Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE 05-JUN-16 5B78 TITLE CRYSTAL STRUCTURE OF MOZ DOUBLE PHD FINGER MUTANT-S210D/N235R IN TITLE 2 COMPLEX WITH HISTONE H3 CROTONYLATION AT K14 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT6A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 194-323; COMPND 5 SYNONYM: MOZ; COMPND 6 EC: 2.3.1.48; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: HISTONE H3; COMPND 11 CHAIN: B; COMPND 12 FRAGMENT: UNP RESIDUES 2-26; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MOZ; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606 KEYWDS MOZ DOUBLE PHD FINGER, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR H.LI,X.XIONG REVDAT 2 30-NOV-16 5B78 1 JRNL REVDAT 1 26-OCT-16 5B78 0 JRNL AUTH X.XIONG,T.PANCHENKO,S.YANG,S.ZHAO,P.YAN,W.ZHANG,W.XIE,Y.LI, JRNL AUTH 2 Y.ZHAO,C.D.ALLIS,H.LI JRNL TITL SELECTIVE RECOGNITION OF HISTONE CROTONYLATION BY DOUBLE PHD JRNL TITL 2 FINGERS OF MOZ AND DPF2 JRNL REF NAT.CHEM.BIOL. V. 12 1111 2016 JRNL REFN ESSN 1552-4469 JRNL PMID 27775714 JRNL DOI 10.1038/NCHEMBIO.2218 REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.10 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 35447 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.170 REMARK 3 R VALUE (WORKING SET) : 0.169 REMARK 3 FREE R VALUE : 0.187 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 1798 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 24.1226 - 3.2861 1.00 2749 163 0.1522 0.1616 REMARK 3 2 3.2861 - 2.6093 1.00 2643 144 0.1727 0.1996 REMARK 3 3 2.6093 - 2.2798 1.00 2598 142 0.1680 0.1897 REMARK 3 4 2.2798 - 2.0714 1.00 2622 120 0.1617 0.1792 REMARK 3 5 2.0714 - 1.9230 1.00 2556 154 0.1617 0.1829 REMARK 3 6 1.9230 - 1.8097 1.00 2601 138 0.1663 0.2046 REMARK 3 7 1.8097 - 1.7191 1.00 2547 156 0.1677 0.1682 REMARK 3 8 1.7191 - 1.6443 1.00 2576 112 0.1639 0.1945 REMARK 3 9 1.6443 - 1.5810 1.00 2557 146 0.1803 0.1843 REMARK 3 10 1.5810 - 1.5264 1.00 2553 135 0.1846 0.2111 REMARK 3 11 1.5264 - 1.4787 1.00 2585 107 0.2093 0.2335 REMARK 3 12 1.4787 - 1.4365 1.00 2542 139 0.2389 0.2675 REMARK 3 13 1.4365 - 1.3987 0.99 2520 142 0.2529 0.2845 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.080 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 1148 REMARK 3 ANGLE : 0.787 1540 REMARK 3 CHIRALITY : 0.083 162 REMARK 3 PLANARITY : 0.006 204 REMARK 3 DIHEDRAL : 13.900 464 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 193 THROUGH 202 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.7769 -5.6754 -12.9465 REMARK 3 T TENSOR REMARK 3 T11: 0.3977 T22: 0.4784 REMARK 3 T33: 0.4018 T12: 0.0839 REMARK 3 T13: 0.0073 T23: 0.1561 REMARK 3 L TENSOR REMARK 3 L11: 0.8026 L22: 4.3920 REMARK 3 L33: 0.7511 L12: 1.6585 REMARK 3 L13: -0.6817 L23: -1.0013 REMARK 3 S TENSOR REMARK 3 S11: 0.2628 S12: 0.7886 S13: 0.7054 REMARK 3 S21: -1.1734 S22: 0.2438 S23: 0.7977 REMARK 3 S31: -0.4938 S32: -0.4749 S33: -0.1361 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.2935 -13.6527 1.2995 REMARK 3 T TENSOR REMARK 3 T11: 0.0953 T22: 0.1867 REMARK 3 T33: 0.1545 T12: 0.0075 REMARK 3 T13: -0.0003 T23: 0.0365 REMARK 3 L TENSOR REMARK 3 L11: 3.6822 L22: 0.3343 REMARK 3 L33: 0.8716 L12: 0.6204 REMARK 3 L13: 1.5990 L23: 0.3426 REMARK 3 S TENSOR REMARK 3 S11: 0.1004 S12: -0.0951 S13: -0.2659 REMARK 3 S21: 0.0361 S22: 0.0541 S23: -0.0130 REMARK 3 S31: 0.0700 S32: -0.0665 S33: -0.1618 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.0887 -6.8183 8.5992 REMARK 3 T TENSOR REMARK 3 T11: 0.1392 T22: 0.2818 REMARK 3 T33: 0.1375 T12: 0.0150 REMARK 3 T13: -0.0019 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 2.3280 L22: 1.9848 REMARK 3 L33: 2.6018 L12: -0.3521 REMARK 3 L13: -0.4327 L23: 0.3386 REMARK 3 S TENSOR REMARK 3 S11: 0.0043 S12: -0.7425 S13: 0.2486 REMARK 3 S21: 0.2776 S22: 0.0252 S23: -0.1187 REMARK 3 S31: -0.1664 S32: -0.1348 S33: -0.0022 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 245 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.6365 -6.9066 -2.2076 REMARK 3 T TENSOR REMARK 3 T11: 0.0944 T22: 0.1360 REMARK 3 T33: 0.1420 T12: 0.0199 REMARK 3 T13: 0.0022 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 1.4720 L22: 0.5888 REMARK 3 L33: 1.3761 L12: 0.2913 REMARK 3 L13: 0.8859 L23: 0.0982 REMARK 3 S TENSOR REMARK 3 S11: -0.0031 S12: -0.1101 S13: 0.1302 REMARK 3 S21: -0.0008 S22: -0.0341 S23: 0.0156 REMARK 3 S31: -0.0601 S32: -0.1078 S33: 0.0150 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 246 THROUGH 264 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2054 -2.5705 -7.0839 REMARK 3 T TENSOR REMARK 3 T11: 0.1333 T22: 0.1421 REMARK 3 T33: 0.1634 T12: 0.0435 REMARK 3 T13: -0.0030 T23: -0.0017 REMARK 3 L TENSOR REMARK 3 L11: 1.1066 L22: 1.7710 REMARK 3 L33: 2.4401 L12: 0.5291 REMARK 3 L13: 0.1518 L23: 0.8000 REMARK 3 S TENSOR REMARK 3 S11: -0.0525 S12: -0.1322 S13: 0.2037 REMARK 3 S21: -0.1572 S22: 0.0125 S23: 0.0487 REMARK 3 S31: -0.2732 S32: -0.1537 S33: 0.0356 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 265 THROUGH 277 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7692 -6.2287 -21.9953 REMARK 3 T TENSOR REMARK 3 T11: 0.3123 T22: 0.1594 REMARK 3 T33: 0.1993 T12: 0.0202 REMARK 3 T13: 0.0469 T23: 0.0204 REMARK 3 L TENSOR REMARK 3 L11: 1.0947 L22: 5.8475 REMARK 3 L33: 4.0731 L12: -0.0771 REMARK 3 L13: 1.7133 L23: 0.7113 REMARK 3 S TENSOR REMARK 3 S11: -0.0465 S12: 0.2787 S13: 0.0623 REMARK 3 S21: -0.8894 S22: 0.0202 S23: -0.5028 REMARK 3 S31: 0.1993 S32: 0.3079 S33: -0.0066 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 297 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5720 2.4107 -18.9486 REMARK 3 T TENSOR REMARK 3 T11: 0.2225 T22: 0.1130 REMARK 3 T33: 0.1473 T12: 0.0061 REMARK 3 T13: -0.0144 T23: 0.0315 REMARK 3 L TENSOR REMARK 3 L11: 1.4984 L22: 1.4452 REMARK 3 L33: 1.9157 L12: 0.3619 REMARK 3 L13: 0.3929 L23: -1.1923 REMARK 3 S TENSOR REMARK 3 S11: -0.1229 S12: 0.1709 S13: 0.2484 REMARK 3 S21: 0.0797 S22: 0.0468 S23: 0.0377 REMARK 3 S31: -0.4247 S32: -0.0279 S33: 0.0599 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 302 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.6923 6.6877 -22.6089 REMARK 3 T TENSOR REMARK 3 T11: 0.2742 T22: 0.1510 REMARK 3 T33: 0.2001 T12: -0.0260 REMARK 3 T13: -0.0226 T23: 0.0335 REMARK 3 L TENSOR REMARK 3 L11: 5.0730 L22: 5.4251 REMARK 3 L33: 8.8020 L12: -0.0216 REMARK 3 L13: -0.7921 L23: 3.9790 REMARK 3 S TENSOR REMARK 3 S11: 0.2683 S12: 0.2385 S13: -0.0368 REMARK 3 S21: 0.1826 S22: -0.2561 S23: -0.3590 REMARK 3 S31: 0.2568 S32: -0.3021 S33: 0.1271 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 303 THROUGH 311 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.8505 8.8061 -15.0477 REMARK 3 T TENSOR REMARK 3 T11: 0.4878 T22: 0.1360 REMARK 3 T33: 0.2052 T12: 0.0967 REMARK 3 T13: -0.0366 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 3.9400 L22: 2.9803 REMARK 3 L33: 3.8699 L12: 0.9220 REMARK 3 L13: 0.4413 L23: 0.0797 REMARK 3 S TENSOR REMARK 3 S11: 0.0451 S12: 0.0319 S13: 0.3453 REMARK 3 S21: 0.3242 S22: -0.0765 S23: 0.4226 REMARK 3 S31: -1.2224 S32: -0.1550 S33: 0.1471 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 11 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.1181 -3.3703 -11.4819 REMARK 3 T TENSOR REMARK 3 T11: 0.2324 T22: 0.2286 REMARK 3 T33: 0.3242 T12: -0.0325 REMARK 3 T13: 0.0025 T23: 0.0195 REMARK 3 L TENSOR REMARK 3 L11: 4.0134 L22: 5.8648 REMARK 3 L33: 3.4969 L12: -0.8892 REMARK 3 L13: 1.4307 L23: -2.3154 REMARK 3 S TENSOR REMARK 3 S11: -0.5800 S12: -0.1329 S13: -0.0880 REMARK 3 S21: -0.0727 S22: 0.0925 S23: -1.1309 REMARK 3 S31: 0.0940 S32: 0.2327 S33: 0.3360 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.5839 -18.7143 -0.8665 REMARK 3 T TENSOR REMARK 3 T11: 0.2197 T22: 0.2744 REMARK 3 T33: 0.4604 T12: -0.0090 REMARK 3 T13: -0.0624 T23: 0.0379 REMARK 3 L TENSOR REMARK 3 L11: 3.3316 L22: 2.9854 REMARK 3 L33: 3.7862 L12: 0.0997 REMARK 3 L13: 1.1114 L23: -0.2678 REMARK 3 S TENSOR REMARK 3 S11: 0.3641 S12: 0.3075 S13: -1.0651 REMARK 3 S21: -0.4445 S22: 0.1029 S23: 0.4223 REMARK 3 S31: 0.6824 S32: -0.4808 S33: -0.2961 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5B78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-16. REMARK 100 THE DEPOSITION ID IS D_1300000655. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35447 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400 REMARK 200 RESOLUTION RANGE LOW (A) : 24.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL 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: 4LLB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 4000, LITHIUM REMARK 280 SULFATE, TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.83550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.18300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.11900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.18300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.83550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.11900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8370 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 PRO A 312 REMARK 465 ARG A 313 REMARK 465 LYS A 314 REMARK 465 LYS A 315 REMARK 465 GLY A 316 REMARK 465 ARG A 317 REMARK 465 LYS A 318 REMARK 465 LEU A 319 REMARK 465 LEU A 320 REMARK 465 GLN A 321 REMARK 465 LYS A 322 REMARK 465 LYS A 323 REMARK 465 LYS B 23 REMARK 465 ALA B 24 REMARK 465 ALA B 25 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 PRO A 207 36.75 -84.49 REMARK 500 GLN A 271 -70.96 -105.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 684 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH A 685 DISTANCE = 6.05 ANGSTROMS REMARK 525 HOH A 686 DISTANCE = 6.20 ANGSTROMS REMARK 525 HOH A 687 DISTANCE = 6.34 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 403 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 209 SG REMARK 620 2 CYS A 212 SG 112.7 REMARK 620 3 HIS A 238 ND1 100.8 97.2 REMARK 620 4 CYS A 241 SG 111.8 111.9 121.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 404 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 230 SG REMARK 620 2 CYS A 233 SG 105.0 REMARK 620 3 CYS A 259 SG 111.0 116.1 REMARK 620 4 CYS A 262 SG 106.8 114.5 103.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 402 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 265 SG REMARK 620 2 CYS A 268 SG 109.3 REMARK 620 3 HIS A 289 ND1 101.6 98.1 REMARK 620 4 CYS A 292 SG 114.6 116.2 115.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 281 SG REMARK 620 2 CYS A 284 SG 106.6 REMARK 620 3 CYS A 307 SG 105.9 114.0 REMARK 620 4 CYS A 310 SG 111.7 105.7 112.8 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404 DBREF 5B78 A 194 323 UNP Q92794 KAT6A_HUMAN 194 323 DBREF 5B78 B 1 25 UNP K7EMV3 K7EMV3_HUMAN 2 26 SEQADV 5B78 SER A 193 UNP Q92794 EXPRESSION TAG SEQADV 5B78 ASP A 210 UNP Q92794 SER 210 ENGINEERED MUTATION SEQADV 5B78 ARG A 235 UNP Q92794 ASN 235 ENGINEERED MUTATION SEQRES 1 A 131 SER LEU PRO HIS GLU LYS ASP LYS PRO VAL ALA GLU PRO SEQRES 2 A 131 ILE PRO ILE CYS ASP PHE CYS LEU GLY THR LYS GLU GLN SEQRES 3 A 131 ASN ARG GLU LYS LYS PRO GLU GLU LEU ILE SER CYS ALA SEQRES 4 A 131 ASP CYS GLY ARG SER GLY HIS PRO SER CYS LEU LYS PHE SEQRES 5 A 131 SER PRO GLU LEU THR VAL ARG VAL LYS ALA LEU ARG TRP SEQRES 6 A 131 GLN CYS ILE GLU CYS LYS THR CYS SER SER CYS ARG ASP SEQRES 7 A 131 GLN GLY LYS ASN ALA ASP ASN MET LEU PHE CYS ASP SER SEQRES 8 A 131 CYS ASP ARG GLY PHE HIS MET GLU CYS CYS ASP PRO PRO SEQRES 9 A 131 LEU THR ARG MET PRO LYS GLY MET TRP ILE CYS GLN ILE SEQRES 10 A 131 CYS ARG PRO ARG LYS LYS GLY ARG LYS LEU LEU GLN LYS SEQRES 11 A 131 LYS SEQRES 1 B 25 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY SEQRES 2 B 25 KCR ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA MODRES 5B78 KCR B 14 LYS MODIFIED RESIDUE HET KCR B 14 14 HET ZN A 401 1 HET ZN A 402 1 HET ZN A 403 1 HET ZN A 404 1 HETNAM KCR N-6-CROTONYL-L-LYSINE HETNAM ZN ZINC ION FORMUL 2 KCR C10 H18 N2 O3 FORMUL 3 ZN 4(ZN 2+) FORMUL 7 HOH *229(H2 O) HELIX 1 AA1 LEU A 194 LYS A 198 5 5 HELIX 2 AA2 HIS A 238 LYS A 243 1 6 HELIX 3 AA3 SER A 245 LYS A 253 1 9 HELIX 4 AA4 ASN A 274 ASN A 277 5 4 HELIX 5 AA5 HIS A 289 CYS A 293 5 5 HELIX 6 AA6 LYS B 4 GLY B 12 1 9 HELIX 7 AA7 PRO B 16 LEU B 20 5 5 SHEET 1 AA1 2 ILE A 228 SER A 229 0 SHEET 2 AA1 2 SER A 236 GLY A 237 -1 O GLY A 237 N ILE A 228 SHEET 1 AA2 3 GLY A 287 PHE A 288 0 SHEET 2 AA2 3 LEU A 279 PHE A 280 -1 N LEU A 279 O PHE A 288 SHEET 3 AA2 3 ARG B 2 THR B 3 -1 O ARG B 2 N PHE A 280 LINK SG CYS A 209 ZN ZN A 403 1555 1555 2.36 LINK SG CYS A 212 ZN ZN A 403 1555 1555 2.31 LINK SG CYS A 230 ZN ZN A 404 1555 1555 2.34 LINK SG CYS A 233 ZN ZN A 404 1555 1555 2.31 LINK ND1 HIS A 238 ZN ZN A 403 1555 1555 2.09 LINK SG CYS A 241 ZN ZN A 403 1555 1555 2.28 LINK SG CYS A 259 ZN ZN A 404 1555 1555 2.32 LINK SG CYS A 262 ZN ZN A 404 1555 1555 2.35 LINK SG CYS A 265 ZN ZN A 402 1555 1555 2.33 LINK SG CYS A 268 ZN ZN A 402 1555 1555 2.29 LINK SG CYS A 281 ZN ZN A 401 1555 1555 2.34 LINK SG CYS A 284 ZN ZN A 401 1555 1555 2.31 LINK ND1 HIS A 289 ZN ZN A 402 1555 1555 2.11 LINK SG CYS A 292 ZN ZN A 402 1555 1555 2.25 LINK SG CYS A 307 ZN ZN A 401 1555 1555 2.33 LINK SG CYS A 310 ZN ZN A 401 1555 1555 2.23 LINK C GLY B 13 N KCR B 14 1555 1555 1.33 LINK C KCR B 14 N ALA B 15 1555 1555 1.33 CISPEP 1 ASP A 294 PRO A 295 0 3.69 SITE 1 AC1 4 CYS A 281 CYS A 284 CYS A 307 CYS A 310 SITE 1 AC2 4 CYS A 265 CYS A 268 HIS A 289 CYS A 292 SITE 1 AC3 4 CYS A 209 CYS A 212 HIS A 238 CYS A 241 SITE 1 AC4 4 CYS A 230 CYS A 233 CYS A 259 CYS A 262 CRYST1 47.671 48.238 76.366 90.00 90.00 90.00 P 21 21 21 4 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 0.020977 0.000000 0.000000 0.00000 SCALE2 0.000000 0.020731 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013095 0.00000 ATOM 1 N SER A 193 5.554 2.269 -10.638 1.00 61.22 N ANISOU 1 N SER A 193 7607 6920 8736 1339 1801 2221 N ATOM 2 CA SER A 193 5.969 1.035 -11.295 1.00 60.84 C ANISOU 2 CA SER A 193 7637 7122 8359 1226 1547 2095 C ATOM 3 C SER A 193 5.619 1.069 -12.779 1.00 60.73 C ANISOU 3 C SER A 193 7777 7195 8102 1309 1255 2346 C ATOM 4 O SER A 193 4.765 1.847 -13.208 1.00 63.65 O ANISOU 4 O SER A 193 8104 7463 8618 1469 1152 2635 O ATOM 5 CB SER A 193 5.296 -0.172 -10.644 1.00 63.53 C ANISOU 5 CB SER A 193 7727 7609 8804 1180 1341 1936 C ATOM 6 OG SER A 193 4.036 -0.430 -11.242 1.00 69.73 O ANISOU 6 OG SER A 193 8367 8469 9658 1312 994 2151 O ATOM 7 N LEU A 194 6.290 0.212 -13.566 1.00 55.06 N ANISOU 7 N LEU A 194 7252 6651 7016 1187 1126 2242 N ATOM 8 CA LEU A 194 5.993 0.037 -14.978 1.00 57.64 C ANISOU 8 CA LEU A 194 7783 7075 7045 1210 827 2444 C ATOM 9 C LEU A 194 4.895 -1.010 -15.154 1.00 58.25 C ANISOU 9 C LEU A 194 7680 7326 7125 1220 411 2482 C ATOM 10 O LEU A 194 4.737 -1.897 -14.309 1.00 49.77 O ANISOU 10 O LEU A 194 6389 6347 6173 1162 386 2267 O ATOM 11 CB LEU A 194 7.245 -0.419 -15.725 1.00 51.62 C ANISOU 11 CB LEU A 194 7341 6387 5886 1054 933 2296 C ATOM 12 CG LEU A 194 8.400 0.582 -15.772 1.00 46.96 C ANISOU 12 CG LEU A 194 6962 5629 5253 1031 1321 2280 C ATOM 13 CD1 LEU A 194 9.620 -0.027 -16.447 1.00 41.15 C ANISOU 13 CD1 LEU A 194 6501 4958 4176 870 1445 2112 C ATOM 14 CD2 LEU A 194 7.967 1.855 -16.483 1.00 46.37 C ANISOU 14 CD2 LEU A 194 7027 5405 5185 1172 1306 2604 C ATOM 15 N PRO A 195 4.110 -0.917 -16.234 1.00 60.68 N ANISOU 15 N PRO A 195 8080 7671 7304 1281 65 2765 N ATOM 16 CA PRO A 195 3.025 -1.897 -16.437 1.00 62.54 C ANISOU 16 CA PRO A 195 8144 8068 7550 1278 -363 2826 C ATOM 17 C PRO A 195 3.483 -3.348 -16.423 1.00 62.56 C ANISOU 17 C PRO A 195 8200 8280 7290 1104 -444 2532 C ATOM 18 O PRO A 195 2.800 -4.199 -15.841 1.00 61.95 O ANISOU 18 O PRO A 195 7858 8312 7369 1098 -622 2436 O ATOM 19 CB PRO A 195 2.432 -1.485 -17.790 1.00 63.18 C ANISOU 19 CB PRO A 195 8430 8140 7435 1316 -707 3185 C ATOM 20 CG PRO A 195 2.734 -0.030 -17.896 1.00 63.44 C ANISOU 20 CG PRO A 195 8566 7955 7586 1430 -452 3371 C ATOM 21 CD PRO A 195 4.076 0.158 -17.241 1.00 61.12 C ANISOU 21 CD PRO A 195 8375 7603 7243 1357 31 3070 C ATOM 22 N HIS A 196 4.628 -3.654 -17.039 1.00 60.61 N ANISOU 22 N HIS A 196 8283 8077 6669 965 -297 2386 N ATOM 23 CA HIS A 196 5.103 -5.033 -17.074 1.00 58.61 C ANISOU 23 CA HIS A 196 8088 7999 6182 801 -344 2114 C ATOM 24 C HIS A 196 5.627 -5.509 -15.722 1.00 48.02 C ANISOU 24 C HIS A 196 6495 6670 5083 758 -88 1805 C ATOM 25 O HIS A 196 5.742 -6.720 -15.508 1.00 42.06 O ANISOU 25 O HIS A 196 5678 6062 4243 649 -175 1592 O ATOM 26 CB HIS A 196 6.149 -5.214 -18.178 1.00 65.26 C ANISOU 26 CB HIS A 196 9364 8851 6582 664 -230 2063 C ATOM 27 CG HIS A 196 5.596 -5.058 -19.563 1.00 75.35 C ANISOU 27 CG HIS A 196 10945 10146 7537 645 -547 2336 C ATOM 28 ND1 HIS A 196 5.015 -3.889 -20.008 1.00 79.94 N ANISOU 28 ND1 HIS A 196 11575 10604 8196 769 -658 2666 N ATOM 29 CD2 HIS A 196 5.531 -5.927 -20.601 1.00 75.67 C ANISOU 29 CD2 HIS A 196 11279 10302 7171 497 -785 2338 C ATOM 30 CE1 HIS A 196 4.619 -4.044 -21.259 1.00 79.22 C ANISOU 30 CE1 HIS A 196 11791 10553 7754 691 -978 2870 C ATOM 31 NE2 HIS A 196 4.920 -5.272 -21.643 1.00 78.36 N ANISOU 31 NE2 HIS A 196 11853 10588 7332 518 -1056 2670 N ATOM 32 N GLU A 197 5.938 -4.588 -14.806 1.00 38.45 N ANISOU 32 N GLU A 197 5153 5296 4161 826 215 1783 N ATOM 33 CA GLU A 197 6.309 -4.962 -13.446 1.00 33.60 C ANISOU 33 CA GLU A 197 4307 4670 3789 767 419 1521 C ATOM 34 C GLU A 197 5.096 -5.201 -12.556 1.00 33.09 C ANISOU 34 C GLU A 197 3903 4625 4047 848 255 1536 C ATOM 35 O GLU A 197 5.214 -5.900 -11.543 1.00 30.44 O ANISOU 35 O GLU A 197 3388 4333 3845 767 318 1304 O ATOM 36 CB GLU A 197 7.178 -3.867 -12.815 1.00 32.75 C ANISOU 36 CB GLU A 197 4244 4365 3836 770 816 1488 C ATOM 37 CG GLU A 197 8.519 -3.631 -13.511 1.00 35.24 C ANISOU 37 CG GLU A 197 4860 4636 3892 678 1043 1440 C ATOM 38 CD GLU A 197 9.155 -2.302 -13.121 1.00 37.44 C ANISOU 38 CD GLU A 197 5207 4701 4319 712 1384 1498 C ATOM 39 OE1 GLU A 197 8.485 -1.492 -12.445 1.00 33.77 O ANISOU 39 OE1 GLU A 197 4591 4113 4128 818 1438 1603 O ATOM 40 OE2 GLU A 197 10.325 -2.062 -13.495 1.00 34.77 O ANISOU 40 OE2 GLU A 197 5075 4303 3833 629 1614 1440 O ATOM 41 N LYS A 198 3.938 -4.648 -12.916 1.00 44.24 N ANISOU 41 N LYS A 198 5218 5990 5600 999 48 1812 N ATOM 42 CA LYS A 198 2.769 -4.697 -12.048 1.00 48.29 C ANISOU 42 CA LYS A 198 5390 6467 6489 1095 -45 1853 C ATOM 43 C LYS A 198 2.155 -6.092 -12.052 1.00 47.66 C ANISOU 43 C LYS A 198 5165 6598 6344 1029 -369 1744 C ATOM 44 O LYS A 198 1.933 -6.685 -13.112 1.00 50.39 O ANISOU 44 O LYS A 198 5644 7091 6412 993 -681 1835 O ATOM 45 CB LYS A 198 1.739 -3.665 -12.510 1.00 53.63 C ANISOU 45 CB LYS A 198 5987 7009 7380 1282 -169 2213 C ATOM 46 CG LYS A 198 0.846 -3.133 -11.399 1.00 57.97 C ANISOU 46 CG LYS A 198 6214 7387 8424 1405 -30 2262 C ATOM 47 CD LYS A 198 -0.010 -1.970 -11.882 1.00 63.26 C ANISOU 47 CD LYS A 198 6812 7880 9344 1598 -91 2638 C ATOM 48 CE LYS A 198 -1.199 -2.448 -12.700 1.00 66.22 C ANISOU 48 CE LYS A 198 7086 8365 9710 1609 -557 2800 C ATOM 49 NZ LYS A 198 -2.206 -3.145 -11.850 1.00 64.40 N ANISOU 49 NZ LYS A 198 6576 8158 9734 1559 -621 2610 N ATOM 50 N ASP A 199 1.890 -6.615 -10.855 1.00 37.02 N ANISOU 50 N ASP A 199 3570 5254 5240 998 -289 1546 N ATOM 51 CA ASP A 199 1.314 -7.938 -10.621 1.00 40.19 C ANISOU 51 CA ASP A 199 3799 5838 5632 933 -549 1409 C ATOM 52 C ASP A 199 2.182 -9.085 -11.141 1.00 40.21 C ANISOU 52 C ASP A 199 3997 6035 5245 765 -637 1202 C ATOM 53 O ASP A 199 1.720 -10.234 -11.173 1.00 35.18 O ANISOU 53 O ASP A 199 3262 5566 4540 705 -886 1107 O ATOM 54 CB ASP A 199 -0.132 -8.069 -11.134 1.00 43.45 C ANISOU 54 CB ASP A 199 4026 6298 6186 1051 -929 1666 C ATOM 55 CG ASP A 199 -1.074 -7.017 -10.547 1.00 43.92 C ANISOU 55 CG ASP A 199 3917 6112 6657 1172 -785 1781 C ATOM 56 OD1 ASP A 199 -0.824 -6.520 -9.427 1.00 41.58 O ANISOU 56 OD1 ASP A 199 3530 5664 6604 1183 -443 1668 O ATOM 57 OD2 ASP A 199 -2.079 -6.696 -11.216 1.00 48.48 O ANISOU 57 OD2 ASP A 199 4485 6640 7296 1230 -1001 1962 O ATOM 58 N LYS A 200 3.421 -8.810 -11.555 1.00 34.46 N ANISOU 58 N LYS A 200 3537 5276 4279 687 -422 1133 N ATOM 59 CA LYS A 200 4.324 -9.867 -12.007 1.00 34.02 C ANISOU 59 CA LYS A 200 3661 5364 3902 529 -436 931 C ATOM 60 C LYS A 200 4.939 -10.555 -10.795 1.00 28.70 C ANISOU 60 C LYS A 200 2834 4705 3366 413 -256 632 C ATOM 61 O LYS A 200 5.680 -9.912 -10.042 1.00 23.22 O ANISOU 61 O LYS A 200 2136 3868 2817 384 45 555 O ATOM 62 CB LYS A 200 5.427 -9.282 -12.870 1.00 30.25 C ANISOU 62 CB LYS A 200 3510 4815 3169 490 -236 977 C ATOM 63 CG LYS A 200 6.488 -10.297 -13.275 1.00 27.75 C ANISOU 63 CG LYS A 200 3375 4596 2575 326 -160 760 C ATOM 64 CD LYS A 200 7.429 -9.729 -14.328 1.00 44.92 C ANISOU 64 CD LYS A 200 5898 6687 4482 294 23 837 C ATOM 65 CE LYS A 200 8.612 -10.656 -14.569 1.00 52.05 C ANISOU 65 CE LYS A 200 6948 7633 5198 134 197 606 C ATOM 66 NZ LYS A 200 8.193 -12.085 -14.638 1.00 57.58 N ANISOU 66 NZ LYS A 200 7582 8511 5785 50 -40 464 N ATOM 67 N PRO A 201 4.679 -11.846 -10.579 1.00 23.14 N ANISOU 67 N PRO A 201 2017 4161 2614 330 -440 466 N ATOM 68 CA PRO A 201 4.942 -12.439 -9.266 1.00 20.13 C ANISOU 68 CA PRO A 201 1438 3779 2431 236 -325 221 C ATOM 69 C PRO A 201 6.401 -12.371 -8.855 1.00 18.27 C ANISOU 69 C PRO A 201 1307 3463 2172 108 -25 54 C ATOM 70 O PRO A 201 7.321 -12.433 -9.678 1.00 18.80 O ANISOU 70 O PRO A 201 1586 3538 2018 55 66 46 O ATOM 71 CB PRO A 201 4.468 -13.888 -9.429 1.00 21.83 C ANISOU 71 CB PRO A 201 1579 4185 2530 167 -598 97 C ATOM 72 CG PRO A 201 3.367 -13.784 -10.439 1.00 24.57 C ANISOU 72 CG PRO A 201 1989 4560 2788 266 -883 322 C ATOM 73 CD PRO A 201 3.864 -12.735 -11.428 1.00 24.58 C ANISOU 73 CD PRO A 201 2218 4519 2602 328 -803 530 C ATOM 74 N VAL A 202 6.601 -12.239 -7.556 1.00 16.57 N ANISOU 74 N VAL A 202 944 3152 2200 44 131 -74 N ATOM 75 CA VAL A 202 7.932 -12.175 -6.982 1.00 16.26 C ANISOU 75 CA VAL A 202 1020 2963 2196 -94 361 -203 C ATOM 76 C VAL A 202 8.252 -13.454 -6.222 1.00 12.81 C ANISOU 76 C VAL A 202 750 2366 1751 -181 218 -319 C ATOM 77 O VAL A 202 7.372 -14.100 -5.635 1.00 14.85 O ANISOU 77 O VAL A 202 1034 2559 2050 -154 84 -311 O ATOM 78 CB VAL A 202 8.180 -10.910 -6.137 1.00 20.69 C ANISOU 78 CB VAL A 202 1644 3270 2946 -75 577 -110 C ATOM 79 CG1 VAL A 202 7.748 -9.668 -6.913 1.00 22.31 C ANISOU 79 CG1 VAL A 202 1855 3475 3146 71 693 80 C ATOM 80 CG2 VAL A 202 7.475 -10.987 -4.822 1.00 19.14 C ANISOU 80 CG2 VAL A 202 1469 2955 2847 -72 469 -88 C ATOM 81 N ALA A 203 9.539 -13.804 -6.245 1.00 12.91 N ANISOU 81 N ALA A 203 1039 2139 1728 -15 -3 407 N ATOM 82 CA ALA A 203 10.049 -15.021 -5.626 1.00 12.15 C ANISOU 82 CA ALA A 203 933 1993 1691 -10 -33 390 C ATOM 83 C ALA A 203 10.079 -14.903 -4.102 1.00 12.07 C ANISOU 83 C ALA A 203 935 1969 1680 -10 -22 457 C ATOM 84 O ALA A 203 10.108 -13.810 -3.529 1.00 14.68 O ANISOU 84 O ALA A 203 1280 2335 1961 2 16 472 O ATOM 85 CB ALA A 203 11.475 -15.282 -6.123 1.00 15.14 C ANISOU 85 CB ALA A 203 1302 2381 2070 2 -46 305 C ATOM 86 N GLU A 204 10.068 -16.056 -3.439 1.00 13.10 N ANISOU 86 N GLU A 204 1046 2056 1874 -28 -69 495 N ATOM 87 CA GLU A 204 10.183 -16.076 -1.990 1.00 13.93 C ANISOU 87 CA GLU A 204 1147 2185 1962 -47 -67 573 C ATOM 88 C GLU A 204 11.542 -15.522 -1.559 1.00 12.90 C ANISOU 88 C GLU A 204 1041 2060 1802 -23 -45 536 C ATOM 89 O GLU A 204 12.586 -16.005 -2.026 1.00 14.26 O ANISOU 89 O GLU A 204 1218 2179 2022 -9 -77 478 O ATOM 90 CB GLU A 204 10.030 -17.510 -1.479 1.00 16.45 C ANISOU 90 CB GLU A 204 1430 2446 2373 -91 -151 650 C ATOM 91 CG GLU A 204 10.142 -17.622 0.039 1.00 17.29 C ANISOU 91 CG GLU A 204 1514 2612 2444 -136 -160 761 C ATOM 92 CD GLU A 204 10.040 -19.044 0.547 1.00 20.92 C ANISOU 92 CD GLU A 204 1928 3006 3012 -201 -272 878 C ATOM 93 OE1 GLU A 204 9.500 -19.910 -0.178 1.00 21.54 O ANISOU 93 OE1 GLU A 204 1987 2996 3200 -212 -340 879 O ATOM 94 OE2 GLU A 204 10.507 -19.284 1.683 1.00 22.58 O ANISOU 94 OE2 GLU A 204 2117 3255 3208 -247 -303 975 O ATOM 95 N PRO A 205 11.582 -14.532 -0.671 1.00 12.87 N ANISOU 95 N PRO A 205 1042 2123 1725 -15 2 549 N ATOM 96 CA PRO A 205 12.873 -13.959 -0.270 1.00 14.83 C ANISOU 96 CA PRO A 205 1313 2373 1951 8 19 511 C ATOM 97 C PRO A 205 13.629 -14.842 0.711 1.00 12.63 C ANISOU 97 C PRO A 205 1021 2079 1697 -15 -21 562 C ATOM 98 O PRO A 205 13.058 -15.417 1.646 1.00 15.53 O ANISOU 98 O PRO A 205 1353 2491 2056 -59 -46 653 O ATOM 99 CB PRO A 205 12.479 -12.624 0.375 1.00 17.42 C ANISOU 99 CB PRO A 205 1630 2774 2213 30 67 493 C ATOM 100 CG PRO A 205 11.066 -12.831 0.851 1.00 17.80 C ANISOU 100 CG PRO A 205 1634 2893 2238 7 71 538 C ATOM 101 CD PRO A 205 10.434 -13.779 -0.129 1.00 15.49 C ANISOU 101 CD PRO A 205 1346 2539 1999 -16 39 569 C ATOM 102 N ILE A 206 14.935 -14.935 0.497 1.00 13.54 N ANISOU 102 N ILE A 206 1157 2145 1842 6 -35 510 N ATOM 103 CA ILE A 206 15.830 -15.649 1.404 1.00 14.63 C ANISOU 103 CA ILE A 206 1285 2257 2017 -12 -83 552 C ATOM 104 C ILE A 206 16.266 -14.675 2.495 1.00 15.04 C ANISOU 104 C ILE A 206 1342 2395 1978 -5 -33 560 C ATOM 105 O ILE A 206 16.830 -13.617 2.172 1.00 15.40 O ANISOU 105 O ILE A 206 1414 2449 1988 35 14 484 O ATOM 106 CB ILE A 206 17.037 -16.204 0.643 1.00 15.32 C ANISOU 106 CB ILE A 206 1378 2258 2185 16 -125 466 C ATOM 107 CG1 ILE A 206 16.574 -17.111 -0.499 1.00 18.89 C ANISOU 107 CG1 ILE A 206 1804 2646 2728 20 -178 416 C ATOM 108 CG2 ILE A 206 17.950 -16.968 1.589 1.00 17.85 C ANISOU 108 CG2 ILE A 206 1682 2531 2569 0 -193 512 C ATOM 109 CD1 ILE A 206 15.628 -18.219 -0.066 1.00 30.30 C ANISOU 109 CD1 ILE A 206 3215 4038 4261 -25 -258 518 C ATOM 110 N PRO A 207 16.059 -14.994 3.782 1.00 14.03 N ANISOU 110 N PRO A 207 1178 2342 1812 -48 -51 653 N ATOM 111 CA PRO A 207 16.288 -13.998 4.840 1.00 14.57 C ANISOU 111 CA PRO A 207 1229 2530 1778 -38 1 634 C ATOM 112 C PRO A 207 17.733 -13.893 5.314 1.00 15.70 C ANISOU 112 C PRO A 207 1391 2647 1925 -22 -9 611 C ATOM 113 O PRO A 207 17.988 -13.663 6.501 1.00 16.88 O ANISOU 113 O PRO A 207 1507 2904 2002 -42 0 640 O ATOM 114 CB PRO A 207 15.355 -14.483 5.958 1.00 17.72 C ANISOU 114 CB PRO A 207 1556 3069 2108 -108 -15 747 C ATOM 115 CG PRO A 207 15.383 -15.971 5.795 1.00 17.75 C ANISOU 115 CG PRO A 207 1553 2975 2215 -168 -110 866 C ATOM 116 CD PRO A 207 15.397 -16.208 4.304 1.00 16.20 C ANISOU 116 CD PRO A 207 1406 2623 2126 -120 -123 785 C ATOM 117 N ILE A 208 18.684 -14.035 4.391 1.00 13.10 N ANISOU 117 N ILE A 208 1106 2202 1671 11 -24 548 N ATOM 118 CA ILE A 208 20.111 -13.954 4.693 1.00 13.72 C ANISOU 118 CA ILE A 208 1201 2248 1764 30 -35 513 C ATOM 119 C ILE A 208 20.771 -13.119 3.610 1.00 12.85 C ANISOU 119 C ILE A 208 1127 2096 1659 78 4 404 C ATOM 120 O ILE A 208 20.412 -13.223 2.436 1.00 13.75 O ANISOU 120 O ILE A 208 1248 2175 1802 84 5 368 O ATOM 121 CB ILE A 208 20.745 -15.360 4.749 1.00 14.05 C ANISOU 121 CB ILE A 208 1228 2196 1913 5 -129 562 C ATOM 122 CG1 ILE A 208 20.085 -16.181 5.863 1.00 21.61 C ANISOU 122 CG1 ILE A 208 2139 3204 2868 -68 -190 716 C ATOM 123 CG2 ILE A 208 22.260 -15.276 4.942 1.00 17.37 C ANISOU 123 CG2 ILE A 208 1664 2579 2359 33 -142 507 C ATOM 124 CD1 ILE A 208 20.699 -17.539 6.101 1.00 34.85 C ANISOU 124 CD1 ILE A 208 3789 4770 4683 -105 -317 795 C ATOM 125 N CYS A 209 21.717 -12.271 4.006 1.00 13.40 N ANISOU 125 N CYS A 209 1211 2187 1695 101 31 360 N ATOM 126 CA CYS A 209 22.500 -11.509 3.038 1.00 11.01 C ANISOU 126 CA CYS A 209 930 1857 1397 125 54 285 C ATOM 127 C CYS A 209 23.510 -12.422 2.339 1.00 12.38 C ANISOU 127 C CYS A 209 1098 1980 1625 127 19 240 C ATOM 128 O CYS A 209 24.316 -13.089 2.998 1.00 12.75 O ANISOU 128 O CYS A 209 1137 1998 1709 129 -19 245 O ATOM 129 CB CYS A 209 23.224 -10.369 3.752 1.00 12.17 C ANISOU 129 CB CYS A 209 1082 2033 1507 144 79 256 C ATOM 130 SG CYS A 209 24.252 -9.389 2.663 1.00 12.61 S ANISOU 130 SG CYS A 209 1154 2067 1571 149 90 202 S ATOM 131 N ASP A 210 23.469 -12.448 1.004 1.00 12.40 N ANISOU 131 N ASP A 210 1091 1986 1634 125 23 187 N ATOM 132 CA ASP A 210 24.380 -13.319 0.270 1.00 13.76 C ANISOU 132 CA ASP A 210 1230 2142 1854 135 -12 102 C ATOM 133 C ASP A 210 25.814 -12.810 0.271 1.00 13.79 C ANISOU 133 C ASP A 210 1230 2177 1833 144 3 46 C ATOM 134 O ASP A 210 26.701 -13.547 -0.157 1.00 15.09 O ANISOU 134 O ASP A 210 1353 2340 2040 160 -31 -46 O ATOM 135 CB ASP A 210 23.903 -13.568 -1.168 1.00 19.76 C ANISOU 135 CB ASP A 210 1957 2944 2609 126 -11 42 C ATOM 136 CG ASP A 210 22.887 -14.716 -1.269 1.00 17.58 C ANISOU 136 CG ASP A 210 1662 2608 2412 128 -62 53 C ATOM 137 OD1 ASP A 210 22.585 -15.367 -0.239 1.00 19.57 O ANISOU 137 OD1 ASP A 210 1922 2786 2726 125 -107 124 O ATOM 138 OD2 ASP A 210 22.409 -14.980 -2.391 1.00 19.96 O ANISOU 138 OD2 ASP A 210 1929 2944 2710 124 -66 -4 O ATOM 139 N PHE A 211 26.062 -11.594 0.758 1.00 11.57 N ANISOU 139 N PHE A 211 978 1921 1495 139 42 85 N ATOM 140 CA PHE A 211 27.401 -11.012 0.764 1.00 13.08 C ANISOU 140 CA PHE A 211 1165 2143 1663 140 54 45 C ATOM 141 C PHE A 211 28.108 -11.176 2.102 1.00 12.86 C ANISOU 141 C PHE A 211 1154 2072 1659 162 39 57 C ATOM 142 O PHE A 211 29.276 -11.577 2.127 1.00 13.20 O ANISOU 142 O PHE A 211 1178 2111 1726 174 20 -1 O ATOM 143 CB PHE A 211 27.294 -9.541 0.339 1.00 12.12 C ANISOU 143 CB PHE A 211 1053 2063 1489 111 84 84 C ATOM 144 CG PHE A 211 26.656 -9.388 -1.000 1.00 13.78 C ANISOU 144 CG PHE A 211 1237 2331 1666 74 88 94 C ATOM 145 CD1 PHE A 211 27.395 -9.578 -2.154 1.00 18.42 C ANISOU 145 CD1 PHE A 211 1771 3021 2208 41 90 40 C ATOM 146 CD2 PHE A 211 25.299 -9.132 -1.114 1.00 18.03 C ANISOU 146 CD2 PHE A 211 1792 2847 2213 68 88 149 C ATOM 147 CE1 PHE A 211 26.798 -9.488 -3.396 1.00 23.54 C ANISOU 147 CE1 PHE A 211 2381 3757 2806 -4 92 51 C ATOM 148 CE2 PHE A 211 24.695 -9.032 -2.353 1.00 24.35 C ANISOU 148 CE2 PHE A 211 2565 3705 2981 29 87 166 C ATOM 149 CZ PHE A 211 25.444 -9.206 -3.498 1.00 27.30 C ANISOU 149 CZ PHE A 211 2885 4191 3298 -11 89 122 C ATOM 150 N CYS A 212 27.429 -10.897 3.219 1.00 12.34 N ANISOU 150 N CYS A 212 1111 1995 1582 166 44 123 N ATOM 151 CA CYS A 212 28.038 -11.036 4.536 1.00 12.42 C ANISOU 151 CA CYS A 212 1124 2000 1594 176 28 144 C ATOM 152 C CYS A 212 27.477 -12.192 5.348 1.00 14.27 C ANISOU 152 C CYS A 212 1345 2217 1860 159 -20 215 C ATOM 153 O CYS A 212 28.028 -12.496 6.410 1.00 15.06 O ANISOU 153 O CYS A 212 1437 2325 1962 153 -49 253 O ATOM 154 CB CYS A 212 27.929 -9.739 5.350 1.00 12.00 C ANISOU 154 CB CYS A 212 1080 1990 1489 186 62 149 C ATOM 155 SG CYS A 212 26.262 -9.404 5.992 1.00 13.50 S ANISOU 155 SG CYS A 212 1254 2236 1640 182 79 190 S ATOM 156 N LEU A 213 26.407 -12.848 4.890 1.00 13.86 N ANISOU 156 N LEU A 213 1360 2209 1698 44 -93 569 N ATOM 157 CA LEU A 213 25.780 -13.979 5.580 1.00 14.28 C ANISOU 157 CA LEU A 213 1443 2347 1638 42 -93 697 C ATOM 158 C LEU A 213 25.035 -13.574 6.847 1.00 14.49 C ANISOU 158 C LEU A 213 1444 2561 1502 39 -107 656 C ATOM 159 O LEU A 213 24.604 -14.448 7.618 1.00 16.99 O ANISOU 159 O LEU A 213 1782 2972 1703 34 -102 769 O ATOM 160 CB LEU A 213 26.758 -15.136 5.857 1.00 15.39 C ANISOU 160 CB LEU A 213 1587 2477 1783 81 -133 827 C ATOM 161 CG LEU A 213 27.516 -15.636 4.622 1.00 16.18 C ANISOU 161 CG LEU A 213 1712 2398 2039 98 -105 864 C ATOM 162 CD1 LEU A 213 28.535 -16.683 5.009 1.00 20.07 C ANISOU 162 CD1 LEU A 213 2196 2890 2539 163 -149 976 C ATOM 