3723 C GLY B 64 16973 21856 16141 -2051 2320 1134 C ATOM 3724 O GLY B 64 -78.189 6.334 50.844 1.00145.21 O ANISOU 3724 O GLY B 64 16847 22297 16031 -1812 2453 932 O ATOM 3725 N TYR B 65 -78.486 4.164 50.397 1.00144.66 N ANISOU 3725 N TYR B 65 16968 21956 16040 -2496 2310 1427 N ATOM 3726 CA TYR B 65 -79.583 4.070 51.326 1.00148.96 C ANISOU 3726 CA TYR B 65 17202 23149 16249 -2747 2489 1526 C ATOM 3727 C TYR B 65 -79.410 3.395 52.672 1.00156.40 C ANISOU 3727 C TYR B 65 18249 24296 16882 -3055 2525 1806 C ATOM 3728 O TYR B 65 -79.615 4.006 53.721 1.00158.02 O ANISOU 3728 O TYR B 65 18269 24983 16788 -2954 2687 1721 O ATOM 3729 CB TYR B 65 -80.725 3.455 50.580 1.00152.18 C ANISOU 3729 CB TYR B 65 17395 23721 16705 -3069 2493 1634 C ATOM 3730 CG TYR B 65 -81.142 4.358 49.471 1.00152.12 C ANISOU 3730 CG TYR B 65 17179 23713 16905 -2727 2506 1324 C ATOM 3731 CD1 TYR B 65 -80.279 4.698 48.470 1.00149.75 C ANISOU 3731 CD1 TYR B 65 17120 22857 16922 -2430 2361 1173 C ATOM 3732 CD2 TYR B 65 -82.383 4.919 49.459 1.00155.68 C ANISOU 3732 CD2 TYR B 65 17182 24758 17212 -2683 2661 1177 C ATOM 3733 CE1 TYR B 65 -80.664 5.533 47.499 1.00148.79 C ANISOU 3733 CE1 TYR B 65 16828 22742 16962 -2138 2361 919 C ATOM 3734 CE2 TYR B 65 -82.757 5.744 48.494 1.00155.21 C ANISOU 3734 CE2 TYR B 65 16955 24689 17329 -2355 2648 906 C ATOM 3735 CZ TYR B 65 -81.918 6.048 47.524 1.00158.73 C ANISOU 3735 CZ TYR B 65 17670 24556 18083 -2098 2495 791 C ATOM 3736 OH TYR B 65 -82.372 6.888 46.573 1.00159.06 O ANISOU 3736 OH TYR B 65 17541 24620 18275 -1792 2475 542 O ATOM 3737 N GLN B 66 -79.041 2.140 52.671 1.00153.78 N ANISOU 3737 N GLN B 66 18225 23604 16601 -3422 2361 2137 N ATOM 3738 CA GLN B 66 -78.908 1.485 53.927 1.00156.71 C ANISOU 3738 CA GLN B 66 18717 24158 16667 -3735 2371 2433 C ATOM 3739 C GLN B 66 -77.836 1.994 54.829 1.00159.12 C ANISOU 3739 C GLN B 66 19204 24393 16862 -3447 2369 2355 C ATOM 3740 O GLN B 66 -78.064 2.113 56.005 1.00161.62 O ANISOU 3740 O GLN B 66 19408 25172 16827 -3555 2498 2437 O ATOM 3741 CB GLN B 66 -78.628 0.028 53.697 1.00159.28 C ANISOU 3741 CB GLN B 66 19415 24005 17100 -4153 2134 2802 C ATOM 3742 CG GLN B 66 -79.708 -0.672 52.963 1.00176.68 C ANISOU 3742 CG GLN B 66 21483 26281 19367 -4554 2105 2946 C ATOM 3743 CD GLN B 66 -79.372 -2.118 52.686 1.00196.87 C ANISOU 3743 CD GLN B 66 24478 28269 22054 -4946 1817 3289 C ATOM 3744 OE1 GLN B 66 -79.440 -2.981 53.564 1.00198.39 O ANISOU 3744 OE1 GLN B 66 24850 28511 22020 -5370 1745 3650 O ATOM 3745 NE2 GLN B 66 -79.009 -2.386 51.462 1.00183.32 N ANISOU 3745 NE2 GLN B 66 22952 26006 20693 -4799 1636 3174 N ATOM 3746 N LYS B 67 -76.656 2.278 54.292 1.00151.51 N ANISOU 3746 N LYS B 67 18509 22882 16176 -3098 2219 2200 N ATOM 3747 CA LYS B 67 -75.482 2.523 55.128 1.00150.32 C ANISOU 3747 CA LYS B 67 18591 22585 15939 -2890 2159 2185 C ATOM 3748 C LYS B 67 -75.487 3.759 56.067 1.00152.99 C ANISOU 3748 C LYS B 67 18716 23389 16023 -2600 2343 1931 C ATOM 3749 O LYS B 67 -75.637 4.883 55.636 1.00150.54 O ANISOU 3749 O LYS B 67 18218 23174 15807 -2253 2426 1593 O ATOM 3750 CB LYS B 67 -74.212 2.505 54.271 1.00149.68 C ANISOU 3750 CB LYS B 67 18810 21855 16208 -2605 1950 2078 C ATOM 3751 CG LYS B 67 -73.478 1.209 54.219 1.00170.61 C ANISOU 3751 CG LYS B 67 21846 24023 18955 -2802 1705 2366 C ATOM 3752 CD LYS B 67 -72.001 1.423 53.911 1.00181.33 C ANISOU 3752 CD LYS B 67 23448 24932 20518 -2439 1540 2224 C ATOM 3753 CE LYS B 67 -71.382 0.298 52.987 1.00194.91 C ANISOU 3753 CE LYS B 67 25485 26059 22514 -2476 1273 2344 C ATOM 3754 NZ LYS B 67 -69.927 0.377 52.522 1.00201.22 N ANISOU 3754 NZ LYS B 67 26489 26447 23519 -2117 1097 2197 N ATOM 3755 N LYS B 68 -75.254 3.506 57.357 1.00151.10 N ANISOU 3755 N LYS B 68 18553 23398 15460 -2741 2372 2102 N ATOM 3756 CA LYS B 68 -75.237 4.551 58.372 1.00151.23 C ANISOU 3756 CA LYS B 68 18401 23871 15190 -2493 2527 1875 C ATOM 3757 C LYS B 68 -73.850 4.879 58.948 1.00151.79 C ANISOU 3757 C LYS B 68 18753 23659 15260 -2243 2400 1807 C ATOM 3758 O LYS B 68 -73.580 6.007 59.340 1.00150.86 O ANISOU 3758 O LYS B 68 18550 23709 15062 -1906 2467 1500 O ATOM 3759 CB LYS B 68 -76.254 4.269 59.476 1.00158.71 C ANISOU 3759 CB LYS B 68 19102 25519 15681 -2816 2717 2050 C ATOM 3760 CG LYS B 68 -77.175 5.431 59.801 1.00174.69 C ANISOU 3760 CG LYS B 68 20700 28193 17482 -2565 2958 1703 C ATOM 3761 CD LYS B 68 -78.268 5.587 58.787 1.00183.39 C ANISOU 3761 CD LYS B 68 21495 29442 18742 -2575 3042 1585 C ATOM 3762 CE LYS B 68 -79.144 6.765 59.113 1.00194.17 C ANISOU 3762 CE LYS B 68 22444 31444 19888 -2254 3252 1208 C ATOM 3763 NZ LYS B 68 -80.440 6.709 58.376 1.00203.40 N ANISOU 3763 NZ LYS B 68 23237 32954 21094 -2364 3359 1168 N ATOM 3764 N LEU B 69 -72.931 3.944 58.992 1.00146.14 N ANISOU 3764 N LEU B 69 18380 22507 14640 -2378 2195 2068 N ATOM 3765 CA LEU B 69 -71.638 4.421 59.385 1.00143.07 C ANISOU 3765 CA LEU B 69 18192 21886 14280 -2087 2079 1940 C ATOM 3766 C LEU B 69 -70.820 4.380 58.095 1.00139.84 C ANISOU 3766 C LEU B 69 17947 20880 14306 -1888 1904 1838 C ATOM 3767 O LEU B 69 -70.426 3.326 57.613 1.00139.16 O ANISOU 3767 O LEU B 69 18088 20397 14390 -2033 1728 2062 O ATOM 3768 CB LEU B 69 -71.045 3.599 60.517 1.00145.82 C ANISOU 3768 CB LEU B 69 18786 22246 14374 -2290 1969 2251 C ATOM 3769 CG LEU B 69 -70.104 4.386 61.410 1.00150.19 C ANISOU 3769 CG LEU B 69 19405 22893 14767 -2015 1945 2074 C ATOM 3770 CD1 LEU B 69 -70.299 4.069 62.872 1.00154.45 C ANISOU 3770 CD1 LEU B 69 19959 23877 14847 -2232 2006 2286 C ATOM 3771 CD2 LEU B 69 -68.670 4.241 60.976 1.00149.73 C ANISOU 3771 CD2 LEU B 69 19621 22289 14982 -1803 1703 2048 C ATOM 3772 N ARG B 70 -70.573 5.558 57.541 1.00131.19 N ANISOU 3772 N ARG B 70 16739 19734 13373 -1550 1943 1490 N ATOM 3773 CA ARG B 70 -69.858 5.687 56.283 1.00126.12 C ANISOU 3773 CA ARG B 70 16198 18617 13106 -1362 1808 1367 C ATOM 3774 C ARG B 70 -68.599 6.516 56.405 1.00124.04 C ANISOU 3774 C ARG B 70 16039 18184 12906 -1067 1711 1163 C ATOM 3775 O ARG B 70 -68.588 7.556 57.001 1.00123.92 O ANISOU 3775 O ARG B 70 15933 18405 12747 -901 1788 951 O ATOM 3776 CB ARG B 70 -70.785 6.292 55.243 1.00125.67 C ANISOU 3776 CB ARG B 70 15913 18618 13218 -1285 1915 1173 C ATOM 3777 CG ARG B 70 -71.259 5.351 54.150 1.00137.85 C ANISOU 3777 CG ARG B 70 17477 19919 14980 -1481 1857 1328 C ATOM 3778 CD ARG B 70 -71.258 6.094 52.797 1.00150.42 C ANISOU 3778 CD ARG B 70 18982 21303 16866 -1252 1843 1081 C ATOM 3779 NE ARG B 70 -72.038 7.338 52.778 1.00164.17 N ANISOU 3779 NE ARG B 70 20471 23357 18548 -1065 1992 816 N ATOM 3780 CZ ARG B 70 -73.219 7.497 52.188 1.00182.30 C ANISOU 3780 CZ ARG B 70 22538 25848 20880 -1104 2090 753 C ATOM 3781 NH1 ARG B 70 -73.785 6.496 51.574 1.00172.49 N ANISOU 3781 NH1 ARG B 70 21280 24532 19728 -1364 2067 943 N ATOM 3782 NH2 ARG B 70 -73.835 8.652 52.216 1.00169.52 N ANISOU 3782 NH2 ARG B 70 20713 24493 19203 -874 2191 491 N ATOM 3783 N SER B 71 -67.523 6.126 55.721 1.00115.37 N ANISOU 3783 N SER B 71 15119 16674 12043 -984 1532 1193 N ATOM 3784 CA SER B 71 -66.283 6.937 55.722 1.00111.73 C ANISOU 3784 CA SER B 71 14722 16078 11652 -734 1433 1000 C ATOM 3785 C SER B 71 -66.300 8.166 54.777 1.00109.42 C ANISOU 3785 C SER B 71 14306 15716 11553 -535 1471 707 C ATOM 3786 O SER B 71 -67.231 8.322 53.987 1.00108.15 O ANISOU 3786 O SER B 71 14016 15570 11505 -556 1559 650 O ATOM 3787 CB SER B 71 -65.071 6.055 55.408 1.00114.24 C ANISOU 3787 CB SER B 71 15241 16056 12109 -705 1223 1135 C ATOM 3788 OG SER B 71 -63.879 6.821 55.374 1.00121.43 O ANISOU 3788 OG SER B 71 16170 16893 13075 -498 1132 957 O ATOM 3789 N MET B 72 -65.275 9.028 54.857 1.00102.21 N ANISOU 3789 N MET B 72 13440 14727 10669 -362 1386 535 N ATOM 3790 CA MET B 72 -65.187 10.202 53.986 1.00 98.84 C ANISOU 3790 CA MET B 72 12945 14195 10414 -210 1382 291 C ATOM 3791 C MET B 72 -64.865 9.752 52.565 1.00 97.89 C ANISOU 3791 C MET B 72 12833 13787 10572 -218 1309 336 C ATOM 3792 O MET B 72 -65.368 10.340 51.608 1.00 96.38 O ANISOU 3792 O MET B 72 12559 13530 10530 -170 1346 217 O ATOM 3793 CB MET B 72 -64.135 11.187 54.503 1.00101.03 C ANISOU 3793 CB MET B 72 13292 14467 10628 -87 1285 127 C ATOM 3794 CG MET B 72 -64.601 11.999 55.693 1.00106.79 C ANISOU 3794 CG MET B 72 13999 15474 11101 -21 1357 -20 C ATOM 3795 SD MET B 72 -65.554 13.463 55.223 1.00110.92 S ANISOU 3795 SD MET B 72 14430 16034 11680 151 1420 -326 S ATOM 3796 CE MET B 72 -67.191 12.963 55.712 1.00109.73 C ANISOU 3796 CE MET B 72 14097 16255 11340 103 1632 -273 C ATOM 3797 N THR B 73 -64.081 8.658 52.447 1.00 92.29 N ANISOU 3797 N THR B 73 12229 12920 9915 -266 1197 505 N ATOM 3798 CA THR B 73 -63.704 8.000 51.195 1.00 89.60 C ANISOU 3798 CA THR B 73 11910 12331 9802 -255 1112 548 C ATOM 3799 C THR B 73 -64.945 7.335 50.591 1.00 91.97 C ANISOU 3799 C THR B 73 12166 12599 10179 -381 1192 639 C ATOM 3800 O THR B 73 -65.222 7.534 49.411 1.00 90.29 O ANISOU 3800 O THR B 73 11884 12278 10143 -353 1203 558 O ATOM 3801 CB THR B 73 -62.554 7.010 51.455 1.00 95.76 C ANISOU 3801 CB THR B 73 12825 12986 10574 -220 950 675 C ATOM 3802 OG1 THR B 73 -61.434 7.731 51.967 1.00 96.04 O ANISOU 3802 OG1 THR B 73 12858 13099 10534 -115 879 573 O ATOM 3803 CG2 THR B 73 -62.139 6.236 50.211 1.00 91.89 C ANISOU 3803 CG2 THR B 73 12361 12263 10291 -166 849 690 C ATOM 3804 N ASP B 74 -65.709 6.592 51.419 1.00 89.26 N ANISOU 3804 N ASP B 74 11855 12379 9682 -545 1244 814 N ATOM 3805 CA ASP B 74 -66.936 5.897 51.027 1.00 89.33 C ANISOU 3805 CA ASP B 74 11812 12406 9721 -730 1312 933 C ATOM 3806 C ASP B 74 -68.031 6.853 50.545 1.00 91.45 C ANISOU 3806 C ASP B 74 11867 12860 10020 -701 1465 767 C ATOM 3807 O ASP B 74 -68.901 6.430 49.785 1.00 91.17 O ANISOU 3807 O ASP B 74 11757 12798 10083 -811 1497 810 O ATOM 3808 CB ASP B 74 -67.441 4.995 52.158 1.00 94.04 C ANISOU 3808 CB ASP B 74 12485 13149 10098 -957 1329 1179 C ATOM 3809 CG ASP B 74 -66.493 3.878 52.543 1.00105.12 C ANISOU 3809 CG ASP B 74 14140 14315 11487 -990 1137 1376 C ATOM 3810 OD1 ASP B 74 -65.745 3.333 51.719 1.00104.86 O ANISOU 3810 OD1 ASP B 74 14225 13969 11647 -888 980 1367 O ATOM 3811 OD2 ASP B 74 -66.534 3.582 53.752 1.00112.31 O ANISOU 3811 OD2 ASP B 74 15123 15390 12161 -1108 1141 1535 O ATOM 3812 N LYS B 75 -67.970 8.141 50.953 1.00 86.67 N ANISOU 3812 N LYS B 75 11176 12421 9333 -539 1531 566 N ATOM 3813 CA LYS B 75 -68.913 9.173 50.514 1.00 85.61 C ANISOU 3813 CA LYS B 75 10866 12433 9229 -440 1634 374 C ATOM 3814 C LYS B 75 -68.549 9.631 49.092 1.00 84.84 C ANISOU 3814 C LYS B 75 10776 12072 9387 -330 1555 260 C ATOM 3815 O LYS B 75 -69.442 9.809 48.261 1.00 83.70 O ANISOU 3815 O LYS B 75 10513 11946 9342 -327 1600 207 O ATOM 3816 CB LYS B 75 -68.952 10.358 51.503 1.00 89.52 C ANISOU 3816 CB LYS B 75 11316 13161 9536 -283 1692 185 C ATOM 3817 CG LYS B 75 -70.042 11.402 51.214 1.00110.77 C ANISOU 3817 CG LYS B 75 13834 16030 12225 -134 1780 -32 C ATOM 3818 CD LYS B 75 -71.473 10.903 51.482 1.00126.09 C ANISOU 3818 CD LYS B 75 15560 18320 14028 -256 1934 36 C ATOM 3819 CE LYS B 75 -72.508 11.927 51.082 1.00138.06 C ANISOU 3819 CE LYS B 75 16886 20013 15557 -54 1996 -202 C ATOM 3820 NZ LYS B 75 -73.893 11.408 51.232 1.00150.09 N ANISOU 3820 NZ LYS B 75 18149 21928 16950 -186 2145 -137 N ATOM 3821 N TYR B 76 -67.238 9.801 48.811 1.00 78.66 N ANISOU 3821 N TYR B 76 10117 11079 8690 -252 1434 232 N ATOM 3822 CA TYR B 76 -66.761 10.184 47.479 1.00 75.68 C ANISOU 3822 CA TYR B 76 9744 10494 8517 -182 1357 150 C ATOM 3823 C TYR B 76 -66.888 9.009 46.528 1.00 77.20 C ANISOU 3823 C TYR B 76 9948 10537 8847 -275 1321 271 C ATOM 3824 O TYR B 76 -67.131 9.223 45.348 1.00 76.31 O ANISOU 3824 O TYR B 76 9783 10333 8878 -251 1307 210 O ATOM 3825 CB TYR B 76 -65.294 10.642 47.495 1.00 75.95 C ANISOU 3825 CB TYR B 76 9869 10422 8568 -109 1243 97 C ATOM 3826 CG TYR B 76 -65.006 11.940 48.218 1.00 78.45 C ANISOU 3826 CG TYR B 76 10210 10817 8780 -24 1229 -51 C ATOM 3827 CD1 TYR B 76 -65.636 13.126 47.844 1.00 80.41 C ANISOU 3827 CD1 TYR B 76 10426 11061 9067 59 1242 -208 C ATOM 3828 CD2 TYR B 76 -64.023 12.009 49.200 1.00 79.85 C ANISOU 3828 CD2 TYR B 76 10465 11042 8831 -15 1168 -45 C ATOM 3829 CE1 TYR B 76 -65.352 14.329 48.487 1.00 81.99 C ANISOU 3829 CE1 TYR B 76 10695 11279 9179 146 1188 -362 C ATOM 3830 CE2 TYR B 76 -63.727 13.206 49.846 1.00 81.46 C ANISOU 3830 CE2 TYR B 76 10714 11295 8940 50 1128 -196 C ATOM 3831 CZ TYR B 76 -64.391 14.365 49.483 1.00 90.01 C ANISOU 3831 CZ TYR B 76 11791 12345 10066 130 1133 -359 C ATOM 3832 OH TYR B 76 -64.101 15.541 50.125 1.00 94.53 O ANISOU 3832 OH TYR B 76 12451 12918 10547 202 1058 -524 O ATOM 3833 N ARG B 77 -66.709 7.772 47.030 1.00 72.76 N ANISOU 3833 N ARG B 77 9479 9932 8235 -380 1282 440 N ATOM 3834 CA ARG B 77 -66.808 6.559 46.215 1.00 71.57 C ANISOU 3834 CA ARG B 77 9391 9595 8207 -463 1208 547 C ATOM 3835 C ARG B 77 -68.216 6.308 45.665 1.00 76.66 C ANISOU 3835 C ARG B 77 9930 10297 8901 -598 1285 577 C ATOM 3836 O ARG B 77 -68.343 5.652 44.629 1.00 76.19 O ANISOU 3836 O ARG B 77 9897 10070 8981 -636 1218 593 O ATOM 3837 CB ARG B 77 -66.208 5.336 46.921 1.00 70.03 C ANISOU 3837 CB ARG B 77 9374 9287 7948 -524 1097 720 C ATOM 3838 CG ARG B 77 -64.682 5.380 46.951 1.00 70.97 C ANISOU 3838 CG ARG B 77 9574 9310 8082 -349 974 664 C ATOM 3839 CD ARG B 77 -64.061 4.181 47.632 1.00 77.51 C ANISOU 3839 CD ARG B 77 10592 10008 8849 -357 829 823 C ATOM 3840 NE ARG B 77 -64.182 2.967 46.826 1.00 84.12 N ANISOU 3840 NE ARG B 77 11553 10593 9815 -382 703 889 N ATOM 3841 CZ ARG B 77 -63.656 1.791 47.150 1.00 99.51 C ANISOU 3841 CZ ARG B 77 13715 12340 11754 -357 521 1014 C ATOM 3842 NH1 ARG B 77 -62.961 1.654 48.272 1.00 90.34 N ANISOU 3842 NH1 ARG B 77 12651 11222 10453 -311 451 1103 N ATOM 3843 NH2 ARG B 77 -63.825 0.742 46.359 1.00 85.95 N ANISOU 3843 NH2 ARG B 77 12133 10361 10161 -367 385 1043 N ATOM 3844 N LEU B 78 -69.264 6.867 46.322 1.00 74.46 N ANISOU 3844 N LEU B 78 9512 10283 8498 -654 1420 561 N ATOM 3845 CA LEU B 78 -70.637 6.775 45.814 1.00 74.97 C ANISOU 3845 CA LEU B 78 9416 10478 8589 -768 1501 565 C ATOM 3846 C LEU B 78 -70.932 7.948 44.868 1.00 77.64 C ANISOU 3846 C LEU B 78 9627 10835 9038 -592 1526 364 C ATOM 3847 O LEU B 78 -71.720 7.791 43.938 1.00 77.32 O ANISOU 3847 O LEU B 78 9490 10791 9097 -641 1530 349 O ATOM 3848 CB LEU B 78 -71.711 6.580 46.905 1.00 77.45 C ANISOU 3848 CB LEU B 78 9608 11125 8696 -937 1628 664 C ATOM 3849 CG LEU B 78 -71.967 7.714 47.876 1.00 82.74 C ANISOU 3849 CG LEU B 78 10150 12103 9183 -795 1747 526 C ATOM 3850 CD1 LEU B 78 -73.171 8.537 47.444 1.00 83.31 C ANISOU 3850 CD1 LEU B 78 9976 12420 9258 -704 1847 365 C ATOM 3851 CD2 LEU B 78 -72.199 7.174 49.268 1.00 87.64 C ANISOU 3851 CD2 LEU B 78 10774 12977 9549 -967 1818 685 C ATOM 3852 N HIS B 79 -70.254 9.101 45.087 1.00 72.86 N ANISOU 3852 N HIS B 79 9047 10224 8412 -400 1516 220 N ATOM 3853 CA HIS B 79 -70.312 10.292 44.239 1.00 71.38 C ANISOU 3853 CA HIS B 79 8811 9988 8323 -235 1491 49 C ATOM 3854 C HIS B 79 -69.708 9.876 42.889 1.00 74.24 C ANISOU 3854 C HIS B 79 9237 10111 8858 -254 1392 74 C ATOM 3855 O HIS B 79 -70.259 10.195 41.836 1.00 73.93 O ANISOU 3855 O HIS B 79 9127 10044 8920 -225 1378 16 O ATOM 3856 CB HIS B 79 -69.446 11.401 44.846 1.00 71.87 C ANISOU 3856 CB HIS B 79 8960 10027 8321 -90 1452 -67 C ATOM 3857 CG HIS B 79 -70.202 12.556 45.412 1.00 76.66 C ANISOU 3857 CG HIS B 79 9490 10806 8831 58 1501 -229 C ATOM 3858 ND1 HIS B 79 -70.538 12.608 46.753 1.00 80.46 N ANISOU 3858 ND1 HIS B 79 9930 11529 9114 75 1586 -253 N ATOM 3859 CD2 HIS B 79 -70.591 13.708 44.820 1.00 78.37 C ANISOU 3859 CD2 HIS B 79 9689 10977 9113 218 1452 -387 C ATOM 3860 CE1 HIS B 79 -71.147 13.770 46.923 1.00 80.87 C ANISOU 3860 CE1 HIS B 79 9925 11686 9117 270 1592 -451 C ATOM 3861 NE2 HIS B 79 -71.202 14.465 45.788 1.00 80.15 N ANISOU 3861 NE2 HIS B 79 9860 11404 9190 366 1500 -533 N ATOM 3862 N LEU B 80 -68.589 9.123 42.950 1.00 70.21 N ANISOU 3862 N LEU B 80 8854 9459 8362 -288 1319 153 N ATOM 3863 CA LEU B 80 -67.850 8.552 41.826 1.00 69.14 C ANISOU 3863 CA LEU B 80 8777 9144 8349 -281 1224 162 C ATOM 3864 C LEU B 80 -68.707 7.488 41.128 1.00 74.48 C ANISOU 3864 C LEU B 80 9433 9762 9103 -396 1213 229 C ATOM 3865 O LEU B 80 -68.710 7.412 39.896 1.00 73.21 O ANISOU 3865 O LEU B 80 9252 9517 9047 -374 1165 177 O ATOM 3866 CB LEU B 80 -66.530 7.937 42.355 1.00 69.09 C ANISOU 3866 CB LEU B 80 8892 9057 8301 -251 1145 214 C ATOM 3867 CG LEU B 80 -65.626 7.198 41.373 1.00 72.76 C ANISOU 3867 CG LEU B 80 9409 9383 8853 -196 1038 200 C ATOM 3868 CD1 LEU B 80 -64.758 8.162 40.606 1.00 71.70 C ANISOU 3868 CD1 LEU B 80 9214 9287 8740 -110 1013 93 C ATOM 3869 CD2 LEU B 80 -64.753 6.207 42.104 1.00 75.90 C ANISOU 3869 CD2 LEU B 80 9931 9708 9201 -163 948 277 C ATOM 3870 N SER B 81 -69.434 6.674 41.925 1.00 73.01 N ANISOU 3870 N SER B 81 9257 9634 8849 -545 1249 351 N ATOM 3871 CA SER B 81 -70.314 5.619 41.423 1.00 73.84 C ANISOU 3871 CA SER B 81 9359 9685 9011 -716 1221 439 C ATOM 3872 C SER B 81 -71.504 6.193 40.646 1.00 77.92 C ANISOU 3872 C SER B 81 9688 10340 9577 -736 1286 362 C ATOM 3873 O SER B 81 -71.937 5.573 39.676 1.00 77.67 O ANISOU 3873 O SER B 81 9652 10216 9642 -818 1226 368 O ATOM 3874 CB SER B 81 -70.806 4.741 42.567 1.00 78.97 C ANISOU 3874 CB SER B 81 10061 10400 9542 -922 1241 619 C ATOM 3875 OG SER B 81 -71.006 3.415 42.109 1.00 88.37 O ANISOU 3875 OG SER B 81 11383 11387 10806 -1089 1122 732 O ATOM 3876 N VAL B 82 -72.023 7.373 41.066 1.00 74.50 N ANISOU 3876 N VAL B 82 9109 10123 9074 -639 1387 273 N ATOM 3877 CA VAL B 82 -73.129 8.076 40.404 1.00 74.54 C ANISOU 3877 CA VAL B 82 8927 10280 9114 -593 1431 177 C ATOM 3878 C VAL B 82 -72.651 8.563 39.031 1.00 76.99 C ANISOU 3878 C VAL B 82 9278 10416 9558 -470 1341 82 C ATOM 3879 O VAL B 82 -73.378 8.432 38.043 1.00 76.39 O ANISOU 3879 O VAL B 82 9115 10352 9557 -504 1313 59 O ATOM 3880 CB VAL B 82 -73.696 9.219 41.295 1.00 79.33 C ANISOU 3880 CB VAL B 82 9400 11146 9597 -459 1531 77 C ATOM 3881 CG1 VAL B 82 -74.514 10.223 40.491 1.00 79.22 C ANISOU 3881 CG1 VAL B 82 9240 11220 9639 -301 1523 -67 C ATOM 3882 CG2 VAL B 82 -74.536 8.655 42.436 1.00 81.51 C ANISOU 3882 CG2 VAL B 82 9554 11704 9710 -621 1642 173 C ATOM 3883 N ALA B 83 -71.404 9.079 38.977 1.00 72.86 N ANISOU 3883 N ALA B 83 8880 9757 9046 -353 1291 40 N ATOM 3884 CA ALA B 83 -70.752 9.574 37.761 1.00 71.24 C ANISOU 3884 CA ALA B 83 8718 9427 8924 -269 1210 -26 C ATOM 3885 C ALA B 83 -70.543 8.446 36.751 1.00 74.35 C ANISOU 3885 C ALA B 83 9153 9702 9396 -346 1142 5 C ATOM 3886 O ALA B 83 -70.900 8.616 35.590 1.00 73.57 O ANISOU 3886 O ALA B 83 9005 9593 9356 -334 1102 -41 O ATOM 3887 CB ALA B 83 -69.420 10.231 38.104 1.00 71.09 C ANISOU 3887 CB ALA B 83 8801 9343 8865 -188 1176 -52 C ATOM 3888 N ASP B 84 -69.997 7.294 37.193 1.00 71.29 N ANISOU 3888 N ASP B 84 8871 9218 8998 -410 1109 76 N ATOM 3889 CA ASP B 84 -69.754 6.134 36.331 1.00 71.53 C ANISOU 3889 CA ASP B 84 8980 9101 9095 -448 1012 77 C ATOM 3890 C ASP B 84 -71.046 5.468 35.851 1.00 75.88 C ANISOU 3890 C ASP B 84 9478 9655 9699 -600 998 108 C ATOM 3891 O ASP B 84 -71.069 4.921 34.749 1.00 75.43 O ANISOU 3891 O ASP B 84 9451 9504 9706 -606 913 55 O ATOM 3892 CB ASP B 84 -68.794 5.122 36.992 1.00 74.51 C ANISOU 3892 CB ASP B 84 9519 9341 9448 -434 940 132 C ATOM 3893 CG ASP B 84 -67.333 5.565 37.046 1.00 89.27 C ANISOU 3893 CG ASP B 84 11420 11220 11279 -272 914 70 C ATOM 3894 OD1 ASP B 84 -66.832 6.100 36.029 1.00 90.16 O ANISOU 3894 OD1 ASP B 84 11472 11380 11406 -188 899 -24 O ATOM 3895 OD2 ASP B 84 -66.667 5.298 38.074 1.00 96.81 O ANISOU 3895 OD2 ASP B 84 12455 12153 12174 -243 897 125 O ATOM 3896 N LEU B 85 -72.124 5.543 36.658 1.00 73.52 N ANISOU 3896 N LEU B 85 9080 9500 9353 -726 1080 182 N ATOM 3897 CA LEU B 85 -73.429 4.987 36.298 1.00 74.71 C ANISOU 3897 CA LEU B 85 9131 9722 9531 -910 1074 224 C ATOM 3898 C LEU B 85 -74.055 5.835 35.189 1.00 77.90 C ANISOU 3898 C LEU B 85 9380 10234 9985 -821 1080 113 C ATOM 3899 O LEU B 85 -74.531 5.284 34.197 1.00 78.27 O ANISOU 3899 O LEU B 85 9411 10232 10095 -902 1003 90 O ATOM 3900 CB LEU B 85 -74.355 4.897 37.527 1.00 76.51 C ANISOU 3900 CB LEU B 85 9250 10165 9654 -1075 1176 335 C ATOM 3901 CG LEU B 85 -75.737 4.264 37.331 1.00 83.57 C ANISOU 3901 CG LEU B 85 10004 11203 10544 -1327 1178 406 C ATOM 3902 CD1 LEU B 85 -75.655 2.740 37.219 1.00 85.24 C ANISOU 3902 CD1 LEU B 85 10417 11171 10799 -1572 1041 533 C ATOM 3903 CD2 LEU B 85 -76.650 4.630 38.474 1.00 88.89 C ANISOU 3903 CD2 LEU B 85 10475 12228 11073 -1424 1322 469 C ATOM 3904 N LEU B 86 -73.989 7.175 35.339 1.00 73.01 N ANISOU 3904 N LEU B 86 8676 9733 9332 -647 1143 40 N ATOM 3905 CA LEU B 86 -74.496 8.174 34.395 1.00 72.01 C ANISOU 3905 CA LEU B 86 8437 9684 9239 -526 1123 -54 C ATOM 3906 C LEU B 86 -73.967 7.931 32.966 1.00 74.07 C ANISOU 3906 C LEU B 86 8776 9801 9567 -504 1019 -97 C ATOM 3907 O LEU B 86 -74.736 8.034 32.006 1.00 74.46 O ANISOU 3907 O LEU B 86 8732 9910 9651 -515 973 -136 O ATOM 3908 CB LEU B 86 -74.095 9.577 34.884 1.00 71.32 C ANISOU 3908 CB LEU B 86 8357 9634 9106 -336 1155 -115 C ATOM 3909 CG LEU B 86 -75.105 10.695 34.656 1.00 76.78 C ANISOU 3909 CG LEU B 86 8906 10475 9793 -198 1153 -198 C ATOM 3910 CD1 LEU B 86 -76.134 10.743 35.778 1.00 78.67 C ANISOU 3910 CD1 LEU B 86 8974 10967 9948 -199 1255 -212 C ATOM 3911 CD2 LEU B 86 -74.404 12.032 34.569 1.00 78.24 C ANISOU 3911 CD2 LEU B 86 9202 10555 9970 -20 1096 -260 C ATOM 3912 N PHE B 87 -72.675 7.555 32.841 1.00 68.19 N ANISOU 3912 N PHE B 87 8183 8905 8820 -470 980 -99 N ATOM 3913 CA PHE B 87 -72.028 7.255 31.565 1.00 66.70 C ANISOU 3913 CA PHE B 87 8055 8634 8653 -433 893 -159 C ATOM 3914 C PHE B 87 -72.390 5.868 31.017 1.00 71.73 C ANISOU 3914 C PHE B 87 8741 9175 9338 -544 813 -172 C ATOM 3915 O PHE B 87 -72.691 5.766 29.827 1.00 71.16 O ANISOU 3915 O PHE B 87 8638 9116 9284 -544 747 -237 O ATOM 3916 CB PHE B 87 -70.501 7.446 31.652 1.00 67.09 C ANISOU 3916 CB PHE B 87 8202 8632 8656 -333 884 -179 C ATOM 3917 CG PHE B 87 -69.730 6.925 30.461 1.00 68.09 C ANISOU 3917 CG PHE B 87 8370 8734 8769 -284 807 -257 C ATOM 3918 CD1 PHE B 87 -68.906 5.813 30.579 1.00 71.23 C ANISOU 3918 CD1 PHE B 87 8868 9035 9161 -240 752 -296 C ATOM 3919 CD2 PHE B 87 -69.852 7.528 29.211 1.00 69.64 C ANISOU 3919 CD2 PHE B 87 8504 9016 8939 -264 776 -301 C ATOM 3920 CE1 PHE B 87 -68.207 5.319 29.469 1.00 72.26 C ANISOU 3920 CE1 PHE B 87 9016 9185 9255 -151 679 -409 C ATOM 3921 CE2 PHE B 87 -69.161 7.026 28.101 1.00 72.37 C ANISOU 3921 CE2 PHE B 87 8866 9398 9235 -215 715 -389 C ATOM 3922 CZ PHE B 87 -68.341 5.929 28.239 1.00 70.85 C ANISOU 3922 CZ PHE B 87 8752 9136 9032 -147 672 -458 C ATOM 3923 N VAL B 88 -72.349 4.805 31.864 1.00 69.49 N ANISOU 3923 N VAL B 88 8559 8778 9066 -645 794 -107 N ATOM 3924 CA VAL B 88 -72.657 3.425 31.435 1.00 70.74 C ANISOU 3924 CA VAL B 88 8826 8777 9274 -770 674 -111 C ATOM 3925 C VAL B 88 -74.025 3.259 30.781 1.00 74.94 C ANISOU 3925 C VAL B 88 9239 9392 9843 -930 645 -112 C ATOM 3926 O VAL B 88 -74.183 2.407 29.909 1.00 75.89 O ANISOU 3926 O VAL B 88 9438 9392 10003 -990 520 -174 O ATOM 3927 CB VAL B 88 -72.307 2.287 32.435 1.00 76.17 C ANISOU 3927 CB VAL B 88 9701 9275 9966 -861 612 -19 C ATOM 3928 CG1 VAL B 88 -70.817 2.264 32.764 1.00 75.36 C ANISOU 3928 CG1 VAL B 88 9722 9082 9830 -659 590 -60 C ATOM 3929 CG2 VAL B 88 -73.149 2.355 33.701 1.00 76.86 C ANISOU 3929 CG2 VAL B 88 9717 9473 10011 -1049 706 138 C ATOM 3930 N ILE B 89 -74.993 4.111 31.187 1.00 70.54 N ANISOU 3930 N ILE B 89 8483 9057 9263 -975 750 -65 N ATOM 3931 CA ILE B 89 -76.368 4.195 30.675 1.00 70.90 C ANISOU 3931 CA ILE B 89 8343 9273 9325 -1099 741 -69 C ATOM 3932 C ILE B 89 -76.372 4.646 29.180 1.00 73.04 C ANISOU 3932 C ILE B 89 8575 9562 9617 -978 667 -187 C ATOM 3933 O ILE B 89 -77.244 4.219 28.422 1.00 73.83 O ANISOU 3933 O ILE B 89 8600 9709 9741 -1097 589 -215 O ATOM 3934 CB ILE B 89 -77.211 5.112 31.624 1.00 74.01 C ANISOU 3934 CB ILE B 89 8519 9939 9661 -1091 877 -20 C ATOM 3935 CG1 ILE B 89 -77.522 4.392 32.955 1.00 75.57 C ANISOU 3935 CG1 ILE B 89 8723 10185 9806 -1301 937 114 C ATOM 3936 CG2 ILE B 89 -78.493 5.650 30.969 1.00 75.56 C ANISOU 3936 CG2 ILE B 89 8471 10378 9860 -1095 872 -70 C ATOM 3937 CD1 ILE B 89 -77.838 5.317 34.148 1.00 82.18 C ANISOU 3937 CD1 ILE B 89 9402 11277 10545 -1219 1090 136 C ATOM 3938 N THR B 90 -75.391 5.482 28.767 1.00 66.91 N ANISOU 3938 N THR B 90 7850 8761 8813 -772 682 -243 N ATOM 3939 CA THR B 90 -75.273 5.969 27.384 1.00 65.94 C ANISOU 3939 CA THR B 90 7705 8678 8672 -674 615 -327 C ATOM 3940 C THR B 90 -74.573 4.959 26.470 1.00 68.60 C ANISOU 3940 C THR B 90 8183 8880 9003 -675 510 -417 C ATOM 3941 O THR B 90 -74.640 5.102 25.248 1.00 68.60 O ANISOU 3941 O THR B 90 8157 8939 8968 -634 442 -493 O ATOM 3942 CB THR B 90 -74.569 7.346 27.304 1.00 75.01 C ANISOU 3942 CB THR B 90 8851 9881 9769 -502 660 -323 C ATOM 3943 OG1 THR B 90 -73.173 7.211 27.586 1.00 75.88 O ANISOU 3943 OG1 THR B 90 9091 9898 9842 -439 681 -329 O ATOM 3944 CG2 THR B 90 -75.220 8.406 28.184 1.00 72.56 C ANISOU 3944 CG2 THR B 90 8435 9674 9460 -445 732 -276 C ATOM 3945 N LEU B 91 -73.883 3.957 27.053 1.00 63.92 N ANISOU 3945 N LEU B 91 7746 8113 8429 -697 483 -419 N ATOM 3946 CA LEU B 91 -73.165 2.941 26.278 1.00 63.53 C ANISOU 3946 CA LEU B 91 7849 7922 8369 -640 362 -542 C ATOM 3947 C LEU B 91 -73.977 2.193 25.194 1.00 67.52 C ANISOU 3947 C LEU B 91 8365 8392 8895 -742 227 -633 C ATOM 3948 O LEU B 91 -73.448 2.081 24.091 1.00 67.19 O ANISOU 3948 O LEU B 91 8357 8380 8793 -621 161 -771 O ATOM 3949 CB LEU B 91 -72.280 2.024 27.136 1.00 63.76 C ANISOU 3949 CB LEU B 91 8063 7747 8415 -601 322 -536 C ATOM 3950 CG LEU B 91 -70.964 2.640 27.636 1.00 66.14 C ANISOU 3950 CG LEU B 91 8369 8107 8655 -418 406 -535 C ATOM 3951 CD1 LEU B 91 -70.468 1.929 28.850 1.00 66.73 C ANISOU 3951 CD1 LEU B 91 8588 8009 8756 -420 384 -468 C ATOM 3952 CD2 LEU B 91 -69.890 2.604 26.569 1.00 67.87 C ANISOU 3952 CD2 LEU B 91 8598 8401 8788 -227 360 -694 C ATOM 3953 N PRO B 92 -75.267 1.788 25.390 1.00 64.24 N ANISOU 3953 N PRO B 92 7893 7973 8543 -966 188 -566 N ATOM 3954 CA PRO B 92 -76.019 1.159 24.277 1.00 65.36 C ANISOU 3954 CA PRO B 92 8036 8101 8695 -1074 44 -662 C ATOM 3955 C PRO B 92 -75.976 1.948 22.958 1.00 68.80 C ANISOU 3955 C PRO B 92 8362 8726 9053 -933 38 -764 C ATOM 3956 O PRO B 92 -75.947 1.334 21.895 1.00 69.30 O ANISOU 3956 O PRO B 92 8498 8748 9083 -920 -92 -905 O ATOM 3957 CB PRO B 92 -77.451 1.077 24.813 1.00 68.13 C ANISOU 3957 CB PRO B 92 8239 8549 9098 -1340 56 -538 C ATOM 3958 CG PRO B 92 -77.309 1.030 26.266 1.00 72.30 C ANISOU 3958 CG PRO B 92 8792 9033 9644 -1411 156 -393 C ATOM 3959 CD PRO B 92 -76.081 1.821 26.623 1.00 65.79 C ANISOU 3959 CD PRO B 92 8008 8211 8779 -1150 266 -406 C ATOM 3960 N PHE B 93 -75.934 3.301 23.032 1.00 64.66 N ANISOU 3960 N PHE B 93 7688 8394 8485 -827 160 -694 N ATOM 3961 CA PHE B 93 -75.854 4.198 21.869 1.00 64.66 C ANISOU 3961 CA PHE B 93 7605 8569 8393 -711 148 -740 C ATOM 3962 C PHE B 93 -74.510 4.067 21.156 1.00 68.24 C ANISOU 3962 C PHE B 93 8169 9022 8739 -558 132 -848 C ATOM 3963 O PHE B 93 -74.467 4.141 19.927 1.00 68.41 O ANISOU 3963 O PHE B 93 8171 9160 8660 -516 64 -938 O ATOM 3964 CB PHE B 93 -76.090 5.668 22.277 1.00 65.58 C ANISOU 3964 CB PHE B 93 7592 8828 8499 -640 248 -621 C ATOM 3965 CG PHE B 93 -77.383 5.924 23.020 1.00 68.26 C ANISOU 3965 CG PHE B 93 7777 9247 8914 -731 279 -543 C ATOM 3966 CD1 PHE B 93 -78.610 5.805 22.377 1.00 72.97 C ANISOU 3966 CD1 PHE B 93 8232 9970 9522 -819 194 -567 C ATOM 3967 CD2 PHE B 93 -77.372 6.304 24.355 1.00 69.99 C ANISOU 3967 CD2 PHE B 93 7965 9458 9169 -720 392 -458 C ATOM 3968 CE1 PHE B 93 -79.801 6.032 23.065 1.00 74.75 C ANISOU 3968 CE1 PHE B 93 8264 10345 9794 -894 229 -510 C ATOM 3969 CE2 PHE B 93 -78.565 6.547 25.039 1.00 73.75 C ANISOU 3969 CE2 PHE B 93 8260 10080 9679 -785 433 -408 C ATOM 3970 CZ PHE B 93 -79.771 6.410 24.389 1.00 73.45 C ANISOU 3970 CZ PHE B 93 8058 10199 9651 -869 354 -435 C ATOM 3971 N TRP B 94 -73.417 3.873 21.932 1.00 63.78 N ANISOU 3971 N TRP B 94 7698 8363 8173 -473 194 -844 N ATOM 3972 CA TRP B 94 -72.052 3.712 21.423 1.00 63.53 C ANISOU 3972 CA TRP B 94 7730 8386 8025 -311 192 -957 C ATOM 3973 C TRP B 94 -71.939 2.435 20.601 1.00 69.16 C ANISOU 3973 C TRP B 94 8555 9014 8709 -263 48 -1157 C ATOM 3974 O TRP B 94 -71.291 2.444 19.552 1.00 69.40 O ANISOU 3974 O TRP B 94 8566 9211 8593 -140 21 -1292 O ATOM 3975 CB TRP B 94 -71.035 3.678 22.580 1.00 61.45 C ANISOU 3975 CB TRP B 94 7526 8041 7783 -234 270 -912 C ATOM 3976 CG TRP B 94 -70.755 5.001 23.234 1.00 60.58 C ANISOU 3976 CG TRP B 94 7330 8035 7654 -238 396 -762 C ATOM 3977 CD1 TRP B 94 -71.636 5.781 23.927 1.00 62.93 C ANISOU 3977 CD1 TRP B 94 7564 8320 8027 -326 452 -627 C ATOM 3978 CD2 TRP B 94 -69.474 5.639 23.352 1.00 59.68 C ANISOU 3978 CD2 TRP B 94 7192 8047 7437 -146 465 -747 C ATOM 3979 NE1 TRP B 94 -70.995 6.895 24.422 1.00 61.37 N ANISOU 3979 NE1 TRP B 94 7340 8191 7786 -284 534 -539 N ATOM 3980 CE2 TRP B 94 -69.663 6.827 24.093 1.00 62.59 C ANISOU 3980 CE2 TRP B 94 7518 8429 7833 -202 543 -595 C ATOM 3981 CE3 TRP B 94 -68.183 5.329 22.892 1.00 61.20 C ANISOU 3981 CE3 TRP B 94 7381 8372 7501 -20 460 -858 C ATOM 3982 CZ2 TRP B 94 -68.609 7.703 24.383 1.00 61.09 C ANISOU 3982 CZ2 TRP B 94 7309 8343 7559 -178 602 -535 C ATOM 3983 CZ3 TRP B 94 -67.142 6.201 23.175 1.00 61.97 C ANISOU 3983 CZ3 TRP B 94 7413 8630 7502 -3 539 -790 C ATOM 3984 CH2 TRP B 94 -67.359 7.371 23.911 1.00 61.37 C ANISOU 3984 CH2 TRP B 94 7322 8527 7469 -101 603 -621 C ATOM 3985 N ALA B 95 -72.585 1.345 21.076 1.00 67.32 N ANISOU 3985 N ALA B 95 8445 8532 8601 -371 -55 -1177 N ATOM 3986 CA ALA B 95 -72.593 0.034 20.421 1.00 69.75 C ANISOU 3986 CA ALA B 95 8921 8672 8911 -343 -241 -1373 C ATOM 3987 C ALA B 95 -73.371 0.055 19.095 1.00 75.30 C ANISOU 3987 C ALA B 95 9557 9506 9548 -403 -330 -1473 C ATOM 3988 O ALA B 95 -72.899 -0.515 18.109 1.00 76.65 O ANISOU 3988 O ALA B 95 9803 9706 9613 -265 -437 -1688 O ATOM 3989 CB ALA B 95 -73.157 -1.027 21.357 1.00 71.74 C ANISOU 3989 CB ALA B 95 9346 8598 9315 -511 -348 -1313 C ATOM 3990 N VAL B 96 -74.543 0.724 19.067 1.00 71.14 N ANISOU 3990 N VAL B 96 8878 9087 9067 -585 -293 -1332 N ATOM 3991 CA VAL B 96 -75.372 0.846 17.865 1.00 72.22 C ANISOU 3991 CA VAL B 96 8929 9373 9139 -650 -383 -1401 C ATOM 3992 C VAL B 96 -74.641 1.707 16.817 1.00 76.39 C ANISOU 3992 C VAL B 96 9370 10179 9475 -477 -327 -1456 C ATOM 3993 O VAL B 96 -74.547 1.306 15.656 1.00 77.56 O ANISOU 3993 O VAL B 96 9549 10420 9499 -417 -432 -1630 O ATOM 3994 CB VAL B 96 -76.810 1.351 18.177 1.00 75.73 C ANISOU 3994 CB VAL B 96 9205 9894 9676 -860 -367 -1240 C ATOM 3995 CG1 VAL B 96 -77.604 1.600 16.897 1.00 76.55 C ANISOU 3995 CG1 VAL B 96 9201 10188 9697 -898 -468 -1306 C ATOM 3996 CG2 VAL B 96 -77.553 0.369 19.076 1.00 76.77 C ANISOU 3996 CG2 VAL B 96 9407 9808 9953 -1090 -436 -1186 C ATOM 3997 N ASP B 97 -74.073 2.851 17.248 1.00 71.49 N ANISOU 3997 N ASP B 97 8658 9691 8815 -411 -174 -1310 N ATOM 3998 CA ASP B 97 -73.308 3.764 16.393 1.00 71.13 C ANISOU 3998 CA ASP