163 CD2 LEU A 213 26.545 -16.183 3.577 1.00 18.27 C ANISOU 163 CD2 LEU A 213 2061 2531 2350 52 -27 886 C ATOM 164 N GLY A 214 24.874 -12.272 7.096 1.00 14.34 N ANISOU 164 N GLY A 214 1389 2591 1469 43 -115 497 N ATOM 165 CA GLY A 214 24.057 -11.826 8.201 1.00 15.52 C ANISOU 165 CA GLY A 214 1519 2914 1463 48 -110 437 C ATOM 166 C GLY A 214 22.581 -11.837 7.860 1.00 15.26 C ANISOU 166 C GLY A 214 1501 2885 1411 29 -28 449 C ATOM 167 O GLY A 214 22.172 -12.025 6.724 1.00 17.01 O ANISOU 167 O GLY A 214 1746 2975 1740 12 11 481 O ATOM 168 N THR A 215 21.769 -11.668 8.888 1.00 17.99 N ANISOU 168 N THR A 215 1824 3405 1607 35 -3 421 N ATOM 169 CA THR A 215 20.329 -11.552 8.746 1.00 17.21 C ANISOU 169 CA THR A 215 1703 3356 1480 25 76 409 C ATOM 170 C THR A 215 19.943 -10.084 8.867 1.00 16.83 C ANISOU 170 C THR A 215 1626 3336 1432 81 86 219 C ATOM 171 O THR A 215 20.798 -9.203 8.986 1.00 18.63 O ANISOU 171 O THR A 215 1864 3518 1697 109 36 100 O ATOM 172 CB THR A 215 19.659 -12.378 9.838 1.00 22.42 C ANISOU 172 CB THR A 215 2352 4197 1970 -6 121 512 C ATOM 173 OG1 THR A 215 19.865 -11.739 11.104 1.00 21.28 O ANISOU 173 OG1 THR A 215 2191 4228 1668 38 98 418 O ATOM 174 CG2 THR A 215 20.235 -13.790 9.871 1.00 28.39 C ANISOU 174 CG2 THR A 215 3160 4897 2729 -47 103 700 C ATOM 175 N LYS A 216 18.633 -9.812 8.895 1.00 16.77 N ANISOU 175 N LYS A 216 1578 3408 1387 99 154 183 N ATOM 176 CA LYS A 216 18.184 -8.447 9.141 1.00 18.43 C ANISOU 176 CA LYS A 216 1765 3650 1587 176 173 3 C ATOM 177 C LYS A 216 18.606 -7.940 10.515 1.00 19.75 C ANISOU 177 C LYS A 216 1931 3966 1606 200 152 -106 C ATOM 178 O LYS A 216 18.555 -6.731 10.766 1.00 21.81 O ANISOU 178 O LYS A 216 2196 4219 1872 262 154 -284 O ATOM 179 CB LYS A 216 16.668 -8.361 9.017 1.00 19.58 C ANISOU 179 CB LYS A 216 1843 3889 1708 205 252 -7 C ATOM 180 CG LYS A 216 15.927 -9.093 10.112 1.00 21.42 C ANISOU 180 CG LYS A 216 2021 4346 1771 167 316 58 C ATOM 181 CD LYS A 216 14.433 -9.079 9.807 1.00 24.22 C ANISOU 181 CD LYS A 216 2290 4762 2151 179 384 53 C ATOM 182 CE LYS A 216 13.595 -9.685 10.911 1.00 31.06 C ANISOU 182 CE LYS A 216 3124 5762 2914 131 427 102 C ATOM 183 NZ LYS A 216 12.158 -9.645 10.511 1.00 36.67 N ANISOU 183 NZ LYS A 216 3748 6503 3683 136 472 86 N ATOM 184 N GLU A 217 19.022 -8.829 11.411 1.00 19.56 N ANISOU 184 N GLU A 217 1912 4073 1445 160 129 -7 N ATOM 185 CA GLU A 217 19.454 -8.419 12.738 1.00 20.64 C ANISOU 185 CA GLU A 217 2053 4378 1411 186 94 -107 C ATOM 186 C GLU A 217 20.915 -7.998 12.801 1.00 19.35 C ANISOU 186 C GLU A 217 1913 4140 1299 181 -18 -187 C ATOM 187 O GLU A 217 21.317 -7.393 13.802 1.00 22.38 O ANISOU 187 O GLU A 217 2295 4649 1559 203 -64 -326 O ATOM 188 CB GLU A 217 19.221 -9.549 13.746 1.00 22.79 C ANISOU 188 CB GLU A 217 2327 4843 1490 157 119 48 C ATOM 189 CG GLU A 217 17.798 -10.105 13.776 1.00 28.77 C ANISOU 189 CG GLU A 217 3049 5618 2264 129 224 137 C ATOM 190 CD GLU A 217 16.730 -9.047 14.037 1.00 41.34 C ANISOU 190 CD GLU A 217 4590 7282 3835 187 290 -28 C ATOM 191 OE1 GLU A 217 17.050 -7.970 14.584 1.00 45.10 O ANISOU 191 OE1 GLU A 217 5076 7810 4251 251 265 -210 O ATOM 192 OE2 GLU A 217 15.556 -9.303 13.694 1.00 45.46 O ANISOU 192 OE2 GLU A 217 5063 7798 4413 171 362 17 O ATOM 193 N GLN A 218 21.725 -8.300 11.783 1.00 19.79 N ANISOU 193 N GLN A 218 1982 4010 1528 149 -61 -115 N ATOM 194 CA GLN A 218 23.160 -8.042 11.889 1.00 21.15 C ANISOU 194 CA GLN A 218 2148 4138 1750 133 -163 -175 C ATOM 195 C GLN A 218 23.764 -7.872 10.502 1.00 20.68 C ANISOU 195 C GLN A 218 2099 3838 1923 107 -163 -158 C ATOM 196 O GLN A 218 23.860 -8.842 9.739 1.00 19.41 O ANISOU 196 O GLN A 218 1950 3590 1833 90 -148 5 O ATOM 197 CB GLN A 218 23.837 -9.179 12.634 1.00 25.87 C ANISOU 197 CB GLN A 218 2738 4870 2222 128 -230 -30 C ATOM 198 CG GLN A 218 25.186 -8.828 13.204 1.00 39.21 C ANISOU 198 CG GLN A 218 4389 6618 3890 128 -354 -127 C ATOM 199 CD GLN A 218 25.707 -9.908 14.119 1.00 48.38 C ANISOU 199 CD GLN A 218 5546 7954 4883 156 -428 21 C ATOM 200 OE1 GLN A 218 24.991 -10.853 14.448 1.00 50.67 O ANISOU 200 OE1 GLN A 218 5879 8306 5066 169 -368 189 O ATOM 201 NE2 GLN A 218 26.961 -9.776 14.538 1.00 50.37 N ANISOU 201 NE2 GLN A 218 5743 8271 5123 165 -555 -39 N ATOM 202 N ASN A 219 24.186 -6.649 10.191 1.00 21.17 N ANISOU 202 N ASN A 219 2163 3786 2096 102 -173 -328 N ATOM 203 CA ASN A 219 24.996 -6.379 9.012 1.00 18.20 C ANISOU 203 CA ASN A 219 1795 3196 1924 68 -172 -322 C ATOM 204 C ASN A 219 26.476 -6.461 9.396 1.00 20.95 C ANISOU 204 C ASN A 219 2085 3575 2299 25 -266 -357 C ATOM 205 O ASN A 219 26.828 -6.957 10.469 1.00 21.51 O ANISOU 205 O ASN A 219 2115 3834 2222 34 -342 -345 O ATOM 206 CB ASN A 219 24.592 -5.040 8.386 1.00 17.31 C ANISOU 206 CB ASN A 219 1727 2920 1929 83 -113 -460 C ATOM 207 CG ASN A 219 24.859 -3.858 9.296 1.00 20.29 C ANISOU 207 CG ASN A 219 2100 3338 2273 76 -144 -682 C ATOM 208 OD1 ASN A 219 25.538 -3.979 10.317 1.00 20.05 O ANISOU 208 OD1 ASN A 219 2020 3457 2139 48 -225 -748 O ATOM 209 ND2 ASN A 219 24.339 -2.699 8.921 1.00 20.52 N ANISOU 209 ND2 ASN A 219 2183 3227 2385 108 -84 -803 N ATOM 210 N ARG A 220 27.362 -5.958 8.530 1.00 17.92 N ANISOU 210 N ARG A 220 1690 3020 2100 -20 -260 -399 N ATOM 211 CA ARG A 220 28.794 -6.039 8.798 1.00 16.80 C ANISOU 211 CA ARG A 220 1461 2914 2008 -66 -345 -436 C ATOM 212 C ARG A 220 29.230 -5.148 9.950 1.00 21.93 C ANISOU 212 C ARG A 220 2062 3688 2583 -99 -428 -644 C ATOM 213 O ARG A 220 30.310 -5.366 10.506 1.00 24.40 O ANISOU 213 O ARG A 220 2280 4114 2876 -126 -531 -677 O ATOM 214 CB ARG A 220 29.596 -5.679 7.546 1.00 19.25 C ANISOU 214 CB ARG A 220 1762 3012 2540 -119 -295 -432 C ATOM 215 CG ARG A 220 29.587 -6.784 6.528 1.00 16.15 C ANISOU 215 CG ARG A 220 1395 2539 2204 -88 -245 -233 C ATOM 216 CD ARG A 220 30.318 -6.402 5.257 1.00 16.83 C ANISOU 216 CD ARG A 220 1482 2426 2488 -133 -174 -229 C ATOM 217 NE ARG A 220 30.464 -7.579 4.408 1.00 15.36 N ANISOU 217 NE ARG A 220 1310 2190 2335 -98 -139 -55 N ATOM 218 CZ ARG A 220 30.442 -7.566 3.080 1.00 13.76 C ANISOU 218 CZ ARG A 220 1168 1816 2242 -102 -45 7 C ATOM 219 NH1 ARG A 220 30.297 -6.422 2.425 1.00 15.39 N ANISOU 219 NH1 ARG A 220 1429 1878 2540 -136 26 -70 N ATOM 220 NH2 ARG A 220 30.575 -8.701 2.405 1.00 14.23 N ANISOU 220 NH2 ARG A 220 1246 1845 2317 -66 -19 146 N ATOM 221 N GLU A 221 28.433 -4.151 10.315 1.00 22.15 N ANISOU 221 N GLU A 221 2147 3702 2568 -91 -390 -795 N ATOM 222 CA GLU A 221 28.710 -3.346 11.495 1.00 27.95 C ANISOU 222 CA GLU A 221 2852 4567 3202 -117 -466 -1012 C ATOM 223 C GLU A 221 28.024 -3.888 12.738 1.00 25.12 C ANISOU 223 C GLU A 221 2500 4467 2576 -49 -507 -994 C ATOM 224 O GLU A 221 27.952 -3.184 13.752 1.00 33.44 O ANISOU 224 O GLU A 221 3554 5644 3506 -50 -552 -1185 O ATOM 225 CB GLU A 221 28.319 -1.890 11.244 1.00 33.86 C ANISOU 225 CB GLU A 221 3669 5138 4060 -142 -396 -1210 C ATOM 226 CG GLU A 221 29.121 -1.247 10.126 1.00 42.68 C ANISOU 226 CG GLU A 221 4785 5999 5432 -226 -351 -1236 C ATOM 227 CD GLU A 221 28.685 0.173 9.830 1.00 57.13 C ANISOU 227 CD GLU A 221 6710 7618 7377 -240 -269 -1404 C ATOM 228 OE1 GLU A 221 27.671 0.619 10.409 1.00 63.05 O ANISOU 228 OE1 GLU A 221 7525 8416 8016 -164 -243 -1495 O ATOM 229 OE2 GLU A 221 29.359 0.844 9.019 1.00 62.79 O ANISOU 229 OE2 GLU A 221 7441 8116 8300 -322 -222 -1441 O ATOM 230 N LYS A 222 27.525 -5.124 12.680 1.00 27.69 N ANISOU 230 N LYS A 222 2839 4874 2809 5 -485 -770 N ATOM 231 CA LYS A 222 26.816 -5.757 13.793 1.00 33.03 C ANISOU 231 CA LYS A 222 3531 5788 3230 63 -497 -709 C ATOM 232 C LYS A 222 25.599 -4.953 14.246 1.00 32.10 C ANISOU 232 C LYS A 222 3466 5713 3016 101 -415 -844 C ATOM 233 O LYS A 222 25.260 -4.937 15.432 1.00 36.21 O ANISOU 233 O LYS A 222 3992 6453 3313 135 -437 -909 O ATOM 234 CB LYS A 222 27.750 -6.081 14.963 1.00 38.64 C ANISOU 234 CB LYS A 222 4181 6728 3771 67 -639 -742 C ATOM 235 CG LYS A 222 28.933 -6.953 14.559 1.00 47.40 C ANISOU 235 CG LYS A 222 5222 7815 4972 58 -721 -598 C ATOM 236 CD LYS A 222 29.785 -7.334 15.760 1.00 55.26 C ANISOU 236 CD LYS A 222 6183 8985 5827 87 -833 -588 C ATOM 237 CE LYS A 222 31.014 -8.129 15.341 1.00 57.54 C ANISOU 237 CE LYS A 222 6400 9229 6234 95 -907 -458 C ATOM 238 NZ LYS A 222 31.940 -7.327 14.491 1.00 59.12 N ANISOU 238 NZ LYS A 222 6502 9298 6661 14 -937 -602 N ATOM 239 N LYS A 223 24.937 -4.278 13.305 1.00 26.12 N ANISOU 239 N LYS A 223 2750 4755 2418 108 -317 -884 N ATOM 240 CA LYS A 223 23.717 -3.535 13.571 1.00 24.16 C ANISOU 240 CA LYS A 223 2544 4526 2109 169 -228 -997 C ATOM 241 C LYS A 223 22.573 -4.098 12.736 1.00 24.44 C ANISOU 241 C LYS A 223 2593 4500 2191 210 -125 -827 C ATOM 242 O LYS A 223 22.800 -4.684 11.670 1.00 22.12 O ANISOU 242 O LYS A 223 2302 4066 2037 182 -117 -674 O ATOM 243 CB LYS A 223 23.881 -2.046 13.232 1.00 28.42 C ANISOU 243 CB LYS A 223 3123 4874 2802 161 -209 -1223 C ATOM 244 CG LYS A 223 24.958 -1.333 14.037 1.00 40.50 C ANISOU 244 CG LYS A 223 4633 6448 4306 99 -309 -1438 C ATOM 245 CD LYS A 223 25.028 0.142 13.666 1.00 48.70 C ANISOU 245 CD LYS A 223 5730 7259 5517 81 -268 -1658 C ATOM 246 CE LYS A 223 26.085 0.878 14.482 1.00 54.86 C ANISOU 246 CE LYS A 223 6484 8079 6281 -6 -370 -1900 C ATOM 247 NZ LYS A 223 27.471 0.447 14.137 1.00 57.18 N ANISOU 247 NZ LYS A 223 6694 8349 6684 -115 -465 -1838 N ATOM 248 N PRO A 224 21.335 -3.944 13.193 1.00 22.58 N ANISOU 248 N PRO A 224 2359 4379 1840 275 -45 -859 N ATOM 249 CA PRO A 224 20.198 -4.387 12.381 1.00 21.21 C ANISOU 249 CA PRO A 224 2176 4160 1723 308 45 -723 C ATOM 250 C PRO A 224 20.086 -3.555 11.115 1.00 23.09 C ANISOU 250 C PRO A 224 2449 4145 2178 336 74 -768 C ATOM 251 O PRO A 224 20.351 -2.349 11.111 1.00 22.86 O ANISOU 251 O PRO A 224 2460 4000 2226 363 72 -946 O ATOM 252 CB PRO A 224 18.991 -4.158 13.299 1.00 25.11 C ANISOU 252 CB PRO A 224 2643 4853 2045 377 125 -798 C ATOM 253 CG PRO A 224 19.554 -4.108 14.673 1.00 27.38 C ANISOU 253 CG PRO A 224 2936 5335 2132 366 72 -895 C ATOM 254 CD PRO A 224 20.908 -3.481 14.524 1.00 26.18 C ANISOU 254 CD PRO A 224 2814 5045 2089 320 -33 -1014 C ATOM 255 N GLU A 225 19.693 -4.218 10.031 1.00 18.11 N ANISOU 255 N GLU A 225 1812 3425 1643 329 102 -603 N ATOM 256 CA GLU A 225 19.456 -3.547 8.758 1.00 18.04 C ANISOU 256 CA GLU A 225 1844 3200 1812 371 132 -611 C ATOM 257 C GLU A 225 18.571 -4.461 7.931 1.00 16.61 C ANISOU 257 C GLU A 225 1630 3034 1646 376 165 -442 C ATOM 258 O GLU A 225 18.929 -5.622 7.703 1.00 17.31 O ANISOU 258 O GLU A 225 1709 3143 1726 301 142 -293 O ATOM 259 CB GLU A 225 20.775 -3.278 8.021 1.00 17.88 C ANISOU 259 CB GLU A 225 1874 2975 1944 310 87 -609 C ATOM 260 CG GLU A 225 20.582 -2.483 6.741 1.00 20.09 C ANISOU 260 CG GLU A 225 2219 3026 2390 358 128 -613 C ATOM 261 CD GLU A 225 21.870 -2.226 6.000 1.00 18.77 C ANISOU 261 CD GLU A 225 2098 2664 2371 286 109 -601 C ATOM 262 OE1 GLU A 225 22.935 -2.739 6.422 1.00 18.84 O ANISOU 262 OE1 GLU A 225 2070 2722 2367 201 55 -589 O ATOM 263 OE2 GLU A 225 21.818 -1.533 4.964 1.00 20.50 O ANISOU 263 OE2 GLU A 225 2388 2686 2718 321 151 -594 O ATOM 264 N GLU A 226 17.427 -3.950 7.491 1.00 17.22 N ANISOU 264 N GLU A 226 1690 3104 1751 465 216 -473 N ATOM 265 CA GLU A 226 16.515 -4.741 6.676 1.00 16.73 C ANISOU 265 CA GLU A 226 1579 3071 1706 465 236 -339 C ATOM 266 C GLU A 226 17.153 -5.111 5.343 1.00 17.74 C ANISOU 266 C GLU A 226 1768 3011 1962 423 202 -231 C ATOM 267 O GLU A 226 17.894 -4.324 4.746 1.00 16.50 O ANISOU 267 O GLU A 226 1688 2670 1911 444 189 -276 O ATOM 268 CB GLU A 226 15.230 -3.951 6.422 1.00 16.23 C ANISOU 268 CB GLU A 226 1471 3039 1656 593 282 -412 C ATOM 269 CG GLU A 226 14.412 -3.706 7.683 1.00 21.21 C ANISOU 269 CG GLU A 226 2022 3884 2151 644 339 -513 C ATOM 270 CD GLU A 226 13.956 -4.998 8.332 1.00 31.83 C ANISOU 270 CD GLU A 226 3281 5443 3369 548 368 -401 C ATOM 271 OE1 GLU A 226 13.460 -5.884 7.608 1.00 25.14 O ANISOU 271 OE1 GLU A 226 2385 4608 2558 494 367 -271 O ATOM 272 OE2 GLU A 226 14.103 -5.131 9.563 1.00 39.20 O ANISOU 272 OE2 GLU A 226 4202 6530 4161 523 393 -442 O ATOM 273 N LEU A 227 16.850 -6.318 4.872 1.00 15.86 N ANISOU 273 N LEU A 227 1498 2815 1711 358 197 -92 N ATOM 274 CA LEU A 227 17.361 -6.787 3.595 1.00 15.01 C ANISOU 274 CA LEU A 227 1449 2549 1705 322 171 5 C ATOM 275 C LEU A 227 16.492 -6.272 2.457 1.00 13.62 C ANISOU 275 C LEU A 227 1278 2309 1588 407 176 1 C ATOM 276 O LEU A 227 15.326 -5.914 2.643 1.00 15.84 O ANISOU 276 O LEU A 227 1487 2701 1830 481 194 -45 O ATOM 277 CB LEU A 227 17.315 -8.308 3.547 1.00 14.47 C ANISOU 277 CB LEU A 227 1356 2542 1600 221 165 139 C ATOM 278 CG LEU A 227 18.119 -9.035 4.620 1.00 13.99 C ANISOU 278 CG LEU A 227 1295 2553 1468 150 153 184 C ATOM 279 CD1 LEU A 227 17.746 -10.524 4.633 1.00 15.77 C ANISOU 279 CD1 LEU A 227 1502 2837 1655 62 167 324 C ATOM 280 CD2 LEU A 227 19.618 -8.853 4.371 1.00 16.43 C ANISOU 280 CD2 LEU A 227 1667 2721 1853 137 115 179 C ATOM 281 N ILE A 228 17.074 -6.238 1.267 1.00 13.20 N ANISOU 281 N ILE A 228 1307 2087 1621 406 159 53 N ATOM 282 CA ILE A 228 16.297 -6.188 0.033 1.00 13.45 C ANISOU 282 CA ILE A 228 1349 2081 1680 467 145 94 C ATOM 283 C ILE A 228 16.516 -7.491 -0.722 1.00 12.33 C ANISOU 283 C ILE A 228 1223 1921 1541 371 124 201 C ATOM 284 O ILE A 228 17.571 -8.126 -0.607 1.00 13.13 O ANISOU 284 O ILE A 228 1367 1959 1664 288 127 247 O ATOM 285 CB ILE A 228 16.551 -4.947 -0.842 1.00 16.60 C ANISOU 285 CB ILE A 228 1848 2304 2154 575 153 65 C ATOM 286 CG1 ILE A 228 17.976 -4.921 -1.366 1.00 16.49 C ANISOU 286 CG1 ILE A 228 1940 2111 2215 513 167 102 C ATOM 287 CG2 ILE A 228 16.224 -3.662 -0.065 1.00 18.94 C ANISOU 287 CG2 ILE A 228 2139 2601 2458 678 179 -55 C ATOM 288 CD1 ILE A 228 18.192 -3.817 -2.412 1.00 19.24 C ANISOU 288 CD1 ILE A 228 2403 2272 2635 604 191 108 C ATOM 289 N SER A 229 15.511 -7.897 -1.492 1.00 13.09 N ANISOU 289 N SER A 229 1279 2077 1618 386 98 232 N ATOM 290 CA SER A 229 15.498 -9.215 -2.110 1.00 12.61 C ANISOU 290 CA SER A 229 1222 2018 1552 282 78 308 C ATOM 291 C SER A 229 15.119 -9.098 -3.575 1.00 11.61 C ANISOU 291 C SER A 229 1143 1834 1436 338 38 325 C ATOM 292 O SER A 229 14.213 -8.345 -3.938 1.00 12.99 O ANISOU 292 O SER A 229 1277 2066 1593 447 11 289 O ATOM 293 CB SER A 229 14.521 -10.151 -1.394 1.00 14.15 C ANISOU 293 CB SER A 229 1295 2388 1693 196 83 322 C ATOM 294 OG SER A 229 14.836 -10.222 -0.015 1.00 14.50 O ANISOU 294 OG SER A 229 1307 2503 1700 159 122 316 O ATOM 295 N CYS A 230 15.820 -9.857 -4.411 1.00 12.09 N ANISOU 295 N CYS A 230 1186 1780 1630 163 4 196 N ATOM 296 CA CYS A 230 15.545 -9.855 -5.837 1.00 10.88 C ANISOU 296 CA CYS A 230 1051 1594 1487 177 -10 214 C ATOM 297 C CYS A 230 14.177 -10.463 -6.111 1.00 10.76 C ANISOU 297 C CYS A 230 1010 1627 1452 156 -24 224 C ATOM 298 O CYS A 230 13.868 -11.561 -5.641 1.00 12.00 O ANISOU 298 O CYS A 230 1163 1815 1582 109 -32 241 O ATOM 299 CB CYS A 230 16.623 -10.680 -6.546 1.00 10.88 C ANISOU 299 CB CYS A 230 1099 1551 1485 163 -14 236 C ATOM 300 SG CYS A 230 16.320 -10.829 -8.324 1.00 11.38 S ANISOU 300 SG CYS A 230 1186 1596 1543 172 -30 254 S ATOM 301 N ALA A 231 13.371 -9.760 -6.908 1.00 10.44 N ANISOU 301 N ALA A 231 951 1589 1425 187 -37 219 N ATOM 302 CA ALA A 231 12.034 -10.240 -7.250 1.00 11.69 C ANISOU 302 CA ALA A 231 1077 1799 1566 170 -54 227 C ATOM 303 C ALA A 231 12.055 -11.522 -8.066 1.00 10.79 C ANISOU 303 C ALA A 231 1001 1666 1432 126 -74 260 C ATOM 304 O ALA A 231 11.064 -12.257 -8.057 1.00 13.53 O ANISOU 304 O ALA A 231 1324 2058 1758 87 -92 274 O ATOM 305 CB ALA A 231 11.285 -9.162 -8.024 1.00 12.97 C ANISOU 305 CB ALA A 231 1217 1957 1755 220 -72 217 C ATOM 306 N ASP A 232 13.136 -11.802 -8.783 1.00 11.49 N