B 97 8539 9914 8574 -307 -116 -1303 C ATOM 3999 C ASP B 97 -72.092 3.064 15.759 1.00 77.22 C ANISOU 3999 C ASP B 97 9376 10780 9186 -139 -140 -1514 C ATOM 4000 O ASP B 97 -71.670 3.450 14.670 1.00 78.14 O ANISOU 4000 O ASP B 97 9426 11171 9094 -83 -139 -1570 O ATOM 4001 CB ASP B 97 -72.898 5.019 17.190 1.00 70.72 C ANISOU 4001 CB ASP B 97 8422 9914 8536 -305 24 -1098 C ATOM 4002 CG ASP B 97 -71.749 5.811 16.606 1.00 79.11 C ANISOU 4002 CG ASP B 97 9444 11218 9396 -235 90 -1070 C ATOM 4003 OD1 ASP B 97 -70.586 5.517 16.965 1.00 79.93 O ANISOU 4003 OD1 ASP B 97 9571 11352 9446 -143 152 -1132 O ATOM 4004 OD2 ASP B 97 -72.011 6.715 15.777 1.00 82.20 O ANISOU 4004 OD2 ASP B 97 9777 11784 9669 -283 67 -978 O ATOM 4005 N ALA B 98 -71.539 2.043 16.441 1.00 74.37 N ANISOU 4005 N ALA B 98 9141 10211 8906 -48 -169 -1630 N ATOM 4006 CA ALA B 98 -70.397 1.280 15.951 1.00 75.81 C ANISOU 4006 CA ALA B 98 9384 10474 8948 172 -213 -1870 C ATOM 4007 C ALA B 98 -70.829 0.283 14.855 1.00 83.06 C ANISOU 4007 C ALA B 98 10396 11361 9801 220 -394 -2121 C ATOM 4008 O ALA B 98 -70.433 0.461 13.700 1.00 83.89 O ANISOU 4008 O ALA B 98 10421 11772 9681 318 -398 -2254 O ATOM 4009 CB ALA B 98 -69.700 0.571 17.105 1.00 76.33 C ANISOU 4009 CB ALA B 98 9573 10298 9131 281 -216 -1901 C ATOM 4010 N VAL B 99 -71.677 -0.724 15.204 1.00 80.80 N ANISOU 4010 N VAL B 99 10279 10724 9696 119 -550 -2173 N ATOM 4011 CA VAL B 99 -72.165 -1.769 14.285 1.00 83.11 C ANISOU 4011 CA VAL B 99 10709 10909 9958 133 -764 -2418 C ATOM 4012 C VAL B 99 -72.993 -1.249 13.118 1.00 87.52 C ANISOU 4012 C VAL B 99 11140 11713 10399 18 -793 -2417 C ATOM 4013 O VAL B 99 -72.873 -1.765 12.005 1.00 90.20 O ANISOU 4013 O VAL B 99 11526 12165 10580 129 -914 -2665 O ATOM 4014 CB VAL B 99 -72.872 -2.974 14.970 1.00 88.12 C ANISOU 4014 CB VAL B 99 11584 11084 10812 -8 -954 -2444 C ATOM 4015 CG1 VAL B 99 -71.891 -3.825 15.751 1.00 88.76 C ANISOU 4015 CG1 VAL B 99 11870 10901 10954 189 -1018 -2547 C ATOM 4016 CG2 VAL B 99 -74.050 -2.546 15.845 1.00 86.28 C ANISOU 4016 CG2 VAL B 99 11273 10746 10765 -330 -895 -2150 C ATOM 4017 N ALA B 100 -73.867 -0.271 13.388 1.00 81.03 N ANISOU 4017 N ALA B 100 10167 10970 9652 -185 -702 -2157 N ATOM 4018 CA ALA B 100 -74.780 0.294 12.407 1.00 80.66 C ANISOU 4018 CA ALA B 100 9994 11135 9516 -299 -747 -2117 C ATOM 4019 C ALA B 100 -74.750 1.818 12.454 1.00 81.31 C ANISOU 4019 C ALA B 100 9894 11467 9535 -323 -585 -1869 C ATOM 4020 O ALA B 100 -73.812 2.400 12.995 1.00 79.82 O ANISOU 4020 O ALA B 100 9678 11337 9314 -237 -441 -1775 O ATOM 4021 CB ALA B 100 -76.187 -0.224 12.674 1.00 82.13 C ANISOU 4021 CB ALA B 100 10204 11115 9887 -538 -879 -2072 C ATOM 4022 N ASN B 101 -75.773 2.454 11.885 1.00 76.51 N ANISOU 4022 N ASN B 101 9175 10991 8905 -439 -634 -1766 N ATOM 4023 CA ASN B 101 -75.970 3.895 11.799 1.00 74.68 C ANISOU 4023 CA ASN B 101 8809 10947 8617 -462 -550 -1535 C ATOM 4024 C ASN B 101 -76.273 4.546 13.181 1.00 77.41 C ANISOU 4024 C ASN B 101 9108 11138 9166 -513 -439 -1323 C ATOM 4025 O ASN B 101 -76.512 3.834 14.165 1.00 77.38 O ANISOU 4025 O ASN B 101 9149 10911 9339 -571 -428 -1339 O ATOM 4026 CB ASN B 101 -77.161 4.113 10.860 1.00 73.95 C ANISOU 4026 CB ASN B 101 8632 10987 8476 -550 -689 -1527 C ATOM 4027 CG ASN B 101 -77.193 5.401 10.098 1.00 87.24 C ANISOU 4027 CG ASN B 101 10236 12922 9990 -526 -687 -1368 C ATOM 4028 OD1 ASN B 101 -76.672 6.432 10.520 1.00 76.99 O ANISOU 4028 OD1 ASN B 101 8926 11652 8673 -494 -582 -1184 O ATOM 4029 ND2 ASN B 101 -77.845 5.369 8.957 1.00 82.06 N ANISOU 4029 ND2 ASN B 101 9541 12436 9203 -557 -827 -1426 N ATOM 4030 N TRP B 102 -76.278 5.904 13.237 1.00 72.24 N ANISOU 4030 N TRP B 102 8380 10600 8470 -495 -377 -1125 N ATOM 4031 CA TRP B 102 -76.672 6.688 14.411 1.00 70.17 C ANISOU 4031 CA TRP B 102 8067 10226 8368 -509 -297 -948 C ATOM 4032 C TRP B 102 -78.098 7.202 14.124 1.00 73.18 C ANISOU 4032 C TRP B 102 8325 10680 8801 -550 -400 -879 C ATOM 4033 O TRP B 102 -78.276 8.115 13.315 1.00 73.01 O ANISOU 4033 O TRP B 102 8278 10802 8661 -509 -469 -796 O ATOM 4034 CB TRP B 102 -75.692 7.845 14.690 1.00 68.09 C ANISOU 4034 CB TRP B 102 7838 10007 8025 -446 -197 -799 C ATOM 4035 CG TRP B 102 -76.198 8.834 15.705 1.00 68.43 C ANISOU 4035 CG TRP B 102 7845 9949 8204 -430 -156 -637 C ATOM 4036 CD1 TRP B 102 -76.966 9.934 15.463 1.00 71.81 C ANISOU 4036 CD1 TRP B 102 8230 10425 8629 -396 -236 -516 C ATOM 4037 CD2 TRP B 102 -75.998 8.790 17.124 1.00 67.38 C ANISOU 4037 CD2 TRP B 102 7726 9657 8218 -419 -45 -602 C ATOM 4038 NE1 TRP B 102 -77.262 10.575 16.641 1.00 70.46 N ANISOU 4038 NE1 TRP B 102 8041 10135 8594 -343 -181 -432 N ATOM 4039 CE2 TRP B 102 -76.673 9.900 17.677 1.00 71.00 C ANISOU 4039 CE2 TRP B 102 8137 10090 8748 -369 -54 -478 C ATOM 4040 CE3 TRP B 102 -75.267 7.948 17.982 1.00 68.22 C ANISOU 4040 CE3 TRP B 102 7891 9641 8388 -427 49 -665 C ATOM 4041 CZ2 TRP B 102 -76.664 10.174 19.050 1.00 69.61 C ANISOU 4041 CZ2 TRP B 102 7957 9798 8692 -337 42 -431 C ATOM 4042 CZ3 TRP B 102 -75.256 8.222 19.344 1.00 68.78 C ANISOU 4042 CZ3 TRP B 102 7963 9592 8579 -418 142 -589 C ATOM 4043 CH2 TRP B 102 -75.949 9.324 19.865 1.00 69.16 C ANISOU 4043 CH2 TRP B 102 7950 9644 8683 -378 147 -479 C ATOM 4044 N TYR B 103 -79.098 6.608 14.795 1.00 69.22 N ANISOU 4044 N TYR B 103 7739 10098 8462 -638 -419 -905 N ATOM 4045 CA TYR B 103 -80.523 6.900 14.623 1.00 70.15 C ANISOU 4045 CA TYR B 103 7687 10333 8633 -680 -516 -872 C ATOM 4046 C TYR B 103 -81.151 7.844 15.661 1.00 73.15 C ANISOU 4046 C TYR B 103 7942 10729 9124 -612 -452 -742 C ATOM 4047 O TYR B 103 -82.243 8.368 15.439 1.00 74.91 O ANISOU 4047 O TYR B 103 8004 11100 9360 -574 -539 -714 O ATOM 4048 CB TYR B 103 -81.308 5.587 14.662 1.00 73.16 C ANISOU 4048 CB TYR B 103 8020 10678 9098 -863 -593 -989 C ATOM 4049 CG TYR B 103 -80.761 4.463 13.810 1.00 76.15 C ANISOU 4049 CG TYR B 103 8552 10986 9395 -918 -682 -1164 C ATOM 4050 CD1 TYR B 103 -80.019 3.429 14.379 1.00 77.49 C ANISOU 4050 CD1 TYR B 103 8885 10933 9623 -958 -646 -1251 C ATOM 4051 CD2 TYR B 103 -81.078 4.370 12.457 1.00 78.73 C ANISOU 4051 CD2 TYR B 103 8866 11466 9584 -919 -828 -1261 C ATOM 4052 CE1 TYR B 103 -79.579 2.350 13.615 1.00 79.14 C ANISOU 4052 CE1 TYR B 103 9251 11058 9760 -967 -761 -1451 C ATOM 4053 CE2 TYR B 103 -80.642 3.296 11.683 1.00 80.97 C ANISOU 4053 CE2 TYR B 103 9292 11694 9781 -947 -927 -1463 C ATOM 4054 CZ TYR B 103 -79.897 2.285 12.269 1.00 87.65 C ANISOU 4054 CZ TYR B 103 10309 12301 10695 -958 -898 -1568 C ATOM 4055 OH TYR B 103 -79.462 1.231 11.505 1.00 90.91 O ANISOU 4055 OH TYR B 103 10883 12640 11019 -937 -1023 -1801 O ATOM 4056 N PHE B 104 -80.485 8.025 16.790 1.00 67.06 N ANISOU 4056 N PHE B 104 7235 9825 8421 -577 -311 -686 N ATOM 4057 CA PHE B 104 -80.927 8.771 17.970 1.00 66.19 C ANISOU 4057 CA PHE B 104 7028 9715 8407 -502 -230 -601 C ATOM 4058 C PHE B 104 -81.169 10.290 17.878 1.00 69.72 C ANISOU 4058 C PHE B 104 7452 10216 8822 -306 -281 -511 C ATOM 4059 O PHE B 104 -81.638 10.889 18.851 1.00 69.50 O ANISOU 4059 O PHE B 104 7337 10204 8868 -206 -233 -481 O ATOM 4060 CB PHE B 104 -80.084 8.359 19.192 1.00 66.50 C ANISOU 4060 CB PHE B 104 7165 9589 8512 -539 -79 -583 C ATOM 4061 CG PHE B 104 -79.741 6.883 19.170 1.00 67.81 C ANISOU 4061 CG PHE B 104 7418 9646 8702 -701 -79 -670 C ATOM 4062 CD1 PHE B 104 -78.459 6.456 18.844 1.00 69.12 C ANISOU 4062 CD1 PHE B 104 7765 9695 8803 -669 -62 -724 C ATOM 4063 CD2 PHE B 104 -80.723 5.919 19.396 1.00 70.51 C ANISOU 4063 CD2 PHE B 104 7661 10013 9116 -885 -124 -705 C ATOM 4064 CE1 PHE B 104 -78.154 5.093 18.792 1.00 70.26 C ANISOU 4064 CE1 PHE B 104 8019 9707 8970 -767 -103 -832 C ATOM 4065 CE2 PHE B 104 -80.417 4.558 19.334 1.00 73.42 C ANISOU 4065 CE2 PHE B 104 8167 10220 9510 -1038 -174 -784 C ATOM 4066 CZ PHE B 104 -79.135 4.156 19.042 1.00 70.52 C ANISOU 4066 CZ PHE B 104 8007 9696 9092 -953 -171 -857 C ATOM 4067 N GLY B 105 -80.891 10.895 16.729 1.00 66.66 N ANISOU 4067 N GLY B 105 7151 9860 8315 -248 -395 -472 N ATOM 4068 CA GLY B 105 -81.148 12.318 16.525 1.00 67.61 C ANISOU 4068 CA GLY B 105 7303 9986 8400 -72 -500 -371 C ATOM 4069 C GLY B 105 -80.122 13.289 17.067 1.00 71.60 C ANISOU 4069 C GLY B 105 7996 10320 8889 0 -452 -265 C ATOM 4070 O GLY B 105 -79.089 12.879 17.601 1.00 69.70 O ANISOU 4070 O GLY B 105 7846 9987 8652 -85 -317 -268 O ATOM 4071 N ASN B 106 -80.407 14.597 16.921 1.00 70.21 N ANISOU 4071 N ASN B 106 7893 10092 8691 159 -589 -173 N ATOM 4072 CA ASN B 106 -79.500 15.681 17.309 1.00 69.99 C ANISOU 4072 CA ASN B 106 8083 9873 8637 205 -603 -54 C ATOM 4073 C ASN B 106 -79.331 15.965 18.799 1.00 73.94 C ANISOU 4073 C ASN B 106 8594 10246 9255 290 -490 -87 C ATOM 4074 O ASN B 106 -78.198 16.198 19.225 1.00 72.14 O ANISOU 4074 O ASN B 106 8520 9888 9001 212 -416 -26 O ATOM 4075 CB ASN B 106 -79.779 16.955 16.523 1.00 72.63 C ANISOU 4075 CB ASN B 106 8561 10143 8893 320 -837 72 C ATOM 4076 CG ASN B 106 -78.548 17.510 15.860 1.00 93.10 C ANISOU 4076 CG ASN B 106 11392 12652 11330 164 -882 240 C ATOM 4077 OD1 ASN B 106 -78.162 17.094 14.762 1.00 86.31 O ANISOU 4077 OD1 ASN B 106 10539 11938 10317 15 -896 281 O ATOM 4078 ND2 ASN B 106 -77.893 18.451 16.521 1.00 85.39 N ANISOU 4078 ND2 ASN B 106 10608 11466 10372 179 -908 336 N ATOM 4079 N PHE B 107 -80.437 15.970 19.584 1.00 72.30 N ANISOU 4079 N PHE B 107 8206 10112 9154 446 -477 -187 N ATOM 4080 CA PHE B 107 -80.381 16.230 21.032 1.00 71.87 C ANISOU 4080 CA PHE B 107 8138 9986 9184 544 -367 -238 C ATOM 4081 C PHE B 107 -79.577 15.169 21.775 1.00 75.20 C ANISOU 4081 C PHE B 107 8547 10397 9630 354 -155 -260 C ATOM 4082 O PHE B 107 -78.729 15.514 22.603 1.00 73.33 O ANISOU 4082 O PHE B 107 8440 10020 9402 354 -81 -233 O ATOM 4083 CB PHE B 107 -81.781 16.394 21.654 1.00 75.31 C ANISOU 4083 CB PHE B 107 8333 10597 9686 751 -387 -356 C ATOM 4084 CG PHE B 107 -81.739 16.735 23.127 1.00 76.88 C ANISOU 4084 CG PHE B 107 8513 10763 9934 874 -277 -424 C ATOM 4085 CD1 PHE B 107 -81.912 15.748 24.094 1.00 79.43 C ANISOU 4085 CD1 PHE B 107 8653 11237 10288 753 -76 -483 C ATOM 4086 CD2 PHE B 107 -81.473 18.034 23.551 1.00 79.89 C ANISOU 4086 CD2 PHE B 107 9091 10947 10318 1093 -389 -421 C ATOM 4087 CE1 PHE B 107 -81.839 16.058 25.460 1.00 80.20 C ANISOU 4087 CE1 PHE B 107 8736 11338 10401 858 31 -543 C ATOM 4088 CE2 PHE B 107 -81.405 18.343 24.916 1.00 82.72 C ANISOU 4088 CE2 PHE B 107 9441 11285 10703 1216 -293 -508 C ATOM 4089 CZ PHE B 107 -81.594 17.354 25.861 1.00 79.83 C ANISOU 4089 CZ PHE B 107 8864 11119 10350 1102 -73 -569 C ATOM 4090 N LEU B 108 -79.843 13.885 21.470 1.00 72.96 N ANISOU 4090 N LEU B 108 8125 10242 9355 193 -83 -310 N ATOM 4091 CA LEU B 108 -79.143 12.754 22.066 1.00 71.79 C ANISOU 4091 CA LEU B 108 7990 10057 9231 23 75 -332 C ATOM 4092 C LEU B 108 -77.668 12.697 21.674 1.00 75.78 C ANISOU 4092 C LEU B 108 8692 10439 9662 -61 100 -280 C ATOM 4093 O LEU B 108 -76.891 12.103 22.408 1.00 74.48 O ANISOU 4093 O LEU B 108 8575 10207 9516 -131 217 -291 O ATOM 4094 CB LEU B 108 -79.867 11.436 21.781 1.00 72.48 C ANISOU 4094 CB LEU B 108 7923 10271 9347 -130 91 -400 C ATOM 4095 CG LEU B 108 -80.635 10.851 22.970 1.00 77.99 C ANISOU 4095 CG LEU B 108 8450 11066 10117 -189 196 -432 C ATOM 4096 CD1 LEU B 108 -81.928 11.621 23.254 1.00 79.89 C ANISOU 4096 CD1 LEU B 108 8472 11511 10371 -32 152 -465 C ATOM 4097 CD2 LEU B 108 -80.981 9.418 22.722 1.00 81.96 C ANISOU 4097 CD2 LEU B 108 8889 11609 10643 -419 198 -466 C ATOM 4098 N CYS B 109 -77.270 13.354 20.559 1.00 73.82 N ANISOU 4098 N CYS B 109 8548 10188 9312 -55 -13 -214 N ATOM 4099 CA CYS B 109 -75.866 13.431 20.148 1.00 73.34 C ANISOU 4099 CA CYS B 109 8633 10091 9142 -147 14 -155 C ATOM 4100 C CYS B 109 -75.139 14.393 21.071 1.00 75.79 C ANISOU 4100 C CYS B 109 9070 10263 9466 -111 43 -77 C ATOM 4101 O CYS B 109 -73.998 14.128 21.455 1.00 75.07 O ANISOU 4101 O CYS B 109 9036 10149 9337 -190 136 -66 O ATOM 4102 CB CYS B 109 -75.726 13.852 18.690 1.00 75.24 C ANISOU 4102 CB CYS B 109 8930 10423 9235 -190 -113 -88 C ATOM 4103 SG CYS B 109 -74.015 13.879 18.101 1.00 79.12 S ANISOU 4103 SG CYS B 109 9534 10989 9538 -334 -63 -19 S ATOM 4104 N LYS B 110 -75.814 15.504 21.431 1.00 71.45 N ANISOU 4104 N LYS B 110 8562 9623 8965 25 -57 -40 N ATOM 4105 CA LYS B 110 -75.300 16.503 22.354 1.00 70.47 C ANISOU 4105 CA LYS B 110 8580 9332 8862 81 -69 9 C ATOM 4106 C LYS B 110 -75.278 15.886 23.757 1.00 73.68 C ANISOU 4106 C LYS B 110 8901 9735 9359 110 95 -83 C ATOM 4107 O LYS B 110 -74.235 15.906 24.411 1.00 72.28 O ANISOU 4107 O LYS B 110 8811 9489 9164 41 171 -58 O ATOM 4108 CB LYS B 110 -76.172 17.765 22.333 1.00 73.74 C ANISOU 4108 CB LYS B 110 9072 9636 9308 273 -254 30 C ATOM 4109 CG LYS B 110 -76.087 18.554 21.043 1.00 79.24 C ANISOU 4109 CG LYS B 110 9919 10288 9903 233 -453 165 C ATOM 4110 CD LYS B 110 -77.114 19.673 21.011 1.00 86.93 C ANISOU 4110 CD LYS B 110 10970 11138 10923 476 -670 163 C ATOM 4111 CE LYS B 110 -77.255 20.296 19.647 1.00100.23 C ANISOU 4111 CE LYS B 110 12786 12794 12501 443 -889 304 C ATOM 4112 NZ LYS B 110 -76.009 20.984 19.211 1.00111.08 N ANISOU 4112 NZ LYS B 110 14422 14033 13751 217 -967 501 N ATOM 4113 N ALA B 111 -76.411 15.271 24.177 1.00 70.97 N ANISOU 4113 N ALA B 111 8373 9500 9092 184 148 -179 N ATOM 4114 CA ALA B 111 -76.570 14.633 25.488 1.00 70.38 C ANISOU 4114 CA ALA B 111 8200 9464 9077 185 298 -245 C ATOM 4115 C ALA B 111 -75.548 13.523 25.773 1.00 72.74 C ANISOU 4115 C ALA B 111 8532 9742 9365 20 422 -235 C ATOM 4116 O ALA B 111 -75.046 13.449 26.894 1.00 71.41 O ANISOU 4116 O ALA B 111 8400 9525 9209 18 515 -238 O ATOM 4117 CB ALA B 111 -77.993 14.128 25.675 1.00 72.32 C ANISOU 4117 CB ALA B 111 8216 9890 9371 231 320 -322 C ATOM 4118 N VAL B 112 -75.218 12.688 24.766 1.00 69.34 N ANISOU 4118 N VAL B 112 8099 9349 8898 -92 408 -236 N ATOM 4119 CA VAL B 112 -74.228 11.612 24.910 1.00 68.59 C ANISOU 4119 CA VAL B 112 8047 9228 8785 -195 488 -256 C ATOM 4120 C VAL B 112 -72.804 12.203 25.036 1.00 72.38 C ANISOU 4120 C VAL B 112 8654 9657 9190 -204 505 -203 C ATOM 4121 O VAL B 112 -71.992 11.708 25.831 1.00 70.37 O ANISOU 4121 O VAL B 112 8432 9366 8938 -225 585 -214 O ATOM 4122 CB VAL B 112 -74.405 10.507 23.826 1.00 72.94 C ANISOU 4122 CB VAL B 112 8559 9839 9315 -273 447 -318 C ATOM 4123 CG1 VAL B 112 -73.135 9.685 23.606 1.00 72.35 C ANISOU 4123 CG1 VAL B 112 8565 9744 9181 -309 478 -362 C ATOM 4124 CG2 VAL B 112 -75.574 9.593 24.181 1.00 73.43 C ANISOU 4124 CG2 VAL B 112 8508 9926 9464 -335 456 -363 C ATOM 4125 N HIS B 113 -72.544 13.310 24.310 1.00 70.46 N ANISOU 4125 N HIS B 113 8481 9416 8873 -201 414 -131 N ATOM 4126 CA HIS B 113 -71.273 14.027 24.372 1.00 70.62 C ANISOU 4126 CA HIS B 113 8611 9415 8805 -262 408 -53 C ATOM 4127 C HIS B 113 -71.105 14.715 25.738 1.00 75.67 C ANISOU 4127 C HIS B 113 9322 9927 9502 -212 435 -37 C ATOM 4128 O HIS B 113 -70.021 14.654 26.323 1.00 74.29 O ANISOU 4128 O HIS B 113 9187 9751 9290 -269 491 -22 O ATOM 4129 CB HIS B 113 -71.156 15.034 23.217 1.00 72.49 C ANISOU 4129 CB HIS B 113 8929 9679 8936 -322 277 53 C ATOM 4130 CG HIS B 113 -70.570 14.439 21.974 1.00 76.36 C ANISOU 4130 CG HIS B 113 9367 10358 9288 -419 281 51 C ATOM 4131 ND1 HIS B 113 -71.370 13.851 21.007 1.00 78.70 N ANISOU 4131 ND1 HIS B 113 9588 10741 9571 -392 239 -7 N ATOM 4132 CD2 HIS B 113 -69.276 14.339 21.588 1.00 78.33 C ANISOU 4132 CD2 HIS B 113 9612 10760 9392 -530 321 81 C ATOM 4133 CE1 HIS B 113 -70.542 13.425 20.068 1.00 78.55 C ANISOU 4133 CE1 HIS B 113 9539 10910 9396 -473 255 -21 C ATOM 4134 NE2 HIS B 113 -69.274 13.705 20.366 1.00 78.81 N ANISOU 4134 NE2 HIS B 113 9597 11010 9337 -553 310 31 N ATOM 4135 N VAL B 114 -72.195 15.316 26.264 1.00 74.42 N ANISOU 4135 N VAL B 114 9162 9692 9422 -87 392 -63 N ATOM 4136 CA VAL B 114 -72.179 16.000 27.560 1.00 74.97 C ANISOU 4136 CA VAL B 114 9298 9658 9530 -2 405 -84 C ATOM 4137 C VAL B 114 -71.946 15.083 28.752 1.00 78.88 C ANISOU 4137 C VAL B 114 9722 10193 10055 -11 555 -139 C ATOM 4138 O VAL B 114 -71.191 15.442 29.657 1.00 78.48 O ANISOU 4138 O VAL B 114 9754 10082 9984 -18 582 -132 O ATOM 4139 CB VAL B 114 -73.299 17.054 27.802 1.00 80.50 C ANISOU 4139 CB VAL B 114 10026 10282 10276 185 295 -125 C ATOM 4140 CG1 VAL B 114 -73.339 18.097 26.692 1.00 81.72 C ANISOU 4140 CG1 VAL B 114 10321 10335 10392 189 102 -40 C ATOM 4141 CG2 VAL B 114 -74.664 16.421 28.013 1.00 80.73 C ANISOU 4141 CG2 VAL B 114 9852 10455 10365 295 354 -219 C ATOM 4142 N ILE B 115 -72.584 13.896 28.743 1.00 75.15 N ANISOU 4142 N ILE B 115 9115 9816 9624 -30 634 -182 N ATOM 4143 CA ILE B 115 -72.465 12.907 29.814 1.00 74.09 C ANISOU 4143 CA ILE B 115 8935 9706 9509 -67 752 -204 C ATOM 4144 C ILE B 115 -71.029 12.379 29.897 1.00 76.66 C ANISOU 4144 C ILE B 115 9339 9997 9790 -143 782 -178 C ATOM 4145 O ILE B 115 -70.494 12.264 30.997 1.00 75.76 O ANISOU 4145 O ILE B 115 9263 9858 9664 -140 840 -173 O ATOM 4146 CB ILE B 115 -73.569 11.816 29.698 1.00 77.63 C ANISOU 4146 CB ILE B 115 9246 10245 10006 -116 789 -231 C ATOM 4147 CG1 ILE B 115 -74.948 12.406 30.102 1.00 79.13 C ANISOU 4147 CG1 ILE B 115 9305 10544 10216 -19 790 -271 C ATOM 4148 CG2 ILE B 115 -73.241 10.597 30.557 1.00 78.32 C ANISOU 4148 CG2 ILE B 115 9343 10315 10101 -211 872 -215 C ATOM 4149 CD1 ILE B 115 -76.177 11.748 29.502 1.00 85.50 C ANISOU 4149 CD1 ILE B 115 9945 11486 11056 -74 773 -292 C ATOM 4150 N TYR B 116 -70.393 12.135 28.737 1.00 73.27 N ANISOU 4150 N TYR B 116 8923 9600 9316 -194 737 -172 N ATOM 4151 CA TYR B 116 -69.007 11.669 28.628 1.00 72.87 C ANISOU 4151 CA TYR B 116 8903 9587 9197 -232 756 -174 C ATOM 4152 C TYR B 116 -68.027 12.723 29.185 1.00 76.55 C ANISOU 4152 C TYR B 116 9439 10043 9602 -257 747 -119 C ATOM 4153 O TYR B 116 -67.132 12.380 29.960 1.00 75.32 O ANISOU 4153 O TYR B 116 9295 9902 9421 -258 790 -127 O ATOM 4154 CB TYR B 116 -68.692 11.321 27.160 1.00 74.68 C ANISOU 4154 CB TYR B 116 9098 9920 9357 -263 709 -199 C ATOM 4155 CG TYR B 116 -67.322 10.730 26.899 1.00 76.52 C ANISOU 4155 CG TYR B 116 9315 10266 9494 -263 728 -241 C ATOM 4156 CD1 TYR B 116 -66.847 9.660 27.651 1.00 78.36 C ANISOU 4156 CD1 TYR B 116 9558 10457 9758 -199 762 -303 C ATOM 4157 CD2 TYR B 116 -66.550 11.164 25.828 1.00 77.97 C ANISOU 4157 CD2 TYR B 116 9461 10625 9539 -317 699 -225 C ATOM 4158 CE1 TYR B 116 -65.601 9.092 27.396 1.00 79.96 C ANISOU 4158 CE1 TYR B 116 9727 10787 9866 -144 762 -371 C ATOM 4159 CE2 TYR B 116 -65.307 10.594 25.552 1.00 79.69 C ANISOU 4159 CE2 TYR B 116 9612 11023 9642 -290 722 -291 C ATOM 4160 CZ TYR B 116 -64.836 9.555 26.338 1.00 88.65 C ANISOU 4160 CZ TYR B 116 10749 12111 10821 -179 750 -379 C ATOM 4161 OH TYR B 116 -63.605 8.993 26.076 1.00 91.41 O ANISOU 4161 OH TYR B 116 11019 12660 11052 -100 757 -471 O ATOM 4162 N THR B 117 -68.238 14.007 28.820 1.00 73.81 N ANISOU 4162 N THR B 117 9154 9655 9234 -281 667 -63 N ATOM 4163 CA THR B 117 -67.464 15.167 29.273 1.00 73.57 C ANISOU 4163 CA THR B 117 9231 9570 9152 -340 612 -1 C ATOM 4164 C THR B 117 -67.558 15.254 30.807 1.00 76.63 C ANISOU 4164 C THR B 117 9655 9873 9587 -265 661 -45 C ATOM 4165 O THR B 117 -66.529 15.196 31.482 1.00 76.26 O ANISOU 4165 O THR B 117 9627 9855 9493 -314 688 -37 O ATOM 4166 CB THR B 117 -67.988 16.423 28.546 1.00 81.30 C ANISOU 4166 CB THR B 117 10315 10455 10121 -361 474 67 C ATOM 4167 OG1 THR B 117 -67.671 16.320 27.160 1.00 80.99 O ANISOU 4167 OG1 THR B 117 10241 10537 9992 -468 435 129 O ATOM 4168 CG2 THR B 117 -67.437 17.722 29.111 1.00 80.88 C ANISOU 4168 CG2 THR B 117 10430 10263 10037 -422 370 126 C ATOM 4169 N VAL B 118 -68.800 15.332 31.342 1.00 72.54 N ANISOU 4169 N VAL B 118 9121 9298 9143 -143 676 -99 N ATOM 4170 CA VAL B 118 -69.105 15.382 32.773 1.00 72.11 C ANISOU 4170 CA VAL B 118 9074 9219 9105 -58 735 -155 C ATOM 4171 C VAL B 118 -68.388 14.241 33.499 1.00 75.02 C ANISOU 4171 C VAL B 118 9398 9654 9451 -105 837 -149 C ATOM 4172 O VAL B 118 -67.667 14.515 34.451 1.00 74.75 O ANISOU 4172 O VAL B 118 9424 9605 9374 -111 846 -151 O ATOM 4173 CB VAL B 118 -70.639 15.409 33.038 1.00 76.66 C ANISOU 4173 CB VAL B 118 9564 9829 9732 75 758 -222 C ATOM 4174 CG1 VAL B 118 -70.979 15.032 34.482 1.00 76.58 C ANISOU 4174 CG1 VAL B 118 9501 9893 9701 130 865 -272 C ATOM 4175 CG2 VAL B 118 -71.231 16.770 32.683 1.00 77.69 C ANISOU 4175 CG2 VAL B 118 9781 9863 9876 193 622 -254 C ATOM 4176 N ASN B 119 -68.529 12.985 33.003 1.00 70.89 N ANISOU 4176 N ASN B 119 8794 9185 8955 -136 884 -145 N ATOM 4177 CA ASN B 119 -67.880 11.801 33.575 1.00 70.02 C ANISOU 4177 CA ASN B 119 8679 9096 8832 -158 937 -138 C ATOM 4178 C ASN B 119 -66.353 11.910 33.570 1.00 73.69 C ANISOU 4178 C ASN B 119 9176 9598 9226 -184 910 -127 C ATOM 4179 O ASN B 119 -65.738 11.651 34.604 1.00 73.53 O ANISOU 4179 O ASN B 119 9184 9581 9172 -169 934 -121 O ATOM 4180 CB ASN B 119 -68.344 10.504 32.900 1.00 69.18 C ANISOU 4180 CB ASN B 119 8524 8988 8771 -181 941 -150 C ATOM 4181 CG ASN B 119 -67.693 9.258 33.469 1.00 89.23 C ANISOU 4181 CG ASN B 119 11108 11492 11305 -180 949 -144 C ATOM 4182 OD1 ASN B 119 -66.724 8.727 32.919 1.00 83.66 O ANISOU 4182 OD1 ASN B 119 10415 10801 10571 -145 907 -180 O ATOM 4183 ND2 ASN B 119 -68.172 8.791 34.610 1.00 80.14 N ANISOU 4183 ND2 ASN B 119 9981 10310 10161 -206 992 -101 N ATOM 4184 N LEU B 120 -65.748 12.306 32.428 1.00 70.13 N ANISOU 4184 N LEU B 120 8705 9212 8730 -232 860 -119 N ATOM 4185 CA LEU B 120 -64.294 12.447 32.299 1.00 70.19 C ANISOU 4185 CA LEU B 120 8690 9338 8642 -281 838 -108 C ATOM 4186 C LEU B 120 -63.718 13.362 33.372 1.00 74.64 C ANISOU 4186 C LEU B 120 9319 9875 9167 -325 819 -77 C ATOM 4187 O LEU B 120 -62.817 12.951 34.104 1.00 74.30 O ANISOU 4187 O LEU B 120 9254 9898 9078 -308 834 -89 O ATOM 4188 CB LEU B 120 -63.888 12.950 30.896 1.00 70.69 C ANISOU 4188 CB LEU B 120 8707 9524 8628 -372 791 -80 C ATOM 4189 CG LEU B 120 -63.858 11.918 29.762 1.00 75.39 C ANISOU 4189 CG LEU B 120 9212 10235 9197 -323 802 -143 C ATOM 4190 CD1 LEU B 120 -63.883 12.599 28.416 1.00 76.08 C ANISOU 4190 CD1 LEU B 120 9272 10434 9202 -425 757 -97 C ATOM 4191 CD2 LEU B 120 -62.633 11.020 29.849 1.00 78.44 C ANISOU 4191 CD2 LEU B 120 9513 10785 9506 -252 820 -215 C ATOM 4192 N TYR B 121 -64.278 14.577 33.496 1.00 72.16 N ANISOU 4192 N TYR B 121 9098 9450 8872 -361 767 -52 N ATOM 4193 CA TYR B 121 -63.827 15.564 34.468 1.00 72.89 C ANISOU 4193 CA TYR B 121 9289 9477 8927 -402 716 -44 C ATOM 4194 C TYR B 121 -64.093 15.160 35.911 1.00 75.46 C ANISOU 4194 C TYR B 121 9634 9770 9267 -299 779 -96 C ATOM 4195 O TYR B 121 -63.149 15.104 36.698 1.00 75.35 O ANISOU 4195 O TYR B 121 9626 9812 9191 -329 775 -95 O ATOM 4196 CB TYR B 121 -64.346 16.976 34.132 1.00 75.76 C ANISOU 4196 CB TYR B 121 9791 9689 9306 -443 599 -19 C ATOM 4197 CG TYR B 121 -63.835 17.517 32.808 1.00 79.52 C ANISOU 4197 CG TYR B 121 10279 10211 9725 -609 513 77 C ATOM 4198 CD1 TYR B 121 -62.483 17.446 32.477 1.00 82.23 C ANISOU 4198 CD1 TYR B 121 10548 10738 9957 -780 508 138 C ATOM 4199 CD2 TYR B 121 -64.696 18.131 31.903 1.00 81.26 C ANISOU 4199 CD2 TYR B 121 10573 10324 9980 -600 429 113 C ATOM 4200 CE1 TYR B 121 -62.007 17.941 31.264 1.00 84.79 C ANISOU 4200 CE1 TYR B 121 10861 11165 10189 -968 439 244 C ATOM 4201 CE2 TYR B 121 -64.230 18.632 30.686 1.00 83.36 C ANISOU 4201 CE2 TYR B 121 10861 10647 10164 -779 342 228 C ATOM 4202 CZ TYR B 121 -62.883 18.536 30.372 1.00 92.87 C ANISOU 4202 CZ TYR B 121 11984 12061 11242 -979 356 299 C ATOM 4203 OH TYR B 121 -62.414 19.027 29.176 1.00 96.62 O ANISOU 4203 OH TYR B 121 12460 12653 11599 -1190 282 429 O ATOM 4204 N SER B 122 -65.349 14.807 36.242 1.00 71.06 N ANISOU 4204 N SER B 122 9062 9166 8770 -192 838 -134 N ATOM 4205 CA SER B 122 -65.747 14.406 37.594 1.00 70.47 C ANISOU 4205 CA SER B 122 8990 9108 8678 -117 910 -167 C ATOM 4206 C SER B 122 -64.948 13.222 38.150 1.00 73.79 C ANISOU 4206 C SER B 122 9378 9599 9062 -133 955 -130 C ATOM 4207 O SER B 122 -64.256 13.401 39.152 1.00 73.69 O ANISOU 4207 O SER B 122 9408 9612 8979 -134 945 -134 O ATOM 4208 CB SER B 122 -67.246 14.144 37.671 1.00 72.94 C ANISOU 4208 CB SER B 122 9243 9433 9037 -39 973 -197 C ATOM 4209 OG SER B 122 -67.587 13.070 36.814 1.00 78.72 O ANISOU 4209 OG SER B 122 9894 10189 9826 -77 1004 -159 O ATOM 4210 N SER B 123 -64.992 12.041 37.479 1.00 69.60 N ANISOU 4210 N SER B 123 8789 9082 8572 -135 977 -104 N ATOM 4211 CA SER B 123 -64.301 10.822 37.932 1.00 69.07 C ANISOU 4211 CA SER B 123 8726 9037 8483 -111 979 -78 C ATOM 4212 C SER B 123 -62.867 11.040 38.419 1.00 72.21 C ANISOU 4212 C SER B 123 9128 9510 8797 -105 933 -82 C ATOM 4213 O SER B 123 -62.517 10.542 39.489 1.00 72.44 O ANISOU 4213 O SER B 123 9197 9547 8778 -70 932 -58 O ATOM 4214 CB SER B 123 -64.384 9.696 36.903 1.00 72.12 C ANISOU 4214 CB SER B 123 9082 9397 8926 -91 959 -85 C ATOM 4215 OG SER B 123 -63.760 10.020 35.670 1.00 80.23 O ANISOU 4215 OG SER B 123 10047 10497 9941 -96 921 -125 O ATOM 4216 N VAL B 124 -62.066 11.830 37.675 1.00 67.67 N ANISOU 4216 N VAL B 124 8509 9014 8189 -160 887 -99 N ATOM 4217 CA VAL B 124 -60.681 12.116 38.051 1.00 67.53 C ANISOU 4217 CA VAL B 124 8455 9124 8079 -191 837 -101 C ATOM 4218 C VAL B 124 -60.590 13.116 39.210 1.00 71.43 C ANISOU 4218 C VAL B 124 9035 9584 8524 -243 814 -99 C ATOM 4219 O VAL B 124 -59.835 12.882 40.154 1.00 71.45 O ANISOU 4219 O VAL B 124 9037 9654 8456 -220 792 -99 O ATOM 4220 CB VAL B 124 -59.756 12.430 36.841 1.00 71.46 C ANISOU 4220 CB VAL B 124 8840 9790 8523 -268 798 -106 C ATOM 4221 CG1 VAL B 124 -60.169 13.709 36.102 1.00 71.16 C ANISOU 4221 CG1 VAL B 124 8846 9702 8492 -415 768 -69 C ATOM 4222 CG2 VAL B 124 -58.284 12.469 37.252 1.00 72.20 C ANISOU 4222 CG2 VAL B 124 8839 10090 8505 -294 751 -115 C ATOM 4223 N TRP B 125 -61.418 14.143 39.194 1.00 67.48 N ANISOU 4223 N TRP B 125 8616 8969 8054 -282 806 -112 N ATOM 4224 CA TRP B 125 -61.414 15.144 40.248 1.00 67.56 C ANISOU 4224 CA TRP B 125 8734 8923 8014 -301 762 -148 C ATOM 4225 C TRP B 125 -62.104 14.734 41.537 1.00 70.31 C ANISOU 4225 C TRP B 125 9121 9259 8334 -192 829 -179 C ATOM 4226 O TRP B 125 -62.026 15.422 42.526 1.00 70.04 O ANISOU 4226 O TRP B 125 9168 9213 8230 -182 797 -231 O ATOM 4227 CB TRP B 125 -62.027 16.437 39.734 1.00 66.92 C ANISOU 4227 CB TRP B 125 8754 8701 7971 -344 690 -173 C ATOM 4228 CG TRP B 125 -61.086 17.194 38.908 1.00 69.02 C ANISOU 4228 CG TRP B 125 9033 8985 8205 -521 585 -119 C ATOM 4229 CD1 TRP B 125 -60.920 17.103 37.569 1.00 71.70 C ANISOU 4229 CD1 TRP B 125 9300 9382 8560 -608 576 -55 C ATOM 4230 CD2 TRP B 125 -60.133 18.150 39.368 1.00 70.12 C ANISOU 4230 CD2 TRP B 125 9257 9118 8269 -672 466 -112 C ATOM 4231 NE1 TRP B 125 -59.927 17.950 37.160 1.00 72.46 N ANISOU 4231 NE1 TRP B 125 9420 9531 8581 -821 469 9 N ATOM 4232 CE2 TRP B 125 -59.428 18.604 38.253 1.00 74.90 C ANISOU 4232 CE2 TRP B 125 9828 9788 8841 -875 393 -22 C ATOM 4233 CE3 TRP B 125 -59.807 18.663 40.621 1.00 72.23 C ANISOU 4233 CE3 TRP B 125 9625 9343 8475 -672 407 -174 C ATOM 4234 CZ2 TRP B 125 -58.426 19.541 38.352 1.00 75.63 C ANISOU 4234 CZ2 TRP B 125 9983 9904 8851 -1109 259 27 C ATOM 4235 CZ3 TRP B 125 -58.821 19.588 40.712 1.00 75.00 C ANISOU 4235 CZ3 TRP B 125 10049 9689 8757 -879 266 -147 C ATOM 4236 CH2 TRP B 125 -58.140 20.020 39.592 1.00 76.39 C ANISOU 4236 CH2 TRP B 125 10189 9928 8909 -1110 191 -39 C ATOM 4237 N ILE B 126 -62.804 13.624 41.513 1.00 66.30 N ANISOU 4237 N ILE B 126 8563 8766 7864 -130 915 -146 N ATOM 4238 CA ILE B 126 -63.338 12.995 42.723 1.00 66.77 C ANISOU 4238 CA ILE B 126 8640 8865 7863 -77 983 -129 C ATOM 4239 C ILE B 126 -62.136 12.271 43.357 1.00 71.32 C ANISOU 4239 C ILE B 126 9225 9506 8368 -78 942 -80 C ATOM 4240 O ILE B 126 -61.887 12.435 44.554 1.00 71.82 O ANISOU 4240 O ILE B 126 9339 9625 8325 -66 936 -86 O ATOM 4241 CB ILE B 126 -64.553 12.053 42.441 1.00 69.65 C ANISOU 4241 CB ILE B 126 8956 9221 8286 -66 1068 -83 C ATOM 4242 CG1 ILE B 126 -65.783 12.864 41.977 1.00 70.14 C ANISOU 4242 CG1 ILE B 126 8983 9269 8397 -34 1101 -150 C ATOM 4243 CG2 ILE B 126 -64.909 11.216 43.688 1.00 70.86 C ANISOU 4243 CG2 ILE B 126 9132 9447 8347 -75 1127 -15 C ATOM 4244 CD1 ILE B 126 -66.801 12.098 41.134 1.00 76.74 C ANISOU 4244 CD1 ILE B 126 9737 10100 9319 -58 1149 -112 C ATOM 4245 N LEU B 127 -61.341 11.552 42.523 1.00 67.07 N ANISOU 4245 N LEU B 127 8630 8981 7873 -72 899 -51 N ATOM 4246 CA LEU B 127 -60.126 10.862 42.963 1.00 67.47 C ANISOU 4246 CA LEU B 127 8665 9111 7858 -26 833 -26 C ATOM 4247 C LEU B 127 -59.111 11.850 43.523 1.00 71.55 C ANISOU 4247 C LEU B 127 9170 9733 8281 -79 769 -65 C ATOM 4248 O LEU B 127 -58.301 11.479 44.376 1.00 71.71 O ANISOU 4248 O LEU B 127 9193 9838 8214 -38 717 -49 O ATOM 4249 CB LEU B 127 -59.491 10.049 41.828 1.00 67.51 C ANISOU 4249 CB LEU B 127 8587 9148 7916 34 790 -38 C ATOM 4250 CG LEU B 127 -60.270 8.846 41.312 1.00 72.33 C ANISOU 4250 CG LEU B 127 9236 9631 8612 92 806 -9 C ATOM 4251 CD1 LEU B 127 -59.664 8.356 40.053 1.00 72.67 C ANISOU 4251 CD1 LEU B 127 9194 9726 8692 165 760 -71 C ATOM 4252 CD2 LEU B 127 -60.302 7.715 42.321 1.00 75.43 C ANISOU 4252 CD2 LEU B 127 9741 9946 8974 154 764 68 C ATOM 4253 N ALA B 128 -59.166 13.110 43.044 1.00 68.00 N ANISOU 4253 N ALA B 128 8726 9266 7847 -180 751 -110 N ATOM 4254 CA ALA B 128 -58.329 14.199 43.532 1.00 68.63 C ANISOU 4254 CA ALA B 128 8830 9403 7843 -282 665 -145 C ATOM 4255 C ALA B 128 -58.819 14.586 44.931 1.00 72.67 C ANISOU 4255 C ALA B 128 9463 9869 8281 -241 672 -187 C ATOM 4256 O ALA B 128 -57.993 14.740 45.833 1.00 73.69 O ANISOU 4256 O ALA B 128 9606 10088 8305 -263 608 -201 O ATOM 4257 CB ALA B 128 -58.390 15.391 42.585 1.00 69.45 C ANISOU 4257 CB ALA B 128 8959 9440 7987 -420 614 -159 C ATOM 4258 N PHE B 129 -60.159 14.659 45.128 1.00 67.38 N ANISOU 4258 N PHE B 129 8855 9103 7644 -172 753 -213 N ATOM 4259 CA PHE B 129 -60.764 14.974 46.421 1.00 67.50 C ANISOU 4259 CA PHE B 129 8954 9135 7559 -109 784 -273 C ATOM 4260 C PHE B 129 -60.541 13.858 47.445 1.00 71.22 C ANISOU 4260 C PHE B 129 9412 9720 7928 -66 823 -196 C ATOM 4261 O PHE B 129 -60.344 14.164 48.621 1.00 71.70 O ANISOU 4261 O PHE B 129 9533 9858 7852 -50 801 -236 O ATOM 4262 CB PHE B 129 -62.248 15.329 46.268 1.00 69.20 C ANISOU 4262 CB PHE B 129 9185 9290 7816 -32 863 -333 C ATOM 4263 CG PHE B 129 -62.523 16.809 46.141 1.00 71.56 C ANISOU 4263 CG PHE B 129 9588 9473 8128 -12 776 -464 C ATOM 4264 CD1 PHE B 129 -62.146 17.510 44.999 1.00 74.41 C ANISOU 4264 CD1 PHE B 129 9985 9700 8588 -101 675 -454 C ATOM 4265 CD2 PHE B 129 -63.197 17.495 47.142 1.00 75.27 C ANISOU 4265 CD2 PHE B 129 10134 9966 8499 105 779 -602 C ATOM 4266 CE1 PHE B 129 -62.415 18.879 44.876 1.00 76.37 C ANISOU 4266 CE1 PHE B 129 10382 9783 8852 -88 551 -559 C ATOM 4267 CE2 PHE B 129 -63.478 18.861 47.010 1.00 79.22 C ANISOU 4267 CE2 PHE B 129 10771 10311 9019 165 658 -747 C ATOM 4268 CZ PHE B 129 -63.083 19.543 45.880 1.00 76.87 C ANISOU 4268 CZ PHE B 129 10545 9824 8837 62 531 -715 C ATOM 4269 N ILE B 130 -60.526 12.576 46.994 1.00 66.92 N ANISOU 4269 N ILE B 130 8813 9172 7441 -48 855 -87 N ATOM 4270 CA ILE B 130 -60.259 11.415 47.853 1.00 67.64 C ANISOU 4270 CA ILE B 130 8934 9320 7447 -13 849 17 C ATOM 4271 C ILE B 130 -58.816 11.499 48.370 1.00 72.70 C ANISOU 4271 C ILE B 130 9568 10054 8001 1 732 7 C ATOM 4272 O ILE B 130 -58.603 11.377 49.574 1.00 74.14 O ANISOU 4272 O ILE B 130 9809 10318 8042 17 708 33 O ATOM 4273 CB ILE B 130 -60.551 10.046 47.167 1.00 70.77 C ANISOU 4273 CB ILE B 130 9320 9629 7940 10 860 122 C ATOM 4274 CG1 ILE B 130 -61.986 9.969 46.613 1.00 70.86 C ANISOU 4274 CG1 ILE B 130 9313 9577 8033 -34 967 133 C ATOM 4275 CG2 ILE B 130 -60.317 8.902 48.145 1.00 73.47 C ANISOU 4275 CG2 ILE B 130 9750 9981 8185 36 814 249 C ATOM 4276 CD1 ILE B 130 -62.365 8.662 45.804 1.00 77.00 C ANISOU 4276 CD1 ILE B 130 10102 10235 8920 -44 956 223 C ATOM 4277 N SER B 131 -57.839 11.733 47.466 1.00 68.88 N ANISOU 4277 N SER B 131 8993 9599 7581 -15 660 -29 N ATOM 4278 CA SER B 131 -56.417 11.870 47.804 1.00 69.51 C ANISOU 4278 CA SER B 131 9009 9826 7575 -18 544 -48 C ATOM 4279 C SER B 131 -56.157 13.125 48.644 1.00 74.78 C ANISOU 4279 C SER B 131 9732 10544 8137 -115 496 -126 C ATOM 4280 O SER B 131 -55.292 13.099 49.520 1.00 75.49 O ANISOU 4280 O SER B 131 9815 10762 8106 -109 410 -128 O ATOM 4281 CB SER B 131 -55.558 11.873 46.548 1.00 71.86 C ANISOU 4281 CB SER B 131 9155 10209 7941 -37 500 -73 C ATOM 4282 OG SER B 131 -55.974 12.894 45.659 1.00 78.44 O ANISOU 4282 OG SER B 131 9981 10978 8845 -166 534 -114 O ATOM 4283 N LEU B 132 -56.939 14.203 48.403 1.00 71.38 N ANISOU 4283 N LEU B 132 9372 10001 7748 -187 532 -199 N ATOM 4284 CA LEU B 132 -56.875 15.467 49.150 1.00 72.01 C ANISOU 4284 CA LEU B 132 9558 10063 7741 -258 462 -305 C ATOM 4285 C LEU B 132 -57.423 15.283 50.570 1.00 75.55 C ANISOU 4285 C LEU B 132 10098 10563 8046 -165 504 -332 C ATOM 4286 O LEU B 132 -56.835 15.805 51.520 1.00 76.49 O ANISOU 4286 O LEU B 132 10274 10757 8031 -194 415 -397 O ATOM 4287 CB LEU B 132 -57.646 16.577 48.410 1.00 71.70 C ANISOU 4287 CB LEU B 132 9597 9848 7796 -310 460 -382 C ATOM 4288 CG LEU B 132 -57.513 17.993 48.942 1.00 77.83 C ANISOU 4288 CG LEU B 132 10527 10536 8511 -384 334 -509 C ATOM 4289 CD1 LEU B 132 -56.320 18.693 48.327 1.00 78.92 C ANISOU 4289 CD1 LEU B 132 10644 10680 8661 -603 185 -484 C ATOM 4290 CD2 LEU B 132 -58.766 18.785 48.659 1.00 79.78 C ANISOU 4290 CD2 LEU B 132 10894 10594 8824 -303 352 -608 C ATOM 4291 N ASP B 133 -58.545 14.547 50.706 1.00 70.72 N ANISOU 4291 N ASP B 133 9491 9935 7442 -76 635 -280 N ATOM 4292 CA ASP B 133 -59.175 14.268 51.995 1.00 71.76 C ANISOU 4292 CA ASP B 133 9683 10175 7408 -14 700 -278 C ATOM 4293 C ASP B 133 -58.250 13.389 52.833 1.00 76.86 C ANISOU 4293 C ASP B 133 10331 10943 7929 -8 635 -169 C ATOM 4294 O ASP B 133 -58.024 13.677 54.011 1.00 78.04 O ANISOU 4294 O ASP B 133 10543 11213 7897 2 597 -212 O ATOM 4295 CB ASP B 133 -60.533 13.593 51.786 1.00 73.16 C ANISOU 4295 CB ASP B 133 9830 10347 7622 22 851 -211 C ATOM 4296 CG ASP B 133 -61.453 13.728 52.967 1.00 84.67 C ANISOU 4296 CG ASP B 133 11318 11965 8889 65 943 -255 C ATOM 4297 OD1 ASP B 133 -61.313 12.931 53.915 1.00 86.95 O ANISOU 4297 OD1 ASP B 133 11630 12386 9022 44 958 -140 O ATOM 4298 OD2 ASP B 133 -62.335 14.620 52.934 1.00 90.13 O ANISOU 4298 OD2 ASP B 133 12005 12667 9572 131 995 -407 O ATOM 4299 N ARG B 134 -57.657 12.366 52.189 1.00 72.81 N ANISOU 4299 N ARG B 134 9755 10398 7510 7 598 -48 N ATOM 4300 CA ARG B 134 -56.700 11.423 52.769 1.00 73.57 C ANISOU 4300 CA ARG B 134 9853 10579 7520 59 498 57 C ATOM 4301 C ARG B 134 -55.466 12.159 53.332 1.00 78.22 C ANISOU 4301 C ARG B 134 10413 11305 8002 32 364 -29 C ATOM 4302 O ARG B 134 -54.917 11.736 54.355 1.00 79.23 O ANISOU 4302 O ARG B 134 10579 11550 7977 75 285 24 O ATOM 4303 CB ARG B 134 -56.321 10.356 51.716 1.00 72.95 C ANISOU 4303 CB ARG B 134 9710 10417 7591 126 462 142 C ATOM 4304 CG ARG B 134 -55.344 9.252 52.156 1.00 85.47 C ANISOU 4304 CG ARG B 134 11307 12055 9113 243 324 238 C ATOM 4305 CD ARG B 134 -55.795 8.387 53.331 1.00 96.44 C ANISOU 4305 CD ARG B 134 12853 13430 10361 261 309 390 C ATOM 4306 NE ARG B 134 -57.078 7.718 53.106 1.00101.15 N ANISOU 4306 NE ARG B 134 13537 13882 11015 204 416 500 N ATOM 4307 CZ ARG B 134 -58.131 7.834 53.909 1.00111.27 C ANISOU 4307 CZ ARG B 134 14889 15217 12172 98 527 561 C ATOM 4308 NH1 ARG B 134 -59.255 7.189 53.630 1.00105.38 N ANISOU 4308 NH1 ARG B 134 14188 14376 11475 16 616 670 N ATOM 4309 NH2 ARG B 134 -58.069 8.594 54.997 1.00 86.12 N ANISOU 4309 NH2 ARG B 134 11715 12210 8796 70 548 505 N ATOM 4310 N TYR B 135 -55.065 13.277 52.683 1.00 74.02 N ANISOU 4310 N TYR B 135 9826 10757 7540 -61 324 -148 N ATOM 4311 CA TYR B 135 -53.957 14.129 53.117 1.00 74.71 C ANISOU 4311 CA TYR B 135 9886 10966 7533 -151 185 -234 C ATOM 4312 C TYR B 135 -54.328 14.780 54.459 1.00 80.33 C ANISOU 4312 C TYR B 135 10741 11713 8066 -157 170 -321 C ATOM 4313 O TYR B 135 -53.573 14.666 55.422 1.00 81.18 O ANISOU 4313 O TYR B 135 10856 11973 8017 -149 70 -318 O ATOM 4314 CB TYR B 135 -53.615 15.177 52.031 1.00 74.96 C ANISOU 4314 CB TYR B 135 9861 10941 7680 -305 141 -309 C ATOM 4315 CG TYR B 135 -52.828 16.372 52.527 1.00 78.23 C ANISOU 4315 CG TYR B 135 10313 11414 7997 -468 -6 -411 C ATOM 4316 CD1 TYR B 135 -51.438 16.365 52.525 1.00 81.52 C ANISOU 4316 CD1 TYR B 135 10579 12044 8351 -566 -137 -394 C ATOM 4317 CD2 TYR B 135 -53.474 17.523 52.973 1.00 79.56 C ANISOU 4317 CD2 TYR B 135 10666 11431 8133 -523 -34 -539 C ATOM 4318 CE1 TYR B 135 -50.709 17.460 52.987 1.00 84.15 C ANISOU 4318 CE1 TYR B 135 10951 12433 8591 -762 -292 -479 C ATOM 4319 CE2 TYR B 135 -52.755 18.621 53.443 1.00 82.17 C ANISOU 4319 CE2 TYR B 135 11074 11772 8377 -687 -205 -642 C ATOM 4320 CZ TYR B 135 -51.372 18.585 53.447 1.00 90.33 C ANISOU 4320 CZ TYR B 135 11960 13012 9349 -832 -334 -600 C ATOM 4321 OH TYR B 135 -50.655 19.663 53.901 1.00 93.28 O ANISOU 4321 OH TYR B 135 12410 13399 9634 -1039 -519 -692 O ATOM 4322 N LEU B 136 -55.515 15.414 54.521 1.00 77.22 N ANISOU 4322 N LEU B 136 10451 11204 7684 -143 266 -409 N ATOM 4323 CA LEU B 136 -56.045 16.090 55.709 1.00 78.97 C ANISOU 4323 CA LEU B 136 10801 11477 7726 -106 269 -538 C ATOM 4324 C LEU B 136 -56.342 15.117 56.857 1.00 84.11 C ANISOU 4324 C LEU B 136 11472 12301 8184 -23 335 -435 C ATOM 4325 O LEU B 136 -56.334 15.521 58.021 1.00 85.27 O ANISOU 4325 O LEU B 136 11699 12579 8120 -1 300 -524 O ATOM 4326 CB LEU B 136 -57.307 16.887 55.345 1.00 78.74 C ANISOU 4326 CB LEU B 136 10843 11310 7764 -57 358 -668 C ATOM 4327 CG LEU B 136 -57.100 18.104 54.452 1.00 83.18 C ANISOU 4327 CG LEU B 136 11463 11670 8470 -145 248 -786 C ATOM 4328 CD1 LEU B 136 -58.348 18.416 53.687 1.00 82.41 C ANISOU 4328 CD1 LEU B 136 11386 11424 8500 -64 347 -837 C ATOM 4329 CD2 LEU B 136 -56.626 19.317 55.256 1.00 87.65 C ANISOU 4329 CD2 LEU B 136 12184 12209 8911 -193 78 -973 C ATOM 4330 N ALA B 137 -56.604 13.842 56.525 1.00 80.08 N ANISOU 4330 N ALA B 137 10907 11784 7734 11 413 -244 N ATOM 4331 CA ALA B 137 -56.870 12.798 57.505 1.00 81.39 C ANISOU 4331 CA ALA B 137 11119 12080 7725 47 451 -89 C ATOM 4332 C ALA B 137 -55.575 12.346 58.192 1.00 87.24 C ANISOU 4332 C ALA B 137 11868 12933 8348 64 285 -16 C ATOM 4333 O ALA B 137 -55.588 12.108 59.399 1.00 88.84 O ANISOU 4333 O ALA B 137 12145 13292 8317 76 265 32 O ATOM 4334 CB ALA B 137 -57.552 11.618 56.832 1.00 81.20 C ANISOU 4334 CB ALA B 137 11074 11953 7826 50 544 94 C ATOM 4335 N ILE B 138 -54.459 12.249 57.435 1.00 83.74 N ANISOU 4335 N ILE B 138 11328 12449 8041 70 164 -13 N ATOM 4336 CA ILE B 138 -53.162 11.803 57.959 1.00 85.44 C ANISOU 4336 CA ILE B 138 11504 12801 8156 118 -10 41 C ATOM 4337 C ILE B 138 -52.275 12.951 58.457 1.00 90.93 C ANISOU 4337 C ILE B 138 12168 13634 8746 35 -135 -122 C ATOM 4338 O ILE B 138 -51.859 12.938 59.619 1.00 92.61 O ANISOU 4338 O ILE B 138 12436 14005 8747 51 -227 -120 O ATOM 4339 CB ILE B 138 -52.440 10.822 56.981 1.00 88.10 C ANISOU 4339 CB ILE B 138 11730 13087 8657 214 -83 137 C ATOM 4340 CG1 ILE B 138 -53.180 9.457 56.929 1.00 88.61 C ANISOU 4340 CG1 ILE B 138 11901 13011 8758 301 -34 326 C ATOM 4341 CG2 ILE B 138 -50.954 10.629 57.352 1.00 90.27 C ANISOU 4341 CG2 ILE B 138 11900 13556 8843 284 -282 131 C ATOM 4342 CD1 ILE B 138 -52.931 8.616 55.664 1.00 95.12 C ANISOU 4342 CD1 ILE B 138 12650 13699 9792 405 -63 367 C ATOM 4343 N VAL B 139 -51.983 13.925 57.580 1.00 86.71 N ANISOU 4343 N VAL B 139 11559 13038 8350 -74 -155 -250 N ATOM 4344 CA VAL B 139 -51.128 15.079 57.887 1.00 87.82 C ANISOU 4344 CA VAL B 139 11684 13269 8415 -213 -300 -396 C ATOM 4345 C VAL B 139 -51.766 16.026 58.920 1.00 93.41 C ANISOU 4345 C VAL B 139 12574 13956 8960 -242 -298 -548 C ATOM 4346 O VAL B 139 -51.038 16.668 59.674 1.00 95.35 O ANISOU 4346 O VAL B 139 12852 14316 9062 -320 -448 -649 O ATOM 4347 CB VAL B 139 -50.662 15.810 56.591 1.00 90.63 C ANISOU 4347 CB VAL B 139 11927 13556 8954 -367 -335 -450 C ATOM 4348 CG1 VAL B 139 -49.705 16.961 56.895 1.00 92.29 C ANISOU 4348 CG1 VAL B 139 12127 13858 9080 -572 -516 -570 C ATOM 4349 CG2 VAL B 139 -50.014 14.833 55.611 1.00 89.58 C ANISOU 4349 CG2 VAL B 139 11588 13510 8940 -301 -331 -332 C ATOM 4350 N HIS B 140 -53.109 16.085 58.988 1.00 89.18 N ANISOU 4350 N HIS B 140 12145 13308 8431 -168 -138 -578 N ATOM 4351 CA HIS B 140 -53.798 16.987 59.912 1.00 90.51 C ANISOU 4351 CA HIS B 140 12468 13489 8433 -143 -127 -762 C ATOM 4352 C HIS B 140 -54.788 16.299 60.864 1.00 95.31 C ANISOU 4352 C HIS B 140 13127 14240 8846 -18 21 -703 C ATOM 4353 O HIS B 140 -55.904 16.787 61.069 1.00 95.84 O ANISOU 4353 O HIS B 140 13259 14297 8859 51 135 -829 O ATOM 4354 CB HIS B 140 -54.433 18.151 59.130 1.00 90.70 C ANISOU 4354 CB HIS B 140 12570 13282 8611 -178 -117 -933 C ATOM 4355 CG HIS B 140 -53.455 18.847 58.237 1.00 93.98 C ANISOU 4355 CG HIS B 140 12951 13576 9181 -360 -273 -955 C ATOM 4356 ND1 HIS B 140 -52.590 19.810 58.726 1.00 97.79 N ANISOU 4356 ND1 HIS B 140 13514 14070 9570 -501 -479 -1088 N ATOM 4357 CD2 HIS B 140 -53.196 18.655 56.923 1.00 94.01 C ANISOU 4357 CD2 HIS B 140 12837 13484 9397 -445 -253 -848 C ATOM 4358 CE1 HIS B 140 -51.861 20.193 57.693 1.00 96.66 C ANISOU 4358 CE1 HIS B 140 13297 13846 9586 -694 -574 -1040 C ATOM 4359 NE2 HIS B 140 -52.187 19.526 56.588 1.00 94.70 N ANISOU 4359 NE2 HIS B 140 12921 13547 9514 -657 -436 -899 N ATOM 4360 N ALA B 141 -54.348 15.192 61.484 1.00 92.01 N ANISOU 4360 N ALA B 141 12678 13981 8300 8 1 -513 N ATOM 4361 CA ALA B 141 -55.154 14.422 62.428 1.00 93.01 C ANISOU 4361 CA ALA B 141 12857 14274 8209 66 119 -395 C ATOM 4362 C ALA B 141 -55.177 15.097 63.797 1.00100.01 C ANISOU 4362 C ALA B 141 13839 15379 8781 88 74 -555 C ATOM 4363 O ALA B 141 -55.779 16.155 63.955 1.00100.39 O ANISOU 4363 O ALA B 141 13943 15421 8782 126 112 -798 O ATOM 4364 CB ALA B 141 -54.605 13.010 62.553 1.00 93.88 C ANISOU 4364 CB ALA B 141 12946 14424 8301 79 64 -118 C ATOM 4365 N GLN B 145 -57.738 20.265 63.030 1.00122.48 N ANISOU 4365 N GLN B 145 17023 17733 11782 374 56 -1728 N ATOM 4366 CA GLN B 145 -59.169 19.981 63.146 1.00122.55 C ANISOU 4366 CA GLN B 145 16952 17905 11706 540 283 -1760 C ATOM 4367 C GLN B 145 -59.754 19.313 61.878 1.00123.10 C ANISOU 4367 C GLN B 145 16887 17837 12048 503 428 -1557 C ATOM 4368 O GLN B 145 -58.988 18.740 61.097 1.00120.81 O ANISOU 4368 O GLN B 145 16547 17396 11958 354 383 -1344 O ATOM 4369 CB GLN B 145 -59.955 21.244 63.569 1.00126.40 C ANISOU 4369 CB GLN B 145 17564 18388 12075 759 240 -2143 C ATOM 4370 CG GLN B 145 -60.978 20.997 64.681 1.00143.82 C ANISOU 4370 CG GLN B 145 19689 21021 13935 937 424 -2249 C ATOM 4371 CD GLN B 145 -60.365 20.966 66.063 1.00166.09 C ANISOU 4371 CD GLN B 145 22578 24114 16414 922 353 -2309 C ATOM 4372 OE1 GLN B 145 -60.290 21.982 66.762 1.00164.47 O ANISOU 4372 OE1 GLN B 145 22525 23926 16039 1060 214 -2639 O ATOM 4373 NE2 GLN B 145 -59.921 19.796 66.500 1.00157.49 N ANISOU 4373 NE2 GLN B 145 21399 23232 15209 765 424 -1997 N ATOM 4374 N ARG B 146 -61.098 19.371 61.679 1.00118.55 N ANISOU 4374 N ARG B 146 16235 17345 11463 647 597 -1637 N ATOM 4375 CA ARG B 146 -61.798 18.708 60.574 1.00115.09 C ANISOU 4375 CA ARG B 146 15659 16822 11246 614 741 -1459 C ATOM 4376 C ARG B 146 -62.481 19.611 59.520 1.00115.97 C ANISOU 4376 C ARG B 146 15795 16686 11582 731 716 -1633 C ATOM 4377 O ARG B 146 -63.709 19.727 59.524 1.00116.41 O ANISOU 4377 O ARG B 146 15758 16890 11581 890 851 -1741 O ATOM 4378 CB ARG B 146 -62.778 17.653 61.123 1.00116.16 C ANISOU 4378 CB ARG B 146 15637 17309 11189 614 972 -1301 C ATOM 4379 CG ARG B 146 -63.021 16.468 60.196 1.00123.89 C ANISOU 4379 CG ARG B 146 16500 18208 12366 472 1077 -997 C ATOM 4380 CD ARG B 146 -64.345 15.775 60.475 1.00137.86 C ANISOU 4380 CD ARG B 146 18109 20285 13985 465 1298 -903 C ATOM 4381 NE ARG B 146 -64.432 15.213 61.828 1.00155.73 N ANISOU 4381 NE ARG B 146 20359 22919 15894 407 1372 -808 N ATOM 4382 CZ ARG B 146 -65.265 15.645 62.774 1.00176.46 C ANISOU 4382 CZ ARG B 146 22907 25929 18211 521 1487 -985 C ATOM 4383 NH1 ARG B 146 -66.087 16.661 62.534 1.00167.67 N ANISOU 4383 NH1 ARG B 146 21729 24867 17112 741 1528 -1294 N ATOM 4384 NH2 ARG B 146 -65.281 15.066 63.966 1.00163.96 N ANISOU 4384 NH2 ARG B 146 21312 24701 16286 431 1552 -861 N ATOM 4385 N PRO B 147 -61.729 20.164 58.532 1.00109.15 N ANISOU 4385 N PRO B 147 15031 15471 10972 638 548 -1628 N ATOM 4386 CA PRO B 147 -62.376 20.930 57.445 1.00107.29 C ANISOU 4386 CA PRO B 147 14834 14979 10952 727 508 -1742 C ATOM 4387 C PRO B 147 -62.757 20.012 56.266 1.00105.03 C ANISOU 4387 C PRO B 147 14384 14643 10878 639 644 -1500 C ATOM 4388 O PRO B 147 -63.028 20.484 55.160 1.00103.40 O ANISOU 4388 O PRO B 147 14204 14201 10881 651 592 -1521 O ATOM 4389 CB PRO B 147 -61.306 21.961 57.065 1.00109.42 C ANISOU 4389 CB PRO B 147 15310 14924 11342 613 244 -1825 C ATOM 4390 CG PRO B 147 -59.985 21.357 57.520 1.00113.82 C ANISOU 4390 CG PRO B 147 15840 15577 11830 405 189 -1658 C ATOM 4391 CD PRO B 147 -60.264 20.127 58.352 1.00109.62 C ANISOU 4391 CD PRO B 147 15155 15385 11111 437 381 -1513 C ATOM 4392 N ARG B 148 -62.784 18.682 56.522 1.00 98.42 N ANISOU 4392 N ARG B 148 13402 14019 9975 546 798 -1267 N ATOM 4393 CA ARG B 148 -63.110 17.605 55.583 1.00 94.98 C ANISOU 4393 CA ARG B 148 12827 13557 9704 451 917 -1031 C ATOM 4394 C ARG B 148 -64.611 17.482 55.351 1.00 98.89 C ANISOU 4394 C ARG B 148 13193 14189 10194 563 1082 -1074 C ATOM 4395 O ARG B 148 -65.023 17.084 54.257 1.00 96.52 O ANISOU 4395 O ARG B 148 12811 13775 10087 519 1130 -968 O ATOM 4396 CB ARG B 148 -62.554 16.268 56.086 1.00 92.43 C ANISOU 4396 CB ARG B 148 12452 13376 9292 320 969 -781 C ATOM 4397 CG ARG B 148 -61.040 16.168 56.041 1.00 94.94 C ANISOU 4397 CG ARG B 148 12837 13579 9657 216 809 -704 C ATOM 4398 CD ARG B 148 -60.525 15.104 56.986 1.00 98.64 C ANISOU 4398 CD ARG B 148 13301 14227 9951 161 817 -528 C ATOM 4399 NE ARG B 148 -60.617 13.754 56.424 1.00100.94 N ANISOU 4399 NE ARG B 148 13527 14477 10347 93 877 -281 N ATOM 4400 CZ ARG B 148 -61.060 12.691 57.089 1.00116.44 C ANISOU 4400 CZ ARG B 148 15487 16588 12168 49 956 -101 C ATOM 4401 NH1 ARG B 148 -61.468 12.805 58.347 1.00107.80 N ANISOU 4401 NH1 ARG B 148 14416 15746 10797 60 1012 -129 N ATOM 4402 NH2 ARG B 148 -61.101 11.504 56.496 1.00100.74 N ANISOU 4402 NH2 ARG B 148 13484 14494 10299 -16 965 111 N ATOM 4403 N LYS B 149 -65.425 17.804 56.392 1.00 97.84 N ANISOU 4403 N LYS B 149 13019 14341 9816 708 1168 -1237 N ATOM 4404 CA LYS B 149 -66.892 17.804 56.340 1.00 98.76 C ANISOU 4404 CA LYS B 149 12966 14688 9868 839 1327 -1323 C ATOM 4405 C LYS B 149 -67.346 18.796 55.268 1.00102.15 C ANISOU 4405 C LYS B 149 13433 14864 10515 998 1235 -1501 C ATOM 4406 O LYS B 149 -68.227 18.471 54.473 1.00101.30 O ANISOU 4406 O LYS B 149 13180 14787 10522 1010 1328 -1444 O ATOM 4407 CB LYS B 149 -67.494 18.182 57.710 1.00104.81 C ANISOU 4407 CB LYS B 149 13684 15845 10295 1001 1408 -1524 C ATOM 4408 CG LYS B 149 -67.593 17.028 58.722 1.00120.59 C ANISOU 4408 CG LYS B 149 15573 18215 12029 833 1563 -1306 C ATOM 4409 CD LYS B 149 -68.884 16.197 58.584 1.00129.22 C ANISOU 4409 CD LYS B 149 16417 19631 13051 758 1778 -1168 C ATOM 4410 CE LYS B 149 -70.039 16.697 59.422 1.00139.69 C ANISOU 4410 CE LYS B 149 17560 21443 14072 953 1920 -1404 C ATOM 4411 NZ LYS B 149 -71.323 16.054 59.024 1.00146.83 N ANISOU 4411 NZ LYS B 149 18188 22645 14955 874 2108 -1293 N ATOM 4412 N LEU B 150 -66.684 19.975 55.211 1.00 98.92 N ANISOU 4412 N LEU B 150 13238 14180 10166 1090 1027 -1694 N ATOM 4413 CA LEU B 150 -66.920 21.029 54.224 1.00 98.45 C ANISOU 4413 CA LEU B 150 13293 13804 10308 1217 874 -1845 C ATOM 4414 C LEU B 150 -66.671 20.506 52.810 1.00 98.45 C ANISOU 4414 C LEU B 150 13252 13578 10577 1032 871 -1608 C ATOM 4415 O LEU B 150 -67.494 20.737 51.925 1.00 97.91 O ANISOU 4415 O LEU B 150 13126 13435 10640 1131 878 -1642 O ATOM 4416 CB LEU B 150 -65.988 22.224 54.494 1.00 99.86 C ANISOU 4416 CB LEU B 150 13756 13695 10491 1242 618 -2022 C ATOM 4417 CG LEU B 150 -66.644 23.586 54.711 1.00107.81 C ANISOU 4417 CG LEU B 150 14924 14584 11454 1554 462 -2375 C ATOM 4418 CD1 LEU B 150 -65.656 24.564 55.315 1.00109.94 C ANISOU 4418 CD1 LEU B 150 15487 14621 11664 1531 212 -2538 C ATOM 4419 CD2 LEU B 150 -67.216 24.151 53.417 1.00109.34 C ANISOU 4419 CD2 LEU B 150 15168 14491 11884 1646 362 -2396 C ATOM 4420 N LEU B 151 -65.551 19.778 52.615 1.00 92.34 N ANISOU 4420 N LEU B 151 12492 12728 9864 787 857 -1381 N ATOM 4421 CA LEU B 151 -65.154 19.206 51.327 1.00 89.25 C ANISOU 4421 CA LEU B 151 12055 12163 9693 616 852 -1171 C ATOM 4422 C LEU B 151 -66.146 18.179 50.777 1.00 91.52 C ANISOU 4422 C LEU B 151 12144 12591 10039 606 1030 -1037 C ATOM 4423 O LEU B 151 -66.628 18.344 49.654 1.00 89.70 O ANISOU 4423 O LEU B 151 11880 12228 9974 625 1015 -1026 O ATOM 4424 CB LEU B 151 -63.751 18.569 51.401 1.00 87.81 C ANISOU 4424 CB LEU B 151 11897 11950 9518 409 803 -995 C ATOM 4425 CG LEU B 151 -62.517 19.462 51.429 1.00 92.23 C ANISOU 4425 CG LEU B 151 12618 12333 10091 312 600 -1052 C ATOM 4426 CD1 LEU B 151 -61.290 18.611 51.539 1.00 91.08 C ANISOU 4426 CD1 LEU B 151 12415 12263 9928 145 588 -877 C ATOM 4427 CD2 LEU B 151 -62.399 20.314 50.171 1.00 93.61 C ANISOU 4427 CD2 LEU B 151 12883 12235 10452 253 466 -1067 C ATOM 4428 N ALA B 152 -66.433 17.120 51.562 1.00 88.37 N ANISOU 4428 N ALA B 152 11627 12455 9494 551 1181 -922 N ATOM 4429 CA ALA B 152 -67.314 16.016 51.183 1.00 87.69 C ANISOU 4429 CA ALA B 152 11369 12511 9438 476 1334 -765 C ATOM 4430 C ALA B 152 -68.813 16.365 51.130 1.00 93.07 C ANISOU 4430 C ALA B 152 11897 13392 10073 627 1437 -899 C ATOM 4431 O ALA B 152 -69.551 15.750 50.350 1.00 91.84 O ANISOU 4431 O ALA B 152 11607 13268 10019 563 1513 -798 O ATOM 4432 CB ALA B 152 -67.079 14.829 52.102 1.00 88.95 C ANISOU 4432 CB ALA B 152 11496 12861 9439 334 1421 -577 C ATOM 4433 N GLU B 153 -69.262 17.338 51.950 1.00 91.85 N ANISOU 4433 N GLU B 153 11753 13389 9756 838 1429 -1143 N ATOM 4434 CA GLU B 153 -70.676 17.724 52.001 1.00 93.71 C ANISOU 4434 CA GLU B 153 11810 13883 9912 1037 1522 -1313 C ATOM 4435 C GLU B 153 -71.045 18.970 51.192 1.00 98.19 C ANISOU 4435 C GLU B 153 12455 14223 10628 1281 1374 -1537 C ATOM 4436 O GLU B 153 -72.191 19.075 50.759 1.00 98.92 O ANISOU 4436 O GLU B 153 12374 14470 10739 1420 1433 -1619 O ATOM 4437 CB GLU B 153 -71.180 17.844 53.450 1.00 98.09 C ANISOU 4437 CB GLU B 153 12269 14857 10145 1154 1634 -1456 C ATOM 4438 CG GLU B 153 -71.174 16.534 54.220 1.00108.39 C ANISOU 4438 CG GLU B 153 13459 16455 11268 899 1796 -1203 C ATOM 4439 CD GLU B 153 -71.822 16.598 55.590 1.00135.18 C ANISOU 4439 CD GLU B 153 16712 20346 14303 986 1933 -1321 C ATOM 4440 OE1 GLU B 153 -72.790 15.839 55.822 1.00136.64 O ANISOU 4440 OE1 GLU B 153 16655 20921 14342 868 2112 -1203 O ATOM 4441 OE2 GLU B 153 -71.368 17.407 56.431 1.00129.99 O ANISOU 4441 OE2 GLU B 153 16182 19714 13495 1157 1858 -1531 O ATOM 4442 N LYS B 154 -70.109 19.921 51.007 1.00 94.19 N ANISOU 4442 N LYS B 154 12211 13362 10215 1326 1167 -1632 N ATOM 4443 CA LYS B 154 -70.417 21.158 50.280 1.00 94.53 C ANISOU 4443 CA LYS B 154 12391 13136 10390 1544 981 -1827 C ATOM 4444 C LYS B 154 -69.494 21.718 49.182 1.00 96.19 C ANISOU 4444 C LYS B 154 12835 12887 10827 1416 770 -1739 C ATOM 4445 O LYS B 154 -69.979 22.457 48.320 1.00 96.77 O ANISOU 4445 O LYS B 154 12981 12759 11029 1552 641 -1820 O ATOM 4446 CB LYS B 154 -70.492 22.373 51.236 1.00 99.87 C ANISOU 4446 CB LYS B 154 13230 13802 10912 1829 847 -2153 C ATOM 4447 CG LYS B 154 -71.464 22.233 52.421 1.00115.68 C ANISOU 4447 CG LYS B 154 15021 16296 12636 2048 1018 -2343 C ATOM 4448 CD LYS B 154 -72.914 22.566 52.061 1.00127.44 C ANISOU 4448 CD LYS B 154 16308 17999 14114 2352 1063 -2529 C ATOM 4449 CE LYS B 154 -73.823 22.558 53.267 1.00141.60 C ANISOU 4449 CE LYS B 154 17871 20338 15591 2587 1224 -2753 C ATOM 4450 NZ LYS B 154 -75.188 23.054 52.936 1.00151.96 N ANISOU 4450 NZ LYS B 154 18977 21880 16879 2945 1234 -2992 N ATOM 4451 N VAL B 155 -68.176 21.375 49.219 1.00 90.11 N ANISOU 4451 N VAL B 155 12171 11982 10085 1154 729 -1570 N ATOM 4452 CA VAL B 155 -67.139 21.858 48.283 1.00 88.33 C ANISOU 4452 CA VAL B 155 12134 11405 10024 973 543 -1466 C ATOM 4453 C VAL B 155 -67.235 20.985 47.016 1.00 89.66 C ANISOU 4453 C VAL B 155 12156 11562 10350 818 632 -1243 C ATOM 4454 O VAL B 155 -67.253 21.534 45.916 1.00 88.45 O ANISOU 4454 O VAL B 155 12088 11182 10336 795 508 -1214 O ATOM 4455 CB VAL B 155 -65.687 21.946 48.851 1.00 91.71 C ANISOU 4455 CB VAL B 155 12699 11756 10393 772 449 -1409 C ATOM 4456 CG1 VAL B 155 -64.708 22.481 47.806 1.00 90.71 C ANISOU 4456 CG1 VAL B 155 12721 11334 10411 555 265 -1294 C ATOM 4457 CG2 VAL B 155 -65.628 22.812 50.106 1.00 94.09 C ANISOU 4457 CG2 VAL B 155 13157 12066 10525 926 346 -1650 C ATOM 4458 N VAL B 156 -67.356 19.649 47.182 1.00 85.44 N ANISOU 4458 N VAL B 156 11421 11262 9782 719 827 -1093 N ATOM 4459 CA VAL B 156 -67.485 18.647 46.109 1.00 83.46 C ANISOU 4459 CA VAL B 156 11032 11019 9658 584 914 -903 C ATOM 4460 C VAL B 156 -68.450 19.048 44.944 1.00 89.18 C ANISOU 4460 C VAL B 156 11716 11653 10514 681 877 -937 C ATOM 4461 O VAL B 156 -68.228 18.651 43.795 1.00 87.79 O ANISOU 4461 O VAL B 156 11513 11381 10464 556 863 -804 O ATOM 4462 CB VAL B 156 -67.752 17.221 46.682 1.00 86.39 C ANISOU 4462 CB VAL B 156 11235 11642 9949 501 1100 -773 C ATOM 4463 CG1 VAL B 156 -69.162 17.086 47.250 1.00 87.75 C ANISOU 4463 CG1 VAL B 156 11248 12079 10014 636 1233 -861 C ATOM 4464 CG2 VAL B 156 -67.463 16.128 45.656 1.00 84.19 C ANISOU 4464 CG2 VAL B 156 10884 11305 9799 337 1136 -581 C ATOM 4465 N TYR B 157 -69.486 19.853 45.243 1.00 87.83 N ANISOU 4465 N TYR B 157 11542 11530 10300 924 848 -1131 N ATOM 4466 CA TYR B 157 -70.455 20.309 44.246 1.00 88.06 C ANISOU 4466 CA TYR B 157 11531 11491 10436 1064 789 -1185 C ATOM 4467 C TYR B 157 -69.915 21.532 43.506 1.00 92.12 C ANISOU 4467 C TYR B 157 12308 11642 11051 1079 540 -1219 C ATOM 4468 O TYR B 157 -69.833 21.523 42.278 1.00 90.22 O ANISOU 4468 O TYR B 157 12089 11258 10934 976 476 -1097 O ATOM 4469 CB TYR B 157 -71.820 20.598 44.915 1.00 91.54 C ANISOU 4469 CB TYR B 157 11823 12192 10768 1352 857 -1393 C ATOM 4470 CG TYR B 157 -72.449 19.376 45.555 1.00 92.76 C ANISOU 4470 CG TYR B 157 11701 12740 10805 1274 1100 -1320 C ATOM 4471 CD1 TYR B 157 -72.205 19.058 46.887 1.00 95.41 C ANISOU 4471 CD1 TYR B 157 12008 13291 10952 1250 1206 -1346 C ATOM 4472 CD2 TYR B 157 -73.261 18.519 44.818 1.00 92.79 C ANISOU 4472 CD2 TYR B 157 11487 12895 10872 1188 1208 -1204 C ATOM 4473 CE1 TYR B 157 -72.746 17.912 47.469 1.00 96.16 C ANISOU 4473 CE1 TYR B 157 11878 13738 10922 1123 1411 -1234 C ATOM 4474 CE2 TYR B 157 -73.815 17.376 45.391 1.00 93.89 C ANISOU 4474 CE2 TYR B 157 11401 13373 10900 1053 1406 -1104 C ATOM 4475 CZ TYR B 157 -73.555 17.075 46.717 1.00101.10 C ANISOU 4475 CZ TYR B 157 12302 14490 11621 1012 1506 -1107 C ATOM 4476 OH TYR B 157 -74.107 15.952 47.283 1.00102.17 O ANISOU 4476 OH TYR B 157 12238 14954 11628 837 1682 -973 O ATOM 4477 N VAL B 158 -69.504 22.555 44.273 1.00 91.00 N ANISOU 4477 N VAL B 158 12381 11353 10840 1178 391 -1373 N ATOM 4478 CA VAL B 158 -68.954 23.838 43.818 1.00 92.21 C ANISOU 4478 CA VAL B 158 12846 11128 11060 1169 111 -1414 C ATOM 4479 C VAL B 158 -67.639 23.641 43.045 1.00 94.30 C ANISOU 4479 C VAL B 158 13192 11242 11395 807 55 -1176 C ATOM 4480 O VAL B 158 -67.408 24.323 42.044 1.00 94.58 O ANISOU 4480 O VAL B 158 13392 11026 11519 712 -126 -1096 O ATOM 4481 CB VAL B 158 -68.788 24.814 45.030 1.00 98.72 C ANISOU 4481 CB VAL B 158 13881 11860 11769 1343 -29 -1653 C ATOM 4482 CG1 VAL B 158 -68.053 26.102 44.649 1.00100.07 C ANISOU 4482 CG1 VAL B 158 14424 11593 12004 1257 -353 -1668 C ATOM 4483 CG2 VAL B 158 -70.139 25.134 45.675 1.00100.89 C ANISOU 4483 CG2 VAL B 158 14061 12316 11955 1750 8 -1926 C ATOM 4484 N GLY B 159 -66.812 22.708 43.514 1.00 88.93 N ANISOU 4484 N GLY B 159 12388 10745 10656 619 203 -1066 N ATOM 4485 CA GLY B 159 -65.501 22.423 42.943 1.00 87.39 C ANISOU 4485 CA GLY B 159 12210 10506 10489 309 172 -873 C ATOM 4486 C GLY B 159 -65.429 21.356 41.873 1.00 89.42 C ANISOU 4486 C GLY B 159 12271 10885 10818 178 304 -692 C ATOM 4487 O GLY B 159 -64.545 21.423 41.016 1.00 88.83 O ANISOU 4487 O GLY B 159 12223 10755 10774 -40 235 -555 O ATOM 4488 N VAL B 160 -66.310 20.339 41.929 1.00 84.80 N ANISOU 4488 N VAL B 160 11485 10491 10244 290 488 -691 N ATOM 4489 CA VAL B 160 -66.275 19.242 40.959 1.00 82.81 C ANISOU 4489 CA VAL B 160 11068 10338 10058 180 597 -545 C ATOM 4490 C VAL B 160 -67.476 19.186 40.013 1.00 86.70 C ANISOU 4490 C VAL B 160 11482 10822 10636 282 614 -551 C ATOM 4491 O VAL B 160 -67.280 19.284 38.801 1.00 86.32 O ANISOU 4491 O VAL B 160 11450 10694 10654 184 550 -461 O ATOM 4492 CB VAL B 160 -65.913 17.871 41.606 1.00 85.66 C ANISOU 4492 CB VAL B 160 11285 10896 10368 126 758 -477 C ATOM 4493 CG1 VAL B 160 -66.121 16.698 40.645 1.00 84.06 C ANISOU 4493 CG1 VAL B 160 10939 10763 10239 64 848 -368 C ATOM 4494 CG2 VAL B 160 -64.486 17.880 42.135 1.00 85.48 C ANISOU 4494 CG2 VAL B 160 11319 10884 10274 -3 708 -436 C ATOM 4495 N TRP B 161 -68.698 19.012 40.553 1.00 83.06 N ANISOU 4495 N TRP B 161 10917 10487 10157 467 703 -654 N ATOM 4496 CA TRP B 161 -69.925 18.872 39.767 1.00 82.69 C ANISOU 4496 CA TRP B 161 10748 10493 10176 571 727 -672 C ATOM 4497 C TRP B 161 -70.356 20.078 38.938 1.00 87.74 C ANISOU 4497 C TRP B 161 11522 10936 10880 691 540 -730 C ATOM 4498 O TRP B 161 -70.709 19.892 37.772 1.00 87.17 O ANISOU 4498 O TRP B 161 11397 10841 10882 652 514 -654 O ATOM 4499 CB TRP B 161 -71.076 18.323 40.612 1.00 82.13 C ANISOU 4499 CB TRP B 161 10485 10683 10037 704 879 -758 C ATOM 4500 CG TRP B 161 -70.931 16.869 40.933 1.00 81.72 C ANISOU 4500 CG TRP B 161 10293 10802 9956 535 1044 -632 C ATOM 4501 CD1 TRP B 161 -70.581 16.327 42.132 1.00 84.79 C ANISOU 4501 CD1 TRP B 161 10666 11317 10232 485 1140 -613 C ATOM 4502 CD2 TRP B 161 -71.104 15.771 40.030 1.00 80.18 C ANISOU 4502 CD2 TRP B 161 9991 10636 9839 393 1100 -504 C ATOM 4503 NE1 TRP B 161 -70.535 14.957 42.037 1.00 83.39 N ANISOU 4503 NE1 TRP B 161 10396 11222 10066 320 1238 -467 N ATOM 4504 CE2 TRP B 161 -70.858 14.587 40.758 1.00 83.92 C ANISOU 4504 CE2 TRP B 161 10410 11223 10254 264 1214 -411 C ATOM 4505 CE3 TRP B 161 -71.464 15.670 38.676 1.00 80.57 C ANISOU 4505 CE3 TRP B 161 9999 10620 9993 364 1049 -464 C ATOM 4506 CZ2 TRP B 161 -70.948 13.316 40.176 1.00 82.42 C ANISOU 4506 CZ2 TRP B 161 10152 11045 10120 115 1258 -290 C ATOM 4507 CZ3 TRP B 161 -71.564 14.411 38.103 1.00 81.09 C ANISOU 4507 CZ3 TRP B 161 9973 10735 10105 219 1113 -360 C ATOM 4508 CH2 TRP B 161 -71.302 13.252 38.847 1.00 81.46 C ANISOU 4508 CH2 TRP B 161 9991 10857 10105 99 1207 -280 C ATOM 4509 N ILE B 162 -70.347 21.296 39.514 1.00 85.53 N ANISOU 4509 N ILE B 162 11432 10498 10566 843 388 -867 N ATOM 4510 CA ILE B 162 -70.717 22.502 38.762 1.00 86.89 C ANISOU 4510 CA ILE B 162 11794 10420 10801 968 156 -915 C ATOM 4511 C ILE B 162 -69.691 22.797 37.645 1.00 90.13 C ANISOU 4511 C ILE B 162 12368 10618 11261 695 22 -722 C ATOM 4512 O ILE B 162 -70.130 22.938 36.504 1.00 89.97 O ANISOU 4512 O ILE B 162 12350 10534 11300 695 -55 -648 O ATOM 4513 CB ILE B 162 -71.082 23.729 39.652 1.00 92.93 C ANISOU 4513 CB ILE B 162 12752 11039 11518 1244 -10 -1142 C ATOM 4514 CG1 ILE B 162 -72.169 23.401 40.724 1.00 94.90 C ANISOU 4514 CG1 ILE B 162 12779 11601 11675 1526 150 -1348 C ATOM 4515 CG2 ILE B 162 -71.454 24.966 38.822 1.00 95.69 C ANISOU 4515 CG2 ILE B 162 13349 11068 11942 1386 -298 -1180 C ATOM 4516 CD1 ILE B 162 -73.569 22.773 40.231 1.00102.09 C ANISOU 4516 CD1 ILE B 162 13383 12798 12609 1679 279 -1375 C ATOM 4517 N PRO B 163 -68.346 22.797 37.892 1.00 86.01 N ANISOU 4517 N PRO B 163 11940 10044 10695 447 6 -625 N ATOM 4518 CA PRO B 163 -67.396 23.032 36.788 1.00 85.35 C ANISOU 4518 CA PRO B 163 11955 9853 10623 163 -100 -434 C ATOM 4519 C PRO B 163 -67.456 21.991 35.670 1.00 87.12 C ANISOU 4519 C PRO B 163 11968 10261 10874 52 35 -302 C ATOM 4520 O PRO B 163 -67.263 22.349 34.506 1.00 86.92 O ANISOU 4520 O PRO B 163 12012 10158 10855 -83 -73 -177 O ATOM 4521 CB PRO B 163 -66.031 23.022 37.488 1.00 86.83 C ANISOU 4521 CB PRO B 163 12192 10065 10735 -54 -96 -390 C ATOM 4522 CG PRO B 163 -66.331 23.365 38.895 1.00 92.42 C ANISOU 4522 CG PRO B 163 12970 10741 11404 144 -101 -578 C ATOM 4523 CD PRO B 163 -67.612 22.646 39.165 1.00 87.48 C ANISOU 4523 CD PRO B 163 12139 10299 10799 404 70 -685 C ATOM 4524 N ALA B 164 -67.759 20.717 36.011 1.00 81.90 N ANISOU 4524 N ALA B 164 11069 9834 10216 106 254 -330 N ATOM 4525 CA ALA B 164 -67.873 19.623 35.045 1.00 80.27 C ANISOU 4525 CA ALA B 164 10678 9786 10036 28 370 -242 C ATOM 4526 C ALA B 164 -68.996 19.899 34.055 1.00 85.80 C ANISOU 4526 C ALA B 164 11363 10441 10795 137 301 -246 C ATOM 4527 O ALA B 164 -68.841 19.613 32.867 1.00 85.54 O ANISOU 4527 O ALA B 164 11291 10447 10766 20 286 -145 O ATOM 4528 CB ALA B 164 -68.116 18.306 35.760 1.00 79.72 C ANISOU 4528 CB ALA B 164 10420 9907 9964 74 567 -280 C ATOM 4529 N LEU B 165 -70.099 20.509 34.537 1.00 83.73 N ANISOU 4529 N LEU B 165 11131 10122 10563 376 245 -375 N ATOM 4530 CA LEU B 165 -71.248 20.884 33.715 1.00 84.36 C ANISOU 4530 CA LEU B 165 11190 10170 10695 533 152 -404 C ATOM 4531 C LEU B 165 -70.922 22.112 32.875 1.00 88.20 C ANISOU 4531 C LEU B 165 11936 10393 11184 484 -99 -322 C ATOM 4532 O LEU B 165 -71.190 22.110 31.679 1.00 87.67 O ANISOU 4532 O LEU B 165 11860 10319 11131 433 -167 -227 O ATOM 4533 CB LEU B 165 -72.498 21.117 34.581 1.00 86.05 C ANISOU 4533 CB LEU B 165 11313 10468 10915 836 174 -593 C ATOM 4534 CG LEU B 165 -73.064 19.876 35.280 1.00 90.29 C ANISOU 4534 CG LEU B 165 11572 11306 11429 847 413 -640 C ATOM 4535 CD1 LEU B 165 -73.857 20.260 36.517 1.00 92.53 C ANISOU 4535 CD1 LEU B 165 11789 11713 11653 1098 451 -828 C ATOM 4536 CD2 LEU B 165 -73.910 19.030 34.324 1.00 92.57 C ANISOU 4536 CD2 LEU B 165 11653 11756 11764 813 478 -591 C ATOM 4537 N LEU B 166 -70.293 23.137 33.482 1.00 85.33 N ANISOU 4537 N LEU B 166 11820 9808 10795 467 -251 -343 N ATOM 4538 CA LEU B 166 -69.898 24.361 32.775 1.00 86.95 C ANISOU 4538 CA LEU B 