ANISOU 306 N ASP A 232 1145 1696 1525 131 -76 269 N ATOM 307 CA ASP A 232 13.161 -12.974 -9.649 1.00 12.33 C ANISOU 307 CA ASP A 232 1290 1781 1614 103 -102 282 C ATOM 308 C ASP A 232 13.827 -14.192 -9.027 1.00 13.83 C ANISOU 308 C ASP A 232 1509 1946 1799 69 -114 286 C ATOM 309 O ASP A 232 13.317 -15.308 -9.184 1.00 16.13 O ANISOU 309 O ASP A 232 1816 2233 2080 28 -150 299 O ATOM 310 CB ASP A 232 13.802 -12.619 -10.990 1.00 14.65 C ANISOU 310 CB ASP A 232 1619 2044 1905 132 -102 281 C ATOM 311 CG ASP A 232 12.936 -11.678 -11.777 1.00 15.18 C ANISOU 311 CG ASP A 232 1665 2129 1975 152 -113 293 C ATOM 312 OD1 ASP A 232 11.858 -12.102 -12.231 1.00 16.93 O ANISOU 312 OD1 ASP A 232 1873 2377 2183 134 -141 300 O ATOM 313 OD2 ASP A 232 13.300 -10.504 -11.915 1.00 21.65 O ANISOU 313 OD2 ASP A 232 2481 2934 2812 182 -104 297 O ATOM 314 N CYS A 233 14.937 -14.025 -8.310 1.00 10.98 N ANISOU 314 N CYS A 233 1159 1564 1450 83 -94 278 N ATOM 315 CA CYS A 233 15.602 -15.176 -7.712 1.00 12.11 C ANISOU 315 CA CYS A 233 1331 1675 1595 56 -117 284 C ATOM 316 C CYS A 233 15.437 -15.275 -6.202 1.00 11.88 C ANISOU 316 C CYS A 233 1276 1679 1558 18 -114 302 C ATOM 317 O CYS A 233 15.788 -16.314 -5.629 1.00 15.46 O ANISOU 317 O CYS A 233 1755 2107 2012 -18 -148 322 O ATOM 318 CB CYS A 233 17.091 -15.221 -8.079 1.00 13.23 C ANISOU 318 CB CYS A 233 1503 1772 1751 95 -108 262 C ATOM 319 SG CYS A 233 18.092 -13.911 -7.321 1.00 12.13 S ANISOU 319 SG CYS A 233 1340 1644 1626 124 -61 254 S ATOM 320 N GLY A 234 14.956 -14.226 -5.537 1.00 11.92 N ANISOU 320 N GLY A 234 1234 1741 1555 26 -81 293 N ATOM 321 CA GLY A 234 14.751 -14.261 -4.103 1.00 13.28 C ANISOU 321 CA GLY A 234 1374 1968 1704 -11 -73 302 C ATOM 322 C GLY A 234 15.990 -14.070 -3.255 1.00 13.61 C ANISOU 322 C GLY A 234 1431 1987 1753 0 -61 295 C ATOM 323 O GLY A 234 15.864 -13.977 -2.025 1.00 13.72 O ANISOU 323 O GLY A 234 1417 2057 1740 -30 -53 299 O ATOM 324 N ARG A 235 17.184 -14.018 -3.844 1.00 11.66 N ANISOU 324 N ARG A 235 1221 1674 1536 38 -62 284 N ATOM 325 CA ARG A 235 18.368 -13.826 -3.021 1.00 11.29 C ANISOU 325 CA ARG A 235 1181 1612 1497 47 -54 278 C ATOM 326 C ARG A 235 18.409 -12.387 -2.516 1.00 10.55 C ANISOU 326 C ARG A 235 1054 1549 1405 75 -17 246 C ATOM 327 O ARG A 235 17.824 -11.479 -3.113 1.00 12.43 O ANISOU 327 O ARG A 235 1276 1795 1654 105 -2 227 O ATOM 328 CB ARG A 235 19.633 -14.202 -3.802 1.00 16.13 C ANISOU 328 CB ARG A 235 1830 2161 2139 80 -65 270 C ATOM 329 CG ARG A 235 19.584 -15.611 -4.427 1.00 16.10 C ANISOU 329 CG ARG A 235 1863 2114 2142 68 -111 282 C ATOM 330 CD ARG A 235 19.251 -16.707 -3.420 1.00 21.39 C ANISOU 330 CD ARG A 235 2546 2780 2801 10 -160 320 C ATOM 331 NE ARG A 235 20.326 -16.892 -2.450 1.00 23.59 N ANISOU 331 NE ARG A 235 2831 3042 3090 9 -174 328 N ATOM 332 CZ ARG A 235 20.420 -17.933 -1.629 1.00 27.40 C ANISOU 332 CZ ARG A 235 3337 3503 3572 -37 -231 368 C ATOM 333 NH1 ARG A 235 19.502 -18.892 -1.660 1.00 30.83 N ANISOU 333 NH1 ARG A 235 3792 3926 3997 -93 -280 406 N ATOM 334 NH2 ARG A 235 21.434 -18.020 -0.777 1.00 22.58 N ANISOU 334 NH2 ARG A 235 2730 2879 2970 -33 -248 376 N ATOM 335 N SER A 236 19.110 -12.176 -1.403 1.00 12.13 N ANISOU 335 N SER A 236 1248 1762 1598 66 -13 240 N ATOM 336 CA SER A 236 18.975 -10.940 -0.652 1.00 12.43 C ANISOU 336 CA SER A 236 1254 1837 1630 84 12 202 C ATOM 337 C SER A 236 20.329 -10.331 -0.318 1.00 11.81 C ANISOU 337 C SER A 236 1190 1722 1576 103 15 188 C ATOM 338 O SER A 236 21.369 -11.003 -0.339 1.00 12.83 O ANISOU 338 O SER A 236 1342 1817 1714 94 1 210 O ATOM 339 CB SER A 236 18.209 -11.174 0.658 1.00 13.10 C ANISOU 339 CB SER A 236 1302 2011 1664 43 15 199 C ATOM 340 OG SER A 236 16.941 -11.767 0.413 1.00 12.78 O ANISOU 340 OG SER A 236 1240 2019 1597 14 11 218 O ATOM 341 N GLY A 237 20.296 -9.049 0.016 1.00 11.64 N ANISOU 341 N GLY A 237 1150 1706 1565 130 28 146 N ATOM 342 CA GLY A 237 21.485 -8.352 0.476 1.00 12.44 C ANISOU 342 CA GLY A 237 1262 1779 1687 138 26 131 C ATOM 343 C GLY A 237 21.108 -7.188 1.361 1.00 12.64 C ANISOU 343 C GLY A 237 1263 1830 1708 157 30 73 C ATOM 344 O GLY A 237 20.041 -6.588 1.207 1.00 13.74 O ANISOU 344 O GLY A 237 1382 1989 1850 186 33 39 O ATOM 345 N HIS A 238 21.979 -6.881 2.319 1.00 12.89 N ANISOU 345 N HIS A 238 1296 1866 1733 145 24 55 N ATOM 346 CA HIS A 238 21.854 -5.611 3.018 1.00 13.37 C ANISOU 346 CA HIS A 238 1345 1932 1803 172 18 -12 C ATOM 347 C HIS A 238 22.169 -4.477 2.047 1.00 14.31 C ANISOU 347 C HIS A 238 1487 1963 1988 204 0 -18 C ATOM 348 O HIS A 238 23.152 -4.563 1.291 1.00 13.60 O ANISOU 348 O HIS A 238 1421 1822 1927 187 -6 29 O ATOM 349 CB HIS A 238 22.858 -5.512 4.166 1.00 12.91 C ANISOU 349 CB HIS A 238 1290 1890 1726 147 8 -27 C ATOM 350 CG HIS A 238 22.672 -6.522 5.252 1.00 13.13 C ANISOU 350 CG HIS A 238 1299 2005 1684 104 15 -13 C ATOM 351 ND1 HIS A 238 23.578 -7.542 5.475 1.00 12.34 N ANISOU 351 ND1 HIS A 238 1216 1901 1573 64 2 46 N ATOM 352 CD2 HIS A 238 21.723 -6.634 6.213 1.00 15.13 C ANISOU 352 CD2 HIS A 238 1518 2360 1873 92 29 -48 C ATOM 353 CE1 HIS A 238 23.176 -8.248 6.522 1.00 13.21 C ANISOU 353 CE1 HIS A 238 1310 2094 1616 22 0 57 C ATOM 354 NE2 HIS A 238 22.049 -7.726 6.977 1.00 15.00 N ANISOU 354 NE2 HIS A 238 1501 2395 1802 33 21 3 N ATOM 355 N PRO A 239 21.376 -3.402 2.044 1.00 14.07 N ANISOU 355 N PRO A 239 1446 1917 1982 249 -16 -75 N ATOM 356 CA PRO A 239 21.759 -2.234 1.233 1.00 14.41 C ANISOU 356 CA PRO A 239 1519 1862 2092 269 -51 -72 C ATOM 357 C PRO A 239 23.203 -1.790 1.454 1.00 15.97 C ANISOU 357 C PRO A 239 1742 2010 2314 235 -70 -55 C ATOM 358 O PRO A 239 23.892 -1.435 0.488 1.00 15.84 O ANISOU 358 O PRO A 239 1750 1933 2335 215 -87 -2 O ATOM 359 CB PRO A 239 20.725 -1.176 1.643 1.00 16.34 C ANISOU 359 CB PRO A 239 1747 2102 2359 330 -77 -157 C ATOM 360 CG PRO A 239 19.519 -1.978 1.999 1.00 17.01 C ANISOU 360 CG PRO A 239 1785 2291 2389 343 -42 -179 C ATOM 361 CD PRO A 239 20.044 -3.236 2.662 1.00 14.32 C ANISOU 361 CD PRO A 239 1437 2021 1984 284 -6 -140 C ATOM 362 N SER A 240 23.704 -1.835 2.692 1.00 15.16 N ANISOU 362 N SER A 240 1631 1945 2184 221 -69 -92 N ATOM 363 CA SER A 240 25.097 -1.457 2.918 1.00 16.17 C ANISOU 363 CA SER A 240 1778 2032 2335 184 -91 -74 C ATOM 364 C SER A 240 26.073 -2.418 2.241 1.00 16.16 C ANISOU 364 C SER A 240 1776 2039 2326 144 -69 6 C ATOM 365 O SER A 240 27.148 -1.992 1.795 1.00 20.78 O ANISOU 365 O SER A 240 2371 2584 2942 114 -85 41 O ATOM 366 CB SER A 240 25.399 -1.360 4.415 1.00 16.54 C ANISOU 366 CB SER A 240 1813 2126 2347 177 -97 -133 C ATOM 367 OG SER A 240 25.141 -2.590 5.065 1.00 16.58 O ANISOU 367 OG SER A 240 1793 2221 2283 160 -63 -120 O ATOM 368 N CYS A 241 25.749 -3.714 2.183 1.00 13.16 N ANISOU 368 N CYS A 241 1383 1715 1905 141 -38 33 N ATOM 369 CA CYS A 241 26.595 -4.653 1.452 1.00 13.30 C ANISOU 369 CA CYS A 241 1398 1735 1920 120 -24 93 C ATOM 370 C CYS A 241 26.495 -4.456 -0.056 1.00 13.47 C ANISOU 370 C CYS A 241 1429 1722 1966 126 -18 130 C ATOM 371 O CYS A 241 27.482 -4.675 -0.771 1.00 15.04 O ANISOU 371 O CYS A 241 1622 1919 2172 107 -12 168 O ATOM 372 CB CYS A 241 26.244 -6.096 1.822 1.00 12.30 C ANISOU 372 CB CYS A 241 1263 1659 1750 116 -10 108 C ATOM 373 SG CYS A 241 26.689 -6.551 3.517 1.00 13.66 S ANISOU 373 SG CYS A 241 1425 1882 1882 89 -24 92 S ATOM 374 N LEU A 242 25.332 -4.035 -0.554 1.00 13.71 N ANISOU 374 N LEU A 242 1467 1736 2004 151 -21 118 N ATOM 375 CA LEU A 242 25.157 -3.727 -1.968 1.00 14.58 C ANISOU 375 CA LEU A 242 1590 1816 2133 152 -23 157 C ATOM 376 C LEU A 242 25.747 -2.379 -2.349 1.00 15.72 C ANISOU 376 C LEU A 242 1751 1901 2321 133 -57 174 C ATOM 377 O LEU A 242 25.809 -2.061 -3.544 1.00 17.82 O ANISOU 377 O LEU A 242 2028 2147 2597 117 -64 221 O ATOM 378 CB LEU A 242 23.665 -3.756 -2.313 1.00 14.91 C ANISOU 378 CB LEU A 242 1632 1862 2171 186 -24 141 C ATOM 379 CG LEU A 242 23.027 -5.141 -2.243 1.00 15.59 C ANISOU 379 CG LEU A 242 1705 2003 2214 190 3 144 C ATOM 380 CD1 LEU A 242 21.518 -5.044 -2.193 1.00 19.35 C ANISOU 380 CD1 LEU A 242 2168 2501 2684 218 0 116 C ATOM 381 CD2 LEU A 242 23.449 -5.952 -3.451 1.00 19.20 C ANISOU 381 CD2 LEU A 242 2170 2464 2660 177 16 189 C ATOM 382 N LYS A 243 26.168 -1.586 -1.368 1.00 16.43 N ANISOU 382 N LYS A 243 1846 1964 2435 126 -84 139 N ATOM 383 CA LYS A 243 26.725 -0.252 -1.594 1.00 17.01 C ANISOU 383 CA LYS A 243 1942 1965 2557 99 -133 154 C ATOM 384 C LYS A 243 25.693 0.716 -2.171 1.00 17.61 C ANISOU 384 C LYS A 243 2044 1973 2673 129 -176 148 C ATOM 385 O LYS A 243 26.039 1.618 -2.938 1.00 18.79 O ANISOU 385 O LYS A 243 2219 2061 2861 95 -220 197 O ATOM 386 CB LYS A 243 28.008 -0.265 -2.442 1.00 16.39 C ANISOU 386 CB LYS A 243 1856 1897 2476 38 -127 228 C ATOM 387 CG LYS A 243 29.010 -1.359 -2.073 1.00 22.26 C ANISOU 387 CG LYS A 243 2564 2713 3183 23 -86 234 C ATOM 388 CD LYS A 243 29.462 -1.235 -0.641 1.00 20.05 C ANISOU 388 CD LYS A 243 2278 2433 2907 21 -101 187 C ATOM 389 CE LYS A 243 30.500 -2.311 -0.263 1.00 23.80 C ANISOU 389 CE LYS A 243 2718 2972 3352 8 -73 198 C ATOM 390 NZ LYS A 243 31.697 -2.291 -1.158 1.00 20.87 N ANISOU 390 NZ LYS A 243 2318 2628 2983 -34 -65 252 N ATOM 391 N PHE A 244 24.427 0.551 -1.793 1.00 16.64 N ANISOU 391 N PHE A 244 1912 1866 2543 188 -170 91 N ATOM 392 CA PHE A 244 23.358 1.456 -2.208 1.00 16.52 C ANISOU 392 CA PHE A 244 1914 1790 2573 233 -218 70 C ATOM 393 C PHE A 244 23.261 2.628 -1.237 1.00 18.68 C ANISOU 393 C PHE A 244 2203 1999 2897 266 -276 -9 C ATOM 394 O PHE A 244 23.350 2.453 -0.017 1.00 21.12 O ANISOU 394 O PHE A 244 2493 2352 3181 281 -259 -79 O ATOM 395 CB PHE A 244 22.007 0.737 -2.203 1.00 16.41 C ANISOU 395 CB PHE A 244 1871 1838 2528 285 -186 35 C ATOM 396 CG PHE A 244 21.790 -0.203 -3.358 1.00 15.37 C ANISOU 396 CG PHE A 244 1734 1744 2362 265 -151 103 C ATOM 397 CD1 PHE A 244 22.771 -0.440 -4.307 1.00 15.40 C ANISOU 397 CD1 PHE A 244 1754 1744 2355 210 -141 180 C ATOM 398 CD2 PHE A 244 20.570 -0.843 -3.492 1.00 16.92 C ANISOU 398 CD2 PHE A 244 1905 1992 2533 300 -130 83 C ATOM 399 CE1 PHE A 244 22.538 -1.308 -5.368 1.00 16.31 C ANISOU 399 CE1 PHE A 244 1863 1900 2433 199 -112 227 C ATOM 400 CE2 PHE A 244 20.325 -1.704 -4.540 1.00 17.45 C ANISOU 400 CE2 PHE A 244 1972 2090 2570 282 -106 137 C ATOM 401 CZ PHE A 244 21.306 -1.944 -5.482 1.00 15.85 C ANISOU 401 CZ PHE A 244 1789 1878 2355 235 -98 204 C ATOM 402 N SER A 245 23.055 3.820 -1.786 1.00 19.10 N ANISOU 402 N SER A 245 2292 1948 3018 277 -352 0 N ATOM 403 CA SER A 245 22.806 4.991 -0.967 1.00 21.89 C ANISOU 403 CA SER A 245 2664 2222 3430 325 -424 -88 C ATOM 404 C SER A 245 21.468 4.851 -0.240 1.00 24.81 C ANISOU 404 C SER A 245 2995 2647 3785 420 -408 -199 C ATOM 405 O SER A 245 20.611 4.056 -0.642 1.00 21.41 O ANISOU 405 O SER A 245 2529 2290 3315 443 -360 -187 O ATOM 406 CB SER A 245 22.758 6.229 -1.857 1.00 23.58 C ANISOU 406 CB SER A 245 2931 2300 3729 318 -524 -43 C ATOM 407 OG SER A 245 21.596 6.221 -2.669 1.00 23.62 O ANISOU 407 OG SER A 245 2930 2297 3747 369 -537 -32 O ATOM 408 N PRO A 246 21.265 5.610 0.845 1.00 24.97 N ANISOU 408 N PRO A 246 3215 2897 3375 222 2 -660 N ATOM 409 CA PRO A 246 19.943 5.593 1.497 1.00 22.36 C ANISOU 409 CA PRO A 246 2863 2610 3023 338 -3 -696 C ATOM 410 C PRO A 246 18.813 5.964 0.553 1.00 20.71 C ANISOU 410 C PRO A 246 2711 2307 2851 446 -13 -666 C ATOM 411 O PRO A 246 17.747 5.338 0.594 1.00 20.13 O ANISOU 411 O PRO A 246 2567 2313 2768 532 -16 -650 O ATOM 412 CB PRO A 246 20.105 6.597 2.650 1.00 25.64 C ANISOU 412 CB PRO A 246 3320 3005 3415 321 -1 -816 C ATOM 413 CG PRO A 246 21.573 6.598 2.928 1.00 25.54 C ANISOU 413 CG PRO A 246 3295 3017 3393 185 -7 -828 C ATOM 414 CD PRO A 246 22.241 6.417 1.601 1.00 24.35 C ANISOU 414 CD PRO A 246 3165 2800 3288 126 2 -746 C ATOM 415 N GLU A 247 19.030 6.944 -0.328 1.00 21.49 N ANISOU 415 N GLU A 247 2938 2240 2986 435 -25 -656 N ATOM 416 CA GLU A 247 17.973 7.376 -1.240 1.00 24.39 C ANISOU 416 CA GLU A 247 3377 2505 3384 550 -58 -624 C ATOM 417 C GLU A 247 17.630 6.294 -2.257 1.00 20.12 C ANISOU 417 C GLU A 247 2782 2022 2842 565 -67 -518 C ATOM 418 O GLU A 247 16.450 6.046 -2.537 1.00 21.95 O ANISOU 418 O GLU A 247 2974 2284 3082 678 -96 -505 O ATOM 419 CB GLU A 247 18.387 8.661 -1.955 1.00 24.88 C ANISOU 419 CB GLU A 247 3625 2359 3471 520 -74 -624 C ATOM 420 CG GLU A 247 18.471 9.891 -1.059 1.00 34.81 C ANISOU 420 CG GLU A 247 4970 3520 4736 530 -74 -738 C ATOM 421 CD GLU A 247 19.732 9.935 -0.209 1.00 43.93 C ANISOU 421 CD GLU A 247 6097 4729 5865 375 -34 -793 C ATOM 422 OE1 GLU A 247 20.632 9.082 -0.399 1.00 35.66 O ANISOU 422 OE1 GLU A 247 4967 3780 4802 265 -11 -741 O ATOM 423 OE2 GLU A 247 19.824 10.835 0.654 1.00 49.69 O ANISOU 423 OE2 GLU A 247 6886 5403 6591 369 -30 -898 O ATOM 424 N LEU A 248 18.646 5.652 -2.840 1.00 19.50 N ANISOU 424 N LEU A 248 2694 1962 2752 451 -42 -452 N ATOM 425 CA LEU A 248 18.381 4.560 -3.768 1.00 17.76 C ANISOU 425 CA LEU A 248 2427 1798 2525 456 -44 -361 C ATOM 426 C LEU A 248 17.667 3.416 -3.059 1.00 17.64 C ANISOU 426 C LEU A 248 2270 1944 2489 506 -41 -364 C ATOM 427 O LEU A 248 16.751 2.798 -3.618 1.00 16.86 O ANISOU 427 O LEU A 248 2135 1884 2387 565 -59 -320 O ATOM 428 CB LEU A 248 19.696 4.075 -4.375 1.00 18.53 C ANISOU 428 CB LEU A 248 2529 1896 2617 325 -5 -314 C ATOM 429 CG LEU A 248 19.549 2.882 -5.318 1.00 20.30 C ANISOU 429 CG LEU A 248 2709 2174 2828 320 3 -231 C ATOM 430 CD1 LEU A 248 18.626 3.256 -6.460 1.00 22.13 C ANISOU 430 CD1 LEU A 248 3040 2313 3056 383 -36 -179 C ATOM 431 CD2 LEU A 248 20.904 2.434 -5.844 1.00 22.47 C ANISOU 431 CD2 LEU A 248 2974 2458 3105 199 53 -208 C ATOM 432 N THR A 249 18.077 3.130 -1.822 1.00 17.00 N ANISOU 432 N THR A 249 2117 1959 2385 473 -20 -415 N ATOM 433 CA THR A 249 17.474 2.047 -1.053 1.00 17.47 C ANISOU 433 CA THR A 249 2067 2165 2407 496 -11 -414 C ATOM 434 C THR A 249 15.980 2.274 -0.858 1.00 19.30 C ANISOU 434 C THR A 249 2265 2429 2640 603 -19 -455 C ATOM 435 O THR A 249 15.178 1.348 -1.016 1.00 17.41 O ANISOU 435 O THR A 249 1954 2278 2384 625 -15 -422 O ATOM 436 CB THR A 249 18.196 1.920 0.288 1.00 16.43 C ANISOU 436 CB THR A 249 1896 2111 2237 442 1 -466 C ATOM 437 OG1 THR A 249 19.565 1.575 0.058 1.00 17.73 O ANISOU 437 OG1 THR A 249 2059 2269 2409 354 0 -432 O ATOM 438 CG2 THR A 249 17.558 0.852 1.153 1.00 19.62 C ANISOU 438 CG2 THR A 249 2218 2656 2583 453 13 -461 C ATOM 439 N VAL A 250 15.587 3.507 -0.519 1.00 17.94 N ANISOU 439 N VAL A 250 2141 2186 2491 669 -30 -537 N ATOM 440 CA VAL A 250 14.169 3.825 -0.365 1.00 20.47 C ANISOU 440 CA VAL A 250 2414 2538 2826 791 -40 -596 C ATOM 441 C VAL A 250 13.410 3.536 -1.655 1.00 17.94 C ANISOU 441 C VAL A 250 2090 2191 2536 852 -83 -527 C ATOM 442 O VAL A 250 12.320 2.949 -1.640 1.00 22.65 O ANISOU 442 O VAL A 250 2583 2896 3128 904 -83 -538 O ATOM 443 CB VAL A 250 13.998 5.291 0.085 1.00 20.97 C ANISOU 443 CB VAL A 250 2552 2495 2921 866 -51 -699 C ATOM 444 CG1 VAL A 250 12.543 5.711 -0.018 1.00 23.86 C ANISOU 444 CG1 VAL A 250 2867 2874 3324 1021 -76 -762 C ATOM 445 CG2 VAL A 250 14.502 5.469 1.508 1.00 23.55 C ANISOU 445 CG2 VAL A 250 2861 2884 3203 809 -7 -785 C ATOM 446 N ARG A 251 13.983 3.924 -2.792 1.00 19.66 N ANISOU 446 N ARG A 251 2421 2273 2775 831 -118 -458 N ATOM 447 CA ARG A 251 13.260 3.792 -4.049 1.00 20.92 C ANISOU 447 CA ARG A 251 2602 2396 2952 893 -173 -395 C ATOM 448 C ARG A 251 13.126 2.331 -4.472 1.00 17.77 C ANISOU 448 C ARG A 251 2117 2115 2522 831 -155 -324 C ATOM 449 O ARG A 251 12.045 1.903 -4.895 1.00 19.64 O ANISOU 449 O ARG A 251 2284 2416 2761 892 -188 -316 O ATOM 450 CB ARG A 251 13.938 4.628 -5.131 1.00 23.85 C ANISOU 450 CB ARG A 251 3144 2583 3334 870 -209 -338 C ATOM 451 CG ARG