166 12328 9715 10994 365 -527 -237 C ATOM 4539 C LEU B 166 -68.935 24.043 31.624 1.00 90.27 C ANISOU 4539 C LEU B 166 12732 10206 11359 14 -515 -6 C ATOM 4540 O LEU B 166 -68.971 24.706 30.588 1.00 91.03 O ANISOU 4540 O LEU B 166 12986 10160 11439 -80 -701 127 O ATOM 4541 CB LEU B 166 -69.279 25.396 33.738 1.00 88.60 C ANISOU 4541 CB LEU B 166 12815 9672 11179 357 -694 -302 C ATOM 4542 CG LEU B 166 -70.162 25.916 34.884 1.00 94.65 C ANISOU 4542 CG LEU B 166 13639 10358 11966 734 -748 -563 C ATOM 4543 CD1 LEU B 166 -69.315 26.532 35.973 1.00 95.86 C ANISOU 4543 CD1 LEU B 166 13999 10353 12071 668 -835 -636 C ATOM 4544 CD2 LEU B 166 -71.208 26.914 34.394 1.00 99.12 C ANISOU 4544 CD2 LEU B 166 14389 10686 12587 1025 -1006 -647 C ATOM 4545 N LEU B 167 -68.118 22.988 31.795 1.00 85.33 N ANISOU 4545 N LEU B 167 11904 9828 10689 -159 -300 34 N ATOM 4546 CA LEU B 167 -67.150 22.501 30.812 1.00 84.65 C ANISOU 4546 CA LEU B 167 11732 9909 10522 -451 -245 204 C ATOM 4547 C LEU B 167 -67.815 21.707 29.673 1.00 89.63 C ANISOU 4547 C LEU B 167 12185 10707 11163 -410 -164 235 C ATOM 4548 O LEU B 167 -67.129 21.246 28.753 1.00 88.97 O ANISOU 4548 O LEU B 167 12011 10799 10995 -611 -115 347 O ATOM 4549 CB LEU B 167 -66.098 21.637 31.529 1.00 82.87 C ANISOU 4549 CB LEU B 167 11349 9889 10247 -567 -65 186 C ATOM 4550 CG LEU B 167 -64.666 22.188 31.699 1.00 87.78 C ANISOU 4550 CG LEU B 167 12068 10517 10770 -854 -142 293 C ATOM 4551 CD1 LEU B 167 -64.596 23.717 31.675 1.00 90.06 C ANISOU 4551 CD1 LEU B 167 12679 10492 11047 -961 -415 365 C ATOM 4552 CD2 LEU B 167 -64.041 21.646 32.958 1.00 88.71 C ANISOU 4552 CD2 LEU B 167 12093 10737 10876 -824 -19 199 C ATOM 4553 N THR B 168 -69.151 21.578 29.721 1.00 87.29 N ANISOU 4553 N THR B 168 11830 10383 10954 -150 -159 124 N ATOM 4554 CA THR B 168 -69.912 20.843 28.715 1.00 86.57 C ANISOU 4554 CA THR B 168 11572 10442 10878 -103 -101 133 C ATOM 4555 C THR B 168 -70.593 21.734 27.644 1.00 91.28 C ANISOU 4555 C THR B 168 12309 10901 11472 -56 -317 210 C ATOM 4556 O THR B 168 -71.148 21.206 26.677 1.00 90.43 O ANISOU 4556 O THR B 168 12077 10926 11357 -44 -295 233 O ATOM 4557 CB THR B 168 -70.728 19.720 29.382 1.00 92.98 C ANISOU 4557 CB THR B 168 12151 11417 11759 63 90 -11 C ATOM 4558 OG1 THR B 168 -70.588 18.539 28.607 1.00 91.98 O ANISOU 4558 OG1 THR B 168 11854 11482 11612 -44 209 21 O ATOM 4559 CG2 THR B 168 -72.202 20.074 29.614 1.00 91.29 C ANISOU 4559 CG2 THR B 168 11895 11176 11617 334 33 -129 C ATOM 4560 N ILE B 169 -70.519 23.077 27.813 1.00 89.45 N ANISOU 4560 N ILE B 169 12359 10388 11240 -33 -549 252 N ATOM 4561 CA ILE B 169 -71.052 24.081 26.880 1.00 91.71 C ANISOU 4561 CA ILE B 169 12855 10473 11517 10 -814 350 C ATOM 4562 C ILE B 169 -70.432 23.915 25.459 1.00 96.41 C ANISOU 4562 C ILE B 169 13448 11194 11987 -291 -839 568 C ATOM 4563 O ILE B 169 -71.213 23.839 24.509 1.00 96.95 O ANISOU 4563 O ILE B 169 13476 11311 12050 -210 -907 600 O ATOM 4564 CB ILE B 169 -70.997 25.534 27.458 1.00 97.39 C ANISOU 4564 CB ILE B 169 13933 10810 12263 90 -1091 343 C ATOM 4565 CG1 ILE B 169 -71.784 25.634 28.792 1.00 98.14 C ANISOU 4565 CG1 ILE B 169 13985 10852 12453 454 -1054 81 C ATOM 4566 CG2 ILE B 169 -71.511 26.573 26.441 1.00100.74 C ANISOU 4566 CG2 ILE B 169 14622 10980 12674 131 -1410 470 C ATOM 4567 CD1 ILE B 169 -71.394 26.820 29.742 1.00108.12 C ANISOU 4567 CD1 ILE B 169 15577 11775 13729 514 -1266 13 C ATOM 4568 N PRO B 170 -69.087 23.739 25.269 1.00 92.39 N ANISOU 4568 N PRO B 170 12932 10810 11360 -625 -766 702 N ATOM 4569 CA PRO B 170 -68.561 23.502 23.904 1.00 92.57 C ANISOU 4569 CA PRO B 170 12900 11045 11228 -888 -763 883 C ATOM 4570 C PRO B 170 -68.982 22.150 23.304 1.00 94.46 C ANISOU 4570 C PRO B 170 12834 11596 11460 -800 -556 786 C ATOM 4571 O PRO B 170 -68.893 21.960 22.094 1.00 94.51 O ANISOU 4571 O PRO B 170 12793 11774 11342 -931 -575 892 O ATOM 4572 CB PRO B 170 -67.039 23.571 24.092 1.00 94.47 C ANISOU 4572 CB PRO B 170 13143 11410 11340 -1223 -705 997 C ATOM 4573 CG PRO B 170 -66.832 24.234 25.417 1.00 99.24 C ANISOU 4573 CG PRO B 170 13917 11752 12038 -1166 -777 925 C ATOM 4574 CD PRO B 170 -67.979 23.774 26.244 1.00 93.37 C ANISOU 4574 CD PRO B 170 13077 10936 11462 -778 -690 692 C ATOM 4575 N ASP B 171 -69.438 21.210 24.150 1.00 89.33 N ANISOU 4575 N ASP B 171 11994 11017 10930 -594 -373 590 N ATOM 4576 CA ASP B 171 -69.930 19.897 23.725 1.00 87.50 C ANISOU 4576 CA ASP B 171 11511 11018 10716 -510 -208 482 C ATOM 4577 C ASP B 171 -71.434 19.982 23.425 1.00 89.39 C ANISOU 4577 C ASP B 171 11722 11194 11049 -281 -295 413 C ATOM 4578 O ASP B 171 -71.948 19.175 22.654 1.00 88.62 O ANISOU 4578 O ASP B 171 11470 11266 10937 -261 -243 373 O ATOM 4579 CB ASP B 171 -69.603 18.816 24.767 1.00 87.97 C ANISOU 4579 CB ASP B 171 11405 11178 10840 -456 5 342 C ATOM 4580 CG ASP B 171 -68.110 18.628 24.986 1.00102.91 C ANISOU 4580 CG ASP B 171 13282 13188 12629 -652 86 393 C ATOM 4581 OD1 ASP B 171 -67.529 17.712 24.363 1.00104.05 O ANISOU 4581 OD1 ASP B 171 13280 13570 12686 -729 190 376 O ATOM 4582 OD2 ASP B 171 -67.520 19.404 25.780 1.00109.62 O ANISOU 4582 OD2 ASP B 171 14263 13908 13479 -717 34 436 O ATOM 4583 N PHE B 172 -72.123 20.988 24.004 1.00 84.99 N ANISOU 4583 N PHE B 172 11314 10402 10576 -99 -447 385 N ATOM 4584 CA PHE B 172 -73.537 21.258 23.751 1.00 85.03 C ANISOU 4584 CA PHE B 172 11287 10366 10655 154 -564 311 C ATOM 4585 C PHE B 172 -73.648 21.953 22.391 1.00 88.79 C ANISOU 4585 C PHE B 172 11915 10783 11038 78 -782 477 C ATOM 4586 O PHE B 172 -74.553 21.652 21.616 1.00 89.45 O ANISOU 4586 O PHE B 172 11884 10979 11122 179 -826 452 O ATOM 4587 CB PHE B 172 -74.120 22.204 24.824 1.00 88.24 C ANISOU 4587 CB PHE B 172 11819 10551 11156 414 -680 203 C ATOM 4588 CG PHE B 172 -74.833 21.596 26.009 1.00 89.17 C ANISOU 4588 CG PHE B 172 11724 10794 11365 621 -510 0 C ATOM 4589 CD1 PHE B 172 -74.620 22.085 27.293 1.00 92.66 C ANISOU 4589 CD1 PHE B 172 12255 11114 11839 730 -499 -98 C ATOM 4590 CD2 PHE B 172 -75.775 20.587 25.835 1.00 90.95 C ANISOU 4590 CD2 PHE B 172 11662 11269 11624 696 -380 -91 C ATOM 4591 CE1 PHE B 172 -75.307 21.550 28.388 1.00 93.19 C ANISOU 4591 CE1 PHE B 172 12113 11344 11952 909 -338 -274 C ATOM 4592 CE2 PHE B 172 -76.449 20.041 26.935 1.00 93.61 C ANISOU 4592 CE2 PHE B 172 11794 11757 12016 838 -226 -249 C ATOM 4593 CZ PHE B 172 -76.212 20.529 28.202 1.00 91.88 C ANISOU 4593 CZ PHE B 172 11653 11448 11808 946 -199 -335 C ATOM 4594 N ILE B 173 -72.718 22.884 22.111 1.00 84.48 N ANISOU 4594 N ILE B 173 11630 10071 10397 -127 -931 658 N ATOM 4595 CA ILE B 173 -72.680 23.696 20.898 1.00 85.75 C ANISOU 4595 CA ILE B 173 11996 10144 10440 -256 -1169 868 C ATOM 4596 C ILE B 173 -72.184 22.928 19.655 1.00 87.79 C ANISOU 4596 C ILE B 173 12108 10720 10529 -503 -1065 976 C ATOM 4597 O ILE B 173 -72.883 22.888 18.638 1.00 88.18 O ANISOU 4597 O ILE B 173 12133 10847 10526 -452 -1165 1019 O ATOM 4598 CB ILE B 173 -71.872 25.020 21.157 1.00 90.76 C ANISOU 4598 CB ILE B 173 12994 10463 11029 -429 -1391 1040 C ATOM 4599 CG1 ILE B 173 -72.381 25.839 22.387 1.00 92.00 C ANISOU 4599 CG1 ILE B 173 13331 10283 11343 -142 -1528 894 C ATOM 4600 CG2 ILE B 173 -71.708 25.889 19.901 1.00 94.23 C ANISOU 4600 CG2 ILE B 173 13688 10800 11316 -639 -1658 1313 C ATOM 4601 CD1 ILE B 173 -73.843 26.376 22.391 1.00101.97 C ANISOU 4601 CD1 ILE B 173 14653 11374 12716 277 -1732 765 C ATOM 4602 N PHE B 174 -70.975 22.345 19.733 1.00 82.33 N ANISOU 4602 N PHE B 174 11314 10229 9738 -749 -878 1006 N ATOM 4603 CA PHE B 174 -70.314 21.701 18.597 1.00 81.83 C ANISOU 4603 CA PHE B 174 11116 10500 9474 -978 -783 1089 C ATOM 4604 C PHE B 174 -70.783 20.318 18.135 1.00 84.79 C ANISOU 4604 C PHE B 174 11211 11150 9855 -863 -606 915 C ATOM 4605 O PHE B 174 -70.696 20.045 16.934 1.00 85.36 O ANISOU 4605 O PHE B 174 11227 11449 9758 -975 -623 979 O ATOM 4606 CB PHE B 174 -68.786 21.852 18.672 1.00 83.51 C ANISOU 4606 CB PHE B 174 11347 10855 9530 -1297 -709 1215 C ATOM 4607 CG PHE B 174 -68.345 23.304 18.676 1.00 87.17 C ANISOU 4607 CG PHE B 174 12129 11066 9927 -1512 -951 1455 C ATOM 4608 CD1 PHE B 174 -68.041 23.954 19.866 1.00 89.61 C ANISOU 4608 CD1 PHE B 174 12599 11093 10355 -1501 -1009 1437 C ATOM 4609 CD2 PHE B 174 -68.282 24.033 17.494 1.00 91.77 C ANISOU 4609 CD2 PHE B 174 12877 11669 10322 -1733 -1147 1704 C ATOM 4610 CE1 PHE B 174 -67.665 25.300 19.872 1.00 93.04 C ANISOU 4610 CE1 PHE B 174 13372 11242 10737 -1711 -1272 1653 C ATOM 4611 CE2 PHE B 174 -67.914 25.382 17.504 1.00 97.02 C ANISOU 4611 CE2 PHE B 174 13885 12046 10930 -1960 -1411 1948 C ATOM 4612 CZ PHE B 174 -67.600 26.003 18.690 1.00 94.93 C ANISOU 4612 CZ PHE B 174 13793 11476 10800 -1950 -1479 1917 C ATOM 4613 N ALA B 175 -71.330 19.479 19.046 1.00 79.21 N ANISOU 4613 N ALA B 175 10348 10419 9327 -655 -462 703 N ATOM 4614 CA ALA B 175 -71.839 18.141 18.702 1.00 77.27 C ANISOU 4614 CA ALA B 175 9875 10377 9108 -566 -328 537 C ATOM 4615 C ALA B 175 -73.123 18.210 17.875 1.00 81.46 C ANISOU 4615 C ALA B 175 10378 10916 9655 -442 -464 525 C ATOM 4616 O ALA B 175 -74.112 18.812 18.304 1.00 81.14 O ANISOU 4616 O ALA B 175 10387 10702 9742 -258 -579 505 O ATOM 4617 CB ALA B 175 -72.058 17.306 19.953 1.00 76.03 C ANISOU 4617 CB ALA B 175 9594 10171 9123 -432 -166 361 C ATOM 4618 N ASN B 176 -73.080 17.624 16.666 1.00 79.04 N ANISOU 4618 N ASN B 176 9989 10841 9202 -529 -463 525 N ATOM 4619 CA ASN B 176 -74.192 17.584 15.710 1.00 80.16 C ANISOU 4619 CA ASN B 176 10088 11047 9321 -443 -596 515 C ATOM 4620 C ASN B 176 -74.209 16.271 14.915 1.00 83.08 C ANISOU 4620 C ASN B 176 10282 11679 9606 -485 -498 375 C ATOM 4621 O ASN B 176 -73.217 15.540 14.906 1.00 81.50 O ANISOU 4621 O ASN B 176 10024 11620 9322 -581 -353 310 O ATOM 4622 CB ASN B 176 -74.130 18.789 14.752 1.00 84.06 C ANISOU 4622 CB ASN B 176 10780 11503 9654 -535 -818 744 C ATOM 4623 CG ASN B 176 -74.417 20.116 15.413 1.00112.53 C ANISOU 4623 CG ASN B 176 14606 14786 13363 -440 -995 859 C ATOM 4624 OD1 ASN B 176 -75.575 20.523 15.577 1.00109.32 O ANISOU 4624 OD1 ASN B 176 14213 14242 13080 -206 -1138 811 O ATOM 4625 ND2 ASN B 176 -73.364 20.808 15.837 1.00104.65 N ANISOU 4625 ND2 ASN B 176 13780 13670 12314 -607 -1002 994 N ATOM 4626 N VAL B 177 -75.344 15.977 14.252 1.00 80.74 N ANISOU 4626 N VAL B 177 9902 11448 9327 -395 -597 311 N ATOM 4627 CA VAL B 177 -75.527 14.782 13.417 1.00 80.45 C ANISOU 4627 CA VAL B 177 9727 11630 9211 -428 -555 163 C ATOM 4628 C VAL B 177 -75.356 15.209 11.962 1.00 86.14 C ANISOU 4628 C VAL B 177 10510 12543 9678 -527 -684 281 C ATOM 4629 O VAL B 177 -76.001 16.169 11.534 1.00 86.99 O ANISOU 4629 O VAL B 177 10708 12586 9759 -488 -870 426 O ATOM 4630 CB VAL B 177 -76.898 14.083 13.668 1.00 83.74 C ANISOU 4630 CB VAL B 177 9990 12025 9801 -308 -581 10 C ATOM 4631 CG1 VAL B 177 -77.066 12.839 12.795 1.00 83.73 C ANISOU 4631 CG1 VAL B 177 9886 12209 9719 -366 -571 -152 C ATOM 4632 CG2 VAL B 177 -77.066 13.721 15.140 1.00 81.89 C ANISOU 4632 CG2 VAL B 177 9694 11636 9782 -244 -451 -74 C ATOM 4633 N SER B 178 -74.483 14.517 11.213 1.00 83.35 N ANISOU 4633 N SER B 178 10111 12438 9122 -639 -598 217 N ATOM 4634 CA SER B 178 -74.240 14.837 9.806 1.00 85.81 C ANISOU 4634 CA SER B 178 10458 13004 9140 -754 -698 323 C ATOM 4635 C SER B 178 -74.231 13.602 8.911 1.00 90.29 C ANISOU 4635 C SER B 178 10897 13840 9568 -745 -655 103 C ATOM 4636 O SER B 178 -73.831 12.525 9.349 1.00 88.76 O ANISOU 4636 O SER B 178 10620 13661 9444 -694 -518 -110 O ATOM 4637 CB SER B 178 -72.938 15.619 9.643 1.00 90.99 C ANISOU 4637 CB SER B 178 11212 13775 9586 -946 -660 523 C ATOM 4638 OG SER B 178 -71.815 14.767 9.485 1.00101.15 O ANISOU 4638 OG SER B 178 12381 15334 10718 -1006 -483 385 O ATOM 4639 N GLU B 179 -74.636 13.772 7.648 1.00 89.11 N ANISOU 4639 N GLU B 179 10754 13895 9208 -788 -791 151 N ATOM 4640 CA GLU B 179 -74.631 12.688 6.673 1.00 90.29 C ANISOU 4640 CA GLU B 179 10802 14319 9184 -777 -780 -67 C ATOM 4641 C GLU B 179 -73.221 12.554 6.080 1.00 96.11 C ANISOU 4641 C GLU B 179 11512 15400 9605 -886 -659 -75 C ATOM 4642 O GLU B 179 -72.673 13.532 5.564 1.00 98.25 O ANISOU 4642 O GLU B 179 11850 15836 9646 -1046 -695 171 O ATOM 4643 CB GLU B 179 -75.681 12.935 5.575 1.00 93.70 C ANISOU 4643 CB GLU B 179 11240 14858 9502 -772 -984 -20 C ATOM 4644 CG GLU B 179 -76.041 11.691 4.776 1.00105.46 C ANISOU 4644 CG GLU B 179 12628 16542 10900 -726 -1007 -301 C ATOM 4645 CD GLU B 179 -77.172 11.814 3.767 1.00129.78 C ANISOU 4645 CD GLU B 179 15692 19728 13890 -714 -1218 -286 C ATOM 4646 OE1 GLU B 179 -77.565 12.953 3.422 1.00130.01 O ANISOU 4646 OE1 GLU B 179 15802 19744 13852 -744 -1364 -29 O ATOM 4647 OE2 GLU B 179 -77.654 10.755 3.303 1.00120.96 O ANISOU 4647 OE2 GLU B 179 14497 18700 12763 -675 -1259 -537 O ATOM 4648 N ALA B 180 -72.624 11.350 6.193 1.00 91.19 N ANISOU 4648 N ALA B 180 10793 14889 8966 -799 -528 -356 N ATOM 4649 CA ALA B 180 -71.299 11.009 5.661 1.00 91.76 C ANISOU 4649 CA ALA B 180 10783 15350 8733 -836 -403 -448 C ATOM 4650 C ALA B 180 -71.188 9.494 5.512 1.00 94.68 C ANISOU 4650 C ALA B 180 11076 15788 9110 -652 -361 -835 C ATOM 4651 O ALA B 180 -71.571 8.766 6.430 1.00 92.45 O ANISOU 4651 O ALA B 180 10820 15178 9129 -537 -348 -983 O ATOM 4652 CB ALA B 180 -70.199 11.533 6.574 1.00 91.36 C ANISOU 4652 CB ALA B 180 10727 15274 8713 -910 -263 -314 C ATOM 4653 N ASP B 181 -70.684 9.025 4.348 1.00 93.09 N ANISOU 4653 N ASP B 181 10797 16011 8564 -627 -357 -1000 N ATOM 4654 CA ASP B 181 -70.513 7.611 3.974 1.00 93.68 C ANISOU 4654 CA ASP B 181 10827 16190 8578 -426 -357 -1403 C ATOM 4655 C ASP B 181 -71.862 6.846 3.956 1.00 96.02 C ANISOU 4655 C ASP B 181 11207 16161 9116 -356 -519 -1565 C ATOM 4656 O ASP B 181 -71.950 5.729 4.481 1.00 94.68 O ANISOU 4656 O ASP B 181 11081 15754 9141 -216 -534 -1825 O ATOM 4657 CB ASP B 181 -69.443 6.917 4.857 1.00 94.73 C ANISOU 4657 CB ASP B 181 10914 16283 8795 -273 -217 -1589 C ATOM 4658 CG ASP B 181 -68.612 5.864 4.146 1.00108.65 C ANISOU 4658 CG ASP B 181 12590 18404 10289 -66 -188 -1961 C ATOM 4659 OD1 ASP B 181 -67.366 5.965 4.188 1.00111.28 O ANISOU 4659 OD1 ASP B 181 12790 19079 10413 -23 -49 -1992 O ATOM 4660 OD2 ASP B 181 -69.204 4.924 3.570 1.00114.43 O ANISOU 4660 OD2 ASP B 181 13382 19080 11016 64 -315 -2238 O ATOM 4661 N ASP B 182 -72.914 7.471 3.342 1.00 92.68 N ANISOU 4661 N ASP B 182 10810 15734 8669 -470 -659 -1397 N ATOM 4662 CA ASP B 182 -74.303 6.969 3.224 1.00 92.37 C ANISOU 4662 CA ASP B 182 10811 15461 8826 -456 -829 -1494 C ATOM 4663 C ASP B 182 -74.854 6.559 4.608 1.00 93.46 C ANISOU 4663 C ASP B 182 10986 15140 9386 -429 -810 -1511 C ATOM 4664 O ASP B 182 -75.619 5.601 4.750 1.00 93.38 O ANISOU 4664 O ASP B 182 11002 14930 9548 -404 -908 -1704 O ATOM 4665 CB ASP B 182 -74.401 5.828 2.186 1.00 96.71 C ANISOU 4665 CB ASP B 182 11359 16203 9181 -363 -930 -1844 C ATOM 4666 CG ASP B 182 -75.816 5.493 1.737 1.00107.64 C ANISOU 4666 CG ASP B 182 12764 17465 10670 -409 -1135 -1909 C ATOM 4667 OD1 ASP B 182 -76.583 6.432 1.433 1.00108.62 O ANISOU 4667 OD1 ASP B 182 12862 17628 10780 -510 -1223 -1660 O ATOM 4668 OD2 ASP B 182 -76.150 4.292 1.675 1.00113.18 O ANISOU 4668 OD2 ASP B 182 13514 18030 11459 -345 -1228 -2210 O ATOM 4669 N ARG B 183 -74.432 7.316 5.631 1.00 87.41 N ANISOU 4669 N ARG B 183 10226 14224 8763 -459 -689 -1295 N ATOM 4670 CA ARG B 183 -74.706 7.084 7.042 1.00 84.51 C ANISOU 4670 CA ARG B 183 9884 13484 8742 -439 -631 -1275 C ATOM 4671 C ARG B 183 -74.833 8.418 7.772 1.00 86.72 C ANISOU 4671 C ARG B 183 10169 13646 9134 -503 -588 -962 C ATOM 4672 O ARG B 183 -74.492 9.466 7.218 1.00 87.10 O ANISOU 4672 O ARG B 183 10231 13874 8988 -571 -601 -761 O ATOM 4673 CB ARG B 183 -73.506 6.319 7.629 1.00 83.08 C ANISOU 4673 CB ARG B 183 9725 13276 8566 -338 -499 -1444 C ATOM 4674 CG ARG B 183 -73.842 5.334 8.722 1.00 89.50 C ANISOU 4674 CG ARG B 183 10597 13728 9680 -293 -501 -1574 C ATOM 4675 CD ARG B 183 -72.634 5.085 9.597 1.00 93.03 C ANISOU 4675 CD ARG B 183 11068 14117 10163 -199 -361 -1614 C ATOM 4676 NE ARG B 183 -72.701 5.862 10.832 1.00 96.60 N ANISOU 4676 NE ARG B 183 11518 14368 10819 -264 -268 -1379 N ATOM 4677 CZ ARG B 183 -72.220 5.449 11.998 1.00107.62 C ANISOU 4677 CZ ARG B 183 12957 15554 12381 -212 -187 -1401 C ATOM 4678 NH1 ARG B 183 -72.326 6.216 13.074 1.00 94.31 N ANISOU 4678 NH1 ARG B 183 11266 13714 10854 -269 -109 -1196 N ATOM 4679 NH2 ARG B 183 -71.631 4.264 12.099 1.00 92.53 N ANISOU 4679 NH2 ARG B 183 11108 13579 10470 -85 -204 -1638 N ATOM 4680 N TYR B 184 -75.306 8.371 9.027 1.00 81.27 N ANISOU 4680 N TYR B 184 9483 12652 8743 -488 -548 -924 N ATOM 4681 CA TYR B 184 -75.380 9.534 9.897 1.00 79.57 C ANISOU 4681 CA TYR B 184 9289 12290 8654 -507 -508 -682 C ATOM 4682 C TYR B 184 -74.235 9.391 10.898 1.00 81.83 C ANISOU 4682 C TYR B 184 9606 12486 8998 -487 -344 -690 C ATOM 4683 O TYR B 184 -74.107 8.355 11.553 1.00 80.30 O ANISOU 4683 O TYR B 184 9412 12158 8939 -438 -287 -855 O ATOM 4684 CB TYR B 184 -76.738 9.630 10.621 1.00 80.19 C ANISOU 4684 CB TYR B 184 9317 12161 8992 -485 -574 -649 C ATOM 4685 CG TYR B 184 -77.947 9.731 9.710 1.00 83.95 C ANISOU 4685 CG TYR B 184 9727 12743 9426 -491 -749 -654 C ATOM 4686 CD1 TYR B 184 -78.299 10.940 9.116 1.00 86.97 C ANISOU 4686 CD1 TYR B 184 10134 13206 9703 -474 -868 -462 C ATOM 4687 CD2 TYR B 184 -78.786 8.639 9.510 1.00 85.65 C ANISOU 4687 CD2 TYR B 184 9868 12956 9720 -521 -820 -839 C ATOM 4688 CE1 TYR B 184 -79.427 11.047 8.303 1.00 89.40 C ANISOU 4688 CE1 TYR B 184 10373 13623 9972 -457 -1046 -466 C ATOM 4689 CE2 TYR B 184 -79.917 8.733 8.700 1.00 88.40 C ANISOU 4689 CE2 TYR B 184 10131 13428 10028 -535 -990 -848 C ATOM 4690 CZ TYR B 184 -80.236 9.940 8.101 1.00 96.47 C ANISOU 4690 CZ TYR B 184 11158 14558 10938 -487 -1099 -665 C ATOM 4691 OH TYR B 184 -81.354 10.037 7.310 1.00 99.70 O ANISOU 4691 OH TYR B 184 11476 15103 11303 -478 -1284 -674 O ATOM 4692 N ILE B 185 -73.369 10.397 10.956 1.00 78.96 N ANISOU 4692 N ILE B 185 9281 12205 8516 -540 -289 -508 N ATOM 4693 CA ILE B 185 -72.235 10.438 11.872 1.00 78.06 C ANISOU 4693 CA ILE B 185 9181 12046 8432 -538 -146 -489 C ATOM 4694 C ILE B 185 -72.581 11.468 12.940 1.00 81.82 C ANISOU 4694 C ILE B 185 9720 12273 9097 -556 -147 -296 C ATOM 4695 O ILE B 185 -73.053 12.560 12.611 1.00 82.09 O ANISOU 4695 O ILE B 185 9813 12282 9096 -600 -254 -113 O ATOM 4696 CB ILE B 185 -70.896 10.787 11.136 1.00 82.67 C ANISOU 4696 CB ILE B 185 9739 12966 8707 -619 -86 -438 C ATOM 4697 CG1 ILE B 185 -70.631 9.902 9.883 1.00 85.38 C ANISOU 4697 CG1 ILE B 185 10008 13631 8803 -575 -103 -645 C ATOM 4698 CG2 ILE B 185 -69.691 10.807 12.094 1.00 82.49 C ANISOU 4698 CG2 ILE B 185 9698 12937 8708 -620 55 -428 C ATOM 4699 CD1 ILE B 185 -70.279 8.378 10.094 1.00 94.21 C ANISOU 4699 CD1 ILE B 185 11089 14732 9974 -403 -54 -974 C ATOM 4700 N CYS B 186 -72.357 11.112 14.214 1.00 77.64 N ANISOU 4700 N CYS B 186 9192 11551 8755 -505 -47 -345 N ATOM 4701 CA CYS B 186 -72.587 11.989 15.359 1.00 76.30 C ANISOU 4701 CA CYS B 186 9078 11159 8753 -495 -32 -207 C ATOM 4702 C CYS B 186 -71.273 12.247 16.100 1.00 77.47 C ANISOU 4702 C CYS B 186 9260 11308 8866 -537 80 -156 C ATOM 4703 O CYS B 186 -70.731 11.332 16.724 1.00 75.80 O ANISOU 4703 O CYS B 186 9011 11077 8711 -486 180 -287 O ATOM 4704 CB CYS B 186 -73.671 11.422 16.279 1.00 76.00 C ANISOU 4704 CB CYS B 186 8994 10927 8956 -415 -22 -295 C ATOM 4705 SG CYS B 186 -73.522 11.904 18.028 1.00 78.51 S ANISOU 4705 SG CYS B 186 9349 11022 9458 -372 73 -230 S ATOM 4706 N ASP B 187 -70.749 13.483 15.981 1.00 74.30 N ANISOU 4706 N ASP B 187 8941 10932 8359 -643 39 39 N ATOM 4707 CA ASP B 187 -69.565 13.988 16.690 1.00 74.06 C ANISOU 4707 CA ASP B 187 8947 10903 8288 -727 114 126 C ATOM 4708 C ASP B 187 -69.514 15.515 16.771 1.00 76.46 C ANISOU 4708 C ASP B 187 9405 11085 8562 -847 0 362 C ATOM 4709 O ASP B 187 -70.471 16.169 16.364 1.00 76.92 O ANISOU 4709 O ASP B 187 9549 11025 8653 -817 -143 447 O ATOM 4710 CB ASP B 187 -68.223 13.338 16.262 1.00 77.05 C ANISOU 4710 CB ASP B 187 9217 11594 8465 -782 221 45 C ATOM 4711 CG ASP B 187 -67.629 13.796 14.953 1.00 91.28 C ANISOU 4711 CG ASP B 187 10987 13728 9966 -943 184 149 C ATOM 4712 OD1 ASP B 187 -68.348 13.775 13.940 1.00 93.44 O ANISOU 4712 OD1 ASP B 187 11268 14075 10159 -942 96 153 O ATOM 4713 OD2 ASP B 187 -66.413 14.071 14.922 1.00 98.77 O ANISOU 4713 OD2 ASP B 187 11878 14911 10738 -1074 250 214 O ATOM 4714 N ARG B 188 -68.439 16.075 17.350 1.00 71.00 N ANISOU 4714 N ARG B 188 8760 10399 7818 -972 41 460 N ATOM 4715 CA ARG B 188 -68.277 17.522 17.492 1.00 70.93 C ANISOU 4715 CA ARG B 188 8941 10229 7780 -1117 -96 686 C ATOM 4716 C ARG B 188 -67.650 18.109 16.227 1.00 74.62 C ANISOU 4716 C ARG B 188 9443 10946 7964 -1367 -176 878 C ATOM 4717 O ARG B 188 -66.509 17.782 15.881 1.00 74.21 O ANISOU 4717 O ARG B 188 9263 11224 7711 -1519 -69 882 O ATOM 4718 CB ARG B 188 -67.448 17.869 18.745 1.00 69.79 C ANISOU 4718 CB ARG B 188 8843 9964 7709 -1168 -38 705 C ATOM 4719 CG ARG B 188 -68.052 17.405 20.063 1.00 73.73 C ANISOU 4719 CG ARG B 188 9324 10232 8457 -946 34 545 C ATOM 4720 CD ARG B 188 -66.976 17.104 21.088 1.00 82.39 C ANISOU 4720 CD ARG B 188 10369 11370 9567 -983 158 496 C ATOM 4721 NE ARG B 188 -66.237 15.877 20.775 1.00 90.48 N ANISOU 4721 NE ARG B 188 11201 12682 10497 -964 301 366 N ATOM 4722 CZ ARG B 188 -64.954 15.682 21.058 1.00103.57 C ANISOU 4722 CZ ARG B 188 12769 14536 12045 -1053 384 358 C ATOM 4723 NH1 ARG B 188 -64.364 14.538 20.734 1.00 82.95 N ANISOU 4723 NH1 ARG B 188 9986 12182 9349 -971 489 207 N ATOM 4724 NH2 ARG B 188 -64.247 16.631 21.661 1.00 96.74 N ANISOU 4724 NH2 ARG B 188 11988 13618 11150 -1213 345 489 N ATOM 4725 N PHE B 189 -68.418 18.947 15.521 1.00 71.96 N ANISOU 4725 N PHE B 189 9265 10485 7592 -1402 -369 1033 N ATOM 4726 CA PHE B 189 -67.980 19.593 14.287 1.00 74.14 C ANISOU 4726 CA PHE B 189 9610 10974 7584 -1662 -479 1258 C ATOM 4727 C PHE B 189 -67.603 21.039 14.577 1.00 81.83 C ANISOU 4727 C PHE B 189 10854 11706 8532 -1884 -662 1531 C ATOM 4728 O PHE B 189 -68.474 21.867 14.864 1.00 82.01 O ANISOU 4728 O PHE B 189 11103 11346 8709 -1771 -862 1602 O ATOM 4729 CB PHE B 189 -69.057 19.482 13.188 1.00 76.14 C ANISOU 4729 CB PHE B 189 9876 11269 7786 -1565 -598 1261 C ATOM 4730 CG PHE B 189 -69.356 18.062 12.768 1.00 75.50 C ANISOU 4730 CG PHE B 189 9555 11435 7697 -1397 -448 997 C ATOM 4731 CD1 PHE B 189 -68.594 17.434 11.790 1.00 78.81 C ANISOU 4731 CD1 PHE B 189 9817 12290 7837 -1515 -349 954 C ATOM 4732 CD2 PHE B 189 -70.402 17.352 13.348 1.00 75.21 C ANISOU 4732 CD2 PHE B 189 9452 11208 7918 -1130 -419 787 C ATOM 4733 CE1 PHE B 189 -68.863 16.114 11.412 1.00 78.71 C ANISOU 4733 CE1 PHE B 189 9623 12463 7822 -1340 -244 683 C ATOM 4734 CE2 PHE B 189 -70.663 16.031 12.974 1.00 77.03 C ANISOU 4734 CE2 PHE B 189 9500 11621 8145 -1011 -315 552 C ATOM 4735 CZ PHE B 189 -69.902 15.429 11.996 1.00 76.16 C ANISOU 4735 CZ PHE B 189 9276 11888 7774 -1103 -242 494 C ATOM 4736 N TYR B 190 -66.289 21.322 14.551 1.00 80.85 N ANISOU 4736 N TYR B 190 10701 11808 8211 -2192 -605 1668 N ATOM 4737 CA TYR B 190 -65.717 22.643 14.828 1.00 83.20 C ANISOU 4737 CA TYR B 190 11256 11902 8452 -2487 -783 1942 C ATOM 4738 C TYR B 190 -65.526 23.445 13.525 1.00 92.50 C ANISOU 4738 C TYR B 190 12579 13232 9334 -2823 -963 2259 C ATOM 4739 O TYR B 190 -65.324 22.832 12.473 1.00 92.56 O ANISOU 4739 O TYR B 190 12388 13680 9103 -2894 -860 2249 O ATOM 4740 CB TYR B 190 -64.394 22.510 15.619 1.00 83.44 C ANISOU 4740 CB TYR B 190 11158 12112 8433 -2670 -630 1922 C ATOM 4741 CG TYR B 190 -64.549 21.777 16.937 1.00 81.56 C ANISOU 4741 CG TYR B 190 10810 11711 8467 -2361 -476 1644 C ATOM 4742 CD1 TYR B 190 -64.269 20.418 17.039 1.00 81.31 C ANISOU 4742 CD1 TYR B 190 10475 11981 8437 -2181 -235 1394 C ATOM 4743 CD2 TYR B 190 -65.008 22.436 18.073 1.00 81.54 C ANISOU 4743 CD2 TYR B 190 11026 11246 8708 -2237 -591 1626 C ATOM 4744 CE1 TYR B 190 -64.422 19.736 18.246 1.00 78.24 C ANISOU 4744 CE1 TYR B 190 10013 11432 8283 -1924 -115 1172 C ATOM 4745 CE2 TYR B 190 -65.185 21.760 19.280 1.00 79.49 C ANISOU 4745 CE2 TYR B 190 10663 10871 8668 -1970 -448 1386 C ATOM 4746 CZ TYR B 190 -64.889 20.411 19.362 1.00 83.23 C ANISOU 4746 CZ TYR B 190 10844 11642 9136 -1833 -212 1179 C ATOM 4747 OH TYR B 190 -65.063 19.752 20.553 1.00 81.71 O ANISOU 4747 OH TYR B 190 10578 11323 9143 -1600 -92 978 O ATOM 4748 N PRO B 191 -65.611 24.801 13.547 1.00 93.06 N ANISOU 4748 N PRO B 191 13014 12943 9403 -3028 -1251 2541 N ATOM 4749 CA PRO B 191 -65.454 25.558 12.290 1.00 97.15 C ANISOU 4749 CA PRO B 191 13701 13591 9621 -3378 -1447 2880 C ATOM 4750 C PRO B 191 -64.009 25.708 11.818 1.00104.41 C ANISOU 4750 C PRO B 191 14492 14990 10188 -3884 -1355 3098 C ATOM 4751 O PRO B 191 -63.775 25.996 10.643 1.00107.64 O ANISOU 4751 O PRO B 191 14921 15701 10276 -4186 -1429 3344 O ATOM 4752 CB PRO B 191 -66.087 26.913 12.611 1.00100.89 C ANISOU 4752 CB PRO B 191 14645 13440 10250 -3381 -1818 3081 C ATOM 4753 CG PRO B 191 -65.900 27.078 14.072 1.00103.28 C ANISOU 4753 CG PRO B 191 15008 13413 10819 -3245 -1788 2924 C ATOM 4754 CD PRO B 191 -65.850 25.704 14.693 1.00 94.63 C ANISOU 4754 CD PRO B 191 13510 12592 9851 -2952 -1433 2562 C ATOM 4755 N ASN B 192 -63.052 25.521 12.735 1.00 99.90 N ANISOU 4755 N ASN B 192 13777 14523 9658 -3981 -1197 3012 N ATOM 4756 CA ASN B 192 -61.624 25.658 12.470 1.00102.35 C ANISOU 4756 CA ASN B 192 13915 15327 9647 -4453 -1098 3191 C ATOM 4757 C ASN B 192 -60.817 24.637 13.284 1.00104.03 C ANISOU 4757 C ASN B 192 13749 15864 9915 -4301 -790 2892 C ATOM 4758 O ASN B 192 -61.356 24.003 14.196 1.00100.07 O ANISOU 4758 O ASN B 192 13202 15095 9724 -3881 -696 2597 O ATOM 4759 CB ASN B 192 -61.181 27.090 12.818 1.00107.37 C ANISOU 4759 CB ASN B 192 14930 15608 10258 -4886 -1385 3541 C ATOM 4760 CG ASN B 192 -59.998 27.607 12.036 1.00142.37 C ANISOU 4760 CG ASN B 192 19297 20530 14268 -5517 -1407 3890 C ATOM 4761 OD1 ASN B 192 -59.212 26.855 11.443 1.00139.16 O ANISOU 4761 OD1 ASN B 192 18477 20832 13567 -5642 -1149 3834 O ATOM 4762 ND2 ASN B 192 -59.833 28.921 12.036 1.00139.83 N ANISOU 4762 ND2 ASN B 192 19386 19849 13894 -5936 -1730 4258 N ATOM 4763 N ASP B 193 -59.521 24.490 12.956 1.00102.85 N ANISOU 4763 N ASP B 193 13320 16311 9445 -4649 -645 2978 N ATOM 4764 CA ASP B 193 -58.607 23.587 13.657 1.00100.89 C ANISOU 4764 CA ASP B 193 12703 16428 9202 -4527 -381 2717 C ATOM 4765 C ASP B 193 -58.006 24.264 14.891 1.00102.97 C ANISOU 4765 C ASP B 193 13099 16409 9617 -4705 -461 2791 C ATOM 4766 O ASP B 193 -57.375 23.594 15.719 1.00100.77 O ANISOU 4766 O ASP B 193 12572 16303 9414 -4551 -282 2568 O ATOM 4767 CB ASP B 193 -57.527 23.048 12.707 1.00105.76 C ANISOU 4767 CB ASP B 193 12907 17890 9387 -4753 -184 2726 C ATOM 4768 CG ASP B 193 -58.100 22.201 11.587 1.00118.16 C ANISOU 4768 CG ASP B 193 14320 19758 10816 -4502 -85 2568 C ATOM 4769 OD1 ASP B 193 -58.049 22.651 10.414 1.00122.37 O ANISOU 4769 OD1 ASP B 193 14876 20596 11022 -4811 -157 2813 O ATOM 4770 OD2 ASP B 193 -58.631 21.099 11.884 1.00120.20 O ANISOU 4770 OD2 ASP B 193 14456 19926 11287 -4013 47 2210 O ATOM 4771 N LEU B 194 -58.238 25.592 15.028 1.00100.14 N ANISOU 4771 N LEU B 194 13160 15580 9309 -5007 -756 3095 N ATOM 4772 CA LEU B 194 -57.803 26.383 16.179 1.00 99.64 C ANISOU 4772 CA LEU B 194 13309 15149 9402 -5183 -895 3173 C ATOM 4773 C LEU B 194 -58.663 26.011 17.389 1.00 98.35 C ANISOU 4773 C LEU B 194 13256 14458 9653 -4653 -875 2862 C ATOM 4774 O LEU B 194 -58.134 25.891 18.494 1.00 96.30 O ANISOU 4774 O LEU B 194 12927 14145 9516 -4607 -808 2732 O ATOM 4775 CB LEU B 194 -57.910 27.895 15.903 1.00103.34 C ANISOU 4775 CB LEU B 194 14254 15203 9809 -5627 -1264 3571 C ATOM 4776 CG LEU B 194 -57.159 28.465 14.702 1.00112.39 C ANISOU 4776 CG LEU B 194 15373 16802 10526 -6239 -1343 3961 C ATOM 4777 CD1 LEU B 194 -57.538 29.907 14.489 1.00116.18 C ANISOU 4777 CD1 LEU B 194 16422 16708 11015 -6586 -1762 4338 C ATOM 4778 CD2 LEU B 194 -55.643 28.338 14.859 1.00116.40 C ANISOU 4778 CD2 LEU B 194 15521 17947 10760 -6668 -1177 4031 C ATOM 4779 N TRP B 195 -59.991 25.813 17.164 1.00 92.40 N ANISOU 4779 N TRP B 195 12652 13363 9093 -4263 -932 2747 N ATOM 4780 CA TRP B 195 -60.970 25.404 18.176 1.00 88.26 C ANISOU 4780 CA TRP B 195 12198 12409 8929 -3756 -901 2458 C ATOM 4781 C TRP B 195 -60.612 24.024 18.701 1.00 87.63 C ANISOU 4781 C TRP B 195 11724 12667 8904 -3477 -586 2146 C ATOM 4782 O TRP B 195 -60.635 23.817 19.911 1.00 84.73 O ANISOU 4782 O TRP B 195 11362 12083 8750 -3271 -534 1970 O ATOM 4783 CB TRP B 195 -62.386 25.384 17.591 1.00 86.54 C ANISOU 4783 CB TRP B 195 12132 11918 8833 -3449 -1008 2417 C ATOM 4784 CG TRP B 195 -62.971 26.739 17.334 1.00 90.67 C ANISOU 4784 CG TRP B 195 13104 11960 9386 -3580 -1365 2667 C ATOM 4785 CD1 TRP B 195 -62.988 27.413 16.149 1.00 96.83 C ANISOU 4785 CD1 TRP B 195 14058 12791 9942 -3883 -1558 2971 C ATOM 4786 CD2 TRP B 195 -63.683 27.556 18.272 1.00 90.59 C ANISOU 4786 CD2 TRP B 195 13443 11336 9641 -3371 -1594 2618 C ATOM 4787 NE1 TRP B 195 -63.653 28.610 16.293 1.00 98.55 N ANISOU 4787 NE1 TRP B 195 14739 12421 10283 -3875 -1917 3126 N ATOM 4788 CE2 TRP B 195 -64.092 28.723 17.586 1.00 97.98 C ANISOU 4788 CE2 TRP B 195 14776 11937 10513 -3544 -1945 2895 C ATOM 4789 CE3 TRP B 195 -64.002 27.424 19.635 1.00 89.58 C ANISOU 4789 CE3 TRP B 195 13334 10922 9780 -3048 -1545 2361 C ATOM 4790 CZ2 TRP B 195 -64.803 29.751 18.216 1.00 98.66 C ANISOU 4790 CZ2 TRP B 195 15284 11395 10806 -3364 -2261 2895 C ATOM 4791 CZ3 TRP B 195 -64.710 28.440 20.257 1.00 92.53 C ANISOU 4791 CZ3 TRP B 195 14094 10723 10339 -2881 -1831 2355 C ATOM 4792 CH2 TRP B 195 -65.103 29.588 19.551 1.00 96.71 C ANISOU 4792 CH2 TRP B 195 15022 10909 10814 -3019 -2192 2605 C ATOM 4793 N VAL B 196 -60.235 23.100 17.787 1.00 84.26 N ANISOU 4793 N VAL B 196 10973 12778 8266 -3474 -395 2079 N ATOM 4794 CA VAL B 196 -59.797 21.731 18.083 1.00 82.08 C ANISOU 4794 CA VAL B 196 10331 12858 7996 -3213 -125 1787 C ATOM 4795 C VAL B 196 -58.577 21.821 18.998 1.00 87.49 C ANISOU 4795 C VAL B 196 10890 13711 8642 -3382 -59 1782 C ATOM 4796 O VAL B 196 -58.498 21.104 19.992 1.00 84.97 O ANISOU 4796 O VAL B 196 10464 13323 8499 -3106 58 1553 O ATOM 4797 CB VAL B 196 -59.501 20.926 16.781 1.00 87.08 C ANISOU 4797 CB VAL B 196 10676 14061 8348 -3223 15 1735 C ATOM 4798 CG1 VAL B 196 -58.820 19.587 17.072 1.00 85.43 C ANISOU 4798 CG1 VAL B 196 10108 14243 8111 -2972 254 1435 C ATOM 4799 CG2 VAL B 196 -60.774 20.705 15.967 1.00 86.31 C ANISOU 4799 CG2 VAL B 196 10691 13789 8315 -3013 -49 1698 C ATOM 4800 N VAL B 197 -57.671 22.758 18.692 1.00 87.98 N ANISOU 4800 N VAL B 197 10987 13970 8472 -3860 -160 2054 N ATOM 4801 CA VAL B 197 -56.467 23.027 19.470 1.00 89.14 C ANISOU 4801 CA VAL B 197 11018 14306 8544 -4109 -136 2097 C ATOM 4802 C VAL B 197 -56.808 23.596 20.869 1.00 91.34 C ANISOU 4802 C VAL B 197 11588 13993 9125 -4009 -268 2056 C ATOM 4803 O VAL B 197 -56.216 23.151 21.855 1.00 89.71 O ANISOU 4803 O VAL B 197 11226 13869 8990 -3900 -164 1896 O ATOM 4804 CB VAL B 197 -55.483 23.877 18.618 1.00 97.91 C ANISOU 4804 CB VAL B 197 12079 