A 251 13.212 4.625 -6.461 1.00 33.97 C ANISOU 451 CG ARG A 251 4479 3809 4617 935 -282 -269 C ATOM 452 CD ARG A 251 11.766 5.099 -6.323 1.00 44.50 C ANISOU 452 CD ARG A 251 5754 5166 5988 1108 -352 -331 C ATOM 453 NE ARG A 251 11.115 5.231 -7.625 1.00 46.44 N ANISOU 453 NE ARG A 251 6067 5346 6233 1181 -447 -265 N ATOM 454 CZ ARG A 251 9.812 5.059 -7.831 1.00 52.72 C ANISOU 454 CZ ARG A 251 6756 6230 7046 1287 -508 -287 C ATOM 455 NH1 ARG A 251 9.013 4.739 -6.821 1.00 56.08 N ANISOU 455 NH1 ARG A 251 7004 6813 7489 1316 -465 -374 N ATOM 456 NH2 ARG A 251 9.308 5.196 -9.052 1.00 50.40 N ANISOU 456 NH2 ARG A 251 6530 5884 6734 1318 -594 -217 N ATOM 457 N VAL A 252 14.195 1.536 -4.350 1.00 17.49 N ANISOU 457 N VAL A 252 2079 2109 2459 714 -109 -279 N ATOM 458 CA VAL A 252 14.098 0.149 -4.810 1.00 16.31 C ANISOU 458 CA VAL A 252 1872 2046 2282 660 -94 -212 C ATOM 459 C VAL A 252 13.150 -0.681 -3.953 1.00 17.65 C ANISOU 459 C VAL A 252 1917 2366 2426 674 -72 -247 C ATOM 460 O VAL A 252 12.576 -1.662 -4.445 1.00 16.41 O ANISOU 460 O VAL A 252 1712 2273 2250 654 -75 -206 O ATOM 461 CB VAL A 252 15.467 -0.537 -4.996 1.00 15.97 C ANISOU 461 CB VAL A 252 1857 1989 2224 551 -56 -160 C ATOM 462 CG1 VAL A 252 16.361 0.278 -5.901 1.00 18.79 C ANISOU 462 CG1 VAL A 252 2331 2212 2599 514 -60 -135 C ATOM 463 CG2 VAL A 252 16.138 -0.791 -3.651 1.00 15.84 C ANISOU 463 CG2 VAL A 252 1788 2040 2189 509 -22 -201 C ATOM 464 N LYS A 253 12.961 -0.312 -2.682 1.00 18.48 N ANISOU 464 N LYS A 253 1974 2529 2520 694 -45 -326 N ATOM 465 CA LYS A 253 12.001 -1.024 -1.839 1.00 20.82 C ANISOU 465 CA LYS A 253 2159 2973 2779 691 -11 -368 C ATOM 466 C LYS A 253 10.560 -0.845 -2.300 1.00 20.33 C ANISOU 466 C LYS A 253 2019 2963 2744 779 -38 -407 C ATOM 467 O LYS A 253 9.684 -1.608 -1.880 1.00 22.56 O ANISOU 467 O LYS A 253 2197 3379 2995 754 -5 -433 O ATOM 468 CB LYS A 253 12.148 -0.588 -0.377 1.00 19.09 C ANISOU 468 CB LYS A 253 1919 2806 2529 685 30 -453 C ATOM 469 CG LYS A 253 13.410 -1.128 0.270 1.00 20.28 C ANISOU 469 CG LYS A 253 2112 2960 2635 588 50 -414 C ATOM 470 CD LYS A 253 13.548 -0.629 1.691 1.00 20.42 C ANISOU 470 CD LYS A 253 2121 3027 2609 579 79 -501 C ATOM 471 CE LYS A 253 14.717 -1.295 2.399 1.00 19.18 C ANISOU 471 CE LYS A 253 1996 2895 2396 489 79 -460 C ATOM 472 NZ LYS A 253 14.889 -0.691 3.762 1.00 21.20 N ANISOU 472 NZ LYS A 253 2259 3195 2599 475 98 -549 N ATOM 473 N ALA A 254 10.292 0.129 -3.159 1.00 18.66 N ANISOU 473 N ALA A 254 1855 2648 2585 876 -103 -413 N ATOM 474 CA ALA A 254 8.952 0.362 -3.672 1.00 18.22 C ANISOU 474 CA ALA A 254 1720 2638 2563 982 -154 -452 C ATOM 475 C ALA A 254 8.778 -0.154 -5.093 1.00 18.54 C ANISOU 475 C ALA A 254 1793 2647 2605 970 -215 -362 C ATOM 476 O ALA A 254 7.717 0.047 -5.694 1.00 22.21 O ANISOU 476 O ALA A 254 2199 3143 3096 1061 -281 -384 O ATOM 477 CB ALA A 254 8.620 1.857 -3.601 1.00 24.39 C ANISOU 477 CB ALA A 254 2545 3322 3401 1121 -202 -526 C ATOM 478 N LEU A 255 9.790 -0.823 -5.638 1.00 18.13 N ANISOU 478 N LEU A 255 1827 2539 2521 863 -197 -268 N ATOM 479 CA LEU A 255 9.795 -1.273 -7.021 1.00 19.29 C ANISOU 479 CA LEU A 255 2033 2641 2656 838 -245 -185 C ATOM 480 C LEU A 255 10.074 -2.769 -7.068 1.00 16.46 C ANISOU 480 C LEU A 255 1642 2359 2252 713 -192 -133 C ATOM 481 O LEU A 255 10.570 -3.357 -6.104 1.00 16.75 O ANISOU 481 O LEU A 255 1652 2447 2267 646 -125 -142 O ATOM 482 CB LEU A 255 10.891 -0.547 -7.817 1.00 19.79 C ANISOU 482 CB LEU A 255 2261 2536 2723 823 -266 -125 C ATOM 483 CG LEU A 255 10.711 0.960 -7.976 1.00 22.61 C ANISOU 483 CG LEU A 255 2703 2770 3118 935 -330 -157 C ATOM 484 CD1 LEU A 255 11.917 1.545 -8.705 1.00 22.97 C ANISOU 484 CD1 LEU A 255 2925 2654 3150 873 -327 -94 C ATOM 485 CD2 LEU A 255 9.403 1.269 -8.699 1.00 25.63 C ANISOU 485 CD2 LEU A 255 3054 3167 3518 1058 -432 -167 C ATOM 486 N ARG A 256 9.769 -3.382 -8.213 1.00 16.18 N ANISOU 486 N ARG A 256 1628 2323 2198 685 -229 -79 N ATOM 487 CA ARG A 256 10.075 -4.794 -8.449 1.00 13.92 C ANISOU 487 CA ARG A 256 1342 2079 1869 570 -183 -28 C ATOM 488 C ARG A 256 11.561 -4.897 -8.786 1.00 14.08 C ANISOU 488 C ARG A 256 1477 1990 1882 511 -147 27 C ATOM 489 O ARG A 256 11.970 -5.081 -9.938 1.00 15.33 O ANISOU 489 O ARG A 256 1720 2081 2025 478 -161 79 O ATOM 490 CB ARG A 256 9.194 -5.367 -9.556 1.00 15.69 C ANISOU 490 CB ARG A 256 1548 2342 2071 557 -237 -4 C ATOM 491 CG ARG A 256 9.195 -6.898 -9.610 1.00 13.37 C ANISOU 491 CG ARG A 256 1237 2109 1733 437 -187 25 C ATOM 492 CD ARG A 256 8.419 -7.472 -10.796 1.00 14.39 C ANISOU 492 CD ARG A 256 1365 2269 1834 406 -241 46 C ATOM 493 NE ARG A 256 8.472 -8.934 -10.725 1.00 14.81 N ANISOU 493 NE ARG A 256 1418 2364 1846 284 -184 67 N ATOM 494 CZ ARG A 256 9.507 -9.678 -11.117 1.00 14.53 C ANISOU 494 CZ ARG A 256 1487 2245 1788 217 -140 118 C ATOM 495 NH1 ARG A 256 10.593 -9.126 -11.664 1.00 15.78 N ANISOU 495 NH1 ARG A 256 1745 2291 1958 245 -138 151 N ATOM 496 NH2 ARG A 256 9.459 -10.991 -10.964 1.00 13.97 N ANISOU 496 NH2 ARG A 256 1424 2201 1683 120 -95 131 N ATOM 497 N TRP A 257 12.379 -4.775 -7.745 1.00 12.16 N ANISOU 497 N TRP A 257 1229 1743 1649 495 -98 7 N ATOM 498 CA TRP A 257 13.824 -4.660 -7.914 1.00 11.36 C ANISOU 498 CA TRP A 257 1207 1554 1555 451 -67 36 C ATOM 499 C TRP A 257 14.437 -6.010 -8.263 1.00 11.65 C ANISOU 499 C TRP A 257 1258 1601 1569 374 -29 81 C ATOM 500 O TRP A 257 14.056 -7.045 -7.712 1.00 12.27 O ANISOU 500 O TRP A 257 1287 1751 1623 343 -11 85 O ATOM 501 CB TRP A 257 14.446 -4.146 -6.618 1.00 12.23 C ANISOU 501 CB TRP A 257 1293 1674 1680 459 -40 -10 C ATOM 502 CG TRP A 257 15.932 -4.050 -6.666 1.00 11.84 C ANISOU 502 CG TRP A 257 1293 1560 1643 410 -11 3 C ATOM 503 CD1 TRP A 257 16.665 -3.067 -7.263 1.00 13.39 C ANISOU 503 CD1 TRP A 257 1566 1659 1862 400 -11 2 C ATOM 504 CD2 TRP A 257 16.869 -4.976 -6.110 1.00 12.49 C ANISOU 504 CD2 TRP A 257 1350 1677 1719 361 21 15 C ATOM 505 NE1 TRP A 257 18.004 -3.330 -7.118 1.00 12.29 N ANISOU 505 NE1 TRP A 257 1428 1508 1734 339 28 2 N ATOM 506 CE2 TRP A 257 18.161 -4.492 -6.405 1.00 10.74 C ANISOU 506 CE2 TRP A 257 1164 1392 1524 328 40 9 C ATOM 507 CE3 TRP A 257 16.742 -6.176 -5.396 1.00 13.50 C ANISOU 507 CE3 TRP A 257 1435 1878 1816 341 32 30 C ATOM 508 CZ2 TRP A 257 19.320 -5.162 -6.010 1.00 13.26 C ANISOU 508 CZ2 TRP A 257 1452 1732 1853 295 61 7 C ATOM 509 CZ3 TRP A 257 17.892 -6.839 -4.999 1.00 14.27 C ANISOU 509 CZ3 TRP A 257 1530 1976 1918 315 44 41 C ATOM 510 CH2 TRP A 257 19.170 -6.331 -5.305 1.00 13.19 C ANISOU 510 CH2 TRP A 257 1404 1788 1819 301 54 26 C ATOM 511 N GLN A 258 15.421 -5.994 -9.162 1.00 11.95 N ANISOU 511 N GLN A 258 1370 1559 1612 338 -10 111 N ATOM 512 CA GLN A 258 16.138 -7.190 -9.579 1.00 11.10 C ANISOU 512 CA GLN A 258 1280 1446 1492 280 30 140 C ATOM 513 C GLN A 258 17.610 -7.075 -9.200 1.00 11.70 C ANISOU 513 C GLN A 258 1357 1490 1598 261 70 125 C ATOM 514 O GLN A 258 18.192 -5.987 -9.254 1.00 12.72 O ANISOU 514 O GLN A 258 1511 1573 1749 260 74 104 O ATOM 515 CB GLN A 258 16.075 -7.345 -11.093 1.00 10.92 C ANISOU 515 CB GLN A 258 1334 1371 1445 248 28 172 C ATOM 516 CG GLN A 258 14.670 -7.594 -11.609 1.00 13.10 C ANISOU 516 CG GLN A 258 1602 1688 1688 260 -23 185 C ATOM 517 CD GLN A 258 14.614 -7.543 -13.117 1.00 14.86 C ANISOU 517 CD GLN A 258 1918 1855 1873 229 -40 217 C ATOM 518 OE1 GLN A 258 15.046 -6.559 -13.733 1.00 16.00 O ANISOU 518 OE1 GLN A 258 2142 1926 2013 234 -49 228 O ATOM 519 NE2 GLN A 258 14.106 -8.607 -13.727 1.00 13.33 N ANISOU 519 NE2 GLN A 258 1732 1692 1642 186 -43 231 N ATOM 520 N CYS A 259 18.217 -8.205 -8.835 1.00 11.30 N ANISOU 520 N CYS A 259 1281 1462 1549 244 94 131 N ATOM 521 CA CYS A 259 19.654 -8.225 -8.573 1.00 9.90 C ANISOU 521 CA CYS A 259 1084 1268 1408 235 122 109 C ATOM 522 C CYS A 259 20.445 -7.989 -9.864 1.00 10.74 C ANISOU 522 C CYS A 259 1237 1318 1528 193 168 104 C ATOM 523 O CYS A 259 19.900 -7.971 -10.972 1.00 12.19 O ANISOU 523 O CYS A 259 1484 1466 1680 169 175 128 O ATOM 524 CB CYS A 259 20.075 -9.550 -7.929 1.00 12.10 C ANISOU 524 CB CYS A 259 1334 1575 1687 248 120 119 C ATOM 525 SG CYS A 259 20.097 -10.983 -9.013 1.00 10.98 S ANISOU 525 SG CYS A 259 1242 1395 1534 229 150 146 S ATOM 526 N ILE A 260 21.764 -7.835 -9.695 1.00 12.39 N ANISOU 526 N ILE A 260 1406 1525 1775 177 201 66 N ATOM 527 CA ILE A 260 22.673 -7.571 -10.818 1.00 12.72 C ANISOU 527 CA ILE A 260 1477 1528 1828 118 266 44 C ATOM 528 C ILE A 260 22.478 -8.588 -11.936 1.00 12.42 C ANISOU 528 C ILE A 260 1487 1469 1763 102 300 64 C ATOM 529 O ILE A 260 22.413 -8.226 -13.121 1.00 14.67 O ANISOU 529 O ILE A 260 1850 1711 2012 46 337 73 O ATOM 530 CB ILE A 260 24.135 -7.550 -10.330 1.00 13.33 C ANISOU 530 CB ILE A 260 1465 1639 1961 108 297 -16 C ATOM 531 CG1 ILE A 260 24.361 -6.356 -9.403 1.00 15.15 C ANISOU 531 CG1 ILE A 260 1667 1882 2207 97 269 -44 C ATOM 532 CG2 ILE A 260 25.117 -7.551 -11.509 1.00 16.89 C ANISOU 532 CG2 ILE A 260 1923 2071 2422 39 386 -53 C ATOM 533 CD1 ILE A 260 25.663 -6.459 -8.581 1.00 21.32 C ANISOU 533 CD1 ILE A 260 2334 2724 3042 101 269 -105 C ATOM 534 N GLU A 261 22.425 -9.881 -11.584 1.00 12.28 N ANISOU 534 N GLU A 261 1440 1473 1754 144 289 71 N ATOM 535 CA GLU A 261 22.385 -10.910 -12.615 1.00 12.37 C ANISOU 535 CA GLU A 261 1500 1455 1744 126 328 75 C ATOM 536 C GLU A 261 21.006 -11.061 -13.224 1.00 14.31 C ANISOU 536 C GLU A 261 1825 1686 1927 104 297 123 C ATOM 537 O GLU A 261 20.891 -11.341 -14.419 1.00 16.95 O ANISOU 537 O GLU A 261 2228 1989 2221 58 331 124 O ATOM 538 CB GLU A 261 22.863 -12.251 -12.066 1.00 15.69 C ANISOU 538 CB GLU A 261 1882 1881 2198 182 323 62 C ATOM 539 CG GLU A 261 24.279 -12.223 -11.496 1.00 17.77 C ANISOU 539 CG GLU A 261 2049 2172 2531 222 338 6 C ATOM 540 CD GLU A 261 25.325 -11.585 -12.409 1.00 22.54 C ANISOU 540 CD GLU A 261 2624 2781 3161 168 422 -56 C ATOM 541 OE1 GLU A 261 25.270 -11.749 -13.654 1.00 23.79 O ANISOU 541 OE1 GLU A 261 2846 2906 3285 114 488 -65 O ATOM 542 OE2 GLU A 261 26.223 -10.908 -11.865 1.00 19.95 O ANISOU 542 OE2 GLU A 261 2209 2494 2879 166 426 -101 O ATOM 543 N CYS A 262 19.955 -10.871 -12.435 1.00 12.48 N ANISOU 543 N CYS A 262 1577 1485 1680 130 233 153 N ATOM 544 CA CYS A 262 18.611 -11.001 -12.978 1.00 11.68 C ANISOU 544 CA CYS A 262 1522 1389 1525 111 196 185 C ATOM 545 C CYS A 262 18.171 -9.773 -13.761 1.00 12.13 C ANISOU 545 C CYS A 262 1630 1425 1555 96 173 197 C ATOM 546 O CYS A 262 17.202 -9.874 -14.524 1.00 14.62 O ANISOU 546 O CYS A 262 1991 1741 1822 80 137 220 O ATOM 547 CB CYS A 262 17.613 -11.267 -11.849 1.00 12.47 C ANISOU 547 CB CYS A 262 1571 1547 1620 138 147 199 C ATOM 548 SG CYS A 262 17.788 -12.909 -11.102 1.00 11.96 S ANISOU 548 SG CYS A 262 1503 1486 1554 136 158 209 S ATOM 549 N LYS A 263 18.850 -8.640 -13.586 1.00 12.46 N ANISOU 549 N LYS A 263 1672 1441 1622 100 185 182 N ATOM 550 CA LYS A 263 18.385 -7.377 -14.151 1.00 12.98 C ANISOU 550 CA LYS A 263 1806 1464 1660 98 149 200 C ATOM 551 C LYS A 263 18.150 -7.515 -15.651 1.00 13.64 C ANISOU 551 C LYS A 263 1998 1507 1678 45 154 228 C ATOM 552 O LYS A 263 19.045 -7.923 -16.400 1.00 14.49 O ANISOU 552 O LYS A 263 2147 1591 1769 -17 228 214 O ATOM 553 CB LYS A 263 19.434 -6.292 -13.895 1.00 13.96 C ANISOU 553 CB LYS A 263 1941 1548 1815 77 184 175 C ATOM 554 CG LYS A 263 18.946 -4.864 -14.153 1.00 18.06 C ANISOU 554 CG LYS A 263 2545 2003 2315 90 135 194 C ATOM 555 CD LYS A 263 18.336 -4.268 -12.908 1.00 17.93 C ANISOU 555 CD LYS A 263 2462 2013 2337 169 79 174 C ATOM 556 CE LYS A 263 19.390 -3.940 -11.861 1.00 13.62 C ANISOU 556 CE LYS A 263 1853 1480 1841 154 120 127 C ATOM 557 NZ LYS A 263 18.696 -3.629 -10.583 1.00 14.22 N ANISOU 557 NZ LYS A 263 1860 1601 1941 229 72 101 N ATOM 558 N THR A 264 16.943 -7.153 -16.083 1.00 13.23 N ANISOU 558 N THR A 264 1987 1455 1585 73 72 260 N ATOM 559 CA THR A 264 16.588 -7.093 -17.494 1.00 15.52 C ANISOU 559 CA THR A 264 2395 1705 1795 28 49 293 C ATOM 560 C THR A 264 16.382 -5.639 -17.901 1.00 16.31 C ANISOU 560 C THR A 264 2596 1732 1869 48 -10 324 C ATOM 561 O THR A 264 15.995 -4.801 -17.085 1.00 16.80 O ANISOU 561 O THR A 264 2619 1788 1976 123 -61 318 O ATOM 562 CB THR A 264 15.304 -7.885 -17.769 1.00 16.52 C ANISOU 562 CB THR A 264 2496 1893 1889 45 -22 306 C ATOM 563 OG1 THR A 264 14.278 -7.488 -16.845 1.00 23.52 O ANISOU 563 OG1 THR A 264 3288 2834 2816 129 -99 299 O ATOM 564 CG2 THR A 264 15.552 -9.376 -17.590 1.00 16.96 C ANISOU 564 CG2 THR A 264 2500 1989 1954 4 40 282 C ATOM 565 N CYS A 265 16.648 -5.340 -19.172 1.00 14.57 N ANISOU 565 N CYS A 265 2442 1339 1756 109 -129 172 N ATOM 566 CA CYS A 265 16.444 -3.988 -19.672 1.00 14.41 C ANISOU 566 CA CYS A 265 2441 1306 1729 97 -186 206 C ATOM 567 C CYS A 265 14.975 -3.591 -19.560 1.00 14.01 C ANISOU 567 C CYS A 265 2370 1292 1659 88 -380 167 C ATOM 568 O CYS A 265 14.079 -4.330 -19.984 1.00 16.17 O ANISOU 568 O CYS A 265 2712 1566 1865 56 -454 132 O ATOM 569 CB CYS A 265 16.909 -3.926 -21.124 1.00 16.82 C ANISOU 569 CB CYS A 265 2961 1530 1901 76 -79 246 C ATOM 570 SG CYS A 265 16.658 -2.340 -21.948 1.00 16.19 S ANISOU 570 SG CYS A 265 3024 1376 1749 36 -170 305 S ATOM 571 N SER A 266 14.730 -2.418 -18.974 1.00 14.47 N ANISOU 571 N SER A 266 2325 1376 1797 125 -476 162 N ATOM 572 CA SER A 266 13.364 -1.951 -18.772 1.00 16.32 C ANISOU 572 CA SER A 266 2488 1662 2052 156 -653 98 C ATOM 573 C SER A 266 12.682 -1.557 -20.076 1.00 21.24 C ANISOU 573 C SER A 266 3281 2204 2585 156 -805 95 C ATOM 574 O SER A 266 11.451 -1.433 -20.100 1.00 25.00 O ANISOU 574 O SER A 266 3680 2720 3098 186 -977 24 O ATOM 575 CB SER A 266 13.353 -0.801 -17.760 1.00 18.82 C ANISOU 575 CB SER A 266 2678 2009 2463 234 -718 74 C ATOM 576 OG SER A 266 13.403 -1.304 -16.434 1.00 19.29 O ANISOU 576 OG SER A 266 2595 2153 2580 243 -640 42 O ATOM 577 N SER A 267 13.440 -1.370 -21.160 1.00 16.41 N ANISOU 577 N SER A 267 2902 1476 1855 122 -745 165 N ATOM 578 CA SER A 267 12.848 -1.072 -22.462 1.00 18.57 C ANISOU 578 CA SER A 267 3429 1633 1993 116 -903 170 C ATOM 579 C SER A 267 12.519 -2.345 -23.235 1.00 22.93 C ANISOU 579 C SER A 267 4127 2153 2433 71 -896 152 C ATOM 580 O SER A 267 11.358 -2.591 -23.575 1.00 26.70 O ANISOU 580 O SER A 267 4618 2615 2911 75 -1115 93 O ATOM 581 CB SER A 267 13.778 -0.160 -23.274 1.00 20.12 C ANISOU 581 CB SER A 267 3872 1700 2074 80 -832 264 C ATOM 582 OG SER A 267 13.217 0.140 -24.547 1.00 25.63 O ANISOU 582 OG SER A 267 4893 2249 2594 73 -1001 275 O ATOM 583 N CYS A 268 13.529 -3.170 -23.514 1.00 19.56 N ANISOU 583 N CYS A 268 3802 1706 1924 36 -663 192 N ATOM 584 CA CYS A 268 13.352 -4.320 -24.390 1.00 20.56 C ANISOU 584 CA CYS A 268 4152 1758 1900 11 -660 175 C ATOM 585 C CYS A 268 13.090 -5.622 -23.644 1.00 22.61 C ANISOU 585 C CYS A 268 4259 2093 2238 -13 -638 128 C ATOM 586 O CYS A 268 12.720 -6.613 -24.283 1.00 25.45 O ANISOU 586 O CYS A 268 4804 2377 2488 -42 -702 103 O ATOM 587 CB CYS A 268 14.563 -4.489 -25.319 1.00 22.63 C ANISOU 587 CB CYS A 268 4676 1933 1989 11 -412 229 C ATOM 588 SG CYS A 268 16.072 -5.048 -24.502 1.00 20.74 S ANISOU 588 SG CYS A 268 4217 1790 1873 41 -81 241 S ATOM 589 N ARG A 269 13.274 -5.647 -22.323 1.00 19.21 N ANISOU 589 N ARG A 269 3545 1784 1972 -9 -566 118 N ATOM 590 CA ARG A 269 13.000 -6.797 -21.462 1.00 21.19 C ANISOU 590 CA ARG A 269 3677 2091 2282 -54 -551 87 C ATOM 591 C ARG A 269 14.003 -7.933 -21.624 1.00 21.59 C ANISOU 591 C ARG A 269 3871 2077 2255 -33 -393 93 C ATOM 592 O ARG A 269 13.793 -9.011 -21.056 1.00 23.42 O ANISOU 592 O ARG A 269 4092 2309 2498 -77 -410 72 O ATOM 593 CB ARG A 269 11.550 -7.298 -21.568 1.00 24.55 C ANISOU 593 CB ARG A 269 4071 2531 2726 -140 -755 41 C ATOM 594 CG ARG A 269 10.504 -6.203 -21.361 