15830 9290 -4706 -220 2428 C ATOM 4805 CG1 VAL B 197 -54.707 24.894 19.442 1.00 99.73 C ANISOU 4805 CG1 VAL B 197 12465 15911 9518 -5106 -378 2616 C ATOM 4806 CG2 VAL B 197 -54.538 22.973 17.837 1.00 99.17 C ANISOU 4806 CG2 VAL B 197 11749 16806 9125 -4745 18 2334 C ATOM 4807 N VAL B 198 -57.804 24.518 20.950 1.00 88.31 N ANISOU 4807 N VAL B 198 11617 13028 8909 -3996 -501 2171 N ATOM 4808 CA VAL B 198 -58.269 25.133 22.205 1.00 87.04 C ANISOU 4808 CA VAL B 198 11760 12293 9017 -3858 -650 2107 C ATOM 4809 C VAL B 198 -58.799 24.045 23.146 1.00 86.46 C ANISOU 4809 C VAL B 198 11534 12138 9179 -3353 -457 1773 C ATOM 4810 O VAL B 198 -58.305 23.907 24.269 1.00 85.25 O ANISOU 4810 O VAL B 198 11332 11951 9109 -3299 -407 1659 O ATOM 4811 CB VAL B 198 -59.329 26.271 21.990 1.00 92.36 C ANISOU 4811 CB VAL B 198 12897 12384 9812 -3859 -952 2256 C ATOM 4812 CG1 VAL B 198 -59.956 26.723 23.310 1.00 91.05 C ANISOU 4812 CG1 VAL B 198 13000 11667 9928 -3585 -1076 2099 C ATOM 4813 CG2 VAL B 198 -58.736 27.470 21.264 1.00 96.47 C ANISOU 4813 CG2 VAL B 198 13653 12888 10112 -4411 -1201 2623 C ATOM 4814 N PHE B 199 -59.793 23.276 22.676 1.00 80.37 N ANISOU 4814 N PHE B 199 10692 11346 8500 -3014 -362 1634 N ATOM 4815 CA PHE B 199 -60.444 22.248 23.474 1.00 76.89 C ANISOU 4815 CA PHE B 199 10138 10804 8274 -2576 -204 1353 C ATOM 4816 C PHE B 199 -59.625 21.014 23.789 1.00 80.57 C ANISOU 4816 C PHE B 199 10261 11665 8685 -2464 28 1178 C ATOM 4817 O PHE B 199 -59.842 20.413 24.840 1.00 77.74 O ANISOU 4817 O PHE B 199 9869 11171 8496 -2201 112 997 O ATOM 4818 CB PHE B 199 -61.864 21.950 22.976 1.00 77.37 C ANISOU 4818 CB PHE B 199 10271 10659 8467 -2283 -222 1274 C ATOM 4819 CG PHE B 199 -62.732 23.186 22.868 1.00 80.42 C ANISOU 4819 CG PHE B 199 11011 10608 8938 -2306 -480 1409 C ATOM 4820 CD1 PHE B 199 -62.769 24.127 23.896 1.00 84.15 C ANISOU 4820 CD1 PHE B 199 11744 10699 9530 -2316 -640 1422 C ATOM 4821 CD2 PHE B 199 -63.508 23.414 21.741 1.00 83.63 C ANISOU 4821 CD2 PHE B 199 11502 10978 9297 -2295 -585 1507 C ATOM 4822 CE1 PHE B 199 -63.556 25.278 23.786 1.00 86.87 C ANISOU 4822 CE1 PHE B 199 12441 10617 9951 -2292 -914 1521 C ATOM 4823 CE2 PHE B 199 -64.310 24.555 21.642 1.00 88.29 C ANISOU 4823 CE2 PHE B 199 12433 11148 9965 -2274 -856 1623 C ATOM 4824 CZ PHE B 199 -64.323 25.483 22.661 1.00 87.11 C ANISOU 4824 CZ PHE B 199 12552 10606 9939 -2262 -1025 1624 C ATOM 4825 N GLN B 200 -58.655 20.660 22.930 1.00 80.61 N ANISOU 4825 N GLN B 200 10017 12173 8440 -2657 117 1231 N ATOM 4826 CA GLN B 200 -57.778 19.520 23.192 1.00 80.90 C ANISOU 4826 CA GLN B 200 9725 12610 8403 -2520 307 1048 C ATOM 4827 C GLN B 200 -56.819 19.830 24.330 1.00 88.40 C ANISOU 4827 C GLN B 200 10644 13587 9359 -2641 297 1054 C ATOM 4828 O GLN B 200 -56.591 18.953 25.156 1.00 86.89 O ANISOU 4828 O GLN B 200 10320 13433 9260 -2384 405 862 O ATOM 4829 CB GLN B 200 -57.016 19.076 21.941 1.00 84.28 C ANISOU 4829 CB GLN B 200 9867 13622 8532 -2651 402 1067 C ATOM 4830 CG GLN B 200 -57.751 18.011 21.138 1.00102.68 C ANISOU 4830 CG GLN B 200 12102 16031 10880 -2344 495 890 C ATOM 4831 CD GLN B 200 -57.424 16.610 21.591 1.00123.19 C ANISOU 4831 CD GLN B 200 14478 18794 13534 -1993 642 605 C ATOM 4832 OE1 GLN B 200 -57.678 16.213 22.738 1.00115.93 O ANISOU 4832 OE1 GLN B 200 13633 17578 12838 -1779 657 489 O ATOM 4833 NE2 GLN B 200 -56.881 15.812 20.681 1.00117.97 N ANISOU 4833 NE2 GLN B 200 13556 18607 12659 -1911 740 479 N ATOM 4834 N PHE B 201 -56.305 21.084 24.405 1.00 89.25 N ANISOU 4834 N PHE B 201 10902 13637 9373 -3038 142 1280 N ATOM 4835 CA PHE B 201 -55.398 21.543 25.463 1.00 91.03 C ANISOU 4835 CA PHE B 201 11127 13869 9592 -3215 93 1307 C ATOM 4836 C PHE B 201 -56.133 21.637 26.804 1.00 94.44 C ANISOU 4836 C PHE B 201 11796 13786 10302 -2949 41 1177 C ATOM 4837 O PHE B 201 -55.577 21.237 27.831 1.00 93.61 O ANISOU 4837 O PHE B 201 11583 13744 10239 -2848 102 1056 O ATOM 4838 CB PHE B 201 -54.770 22.902 25.103 1.00 96.70 C ANISOU 4838 CB PHE B 201 11994 14612 10137 -3753 -98 1600 C ATOM 4839 CG PHE B 201 -53.617 23.326 25.990 1.00100.31 C ANISOU 4839 CG PHE B 201 12381 15212 10521 -4020 -147 1642 C ATOM 4840 CD1 PHE B 201 -53.844 24.023 27.171 1.00103.37 C ANISOU 4840 CD1 PHE B 201 13065 15120 11092 -4016 -301 1625 C ATOM 4841 CD2 PHE B 201 -52.303 23.055 25.627 1.00105.11 C ANISOU 4841 CD2 PHE B 201 12612 16467 10857 -4276 -49 1689 C ATOM 4842 CE1 PHE B 201 -52.779 24.426 27.982 1.00106.28 C ANISOU 4842 CE1 PHE B 201 13374 15624 11385 -4280 -364 1660 C ATOM 4843 CE2 PHE B 201 -51.238 23.466 26.436 1.00109.94 C ANISOU 4843 CE2 PHE B 201 13137 17243 11392 -4544 -107 1732 C ATOM 4844 CZ PHE B 201 -51.484 24.147 27.607 1.00107.69 C ANISOU 4844 CZ PHE B 201 13170 16445 11303 -4554 -269 1722 C ATOM 4845 N GLN B 202 -57.377 22.174 26.786 1.00 91.12 N ANISOU 4845 N GLN B 202 11681 12889 10050 -2826 -77 1199 N ATOM 4846 CA GLN B 202 -58.259 22.327 27.949 1.00 89.42 C ANISOU 4846 CA GLN B 202 11686 12217 10074 -2549 -126 1065 C ATOM 4847 C GLN B 202 -58.583 20.954 28.543 1.00 91.86 C ANISOU 4847 C GLN B 202 11793 12613 10497 -2163 79 833 C ATOM 4848 O GLN B 202 -58.683 20.829 29.757 1.00 90.80 O ANISOU 4848 O GLN B 202 11710 12312 10477 -2004 96 718 O ATOM 4849 CB GLN B 202 -59.553 23.053 27.547 1.00 90.75 C ANISOU 4849 CB GLN B 202 12150 11970 10360 -2455 -282 1116 C ATOM 4850 CG GLN B 202 -60.407 23.534 28.716 1.00 98.11 C ANISOU 4850 CG GLN B 202 13329 12453 11494 -2211 -378 991 C ATOM 4851 CD GLN B 202 -61.809 23.873 28.277 1.00116.96 C ANISOU 4851 CD GLN B 202 15900 14537 14002 -1989 -478 972 C ATOM 4852 OE1 GLN B 202 -62.599 23.001 27.885 1.00109.50 O ANISOU 4852 OE1 GLN B 202 14802 13686 13118 -1746 -343 875 O ATOM 4853 NE2 GLN B 202 -62.162 25.148 28.365 1.00112.13 N ANISOU 4853 NE2 GLN B 202 15630 13545 13429 -2057 -738 1053 N ATOM 4854 N HIS B 203 -58.720 19.929 27.692 1.00 88.43 N ANISOU 4854 N HIS B 203 11146 12437 10016 -2028 217 770 N ATOM 4855 CA HIS B 203 -58.998 18.572 28.141 1.00 86.69 C ANISOU 4855 CA HIS B 203 10767 12277 9893 -1695 377 570 C ATOM 4856 C HIS B 203 -57.753 17.925 28.745 1.00 89.66 C ANISOU 4856 C HIS B 203 10926 12959 10180 -1690 464 494 C ATOM 4857 O HIS B 203 -57.867 17.295 29.789 1.00 87.92 O ANISOU 4857 O HIS B 203 10702 12630 10073 -1475 518 372 O ATOM 4858 CB HIS B 203 -59.612 17.729 27.009 1.00 87.53 C ANISOU 4858 CB HIS B 203 10765 12506 9986 -1551 454 512 C ATOM 4859 CG HIS B 203 -59.316 16.261 27.090 1.00 90.44 C ANISOU 4859 CG HIS B 203 10921 13087 10356 -1313 594 333 C ATOM 4860 ND1 HIS B 203 -59.859 15.468 28.086 1.00 90.78 N ANISOU 4860 ND1 HIS B 203 11001 12923 10570 -1061 647 203 N ATOM 4861 CD2 HIS B 203 -58.548 15.488 26.285 1.00 93.40 C ANISOU 4861 CD2 HIS B 203 11065 13852 10569 -1290 669 264 C ATOM 4862 CE1 HIS B 203 -59.399 14.248 27.860 1.00 90.32 C ANISOU 4862 CE1 HIS B 203 10771 13080 10466 -899 727 72 C ATOM 4863 NE2 HIS B 203 -58.610 14.212 26.785 1.00 92.20 N ANISOU 4863 NE2 HIS B 203 10839 13683 10509 -1000 743 82 N ATOM 4864 N ILE B 204 -56.580 18.079 28.108 1.00 87.63 N ANISOU 4864 N ILE B 204 10479 13109 9709 -1925 471 571 N ATOM 4865 CA ILE B 204 -55.321 17.509 28.601 1.00 88.20 C ANISOU 4865 CA ILE B 204 10301 13543 9668 -1912 539 492 C ATOM 4866 C ILE B 204 -54.969 18.109 29.976 1.00 92.59 C ANISOU 4866 C ILE B 204 10979 13908 10294 -1990 462 512 C ATOM 4867 O ILE B 204 -54.617 17.367 30.893 1.00 91.15 O ANISOU 4867 O ILE B 204 10705 13768 10157 -1783 516 384 O ATOM 4868 CB ILE B 204 -54.160 17.625 27.550 1.00 93.90 C ANISOU 4868 CB ILE B 204 10745 14827 10104 -2168 566 570 C ATOM 4869 CG1 ILE B 204 -54.489 16.933 26.186 1.00 94.63 C ANISOU 4869 CG1 ILE B 204 10702 15153 10098 -2051 649 512 C ATOM 4870 CG2 ILE B 204 -52.812 17.144 28.096 1.00 95.63 C ANISOU 4870 CG2 ILE B 204 10673 15470 10192 -2151 618 481 C ATOM 4871 CD1 ILE B 204 -54.875 15.377 26.181 1.00100.68 C ANISOU 4871 CD1 ILE B 204 11366 15923 10964 -1592 756 254 C ATOM 4872 N MET B 205 -55.129 19.438 30.126 1.00 90.85 N ANISOU 4872 N MET B 205 10996 13440 10085 -2269 313 666 N ATOM 4873 CA MET B 205 -54.840 20.149 31.373 1.00 91.23 C ANISOU 4873 CA MET B 205 11201 13276 10187 -2364 207 675 C ATOM 4874 C MET B 205 -55.852 19.841 32.487 1.00 91.25 C ANISOU 4874 C MET B 205 11384 12888 10400 -2033 228 533 C ATOM 4875 O MET B 205 -55.465 19.261 33.503 1.00 89.92 O ANISOU 4875 O MET B 205 11133 12778 10253 -1883 281 427 O ATOM 4876 CB MET B 205 -54.707 21.663 31.134 1.00 96.29 C ANISOU 4876 CB MET B 205 12081 13737 10769 -2765 4 873 C ATOM 4877 CG MET B 205 -53.724 22.321 32.069 1.00102.37 C ANISOU 4877 CG MET B 205 12878 14546 11473 -3014 -107 910 C ATOM 4878 SD MET B 205 -52.110 22.642 31.306 1.00110.81 S ANISOU 4878 SD MET B 205 13649 16212 12240 -3512 -130 1091 S ATOM 4879 CE MET B 205 -51.142 23.110 32.764 1.00108.77 C ANISOU 4879 CE MET B 205 13406 15957 11962 -3677 -243 1055 C ATOM 4880 N VAL B 206 -57.140 20.213 32.287 1.00 85.66 N ANISOU 4880 N VAL B 206 10900 11820 9826 -1918 183 534 N ATOM 4881 CA VAL B 206 -58.231 20.025 33.256 1.00 83.07 C ANISOU 4881 CA VAL B 206 10723 11170 9670 -1624 205 406 C ATOM 4882 C VAL B 206 -58.521 18.544 33.551 1.00 84.70 C ANISOU 4882 C VAL B 206 10751 11496 9936 -1327 381 275 C ATOM 4883 O VAL B 206 -58.621 18.167 34.716 1.00 84.05 O ANISOU 4883 O VAL B 206 10690 11339 9907 -1173 420 186 O ATOM 4884 CB VAL B 206 -59.517 20.834 32.895 1.00 86.42 C ANISOU 4884 CB VAL B 206 11395 11241 10200 -1564 98 430 C ATOM 4885 CG1 VAL B 206 -60.613 20.645 33.938 1.00 84.82 C ANISOU 4885 CG1 VAL B 206 11291 10800 10138 -1259 136 281 C ATOM 4886 CG2 VAL B 206 -59.208 22.321 32.724 1.00 88.51 C ANISOU 4886 CG2 VAL B 206 11906 11310 10413 -1850 -128 562 C ATOM 4887 N GLY B 207 -58.641 17.732 32.508 1.00 80.26 N ANISOU 4887 N GLY B 207 10036 11107 9351 -1264 466 269 N ATOM 4888 CA GLY B 207 -58.940 16.309 32.641 1.00 78.66 C ANISOU 4888 CA GLY B 207 9708 10971 9208 -1003 592 152 C ATOM 4889 C GLY B 207 -57.737 15.654 33.297 1.00 82.94 C ANISOU 4889 C GLY B 207 10094 11750 9668 -967 627 100 C ATOM 4890 O GLY B 207 -57.877 15.100 34.393 1.00 82.77 O ANISOU 4890 O GLY B 207 10109 11628 9713 -807 656 34 O ATOM 4891 N LEU B 208 -56.555 15.675 32.643 1.00 79.97 N ANISOU 4891 N LEU B 208 9528 11723 9133 -1108 622 129 N ATOM 4892 CA LEU B 208 -55.371 15.038 33.230 1.00 80.21 C ANISOU 4892 CA LEU B 208 9374 12028 9073 -1038 642 61 C ATOM 4893 C LEU B 208 -54.182 15.662 33.971 1.00 84.48 C ANISOU 4893 C LEU B 208 9838 12759 9501 -1222 577 102 C ATOM 4894 O LEU B 208 -53.729 15.070 34.953 1.00 84.09 O ANISOU 4894 O LEU B 208 9741 12751 9459 -1066 581 27 O ATOM 4895 CB LEU B 208 -54.881 14.248 31.990 1.00 81.12 C ANISOU 4895 CB LEU B 208 9256 12492 9073 -966 701 0 C ATOM 4896 CG LEU B 208 -53.739 13.228 32.182 1.00 86.85 C ANISOU 4896 CG LEU B 208 9736 13569 9694 -774 726 -128 C ATOM 4897 CD1 LEU B 208 -54.157 12.060 33.080 1.00 86.07 C ANISOU 4897 CD1 LEU B 208 9735 13231 9737 -446 731 -240 C ATOM 4898 CD2 LEU B 208 -53.259 12.703 30.845 1.00 89.85 C ANISOU 4898 CD2 LEU B 208 9881 14336 9921 -721 773 -204 C ATOM 4899 N ILE B 209 -53.674 16.829 33.511 1.00 81.70 N ANISOU 4899 N ILE B 209 9484 12522 9037 -1568 501 230 N ATOM 4900 CA ILE B 209 -52.516 17.496 34.124 1.00 82.88 C ANISOU 4900 CA ILE B 209 9553 12876 9063 -1811 419 284 C ATOM 4901 C ILE B 209 -52.880 18.044 35.507 1.00 85.04 C ANISOU 4901 C ILE B 209 10073 12791 9446 -1797 337 268 C ATOM 4902 O ILE B 209 -52.294 17.608 36.497 1.00 85.07 O ANISOU 4902 O ILE B 209 9999 12895 9430 -1687 337 195 O ATOM 4903 CB ILE B 209 -51.829 18.563 33.210 1.00 88.36 C ANISOU 4903 CB ILE B 209 10179 13812 9583 -2248 342 452 C ATOM 4904 CG1 ILE B 209 -51.323 17.949 31.887 1.00 89.84 C ANISOU 4904 CG1 ILE B 209 10061 14472 9603 -2253 442 447 C ATOM 4905 CG2 ILE B 209 -50.690 19.289 33.953 1.00 91.03 C ANISOU 4905 CG2 ILE B 209 10453 14334 9802 -2543 234 514 C ATOM 4906 CD1 ILE B 209 -51.021 18.983 30.764 1.00 99.90 C ANISOU 4906 CD1 ILE B 209 11317 15937 10703 -2696 379 652 C ATOM 4907 N LEU B 210 -53.844 18.984 35.567 1.00 79.92 N ANISOU 4907 N LEU B 210 9720 11744 8900 -1881 257 324 N ATOM 4908 CA LEU B 210 -54.294 19.635 36.800 1.00 79.05 C ANISOU 4908 CA LEU B 210 9865 11293 8876 -1851 167 282 C ATOM 4909 C LEU B 210 -54.669 18.690 37.966 1.00 79.48 C ANISOU 4909 C LEU B 210 9916 11274 9007 -1520 257 148 C ATOM 4910 O LEU B 210 -54.122 18.903 39.048 1.00 79.50 O ANISOU 4910 O LEU B 210 9947 11294 8966 -1549 198 111 O ATOM 4911 CB LEU B 210 -55.356 20.716 36.529 1.00 79.35 C ANISOU 4911 CB LEU B 210 10210 10930 9009 -1918 57 329 C ATOM 4912 CG LEU B 210 -55.078 22.118 37.094 1.00 85.96 C ANISOU 4912 CG LEU B 210 11300 11540 9820 -2175 -155 375 C ATOM 4913 CD1 LEU B 210 -53.905 22.797 36.379 1.00 88.39 C ANISOU 4913 CD1 LEU B 210 11529 12083 9970 -2616 -267 543 C ATOM 4914 CD2 LEU B 210 -56.305 22.992 36.963 1.00 88.66 C ANISOU 4914 CD2 LEU B 210 11965 11443 10280 -2101 -270 365 C ATOM 4915 N PRO B 211 -55.502 17.620 37.810 1.00 73.27 N ANISOU 4915 N PRO B 211 9094 10430 8314 -1238 384 86 N ATOM 4916 CA PRO B 211 -55.749 16.734 38.961 1.00 71.58 C ANISOU 4916 CA PRO B 211 8890 10166 8142 -989 446 0 C ATOM 4917 C PRO B 211 -54.569 15.814 39.274 1.00 74.50 C ANISOU 4917 C PRO B 211 9047 10843 8419 -915 463 -29 C ATOM 4918 O PRO B 211 -54.329 15.540 40.446 1.00 73.95 O ANISOU 4918 O PRO B 211 9008 10764 8326 -822 445 -66 O ATOM 4919 CB PRO B 211 -57.007 15.954 38.570 1.00 71.84 C ANISOU 4919 CB PRO B 211 8962 10040 8294 -782 548 -28 C ATOM 4920 CG PRO B 211 -57.099 16.047 37.108 1.00 76.21 C ANISOU 4920 CG PRO B 211 9443 10664 8850 -868 559 18 C ATOM 4921 CD PRO B 211 -56.229 17.155 36.608 1.00 73.71 C ANISOU 4921 CD PRO B 211 9108 10470 8428 -1159 458 102 C ATOM 4922 N GLY B 212 -53.828 15.392 38.239 1.00 70.93 N ANISOU 4922 N GLY B 212 8376 10681 7894 -946 486 -19 N ATOM 4923 CA GLY B 212 -52.645 14.541 38.357 1.00 71.46 C ANISOU 4923 CA GLY B 212 8202 11093 7855 -837 485 -73 C ATOM 4924 C GLY B 212 -51.605 15.120 39.292 1.00 76.21 C ANISOU 4924 C GLY B 212 8747 11862 8349 -984 392 -62 C ATOM 4925 O GLY B 212 -51.030 14.396 40.111 1.00 76.56 O ANISOU 4925 O GLY B 212 8711 12026 8354 -806 371 -119 O ATOM 4926 N ILE B 213 -51.410 16.451 39.211 1.00 72.67 N ANISOU 4926 N ILE B 213 8371 11387 7852 -1315 312 18 N ATOM 4927 CA ILE B 213 -50.507 17.213 40.066 1.00 73.49 C ANISOU 4927 CA ILE B 213 8463 11606 7855 -1528 195 37 C ATOM 4928 C ILE B 213 -51.056 17.264 41.497 1.00 74.75 C ANISOU 4928 C ILE B 213 8851 11469 8080 -1388 161 -20 C ATOM 4929 O ILE B 213 -50.303 16.992 42.431 1.00 75.77 O ANISOU 4929 O ILE B 213 8900 11759 8131 -1337 112 -60 O ATOM 4930 CB ILE B 213 -50.210 18.606 39.435 1.00 78.45 C ANISOU 4930 CB ILE B 213 9147 12245 8416 -1957 90 155 C ATOM 4931 CG1 ILE B 213 -48.958 18.539 38.530 1.00 81.42 C ANISOU 4931 CG1 ILE B 213 9172 13152 8610 -2170 95 213 C ATOM 4932 CG2 ILE B 213 -50.046 19.719 40.480 1.00 80.20 C ANISOU 4932 CG2 ILE B 213 9585 12265 8621 -2174 -69 167 C ATOM 4933 CD1 ILE B 213 -49.162 18.011 37.103 1.00 88.62 C ANISOU 4933 CD1 ILE B 213 9924 14249 9499 -2109 210 232 C ATOM 4934 N VAL B 214 -52.369 17.570 41.663 1.00 67.74 N ANISOU 4934 N VAL B 214 8227 10193 7319 -1307 190 -32 N ATOM 4935 CA VAL B 214 -53.052 17.630 42.965 1.00 65.90 C ANISOU 4935 CA VAL B 214 8200 9717 7124 -1161 181 -98 C ATOM 4936 C VAL B 214 -52.907 16.277 43.686 1.00 68.69 C ANISOU 4936 C VAL B 214 8454 10187 7460 -888 252 -134 C ATOM 4937 O VAL B 214 -52.463 16.246 44.834 1.00 68.70 O ANISOU 4937 O VAL B 214 8480 10241 7382 -855 195 -166 O ATOM 4938 CB VAL B 214 -54.532 18.081 42.821 1.00 67.74 C ANISOU 4938 CB VAL B 214 8663 9599 7477 -1086 218 -119 C ATOM 4939 CG1 VAL B 214 -55.313 17.866 44.110 1.00 67.09 C ANISOU 4939 CG1 VAL B 214 8723 9364 7403 -886 255 -200 C ATOM 4940 CG2 VAL B 214 -54.628 19.535 42.380 1.00 68.55 C ANISOU 4940 CG2 VAL B 214 8936 9522 7588 -1334 84 -91 C ATOM 4941 N ILE B 215 -53.225 15.170 42.970 1.00 63.78 N ANISOU 4941 N ILE B 215 7734 9599 6901 -704 350 -126 N ATOM 4942 CA ILE B 215 -53.132 13.771 43.412 1.00 62.74 C ANISOU 4942 CA ILE B 215 7544 9525 6770 -442 386 -143 C ATOM 4943 C ILE B 215 -51.688 13.414 43.816 1.00 68.52 C ANISOU 4943 C ILE B 215 8084 10576 7376 -409 299 -166 C ATOM 4944 O ILE B 215 -51.490 12.816 44.876 1.00 68.94 O ANISOU 4944 O ILE B 215 8179 10631 7385 -261 259 -172 O ATOM 4945 CB ILE B 215 -53.712 12.827 42.314 1.00 64.33 C ANISOU 4945 CB ILE B 215 7700 9675 7068 -297 469 -144 C ATOM 4946 CG1 ILE B 215 -55.260 12.887 42.285 1.00 62.71 C ANISOU 4946 CG1 ILE B 215 7684 9162 6982 -273 551 -124 C ATOM 4947 CG2 ILE B 215 -53.212 11.386 42.464 1.00 65.42 C ANISOU 4947 CG2 ILE B 215 7753 9914 7190 -41 447 -173 C ATOM 4948 CD1 ILE B 215 -55.922 12.579 40.948 1.00 65.23 C ANISOU 4948 CD1 ILE B 215 7971 9421 7394 -252 614 -122 C ATOM 4949 N LEU B 216 -50.690 13.783 42.984 1.00 66.29 N ANISOU 4949 N LEU B 216 7578 10594 7016 -553 264 -171 N ATOM 4950 CA LEU B 216 -49.286 13.503 43.294 1.00 68.50 C ANISOU 4950 CA LEU B 216 7617 11253 7158 -525 179 -206 C ATOM 4951 C LEU B 216 -48.808 14.282 44.503 1.00 73.94 C ANISOU 4951 C LEU B 216 8371 11965 7760 -682 76 -197 C ATOM 4952 O LEU B 216 -48.027 13.748 45.290 1.00 74.69 O ANISOU 4952 O LEU B 216 8363 12249 7766 -546 1 -228 O ATOM 4953 CB LEU B 216 -48.353 13.813 42.109 1.00 70.22 C ANISOU 4953 CB LEU B 216 7540 11863 7276 -689 178 -209 C ATOM 4954 CG LEU B 216 -48.144 12.751 41.030 1.00 75.38 C ANISOU 4954 CG LEU B 216 7991 12727 7924 -449 239 -279 C ATOM 4955 CD1 LEU B 216 -46.910 13.076 40.215 1.00 77.74 C ANISOU 4955 CD1 LEU B 216 7928 13564 8046 -611 223 -298 C ATOM 4956 CD2 LEU B 216 -48.030 11.337 41.616 1.00 78.57 C ANISOU 4956 CD2 LEU B 216 8401 13098 8355 -36 202 -362 C ATOM 4957 N SER B 217 -49.256 15.554 44.629 1.00 70.43 N ANISOU 4957 N SER B 217 8105 11322 7334 -955 48 -164 N ATOM 4958 CA SER B 217 -48.881 16.453 45.715 1.00 71.36 C ANISOU 4958 CA SER B 217 8327 11416 7369 -1133 -72 -177 C ATOM 4959 C SER B 217 -49.284 15.869 47.068 1.00 76.92 C ANISOU 4959 C SER B 217 9182 11980 8062 -896 -73 -216 C ATOM 4960 O SER B 217 -48.424 15.728 47.936 1.00 78.09 O ANISOU 4960 O SER B 217 9248 12329 8094 -878 -169 -239 O ATOM 4961 CB SER B 217 -49.479 17.841 45.505 1.00 72.42 C ANISOU 4961 CB SER B 217 8690 11277 7551 -1410 -121 -156 C ATOM 4962 OG SER B 217 -48.818 18.522 44.454 1.00 73.06 O ANISOU 4962 OG SER B 217 8634 11540 7585 -1719 -171 -85 O ATOM 4963 N CYS B 218 -50.567 15.457 47.207 1.00 73.26 N ANISOU 4963 N CYS B 218 8913 11219 7703 -721 32 -214 N ATOM 4964 CA CYS B 218 -51.138 14.852 48.410 1.00 73.88 C ANISOU 4964 CA CYS B 218 9142 11174 7754 -523 55 -222 C ATOM 4965 C CYS B 218 -50.352 13.626 48.849 1.00 80.22 C ANISOU 4965 C CYS B 218 9812 12180 8487 -315 10 -197 C ATOM 4966 O CYS B 218 -49.854 13.614 49.970 1.00 81.30 O ANISOU 4966 O CYS B 218 9974 12413 8504 -289 -78 -207 O ATOM 4967 CB CYS B 218 -52.614 14.531 48.206 1.00 72.94 C ANISOU 4967 CB CYS B 218 9184 10780 7750 -409 188 -204 C ATOM 4968 SG CYS B 218 -53.664 15.991 47.989 1.00 76.67 S ANISOU 4968 SG CYS B 218 9851 10994 8286 -568 206 -262 S ATOM 4969 N TYR B 219 -50.170 12.637 47.950 1.00 77.36 N ANISOU 4969 N TYR B 219 9312 11891 8190 -156 46 -180 N ATOM 4970 CA TYR B 219 -49.392 11.426 48.234 1.00 78.63 C ANISOU 4970 CA TYR B 219 9361 12221 8296 95 -33 -177 C ATOM 4971 C TYR B 219 -47.912 11.659 48.502 1.00 85.47 C ANISOU 4971 C TYR B 219 9988 13464 9021 61 -164 -223 C ATOM 4972 O TYR B 219 -47.325 10.905 49.272 1.00 86.62 O ANISOU 4972 O TYR B 219 10105 13721 9085 260 -268 -221 O ATOM 4973 CB TYR B 219 -49.603 10.353 47.163 1.00 79.25 C ANISOU 4973 CB TYR B 219 9377 12256 8477 298 13 -184 C ATOM 4974 CG TYR B 219 -50.929 9.643 47.316 1.00 79.60 C ANISOU 4974 CG TYR B 219 9668 11950 8628 397 89 -118 C ATOM 4975 CD1 TYR B 219 -51.845 9.603 46.272 1.00 79.98 C ANISOU 4975 CD1 TYR B 219 9755 11829 8806 362 198 -118 C ATOM 4976 CD2 TYR B 219 -51.285 9.043 48.521 1.00 80.89 C ANISOU 4976 CD2 TYR B 219 10016 11975 8742 493 46 -41 C ATOM 4977 CE1 TYR B 219 -53.076 8.965 46.415 1.00 80.00 C ANISOU 4977 CE1 TYR B 219 9957 11544 8895 415 263 -51 C ATOM 4978 CE2 TYR B 219 -52.523 8.431 48.686 1.00 80.96 C ANISOU 4978 CE2 TYR B 219 10232 11705 8823 521 119 43 C ATOM 4979 CZ TYR B 219 -53.413 8.386 47.628 1.00 87.12 C ANISOU 4979 CZ TYR B 219 11029 12332 9741 479 226 34 C ATOM 4980 OH TYR B 219 -54.619 7.753 47.796 1.00 87.33 O ANISOU 4980 OH TYR B 219 11233 12120 9827 479 288 122 O ATOM 4981 N CYS B 220 -47.316 12.703 47.895 1.00 83.68 N ANISOU 4981 N CYS B 220 9595 13443 8755 -207 -175 -252 N ATOM 4982 CA CYS B 220 -45.916 13.062 48.107 1.00 86.80 C ANISOU 4982 CA CYS B 220 9728 14251 9000 -315 -299 -289 C ATOM 4983 C CYS B 220 -45.729 13.550 49.543 1.00 89.60 C ANISOU 4983 C CYS B 220 10218 14572 9254 -396 -406 -288 C ATOM 4984 O CYS B 220 -44.715 13.231 50.163 1.00 91.58 O ANISOU 4984 O CYS B 220 10304 15114 9378 -310 -530 -314 O ATOM 4985 CB CYS B 220 -45.459 14.107 47.088 1.00 88.99 C ANISOU 4985 CB CYS B 220 9829 14733 9250 -658 -285 -284 C ATOM 4986 SG CYS B 220 -43.805 14.796 47.394 1.00 96.94 S ANISOU 4986 SG CYS B 220 10509 16274 10052 -921 -443 -306 S ATOM 4987 N ILE B 221 -46.715 14.295 50.075 1.00 83.10 N ANISOU 4987 N ILE B 221 9686 13415 8473 -532 -367 -275 N ATOM 4988 CA ILE B 221 -46.670 14.803 51.446 1.00 83.38 C ANISOU 4988 CA ILE B 221 9879 13404 8396 -597 -462 -300 C ATOM 4989 C ILE B 221 -46.997 13.679 52.452 1.00 86.30 C ANISOU 4989 C ILE B 221 10368 13701 8722 -293 -463 -263 C ATOM 4990 O ILE B 221 -46.332 13.580 53.485 1.00 87.52 O ANISOU 4990 O ILE B 221 10503 14019 8731 -252 -587 -273 O ATOM 4991 CB ILE B 221 -47.513 16.102 51.647 1.00 85.91 C ANISOU 4991 CB ILE B 221 10458 13434 8751 -832 -447 -338 C ATOM 4992 CG1 ILE B 221 -47.203 17.157 50.550 1.00 86.43 C ANISOU 4992 CG1 ILE B 221 10447 13527 8867 -1151 -476 -335 C ATOM 4993 CG2 ILE B 221 -47.243 16.701 53.037 1.00 89.11 C ANISOU 4993 CG2 ILE B 221 10995 13858 9006 -907 -576 -403 C ATOM 4994 CD1 ILE B 221 -48.305 18.214 50.272 1.00 89.66 C ANISOU 4994 CD1 ILE B 221 11135 13556 9375 -1297 -447 -360 C ATOM 4995 N ILE B 222 -47.998 12.825 52.130 1.00 80.76 N ANISOU 4995 N ILE B 222 9791 12763 8133 -104 -342 -206 N ATOM 4996 CA ILE B 222 -48.437 11.684 52.947 1.00 80.27 C ANISOU 4996 CA ILE B 222 9875 12590 8035 139 -345 -128 C ATOM 4997 C ILE B 222 -47.264 10.734 53.191 1.00 86.71 C ANISOU 4997 C ILE B 222 10526 13651 8768 357 -498 -113 C ATOM 4998 O ILE B 222 -46.947 10.442 54.347 1.00 88.17 O ANISOU 4998 O ILE B 222 10785 13901 8814 439 -607 -77 O ATOM 4999 CB ILE B 222 -49.667 10.952 52.322 1.00 81.14 C ANISOU 4999 CB ILE B 222 10119 12415 8294 244 -203 -62 C ATOM 5000 CG1 ILE B 222 -50.947 11.811 52.412 1.00 79.80 C ANISOU 5000 CG1 ILE B 222 10126 12025 8168 85 -67 -79 C ATOM 5001 CG2 ILE B 222 -49.893 9.566 52.968 1.00 82.56 C ANISOU 5001 CG2 ILE B 222 10430 12498 8439 475 -252 51 C ATOM 5002 CD1 ILE B 222 -52.046 11.454 51.355 1.00 82.17 C ANISOU 5002 CD1 ILE B 222 10472 12108 8642 110 75 -47 C ATOM 5003 N ILE B 223 -46.598 10.291 52.105 1.00 83.71 N ANISOU 5003 N ILE B 223 9915 13435 8454 463 -517 -155 N ATOM 5004 CA ILE B 223 -45.462 9.369 52.194 1.00 86.02 C ANISOU 5004 CA ILE B 223 10020 13992 8673 732 -675 -180 C ATOM 5005 C ILE B 223 -44.215 9.971 52.871 1.00 92.41 C ANISOU 5005 C ILE B 223 10620 15184 9309 639 -821 -235 C ATOM 5006 O ILE B 223 -43.333 9.222 53.293 1.00 94.36 O ANISOU 5006 O ILE B 223 10743 15647 9462 888 -980 -249 O ATOM 5007 CB ILE B 223 -45.179 8.562 50.893 1.00 89.25 C ANISOU 5007 CB ILE B 223 10249 14481 9180 949 -660 -241 C ATOM 5008 CG1 ILE B 223 -44.467 9.388 49.814 1.00 90.33 C ANISOU 5008 CG1 ILE B 223 10058 14962 9302 757 -609 -337 C ATOM 5009 CG2 ILE B 223 -46.425 7.848 50.360 1.00 87.50 C ANISOU 5009 CG2 ILE B 223 10268 13858 9119 1045 -552 -182 C ATOM 5010 CD1 ILE B 223 -43.020 8.981 49.626 1.00103.90 C ANISOU 5010 CD1 ILE B 223 11412 17168 10897 949 -748 -437 C ATOM 5011 N SER B 224 -44.168 11.316 52.997 1.00 88.57 N ANISOU 5011 N SER B 224 10113 14761 8780 286 -791 -267 N ATOM 5012 CA SER B 224 -43.088 12.029 53.679 1.00 90.57 C ANISOU 5012 CA SER B 224 10199 15345 8867 120 -938 -316 C ATOM 5013 C SER B 224 -43.314 11.976 55.199 1.00 93.31 C ANISOU 5013 C SER B 224 10784 15579 9092 169 -1026 -279 C ATOM 5014 O SER B 224 -42.374 11.679 55.934 1.00 95.16 O ANISOU 5014 O SER B 224 10892 16084 9180 277 -1193 -291 O ATOM 5015 CB SER B 224 -42.992 13.473 53.192 1.00 94.90 C ANISOU 5015 CB SER B 224 10689 15948 9422 -303 -905 -357 C ATOM 5016 OG SER B 224 -42.666 13.538 51.812 1.00104.20 O ANISOU 5016 OG SER B 224 11619 17303 10667 -380 -835 -372 O ATOM 5017 N LYS B 225 -44.569 12.215 55.654 1.00 87.02 N ANISOU 5017 N LYS B 225 10311 14418 8336 110 -914 -237 N ATOM 5018 CA LYS B 225 -44.997 12.171 57.061 1.00 86.96 C ANISOU 5018 CA LYS B 225 10547 14306 8189 147 -958 -199 C ATOM 5019 C LYS B 225 -44.900 10.761 57.654 1.00 90.79 C ANISOU 5019 C LYS B 225 11097 14786 8612 469 -1041 -85 C ATOM 5020 O LYS B 225 -44.549 10.620 58.826 1.00 92.26 O ANISOU 5020 O LYS B 225 11354 15081 8618 522 -1169 -54 O ATOM 5021 CB LYS B 225 -46.433 12.709 57.214 1.00 87.54 C ANISOU 5021 CB LYS B 225 10899 14047 8317 33 -791 -198 C ATOM 5022 CG LYS B 225 -46.513 14.121 57.787 1.00104.66 C ANISOU 5022 CG LYS B 225 13165 16207 10395 -225 -824 -317 C ATOM 5023 CD LYS B 225 -46.310 15.196 56.716 1.00115.15 C ANISOU 5023 CD LYS B 225 14393 17512 11845 -481 -811 -398 C ATOM 5024 CE LYS B 225 -45.918 16.525 57.313 1.00126.14 C ANISOU 5024 CE LYS B 225 15856 18943 13127 -747 -944 -518 C ATOM 5025 NZ LYS B 225 -45.598 17.524 56.259 1.00132.77 N ANISOU 5025 NZ LYS B 225 16613 19761 14072 -1038 -974 -556 N ATOM 5026 N LEU B 226 -45.205 9.728 56.842 1.00 85.64 N ANISOU 5026 N LEU B 226 10445 13993 8102 679 -991 -22 N ATOM 5027 CA LEU B 226 -45.153 8.319 57.234 1.00 86.41 C ANISOU 5027 CA LEU B 226 10652 14006 8172 991 -1103 95 C ATOM 5028 C LEU B 226 -43.716 7.810 57.446 1.00 92.10 C ANISOU 5028 C LEU B 226 11146 15057 8791 1220 -1335 53 C ATOM 5029 O LEU B 226 -42.743 8.435 57.018 1.00 92.08 O ANISOU 5029 O LEU B 226 10835 15390 8763 1142 -1379 -72 O ATOM 5030 CB LEU B 226 -45.877 7.461 56.182 1.00 85.06 C ANISOU 5030 CB LEU B 226 10555 13565 8197 1128 -1006 141 C ATOM 5031 CG LEU B 226 -47.298 6.974 56.521 1.00 88.65 C ANISOU 5031 CG LEU B 226 11337 13656 8692 1087 -891 290 C ATOM 5032 CD1 LEU B 226 -48.310 8.103 56.460 1.00 86.38 C ANISOU 5032 CD1 LEU B 226 11112 13275 8434 799 -680 248 C ATOM 5033 CD2 LEU B 226 -47.741 5.883 55.557 1.00 90.92 C ANISOU 5033 CD2 LEU B 226 11693 13699 9153 1265 -879 338 C ATOM 5034 N ASN B1002 -44.793 4.063 66.469 1.00 93.97 N ANISOU 5034 N ASN B1002 12080 14047 9577 -616 469 1699 N ATOM 5035 CA ASN B1002 -46.215 3.965 66.821 1.00 93.48 C ANISOU 5035 CA ASN B1002 12042 14005 9471 -501 388 1823 C ATOM 5036 C ASN B1002 -46.492 4.264 68.305 1.00 96.46 C ANISOU 5036 C ASN B1002 12417 14299 9936 -346 330 1823 C ATOM 5037 O ASN B1002 -47.361 5.084 68.606 1.00 95.84 O ANISOU 5037 O ASN B1002 12378 14196 9842 -254 286 1923 O ATOM 5038 CB ASN B1002 -46.824 2.625 66.370 1.00 95.93 C ANISOU 5038 CB ASN B1002 12299 14427 9724 -526 374 1798 C ATOM 5039 CG ASN B1002 -46.087 1.393 66.854 1.00126.86 C ANISOU 5039 CG ASN B1002 16139 18324 13737 -522 373 1635 C ATOM 5040 OD1 ASN B1002 -46.172 1.003 68.029 1.00122.18 O ANISOU 5040 OD1 ASN B1002 15528 17672 13223 -427 311 1621 O ATOM 5041 ND2 ASN B1002 -45.365 0.739 65.949 1.00119.34 N ANISOU 5041 ND2 ASN B1002 15142 17423 12777 -626 431 1503 N ATOM 5042 N ILE B1003 -45.753 3.604 69.224 1.00 92.79 N ANISOU 5042 N ILE B1003 11901 13795 9559 -315 320 1703 N ATOM 5043 CA ILE B1003 -45.837 3.830 70.676 1.00 91.99 C ANISOU 5043 CA ILE B1003 11804 13635 9511 -197 267 1686 C ATOM 5044 C ILE B1003 -45.181 5.188 71.016 1.00 96.85 C ANISOU 5044 C ILE B1003 12472 14139 10187 -178 277 1663 C ATOM 5045 O ILE B1003 -45.685 5.909 71.876 1.00 96.72 O ANISOU 5045 O ILE B1003 12490 14083 10177 -71 241 1685 O ATOM 5046 CB ILE B1003 -45.282 2.630 71.522 1.00 94.30 C ANISOU 5046 CB ILE B1003 12045 13917 9866 -184 217 1591 C ATOM 5047 CG1 ILE B1003 -45.537 2.832 73.046 1.00 94.32 C ANISOU 5047 CG1 ILE B1003 12069 13899 9868 -84 157 1598 C ATOM 5048 CG2 ILE B1003 -43.806 2.307 71.199 1.00 95.16 C ANISOU 5048 CG2 ILE B1003 12103 13972 10082 -253 237 1445 C ATOM 5049 CD1 ILE B1003 -45.244 1.635 73.963 1.00100.13 C ANISOU 5049 CD1 ILE B1003 12784 14628 10633 -82 71 1563 C ATOM 5050 N PHE B1004 -44.079 5.535 70.309 1.00 93.99 N ANISOU 5050 N PHE B1004 12109 13735 9867 -294 330 1608 N ATOM 5051 CA PHE B1004 -43.344 6.791 70.460 1.00 94.57 C ANISOU 5051 CA PHE B1004 12234 13694 10006 -326 338 1593 C ATOM 5052 C PHE B1004 -44.262 7.968 70.153 1.00 99.77 C ANISOU 5052 C PHE B1004 12994 14290 10625 -285 307 1733 C ATOM 5053 O PHE B1004 -44.308 8.922 70.929 1.00 99.64 O ANISOU 5053 O PHE B1004 13030 14157 10672 -200 259 1723 O ATOM 5054 CB PHE B1004 -42.089 6.787 69.563 1.00 97.08 C ANISOU 5054 CB PHE B1004 12509 14027 10351 -501 420 1518 C ATOM 5055 CG PHE B1004 -41.305 8.078 69.494 1.00 99.74 C ANISOU 5055 CG PHE B1004 12900 14254 10744 -593 438 1524 C ATOM 5056 CD1 PHE B1004 -40.437 8.440 70.518 1.00102.95 C ANISOU 5056 CD1 PHE B1004 13278 14566 11271 -563 403 1411 C ATOM 5057 CD2 PHE B1004 -41.406 8.912 68.386 1.00102.91 C ANISOU 5057 CD2 PHE B1004 13387 14644 11072 -732 476 1651 C ATOM 5058 CE1 PHE B1004 -39.703 9.628 70.445 1.00105.17 C ANISOU 5058 CE1 PHE B1004 13609 14735 11614 -670 412 1414 C ATOM 5059 CE2 PHE B1004 -40.677 10.102 68.317 1.00107.13 C ANISOU 5059 CE2 PHE B1004 13985 15057 11662 -847 479 1676 C ATOM 5060 CZ PHE B1004 -39.828 10.450 69.345 1.00105.47 C ANISOU 5060 CZ PHE B1004 13739 14749 11588 -817 451 1550 C ATOM 5061 N GLU B1005 -45.036 7.853 69.060 1.00 97.54 N ANISOU 5061 N GLU B1005 12736 14082 10244 -331 316 1854 N ATOM 5062 CA GLU B1005 -46.012 8.837 68.588 1.00 98.86 C ANISOU 5062 CA GLU B1005 12990 14193 10377 -286 254 2007 C ATOM 5063 C GLU B1005 -47.091 9.069 69.651 1.00103.71 C ANISOU 5063 C GLU B1005 13587 14789 11029 -76 184 2002 C ATOM 5064 O GLU B1005 -47.503 10.208 69.867 1.00104.16 O ANISOU 5064 O GLU B1005 13709 14722 11147 17 117 2045 O ATOM 5065 CB GLU B1005 -46.651 8.363 67.269 1.00100.56 C ANISOU 5065 CB GLU B1005 13213 14534 10462 -378 261 2122 C ATOM 5066 CG GLU B1005 -45.648 7.934 66.210 1.00112.18 C ANISOU 5066 CG GLU B1005 14678 16086 11861 -593 356 2087 C ATOM 5067 CD GLU B1005 -45.102 9.037 65.327 1.00135.31 C ANISOU 5067 CD GLU B1005 17717 18945 14749 -761 367 2193 C ATOM 5068 OE1 GLU B1005 -44.277 9.844 65.814 1.00128.07 O ANISOU 5068 OE1 GLU B1005 16834 17896 13933 -791 373 2158 O ATOM 5069 OE2 GLU B1005 -45.469 9.066 64.130 1.00132.82 O ANISOU 5069 OE2 GLU B1005 17458 18715 14292 -884 365 2316 O ATOM 5070 N MET B1006 -47.512 7.985 70.333 1.00100.37 N ANISOU 5070 N MET B1006 13072 14489 10574 -10 200 1941 N ATOM 5071 CA MET B1006 -48.511 7.988 71.401 1.00100.66 C ANISOU 5071 CA MET B1006 13062 14573 10610 155 166 1917 C ATOM 5072 C MET B1006 -48.034 8.837 72.593 1.00105.91 C ANISOU 5072 C MET B1006 13761 15124 11358 247 149 1807 C ATOM 5073 O MET B1006 -48.798 9.658 73.103 1.00106.37 O ANISOU 5073 O MET B1006 13824 15147 11445 390 110 1792 O ATOM 5074 CB MET B1006 -48.811 6.538 71.835 1.00101.97 C ANISOU 5074 CB MET B1006 13142 14893 10710 138 190 1889 C ATOM 5075 CG MET B1006 -49.744 6.423 73.011 1.00105.70 C ANISOU 5075 CG MET B1006 13557 15458 11148 260 179 1861 C ATOM 5076 SD MET B1006 -49.631 4.825 73.826 1.00109.10 S ANISOU 5076 SD MET B1006 13932 16005 11514 193 185 1832 S ATOM 5077 CE MET B1006 -51.330 4.635 74.345 1.00106.48 C ANISOU 5077 CE MET B1006 13507 15865 11086 270 194 1885 C ATOM 5078 N LEU B1007 -46.773 8.646 73.018 1.00102.77 N ANISOU 5078 N LEU B1007 13374 14671 11003 171 169 1714 N ATOM 5079 CA LEU B1007 -46.190 9.374 74.144 1.00103.38 C ANISOU 5079 CA LEU B1007 13485 14646 11150 233 142 1597 C ATOM 5080 C LEU B1007 -45.670 10.762 73.770 1.00109.21 C ANISOU 5080 C LEU B1007 14316 15189 11988 208 111 1602 C ATOM 5081 O LEU B1007 -45.457 11.596 74.651 1.00109.58 O ANISOU 5081 O LEU B1007 14404 15129 12103 285 71 1504 O ATOM 5082 CB LEU B1007 -45.148 8.523 74.871 1.00102.74 C ANISOU 5082 CB LEU B1007 13364 14595 11077 173 145 1496 C ATOM 5083 CG LEU B1007 -45.741 7.567 75.908 1.00107.37 C ANISOU 5083 CG LEU B1007 13901 15321 11574 238 129 1474 C ATOM 5084 CD1 LEU B1007 -46.070 6.208 75.300 1.00106.78 C ANISOU 5084 CD1 LEU B1007 13770 15359 11442 169 145 1551 C ATOM 5085 CD2 LEU B1007 -44.803 7.391 77.069 1.00110.71 C ANISOU 5085 CD2 LEU B1007 14330 15717 12018 234 81 1362 C ATOM 5086 N ARG B1008 -45.518 11.017 72.456 1.00106.75 N ANISOU 5086 N ARG B1008 14049 14836 11677 89 123 1720 N ATOM 5087 CA ARG B1008 -45.114 12.301 71.883 1.00108.36 C ANISOU 5087 CA ARG B1008 14363 14850 11959 20 81 1781 C ATOM 5088 C ARG B1008 -46.288 13.286 72.044 1.00115.32 C ANISOU 5088 C ARG B1008 15304 15625 12889 196 -15 1831 C ATOM 5089 O ARG B1008 -46.061 14.476 72.264 1.00116.72 O ANISOU 5089 O ARG B1008 15574 15595 13179 226 -88 1812 O ATOM 5090 CB ARG B1008 -44.730 12.096 70.399 1.00107.83 C ANISOU 5090 CB ARG B1008 14322 14825 11824 -184 128 1911 C ATOM 5091 CG ARG B1008 -44.571 13.344 69.534 1.00117.41 C ANISOU 5091 CG ARG B1008 15673 15867 13072 -294 71 2050 C ATOM 5092 CD ARG B1008 -45.778 13.518 68.629 1.00123.57 C ANISOU 5092 CD ARG B1008 16506 16665 13781 -250 0 2229 C ATOM 5093 NE ARG B1008 -45.465 14.309 67.443 1.00128.96 N ANISOU 5093 NE ARG B1008 17322 17248 14430 -443 -39 2406 N ATOM 5094 CZ ARG B1008 -45.200 13.790 66.249 1.00139.72 C ANISOU 5094 CZ ARG B1008 18690 18755 15641 -649 31 2504 C ATOM 5095 NH1 ARG B1008 -45.216 12.475 66.070 1.00119.99 N ANISOU 5095 NH1 ARG B1008 16066 16485 13038 -668 136 2422 N ATOM 5096 NH2 ARG B1008 -44.922 14.583 65.223 1.00129.37 N ANISOU 5096 NH2 ARG B1008 17518 17363 14275 -849 -10 2682 N ATOM 5097 N ILE B1009 -47.534 12.774 71.936 1.00112.55 N ANISOU 5097 N ILE B1009 14885 15410 12469 314 -23 1880 N ATOM 5098 CA ILE B1009 -48.782 13.531 72.080 1.00114.28 C ANISOU 5098 CA ILE B1009 15106 15573 12741 510 -113 1902 C ATOM 5099 C ILE B1009 -49.141 13.693 73.571 1.00120.70 C ANISOU 5099 C ILE B1009 15854 16416 13590 696 -104 1710 C ATOM 5100 O ILE B1009 -49.444 14.804 74.013 1.00122.18 O ANISOU 5100 O ILE B1009 16085 16445 13894 841 -183 1635 O ATOM 5101 CB ILE B1009 -49.938 12.851 71.273 1.00116.94 C ANISOU 5101 CB ILE B1009 15370 16078 12984 535 -122 2029 C ATOM 5102 CG1 ILE B1009 -49.631 12.813 69.755 1.00117.61 C ANISOU 5102 CG1 ILE B1009 15538 16141 13007 345 -142 2214 C ATOM 5103 CG2 ILE B1009 -51.298 13.517 71.549 1.00119.09 C ANISOU 5103 CG2 ILE B1009 15590 16331 13328 768 -215 2016 C ATOM 5104 CD1 ILE B1009 -50.367 11.711 68.964 1.00123.49 C ANISOU 5104 CD1 ILE B1009 16201 17102 13617 294 -115 2304 C ATOM 5105 N ASP B1010 -49.126 12.577 74.327 1.00117.40 N ANISOU 5105 N ASP B1010 15338 16202 13066 686 -18 1631 N ATOM 5106 CA ASP B1010 -49.512 12.528 75.737 1.00118.18 C ANISOU 5106 CA ASP B1010 15370 16398 13134 821 9 1464 C ATOM 5107 C ASP B1010 -48.552 13.208 76.713 1.00125.38 C ANISOU 5107 C ASP B1010 16352 17178 14110 830 -10 1305 C ATOM 5108 O ASP B1010 -49.001 14.007 77.535 1.00126.25 O ANISOU 5108 O ASP B1010 16459 17245 14264 987 -37 1162 O ATOM 5109 CB ASP B1010 -49.830 11.083 76.174 1.00118.24 C ANISOU 5109 CB ASP B1010 15274 16662 12991 769 86 1472 C ATOM 5110 CG ASP B1010 -50.946 10.390 75.402 1.00124.45 C ANISOU 5110 CG ASP B1010 15972 17604 13711 770 100 1598 C ATOM 5111 OD1 ASP B1010 -51.735 11.092 74.727 1.00125.92 O ANISOU 5111 OD1 ASP B1010 16149 17736 13959 863 46 1656 O ATOM 5112 OD2 ASP B1010 -51.040 9.150 75.485 1.00127.30 O ANISOU 5112 OD2 ASP B1010 16275 18128 13967 677 146 1639 O ATOM 5113 N GLU B1011 -47.248 12.884 76.644 1.00123.59 N ANISOU 5113 N GLU B1011 16171 16896 13891 668 2 1308 N ATOM 5114 CA GLU B1011 -46.251 13.443 77.562 1.00125.23 C ANISOU 5114 CA GLU B1011 16434 16992 14158 654 -27 1158 C ATOM 5115 C GLU B1011 -45.406 14.588 76.983 1.00132.26 C ANISOU 5115 C GLU B1011 17434 17619 15199 574 -88 1175 C ATOM 5116 O GLU B1011 -44.693 15.265 77.732 1.00132.99 O ANISOU 5116 O GLU B1011 17578 17587 15364 573 -132 1039 O ATOM 5117 CB GLU B1011 -45.379 12.332 78.169 1.00125.50 C ANISOU 5117 CB GLU B1011 16422 17152 14110 548 3 1116 C ATOM 5118 CG GLU B1011 -45.011 12.582 79.624 1.00139.10 C ANISOU 5118 CG GLU B1011 18160 18889 15803 604 -30 937 C ATOM 5119 CD GLU B1011 -44.137 11.532 80.282 1.00164.06 C ANISOU 5119 CD GLU B1011 21289 22155 18893 507 -44 909 C ATOM 5120 OE1 GLU B1011 -42.995 11.319 79.810 1.00163.54 O ANISOU 5120 OE1 GLU B1011 21219 22007 18912 383 -64 927 O ATOM 5121 OE2 GLU B1011 -44.577 10.955 81.303 1.00157.99 O ANISOU 5121 OE2 GLU B1011 20494 21550 17985 552 -42 862 O ATOM 5122 N GLY B1012 -45.506 14.806 75.674 1.00130.20 N ANISOU 5122 N GLY B1012 17216 17281 14974 490 -99 1344 N ATOM 5123 CA GLY B1012 -44.782 15.871 74.986 1.00131.94 C ANISOU 5123 CA GLY B1012 17555 17260 15317 371 -158 1408 C ATOM 5124 C GLY B1012 -43.341 15.549 74.645 1.00136.21 C ANISOU 5124 C GLY B1012 18089 17800 15863 139 -106 1413 C ATOM 5125 O GLY B1012 -42.664 14.827 75.386 1.00134.60 O ANISOU 5125 O GLY B1012 17807 17707 15628 115 -66 1294 O ATOM 5126 N LEU B1013 -42.864 16.103 73.517 1.00134.66 N ANISOU 5126 N LEU B1013 17973 17485 15707 -39 -115 1553 N ATOM 5127 CA LEU B1013 -41.499 15.909 73.036 1.00135.05 C ANISOU 5127 CA LEU B1013 17998 17552 15765 -284 -49 1554 C ATOM 5128 C LEU B1013 -40.730 17.228 73.019 1.00143.03 C ANISOU 5128 C LEU B1013 19124 18312 16911 -410 -120 1555 C ATOM 5129 O LEU B1013 -41.247 18.246 72.550 1.00144.33 O ANISOU 5129 O LEU B1013 19426 18277 17134 -403 -214 1678 O ATOM 5130 CB LEU B1013 -41.504 15.234 71.646 1.00134.58 C ANISOU 5130 CB LEU B1013 17908 17637 15588 -446 38 1710 C ATOM 5131 CG LEU B1013 -40.155 14.927 70.967 1.00139.36 C ANISOU 5131 CG LEU B1013 18452 18320 16179 -711 140 1695 C ATOM 5132 CD1 LEU B1013 -39.375 13.853 71.709 1.00138.06 C ANISOU 5132 CD1 LEU B1013 18124 18305 16029 -688 200 1506 C ATOM 5133 CD2 LEU B1013 -40.367 14.481 69.543 1.00141.70 C ANISOU 5133 CD2 LEU B1013 18750 18753 16338 -861 217 1847 C ATOM 5134 N ARG B1014 -39.504 17.201 73.566 1.00141.29 N ANISOU 5134 N ARG B1014 18844 18088 16751 -525 -95 1418 N ATOM 5135 CA ARG B1014 -38.583 18.337 73.638 1.00143.90 C ANISOU 5135 CA ARG B1014 19259 18201 17216 -685 -154 1393 C ATOM 5136 C ARG B1014 -37.194 17.844 73.210 1.00149.53 C ANISOU 5136 C ARG B1014 19848 19044 17922 -943 -47 1356 C ATOM 5137 O ARG B1014 -36.662 16.917 73.825 1.00147.76 O ANISOU 5137 O ARG B1014 19473 18985 17685 -901 -2 1205 O ATOM 5138 CB ARG B1014 -38.544 18.949 75.064 1.00144.51 C ANISOU 5138 CB ARG B1014 19370 18136 17402 -524 -259 1195 C ATOM 5139 CG ARG B1014 -39.887 19.463 75.619 1.00154.58 C ANISOU 5139 CG ARG B1014 20732 19303 18696 -249 -353 1166 C ATOM 5140 CD ARG B1014 -40.369 20.760 74.981 1.00165.60 C ANISOU 5140 CD ARG B1014 22305 20406 20211 -258 -472 1299 C ATOM 5141 NE ARG B1014 -39.709 21.942 75.543 1.00174.12 N ANISOU 5141 NE ARG B1014 23491 21204 21461 -314 -586 1190 N ATOM 5142 CZ ARG B1014 -39.848 23.178 75.071 1.00188.16 C ANISOU 5142 CZ ARG B1014 25444 22664 23384 -366 -721 1296 C ATOM 5143 NH1 ARG B1014 -39.215 24.189 75.648 1.00175.83 N ANISOU 5143 NH1 ARG B1014 23978 20843 21988 -425 -831 1177 N ATOM 5144 NH2 ARG B1014 -40.618 23.411 74.014 1.00174.70 N ANISOU 5144 NH2 ARG B1014 23828 20884 21665 -366 -768 1526 N ATOM 5145 N LEU B1015 -36.626 18.434 72.142 1.00149.27 N ANISOU 5145 N LEU B1015 19872 18949 17896 -1212 -11 1495 N ATOM 5146 CA LEU B1015 -35.318 18.034 71.604 1.00150.32 C ANISOU 5146 CA LEU B1015 19864 19236 18017 -1482 114 1449 C ATOM 5147 C LEU B1015 -34.117 18.820 72.173 1.00157.87 C ANISOU 5147 C LEU B1015 20799 20059 19126 -1644 72 1331 C ATOM 5148 O LEU B1015 -33.060 18.892 71.536 1.00158.42 O ANISOU 5148 O LEU B1015 20781 20210 19203 -1928 167 1334 O ATOM 5149 CB LEU B1015 -35.331 18.044 70.061 1.00151.42 C ANISOU 5149 CB LEU B1015 20042 19466 18025 -1724 215 1654 C ATOM 5150 CG LEU B1015 -36.282 17.063 69.367 1.00154.44 C ANISOU 5150 CG LEU B1015 20399 20040 18240 -1615 279 1741 C ATOM 5151 CD1 LEU B1015 -36.495 17.449 67.919 1.00156.28 C ANISOU 5151 CD1 LEU B1015 20746 20297 18336 -1849 322 1979 C ATOM 5152 CD2 LEU B1015 -35.776 15.636 69.461 1.00155.18 C ANISOU 5152 CD2 LEU B1015 20265 20406 18288 -1581 405 1565 C ATOM 5153 N LYS B1016 -34.275 19.377 73.390 1.00156.43 N ANISOU 5153 N LYS B1016 20682 19696 19059 -1471 -65 1206 N ATOM 5154 CA LYS B1016 -33.244 20.140 74.102 1.00158.64 C ANISOU 5154 CA LYS B1016 20952 19832 19491 -1592 -138 1069 C ATOM 5155 C LYS B1016 -33.374 19.928 75.616 1.00163.29 C ANISOU 5155 C LYS B1016 21508 20408 20128 -1336 -239 850 C ATOM 5156 O LYS B1016 -34.484 19.698 76.107 1.00161.57 O ANISOU 5156 O LYS B1016 21352 20190 19845 -1073 -281 843 O ATOM 5157 CB LYS B1016 -33.329 21.636 73.749 1.00163.67 C ANISOU 5157 CB LYS B1016 21809 20149 20231 -1740 -244 1204 C ATOM 5158 CG LYS B1016 -31.992 22.370 73.851 1.00179.10 C ANISOU 5158 CG LYS B1016 23731 22000 22319 -2033 -264 1137 C ATOM 5159 CD LYS B1016 -32.031 23.750 73.193 1.00191.10 C ANISOU 5159 CD LYS B1016 25479 23209 23921 -2254 -358 1335 C ATOM 5160 CE LYS B1016 -31.481 23.761 71.782 1.00201.65 C ANISOU 5160 CE LYS B1016 26797 24663 25158 -2624 -223 1547 C ATOM 5161 NZ LYS B1016 -32.430 23.173 70.796 1.00208.05 N ANISOU 5161 NZ LYS B1016 27650 25615 25782 -2555 -147 1741 N ATOM 5162 N ILE B1017 -32.236 19.998 76.346 1.00162.19 N ANISOU 5162 N ILE B1017 21261 20276 20087 -1429 -277 671 N ATOM 5163 CA ILE B1017 -32.161 19.820 77.805 1.00162.44 C ANISOU 5163 CA ILE B1017 21261 20314 20146 -1235 -386 457 C ATOM 5164 C ILE B1017 -33.006 20.886 78.515 1.00169.39 C ANISOU 5164 C ILE B1017 22347 20943 21069 -1073 -517 417 C ATOM 5165 O ILE B1017 -32.806 22.083 78.293 1.00171.22 O ANISOU 5165 O ILE B1017 22712 20919 21427 -1204 -590 449 O ATOM 5166 CB ILE B1017 -30.690 19.766 78.330 1.00166.78 C ANISOU 5166 CB ILE B1017 21649 20915 20805 -1398 -423 283 C ATOM 5167 CG1 ILE B1017 -29.851 18.694 77.600 1.00166.70 C ANISOU 5167 CG1 ILE B1017 21401 21160 20777 -1534 -292 286 C ATOM 5168 CG2 ILE B1017 -30.635 19.540 79.846 1.00167.18 C ANISOU 5168 CG2 ILE B1017 21682 20989 20850 -1205 -556 77 C ATOM 5169 CD1 ILE B1017 -28.913 19.237 76.533 1.00176.53 C ANISOU 5169 CD1 ILE B1017 22579 22396 22099 -1874 -194 352 C ATOM 5170 N TYR B1018 -33.966 20.437 79.344 1.00166.20 N ANISOU 5170 N TYR B1018 21967 20617 20565 -794 -547 341 N ATOM 5171 CA TYR B1018 -34.886 21.309 80.076 1.00167.84 C ANISOU 5171 CA TYR B1018 22333 20640 20797 -595 -651 255 C ATOM 5172 C TYR B1018 -34.984 20.979 81.573 1.00172.53 C ANISOU 5172 C TYR B1018 22895 21346 21313 -412 -715 25 C ATOM 5173 O TYR B1018 -34.525 19.920 82.008 1.00170.84 O ANISOU 5173 O TYR B1018 22546 21360 21004 -413 -688 -22 O ATOM 5174 CB TYR B1018 -36.280 21.306 79.405 1.00168.58 C ANISOU 5174 CB TYR B1018 22509 20718 20828 -437 -610 414 C ATOM 5175 CG TYR B1018 -36.992 19.968 79.417 1.00168.08 C ANISOU 5175 CG TYR B1018 22333 20946 20584 -292 -509 461 C ATOM 5176 CD1 TYR B1018 -37.916 19.656 80.411 1.00169.49 C ANISOU 5176 CD1 TYR B1018 22508 21232 20657 -48 -524 343 C ATOM 5177 CD2 TYR B1018 -36.790 19.038 78.400 1.00167.43 C ANISOU 5177 CD2 TYR B1018 22151 21033 20430 -411 -396 621 C ATOM 5178 CE1 TYR B1018 -38.589 18.434 80.418 1.00168.19 C ANISOU 5178 CE1 TYR B1018 22249 21325 20329 55 -439 404 C ATOM 5179 CE2 TYR B1018 -37.453 17.810 78.399 1.00166.28 C ANISOU 5179 CE2 TYR B1018 21915 21127 20137 -288 -321 663 C ATOM 5180 CZ TYR B1018 -38.358 17.516 79.407 1.00173.36 C ANISOU 5180 CZ TYR B1018 22817 22113 20939 -63 -347 568 C ATOM 5181 OH TYR B1018 -39.023 16.312 79.408 1.00172.63 O ANISOU 5181 OH TYR B1018 22643 22248 20702 28 -280 626 O ATOM 5182 N LYS B1019 -35.580 21.884 82.342 1.00171.28 N ANISOU 5182 N LYS B1019 22862 21024 21191 -260 -808 -120 N ATOM 5183 CA LYS B1019 -35.738 21.685 83.778 1.00171.51 C ANISOU 5183 CA LYS B1019 22880 21173 21113 -102 -864 -351 C ATOM 5184 C LYS B1019 -37.097 21.074 84.103 1.00175.17 C ANISOU 5184 C LYS B1019 23333 21825 21400 139 -793 -345 C ATOM 5185 O LYS B1019 -38.134 21.711 83.920 1.00175.30 O ANISOU 5185 O LYS B1019 23430 21724 21452 291 -794 -348 O ATOM 5186 CB LYS B1019 -35.564 23.009 84.525 1.00176.49 C ANISOU 5186 CB LYS B1019 23640 21546 21873 -79 -1000 -568 C ATOM 5187 CG LYS B1019 -35.341 22.854 86.020 1.00190.07 C ANISOU 5187 CG LYS B1019 25343 23402 23473 6 -1071 -830 C ATOM 5188 CD LYS B1019 -35.832 24.074 86.782 1.00201.45 C ANISOU 5188 CD LYS B1019 26925 24632 24986 145 -1171 -1074 C ATOM 5189 CE LYS B1019 -34.686 24.784 87.484 1.00212.90 C ANISOU 5189 CE LYS B1019 28416 25935 26542 -1 -1314 -1274 C ATOM 5190 NZ LYS B1019 -34.636 24.455 88.936 1.00221.77 N ANISOU 5190 NZ LYS B1019 29520 27274 27470 93 -1365 -1525 N ATOM 5191 N ASP B1020 -37.084 19.836 84.586 1.00171.10 N ANISOU 5191 N ASP B1020 22710 21596 20704 168 -744 -337 N ATOM 5192 CA ASP B1020 -38.314 19.138 84.938 1.00170.31 C ANISOU 5192 CA ASP B1020 22584 21710 20415 353 -669 -319 C ATOM 5193 C ASP B1020 -39.074 19.887 86.028 1.00176.82 C ANISOU 5193 C ASP B1020 23482 22520 21180 535 -708 -553 C ATOM 5194 O ASP B1020 -38.608 20.910 86.531 1.00178.35 O ANISOU 5194 O ASP B1020 23757 22524 21483 524 -806 -736 O ATOM 5195 CB ASP B1020 -37.998 17.791 85.592 1.00170.76 C ANISOU 5195 CB ASP B1020 22544 22047 20289 327 -659 -306 C ATOM 5196 N THR B1021 -40.254 19.384 86.373 1.00173.52 N ANISOU 5196 N THR B1021 23028 22310 20592 695 -626 -560 N ATOM 5197 CA THR B1021 -41.152 20.071 87.293 1.00175.59 C ANISOU 5197 CA THR B1021 23329 22599 20790 886 -627 -798 C ATOM 5198 C THR B1021 -40.697 19.938 88.743 1.00181.32 C ANISOU 5198 C THR B1021 24069 23487 21338 871 -678 -1021 C ATOM 5199 O THR B1021 -41.202 20.629 89.628 1.00183.16 O ANISOU 5199 O THR B1021 24342 23737 21514 1002 -689 -1278 O ATOM 5200 CB THR B1021 -42.590 19.537 87.166 1.00182.47 C ANISOU 5200 CB THR B1021 24123 23683 21526 1045 -506 -738 C ATOM 5201 OG1 THR B1021 -43.046 19.700 85.817 1.00181.02 O ANISOU 5201 OG1 THR B1021 23933 23348 21499 1063 -482 -533 O ATOM 5202 CG2 THR B1021 -43.522 20.287 88.106 1.00183.08 C ANISOU 5202 CG2 THR B1021 24207 23809 21545 1250 -491 -1024 C ATOM 5203 N GLU B1022 -39.740 19.046 88.979 1.00177.10 N ANISOU 5203 N GLU B1022 23498 23075 20717 713 -718 -932 N ATOM 5204 CA GLU B1022 -39.216 18.821 90.320 1.00178.26 C ANISOU 5204 CA GLU B1022 23666 23384 20679 672 -798 -1104 C ATOM 5205 C GLU B1022 -37.725 19.135 90.391 1.00183.22 C ANISOU 5205 C GLU B1022 24315 23845 21456 509 -942 -1148 C ATOM 5206 O GLU B1022 -37.019 18.645 91.272 1.00183.12 O ANISOU 5206 O GLU B1022 24294 23971 21311 430 -1038 -1209 O ATOM 5207 CB GLU B1022 -39.471 17.378 90.760 1.00178.13 C ANISOU 5207 CB GLU B1022 23588 23694 20401 637 -757 -965 C ATOM 5208 CG GLU B1022 -39.434 17.173 92.266 1.00188.39 C ANISOU 5208 CG GLU B1022 24930 25226 21425 630 -816 -1141 C ATOM 5209 CD GLU B1022 -39.905 18.393 93.033 1.00206.74 C ANISOU 5209 CD GLU B1022 27322 27511 23718 750 -809 -1460 C ATOM 5210 OE1 GLU B1022 -40.844 19.068 92.560 1.00198.50 O ANISOU 5210 OE1 GLU B1022 26269 26375 22777 898 -712 -1523 O ATOM 5211 OE2 GLU B1022 -39.337 18.677 94.108 1.00199.42 O ANISOU 5211 OE2 GLU B1022 26456 26642 22671 703 -914 -1659 O ATOM 5212 N GLY B1023 -37.253 19.953 89.456 1.00180.51 N ANISOU 5212 N GLY B1023 23994 23209 21382 447 -966 -1108 N ATOM 5213 CA GLY B1023 -35.853 20.332 89.411 1.00181.37 C ANISOU 5213 CA GLY B1023 24100 23156 21655 269 -1087 -1149 C ATOM 5214 C GLY B1023 -34.950 19.173 89.037 1.00184.17 C ANISOU 5214 C GLY B1023 24331 23641 22005 127 -1099 -973 C ATOM 5215 O GLY B1023 -34.238 18.631 89.882 1.00184.19 O ANISOU 5215 O GLY B1023 24294 23779 21909 72 -1204 -1042 O ATOM 5216 N TYR B1024 -34.980 18.793 87.764 1.00179.42 N ANISOU 5216 N TYR B1024 23664 22996 21510 72 -1003 -756 N ATOM 5217 CA TYR B1024 -34.159 17.692 87.273 1.00177.78 C ANISOU 5217 CA TYR B1024 23319 22901 21327 -45 -1001 -612 C ATOM 5218 C TYR B1024 -33.986 17.767 85.760 1.00180.68 C ANISOU 5218 C TYR B1024 23635 23154 21861 -149 -897 -437 C ATOM 5219 O TYR B1024 -34.964 17.865 85.018 1.00179.33 O ANISOU 5219 O TYR B1024 23510 22954 21674 -77 -792 -314 O ATOM 5220 CB TYR B1024 -34.774 16.348 87.667 1.00177.46 C ANISOU 5220 CB TYR B1024 23236 23120 21069 48 -971 -517 C ATOM 5221 CG TYR B1024 -34.402 15.888 89.059 1.00180.15 C ANISOU 5221 CG TYR B1024 23587 23617 21244 59 -1110 -636 C ATOM 5222 CD1 TYR B1024 -35.211 15.004 89.759 1.00181.56 C ANISOU 5222 CD1 TYR B1024 23792 24021 21171 145 -1098 -584 C ATOM 5223 CD2 TYR B1024 -33.240 16.339 89.672 1.00182.57 C ANISOU 5223 CD2 TYR B1024 23881 23854 21633 -37 -1263 -789 C ATOM 5224 CE1 TYR B1024 -34.875 14.581 91.031 1.00183.33 C ANISOU 5224 CE1 TYR B1024 24048 24397 21214 130 -1240 -667 C ATOM 5225 CE2 TYR B1024 -32.895 15.921 90.944 1.00184.57 C ANISOU 5225 CE2 TYR B1024 24156 24257 21718 -35 -1414 -887 C ATOM 5226 CZ TYR B1024 -33.716 15.043 91.618 1.00191.23 C ANISOU 5226 CZ TYR B1024 25042 25322 22293 46 -1404 -817 C ATOM 5227 OH TYR B1024 -33.377 14.625 92.884 1.00193.62 O ANISOU 5227 OH TYR B1024 25386 25782 22399 24 -1568 -889 O ATOM 5228 N TYR B1025 -32.737 17.719 85.309 1.00177.75 N ANISOU 5228 N TYR B1025 23158 22737 21640 -328 -929 -431 N ATOM 5229 CA TYR B1025 -32.434 17.784 83.884 1.00177.17 C ANISOU 5229 CA TYR B1025 23025 22594 21699 -470 -820 -280 C ATOM 5230 C TYR B1025 -32.890 16.577 83.059 1.00179.18 C ANISOU 5230 C TYR B1025 23191 23018 21871 -432 -701 -109 C ATOM 5231 O TYR B1025 -32.444 15.460 83.288 1.00177.89 O ANISOU 5231 O TYR B1025 22903 23015 21671 -422 -728 -115 O ATOM 5232 CB TYR B1025 -30.918 17.993 83.682 1.00179.61 C ANISOU 5232 CB TYR B1025 23207 22859 22179 -688 -870 -351 C ATOM 5233 N THR B1026 -33.766 16.817 82.089 1.00175.28 N ANISOU 5233 N THR B1026 22765 22471 21362 -412 -591 40 N ATOM 5234 CA THR B1026 -34.259 15.769 81.185 1.00173.22 C ANISOU 5234 CA THR B1026 22433 22357 21025 -391 -477 200 C ATOM 5235 C THR B1026 -34.213 16.186 79.702 1.00176.83 C ANISOU 5235 C THR B1026 22898 22736 21555 -543 -368 348 C ATOM 5236 O THR B1026 -34.104 17.375 79.394 1.00178.00 O ANISOU 5236 O THR B1026 23147 22689 21795 -636 -387 364 O ATOM 5237 CB THR B1026 -35.670 15.300 81.609 1.00180.96 C ANISOU 5237 CB THR B1026 23482 23437 21837 -186 -457 250 C ATOM 5238 OG1 THR B1026 -36.466 16.426 81.992 1.00181.62 O ANISOU 5238 OG1 THR B1026 23706 23381 21920 -84 -485 200 O ATOM 5239 CG2 THR B1026 -35.639 14.276 82.736 1.00179.30 C ANISOU 5239 CG2 THR B1026 23221 23401 21504 -95 -528 179 C ATOM 5240 N ILE B1027 -34.293 15.192 78.791 1.00171.78 N ANISOU 5240 N ILE B1027 22160 22244 20863 -577 -265 455 N ATOM 5241 CA ILE B1027 -34.291 15.370 77.332 1.00171.81 C ANISOU 5241 CA ILE B1027 22163 22238 20879 -733 -148 602 C ATOM 5242 C ILE B1027 -35.131 14.266 76.645 1.00173.72 C ANISOU 5242 C ILE B1027 22367 22644 20994 -652 -60 717 C ATOM 5243 O ILE B1027 -35.075 13.106 77.057 1.00172.30 O ANISOU 5243 O ILE B1027 22084 22609 20772 -565 -70 662 O ATOM 5244 CB ILE B1027 -32.846 15.532 76.756 1.00176.40 C ANISOU 5244 CB ILE B1027 22614 22833 21576 -986 -100 547 C ATOM 5245 CG1 ILE B1027 -32.859 16.075 75.305 1.00177.93 C ANISOU 5245 CG1 ILE B1027 22856 22994 21755 -1195 14 712 C ATOM 5246 CG2 ILE B1027 -31.997 14.253 76.907 1.00176.46 C ANISOU 5246 CG2 ILE B1027 22402 23036 21609 -984 -84 427 C ATOM 5247 CD1 ILE B1027 -31.608 16.824 74.865 1.00186.70 C ANISOU 5247 CD1 ILE B1027 23908 24051 22978 -1483 47 679 C ATOM 5248 N GLY B1028 -35.911 14.651 75.633 1.00169.91 N ANISOU 5248 N GLY B1028 21978 22123 20458 -685 2 881 N ATOM 5249 CA GLY B1028 -36.782 13.743 74.891 1.00168.04 C ANISOU 5249 CA GLY B1028 21721 22029 20099 -626 77 997 C ATOM 5250 C GLY B1028 -38.164 13.696 75.502 1.00170.43 C ANISOU 5250 C GLY B1028 22108 22328 20321 -402 24 1037 C ATOM 5251 O GLY B1028 -38.828 14.733 75.601 1.00170.77 O ANISOU 5251 O GLY B1028 22275 22222 20387 -336 -27 1081 O ATOM 5252 N ILE B1029 -38.600 12.496 75.935 1.00165.30 N ANISOU 5252 N ILE B1029 21382 21837 19585 -287 31 1013 N ATOM 5253 CA ILE B1029 -39.897 12.302 76.596 1.00164.30 C ANISOU 5253 CA ILE B1029 21302 21761 19363 -96 -1 1038 C ATOM 5254 C ILE B1029 -39.399 11.940 78.014 1.00168.01 C ANISOU 5254 C ILE B1029 21736 22270 19830 -31 -76 889 C ATOM 5255 O ILE B1029 -39.159 10.772 78.332 1.00166.80 O ANISOU 5255 O ILE B1029 21502 22239 19634 -25 -89 870 O ATOM 5256 CB ILE B1029 -40.848 11.301 75.854 1.00166.05 C ANISOU 5256 CB ILE B1029 21485 22131 19475 -63 60 1162 C ATOM 5257 CG1 ILE B1029 -40.859 11.547 74.325 1.00166.77 C ANISOU 5257 CG1 ILE B1029 21597 22202 19565 -196 127 1292 C ATOM 5258 CG2 ILE B1029 -42.275 11.377 76.422 1.00166.44 C ANISOU 5258 CG2 ILE B1029 21574 22229 19437 113 39 1194 C ATOM 5259 CD1 ILE B1029 -41.494 10.442 73.480 1.00172.79 C ANISOU 5259 CD1 ILE B1029 22305 23122 20225 -208 186 1383 C ATOM 5260 N GLY B1030 -39.215 12.978 78.831 1.00165.55 N ANISOU 5260 N GLY B1030 21497 21837 19569 8 -141 786 N ATOM 5261 CA GLY B1030 -38.750 12.873 80.210 1.00165.68 C ANISOU 5261 CA GLY B1030 21504 21882 19564 58 -229 637 C ATOM 5262 C GLY B1030 -37.659 11.882 80.569 1.00168.65 C ANISOU 5262 C GLY B1030 21775 22340 19962 -13 -280 581 C ATOM 5263 O GLY B1030 -37.710 11.280 81.647 1.00168.14 O ANISOU 5263 O GLY B1030 21706 22370 19808 54 -357 528 O ATOM 5264 N HIS B1031 -36.656 11.714 79.682 1.00164.81 N ANISOU 5264 N HIS B1031 21200 21827 19594 -154 -247 586 N ATOM 5265 CA HIS B1031 -35.537 10.795 79.904 1.00164.46 C ANISOU 5265 CA HIS B1031 21021 21847 19618 -208 -305 508 C ATOM 5266 C HIS B1031 -34.420 11.439 80.740 1.00169.55 C ANISOU 5266 C HIS B1031 21643 22414 20364 -261 -413 355 C ATOM 5267 O HIS B1031 -33.817 12.429 80.319 1.00170.06 O ANISOU 5267 O HIS B1031 21709 22369 20536 -380 -385 316 O ATOM 5268 CB HIS B1031 -35.015 10.220 78.573 1.00164.88 C ANISOU 5268 CB HIS B1031 20953 21948 19746 -323 -205 545 C ATOM 5269 CG HIS B1031 -33.826 9.321 78.718 1.00168.61 C ANISOU 5269 CG HIS B1031 21257 22476 20330 -359 -268 429 C ATOM 5270 ND1 HIS B1031 -33.950 8.033 79.205 1.00169.76 N ANISOU 5270 ND1 HIS B1031 21356 22696 20448 -258 -358 429 N ATOM 5271 CD2 HIS B1031 -32.526 9.557 78.432 1.00171.61 C ANISOU 5271 CD2 HIS B1031 21498 22843 20862 -484 -265 309 C ATOM 5272 CE1 HIS B1031 -32.728 7.528 79.201 1.00169.98 C ANISOU 5272 CE1 HIS B1031 21220 22736 20628 -299 -421 302 C ATOM 5273 NE2 HIS B1031 -31.837 8.409 78.745 1.00171.52 N ANISOU 5273 NE2 HIS B1031 21339 22897 20933 -433 -358 215 N ATOM 5274 N LEU B1032 -34.164 10.867 81.932 1.00166.38 N ANISOU 5274 N LEU B1032 21228 22070 19918 -188 -550 281 N ATOM 5275 CA LEU B1032 -33.151 11.333 82.882 1.00167.71 C ANISOU 5275 CA LEU B1032 21374 22190 20159 -225 -688 131 C ATOM 5276 C LEU B1032 -31.733 11.018 82.403 1.00172.19 C ANISOU 5276 C LEU B1032 21754 22756 20917 -343 -717 47 C ATOM 5277 O LEU B1032 -31.478 9.919 81.903 1.00170.94 O ANISOU 5277 O LEU B1032 21472 22676 20803 -334 -706 72 O ATOM 5278 CB LEU B1032 -33.401 10.713 84.273 1.00167.97 C ANISOU 5278 CB LEU B1032 21461 22312 20048 -120 -837 104 C ATOM 5279 CG LEU B1032 -32.538 11.225 85.433 1.00174.42 C ANISOU 5279 CG LEU B1032 22288 23097 20887 -145 -1004 -51 C ATOM 5280 CD1 LEU B1032 -33.134 12.474 86.053 1.00175.52 C ANISOU 5280 CD1 LEU B1032 22579 23172 20937 -112 -988 -131 C ATOM 5281 CD2 LEU B1032 -32.359 10.155 86.489 1.00177.30 C ANISOU 5281 CD2 LEU B1032 22646 23572 21148 -89 -1182 -43 C ATOM 5282 N LEU B1033 -30.812 11.984 82.585 1.00170.48 N ANISOU 5282 N LEU B1033 21505 22450 20821 -454 -759 -72 N ATOM 5283 CA LEU B1033 -29.398 11.865 82.218 1.00171.53 C ANISOU 5283 CA LEU B1033 21432 22596 21146 -585 -784 -184 C ATOM 5284 C LEU B1033 -28.545 11.598 83.469 1.00176.87 C ANISOU 5284 C LEU B1033 22040 23291 21871 -547 -1005 -322 C ATOM 5285 O LEU B1033 -27.860 10.576 83.532 1.00176.74 O ANISOU 5285 O LEU B1033 21857 23351 21943 -514 -1097 -371 O ATOM 5286 CB LEU B1033 -28.911 13.126 81.470 1.00172.82 C ANISOU 5286 CB LEU B1033 21591 22655 21417 -779 -679 -206 C ATOM 5287 CG LEU B1033 -29.611 13.456 80.146 1.00176.68 C ANISOU 5287 CG LEU B1033 22149 23122 21861 -853 -483 -54 C ATOM 5288 CD1 LEU B1033 -29.693 14.953 79.930 1.00178.15 C ANISOU 5288 CD1 LEU B1033 22475 23131 22082 -981 -455 -24 C ATOM 5289 CD2 LEU B1033 -28.928 12.781 78.970 1.00179.06 C ANISOU 5289 CD2 LEU B1033 22248 23547 22240 -976 -355 -59 C ATOM 5290 N THR B1034 -28.610 12.506 84.469 1.00174.63 N ANISOU 5290 N THR B1034 21888 22933 21530 -543 -1107 -392 N ATOM 5291 CA THR B1034 -27.877 12.410 85.739 1.00176.01 C ANISOU 5291 CA THR B1034 22033 23128 21713 -519 -1335 -522 C ATOM 5292 C THR B1034 -28.674 13.012 86.919 1.00180.51 C ANISOU 5292 C THR B1034 22826 23677 22083 -437 -1414 -548 C ATOM 5293 O THR B1034 -29.695 13.671 86.700 1.00179.46 O ANISOU 5293 O THR B1034 22846 23489 21854 -400 -1286 -494 O ATOM 5294 CB THR B1034 -26.432 12.955 85.594 1.00185.88 C ANISOU 5294 CB THR B1034 23100 24336 23190 -681 -1395 -677 C ATOM 5295 OG1 THR B1034 -25.651 12.530 86.712 1.00187.05 O ANISOU 5295 OG1 THR B1034 23173 24533 23363 -642 -1642 -790 O ATOM 5296 CG2 THR B1034 -26.369 14.478 85.454 1.00185.43 C ANISOU 5296 CG2 THR B1034 23143 24132 23181 -821 -1330 -732 C ATOM 5297 N LYS B1035 -28.192 12.754 88.133 1.00178.38 N ANISOU 5297 N LYS B1035 22561 23462 21755 -406 -1628 -639 N ATOM 5298 CA LYS B1035 -28.751 13.319 89.353 1.00179.07 C ANISOU 5298 CA LYS B1035 22836 23564 21638 -351 -1717 -711 C ATOM 5299 C LYS B1035 -27.809 14.409 89.848 1.00184.99 C ANISOU 5299 C LYS B1035 23572 24214 22503 -462 -1831 -906 C ATOM 5300 O LYS B1035 -26.923 14.166 90.667 1.00186.02 O ANISOU 5300 O LYS B1035 23634 24393 22652 -491 -2043 -1004 O ATOM 5301 CB LYS B1035 -28.920 12.239 90.421 1.00181.71 C ANISOU 5301 CB LYS B1035 23214 24052 21777 -266 -1892 -661 C ATOM 5302 CG LYS B1035 -30.067 11.278 90.155 1.00191.71 C ANISOU 5302 CG LYS B1035 24544 25414 22881 -170 -1787 -470 C ATOM 5303 CD LYS B1035 -30.017 10.084 91.095 1.00200.60 C ANISOU 5303 CD LYS B1035 25697 26668 23854 -128 -1992 -387 C ATOM 5304 CE LYS B1035 -31.093 10.178 92.164 1.00209.66 C ANISOU 5304 CE LYS B1035 27046 27951 24665 -89 -1992 -362 C ATOM 5305 NZ LYS B1035 -30.661 11.018 93.316 1.00220.07 N ANISOU 5305 NZ LYS B1035 28446 29295 25877 -128 -2133 -545 N ATOM 5306 N SER B1036 -28.012 15.611 89.324 1.00181.82 N ANISOU 5306 N SER B1036 23238 23658 22187 -528 -1707 -954 N ATOM 5307 CA SER B1036 -27.116 16.752 89.539 1.00183.71 C ANISOU 5307 CA SER B1036 23462 23758 22582 -669 -1791 -1126 C ATOM 5308 C SER B1036 -27.846 18.069 89.195 1.00187.48 C ANISOU 5308 C SER B1036 24111 24042 23080 -683 -1671 -1152 C ATOM 5309 O SER B1036 -28.482 18.147 88.140 1.00185.47 O ANISOU 5309 O SER B1036 23880 23728 22861 -675 -1495 -1007 O ATOM 5310 CB SER B1036 -25.750 16.721 88.853 1.00188.13 C ANISOU 5310 CB SER B1036 23789 24289 23402 -844 -1815 -1160 C ATOM 5311 OG SER B1036 -24.952 15.638 89.301 1.00197.18 O ANISOU 5311 OG SER B1036 24763 25582 24574 -815 -1977 -1185 O ATOM 5312 N PRO B1037 -27.727 19.131 90.040 1.00186.01 N ANISOU 5312 N PRO B1037 24045 23740 22889 -708 -1783 -1343 N ATOM 5313 CA PRO B1037 -28.385 20.411 89.714 1.00186.46 C ANISOU 5313 CA PRO B1037 24267 23569 23008 -707 -1702 -1384 C ATOM 5314 C PRO B1037 -27.619 21.263 88.691 1.00190.80 C ANISOU 5314 C PRO B1037 24766 23902 23827 -925 -1663 -1350 C ATOM 5315 O PRO B1037 -28.128 22.301 88.262 1.00191.00 O ANISOU 5315 O PRO B1037 24936 23701 23936 -942 -1613 -1342 O ATOM 5316 CB PRO B1037 -28.499 21.118 91.077 1.00190.46 C ANISOU 5316 CB PRO B1037 24915 24047 23405 -646 -1853 -1632 C ATOM 5317 CG PRO B1037 -27.853 20.193 92.093 1.00195.42 C ANISOU 5317 CG PRO B1037 25453 24906 23890 -642 -2015 -1694 C ATOM 5318 CD PRO B1037 -27.013 19.226 91.328 1.00189.71 C ANISOU 5318 CD PRO B1037 24513 24269 23298 -733 -2004 -1538 C ATOM 5319 N SER B1038 -26.398 20.828 88.308 1.00187.46 N ANISOU 5319 N SER B1038 24133 23549 23543 -1098 -1692 -1333 N ATOM 5320 CA SER B1038 -25.528 21.493 87.329 1.00188.36 C ANISOU 5320 CA SER B1038 24155 23522 23891 -1355 -1639 -1296 C ATOM 5321 C SER B1038 -25.990 21.215 85.886 1.00189.97 C ANISOU 5321 C SER B1038 24333 23730 24117 -1395 -1424 -1062 C ATOM 5322 O SER B1038 -26.809 20.318 85.672 1.00187.23 O ANISOU 5322 O SER B1038 23992 23522 23625 -1222 -1333 -944 O ATOM 5323 CB SER B1038 -24.080 21.051 87.523 1.00193.00 C ANISOU 5323 CB SER B1038 24489 24236 24605 -1510 -1744 -1396 C ATOM 5324 OG SER B1038 -23.948 19.643 87.417 1.00199.57 O ANISOU 5324 OG SER B1038 25146 25309 25372 -1404 -1721 -1327 O ATOM 5325 N LEU B1039 -25.464 21.979 84.902 1.00187.44 N ANISOU 5325 N LEU B1039 23989 23265 23964 -1643 -1349 -990 N ATOM 5326 CA LEU B1039 -25.837 21.842 83.491 1.00185.93 C ANISOU 5326 CA LEU B1039 23791 23080 23776 -1726 -1154 -766 C ATOM 5327 C LEU B1039 -24.885 20.974 82.654 1.00189.16 C ANISOU 5327 C LEU B1039 23919 23708 24244 -1887 -1039 -723 C ATOM 5328 O LEU B1039 -25.358 20.116 81.906 1.00186.71 O ANISOU 5328 O LEU B1039 23554 23543 23842 -1812 -898 -591 O ATOM 5329 CB LEU B1039 -26.038 23.227 82.843 1.00187.91 C ANISOU 5329 CB LEU B1039 24229 23031 24136 -1903 -1138 -674 C ATOM 5330 CG LEU B1039 -26.657 23.253 81.438 1.00191.74 C ANISOU 5330 CG LEU B1039 24779 23487 24585 -1975 -967 -416 C ATOM 5331 CD1 LEU B1039 -28.176 23.235 81.499 1.00190.28 C ANISOU 5331 CD1 LEU B1039 24793 23231 24271 -1694 -956 -327 C ATOM 5332 CD2 LEU B1039 -26.194 24.466 80.670 1.00196.89 C ANISOU 5332 CD2 LEU B1039 25525 23898 25385 -2289 -966 -316 C ATOM 5333 N ASN B1040 -23.564 21.209 82.758 1.00187.76 N ANISOU 5333 N ASN B1040 23553 23561 24224 -2108 -1095 -851 N ATOM 5334 CA ASN B1040 -22.546 20.491 81.982 1.00187.96 C ANISOU 5334 CA ASN B1040 23273 23806 24337 -2275 -983 -862 C ATOM 5335 C ASN B1040 -22.383 18.991 82.306 1.00190.12 C ANISOU 5335 C ASN B1040 23340 24332 24564 -2065 -1008 -932 C ATOM 5336 O ASN B1040 -21.866 18.248 81.465 1.00189.50 O ANISOU 5336 O ASN B1040 23029 24438 24533 -2139 -877 -924 O ATOM 5337 CB ASN B1040 -21.203 21.229 82.024 1.00192.21 C ANISOU 5337 CB ASN B1040 23650 24312 25071 -2581 -1039 -992 C ATOM 5338 CG ASN B1040 -20.312 20.984 80.824 1.00217.66 C ANISOU 5338 CG ASN B1040 26606 27713 28383 -2854 -849 -961 C ATOM 5339 OD1 ASN B1040 -20.769 20.845 79.679 1.00210.53 O ANISOU 5339 OD1 ASN B1040 25738 26860 27395 -2927 -650 -787 O ATOM 5340 ND2 ASN B1040 -19.009 20.970 81.056 1.00211.60 N ANISOU 5340 ND2 ASN B1040 25557 27060 27781 -3028 -905 -1140 N ATOM 5341 N ALA B1041 -22.829 18.547 83.506 1.00185.71 N ANISOU 5341 N ALA B1041 22871 23781 23909 -1811 -1179 -1003 N ATOM 5342 CA ALA B1041 -22.756 17.145 83.945 1.00184.16 C ANISOU 5342 CA ALA B1041 22529 23780 23665 -1606 -1253 -1043 C ATOM 5343 C ALA B1041 -23.741 16.235 83.190 1.00185.72 C ANISOU 5343 C ALA B1041 22771 24064 23729 -1458 -1096 -874 C ATOM 5344 O ALA B1041 -23.437 15.060 82.964 1.00184.45 O ANISOU 5344 O ALA B1041 22422 24064 23597 -1377 -1090 -891 O ATOM 5345 CB ALA B1041 -22.994 17.048 85.445 1.00184.92 C ANISOU 5345 CB ALA B1041 22747 23855 23658 -1425 -1486 -1137 C ATOM 5346 N ALA B1042 -24.914 16.780 82.809 1.00181.35 N ANISOU 5346 N ALA B1042 22461 23396 23048 -1419 -988 -723 N ATOM 5347 CA ALA B1042 -25.962 16.065 82.076 1.00178.89 C ANISOU 5347 CA ALA B1042 22215 23152 22602 -1294 -843 -556 C ATOM 5348 C ALA B1042 -25.685 16.013 80.573 1.00182.74 C ANISOU 5348 C ALA B1042 22586 23702 23145 -1479 -635 -465 C ATOM 5349 O ALA B1042 -26.081 15.049 79.917 1.00180.66 O ANISOU 5349 O ALA B1042 22260 23568 22814 -1400 -531 -390 O ATOM 5350 CB ALA B1042 -27.315 16.707 82.341 1.00178.74 C ANISOU 5350 CB ALA B1042 22481 22995 22437 -1168 -834 -453 C ATOM 5351 N LYS B1043 -25.004 17.044 80.034 1.00181.41 N ANISOU 5351 N LYS B1043 22394 23449 23085 -1742 -577 -474 N ATOM 5352 CA LYS B1043 -24.641 17.160 78.616 1.00182.00 C ANISOU 5352 CA LYS B1043 22366 23600 23187 -1982 -374 -388 C ATOM 5353 C LYS B1043 -23.664 16.062 78.176 1.00186.72 C ANISOU 5353 C LYS B1043 22628 24449 23868 -2024 -299 -519 C ATOM 5354 O LYS B1043 -23.723 15.619 77.027 1.00185.89 O ANISOU 5354 O LYS B1043 22437 24481 23712 -2110 -112 -454 O ATOM 5355 CB LYS B1043 -24.072 18.555 78.306 1.00186.78 C ANISOU 5355 CB LYS B1043 23032 24047 23889 -2285 -359 -366 C ATOM 5356 CG LYS B1043 -25.113 19.674 78.366 1.00198.18 C ANISOU 5356 CG LYS B1043 24813 25217 25271 -2261 -406 -212 C ATOM 5357 CD LYS B1043 -24.581 20.999 77.828 1.00209.25 C ANISOU 5357 CD LYS B1043 26292 26439 26773 -2594 -389 -145 C ATOM 5358 CE LYS B1043 -24.802 21.163 76.341 1.00219.01 C ANISOU 5358 CE LYS B1043 27570 27717 27928 -2812 -200 75 C ATOM 5359 NZ LYS B1043 -24.144 22.387 75.819 1.00231.94 N ANISOU 5359 NZ LYS B1043 29270 29198 29660 -3187 -189 155 N ATOM 5360 N SER B1044 -22.781 15.622 79.097 1.00184.63 N ANISOU 5360 N SER B1044 22173 24245 23733 -1953 -458 -715 N ATOM 5361 CA SER B1044 -21.795 14.561 78.871 1.00185.34 C ANISOU 5361 CA SER B1044 21919 24550 23951 -1943 -443 -883 C ATOM 5362 C SER B1044 -22.464 13.183 78.887 1.00187.12 C ANISOU 5362 C SER B1044 22137 24863 24098 -1668 -461 -855 C ATOM 5363 O SER B1044 -22.047 12.299 78.136 1.00186.88 O ANISOU 5363 O SER B1044 21878 25000 24128 -1669 -356 -935 O ATOM 5364 CB SER B1044 -20.693 14.623 79.925 1.00190.80 C ANISOU 5364 CB SER B1044 22430 25246 24818 -1944 -655 -1088 C ATOM 5365 OG SER B1044 -19.654 13.699 79.649 1.00200.11 O ANISOU 5365 OG SER B1044 23244 26625 26164 -1941 -649 -1273 O ATOM 5366 N GLU B1045 -23.505 13.009 79.738 1.00181.88 N ANISOU 5366 N GLU B1045 21719 24089 23298 -1445 -591 -752 N ATOM 5367 CA GLU B1045 -24.282 11.770 79.891 1.00179.65 C ANISOU 5367 CA GLU B1045 21479 23859 22921 -1201 -633 -690 C ATOM 5368 C GLU B1045 -25.047 11.381 78.613 1.00182.08 C ANISOU 5368 C GLU B1045 21827 24235 23121 -1219 -412 -560 C ATOM 5369 O GLU B1045 -25.308 10.194 78.398 1.00180.75 O ANISOU 5369 O GLU B1045 21588 24151 22939 -1075 -412 -564 O ATOM 5370 CB GLU B1045 -25.247 11.877 81.086 1.00179.75 C ANISOU 5370 CB GLU B1045 21754 23760 22782 -1017 -794 -602 C ATOM 5371 CG GLU B1045 -24.569 11.770 82.443 1.00192.11 C ANISOU 5371 CG GLU B1045 23271 25308 24414 -943 -1052 -734 C ATOM 5372 CD GLU B1045 -24.521 10.383 83.058 1.00211.54 C ANISOU 5372 CD GLU B1045 25656 27841 26881 -747 -1227 -753 C ATOM 5373 OE1 GLU B1045 -24.941 10.243 84.230 1.00204.08 O ANISOU 5373 OE1 GLU B1045 24864 26862 25813 -626 -1410 -719 O ATOM 5374 OE2 GLU B1045 -24.052 9.440 82.382 1.00206.16 O ANISOU 5374 OE2 GLU B1045 24764 27246 26323 -720 -1190 -806 O ATOM 5375 N LEU B1046 -25.400 12.381 77.776 1.00178.67 N ANISOU 5375 N LEU B1046 21518 23755 22615 -1402 -245 -441 N ATOM 5376 CA LEU B1046 -26.113 12.207 76.507 1.00177.43 C ANISOU 5376 CA LEU B1046 21421 23662 22333 -1460 -43 -301 C ATOM 5377 C LEU B1046 -25.230 11.481 75.484 1.00181.87 C ANISOU 5377 C LEU B1046 21695 24431 22978 -1579 107 -432 C ATOM 5378 O LEU B1046 -25.686 10.509 74.880 1.00180.28 O ANISOU 5378 O LEU B1046 21456 24330 22711 -1483 183 -417 O ATOM 5379 CB LEU B1046 -26.573 13.575 75.968 1.00178.14 C ANISOU 5379 CB LEU B1046 21721 23623 22342 -1645 48 -137 C ATOM 5380 CG LEU B1046 -27.489 13.562 74.746 1.00181.97 C ANISOU 5380 CG LEU B1046 22328 24145 22667 -1700 215 51 C ATOM 5381 CD1 LEU B1046 -28.689 14.443 74.965 1.00181.35 C ANISOU 5381 CD1 LEU B1046 22551 23868 22484 -1629 160 238 C ATOM 5382 CD2 LEU B1046 -26.745 14.002 73.499 1.00186.39 C ANISOU 5382 CD2 LEU B1046 22776 24813 23230 -2018 402 62 C ATOM 5383 N ASP B1047 -23.968 11.944 75.313 1.00180.24 N ANISOU 5383 N ASP B1047 21272 24294 22916 -1788 149 -581 N ATOM 5384 CA ASP B1047 -22.973 11.382 74.388 1.00181.41 C ANISOU 5384 CA ASP B1047 21098 24671 23158 -1927 308 -758 C ATOM 5385 C ASP B1047 -22.650 9.912 74.699 1.00183.87 C ANISOU 5385 C ASP B1047 21189 25079 23594 -1681 209 -946 C ATOM 5386 O ASP B1047 -22.304 9.158 73.786 1.00184.11 O ANISOU 5386 O ASP B1047 21008 25293 23654 -1709 356 -1073 O ATOM 5387 CB ASP B1047 -21.687 12.230 74.382 1.00186.08 C ANISOU 5387 CB ASP B1047 21491 25314 23896 -2196 341 -891 C ATOM 5388 CG ASP B1047 -21.901 13.718 74.160 1.00195.99 C ANISOU 5388 CG ASP B1047 22973 26429 25066 -2456 396 -707 C ATOM 5389 OD1 ASP B1047 -22.493 14.087 73.124 1.00196.16 O ANISOU 5389 OD1 ASP B1047 23141 26469 24922 -2609 568 -529 O ATOM 5390 OD2 ASP B1047 -21.448 14.513 75.009 1.00202.63 O ANISOU 5390 OD2 ASP B1047 23845 27133 26012 -2514 253 -744 O ATOM 5391 N LYS B1048 -22.780 9.513 75.985 1.00178.78 N ANISOU 5391 N LYS B1048 20604 24308 23016 -1445 -49 -963 N ATOM 5392 CA LYS B1048 -22.565 8.149 76.479 1.00177.99 C ANISOU 5392 CA LYS B1048 20353 24234 23040 -1194 -216 -1095 C ATOM 5393 C LYS B1048 -23.595 7.180 75.885 1.00178.90 C ANISOU 5393 C LYS B1048 20578 24368 23029 -1053 -145 -995 C ATOM 5394 O LYS B1048 -23.254 6.034 75.586 1.00178.96 O ANISOU 5394 O LYS B1048 20389 24453 23155 -933 -167 -1146 O ATOM 5395 CB LYS B1048 -22.652 8.115 78.015 1.00180.00 C ANISOU 5395 CB LYS B1048 20729 24337 23326 -1018 -515 -1065 C ATOM 5396 CG LYS B1048 -21.374 8.553 78.725 1.00195.53 C ANISOU 5396 CG LYS B1048 22490 26312 25491 -1088 -663 -1247 C ATOM 5397 CD LYS B1048 -21.573 8.748 80.232 1.00204.07 C ANISOU 5397 CD LYS B1048 23749 27250 26536 -957 -946 -1192 C ATOM 5398 CE LYS B1048 -21.575 7.461 81.030 1.00212.60 C ANISOU 5398 CE LYS B1048 24792 28305 27680 -702 -1203 -1221 C ATOM 5399 NZ LYS B1048 -21.695 7.716 82.490 1.00220.43 N ANISOU 5399 NZ LYS B1048 25957 29193 28602 -619 -1473 -1167 N ATOM 5400 N ALA B1049 -24.851 7.649 75.717 1.00172.50 N ANISOU 5400 N ALA B1049 20071 23477 21994 -1062 -73 -754 N ATOM 5401 CA ALA B1049 -25.961 6.866 75.173 1.00169.92 C ANISOU 5401 CA ALA B1049 19875 23162 21524 -952 -10 -633 C ATOM 5402 C ALA B1049 -26.151 7.076 73.667 1.00172.90 C ANISOU 5402 C ALA B1049 20228 23675 21789 -1138 261 -602 C ATOM 5403 O ALA B1049 -26.327 6.096 72.941 1.00172.18 O ANISOU 5403 O ALA B1049 20050 23683 21687 -1081 337 -667 O ATOM 5404 CB ALA B1049 -27.247 7.192 75.921 1.00168.51 C ANISOU 5404 CB ALA B1049 20014 22842 21172 -840 -105 -404 C ATOM 5405 N ILE B1050 -26.115 8.344 73.203 1.00169.30 N ANISOU 5405 N ILE B1050 19863 23218 21246 -1368 393 -502 N ATOM 5406 CA ILE B1050 -26.304 8.723 71.796 1.00169.29 C ANISOU 5406 CA ILE B1050 19880 23343 21099 -1591 636 -428 C ATOM 5407 C ILE B1050 -25.159 8.248 70.890 1.00174.69 C ANISOU 5407 C ILE B1050 20236 24264 21874 -1741 805 -671 C ATOM 5408 O ILE B1050 -25.417 7.586 69.881 1.00174.19 O ANISOU 5408 O ILE B1050 20119 24350 21714 -1765 952 -708 O ATOM 5409 CB ILE B1050 -26.654 10.239 71.642 1.00172.56 C ANISOU 5409 CB ILE B1050 20521 23643 21400 -1793 682 -216 C ATOM 5410 CG1 ILE B1050 -27.969 10.621 72.384 1.00170.56 C ANISOU 5410 CG1 ILE B1050 20580 23181 21046 -1614 541 -2 C ATOM 5411 CG2 ILE B1050 -26.664 10.707 70.180 1.00174.65 C ANISOU 5411 CG2 ILE B1050 20801 24047 21511 -2076 915 -125 C ATOM 5412 CD1 ILE B1050 -29.272 9.901 71.959 1.00174.68 C ANISOU 5412 CD1 ILE B1050 21242 23721 21407 -1463 564 136 C ATOM 5413 N GLY B1051 -23.924 8.588 71.260 1.00172.87 N ANISOU 5413 N GLY B1051 19781 24079 21824 -1841 782 -850 N ATOM 5414 CA GLY B1051 -22.726 8.202 70.520 1.00175.09 C ANISOU 5414 CA GLY B1051 19699 24606 22219 -1984 941 -1122 C ATOM 5415 C GLY B1051 -22.194 9.231 69.539 1.00180.38 C ANISOU 5415 C GLY B1051 20317 25434 22785 -2371 1183 -1091 C ATOM 5416 O GLY B1051 -21.339 8.898 68.712 1.00182.35 O ANISOU 5416 O GLY B1051 20270 25945 23069 -2526 1374 -1311 O ATOM 5417 N ARG B1052 -22.692 10.484 69.616 1.00175.77 N ANISOU 5417 N ARG B1052 20017 24694 22074 -2539 1173 -823 N ATOM 5418 CA ARG B1052 -22.260 11.591 68.755 1.00177.52 C ANISOU 5418 CA ARG B1052 20252 25012 22186 -2939 1364 -728 C ATOM 5419 C ARG B1052 -22.286 12.933 69.489 1.00180.46 C ANISOU 5419 C ARG B1052 20837 25132 22598 -3053 1227 -551 C ATOM 5420 O ARG B1052 -23.091 13.120 70.406 1.00177.60 O ANISOU 5420 O ARG B1052 20716 24517 22247 -2825 1026 -423 O ATOM 5421 CB ARG B1052 -23.067 11.652 67.436 1.00177.42 C ANISOU 5421 CB ARG B1052 20412 25110 21889 -3099 1558 -538 C ATOM 5422 CG ARG B1052 -24.477 12.236 67.554 1.00185.11 C ANISOU 5422 CG ARG B1052 21801 25830 22702 -3013 1445 -199 C ATOM 5423 CD ARG B1052 -25.042 12.636 66.207 1.00195.23 C ANISOU 5423 CD ARG B1052 23250 27218 23710 -3266 1620 15 C ATOM 5424 NE ARG B1052 -26.236 13.473 66.343 1.00202.72 N ANISOU 5424 NE ARG B1052 24578 27897 24547 -3223 1488 342 N ATOM 5425 CZ ARG B1052 -26.234 14.803 66.297 1.00218.64 C ANISOU 5425 CZ ARG B1052 26793 29741 26541 -3450 1447 553 C ATOM 5426 NH1 ARG B1052 -25.097 15.466 66.118 1.00209.68 N ANISOU 5426 NH1 ARG B1052 25520 28681 25469 -3770 1536 490 N ATOM 5427 NH2 ARG B1052 -27.366 15.479 66.431 1.00202.91 N ANISOU 5427 NH2 ARG B1052 25128 27492 24477 -3360 1307 820 N ATOM 5428 N ASN B1053 -21.412 13.866 69.071 1.00179.35 N ANISOU 5428 N ASN B1053 20605 25067 22475 -3418 1343 -554 N ATOM 5429 CA ASN B1053 -21.320 15.207 69.648 1.00179.74 C ANISOU 5429 CA ASN B1053 20845 24871 22577 -3579 1221 -402 C ATOM 5430 C ASN B1053 -22.508 16.043 69.167 1.00181.89 C ANISOU 5430 C ASN B1053 21525 24941 22645 -3655 1213 -54 C ATOM 5431 O ASN B1053 -22.759 16.121 67.960 1.00182.35 O ANISOU 5431 O ASN B1053 21640 25140 22504 -3872 1396 82 O ATOM 5432 CB ASN B1053 -19.982 15.868 69.289 1.00184.43 C ANISOU 5432 CB ASN B1053 21194 25622 23260 -3975 1349 -516 C ATOM 5433 CG ASN B1053 -18.766 15.086 69.736 1.00207.97 C ANISOU 5433 CG ASN B1053 23737 28813 26470 -3899 1347 -879 C ATOM 5434 OD1 ASN B1053 -18.549 14.842 70.930 1.00200.90 O ANISOU 5434 OD1 ASN B1053 22782 27784 25767 -3647 1120 -1008 O ATOM 5435 ND2 ASN B1053 -17.936 14.689 68.783 1.00201.28 N ANISOU 5435 ND2 ASN B1053 22564 28310 25603 -4121 1593 -1059 N ATOM 5436 N THR B1054 -23.266 16.621 70.118 1.00176.15 N ANISOU 5436 N THR B1054 21072 23893 21962 -3460 992 76 N ATOM 5437 CA THR B1054 -24.467 17.413 69.830 1.00174.83 C ANISOU 5437 CA THR B1054 21285 23493 21651 -3460 934 381 C ATOM 5438 C THR B1054 -24.337 18.878 70.250 1.00179.27 C ANISOU 5438 C THR B1054 22053 23761 22302 -3641 803 508 C ATOM 5439 O THR B1054 -24.695 19.764 69.470 1.00180.51 O ANISOU 5439 O THR B1054 22428 23805 22353 -3878 835 754 O ATOM 5440 CB THR B1054 -25.716 16.760 70.447 1.00180.30 C ANISOU 5440 CB THR B1054 22135 24074 22298 -3046 802 423 C ATOM 5441 OG1 THR B1054 -25.564 16.705 71.867 1.00178.93 O ANISOU 5441 OG1 THR B1054 21936 23761 22287 -2811 609 275 O ATOM 5442 CG2 THR B1054 -25.999 15.367 69.884 1.00177.61 C ANISOU 5442 CG2 THR B1054 21644 23984 21856 -2895 921 342 C ATOM 5443 N ASN B1055 -23.842 19.126 71.487 1.00174.72 N ANISOU 5443 N ASN B1055 21418 23047 21919 -3528 635 342 N ATOM 5444 CA ASN B1055 -23.655 20.452 72.098 1.00175.72 C ANISOU 5444 CA ASN B1055 21723 22875 22169 -3660 478 398 C ATOM 5445 C ASN B1055 -24.968 21.273 72.207 1.00177.68 C ANISOU 5445 C ASN B1055 22362 22792 22356 -3526 339 633 C ATOM 5446 O ASN B1055 -24.958 22.501 72.071 1.00179.48 O ANISOU 5446 O ASN B1055 22793 22767 22635 -3739 261 777 O ATOM 5447 CB ASN B1055 -22.499 21.236 71.432 1.00179.10 C ANISOU 5447 CB ASN B1055 22035 23366 22648 -4136 589 416 C ATOM 5448 CG ASN B1055 -21.152 20.546 71.490 1.00197.02 C ANISOU 5448 CG ASN B1055 23885 25949 25026 -4250 701 138 C ATOM 5449 OD1 ASN B1055 -20.667 20.143 72.554 1.00188.90 O ANISOU 5449 OD1 ASN B1055 22688 24928 24159 -4051 571 -94 O ATOM 5450 ND2 ASN B1055 -20.496 20.432 70.346 1.00188.96 N ANISOU 5450 ND2 ASN B1055 22679 25200 23917 -4585 937 149 N ATOM 5451 N GLY B1056 -26.074 20.569 72.471 1.00170.25 N ANISOU 5451 N GLY B1056 21510 21853 21323 -3172 298 658 N ATOM 5452 CA GLY B1056 -27.401 21.155 72.624 1.00168.57 C ANISOU 5452 CA GLY B1056 21614 21375 21060 -2981 172 836 C ATOM 5453 C GLY B1056 -28.506 20.455 71.854 1.00168.99 C ANISOU 5453 C GLY B1056 21740 21541 20927 -2830 255 991 C ATOM 5454 O GLY B1056 -29.310 19.728 72.447 1.00166.05 O ANISOU 5454 O GLY B1056 21375 21201 20516 -2499 205 932 O ATOM 5455 N VAL B1057 -28.558 20.685 70.523 1.00165.69 N ANISOU 5455 N VAL B1057 21383 21190 20380 -3095 378 1197 N ATOM 5456 CA VAL B1057 -29.587 20.153 69.612 1.00163.64 C ANISOU 5456 CA VAL B1057 21212 21035 19927 -3011 450 1372 C ATOM 5457 C VAL B1057 -29.424 18.654 69.288 1.00163.92 C ANISOU 5457 C VAL B1057 20997 21423 19860 -2917 613 1228 C ATOM 5458 O VAL B1057 -28.358 18.229 68.831 1.00164.70 O ANISOU 5458 O VAL B1057 20865 21759 19955 -3130 768 1103 O ATOM 5459 CB VAL B1057 -29.761 21.015 68.319 1.00170.25 C ANISOU 5459 CB VAL B1057 22245 21802 20642 -3339 488 1669 C ATOM 5460 CG1 VAL B1057 -31.045 20.648 67.570 1.00168.79 C ANISOU 5460 CG1 VAL B1057 22206 21652 20275 -3196 487 1865 C ATOM 5461 CG2 VAL B1057 -29.738 22.513 68.627 1.00172.56 C ANISOU 5461 CG2 VAL B1057 22776 21714 21076 -3468 307 1800 C ATOM 5462 N ILE B1058 -30.510 17.873 69.505 1.00156.26 N ANISOU 5462 N ILE B1058 20072 20483 18817 -2600 574 1239 N ATOM 5463 CA ILE B1058 -30.603 16.434 69.207 1.00153.26 C ANISOU 5463 CA ILE B1058 19505 20381 18346 -2473 690 1127 C ATOM 5464 C ILE B1058 -31.756 16.167 68.213 1.00154.64 C ANISOU 5464 C ILE B1058 19821 20613 18322 -2441 733 1331 C ATOM 5465 O ILE B1058 -32.744 16.909 68.209 1.00154.24 O ANISOU 5465 O ILE B1058 20005 20356 18243 -2364 615 1525 O ATOM 5466 CB ILE B1058 -30.671 15.529 70.477 1.00153.81 C ANISOU 5466 CB ILE B1058 19454 20466 18519 -2148 595 921 C ATOM 5467 CG1 ILE B1058 -31.994 15.698 71.258 1.00152.22 C ANISOU 5467 CG1 ILE B1058 19454 20083 18301 -1852 443 1010 C ATOM 5468 CG2 ILE B1058 -29.446 15.723 71.380 1.00155.49 C ANISOU 5468 CG2 ILE B1058 19508 20655 18917 -2198 542 714 C ATOM 5469 CD1 ILE B1058 -32.529 14.413 71.882 1.00155.91 C ANISOU 5469 CD1 ILE B1058 19833 20666 18739 -1570 414 910 C ATOM 5470 N THR B1059 -31.619 15.127 67.365 1.00149.17 N ANISOU 5470 N THR B1059 18978 20196 17504 -2497 889 1271 N ATOM 5471 CA THR B1059 -32.635 14.770 66.364 1.00147.58 C ANISOU 5471 CA THR B1059 18889 20087 17100 -2488 934 1441 C ATOM 5472 C THR B1059 -33.770 13.932 66.961 1.00146.74 C ANISOU 5472 C THR B1059 18809 19955 16989 -2133 838 1423 C ATOM 5473 O THR B1059 -33.624 13.400 68.063 1.00144.75 O ANISOU 5473 O THR B1059 18457 19673 16869 -1919 771 1255 O ATOM 5474 CB THR B1059 -32.002 14.084 65.139 1.00156.34 C ANISOU 5474 CB THR B1059 19835 21512 18056 -2729 1149 1371 C ATOM 5475 OG1 THR B1059 -31.228 12.960 65.562 1.00154.61 O ANISOU 5475 OG1 THR B1059 19336 21465 17944 -2620 1222 1072 O ATOM 5476 CG2 THR B1059 -31.156 15.035 64.300 1.00158.36 C ANISOU 5476 CG2 THR B1059 20115 21819 18237 -3138 1258 1469 C ATOM 5477 N LYS B1060 -34.878 13.822 66.236 1.00141.60 N ANISOU 5477 N LYS B1060 18294 19327 16182 -2093 825 1602 N ATOM 5478 CA LYS B1060 -36.019 13.039 66.695 1.00138.47 C ANISOU 5478 CA LYS B1060 17917 18929 15767 -1795 746 1600 C ATOM 5479 C LYS B1060 -35.683 11.552 66.725 1.00139.36 C ANISOU 5479 C LYS B1060 17818 19256 15877 -1712 834 1392 C ATOM 5480 O LYS B1060 -36.190 10.807 67.563 1.00136.94 O ANISOU 5480 O LYS B1060 17475 18930 15628 -1467 757 1318 O ATOM 5481 CB LYS B1060 -37.235 13.286 65.800 1.00141.39 C ANISOU 5481 CB LYS B1060 18459 19289 15973 -1798 706 1839 C ATOM 5482 CG LYS B1060 -38.568 13.195 66.524 1.00154.76 C ANISOU 5482 CG LYS B1060 20235 20866 17699 -1495 564 1898 C ATOM 5483 CD LYS B1060 -39.727 13.139 65.542 1.00166.31 C ANISOU 5483 CD LYS B1060 21809 22382 19000 -1492 532 2097 C ATOM 5484 CE LYS B1060 -40.185 14.534 65.148 1.00180.92 C ANISOU 5484 CE LYS B1060 23872 24020 20849 -1564 408 2332 C ATOM 5485 NZ LYS B1060 -41.053 15.148 66.191 1.00190.13 N ANISOU 5485 NZ LYS B1060 25115 24962 22162 -1289 245 2344 N ATOM 5486 N ASP B1061 -34.782 11.107 65.869 1.00135.87 N ANISOU 5486 N ASP B1061 17230 19015 15379 -1917 991 1282 N ATOM 5487 CA ASP B1061 -34.483 9.691 65.823 1.00134.11 C ANISOU 5487 CA ASP B1061 16808 18972 15178 -1824 1058 1067 C ATOM 5488 C ASP B1061 -33.480 9.211 66.856 1.00135.76 C ANISOU 5488 C ASP B1061 16824 19161 15598 -1718 1023 827 C ATOM 5489 O ASP B1061 -33.496 8.054 67.236 1.00134.31 O ANISOU 5489 O ASP B1061 16523 19026 15482 -1545 988 680 O ATOM 5490 CB ASP B1061 -34.076 9.320 64.421 1.00137.65 C ANISOU 5490 CB ASP B1061 17171 19666 15464 -2059 1241 1018 C ATOM 5491 CG ASP B1061 -34.977 9.954 63.405 1.00148.50 C ANISOU 5491 CG ASP B1061 18756 21051 16614 -2200 1250 1284 C ATOM 5492 OD1 ASP B1061 -35.164 11.182 63.485 1.00149.67 O ANISOU 5492 OD1 ASP B1061 19077 21031 16757 -2287 1177 1488 O ATOM 5493 OD2 ASP B1061 -35.526 9.233 62.553 1.00154.83 O ANISOU 5493 OD2 ASP B1061 19560 22013 17256 -2215 1306 1292 O ATOM 5494 N GLU B1062 -32.613 10.096 67.317 1.00131.80 N ANISOU 5494 N GLU B1062 16296 18574 15207 -1827 1010 794 N ATOM 5495 CA GLU B1062 -31.804 9.821 68.497 1.00130.46 C ANISOU 5495 CA GLU B1062 15981 18343 15244 -1700 919 601 C ATOM 5496 C GLU B1062 -32.671 9.757 69.749 1.00129.72 C ANISOU 5496 C GLU B1062 16018 18072 15199 -1430 734 666 C ATOM 5497 O GLU B1062 -32.398 8.984 70.667 1.00128.48 O ANISOU 5497 O GLU B1062 15758 17903 15155 -1259 637 527 O ATOM 5498 CB GLU B1062 -30.718 10.887 68.663 1.00133.99 C ANISOU 5498 CB GLU B1062 16378 18742 15789 -1907 943 561 C ATOM 5499 CG GLU B1062 -29.305 10.330 68.716 1.00148.02 C ANISOU 5499 CG GLU B1062 17854 20673 17715 -1981 1012 287 C ATOM 5500 CD GLU B1062 -28.388 10.967 67.690 1.00175.52 C ANISOU 5500 CD GLU B1062 21233 24310 21147 -2331 1200 262 C ATOM 5501 OE1 GLU B1062 -28.715 12.069 67.202 1.00174.42 O ANISOU 5501 OE1 GLU B1062 21290 24090 20890 -2531 1228 483 O ATOM 5502 OE2 GLU B1062 -27.341 10.366 67.372 1.00171.65 O ANISOU 5502 OE2 GLU B1062 20460 24022 20736 -2413 1313 20 O ATOM 5503 N ALA B1063 -33.719 10.574 69.778 1.00123.68 N ANISOU 5503 N ALA B1063 15476 17175 14342 -1395 680 874 N ATOM 5504 CA ALA B1063 -34.635 10.604 70.912 1.00120.83 C ANISOU 5504 CA ALA B1063 15233 16678 13999 -1154 531 926 C ATOM 5505 C ALA B1063 -35.392 9.287 71.037 1.00120.92 C ANISOU 5505 C ALA B1063 15206 16783 13954 -975 507 911 C ATOM 5506 O ALA B1063 -35.498 8.721 72.125 1.00119.58 O ANISOU 5506 O ALA B1063 15011 16582 13841 -804 400 842 O ATOM 5507 CB ALA B1063 -35.607 11.766 70.777 1.00121.70 C ANISOU 5507 CB ALA B1063 15562 16638 14041 -1150 485 1127 C ATOM 5508 N GLU B1064 -35.916 8.803 69.915 1.00115.47 N ANISOU 5508 N GLU B1064 14523 16210 13142 -1033 598 983 N ATOM 5509 CA GLU B1064 -36.658 7.540 69.895 1.00112.92 C ANISOU 5509 CA GLU B1064 14168 15969 12766 -894 576 973 C ATOM 5510 C GLU B1064 -35.779 6.409 70.444 1.00113.56 C ANISOU 5510 C GLU B1064 14072 16094 12982 -823 538 766 C ATOM 5511 O GLU B1064 -36.299 5.509 71.105 1.00111.99 O ANISOU 5511 O GLU B1064 13876 15879 12797 -665 440 760 O ATOM 5512 CB GLU B1064 -37.146 7.216 68.470 1.00114.69 C ANISOU 5512 CB GLU B1064 14408 16327 12840 -1009 686 1048 C ATOM 5513 CG GLU B1064 -38.294 6.214 68.430 1.00123.16 C ANISOU 5513 CG GLU B1064 15510 17448 13836 -871 640 1102 C ATOM 5514 CD GLU B1064 -38.862 5.836 67.072 1.00138.40 C ANISOU 5514 CD GLU B1064 17462 19516 15609 -974 725 1167 C ATOM 5515 OE1 GLU B1064 -38.278 6.224 66.032 1.00129.32 O ANISOU 5515 OE1 GLU B1064 16293 18460 14384 -1173 842 1155 O ATOM 5516 OE2 GLU B1064 -39.895 5.129 67.053 1.00128.95 O ANISOU 5516 OE2 GLU B1064 16299 18346 14349 -873 674 1228 O ATOM 5517 N LYS B1065 -34.451 6.470 70.180 1.00109.04 N ANISOU 5517 N LYS B1065 13341 15574 12515 -945 603 600 N ATOM 5518 CA LYS B1065 -33.449 5.509 70.657 1.00107.98 C ANISOU 5518 CA LYS B1065 13009 15469 12549 -875 548 378 C ATOM 5519 C LYS B1065 -33.434 5.473 72.186 1.00107.98 C ANISOU 5519 C LYS B1065 13048 15334 12646 -709 360 375 C ATOM 5520 O LYS B1065 -33.379 4.390 72.769 1.00106.96 O ANISOU 5520 O LYS B1065 12856 15188 12594 -571 242 302 O ATOM 5521 CB LYS B1065 -32.050 5.856 70.100 1.00112.43 C ANISOU 5521 CB LYS B1065 13381 16128 13208 -1055 664 202 C ATOM 5522 CG LYS B1065 -31.568 4.931 68.981 1.00128.01 C ANISOU 5522 CG LYS B1065 15170 18285 15184 -1126 800 25 C ATOM 5523 N LEU B1066 -33.527 6.656 72.824 1.00102.43 N ANISOU 5523 N LEU B1066 12461 14530 11926 -730 320 460 N ATOM 5524 CA LEU B1066 -33.577 6.810 74.277 1.00100.76 C ANISOU 5524 CA LEU B1066 12312 14211 11760 -596 154 458 C ATOM 5525 C LEU B1066 -34.933 6.350 74.813 1.00100.58 C ANISOU 5525 C LEU B1066 12434 14170 11612 -445 84 597 C ATOM 5526 O LEU B1066 -34.996 5.799 75.916 1.00 99.67 O ANISOU 5526 O LEU B1066 12331 14027 11514 -326 -57 577 O ATOM 5527 CB LEU B1066 -33.332 8.275 74.687 1.00101.62 C ANISOU 5527 CB LEU B1066 12510 14217 11883 -674 146 485 C ATOM 5528 CG LEU B1066 -31.941 8.869 74.443 1.00108.10 C ANISOU 5528 CG LEU B1066 13191 15043 12839 -844 188 350 C ATOM 5529 CD1 LEU B1066 -31.974 10.374 74.583 1.00109.19 C ANISOU 5529 CD1 LEU B1066 13466 15053 12967 -949 192 424 C ATOM 5530 CD2 LEU B1066 -30.901 8.293 75.401 1.00110.94 C ANISOU 5530 CD2 LEU B1066 13391 15406 13357 -773 50 168 C ATOM 5531 N PHE B1067 -36.013 6.579 74.026 1.00 94.56 N ANISOU 5531 N PHE B1067 11776 13438 10716 -464 176 742 N ATOM 5532 CA PHE B1067 -37.391 6.205 74.367 1.00 92.30 C ANISOU 5532 CA PHE B1067 11601 13163 10304 -343 137 875 C ATOM 5533 C PHE B1067 -37.586 4.683 74.415 1.00 94.73 C ANISOU 5533 C PHE B1067 11844 13532 10616 -278 83 852 C ATOM 5534 O PHE B1067 -38.296 4.196 75.296 1.00 93.33 O ANISOU 5534 O PHE B1067 11729 13352 10381 -178 -11 916 O ATOM 5535 CB PHE B1067 -38.398 6.878 73.411 1.00 93.53 C ANISOU 5535 CB PHE B1067 11859 13336 10343 -387 232 1024 C ATOM 5536 CG PHE B1067 -39.838 6.459 73.603 1.00 93.61 C ANISOU 5536 CG PHE B1067 11945 13390 10235 -275 206 1147 C ATOM 5537 CD1 PHE B1067 -40.609 7.003 74.623 1.00 95.89 C ANISOU 5537 CD1 PHE B1067 12319 13640 10477 -160 144 1192 C ATOM 5538 CD2 PHE B1067 -40.425 5.525 72.758 1.00 95.07 C ANISOU 5538 CD2 PHE B1067 12101 13669 10352 -293 247 1199 C ATOM 5539 CE1 PHE B1067 -41.937 6.607 74.804 1.00 95.91 C ANISOU 5539 CE1 PHE B1067 12358 13716 10370 -70 135 1290 C ATOM 5540 CE2 PHE B1067 -41.746 5.115 72.955 1.00 96.88 C ANISOU 5540 CE2 PHE B1067 12379 13951 10479 -208 219 1308 C ATOM 5541 CZ PHE B1067 -42.497 5.672 73.966 1.00 94.48 C ANISOU 5541 CZ PHE B1067 12142 13625 10132 -101 169 1357 C ATOM 5542 N ASN B1068 -36.964 3.945 73.470 1.00 91.64 N ANISOU 5542 N ASN B1068 11331 13197 10292 -344 141 755 N ATOM 5543 CA ASN B1068 -37.026 2.482 73.402 1.00 91.38 C ANISOU 5543 CA ASN B1068 11229 13186 10303 -284 75 704 C ATOM 5544 C ASN B1068 -36.335 1.845 74.613 1.00 96.03 C ANISOU 5544 C ASN B1068 11769 13696 11022 -189 -105 621 C ATOM 5545 O ASN B1068 -36.811 0.826 75.117 1.00 94.88 O ANISOU 5545 O ASN B1068 11658 13521 10870 -114 -226 671 O ATOM 5546 CB ASN B1068 -36.413 1.969 72.100 1.00 92.96 C ANISOU 5546 CB ASN B1068 11295 13467 10558 -372 187 568 C ATOM 5547 CG ASN B1068 -37.115 2.427 70.842 1.00112.01 C ANISOU 5547 CG ASN B1068 13768 15975 12814 -483 343 663 C ATOM 5548 OD1 ASN B1068 -38.250 2.930 70.860 1.00103.36 O ANISOU 5548 OD1 ASN B1068 12813 14876 11583 -468 349 844 O ATOM 5549 ND2 ASN B1068 -36.440 2.262 69.715 1.00104.61 N ANISOU 5549 ND2 ASN B1068 12718 15140 11891 -599 469 532 N ATOM 5550 N GLN B1069 -35.241 2.478 75.100 1.00 94.28 N ANISOU 5550 N GLN B1069 11476 13437 10909 -208 -140 511 N ATOM 5551 CA GLN B1069 -34.476 2.070 76.288 1.00 95.13 C ANISOU 5551 CA GLN B1069 11537 13470 11137 -127 -333 433 C ATOM 5552 C GLN B1069 -35.337 2.192 77.552 1.00 98.97 C ANISOU 5552 C GLN B1069 12193 13925 11486 -57 -450 583 C ATOM 5553 O GLN B1069 -35.148 1.425 78.497 1.00 99.16 O ANISOU 5553 O GLN B1069 12228 13902 11546 12 -636 590 O ATOM 5554 CB GLN B1069 -33.221 2.944 76.454 1.00 97.68 C ANISOU 5554 CB GLN B1069 11749 13781 11585 -188 -326 290 C ATOM 5555 CG GLN B1069 -32.140 2.711 75.404 1.00114.67 C ANISOU 5555 CG GLN B1069 13684 15995 13892 -265 -225 99 C ATOM 5556 CD GLN B1069 -30.970 3.645 75.581 1.00136.37 C ANISOU 5556 CD GLN B1069 16317 18748 16752 -355 -207 -28 C ATOM 5557 OE1 GLN B1069 -31.106 4.873 75.571 1.00131.04 O ANISOU 5557 OE1 GLN B1069 15734 18061 15995 -456 -124 44 O ATOM 5558 NE2 GLN B1069 -29.780 3.080 75.716 1.00132.67 N ANISOU 5558 NE2 GLN B1069 15631 18288 16490 -325 -294 -230 N ATOM 5559 N ASP B1070 -36.269 3.168 77.564 1.00 95.01 N ANISOU 5559 N ASP B1070 11819 13455 10827 -77 -347 698 N ATOM 5560 CA ASP B1070 -37.187 3.416 78.677 1.00 94.62 C ANISOU 5560 CA ASP B1070 11911 13416 10622 -18 -412 811 C ATOM 5561 C ASP B1070 -38.429 2.534 78.609 1.00 97.10 C ANISOU 5561 C ASP B1070 12292 13791 10811 10 -410 952 C ATOM 5562 O ASP B1070 -39.001 2.236 79.656 1.00 97.46 O ANISOU 5562 O ASP B1070 12421 13867 10742 46 -501 1032 O ATOM 5563 CB ASP B1070 -37.562 4.903 78.778 1.00 96.79 C ANISOU 5563 CB ASP B1070 12270 13684 10823 -31 -319 826 C ATOM 5564 CG ASP B1070 -36.376 5.829 78.983 1.00110.49 C ANISOU 5564 CG ASP B1070 13957 15346 12678 -81 -339 695 C ATOM 5565 OD1 ASP B1070 -35.586 5.590 79.934 1.00112.31 O ANISOU 5565 OD1 ASP B1070 14154 15552 12968 -58 -484 612 O ATOM 5566 OD2 ASP B1070 -36.257 6.817 78.222 1.00116.13 O ANISOU 5566 OD2 ASP B1070 14676 16025 13422 -154 -226 687 O ATOM 5567 N VAL B1071 -38.843 2.114 77.386 1.00 91.85 N ANISOU 5567 N VAL B1071 11590 13158 10152 -24 -306 982 N ATOM 5568 CA VAL B1071 -39.979 1.201 77.166 1.00 90.29 C ANISOU 5568 CA VAL B1071 11435 13014 9856 -18 -307 1105 C ATOM 5569 C VAL B1071 -39.544 -0.199 77.619 1.00 93.96 C ANISOU 5569 C VAL B1071 11872 13418 10411 0 -477 1088 C ATOM 5570 O VAL B1071 -40.292 -0.864 78.336 1.00 92.89 O ANISOU 5570 O VAL B1071 11815 13300 10178 4 -567 1210 O ATOM 5571 CB VAL B1071 -40.506 1.248 75.703 1.00 93.05 C ANISOU 5571 CB VAL B1071 11758 13417 10181 -70 -160 1129 C ATOM 5572 CG1 VAL B1071 -41.419 0.065 75.383 1.00 92.34 C ANISOU 5572 CG1 VAL B1071 11683 13367 10036 -78 -189 1216 C ATOM 5573 CG2 VAL B1071 -41.232 2.556 75.442 1.00 92.42 C ANISOU 5573 CG2 VAL B1071 11743 13378 9995 -73 -46 1202 C ATOM 5574 N ASP B1072 -38.297 -0.601 77.259 1.00 91.50 N ANISOU 5574 N ASP B1072 11442 13030 10292 8 -531 932 N ATOM 5575 CA ASP B1072 -37.665 -1.856 77.673 1.00 92.40 C ANISOU 5575 CA ASP B1072 11512 13042 10553 53 -730 882 C ATOM 5576 C ASP B1072 -37.644 -1.924 79.206 1.00 97.03 C ANISOU 5576 C ASP B1072 12197 13594 11077 81 -916 974 C ATOM 5577 O ASP B1072 -37.907 -2.982 79.781 1.00 97.48 O ANISOU 5577 O ASP B1072 12318 13591 11131 88 -1089 1070 O ATOM 5578 CB ASP B1072 -36.219 -1.934 77.136 1.00 95.26 C ANISOU 5578 CB ASP B1072 11697 13352 11147 75 -742 656 C ATOM 5579 CG ASP B1072 -36.067 -2.246 75.659 1.00104.55 C ANISOU 5579 CG ASP B1072 12757 14572 12396 39 -593 529 C ATOM 5580 OD1 ASP B1072 -36.947 -2.936 75.102 1.00105.12 O ANISOU 5580 OD1 ASP B1072 12880 14657 12401 24 -565 601 O ATOM 5581 OD2 ASP B1072 -35.034 -1.856 75.074 1.00109.60 O ANISOU 5581 OD2 ASP B1072 13245 15242 13157 15 -509 346 O ATOM 5582 N ALA B1073 -37.362 -0.771 79.854 1.00 93.46 N ANISOU 5582 N ALA B1073 11769 13180 10560 81 -885 949 N ATOM 5583 CA ALA B1073 -37.321 -0.604 81.301 1.00 94.07 C ANISOU 5583 CA ALA B1073 11944 13261 10536 93 -1036 1012 C ATOM 5584 C ALA B1073 -38.727 -0.733 81.905 1.00 98.19 C ANISOU 5584 C ALA B1073 12612 13887 10811 59 -1009 1198 C ATOM 5585 O ALA B1073 -38.891 -1.426 82.913 1.00 98.70 O ANISOU 5585 O ALA B1073 12764 13950 10788 39 -1178 1304 O ATOM 5586 CB ALA B1073 -36.711 0.746 81.652 1.00 94.90 C ANISOU 5586 CB ALA B1073 12031 13385 10642 94 -981 904 C ATOM 5587 N ALA B1074 -39.739 -0.095 81.272 1.00 94.37 N ANISOU 5587 N ALA B1074 12145 13498 10214 44 -805 1240 N ATOM 5588 CA ALA B1074 -41.132 -0.143 81.720 1.00 94.54 C ANISOU 5588 CA ALA B1074 12259 13650 10014 15 -746 1387 C ATOM 5589 C ALA B1074 -41.688 -1.564 81.640 1.00101.30 C ANISOU 5589 C ALA B1074 13144 14495 10851 -40 -839 1521 C ATOM 5590 O ALA B1074 -42.364 -1.997 82.572 1.00102.32 O ANISOU 5590 O ALA B1074 13362 14704 10811 -96 -907 1653 O ATOM 5591 CB ALA B1074 -41.988 0.809 80.904 1.00 94.11 C ANISOU 5591 CB ALA B1074 12185 13674 9900 32 -537 1383 C ATOM 5592 N VAL B1075 -41.358 -2.299 80.553 1.00 98.52 N ANISOU 5592 N VAL B1075 12719 14045 10670 -37 -847 1478 N ATOM 5593 CA VAL B1075 -41.766 -3.690 80.320 1.00 99.02 C ANISOU 5593 CA VAL B1075 12805 14049 10768 -86 -953 1575 C ATOM 5594 C VAL B1075 -41.163 -4.602 81.402 1.00104.60 C ANISOU 5594 C VAL B1075 13580 14641 11520 -98 -1218 1637 C ATOM 5595 O VAL B1075 -41.911 -5.341 82.046 1.00105.28 O ANISOU 5595 O VAL B1075 13771 14753 11478 -184 -1314 1813 O ATOM 5596 CB VAL B1075 -41.404 -4.157 78.883 1.00102.83 C ANISOU 5596 CB VAL B1075 13184 14450 11436 -66 -899 1456 C ATOM 5597 CG1 VAL B1075 -41.612 -5.659 78.705 1.00103.59 C ANISOU 5597 CG1 VAL B1075 13306 14433 11619 -102 -1054 1516 C ATOM 5598 CG2 VAL B1075 -42.197 -3.382 77.836 1.00101.45 C ANISOU 5598 CG2 VAL B1075 12976 14400 11171 -84 -669 1452 C ATOM 5599 N ARG B1076 -39.827 -4.511 81.624 1.00101.47 N ANISOU 5599 N ARG B1076 13126 14129 11301 -25 -1344 1501 N ATOM 5600 CA ARG B1076 -39.078 -5.294 82.619 1.00102.86 C ANISOU 5600 CA ARG B1076 13354 14173 11555 -14 -1634 1545 C ATOM 5601 C ARG B1076 -39.653 -5.145 84.034 1.00107.13 C ANISOU 5601 C ARG B1076 14052 14824 11829 -98 -1717 1726 C ATOM 5602 O ARG B1076 -39.741 -6.136 84.763 1.00108.06 O ANISOU 5602 O ARG B1076 14280 14867 11911 -162 -1942 1884 O ATOM 5603 CB ARG B1076 -37.587 -4.918 82.600 1.00103.61 C ANISOU 5603 CB ARG B1076 13323 14172 11871 85 -1719 1341 C ATOM 5604 CG ARG B1076 -36.650 -6.120 82.635 1.00116.09 C ANISOU 5604 CG ARG B1076 14852 15540 13716 152 -1999 1287 C ATOM 5605 CD ARG B1076 -36.041 -6.392 81.271 1.00126.86 C ANISOU 5605 CD ARG B1076 16029 16832 15340 229 -1908 1065 C ATOM 5606 NE ARG B1076 -35.708 -7.808 81.091 1.00136.69 N ANISOU 5606 NE ARG B1076 17253 17870 16814 286 -2145 1042 N ATOM 5607 CZ ARG B1076 -35.413 -8.368 79.922 1.00148.61 C ANISOU 5607 CZ ARG B1076 18624 19307 18532 345 -2089 857 C ATOM 5608 NH1 ARG B1076 -35.406 -7.642 78.810 1.00134.24 N ANISOU 5608 NH1 ARG B1076 16682 17629 16695 332 -1797 701 N ATOM 5609 NH2 ARG B1076 -35.129 -9.662 79.853 1.00134.17 N ANISOU 5609 NH2 ARG B1076 16787 17263 16927 412 -2334 824 N ATOM 5610 N GLY B1077 -40.058 -3.918 84.380 1.00102.64 N ANISOU 5610 N GLY B1077 13498 14430 11073 -105 -1535 1697 N ATOM 5611 CA GLY B1077 -40.653 -3.571 85.668 1.00103.04 C ANISOU 5611 CA GLY B1077 13674 14639 10837 -183 -1554 1814 C ATOM 5612 C GLY B1077 -42.053 -4.123 85.855 1.00105.82 C ANISOU 5612 C GLY B1077 14109 15128 10969 -305 -1487 2008 C ATOM 5613 O GLY B1077 -42.398 -4.580 86.950 1.00106.75 O ANISOU 5613 O GLY B1077 14352 15326 10885 -418 -1609 2166 O ATOM 5614 N ILE B1078 -42.867 -4.079 84.778 1.00100.16 N ANISOU 5614 N ILE B1078 13322 14454 10282 -299 -1294 2001 N ATOM 5615 CA ILE B1078 -44.234 -4.610 84.734 1.00 99.80 C ANISOU 5615 CA ILE B1078 13313 14542 10064 -416 -1212 2164 C ATOM 5616 C ILE B1078 -44.152 -6.132 84.927 1.00104.39 C ANISOU 5616 C ILE B1078 13982 14975 10707 -521 -1451 2332 C ATOM 5617 O ILE B1078 -44.904 -6.690 85.733 1.00105.04 O ANISOU 5617 O ILE B1078 14167 15161 10580 -677 -1510 2524 O ATOM 5618 CB ILE B1078 -44.941 -4.196 83.397 1.00101.03 C ANISOU 5618 CB ILE B1078 13357 14745 10284 -367 -987 2095 C ATOM 5619 CG1 ILE B1078 -45.466 -2.745 83.470 1.00100.68 C ANISOU 5619 CG1 ILE B1078 13264 14878 10112 -299 -771 2000 C ATOM 5620 CG2 ILE B1078 -46.074 -5.160 83.010 1.00101.75 C ANISOU 5620 CG2 ILE B1078 13459 14889 10311 -487 -971 2251 C ATOM 5621 CD1 ILE B1078 -45.737 -2.082 82.109 1.00107.36 C ANISOU 5621 CD1 ILE B1078 14008 15713 11071 -217 -596 1905 C ATOM 5622 N LEU B1079 -43.195 -6.779 84.217 1.00100.76 N ANISOU 5622 N LEU B1079 13478 14270 10538 -440 -1595 2247 N ATOM 5623 CA LEU B1079 -42.944 -8.222 84.263 1.00102.19 C ANISOU 5623 CA LEU B1079 13732 14238 10858 -498 -1859 2363 C ATOM 5624 C LEU B1079 -42.520 -8.727 85.649 1.00108.68 C ANISOU 5624 C LEU B1079 14704 15002 11588 -577 -2136 2522 C ATOM 5625 O LEU B1079 -42.675 -9.917 85.929 1.00110.11 O ANISOU 5625 O LEU B1079 14996 15040 11800 -682 -2361 2701 O ATOM 5626 CB LEU B1079 -41.908 -8.637 83.199 1.00101.81 C ANISOU 5626 CB LEU B1079 13568 13955 11160 -356 -1936 2167 C ATOM 5627 CG LEU B1079 -42.347 -8.629 81.730 1.00104.80 C ANISOU 5627 CG LEU B1079 13834 14348 11638 -324 -1734 2050 C ATOM 5628 CD1 LEU B1079 -41.149 -8.780 80.822 1.00105.05 C ANISOU 5628 CD1 LEU B1079 13730 14210 11974 -181 -1774 1807 C ATOM 5629 CD2 LEU B1079 -43.359 -9.733 81.429 1.00107.39 C ANISOU 5629 CD2 LEU B1079 14232 14635 11935 -452 -1785 2207 C ATOM 5630 N ARG B1080 -41.982 -7.826 86.503 1.00105.41 N ANISOU 5630 N ARG B1080 14302 14689 11060 -536 -2137 2463 N ATOM 5631 CA ARG B1080 -41.549 -8.131 87.871 1.00107.18 C ANISOU 5631 CA ARG B1080 14673 14900 11152 -615 -2395 2605 C ATOM 5632 C ARG B1080 -42.645 -7.854 88.892 1.00111.01 C ANISOU 5632 C ARG B1080 15278 15671 11229 -801 -2291 2781 C ATOM 5633 O ARG B1080 -42.683 -8.518 89.928 1.00113.46 O ANISOU 5633 O ARG B1080 15752 15985 11374 -952 -2511 2992 O ATOM 5634 CB ARG B1080 -40.270 -7.368 88.233 1.00107.62 C ANISOU 5634 CB ARG B1080 14669 14905 11318 -475 -2481 2423 C ATOM 5635 CG ARG B1080 -39.015 -8.056 87.722 1.00120.03 C ANISOU 5635 CG ARG B1080 16156 16178 13271 -337 -2724 2312 C ATOM 5636 CD ARG B1080 -37.753 -7.459 88.310 1.00131.86 C ANISOU 5636 CD ARG B1080 17604 17636 14860 -234 -2869 2170 C ATOM 5637 NE ARG B1080 -37.466 -6.131 87.767 1.00140.29 N ANISOU 5637 NE ARG B1080 18522 18823 15961 -139 -2597 1932 N ATOM 5638 CZ ARG B1080 -36.732 -5.907 86.682 1.00157.03 C ANISOU 5638 CZ ARG B1080 20454 20842 18369 -11 -2510 1711 C ATOM 5639 NH1 ARG B1080 -36.208 -6.920 86.002 1.00146.33 N ANISOU 5639 NH1 ARG B1080 19018 19278 17302 62 -2658 1660 N ATOM 5640 NH2 ARG B1080 -36.518 -4.666 86.265 1.00145.56 N ANISOU 5640 NH2 ARG B1080 18894 19497 16915 35 -2274 1533 N ATOM 5641 N ASN B1081 -43.525 -6.873 88.605 1.00105.02 N ANISOU 5641 N ASN B1081 14435 15157 10310 -792 -1964 2690 N ATOM 5642 CA ASN B1081 -44.656 -6.505 89.457 1.00105.40 C ANISOU 5642 CA ASN B1081 14545 15521 9982 -948 -1808 2796 C ATOM 5643 C ASN B1081 -45.721 -7.605 89.357 1.00110.86 C ANISOU 5643 C ASN B1081 15296 16252 10574 -1146 -1824 3032 C ATOM 5644 O ASN B1081 -46.357 -7.756 88.311 1.00108.90 O ANISOU 5644 O ASN B1081 14948 15988 10440 -1123 -1678 3003 O ATOM 5645 CB ASN B1081 -45.220 -5.140 89.045 1.00102.04 C ANISOU 5645 CB ASN B1081 13983 15299 9490 -836 -1479 2594 C ATOM 5646 CG ASN B1081 -46.162 -4.524 90.046 1.00116.21 C ANISOU 5646 CG ASN B1081 15807 17431 10917 -944 -1317 2613 C ATOM 5647 OD1 ASN B1081 -47.282 -5.000 90.270 1.00108.23 O ANISOU 5647 OD1 ASN B1081 14811 16611 9702 -1109 -1231 2762 O ATOM 5648 ND2 ASN B1081 -45.747 -3.409 90.625 1.00107.56 N ANISOU 5648 ND2 ASN B1081 14702 16430 9738 -851 -1255 2437 N ATOM 5649 N ALA B1082 -45.881 -8.390 90.446 1.00111.02 N ANISOU 5649 N ALA B1082 15489 16317 10378 -1359 -2019 3274 N ATOM 5650 CA ALA B1082 -46.799 -9.533 90.577 1.00112.77 C ANISOU 5650 CA ALA B1082 15806 16562 10478 -1606 -2088 3545 C ATOM 5651 C ALA B1082 -48.270 -9.266 90.212 1.00115.98 C ANISOU 5651 C ALA B1082 16101 17260 10704 -1710 -1771 3554 C ATOM 5652 O ALA B1082 -48.953 -10.188 89.761 1.00116.13 O ANISOU 5652 O ALA B1082 16135 17225 10764 -1854 -1801 3710 O ATOM 5653 CB ALA B1082 -46.702 -10.120 91.977 1.00116.91 C ANISOU 5653 CB ALA B1082 16543 17149 10727 -1838 -2323 3799 C ATOM 5654 N LYS B1083 -48.752 -8.022 90.410 1.00111.16 N ANISOU 5654 N LYS B1083 15375 16948 9914 -1634 -1487 3377 N ATOM 5655 CA LYS B1083 -50.133 -7.636 90.113 1.00110.21 C ANISOU 5655 CA LYS B1083 15114 17124 9635 -1697 -1188 3348 C ATOM 5656 C LYS B1083 -50.362 -7.336 88.624 1.00109.68 C ANISOU 5656 C LYS B1083 14879 16943 9851 -1511 -1045 3193 C ATOM 5657 O LYS B1083 -51.388 -7.749 88.078 1.00109.72 O ANISOU 5657 O LYS B1083 14807 17043 9840 -1612 -939 3268 O ATOM 5658 CB LYS B1083 -50.565 -6.446 90.985 1.00113.76 C ANISOU 5658 CB LYS B1083 15504 17930 9789 -1677 -966 3202 C ATOM 5659 CG LYS B1083 -52.077 -6.278 91.072 1.00131.66 C ANISOU 5659 CG LYS B1083 17640 20565 11820 -1810 -699 3216 C ATOM 5660 CD LYS B1083 -52.483 -5.160 92.007 1.00144.13 C ANISOU 5660 CD LYS B1083 19154 22500 13109 -1784 -490 3041 C ATOM 5661 CE LYS B1083 -53.981 -5.106 92.168 1.00158.08 C ANISOU 5661 CE LYS B1083 20767 24656 14640 -1931 -236 3050 C ATOM 5662 NZ LYS B1083 -54.388 -4.064 93.145 1.00170.82 N ANISOU 5662 NZ LYS B1083 22306 26636 15961 -1907 -30 2847 N ATOM 5663 N LEU B1084 -49.415 -6.624 87.979 1.00102.28 N ANISOU 5663 N LEU B1084 13887 15817 9158 -1262 -1046 2986 N ATOM 5664 CA LEU B1084 -49.495 -6.213 86.572 1.00 98.64 C ANISOU 5664 CA LEU B1084 13283 15255 8941 -1090 -915 2833 C ATOM 5665 C LEU B1084 -49.077 -7.296 85.571 1.00101.05 C ANISOU 5665 C LEU B1084 13607 15268 9519 -1091 -1076 2888 C ATOM 5666 O LEU B1084 -49.702 -7.394 84.516 1.00 99.38 O ANISOU 5666 O LEU B1084 13299 15061 9401 -1072 -966 2859 O ATOM 5667 CB LEU B1084 -48.694 -4.920 86.325 1.00 96.82 C ANISOU 5667 CB LEU B1084 12987 14973 8826 -859 -830 2593 C ATOM 5668 CG LEU B1084 -49.036 -3.696 87.194 1.00101.76 C ANISOU 5668 CG LEU B1084 13583 15849 9230 -812 -669 2475 C ATOM 5669 CD1 LEU B1084 -47.832 -2.796 87.361 1.00101.34 C ANISOU 5669 CD1 LEU B1084 13549 15664 9292 -650 -719 2297 C ATOM 5670 CD2 LEU B1084 -50.191 -2.903 86.617 1.00102.23 C ANISOU 5670 CD2 LEU B1084 13493 16103 9248 -743 -417 2381 C ATOM 5671 N LYS B1085 -48.017 -8.085 85.889 1.00 98.32 N ANISOU 5671 N LYS B1085 13380 14669 9309 -1101 -1346 2948 N ATOM 5672 CA LYS B1085 -47.460 -9.171 85.058 1.00 97.89 C ANISOU 5672 CA LYS B1085 13348 14305 9542 -1080 -1538 2964 C ATOM 5673 C LYS B1085 -48.498 -10.109 84.366 1.00102.76 C ANISOU 5673 C LYS B1085 13954 14915 10175 -1226 -1520 3088 C ATOM 5674 O LYS B1085 -48.425 -10.214 83.138 1.00100.23 O ANISOU 5674 O LYS B1085 13542 14479 10061 -1127 -1468 2961 O ATOM 5675 CB LYS B1085 -46.365 -9.955 85.825 1.00101.41 C ANISOU 5675 CB LYS B1085 13934 14510 10086 -1098 -1868 3050 C ATOM 5676 CG LYS B1085 -45.715 -11.127 85.074 1.00108.55 C ANISOU 5676 CG LYS B1085 14858 15066 11319 -1053 -2103 3039 C ATOM 5677 CD LYS B1085 -46.141 -12.500 85.624 1.00119.34 C ANISOU 5677 CD LYS B1085 16396 16302 12647 -1272 -2358 3316 C ATOM 5678 CE LYS B1085 -45.270 -13.037 86.748 1.00132.68 C ANISOU 5678 CE LYS B1085 18249 17819 14346 -1310 -2696 3456 C ATOM 5679 NZ LYS B1085 -45.595 -12.438 88.075 1.00139.29 N ANISOU 5679 NZ LYS B1085 19179 18935 14810 -1449 -2648 3598 N ATOM 5680 N PRO B1086 -49.455 -10.784 85.081 1.00102.29 N ANISOU 5680 N PRO B1086 13981 14986 9898 -1473 -1558 3325 N ATOM 5681 CA PRO B1086 -50.393 -11.686 84.377 1.00102.84 C ANISOU 5681 CA PRO B1086 14034 15031 10010 -1622 -1556 3433 C ATOM 5682 C PRO B1086 -51.320 -11.030 83.351 1.00106.10 C ANISOU 5682 C PRO B1086 14265 15637 10410 -1560 -1281 3307 C ATOM 5683 O PRO B1086 -51.594 -11.641 82.314 1.00105.39 O ANISOU 5683 O PRO B1086 14136 15426 10482 -1573 -1303 3284 O ATOM 5684 CB PRO B1086 -51.172 -12.358 85.515 1.00107.16 C ANISOU 5684 CB PRO B1086 14705 15723 10286 -1923 -1633 3716 C ATOM 5685 CG PRO B1086 -51.055 -11.432 86.656 1.00111.91 C ANISOU 5685 CG PRO B1086 15324 16571 10626 -1915 -1539 3706 C ATOM 5686 CD PRO B1086 -49.700 -10.810 86.539 1.00106.02 C ANISOU 5686 CD PRO B1086 14575 15637 10070 -1653 -1613 3508 C ATOM 5687 N VAL B1087 -51.798 -9.800 83.640 1.00102.53 N ANISOU 5687 N VAL B1087 13707 15475 9774 -1489 -1042 3219 N ATOM 5688 CA VAL B1087 -52.696 -9.024 82.767 1.00101.09 C ANISOU 5688 CA VAL B1087 13349 15486 9575 -1408 -799 3103 C ATOM 5689 C VAL B1087 -51.961 -8.608 81.478 1.00103.00 C ANISOU 5689 C VAL B1087 13527 15537 10071 -1190 -777 2905 C ATOM 5690 O VAL B1087 -52.502 -8.787 80.385 1.00101.86 O ANISOU 5690 O VAL B1087 13302 15391 10011 -1187 -717 2871 O ATOM 5691 CB VAL B1087 -53.334 -7.811 83.510 1.00105.08 C ANISOU 5691 CB VAL B1087 13762 16322 9842 -1368 -581 3042 C ATOM 5692 CG1 VAL B1087 -54.298 -7.041 82.606 1.00103.75 C ANISOU 5692 CG1 VAL B1087 13407 16328 9684 -1271 -370 2932 C ATOM 5693 CG2 VAL B1087 -54.042 -8.256 84.789 1.00107.45 C ANISOU 5693 CG2 VAL B1087 14116 16855 9856 -1613 -583 3224 C ATOM 5694 N TYR B1088 -50.721 -8.086 81.618 1.00 98.65 N ANISOU 5694 N TYR B1088 13014 14840 9630 -1030 -831 2779 N ATOM 5695 CA TYR B1088 -49.858 -7.642 80.522 1.00 96.61 C ANISOU 5695 CA TYR B1088 12698 14420 9591 -848 -804 2588 C ATOM 5696 C TYR B1088 -49.645 -8.756 79.491 1.00101.44 C ANISOU 5696 C TYR B1088 13317 14822 10405 -879 -922 2572 C ATOM 5697 O TYR B1088 -49.793 -8.502 78.297 1.00100.15 O ANISOU 5697 O TYR B1088 13067 14663 10323 -815 -818 2462 O ATOM 5698 CB TYR B1088 -48.513 -7.127 81.075 1.00 97.16 C ANISOU 5698 CB TYR B1088 12811 14366 9739 -723 -883 2481 C ATOM 5699 CG TYR B1088 -47.595 -6.522 80.033 1.00 96.89 C ANISOU 5699 CG TYR B1088 12699 14210 9903 -560 -825 2279 C ATOM 5700 CD1 TYR B1088 -47.716 -5.187 79.659 1.00 97.51 C ANISOU 5700 CD1 TYR B1088 12702 14406 9940 -455 -637 2172 C ATOM 5701 CD2 TYR B1088 -46.581 -7.273 79.448 1.00 97.60 C ANISOU 5701 CD2 TYR B1088 12790 14068 10225 -516 -965 2189 C ATOM 5702 CE1 TYR B1088 -46.874 -4.623 78.702 1.00 96.49 C ANISOU 5702 CE1 TYR B1088 12513 14179 9969 -346 -581 2010 C ATOM 5703 CE2 TYR B1088 -45.736 -6.723 78.485 1.00 97.35 C ANISOU 5703 CE2 TYR B1088 12670 13966 10351 -395 -889 1995 C ATOM 5704 CZ TYR B1088 -45.889 -5.397 78.112 1.00102.49 C ANISOU 5704 CZ TYR B1088 13261 14750 10931 -328 -693 1921 C ATOM 5705 OH TYR B1088 -45.065 -4.850 77.161 1.00101.61 O ANISOU 5705 OH TYR B1088 13074 14582 10951 -249 -615 1754 O ATOM 5706 N ASP B1089 -49.339 -9.987 79.953 1.00100.18 N ANISOU 5706 N ASP B1089 13267 14480 10318 -986 -1149 2683 N ATOM 5707 CA ASP B1089 -49.119 -11.151 79.090 1.00100.85 C ANISOU 5707 CA ASP B1089 13371 14332 10614 -1014 -1294 2652 C ATOM 5708 C ASP B1089 -50.375 -11.560 78.317 1.00105.34 C ANISOU 5708 C ASP B1089 13891 15009 11124 -1141 -1209 2713 C ATOM 5709 O ASP B1089 -50.259 -12.027 77.184 1.00104.89 O ANISOU 5709 O ASP B1089 13795 14832 11225 -1109 -1227 2595 O ATOM 5710 CB ASP B1089 -48.549 -12.334 79.892 1.00104.85 C ANISOU 5710 CB ASP B1089 14024 14593 11222 -1096 -1592 2775 C ATOM 5711 CG ASP B1089 -47.128 -12.146 80.409 1.00115.65 C ANISOU 5711 CG ASP B1089 15421 15792 12728 -947 -1736 2676 C ATOM 5712 OD1 ASP B1089 -46.583 -11.025 80.272 1.00114.66 O ANISOU 5712 OD1 ASP B1089 15206 15763 12595 -799 -1586 2519 O ATOM 5713 OD2 ASP B1089 -46.563 -13.116 80.957 1.00123.04 O ANISOU 5713 OD2 ASP B1089 16469 16491 13790 -983 -2014 2760 O ATOM 5714 N SER B1090 -51.569 -11.350 78.915 1.00102.56 N ANISOU 5714 N SER B1090 13524 14905 10539 -1285 -1107 2877 N ATOM 5715 CA SER B1090 -52.861 -11.663 78.295 1.00102.76 C ANISOU 5715 CA SER B1090 13477 15077 10491 -1419 -1022 2945 C ATOM 5716 C SER B1090 -53.249 -10.621 77.241 1.00105.44 C ANISOU 5716 C SER B1090 13667 15578 10816 -1282 -811 2796 C ATOM 5717 O SER B1090 -53.960 -10.955 76.288 1.00105.48 O ANISOU 5717 O SER B1090 13610 15622 10848 -1339 -782 2783 O ATOM 5718 CB SER B1090 -53.956 -11.765 79.350 1.00107.61 C ANISOU 5718 CB SER B1090 14097 15930 10861 -1624 -978 3155 C ATOM 5719 OG SER B1090 -54.374 -10.486 79.798 1.00115.08 O ANISOU 5719 OG SER B1090 14940 17159 11627 -1538 -767 3109 O ATOM 5720 N LEU B1091 -52.802 -9.357 77.435 1.00100.20 N ANISOU 5720 N LEU B1091 12959 15003 10109 -1113 -683 2693 N ATOM 5721 CA LEU B1091 -53.078 -8.234 76.533 1.00 98.00 C ANISOU 5721 CA LEU B1091 12565 14851 9818 -976 -508 2573 C ATOM 5722 C LEU B1091 -52.330 -8.356 75.207 1.00100.04 C ANISOU 5722 C LEU B1091 12815 14943 10251 -890 -528 2420 C ATOM 5723 O LEU B1091 -51.380 -9.131 75.087 1.00 99.37 O ANISOU 5723 O LEU B1091 12798 14640 10320 -885 -661 2356 O ATOM 5724 CB LEU B1091 -52.739 -6.878 77.196 1.00 97.21 C ANISOU 5724 CB LEU B1091 12444 14851 9642 -833 -395 2510 C ATOM 5725 CG LEU B1091 -53.651 -6.355 78.317 1.00102.54 C ANISOU 5725 CG LEU B1091 13076 15773 10110 -877 -301 2594 C ATOM 5726 CD1 LEU B1091 -52.994 -5.199 79.045 1.00102.13 C ANISOU 5726 CD1 LEU B1091 13041 15741 10021 -733 -241 2498 C ATOM 5727 CD2 LEU B1091 -54.996 -5.902 77.787 1.00104.71 C ANISOU 5727 CD2 LEU B1091 13206 16275 10304 -881 -168 2607 C ATOM 5728 N ASP B1092 -52.776 -7.572 74.216 1.00 96.00 N ANISOU 5728 N ASP B1092 12217 14548 9710 -824 -400 2355 N ATOM 5729 CA ASP B1092 -52.210 -7.479 72.869 1.00 95.03 C ANISOU 5729 CA ASP B1092 12076 14341 9688 -764 -377 2213 C ATOM 5730 C ASP B1092 -51.276 -6.259 72.789 1.00 97.10 C ANISOU 5730 C ASP B1092 12334 14582 9977 -617 -287 2105 C ATOM 5731 O ASP B1092 -51.382 -5.366 73.632 1.00 96.71 O ANISOU 5731 O ASP B1092 12280 14609 9854 -553 -230 2145 O ATOM 5732 CB ASP B1092 -53.339 -7.373 71.828 1.00 97.03 C ANISOU 5732 CB ASP B1092 12253 14746 9866 -813 -315 2241 C ATOM 5733 CG ASP B1092 -54.431 -6.395 72.214 1.00107.93 C ANISOU 5733 CG ASP B1092 13552 16347 11111 -779 -214 2335 C ATOM 5734 OD1 ASP B1092 -55.436 -6.836 72.810 1.00109.71 O ANISOU 5734 OD1 ASP B1092 13732 16696 11256 -881 -227 2449 O ATOM 5735 OD2 ASP B1092 -54.263 -5.185 71.953 1.00113.48 O ANISOU 5735 OD2 ASP B1092 14230 17094 11795 -652 -126 2288 O ATOM 5736 N ALA B1093 -50.377 -6.223 71.775 1.00 92.19 N ANISOU 5736 N ALA B1093 11708 13866 9453 -578 -270 1960 N ATOM 5737 CA ALA B1093 -49.390 -5.157 71.547 1.00 90.86 C ANISOU 5737 CA ALA B1093 11533 13669 9321 -479 -187 1853 C ATOM 5738 C ALA B1093 -49.946 -3.727 71.628 1.00 93.33 C ANISOU 5738 C ALA B1093 11828 14108 9526 -412 -78 1918 C ATOM 5739 O ALA B1093 -49.294 -2.858 72.211 1.00 92.25 O ANISOU 5739 O ALA B1093 11707 13933 9409 -335 -47 1882 O ATOM 5740 CB ALA B1093 -48.683 -5.373 70.221 1.00 91.71 C ANISOU 5740 CB ALA B1093 11616 13732 9497 -496 -154 1701 C ATOM 5741 N VAL B1094 -51.148 -3.489 71.059 1.00 89.80 N ANISOU 5741 N VAL B1094 11342 13799 8980 -437 -39 2003 N ATOM 5742 CA VAL B1094 -51.809 -2.174 71.069 1.00 89.31 C ANISOU 5742 CA VAL B1094 11252 13838 8842 -354 33 2060 C ATOM 5743 C VAL B1094 -52.181 -1.787 72.502 1.00 92.01 C ANISOU 5743 C VAL B1094 11583 14233 9143 -294 40 2104 C ATOM 5744 O VAL B1094 -51.882 -0.673 72.929 1.00 91.27 O ANISOU 5744 O VAL B1094 11503 14120 9056 -193 83 2070 O ATOM 5745 CB VAL B1094 -53.044 -2.096 70.130 1.00 93.94 C ANISOU 5745 CB VAL B1094 11781 14561 9350 -385 41 2138 C ATOM 5746 CG1 VAL B1094 -53.472 -0.645 69.911 1.00 93.86 C ANISOU 5746 CG1 VAL B1094 11755 14600 9309 -275 85 2175 C ATOM 5747 CG2 VAL B1094 -52.778 -2.784 68.793 1.00 94.08 C ANISOU 5747 CG2 VAL B1094 11816 14556 9373 -481 21 2088 C ATOM 5748 N ARG B1095 -52.821 -2.721 73.234 1.00 88.30 N ANISOU 5748 N ARG B1095 11094 13833 8624 -374 -4 2175 N ATOM 5749 CA ARG B1095 -53.247 -2.541 74.620 1.00 88.30 C ANISOU 5749 CA ARG B1095 11080 13930 8542 -361 11 2219 C ATOM 5750 C ARG B1095 -52.077 -2.552 75.621 1.00 92.48 C ANISOU 5750 C ARG B1095 11695 14337 9106 -338 -35 2169 C ATOM 5751 O ARG B1095 -52.129 -1.823 76.614 1.00 92.72 O ANISOU 5751 O ARG B1095 11727 14433 9069 -276 4 2150 O ATOM 5752 CB ARG B1095 -54.345 -3.541 74.982 1.00 87.49 C ANISOU 5752 CB ARG B1095 10928 13965 8351 -497 -16 2331 C ATOM 5753 CG ARG B1095 -55.733 -3.010 74.677 1.00 92.86 C ANISOU 5753 CG ARG B1095 11475 14853 8954 -471 59 2369 C ATOM 5754 CD ARG B1095 -56.678 -4.125 74.304 1.00101.27 C ANISOU 5754 CD ARG B1095 12482 16013 9984 -633 17 2463 C ATOM 5755 NE ARG B1095 -57.968 -3.607 73.849 1.00112.39 N ANISOU 5755 NE ARG B1095 13739 17622 11344 -599 72 2484 N ATOM 5756 CZ ARG B1095 -58.852 -4.307 73.144 1.00129.67 C ANISOU 5756 CZ ARG B1095 15849 19899 13519 -713 35 2545 C ATOM 5757 NH1 ARG B1095 -58.590 -5.561 72.793 1.00117.66 N ANISOU 5757 NH1 ARG B1095 14403 18270 12032 -873 -55 2584 N ATOM 5758 NH2 ARG B1095 -60.002 -3.757 72.780 1.00118.55 N ANISOU 5758 NH2 ARG B1095 14285 18680 12081 -663 72 2556 N ATOM 5759 N ARG B1096 -51.007 -3.336 75.337 1.00 88.26 N ANISOU 5759 N ARG B1096 11222 13628 8685 -378 -123 2124 N ATOM 5760 CA ARG B1096 -49.791 -3.390 76.158 1.00 87.70 C ANISOU 5760 CA ARG B1096 11218 13425 8680 -348 -197 2066 C ATOM 5761 C ARG B1096 -49.131 -2.008 76.165 1.00 91.37 C ANISOU 5761 C ARG B1096 11680 13863 9175 -227 -121 1964 C ATOM 5762 O ARG B1096 -48.625 -1.575 77.200 1.00 91.56 O ANISOU 5762 O ARG B1096 11740 13870 9179 -187 -145 1933 O ATOM 5763 CB ARG B1096 -48.810 -4.442 75.616 1.00 86.09 C ANISOU 5763 CB ARG B1096 11041 13037 8633 -384 -308 2003 C ATOM 5764 CG ARG B1096 -49.131 -5.855 76.066 1.00 91.19 C ANISOU 5764 CG ARG B1096 11733 13631 9282 -500 -449 2105 C ATOM 5765 CD ARG B1096 -48.109 -6.847 75.562 1.00 95.99 C ANISOU 5765 CD ARG B1096 12361 14028 10084 -500 -579 2006 C ATOM 5766 NE ARG B1096 -48.519 -8.221 75.852 1.00105.27 N ANISOU 5766 NE ARG B1096 13595 15118 11286 -618 -735 2113 N ATOM 5767 CZ ARG B1096 -47.893 -9.306 75.409 1.00122.15 C ANISOU 5767 CZ ARG B1096 15752 17053 13605 -627 -880 2036 C ATOM 5768 NH1 ARG B1096 -46.817 -9.194 74.640 1.00113.38 N ANISOU 5768 NH1 ARG B1096 14584 15839 12657 -524 -866 1831 N ATOM 5769 NH2 ARG B1096 -48.343 -10.513 75.723 1.00109.76 N ANISOU 5769 NH2 ARG B1096 14255 15384 12064 -747 -1040 2154 N ATOM 5770 N ALA B1097 -49.196 -1.305 75.014 1.00 87.20 N ANISOU 5770 N ALA B1097 11116 13335 8680 -188 -39 1922 N ATOM 5771 CA ALA B1097 -48.671 0.043 74.807 1.00 86.80 C ANISOU 5771 CA ALA B1097 11073 13241 8665 -101 28 1849 C ATOM 5772 C ALA B1097 -49.473 1.088 75.587 1.00 91.66 C ANISOU 5772 C ALA B1097 11679 13953 9192 -14 78 1870 C ATOM 5773 O ALA B1097 -48.924 2.134 75.939 1.00 91.35 O ANISOU 5773 O ALA B1097 11670 13850 9190 60 97 1797 O ATOM 5774 CB ALA B1097 -48.681 0.375 73.328 1.00 87.23 C ANISOU 5774 CB ALA B1097 11110 13284 8749 -120 83 1840 C ATOM 5775 N ALA B1098 -50.769 0.810 75.846 1.00 89.17 N ANISOU 5775 N ALA B1098 11313 13796 8773 -25 99 1950 N ATOM 5776 CA ALA B1098 -51.655 1.695 76.607 1.00 89.97 C ANISOU 5776 CA ALA B1098 11369 14025 8791 66 156 1937 C ATOM 5777 C ALA B1098 -51.349 1.586 78.102 1.00 94.65 C ANISOU 5777 C ALA B1098 11998 14662 9304 57 138 1900 C ATOM 5778 O ALA B1098 -51.383 2.594 78.809 1.00 94.71 O ANISOU 5778 O ALA B1098 12006 14697 9282 156 177 1812 O ATOM 5779 CB ALA B1098 -53.110 1.350 76.334 1.00 91.34 C ANISOU 5779 CB ALA B1098 11440 14380 8884 42 189 2018 C ATOM 5780 N LEU B1099 -51.026 0.365 78.569 1.00 91.53 N ANISOU 5780 N LEU B1099 11644 14260 8873 -65 63 1965 N ATOM 5781 CA LEU B1099 -50.673 0.077 79.957 1.00 92.50 C ANISOU 5781 CA LEU B1099 11826 14423 8898 -110 11 1966 C ATOM 5782 C LEU B1099 -49.331 0.741 80.303 1.00 96.91 C ANISOU 5782 C LEU B1099 12453 14823 9546 -37 -37 1852 C ATOM 5783 O LEU B1099 -49.181 1.262 81.409 1.00 97.13 O ANISOU 5783 O LEU B1099 12514 14910 9482 -8 -38 1793 O ATOM 5784 CB LEU B1099 -50.631 -1.449 80.173 1.00 92.90 C ANISOU 5784 CB LEU B1099 11920 14456 8920 -267 -99 2093 C ATOM 5785 CG LEU B1099 -50.612 -1.965 81.614 1.00 98.93 C ANISOU 5785 CG LEU B1099 12755 15307 9527 -368 -169 2163 C ATOM 5786 CD1 LEU B1099 -51.948 -1.745 82.309 1.00100.60 C ANISOU 5786 CD1 LEU B1099 12897 15802 9526 -420 -51 2203 C ATOM 5787 CD2 LEU B1099 -50.288 -3.441 81.646 1.00101.46 C ANISOU 5787 CD2 LEU B1099 13151 15513 9888 -511 -330 2293 C ATOM 5788 N ILE B1100 -48.385 0.763 79.331 1.00 93.31 N ANISOU 5788 N ILE B1100 12006 14189 9260 -18 -69 1806 N ATOM 5789 CA ILE B1100 -47.061 1.394 79.435 1.00 93.26 C ANISOU 5789 CA ILE B1100 12035 14031 9367 33 -107 1692 C ATOM 5790 C ILE B1100 -47.226 2.922 79.562 1.00 99.15 C ANISOU 5790 C ILE B1100 12780 14785 10107 138 -23 1602 C ATOM 5791 O ILE B1100 -46.487 3.551 80.328 1.00 99.08 O ANISOU 5791 O ILE B1100 12813 14722 10113 174 -57 1507 O ATOM 5792 CB ILE B1100 -46.143 0.953 78.249 1.00 95.31 C ANISOU 5792 CB ILE B1100 12272 14145 9795 3 -133 1657 C ATOM 5793 CG1 ILE B1100 -45.595 -0.471 78.481 1.00 95.91 C ANISOU 5793 CG1 ILE B1100 12362 14154 9927 -67 -268 1687 C ATOM 5794 CG2 ILE B1100 -44.990 1.942 77.985 1.00 95.58 C ANISOU 5794 CG2 ILE B1100 12305 14060 9950 45 -115 1534 C ATOM 5795 CD1 ILE B1100 -45.235 -1.246 77.219 1.00102.88 C ANISOU 5795 CD1 ILE B1100 13198 14954 10939 -104 -275 1658 C ATOM 5796 N ASN B1101 -48.218 3.503 78.842 1.00 97.07 N ANISOU 5796 N ASN B1101 12471 14580 9830 190 65 1629 N ATOM 5797 CA ASN B1101 -48.531 4.938 78.875 1.00 98.20 C ANISOU 5797 CA ASN B1101 12614 14702 9994 307 120 1552 C ATOM 5798 C ASN B1101 -48.894 5.370 80.298 1.00104.64 C ANISOU 5798 C ASN B1101 13435 15629 10692 367 132 1466 C ATOM 5799 O ASN B1101 -48.415 6.410 80.760 1.00104.99 O ANISOU 5799 O ASN B1101 13521 15590 10781 443 125 1345 O ATOM 5800 CB ASN B1101 -49.653 5.281 77.888 1.00 99.57 C ANISOU 5800 CB ASN B1101 12730 14928 10175 356 175 1617 C ATOM 5801 CG ASN B1101 -49.795 6.757 77.605 1.00125.05 C ANISOU 5801 CG ASN B1101 15975 18055 13485 478 189 1554 C ATOM 5802 OD1 ASN B1101 -50.337 7.523 78.410 1.00122.40 O ANISOU 5802 OD1 ASN B1101 15620 17767 13121 592 208 1462 O ATOM 5803 ND2 ASN B1101 -49.331 7.184 76.440 1.00116.04 N ANISOU 5803 ND2 ASN B1101 14873 16772 12444 450 175 1599 N ATOM 5804 N MET B1102 -49.693 4.536 81.001 1.00102.42 N ANISOU 5804 N MET B1102 13118 15543 10254 312 148 1525 N ATOM 5805 CA MET B1102 -50.110 4.745 82.390 1.00104.01 C ANISOU 5805 CA MET B1102 13317 15914 10287 327 176 1450 C ATOM 5806 C MET B1102 -48.919 4.621 83.349 1.00109.26 C ANISOU 5806 C MET B1102 14081 16509 10923 278 82 1397 C ATOM 5807 O MET B1102 -48.783 5.448 84.251 1.00110.22 O ANISOU 5807 O MET B1102 14230 16667 10981 341 94 1259 O ATOM 5808 CB MET B1102 -51.209 3.743 82.776 1.00107.00 C ANISOU 5808 CB MET B1102 13631 16533 10492 225 218 1560 C ATOM 5809 CG MET B1102 -52.589 4.178 82.348 1.00111.34 C ANISOU 5809 CG MET B1102 14047 17236 11023 305 327 1544 C ATOM 5810 SD MET B1102 -53.859 2.909 82.581 1.00116.26 S ANISOU 5810 SD MET B1102 14569 18139 11464 142 378 1691 S ATOM 5811 CE MET B1102 -54.190 3.091 84.306 1.00115.16 C ANISOU 5811 CE MET B1102 14420 18264 11070 100 450 1592 C ATOM 5812 N VAL B1103 -48.062 3.585 83.151 1.00105.23 N ANISOU 5812 N VAL B1103 13619 15895 10467 173 -26 1493 N ATOM 5813 CA VAL B1103 -46.865 3.302 83.961 1.00105.31 C ANISOU 5813 CA VAL B1103 13712 15822 10480 124 -157 1463 C ATOM 5814 C VAL B1103 -45.854 4.458 83.870 1.00110.46 C ANISOU 5814 C VAL B1103 14385 16310 11274 211 -173 1308 C ATOM 5815 O VAL B1103 -45.220 4.800 84.867 1.00110.60 O ANISOU 5815 O VAL B1103 14457 16325 11240 212 -243 1218 O ATOM 5816 CB VAL B1103 -46.276 1.889 83.651 1.00108.18 C ANISOU 5816 CB VAL B1103 14098 16092 10913 18 -287 1591 C ATOM 5817 CG1 VAL B1103 -44.881 1.693 84.252 1.00108.22 C ANISOU 5817 CG1 VAL B1103 14162 15965 10993 2 -449 1542 C ATOM 5818 CG2 VAL B1103 -47.220 0.791 84.141 1.00108.66 C ANISOU 5818 CG2 VAL B1103 14174 16313 10798 -101 -304 1749 C ATOM 5819 N PHE B1104 -45.775 5.105 82.699 1.00108.05 N ANISOU 5819 N PHE B1104 14042 15882 11131 267 -110 1282 N ATOM 5820 CA PHE B1104 -44.914 6.267 82.463 1.00108.67 C ANISOU 5820 CA PHE B1104 14142 15796 11352 321 -116 1157 C ATOM 5821 C PHE B1104 -45.419 7.500 83.238 1.00114.75 C ANISOU 5821 C PHE B1104 14938 16605 12055 423 -71 1024 C ATOM 5822 O PHE B1104 -44.616 8.347 83.634 1.00115.21 O ANISOU 5822 O PHE B1104 15042 16550 12184 447 -116 897 O ATOM 5823 CB PHE B1104 -44.871 6.589 80.961 1.00109.55 C ANISOU 5823 CB PHE B1104 14220 15790 11614 322 -57 1201 C ATOM 5824 CG PHE B1104 -43.578 6.244 80.262 1.00110.52 C ANISOU 5824 CG PHE B1104 14326 15779 11886 242 -103 1192 C ATOM 5825 CD1 PHE B1104 -43.344 4.957 79.791 1.00112.84 C ANISOU 5825 CD1 PHE B1104 14577 16092 12203 173 -137 1263 C ATOM 5826 CD2 PHE B1104 -42.619 7.221 80.018 1.00113.09 C ANISOU 5826 CD2 PHE B1104 14666 15962 12341 230 -109 1099 C ATOM 5827 CE1 PHE B1104 -42.160 4.647 79.113 1.00113.48 C ANISOU 5827 CE1 PHE B1104 14613 16072 12435 113 -166 1214 C ATOM 5828 CE2 PHE B1104 -41.437 6.910 79.337 1.00115.60 C ANISOU 5828 CE2 PHE B1104 14934 16194 12793 144 -129 1071 C ATOM 5829 CZ PHE B1104 -41.215 5.625 78.891 1.00113.01 C ANISOU 5829 CZ PHE B1104 14545 15906 12486 96 -152 1116 C ATOM 5830 N GLN B1105 -46.749 7.582 83.449 1.00112.08 N ANISOU 5830 N GLN B1105 14559 16433 11594 484 16 1035 N ATOM 5831 CA GLN B1105 -47.434 8.685 84.115 1.00113.69 C ANISOU 5831 CA GLN B1105 14755 16699 11741 607 73 880 C ATOM 5832 C GLN B1105 -47.338 8.919 85.631 1.00121.04 C ANISOU 5832 C GLN B1105 15726 17763 12501 614 57 732 C ATOM 5833 O GLN B1105 -46.953 10.008 86.049 1.00121.94 O ANISOU 5833 O GLN B1105 15883 17777 12673 693 36 557 O ATOM 5834 CB GLN B1105 -48.936 8.636 83.806 1.00115.15 C ANISOU 5834 CB GLN B1105 14841 17051 11860 676 176 919 C ATOM 5835 CG GLN B1105 -49.639 9.982 83.878 1.00128.16 C ANISOU 5835 CG GLN B1105 16453 18672 13572 855 224 755 C ATOM 5836 CD GLN B1105 -51.024 9.939 83.274 1.00147.44 C ANISOU 5836 CD GLN B1105 18771 21238 16011 935 300 807 C ATOM 5837 OE1 GLN B1105 -51.526 8.891 82.845 1.00142.54 O ANISOU 5837 OE1 GLN B1105 18091 20748 15319 841 328 966 O ATOM 5838 NE2 GLN B1105 -51.679 11.090 83.221 1.00140.73 N ANISOU 5838 NE2 GLN B1105 17874 20340 15257 1116 317 665 N ATOM 5839 N MET B1106 -47.716 7.915 86.446 1.00119.00 N ANISOU 5839 N MET B1106 15462 17731 12023 516 62 803 N ATOM 5840 CA MET B1106 -47.749 8.017 87.908 1.00121.17 C ANISOU 5840 CA MET B1106 15778 18191 12071 488 56 683 C ATOM 5841 C MET B1106 -46.892 6.916 88.563 1.00125.25 C ANISOU 5841 C MET B1106 16381 18734 12475 325 -81 807 C ATOM 5842 O MET B1106 -46.731 6.906 89.791 1.00126.55 O ANISOU 5842 O MET B1106 16608 19044 12432 268 -122 736 O ATOM 5843 CB MET B1106 -49.143 8.132 88.576 1.00125.50 C ANISOU 5843 CB MET B1106 16241 19042 12401 522 200 604 C ATOM 5844 CG MET B1106 -50.339 7.978 87.633 1.00128.71 C ANISOU 5844 CG MET B1106 16517 19518 12870 577 310 688 C ATOM 5845 SD MET B1106 -50.714 6.268 87.172 1.00131.70 S ANISOU 5845 SD MET B1106 16872 20005 13164 383 294 986 S ATOM 5846 CE MET B1106 -52.291 6.504 86.363 1.00128.67 C ANISOU 5846 CE MET B1106 16306 19761 12821 482 440 986 C ATOM 5847 N GLY B1107 -46.335 6.029 87.740 1.00120.15 N ANISOU 5847 N GLY B1107 15739 17943 11969 256 -164 977 N ATOM 5848 CA GLY B1107 -45.503 4.919 88.192 1.00119.98 C ANISOU 5848 CA GLY B1107 15788 17893 11905 126 -328 1103 C ATOM 5849 C GLY B1107 -46.258 3.607 88.269 1.00124.20 C ANISOU 5849 C GLY B1107 16322 18573 12294 -1 -335 1309 C ATOM 5850 O GLY B1107 -47.456 3.564 87.979 1.00123.52 O ANISOU 5850 O GLY B1107 16164 18638 12129 2 -193 1347 O ATOM 5851 N GLU B1108 -45.561 2.530 88.669 1.00121.90 N ANISOU 5851 N GLU B1108 16108 18228 11981 -116 -515 1445 N ATOM 5852 CA GLU B1108 -46.125 1.182 88.787 1.00122.78 C ANISOU 5852 CA GLU B1108 16250 18426 11976 -265 -571 1665 C ATOM 5853 C GLU B1108 -47.120 1.021 89.935 1.00130.22 C ANISOU 5853 C GLU B1108 17229 19677 12571 -389 -503 1720 C ATOM 5854 O GLU B1108 -48.121 0.324 89.761 1.00130.28 O ANISOU 5854 O GLU B1108 17202 19820 12477 -492 -432 1860 O ATOM 5855 CB GLU B1108 -45.012 0.138 88.905 1.00124.40 C ANISOU 5855 CB GLU B1108 16536 18440 12291 -334 -822 1783 C ATOM 5856 CG GLU B1108 -44.340 -0.175 87.581 1.00134.46 C ANISOU 5856 CG GLU B1108 17739 19461 13888 -257 -862 1771 C ATOM 5857 CD GLU B1108 -43.081 -1.015 87.670 1.00158.27 C ANISOU 5857 CD GLU B1108 20797 22269 17071 -273 -1114 1812 C ATOM 5858 OE1 GLU B1108 -42.983 -1.871 88.580 1.00153.89 O ANISOU 5858 OE1 GLU B1108 20347 21734 16389 -383 -1299 1955 O ATOM 5859 OE2 GLU B1108 -42.200 -0.835 86.800 1.00154.62 O ANISOU 5859 OE2 GLU B1108 20253 21623 16870 -181 -1132 1703 O ATOM 5860 N THR B1109 -46.836 1.638 91.108 1.00129.25 N ANISOU 5860 N THR B1109 17173 19681 12255 -399 -525 1604 N ATOM 5861 CA THR B1109 -47.688 1.579 92.306 1.00131.88 C ANISOU 5861 CA THR B1109 17542 20352 12216 -533 -446 1619 C ATOM 5862 C THR B1109 -49.056 2.247 92.055 1.00136.63 C ANISOU 5862 C THR B1109 17995 21182 12737 -465 -176 1499 C ATOM 5863 O THR B1109 -50.076 1.768 92.562 1.00138.14 O ANISOU 5863 O THR B1109 18155 21659 12671 -611 -75 1585 O ATOM 5864 CB THR B1109 -46.937 2.132 93.539 1.00142.34 C ANISOU 5864 CB THR B1109 18974 21745 13364 -550 -546 1491 C ATOM 5865 OG1 THR B1109 -45.621 1.575 93.584 1.00141.55 O ANISOU 5865 OG1 THR B1109 18976 21397 13410 -574 -814 1587 O ATOM 5866 CG2 THR B1109 -47.654 1.835 94.855 1.00143.97 C ANISOU 5866 CG2 THR B1109 19248 22316 13137 -743 -501 1544 C ATOM 5867 N GLY B1110 -49.057 3.317 91.256 1.00131.80 N ANISOU 5867 N GLY B1110 17287 20438 12354 -255 -75 1311 N ATOM 5868 CA GLY B1110 -50.259 4.047 90.865 1.00131.80 C ANISOU 5868 CA GLY B1110 17132 20590 12356 -139 142 1180 C ATOM 5869 C GLY B1110