1.00 29.46 C ANISOU 594 CG ARG A 269 4498 3231 3464 -124 -921 3 C ATOM 595 CD ARG A 269 10.283 -5.913 -19.889 1.00 42.53 C ANISOU 595 CD ARG A 269 5853 5038 5266 -122 -844 -21 C ATOM 596 NE ARG A 269 9.560 -4.663 -19.665 1.00 55.48 N ANISOU 596 NE ARG A 269 7321 6748 7012 -43 -965 -71 N ATOM 597 CZ ARG A 269 9.408 -4.083 -18.476 1.00 54.24 C ANISOU 597 CZ ARG A 269 6943 6709 6956 6 -900 -106 C ATOM 598 NH1 ARG A 269 9.930 -4.634 -17.387 1.00 47.64 N ANISOU 598 NH1 ARG A 269 6053 5927 6121 -33 -725 -84 N ATOM 599 NH2 ARG A 269 8.732 -2.947 -18.376 1.00 50.86 N ANISOU 599 NH2 ARG A 269 6385 6326 6615 112 -1030 -170 N ATOM 600 N ASP A 270 15.103 -7.711 -22.338 1.00 19.45 N ANISOU 600 N ASP A 270 3730 1750 1911 36 -232 118 N ATOM 601 CA ASP A 270 16.110 -8.731 -22.605 1.00 19.52 C ANISOU 601 CA ASP A 270 3859 1700 1856 101 -67 99 C ATOM 602 C ASP A 270 17.357 -8.477 -21.759 1.00 19.89 C ANISOU 602 C ASP A 270 3688 1807 2061 170 98 108 C ATOM 603 O ASP A 270 17.528 -7.421 -21.142 1.00 16.84 O ANISOU 603 O ASP A 270 3109 1488 1803 156 94 142 O ATOM 604 CB ASP A 270 16.461 -8.721 -24.102 1.00 22.08 C ANISOU 604 CB ASP A 270 4485 1923 1980 138 32 103 C ATOM 605 CG ASP A 270 17.225 -9.959 -24.561 1.00 25.50 C ANISOU 605 CG ASP A 270 5102 2279 2307 232 176 50 C ATOM 606 OD1 ASP A 270 17.143 -11.014 -23.902 1.00 25.13 O ANISOU 606 OD1 ASP A 270 5029 2215 2306 249 105 9 O ATOM 607 OD2 ASP A 270 17.897 -9.865 -25.610 1.00 29.30 O ANISOU 607 OD2 ASP A 270 5784 2707 2642 292 363 47 O ATOM 608 N GLN A 271 18.228 -9.485 -21.714 1.00 21.71 N ANISOU 608 N GLN A 271 3960 1996 2293 259 209 66 N ATOM 609 CA GLN A 271 19.599 -9.317 -21.244 1.00 20.79 C ANISOU 609 CA GLN A 271 3650 1913 2336 352 370 56 C ATOM 610 C GLN A 271 20.553 -9.345 -22.433 1.00 22.43 C ANISOU 610 C GLN A 271 3957 2097 2470 428 618 40 C ATOM 611 O GLN A 271 21.101 -8.306 -22.814 1.00 23.16 O ANISOU 611 O GLN A 271 3960 2233 2607 391 764 90 O ATOM 612 CB GLN A 271 19.949 -10.368 -20.190 1.00 19.42 C ANISOU 612 CB GLN A 271 3416 1708 2255 423 295 5 C ATOM 613 CG GLN A 271 19.085 -10.243 -18.950 1.00 18.69 C ANISOU 613 CG GLN A 271 3239 1647 2214 329 108 30 C ATOM 614 CD GLN A 271 19.340 -11.336 -17.947 1.00 19.71 C ANISOU 614 CD GLN A 271 3405 1707 2377 374 16 -8 C ATOM 615 OE1 GLN A 271 19.748 -12.444 -18.300 1.00 21.72 O ANISOU 615 OE1 GLN A 271 3817 1866 2571 460 25 -61 O ATOM 616 NE2 GLN A 271 19.118 -11.029 -16.679 1.00 25.01 N ANISOU 616 NE2 GLN A 271 3970 2407 3125 326 -84 14 N ATOM 617 N GLY A 272 20.749 -10.500 -23.054 1.00 20.93 N ANISOU 617 N GLY A 272 3975 1829 2149 527 681 -30 N ATOM 618 CA GLY A 272 21.394 -10.540 -24.355 1.00 23.21 C ANISOU 618 CA GLY A 272 4441 2089 2291 596 936 -53 C ATOM 619 C GLY A 272 22.906 -10.406 -24.311 1.00 24.88 C ANISOU 619 C GLY A 272 4402 2372 2680 707 1219 -91 C ATOM 620 O GLY A 272 23.537 -10.381 -23.254 1.00 26.50 O ANISOU 620 O GLY A 272 4297 2628 3143 753 1176 -109 O ATOM 621 N LYS A 273 23.493 -10.310 -25.509 1.00 27.37 N ANISOU 621 N LYS A 273 4862 2686 2854 748 1517 -106 N ATOM 622 CA LYS A 273 24.950 -10.312 -25.621 1.00 32.80 C ANISOU 622 CA LYS A 273 5289 3456 3717 861 1841 -163 C ATOM 623 C LYS A 273 25.599 -9.074 -25.012 1.00 37.68 C ANISOU 623 C LYS A 273 5517 4184 4614 737 1907 -80 C ATOM 624 O LYS A 273 26.769 -9.140 -24.621 1.00 42.06 O ANISOU 624 O LYS A 273 5725 4815 5440 826 2060 -135 O ATOM 625 CB LYS A 273 25.380 -10.483 -27.080 1.00 42.38 C ANISOU 625 CB LYS A 273 6773 4651 4680 920 2197 -200 C ATOM 626 CG LYS A 273 24.919 -9.370 -28.000 1.00 47.35 C ANISOU 626 CG LYS A 273 7646 5261 5084 721 2294 -75 C ATOM 627 CD LYS A 273 25.422 -9.580 -29.426 1.00 55.42 C ANISOU 627 CD LYS A 273 8902 6258 5898 738 2541 -92 C ATOM 628 CE LYS A 273 26.943 -9.612 -29.484 1.00 60.48 C ANISOU 628 CE LYS A 273 9165 7045 6771 807 2877 -149 C ATOM 629 NZ LYS A 273 27.453 -9.614 -30.886 1.00 63.79 N ANISOU 629 NZ LYS A 273 9797 7461 6981 790 3149 -154 N ATOM 630 N ASN A 274 24.875 -7.958 -24.915 1.00 36.79 N ANISOU 630 N ASN A 274 5451 4069 4457 544 1769 41 N ATOM 631 CA ASN A 274 25.401 -6.726 -24.340 1.00 45.57 C ANISOU 631 CA ASN A 274 6254 5250 5809 411 1782 128 C ATOM 632 C ASN A 274 25.003 -6.540 -22.879 1.00 40.81 C ANISOU 632 C ASN A 274 5448 4649 5409 402 1441 137 C ATOM 633 O ASN A 274 24.979 -5.404 -22.393 1.00 38.95 O ANISOU 633 O ASN A 274 5079 4429 5291 275 1344 219 O ATOM 634 CB ASN A 274 24.953 -5.515 -25.161 1.00 48.22 C ANISOU 634 CB ASN A 274 6808 5555 5958 216 1840 251 C ATOM 635 CG ASN A 274 25.532 -5.509 -26.560 1.00 53.47 C ANISOU 635 CG ASN A 274 7684 6216 6418 190 2230 262 C ATOM 636 OD1 ASN A 274 26.646 -5.981 -26.786 1.00 56.88 O ANISOU 636 OD1 ASN A 274 7924 6723 6966 279 2544 194 O ATOM 637 ND2 ASN A 274 24.775 -4.971 -27.511 1.00 54.88 N ANISOU 637 ND2 ASN A 274 8269 6300 6285 77 2212 339 N ATOM 638 N ALA A 275 24.705 -7.630 -22.166 1.00 29.25 N ANISOU 638 N ALA A 275 3996 3151 3966 532 1257 54 N ATOM 639 CA ALA A 275 24.169 -7.501 -20.815 1.00 26.71 C ANISOU 639 CA ALA A 275 3571 2817 3760 510 951 67 C ATOM 640 C ALA A 275 25.176 -6.862 -19.863 1.00 23.05 C ANISOU 640 C ALA A 275 2759 2387 3612 510 914 77 C ATOM 641 O ALA A 275 24.800 -6.034 -19.022 1.00 23.82 O ANISOU 641 O ALA A 275 2789 2480 3780 426 721 132 O ATOM 642 CB ALA A 275 23.728 -8.870 -20.296 1.00 27.74 C ANISOU 642 CB ALA A 275 3832 2884 3824 623 790 -14 C ATOM 643 N ASP A 276 26.457 -7.220 -19.986 1.00 26.14 N ANISOU 643 N ASP A 276 2922 2807 4204 613 1085 13 N ATOM 644 CA ASP A 276 27.479 -6.734 -19.060 1.00 31.39 C ANISOU 644 CA ASP A 276 3228 3485 5212 623 1002 7 C ATOM 645 C ASP A 276 27.612 -5.215 -19.062 1.00 32.17 C ANISOU 645 C ASP A 276 3205 3613 5405 423 1017 123 C ATOM 646 O ASP A 276 28.082 -4.647 -18.066 1.00 27.15 O ANISOU 646 O ASP A 276 2352 2953 5012 396 826 138 O ATOM 647 CB ASP A 276 28.831 -7.359 -19.393 1.00 37.86 C ANISOU 647 CB ASP A 276 3780 4347 6259 773 1213 -96 C ATOM 648 CG ASP A 276 29.280 -8.360 -18.352 1.00 46.63 C ANISOU 648 CG ASP A 276 4783 5383 7550 979 969 -213 C ATOM 649 OD1 ASP A 276 28.448 -8.739 -17.504 1.00 46.64 O ANISOU 649 OD1 ASP A 276 5000 5296 7426 992 682 -206 O ATOM 650 OD2 ASP A 276 30.463 -8.767 -18.390 1.00 47.20 O ANISOU 650 OD2 ASP A 276 4576 5488 7868 1117 1055 -312 O ATOM 651 N ASN A 277 27.226 -4.549 -20.152 1.00 28.12 N ANISOU 651 N ASN A 277 2866 3124 4694 284 1210 205 N ATOM 652 CA ASN A 277 27.330 -3.100 -20.264 1.00 27.93 C ANISOU 652 CA ASN A 277 2793 3095 4725 81 1216 324 C ATOM 653 C ASN A 277 25.989 -2.387 -20.115 1.00 26.29 C ANISOU 653 C ASN A 277 2865 2828 4297 1 985 391 C ATOM 654 O ASN A 277 25.898 -1.190 -20.407 1.00 25.59 O ANISOU 654 O ASN A 277 2837 2704 4180 -157 976 489 O ATOM 655 CB ASN A 277 28.023 -2.712 -21.573 1.00 32.24 C ANISOU 655 CB ASN A 277 3336 3688 5226 -40 1604 378 C ATOM 656 CG ASN A 277 29.497 -3.051 -21.565 1.00 42.33 C ANISOU 656 CG ASN A 277 4211 5049 6824 7 1840 315 C ATOM 657 OD1 ASN A 277 29.962 -3.870 -22.355 1.00 48.12 O ANISOU 657 OD1 ASN A 277 4936 5843 7505 115 2141 238 O ATOM 658 ND2 ASN A 277 30.242 -2.427 -20.659 1.00 47.82 N ANISOU 658 ND2 ASN A 277 4564 5741 7866 -59 1689 336 N ATOM 659 N MET A 278 24.953 -3.093 -19.671 1.00 19.00 N ANISOU 659 N MET A 278 2619 2323 2278 -195 60 257 N ATOM 660 CA MET A 278 23.684 -2.454 -19.345 1.00 17.07 C ANISOU 660 CA MET A 278 2446 2017 2024 -154 18 235 C ATOM 661 C MET A 278 23.908 -1.414 -18.251 1.00 15.52 C ANISOU 661 C MET A 278 2323 1728 1848 -176 -41 257 C ATOM 662 O MET A 278 24.594 -1.688 -17.263 1.00 18.17 O ANISOU 662 O MET A 278 2650 2045 2210 -203 -51 253 O ATOM 663 CB MET A 278 22.739 -3.543 -18.840 1.00 16.52 C ANISOU 663 CB MET A 278 2354 1956 1969 -91 43 166 C ATOM 664 CG MET A 278 21.335 -3.112 -18.533 1.00 16.66 C ANISOU 664 CG MET A 278 2413 1938 1978 -33 19 152 C ATOM 665 SD MET A 278 20.356 -4.448 -17.778 1.00 16.98 S ANISOU 665 SD MET A 278 2407 2003 2041 21 41 97 S ATOM 666 CE MET A 278 20.337 -5.688 -19.072 1.00 16.99 C ANISOU 666 CE MET A 278 2356 2078 2022 -1 71 73 C ATOM 667 N LEU A 279 23.336 -0.221 -18.432 1.00 14.18 N ANISOU 667 N LEU A 279 2232 1493 1663 -166 -84 281 N ATOM 668 CA LEU A 279 23.442 0.849 -17.443 1.00 14.34 C ANISOU 668 CA LEU A 279 2357 1400 1691 -180 -143 287 C ATOM 669 C LEU A 279 22.430 0.633 -16.325 1.00 16.26 C ANISOU 669 C LEU A 279 2642 1599 1936 -92 -129 216 C ATOM 670 O LEU A 279 21.311 0.174 -16.570 1.00 16.20 O ANISOU 670 O LEU A 279 2601 1630 1926 -13 -91 189 O ATOM 671 CB LEU A 279 23.154 2.203 -18.096 1.00 16.90 C ANISOU 671 CB LEU A 279 2760 1654 2006 -188 -192 340 C ATOM 672 CG LEU A 279 23.949 2.567 -19.348 1.00 18.17 C ANISOU 672 CG LEU A 279 2880 1870 2154 -272 -208 428 C ATOM 673 CD1 LEU A 279 23.529 3.939 -19.841 1.00 18.46 C ANISOU 673 CD1 LEU A 279 3005 1819 2191 -276 -269 486 C ATOM 674 CD2 LEU A 279 25.428 2.530 -19.064 1.00 21.34 C ANISOU 674 CD2 LEU A 279 3250 2291 2566 -377 -230 478 C ATOM 675 N PHE A 280 22.814 0.975 -15.092 1.00 14.71 N ANISOU 675 N PHE A 280 2522 1332 1737 -113 -161 193 N ATOM 676 CA PHE A 280 21.909 0.900 -13.947 1.00 15.56 C ANISOU 676 CA PHE A 280 2684 1401 1829 -30 -141 128 C ATOM 677 C PHE A 280 21.614 2.318 -13.468 1.00 17.02 C ANISOU 677 C PHE A 280 3026 1451 1991 -1 -183 115 C ATOM 678 O PHE A 280 22.543 3.070 -13.149 1.00 19.76 O ANISOU 678 O PHE A 280 3462 1718 2327 -90 -250 134 O ATOM 679 CB PHE A 280 22.545 0.130 -12.787 1.00 15.56 C ANISOU 679 CB PHE A 280 2664 1424 1824 -73 -144 103 C ATOM 680 CG PHE A 280 22.686 -1.362 -13.004 1.00 14.26 C ANISOU 680 CG PHE A 280 2358 1370 1690 -76 -98 105 C ATOM 681 CD1 PHE A 280 22.208 -2.000 -14.138 1.00 13.55 C ANISOU 681 CD1 PHE A 280 2182 1349 1617 -42 -57 111 C ATOM 682 CD2 PHE A 280 23.289 -2.132 -12.022 1.00 18.57 C ANISOU 682 CD2 PHE A 280 2870 1940 2245 -117 -104 100 C ATOM 683 CE1 PHE A 280 22.360 -3.387 -14.295 1.00 14.32 C ANISOU 683 CE1 PHE A 280 2176 1523 1742 -45 -20 101 C ATOM 684 CE2 PHE A 280 23.435 -3.508 -12.169 1.00 19.76 C ANISOU 684 CE2 PHE A 280 2901 2171 2434 -113 -67 103 C ATOM 685 CZ PHE A 280 22.966 -4.132 -13.301 1.00 15.98 C ANISOU 685 CZ PHE A 280 2353 1745 1975 -74 -23 98 C ATOM 686 N CYS A 281 20.326 2.676 -13.391 1.00 15.45 N ANISOU 686 N CYS A 281 2864 1222 1786 123 -145 86 N ATOM 687 CA CYS A 281 19.926 4.018 -12.978 1.00 16.62 C ANISOU 687 CA CYS A 281 3170 1227 1918 181 -170 66 C ATOM 688 C CYS A 281 20.325 4.287 -11.530 1.00 16.37 C ANISOU 688 C CYS A 281 3268 1116 1836 162 -190 0 C ATOM 689 O CYS A 281 20.082 3.465 -10.640 1.00 16.77 O ANISOU 689 O CYS A 281 3283 1232 1859 191 -146 -45 O ATOM 690 CB CYS A 281 18.413 4.175 -13.129 1.00 17.49 C ANISOU 690 CB CYS A 281 3263 1344 2038 340 -107 58 C ATOM 691 SG CYS A 281 17.806 5.795 -12.604 1.00 20.68 S ANISOU 691 SG CYS A 281 3865 1559 2431 454 -115 26 S ATOM 692 N ASP A 282 20.935 5.445 -11.290 1.00 19.57 N ANISOU 692 N ASP A 282 3834 1378 2225 103 -265 -2 N ATOM 693 CA ASP A 282 21.341 5.803 -9.936 1.00 19.95 C ANISOU 693 CA ASP A 282 4037 1336 2208 68 -300 -69 C ATOM 694 C ASP A 282 20.197 6.331 -9.087 1.00 21.10 C ANISOU 694 C ASP A 282 4271 1441 2305 222 -232 -151 C ATOM 695 O ASP A 282 20.404 6.599 -7.899 1.00 26.28 O ANISOU 695 O ASP A 282 5033 2065 2888 204 -243 -211 O ATOM 696 CB ASP A 282 22.502 6.794 -9.969 1.00 20.71 C ANISOU 696 CB ASP A 282 4206 1366 2295 -77 -408 -30 C ATOM 697 CG ASP A 282 23.788 6.135 -10.385 1.00 23.59 C ANISOU 697 CG ASP A 282 4467 1806 2691 -239 -466 53 C ATOM 698 OD1 ASP A 282 24.091 5.049 -9.854 1.00 25.49 O ANISOU 698 OD1 ASP A 282 4634 2127 2923 -273 -445 47 O ATOM 699 OD2 ASP A 282 24.479 6.663 -11.271 1.00 22.89 O ANISOU 699 OD2 ASP A 282 4341 1719 2636 -326 -523 133 O ATOM 700 N SER A 283 19.000 6.454 -9.649 1.00 23.98 N ANISOU 700 N SER A 283 4585 1821 2705 371 -159 -144 N ATOM 701 CA SER A 283 17.814 6.805 -8.885 1.00 23.21 C ANISOU 701 CA SER A 283 4528 1719 2571 532 -73 -202 C ATOM 702 C SER A 283 16.938 5.600 -8.548 1.00 23.43 C ANISOU 702 C SER A 283 4439 1875 2590 633 24 -212 C ATOM 703 O SER A 283 16.472 5.486 -7.410 1.00 23.71 O ANISOU 703 O SER A 283 4510 1939 2560 699 83 -269 O ATOM 704 CB SER A 283 16.995 7.858 -9.640 1.00 26.78 C ANISOU 704 CB SER A 283 4990 2111 3076 635 -57 -170 C ATOM 705 OG SER A 283 15.797 8.142 -8.951 1.00 34.87 O ANISOU 705 OG SER A 283 6027 3145 4075 798 37 -212 O ATOM 706 N CYS A 284 16.715 4.684 -9.501 1.00 20.07 N ANISOU 706 N CYS A 284 3847 1556 2224 627 38 -147 N ATOM 707 CA CYS A 284 15.782 3.584 -9.311 1.00 19.99 C ANISOU 707 CA CYS A 284 3679 1700 2217 703 119 -132 C ATOM 708 C CYS A 284 16.406 2.211 -9.497 1.00 16.90 C ANISOU 708 C CYS A 284 3141 1437 1843 579 96 -104 C ATOM 709 O CYS A 284 15.724 1.208 -9.262 1.00 17.40 O ANISOU 709 O CYS A 284 3082 1621 1909 619 147 -89 O ATOM 710 CB CYS A 284 14.585 3.714 -10.268 1.00 22.04 C ANISOU 710 CB CYS A 284 3835 2005 2535 820 161 -65 C ATOM 711 SG CYS A 284 14.982 3.440 -12.011 1.00 18.60 S ANISOU 711 SG CYS A 284 3279 1618 2169 711 93 25 S ATOM 712 N ASP A 285 17.666 2.137 -9.926 1.00 15.00 N ANISOU 712 N ASP A 285 2906 1173 1619 435 22 -88 N ATOM 713 CA ASP A 285 18.410 0.904 -10.193 1.00 13.86 C ANISOU 713 CA ASP A 285 2632 1132 1502 326 3 -59 C ATOM 714 C ASP A 285 17.856 0.076 -11.342 1.00 12.14 C ANISOU 714 C ASP A 285 2261 1017 1335 341 27 -11 C ATOM 715 O ASP A 285 18.286 -1.062 -11.517 1.00 12.88 O ANISOU 715 O ASP A 285 2252 1192 1450 277 26 1 O ATOM 716 CB ASP A 285 18.642 0.024 -8.955 1.00 14.33 C ANISOU 716 CB ASP A 285 2672 1248 1526 297 17 -90 C ATOM 717 CG ASP A 285 19.942 -0.759 -9.035 1.00 14.13 C ANISOU 717 CG ASP A 285 2580 1261 1528 160 -33 -61 C ATOM 718 OD1 ASP A 285 20.966 -0.146 -9.407 1.00 17.92 O ANISOU 718 OD1 ASP A 285 3111 1680 2017 71 -93 -39 O ATOM 719 OD2 ASP A 285 19.948 -1.967 -8.741 1.00 14.39 O ANISOU 719 OD2 ASP A 285 2505 1383 1579 142 -14 -49 O ATOM 720 N ARG A 286 16.934 0.609 -12.146 1.00 13.88 N ANISOU 720 N ARG A 286 2469 1232 1574 421 44 20 N ATOM 721 CA ARG A 286 16.533 -0.137 -13.328 1.00 13.81 C ANISOU 721 CA ARG A 286 2331 1317 1600 406 47 69 C ATOM 722 C ARG A 286 17.692 -0.202 -14.319 1.00 13.80 C ANISOU 722 C ARG A 286 2317 1315 1612 290 2 91 C ATOM 723 O ARG A 286 18.565 0.669 -14.344 1.00 15.76 O ANISOU 723 O ARG A 286 2652 1483 1854 237 -38 96 O ATOM 724 CB ARG A 286 15.316 0.518 -13.990 1.00 16.39 C ANISOU 724 CB ARG A 286 2642 1642 1942 506 62 117 C ATOM 725 CG ARG A 286 14.006 0.302 -13.240 1.00 18.08 C ANISOU 725 CG ARG A 286 2811 1907 2152 629 122 123 C ATOM 726 CD ARG A 286 12.873 0.986 -13.993 1.00 20.92 C ANISOU 726 CD ARG A 286 3138 2270 2541 727 132 194 C ATOM 727 NE ARG A 286 11.572 0.887 -13.328 1.00 23.53 N ANISOU 727 NE ARG A 286 3408 2659 2873 861 198 222 N ATOM 728 CZ ARG A 286 11.013 1.871 -12.626 1.00 21.96 C ANISOU 728 CZ ARG A 286 3288 2389 2667 1002 252 209 C ATOM 729 NH1 ARG A 286 11.650 3.023 -12.465 1.00 22.06 N ANISOU 729 NH1 ARG A 286 3462 2251 2669 1017 235 159 N ATOM 730 NH2 ARG A 286 9.814 1.697 -12.080 1.00 28.84 N ANISOU 730 NH2 ARG A 286 4079 3339 3539 1130 325 249 N ATOM 731 N GLY A 287 17.690 -1.245 -15.141 1.00 12.22 N ANISOU 731 N GLY A 287 2011 1206 1424 249 9 108 N ATOM 732 CA GLY A 287 18.687 -1.418 -16.184 1.00 13.87 C ANISOU 732 CA GLY A 287 2197 1438 1636 158 -12 129 C ATOM 733 C GLY A 287 18.176 -0.993 -17.552 1.00 13.24 C ANISOU 733 C GLY A 287 2101 1384 1547 161 -25 178 C ATOM 734 O GLY A 287 17.010 -1.211 -17.890 1.00 14.71 O ANISOU 734 O GLY A 287 2243 1613 1733 215 -18 198 O ATOM 735 N PHE A 288 19.067 -0.398 -18.343 1.00 13.60 N ANISOU 735 N PHE A 288 2172 1413 1581 93 -51 213 N ATOM 736 CA PHE A 288 18.794 -0.093 -19.743 1.00 12.71 C ANISOU 736 CA PHE A 288 2040 1343 1447 71 -67 267 C ATOM 737 C PHE A 288 20.043 -0.369 -20.564 1.00 14.70 C ANISOU 737 C PHE A 288 2266 1645 1674 -22 -61 283 C ATOM 738 O PHE A 288 21.116 0.130 -20.231 1.00 15.82 O ANISOU 738 O PHE A 288 2439 1746 1826 -73 -77 300 O ATOM 739 CB PHE A 288 18.458 1.390 -19.940 1.00 15.72 C ANISOU 739 CB PHE A 288 2495 1640 1838 99 -109 324 C ATOM 740 CG PHE A 288 17.123 1.797 -19.400 1.00 17.08 C ANISOU 740 CG PHE A 288 2684 1771 2034 214 -102 327 C ATOM 741 CD1 PHE A 288 16.016 1.841 -20.234 1.00 18.63 C ANISOU 741 CD1 PHE A 288 2828 2020 2232 255 -111 386 C ATOM 742 CD2 PHE A 288 16.978 2.161 -18.070 1.00 18.16 C ANISOU 742 CD2 PHE A 288 2889 1825 2188 282 -86 280 C ATOM 743 CE1 PHE A 288 14.778 2.224 -19.745 1.00 21.82 C ANISOU 743 CE1 PHE A 288 3226 2398 2666 373 -96 408 C ATOM 744 CE2 PHE A 288 15.745 2.541 -17.571 1.00 21.81 C ANISOU 744 CE2 PHE A 288 3360 2259 2668 407 -61 286 C ATOM 745 CZ PHE A 288 14.647 2.577 -18.408 1.00 23.52 C ANISOU 745 CZ PHE A 288 3505 2533 2899 457 -63 355 C ATOM 746 N HIS A 289 19.902 -1.125 -21.650 1.00 14.74 N ANISOU 746 N HIS A 289 2218 1741 1640 -47 -40 283 N ATOM 747 CA HIS A 289 20.965 -1.158 -22.647 1.00 15.26 C ANISOU 747 CA HIS A 289 2267 1866 1666 -120 -24 311 C ATOM 748 C HIS A 289 21.180 0.253 -23.174 1.00 17.20 C ANISOU 748 C HIS A 289 2557 2076 1902 -157 -73 398 C ATOM 749 O HIS A 289 20.224 1.007 -23.354 1.00 16.14 O ANISOU 749 O HIS A 289 2455 1902 1774 -122 -113 437 O ATOM 750 CB HIS A 289 20.560 -2.040 -23.832 1.00 17.33 C ANISOU 750 CB HIS A 289 2494 2224 1865 -135 2 293 C ATOM 751 CG HIS A 289 20.345 -3.478 -23.487 1.00 15.71 C ANISOU 751 CG HIS A 289 2258 2043 1668 -110 39 211 C ATOM 752 ND1 HIS A 289 19.120 -4.096 -23.588 1.00 20.22 N ANISOU 752 ND1 HIS A 289 2820 2633 2230 -87 20 189 N ATOM 753 CD2 HIS A 289 21.214 -4.427 -23.064 1.00 21.42 C ANISOU 753 CD2 HIS A 289 2953 2772 2413 -110 89 158 C ATOM 754 CE1 HIS A 289 19.240 -5.364 -23.225 1.00 18.22 C ANISOU 754 CE1 HIS A 289 2546 2386 1992 -79 51 120 C ATOM 755 NE2 HIS A 289 20.500 -5.587 -22.905 1.00 17.88 N ANISOU 755 NE2 HIS A 289 2491 2332 1970 -86 96 99 N ATOM 756 N MET A 290 22.440 0.613 -23.435 1.00 17.98 N ANISOU 756 N MET A 290 2650 2190 1992 -229 -71 443 N ATOM 757 CA MET A 290 22.713 1.922 -24.030 1.00 18.96 C ANISOU 757 CA MET A 290 2813 2285 2106 -283 -126 542 C ATOM 758 C MET A 290 21.876 2.163 -25.283 1.00 17.46 C ANISOU 758 C MET A 290 2618 2151 1864 -284 -142 589 C ATOM 759 O MET A 290 21.326 3.254 -25.473 1.00 18.01 O ANISOU 759 O MET A 290 2735 2156 1951 -278 -203 658 O ATOM 760 CB MET A 290 24.202 2.078 -24.340 1.00 23.17 C ANISOU 760 CB MET A 290 3311 2868 2626 -373 -115 603 C ATOM 761 CG MET A 290 25.025 2.491 -23.127 1.00 22.40 C ANISOU 761 CG MET A 290 3243 2682 2586 -406 -152 612 C ATOM 762 SD MET A 290 26.768 2.691 -23.518 1.00 31.26 S ANISOU 762 SD MET A 290 4296 3882 3700 -523 -148 718 S ATOM 763 CE MET A 290 27.186 1.004 -23.924 1.00 28.16 C ANISOU 763 CE MET A 290 3789 3634 3278 -476 -23 652 C ATOM 764 N GLU A 291 21.751 1.147 -26.142 1.00 21.22 N ANISOU 764 N GLU A 291 3045 2743 2273 -293 -91 556 N ATOM 765 CA GLU A 291 20.994 1.307 -27.379 1.00 24.19 C ANISOU 765 CA GLU A 291 3420 3189 2583 -314 -114 605 C ATOM 766 C GLU A 291 19.485 1.384 -27.156 1.00 18.87 C ANISOU 766 C GLU A 291 2757 2474 1939 -248 -157 602 C ATOM 767 O GLU A 291 18.753 1.697 -28.101 1.00 22.72 O ANISOU 767 O GLU A 291 3240 3008 2383 -268 -197 668 O ATOM 768 CB GLU A 291 21.345 0.185 -28.363 1.00 25.03 C ANISOU 768 CB GLU A 291 3493 3426 2591 -349 -49 559 C ATOM 769 CG GLU A 291 20.961 -1.217 -27.896 1.00 30.48 C ANISOU 769 CG GLU A 291 4171 4124 3287 -299 -4 441 C ATOM 770 CD GLU A 291 22.035 -1.895 -27.053 1.00 34.96 C ANISOU 770 CD GLU A 291 4711 4671 3901 -278 60 379 C ATOM 771 OE1 GLU A 291 22.903 -1.195 -26.487 1.00 28.55 O ANISOU 771 OE1 GLU A 291 3892 3818 3139 -295 53 426 O ATOM 772 OE2 GLU A 291 22.013 -3.143 -26.960 1.00 43.54 O ANISOU 772 OE2 GLU A 291 5786 5779 4978 -251 109 290 O ATOM 773 N CYS A 292 19.004 1.116 -25.940 1.00 17.34 N ANISOU 773 N CYS A 292 2568 2206 1814 -172 -150 542 N ATOM 774 CA CYS A 292 17.586 1.188 -25.610 1.00 18.17 C ANISOU 774 CA CYS A 292 2665 2283 1955 -96 -178 552 C ATOM 775 C CYS A 292 17.215 2.448 -24.840 1.00 20.70 C ANISOU 775 C CYS A 292 3036 2479 2350 -27 -213 596 C ATOM 776 O CYS A 292 16.047 2.616 -24.477 1.00 22.18 O ANISOU 776 O CYS A 292 3210 2641 2575 58 -223 614 O ATOM 777 CB CYS A 292 17.183 -0.035 -24.786 1.00 17.10 C ANISOU 777 CB CYS A 292 2495 2163 1839 -52 -139 461 C ATOM 778 SG CYS A 292 17.376 -1.612 -25.664 1.00 20.61 S ANISOU 778 SG CYS A 292 2905 2724 2202 -117 -105 396 S ATOM 779 N CYS A 293 18.178 3.322 -24.564 1.00 17.58 N ANISOU 779 N CYS A 293 2700 2004 1975 -59 -230 616 N ATOM 780 CA CYS A 293 17.873 4.576 -23.905 1.00 16.99 C ANISOU 780 CA CYS A 293 2704 1788 1964 2 -270 650 C ATOM 781 C CYS A 293 17.186 5.536 -24.871 1.00 19.63 C ANISOU 781 C CYS A 293 3044 2109 2305 9 -326 765 C ATOM 782 O CYS A 293 17.204 5.361 -26.092 1.00 19.69 O ANISOU 782 O CYS A 293 3003 2220 2257 -62 -344 828 O ATOM 783 CB CYS A 293 19.151 5.203 -23.354 1.00 17.20 C ANISOU 783 CB CYS A 293 2803 1726 2005 -60 -291 645 C ATOM 784 SG CYS A 293 19.865 4.224 -22.032 1.00 19.00 S ANISOU 784 SG CYS A 293 3027 1955 2239 -60 -240 530 S ATOM 785 N ASP A 294 16.563 6.557 -24.298 1.00 21.24 N ANISOU 785 N ASP A 294 3313 2180 2575 102 -352 792 N ATOM 786 CA ASP A 294 15.908 7.595 -25.073 1.00 22.20 C ANISOU 786 CA ASP A 294 3447 2259 2727 127 -411 912 C ATOM 787 C ASP A 294 16.563 8.932 -24.767 1.00 25.36 C ANISOU 787 C ASP A 294 3971 2491 3175 112 -466 948 C ATOM 788 O ASP A 294 16.261 9.549 -23.746 1.00 31.09 O ANISOU 788 O ASP A 294 4789 3068 3957 213 -461 904 O ATOM 789 CB ASP A 294 14.423 7.640 -24.721 1.00 24.33 C ANISOU 789 CB ASP A 294 3681 2514 3050 274 -391 930 C ATOM 790 CG ASP A 294 13.721 8.822 -25.346 1.00 30.11 C ANISOU 790 CG ASP A 294 4429 3174 3836 326 -451 1062 C ATOM 791 OD1 ASP A 294 14.167 9.279 -26.422 1.00 27.65 O ANISOU 791 OD1 ASP A 294 4117 2890 3499 221 -513 1157 O ATOM 792 OD2 ASP A 294 12.731 9.304 -24.755 1.00 36.99 O ANISOU 792 OD2 ASP A 294 5312 3966 4779 476 -431 1078 O ATOM 793 N PRO A 295 17.458 9.396 -25.653 1.00 22.95 N ANISOU 793 N PRO A 295 3675 2206 2840 -17 -520 1031 N ATOM 794 CA PRO A 295 17.858 8.823 -26.945 1.00 20.81 C ANISOU 794 CA PRO A 295 3312 2109 2487 -135 -522 1091 C ATOM 795 C PRO A 295 18.900 7.722 -26.781 1.00 18.11 C ANISOU 795 C PRO A 295 2927 1873 2081 -211 -461 1003 C ATOM 796 O PRO A 295 19.508 7.601 -25.710 1.00 18.28 O ANISOU 796 O PRO A 295 2992 1823 2130 -201 -440 923 O ATOM 797 CB PRO A 295 18.480 10.023 -27.660 1.00 23.62 C ANISOU 797 CB PRO A 295 3700 2421 2854 -219 -587 1192 C ATOM 798 CG PRO A 295 19.111 10.778 -26.550 1.00 28.16 C ANISOU 798 CG PRO A 295 4377 2830 3492 -206 -603 1137 C ATOM 799 CD PRO A 295 18.147 10.676 -25.401 1.00 27.58 C ANISOU 799 CD PRO A 295 4362 2645 3473 -53 -574 1059 C ATOM 800 N PRO A 296 19.088 6.902 -27.815 1.00 21.64 N ANISOU 800 N PRO A 296 3294 2488 2442 -281 -431 1016 N ATOM 801 CA PRO A 296 20.082 5.829 -27.719 1.00 21.21 C ANISOU 801 CA PRO A 296 3196 2530 2333 -334 -362 935 C ATOM 802 C PRO A 296 21.470 6.417 -27.543 1.00 24.32 C ANISOU 802 C PRO A 296 3616 2888 2735 -422 -379 978 C ATOM 803 O PRO A 296 21.794 7.464 -28.106 1.00 22.97 O ANISOU 803 O PRO A 296 3473 2686 2567 -489 -444 1094 O ATOM 804 CB PRO A 296 19.953 5.100 -29.062 1.00 26.76 C ANISOU 804 CB PRO A 296 3834 3403 2930 -391 -335 957 C ATOM 805 CG PRO A 296 18.595 5.452 -29.556 1.00 30.15 C ANISOU 805 CG PRO A 296 4259 3829 3366 -348 -388 1019 C ATOM 806 CD PRO A 296 18.345 6.851 -29.085 1.00 25.47 C ANISOU 806 CD PRO A 296 3728 3080 2869 -307 -456 1099 C ATOM 807 N LEU A 297 22.287 5.731 -26.747 1.00 21.07 N ANISOU 807 N LEU A 297 3189 2484 2333 -428 -330 899 N ATOM 808 CA LEU A 297 23.607 6.214 -26.378 1.00 23.27 C ANISOU 808 CA LEU A 297 3482 2729 2631 -515 -354 945 C ATOM 809 C LEU A 297 24.687 5.382 -27.051 1.00 20.84 C ANISOU 809 C LEU A 297 3076 2585 2256 -583 -282 959 C ATOM 810 O LEU A 297 24.615 4.151 -27.083 1.00 24.14 O ANISOU 810 O LEU A 297 3440 3091 2641 -537 -199 868 O ATOM 811 CB LEU A 297 23.797 6.185 -24.865 1.00 22.48 C ANISOU 811 CB LEU A 297 3437 2507 2596 -476 -363 864 C ATOM 812 CG LEU A 297 22.849 7.126 -24.124 1.00 22.44 C ANISOU 812 CG LEU A 297 3548 2329 2651 -399 -423 847 C ATOM 813 CD1 LEU A 297 22.978 6.934 -22.620 1.00 24.11 C ANISOU 813 CD1 LEU A 297 3820 2442 2899 -357 -417 749 C ATOM 814 CD2 LEU A 297 23.123 8.565 -24.522 1.00 28.70 C ANISOU 814 CD2 LEU A 297 4418 3019 3468 -467 -519 964 C ATOM 815 N THR A 298 25.685 6.076 -27.596 1.00 21.35 N ANISOU 815 N THR A 298 2909 3341 1861 156 -116 -142 N ATOM 816 CA THR A 298 26.823 5.431 -28.232 1.00 23.16 C ANISOU 816 CA THR A 298 3230 3408 2159 144 -64 -94 C ATOM 817 C THR A 298 27.954 5.158 -27.251 1.00 23.20 C ANISOU 817 C THR A 298 3352 3054 2411 18 -51 14 C ATOM 818 O THR A 298 28.672 4.163 -27.393 1.00 26.10 O ANISOU 818 O THR A 298 3772 3273 2874 -38 -52 -50 O ATOM 819 CB THR A 298 27.344 6.333 -29.358 1.00 26.48 C ANISOU 819 CB THR A 298 3697 3903 2460 401 2 70 C ATOM 820 OG1 THR A 298 26.290 6.591 -30.299 1.00 34.59 O ANISOU 820 OG1 THR A 298 4652 5291 3199 597 -69 -17 O ATOM 821 CG2 THR A 298 28.511 5.687 -30.072 1.00 30.90 C ANISOU 821 CG2 THR A 298 4295 4369 3077 379 100 60 C ATOM 822 N AARG A 299 28.130 6.022 -26.257 0.46 18.44 N ANISOU 822 N AARG A 299 2785 2319 1904 5 -61 148 N ATOM 823 N BARG A 299 28.122 6.020 -26.255 0.54 18.24 N ANISOU 823 N BARG A 299 2759 2295 1878 5 -61 147 N ATOM 824 CA AARG A 299 29.185 5.882 -25.268 0.46 18.07 C ANISOU 824 CA AARG A 299 2817 1997 2052 -81 -99 226 C ATOM 825 CA BARG A 299 29.178 5.888 -25.269 0.54 18.05 C ANISOU 825 CA BARG A 299 2813 1995 2048 -80 -99 226 C ATOM 826 C AARG A 299 28.565 5.906 -23.880 0.46 18.56 C ANISOU 826 C AARG A 299 2950 2001 2101 -243 -161 214 C ATOM 827 C BARG A 299 28.571 5.931 -23.877 0.54 18.67 C ANISOU 827 C BARG A 299 2963 2015 2116 -241 -160 216 C ATOM 828 O AARG A 299 27.475 6.447 -23.675 0.46 18.52 O ANISOU 828 O AARG A 299 2885 2168 1984 -260 -133 159 O ATOM 829 O BARG A 299 27.489 6.483 -23.662 0.54 18.29 O ANISOU 829 O BARG A 299 2856 2137 1957 -257 -133 163 O ATOM 830 CB AARG A 299 30.205 7.022 -25.382 0.46 18.04 C ANISOU 830 CB AARG A 299 2785 1903 2165 16 -27 364 C ATOM 831 CB BARG A 299 30.211 7.013 -25.402 0.54 17.96 C ANISOU 831 CB BARG A 299 2775 1895 2155 17 -26 363 C ATOM 832 CG AARG A 299 30.996 7.033 -26.680 0.46 19.07 C ANISOU 832 CG AARG A 299 2864 2088 2291 118 98 379 C ATOM 833 CG BARG A 299 31.067 6.923 -26.649 0.54 19.44 C ANISOU 833 CG BARG A 299 2907 2127 2352 112 91 369 C ATOM 834 CD AARG A 299 31.936 5.841 -26.769 0.46 19.56 C ANISOU 834 CD AARG A 299 2871 2075 2486 108 54 259 C ATOM 835 CD BARG A 299 32.064 8.072 -26.729 0.54 23.79 C ANISOU 835 CD BARG A 299 3440 2583 3018 105 230 480 C ATOM 836 NE AARG A 299 32.938 6.014 -27.818 0.46 25.30 N ANISOU 836 NE AARG A 299 3495 2870 3247 174 217 236 N ATOM 837 NE BARG A 299 32.934 8.148 -25.558 0.54 26.19 N ANISOU 837 NE BARG A 299 3677 2732 3544 1 147 443 N ATOM 838 CZ AARG A 299 32.798 5.577 -29.065 0.46 22.70 C ANISOU 838 CZ AARG A 299 3157 2705 2762 247 317 162 C ATOM 839 CZ BARG A 299 32.811 9.045 -24.582 0.54 24.36 C ANISOU 839 CZ BARG A 299 3490 2395 3369 -75 118 490 C ATOM 840 NH1AARG A 299 31.694 4.934 -29.420 0.46 24.06 N ANISOU 840 NH1AARG A 299 3393 2992 2756 264 240 80 N ATOM 841 NH1BARG A 299 31.846 9.970 -24.616 0.54 18.22 N ANISOU 841 NH1BARG A 299 2835 1615 2473 -32 175 579 N ATOM 842 NH2AARG A 299 33.762 5.782 -29.957 0.46 24.73 N ANISOU 842 NH2AARG A 299 3326 3044 3027 272 511 131 N ATOM 843 NH2BARG A 299 33.666 9.018 -23.569 0.54 24.13 N ANISOU 843 NH2BARG A 299 3379 2282 3508 -160 10 416 N ATOM 844 N AMET A 300 29.276 5.325 -22.924 0.46 19.79 N ANISOU 844 N AMET A 300 3235 1937 2348 -336 -251 249 N ATOM 845 N BMET A 300 29.294 5.349 -22.934 0.54 19.72 N ANISOU 845 N BMET A 300 3223 1928 2342 -332 -250 250 N ATOM 846 CA AMET A 300 28.766 5.269 -21.559 0.46 22.46 C ANISOU 846 CA AMET A 300 3707 2218 2611 -515 -295 253 C ATOM 847 CA BMET A 300 28.841 5.305 -21.554 0.54 22.58 C ANISOU 847 CA BMET A 300 3720 2226 2636 -506 -299 259 C ATOM 848 C AMET A 300 28.741 6.667 -20.951 0.46 20.47 C ANISOU 848 C AMET A 300 3380 2016 2382 -474 -275 294 C ATOM 849 C BMET A 300 28.734 6.720 -20.998 0.54 20.62 C ANISOU 849 C BMET A 300 3391 2041 2403 -466 -270 294 C ATOM 850 O AMET A 300 29.738 7.394 -21.031 0.46 20.17 O ANISOU 850 O AMET A 300 3286 1892 2485 -367 -292 359 O ATOM 851 O BMET A 300 29.673 7.514 -21.152 0.54 20.39 O ANISOU 851 O BMET A 300 3298 1936 2512 -353 -275 360 O ATOM 852 CB AMET A 300 29.624 4.356 -20.693 0.46 26.40 C ANISOU 852 CB AMET A 300 4429 2455 3148 -556 -441 316 C ATOM 853 CB BMET A 300 29.870 4.546 -20.730 0.54 25.51 C ANISOU 853 CB BMET A 300 4281 2341 3071 -512 -453 328 C ATOM 854 CG AMET A 300 29.128 4.258 -19.257 0.46 34.48 C ANISOU 854 CG AMET A 300 5670 3419 4014 -759 -475 350 C ATOM 855 CG BMET A 300 29.445 4.339 -19.307 0.54 34.60 C ANISOU 855 CG BMET A 300 5664 3412 4071 -703 -506 366 C ATOM 856 SD AMET A 300 30.228 3.317 -18.191 0.46 38.24 S ANISOU 856 SD AMET A 300 6461 3605 4464 -692 -710 466 S ATOM 857 SD BMET A 300 28.896 2.651 -19.123 0.54 43.88 S ANISOU 857 SD BMET A 300 7190 4380 5101 -912 -492 358 S ATOM 858 CE AMET A 300 30.488 1.861 -19.203 0.46 45.85 C ANISOU 858 CE AMET A 300 7525 4388 5506 -594 -717 425 C ATOM 859 CE BMET A 300 30.471 1.797 -19.157 0.54 46.17 C ANISOU 859 CE BMET A 300 7582 4422 5538 -599 -718 426 C ATOM 860 N PRO A 301 27.632 7.075 -20.341 1.00 19.06 N ANISOU 860 N PRO A 301 3187 1977 2078 -576 -216 215 N ATOM 861 CA PRO A 301 27.583 8.376 -19.672 1.00 17.20 C ANISOU 861 CA PRO A 301 2915 1748 1871 -525 -195 213 C ATOM 862 C PRO A 301 28.589 8.421 -18.534 1.00 21.73 C ANISOU 862 C PRO A 301 3619 2143 2496 -610 -304 267 C ATOM 863 O PRO A 301 28.922 7.401 -17.925 1.00 23.25 O ANISOU 863 O PRO A 301 3976 2243 2617 -721 -406 305 O ATOM 864 CB PRO A 301 26.150 8.439 -19.131 1.00 22.05 C ANISOU 864 CB PRO A 301 3471 2587 2319 -641 -110 49 C ATOM 865 CG PRO A 301 25.382 7.457 -19.964 1.00 27.93 C ANISOU 865 CG PRO A 301 4133 3505 2976 -708 -68 -47 C ATOM 866 CD PRO A 301 26.352 6.357 -20.256 1.00 22.18 C ANISOU 866 CD PRO A 301 3570 2548 2309 -765 -140 69 C ATOM 867 N LYS A 302 29.072 9.622 -18.248 1.00 19.02 N ANISOU 867 N LYS A 302 3227 1738 2260 -545 -294 261 N ATOM 868 CA LYS A 302 30.069 9.828 -17.211 1.00 19.80 C ANISOU 868 CA LYS A 302 3385 1730 2408 -617 -419 250 C ATOM 869 C LYS A 302 29.387 10.280 -15.924 1.00 19.94 C ANISOU 869 C LYS A 302 3495 1815 2265 -746 -410 145 C ATOM 870 O LYS A 302 28.438 11.069 -15.954 1.00 21.00 O ANISOU 870 O LYS A 302 3573 2034 2370 -715 -273 51 O ATOM 871 CB LYS A 302 31.086 10.881 -17.664 1.00 24.24 C ANISOU 871 CB LYS A 302 3826 2186 3199 -550 -377 242 C ATOM 872 CG LYS A 302 32.343 10.937 -16.796 1.00 36.18 C ANISOU 872 CG LYS A 302 5297 3653 4797 -621 -543 167 C ATOM 873 CD LYS A 302 33.434 11.799 -17.423 1.00 38.45 C ANISOU 873 CD LYS A 302 5411 3862 5336 -637 -448 114 C ATOM 874 CE LYS A 302 34.659 11.892 -16.519 1.00 39.61 C ANISOU 874 CE LYS A 302 5425 4050 5577 -720 -635 -51 C ATOM 875 NZ LYS A 302 35.698 12.805 -17.075 1.00 42.33 N ANISOU 875 NZ LYS A 302 5561 4342 6181 -836 -481 -170 N ATOM 876 N GLY A 303 29.862 9.764 -14.792 1.00 25.65 N ANISOU 876 N GLY A 303 5420 2385 1941 -1420 -910 314 N ATOM 877 CA GLY A 303 29.300 10.158 -13.519 1.00 26.99 C ANISOU 877 CA GLY A 303 5829 2364 2060 -1345 -887 278 C ATOM 878 C GLY A 303 27.950 9.514 -13.246 1.00 24.75 C ANISOU 878 C GLY A 303 5529 2030 1843 -1036 -835 206 C ATOM 879 O GLY A 303 27.549 8.540 -13.885 1.00 25.52 O ANISOU 879 O GLY A 303 5371 2283 2043 -876 -830 203 O ATOM 880 N AMET A 304 27.239 10.090 -12.272 0.51 26.43 N ANISOU 880 N AMET A 304 6015 2054 1971 -943 -780 165 N ATOM 881 N BMET A 304 27.246 10.077 -12.266 0.49 26.39 N ANISOU 881 N BMET A 304 6007 2052 1967 -944 -781 165 N ATOM 882 CA AMET A 304 25.901 9.623 -11.917 0.51 25.98 C ANISOU 882 CA AMET A 304 5978 1951 1941 -655 -704 98 C ATOM 883 CA BMET A 304 25.919 9.580 -11.931 0.49 25.89 C ANISOU 883 CA BMET A 304 5954 1948 1935 -656 -706 99 C ATOM 884 C AMET A 304 24.977 9.722 -13.126 0.51 24.35 C ANISOU 884 C AMET A 304 5731 1710 1813 -425 -666 107 C ATOM 885 C BMET A 304 24.999 9.701 -13.138 0.49 24.27 C ANISOU 885 C BMET A 304 5715 1704 1804 -429 -668 108 C ATOM 886 O AMET A 304 25.018 10.697 -13.878 0.51 25.45 O ANISOU 886 O AMET A 304 5984 1764 1922 -445 -670 120 O ATOM 887 O BMET A 304 25.068 10.668 -13.899 0.49 25.27 O ANISOU 887 O BMET A 304 5953 1748 1900 -455 -674 123 O ATOM 888 CB AMET A 304 25.353 10.483 -10.772 0.51 28.80 C ANISOU 888 CB AMET A 304 6611 2155 2176 -592 -613 40 C ATOM 889 CB BMET A 304 25.349 10.364 -10.752 0.49 28.56 C ANISOU 889 CB BMET A 304 6559 2139 2155 -589 -615 40 C ATOM 890 CG AMET A 304 24.008 10.037 -10.188 0.51 32.23 C ANISOU 890 CG AMET A 304 7038 2565 2643 -315 -491 -40 C ATOM 891 CG BMET A 304 26.066 10.085 -9.444 0.49 30.77 C ANISOU 891 CG BMET A 304 6807 2500 2386 -773 -637 30 C ATOM 892 SD AMET A 304 23.459 11.047 -8.781 0.51 39.49 S ANISOU 892 SD AMET A 304 8232 3338 3433 -267 -357 -142 S ATOM 893 SD BMET A 304 25.210 10.724 -7.992 0.49 40.58 S ANISOU 893 SD BMET A 304 8313 3614 3493 -672 -504 -81 S ATOM 894 CE AMET A 304 22.002 10.147 -8.250 0.51 37.22 C ANISOU 894 CE AMET A 304 7822 3118 3202 26 -202 -215 C ATOM 895 CE BMET A 304 23.530 10.880 -8.600 0.49 38.97 C ANISOU 895 CE BMET A 304 8150 3299 3360 -290 -361 -143 C ATOM 896 N TRP A 305 24.142 8.702 -13.320 1.00 22.71 N ANISOU 896 N TRP A 305 5276 1615 1736 -202 -622 119 N ATOM 897 CA TRP A 305 23.266 8.633 -14.480 1.00 21.87 C ANISOU 897 CA TRP A 305 5042 1526 1742 16 -596 151 C ATOM 898 C TRP A 305 21.845 8.323 -14.043 1.00 21.69 C ANISOU 898 C TRP A 305 4954 1474 1813 305 -490 103 C ATOM 899 O TRP A 305 21.618 7.369 -13.290 1.00 22.03 O ANISOU 899 O TRP A 305 4837 1625 1907 336 -451 79 O ATOM 900 CB TRP A 305 23.752 7.588 -15.480 1.00 21.38 C ANISOU 900 CB TRP A 305 4645 1708 1769 -33 -661 190 C ATOM 901 CG TRP A 305 22.852 7.479 -16.670 1.00 20.40 C ANISOU 901 CG TRP A 305 4399 1627 1726 168 -654 215 C ATOM 902 CD1 TRP A 305 22.785 8.336 -17.727 1.00 21.47 C ANISOU 902 CD1 TRP A 305 4645 1708 1803 169 -681 276 C ATOM 903 CD2 TRP A 305 21.889 6.450 -16.922 1.00 20.53 C ANISOU 903 CD2 TRP A 305 4139 1766 1894 374 -627 180 C ATOM 904 NE1 TRP A 305 21.833 7.911 -18.622 1.00 23.26 N ANISOU 904 NE1 TRP A 305 4698 2028 2113 375 -690 290 N ATOM 905 CE2 TRP A 305 21.270 6.753 -18.150 1.00 19.24 C ANISOU 905 CE2 TRP A 305 3944 1627 1739 499 -657 220 C ATOM 906 CE3 TRP A 305 21.487 5.308 -16.227 1.00 19.76 C ANISOU 906 CE3 TRP A 305 3828 1758 1924 444 -589 133 C ATOM 907 CZ2 TRP A 305 20.267 5.955 -18.699 1.00 24.20 C ANISOU 907 CZ2 TRP A 305 4319 2380 2497 688 -658 189 C ATOM 908 CZ3 TRP A 305 20.493 4.512 -16.775 1.00 20.55 C ANISOU 908 CZ3 TRP A 305 3682 1956 2169 621 -576 108 C ATOM 909 CH2 TRP A 305 19.901 4.834 -18.000 1.00 22.43 C ANISOU 909 CH2 TRP A 305 3879 2233 2412 737 -614 124 C ATOM 910 N ILE A 306 20.899 9.117 -14.541 1.00 23.71 N ANISOU 910 N ILE A 306 5250 1657 2103 492 -436 90 N ATOM 911 CA ILE A 306 19.488 9.006 -14.203 1.00 24.80 C ANISOU 911 CA ILE A 306 5282 1804 2336 757 -325 46 C ATOM 912 C ILE A 306 18.735 8.615 -15.467 1.00 26.90 C ANISOU 912 C ILE A 306 5288 2195 2736 908 -362 94 C ATOM 913 O ILE A 306 18.885 9.262 -16.511 1.00 27.20 O ANISOU 913 O ILE A 306 5378 2203 2753 891 -432 151 O ATOM 914 CB ILE A 306 18.950 10.329 -13.632 1.00 33.27 C ANISOU 914 CB ILE A 306 6595 2701 3347 848 -241 -6 C ATOM 915 CG1 ILE A 306 19.830 10.798 -12.473 1.00 35.59 C ANISOU 915 CG1 ILE A 306 7170 2880 3474 652 -227 -62 C ATOM 916 CG2 ILE A 306 17.526 10.161 -13.161 1.00 36.90 C ANISOU 916 CG2 ILE A 306 6911 3198 3911 1103 -113 -57 C ATOM 917 CD1 ILE A 306 19.797 9.880 -11.294 1.00 34.73 C ANISOU 917 CD1 ILE A 306 7029 2838 3328 629 -159 -114 C ATOM 918 N CYS A 307 17.922 7.568 -15.369 1.00 23.61 N ANISOU 918 N CYS A 307 4600 1921 2448 1035 -319 75 N ATOM 919 CA CYS A 307 17.290 6.969 -16.534 1.00 22.12 C ANISOU 919 CA CYS A 307 4135 1889 2382 1128 -372 104 C ATOM 920 C CYS A 307 16.144 7.839 -17.051 1.00 28.01 C ANISOU 920 C CYS A 307 4865 2600 3177 1305 -350 122 C ATOM 921 O CYS A 307 15.767 8.856 -16.457 1.00 28.02 O ANISOU 921 O CYS A 307 5045 2453 3146 1384 -282 102 O ATOM 922 CB CYS A 307 16.805 5.559 -16.198 1.00 21.16 C ANISOU 922 CB CYS A 307 3722 1923 2396 1161 -338 72 C ATOM 923 SG CYS A 307 15.229 5.529 -15.286 1.00 23.35 S ANISOU 923 SG CYS A 307 3875 2221 2776 1343 -181 30 S ATOM 924 N GLN A 308 15.572 7.417 -18.180 1.00 26.30 N ANISOU 924 N GLN A 308 4428 2523 3044 1369 -420 156 N ATOM 925 CA GLN A 308 14.500 8.177 -18.813 1.00 29.17 C ANISOU 925 CA GLN A 308 4754 2865 3466 1532 -437 199 C ATOM 926 C GLN A 308 13.221 8.196 -17.980 1.00 32.11 C ANISOU 926 C GLN A 308 4995 3240 3965 1690 -321 147 C ATOM 927 O GLN A 308 12.411 9.120 -18.130 1.00 33.36 O ANISOU 927 O GLN A 308 5190 3312 4174 1844 -314 170 O ATOM 928 CB GLN A 308 14.229 7.626 -20.214 1.00 27.47 C ANISOU 928 CB GLN A 308 4335 2821 3283 1539 -555 248 C ATOM 929 CG GLN A 308 13.730 6.185 -20.249 1.00 28.68 C ANISOU 929 CG GLN A 308 4165 3174 3559 1517 -543 184 C ATOM 930 CD GLN A 308 14.020 5.502 -21.576 1.00 28.88 C ANISOU 930 CD GLN A 308 4052 3367 3552 1451 -669 192 C ATOM 931 OE1 GLN A 308 15.181 5.291 -21.944 1.00 32.50 O ANISOU 931 OE1 GLN A 308 4597 3850 3904 1333 -729 187 O ATOM 932 NE2 GLN A 308 12.965 5.150 -22.301 1.00 34.77 N ANISOU 932 NE2 GLN A 308 4582 4244 4384 1518 -714 196 N ATOM 933 N ILE A 309 13.018 7.198 -17.113 1.00 31.95 N ANISOU 933 N ILE A 309 4822 3312 4005 1659 -232 84 N ATOM 934 CA ILE A 309 11.822 7.177 -16.276 1.00 28.42 C ANISOU 934 CA ILE A 309 4248 2884 3665 1797 -106 33 C ATOM 935 C ILE A 309 11.948 8.181 -15.140 1.00 31.54 C ANISOU 935 C ILE A 309 4915 3103 3967 1861 9 -22 C ATOM 936 O ILE A 309 10.983 8.874 -14.791 1.00 34.48 O ANISOU 936 O ILE A 309 5275 3420 4407 2031 90 -63 O ATOM 937 CB ILE A 309 11.560 5.753 -15.757 1.00 30.14 C ANISOU 937 CB ILE A 309 4223 3255 3973 1730 -47 0 C ATOM 938 CG1 ILE A 309 11.428 4.769 -16.916 1.00 29.84 C ANISOU 938 CG1 ILE A 309 3931 3369 4036 1649 -163 32 C ATOM 939 CG2 ILE A 309 10.326 5.718 -14.871 1.00 30.44 C ANISOU 939 CG2 ILE A 309 4126 3334 4108 1866 101 -55 C ATOM 940 CD1 ILE A 309 11.315 3.336 -16.483 1.00 28.89 C ANISOU 940 CD1 ILE A 309 3594 3360 4022 1551 -125 7 C ATOM 941 N CYS A 310 13.138 8.282 -14.550 1.00 32.23 N ANISOU 941 N CYS A 310 5250 3095 3900 1722 14 -36 N ATOM 942 CA CYS A 310 13.322 9.150 -13.395 1.00 32.05 C ANISOU 942 CA CYS A 310 5508 2907 3763 1746 124 -108 C ATOM 943 C CYS A 310 13.609 10.592 -13.784 1.00 35.48 C ANISOU 943 C CYS A 310 6205 3136 4142 1768 68 -94 C ATOM 944 O CYS A 310 13.294 11.502 -13.013 1.00 37.27 O ANISOU 944 O CYS A 310 6607 3213 4340 1857 163 -172 O ATOM 945 CB CYS A 310 14.480 8.644 -12.541 1.00 26.04 C ANISOU 945 CB CYS A 310 4922 2122 2852 1560 139 -127 C ATOM 946 SG CYS A 310 14.290 6.984 -11.905 1.00 25.62 S ANISOU 946 SG CYS A 310 4630 2251 2852 1535 209 -126 S ATOM 947 N ARG A 311 14.217 10.825 -14.943 1.00 35.52 N ANISOU 947 N ARG A 311 6248 3120 4128 1684 -77 -3 N ATOM 948 CA ARG A 311 14.660 12.170 -15.307 1.00 38.23 C ANISOU 948 CA ARG A 311 6873 3248 4405 1663 -137 31 C ATOM 949 C ARG A 311 13.482 13.071 -15.658 1.00 38.96 C ANISOU 949 C ARG A 311 6928 3243 4633 1902 -126 45 C ATOM 950 O ARG A 311 13.261 14.078 -14.994 1.00 47.75 O ANISOU 950 O ARG A 311 8236 4159 5746 1988 -58 -21 O ATOM 951 CB ARG A 311 15.662 12.120 -16.465 1.00 40.58 C ANISOU 951 CB ARG A 311 7220 3567 4631 1491 -284 136 C ATOM 952 CG ARG A 311 15.026 12.161 -17.846 1.00 44.62 C ANISOU 952 CG ARG A 311 7566 4153 5234 1601 -383 240 C ATOM 953 CD ARG A 311 16.034 11.809 -18.935 1.00 47.33 C ANISOU 953 CD ARG A 311 7917 4580 5485 1416 -506 329 C ATOM 954 NE ARG A 311 15.481 12.008 -20.273 1.00 54.65 N ANISOU 954 NE ARG A 311 8741 5568 6454 1508 -611 446 N ATOM 955 CZ ARG A 311 15.985 11.471 -21.380 1.00 51.99 C ANISOU 955 CZ ARG A 311 8319 5384 6051 1399 -711 521 C ATOM 956 NH1 ARG A 311 17.053 10.688 -21.312 1.00 49.55 N ANISOU 956 NH1 ARG A 311 7996 5173 5659 1206 -717 485 N ATOM 957 NH2 ARG A 311 15.417 11.708 -22.555 1.00 49.39 N ANISOU 957 NH2 ARG A 311 7912 5122 5734 1483 -812 636 N TER 958 ARG A 311 ATOM 959 N ALA B 1 28.748 6.213 -15.049 1.00 33.68 N ANISOU 959 N ALA B 1 4118 3565 5113 -1124 -1273 283 N ATOM 960 CA ALA B 1 27.559 5.409 -14.797 1.00 24.10 C ANISOU 960 CA ALA B 1 3076 2485 3598 -1048 -1193 132 C ATOM 961 C ALA B 1 27.935 4.032 -14.268 1.00 23.87 C ANISOU 961 C ALA B 1 2966 2525 3578 -971 -999 114 C ATOM 962 O ALA B 1 29.071 3.589 -14.423 1.00 28.98 O ANISOU 962 O ALA B 1 3422 3120 4470 -1016 -847 233 O ATOM 963 CB ALA B 1 26.727 5.281 -16.062 1.00 29.13 C ANISOU 963 CB ALA B 1 3853 3199 4016 -1198 -961 162 C ATOM 964 N ARG B 2 26.979 3.373 -13.626 1.00 20.61 N ANISOU 964 N ARG B 2 2681 2238 2911 -815 -974 -8 N ATOM 965 CA ARG B 2 27.167 2.000 -13.187 1.00 20.51 C ANISOU 965 CA ARG B 2 2623 2297 2872 -719 -750 -6 C ATOM 966 C ARG B 2 26.668 1.047 -14.262 1.00 21.16 C ANISOU 966 C ARG B 2 2801 2435 2805 -836 -377 8 C ATOM 967 O ARG B 2 25.684 1.320 -14.954 1.00 19.64 O ANISOU 967 O ARG B 2 2756 2293 2413 -930 -358 -24 O ATOM 968 CB ARG B 2 26.396 1.729 -11.892 1.00 23.77 C ANISOU 968 CB ARG B 2 3121 2821 3090 -493 -908 -103 C ATOM 969 CG ARG B 2 26.960 2.392 -10.641 1.00 23.72 C ANISOU 969 CG ARG B 2 3083 2758 3170 -327 -1280 -150 C ATOM 970 CD ARG B 2 26.125 2.009 -9.403 1.00 24.91 C ANISOU 970 CD ARG B 2 3358 3062 3042 -72 -1357 -231 C ATOM 971 NE ARG B 2 24.733 2.409 -9.582 1.00 22.89 N ANISOU 971 NE ARG B 2 3235 2922 2539 -22 -1299 -292 N ATOM 972 CZ ARG B 2 23.672 1.616 -9.468 1.00 19.39 C ANISOU 972 CZ ARG B 2 2841 2650 1878 41 -1118 -267 C ATOM 973 NH1 ARG B 2 23.808 0.340 -9.113 1.00 19.85 N ANISOU 973 NH1 ARG B 2 2843 2773 1927 68 -921 -181 N ATOM 974 NH2 ARG B 2 22.468 2.118 -9.694 1.00 19.17 N ANISOU 974 NH2 ARG B 2 2844 2710 1728 64 -1038 -275 N ATOM 975 N THR B 3 27.342 -0.093 -14.381 1.00 21.90 N ANISOU 975 N THR B 3 2823 2501 2999 -820 -108 51 N ATOM 976 CA THR B 3 26.904 -1.184 -15.241 1.00 20.60 C ANISOU 976 CA THR B 3 2798 2346 2683 -896 219 25 C ATOM 977 C THR B 3 26.866 -2.461 -14.422 1.00 18.37 C ANISOU 977 C THR B 3 2495 2069 2415 -757 307 15 C ATOM 978 O THR B 3 27.255 -2.487 -13.252 1.00 21.65 O ANISOU 978 O THR B 3 2783 2499 2943 -603 140 46 O ATOM 979 CB THR B 3 27.858 -1.407 -16.419 1.00 20.23 C ANISOU 979 CB THR B 3 2725 2215 2747 -998 534 89 C ATOM 980 OG1 THR B 3 29.152 -1.794 -15.925 1.00 24.69 O ANISOU 980 OG1 THR B 3 3049 2709 3622 -886 619 179 O ATOM 981 CG2 THR B 3 28.000 -0.148 -17.252 1.00 21.89 C ANISOU 981 CG2 THR B 3 2937 2420 2960 -1149 465 157 C ATOM 982 N LYS B 4 26.368 -3.538 -15.039 1.00 18.43 N ANISOU 982 N LYS B 4 2655 2047 2300 -817 544 -24 N ATOM 983 CA LYS B 4 26.467 -4.845 -14.400 1.00 20.07 C ANISOU 983 CA LYS B 4 2843 2207 2575 -705 656 -5 C ATOM 984 C LYS B 4 27.895 -5.118 -13.939 1.00 21.45 C ANISOU 984 C LYS B 4 2805 2296 3049 -571 727 73 C ATOM 985 O LYS B 4 28.120 -5.549 -12.804 1.00 21.70 O ANISOU 985 O LYS B 4 2727 2339 3178 -423 612 134 O ATOM 986 CB LYS B 4 26.008 -5.938 -15.373 1.00 28.41 C ANISOU 986 CB LYS B 4 4115 3161 3516 -814 904 -72 C ATOM 987 CG LYS B 4 24.772 -6.679 -14.963 1.00 29.82 C ANISOU 987 CG LYS B 4 4400 3372 3561 -847 823 -67 C ATOM 988 CD LYS B 4 24.275 -7.621 -16.052 1.00 29.04 C ANISOU 988 CD LYS B 4 4556 3129 3349 -1002 986 -153 C ATOM 989 CE LYS B 4 22.782 -7.400 -16.327 1.00 25.43 C ANISOU 989 CE LYS B 4 4215 2761 2687 -1173 800 -150 C ATOM 990 NZ LYS B 4 21.896 -8.490 -15.815 1.00 20.27 N ANISOU 990 NZ LYS B 4 3584 2064 2055 -1211 749 -78 N ATOM 991 N GLN B 5 28.871 -4.842 -14.804 1.00 23.77 N ANISOU 991 N GLN B 5 3021 2515 3495 -617 912 101 N ATOM 992 CA GLN B 5 30.274 -5.090 -14.478 1.00 29.12 C ANISOU 992 CA GLN B 5 3438 3111 4517 -495 1001 216 C ATOM 993 C GLN B 5 30.717 -4.310 -13.246 1.00 30.31 C ANISOU 993 C GLN B 5 3373 3308 4836 -416 621 299 C ATOM 994 O GLN B 5 31.332 -4.870 -12.332 1.00 30.37 O ANISOU 994 O GLN B 5 3225 3279 5035 -271 544 379 O ATOM 995 CB GLN B 5 31.146 -4.696 -15.666 1.00 33.29 C ANISOU 995 CB GLN B 5 3888 3593 5169 -568 1272 274 C ATOM 996 CG GLN B 5 31.621 -5.839 -16.512 1.00 44.58 C ANISOU 996 CG GLN B 5 5396 4913 6631 -496 1718 247 C ATOM 997 CD GLN B 5 32.432 -5.358 -17.695 1.00 57.07 C ANISOU 997 CD GLN B 5 6911 6493 8279 -545 2028 328 C ATOM 998 OE1 GLN B 5 32.096 -5.637 -18.845 1.00 61.92 O ANISOU 998 OE1 GLN B 5 7802 7092 8630 -602 2310 228 O ATOM 999 NE2 GLN B 5 33.504 -4.623 -17.420 1.00 62.10 N ANISOU 999 NE2 GLN B 5 7186 7147 9263 -529 1964 526 N ATOM 1000 N THR B 6 30.457 -3.002 -13.220 1.00 25.81 N ANISOU 1000 N THR B 6 2809 2796 4202 -505 356 281 N ATOM 1001 CA THR B 6 30.929 -2.197 -12.097 1.00 24.42 C ANISOU 1001 CA THR B 6 2480 2621 4176 -432 -48 327 C ATOM 1002 C THR B 6 30.204 -2.551 -10.808 1.00 27.23 C ANISOU 1002 C THR B 6 2951 3065 4328 -272 -270 265 C ATOM 1003 O THR B 6 30.804 -2.527 -9.727 1.00 24.70 O ANISOU 1003 O THR B 6 2519 2730 4133 -146 -527 319 O ATOM 1004 CB THR B 6 30.795 -0.701 -12.403 1.00 29.91 C ANISOU 1004 CB THR B 6 3194 3311 4862 -559 -298 308 C ATOM 1005 OG1 THR B 6 29.427 -0.293 -12.271 1.00 26.92 O ANISOU 1005 OG1 THR B 6 3065 3029 4136 -554 -425 168 O ATOM 1006 CG2 THR B 6 31.282 -0.407 -13.806 1.00 34.74 C ANISOU 1006 CG2 THR B 6 3737 3872 5589 -731 -16 399 C ATOM 1007 N ALA B 7 28.924 -2.897 -10.898 1.00 20.43 N ANISOU 1007 N ALA B 7 2306 2303 3154 -274 -180 176 N ATOM 1008 CA ALA B 7 28.183 -3.260 -9.699 1.00 22.09 C ANISOU 1008 CA ALA B 7 2607 2628 3158 -113 -329 163 C ATOM 1009 C ALA B 7 28.728 -4.544 -9.091 1.00 21.27 C ANISOU 1009 C ALA B 7 2416 2482 3184 2 -218 272 C ATOM 1010 O ALA B 7 28.754 -4.694 -7.865 1.00 23.77 O ANISOU 1010 O ALA B 7 2730 2866 3435 166 -421 321 O ATOM 1011 CB ALA B 7 26.694 -3.385 -10.029 1.00 22.25 C ANISOU 1011 CB ALA B 7 2812 2762 2878 -163 -227 102 C ATOM 1012 N ARG B 8 29.164 -5.488 -9.933 1.00 22.62 N ANISOU 1012 N ARG B 8 2540 2532 3522 -63 104 311 N ATOM 1013 CA ARG B 8 29.782 -6.706 -9.413 1.00 25.10 C ANISOU 1013 CA ARG B 8 2758 2760 4018 60 208 424 C ATOM 1014 C ARG B 8 31.028 -6.394 -8.603 1.00 24.67 C ANISOU 1014 C ARG B 8 2473 2667 4235 175 -29 533 C ATOM 1015 O ARG B 8 31.259 -6.994 -7.547 1.00 26.02 O ANISOU 1015 O ARG B 8 2599 2847 4439 323 -163 637 O ATOM 1016 CB ARG B 8 30.165 -7.635 -10.556 1.00 28.25 C ANISOU 1016 CB ARG B 8 3163 2996 4573 0 596 414 C ATOM 1017 CG ARG B 8 29.044 -8.490 -11.043 1.00 25.20 C ANISOU 1017 CG ARG B 8 3014 2585 3975 -79 781 345 C ATOM 1018 CD ARG B 8 29.555 -9.513 -12.030 1.00 30.40 C ANISOU 1018 CD ARG B 8 3728 3037 4787 -86 1133 308 C ATOM 1019 NE ARG B 8 28.483 -9.891 -12.934 1.00 26.59 N ANISOU 1019 NE ARG B 8 3524 2513 4066 -244 1262 183 N ATOM 1020 CZ ARG B 8 28.433 -9.543 -14.212 1.00 27.97 C ANISOU 1020 CZ ARG B 8 3844 2655 4130 -370 1431 60 C ATOM 1021 NH1 ARG B 8 29.419 -8.830 -14.745 1.00 34.44 N ANISOU 1021 NH1 ARG B 8 4531 3484 5072 -350 1541 71 N ATOM 1022 NH2 ARG B 8 27.406 -9.922 -14.958 1.00 31.60 N ANISOU 1022 NH2 ARG B 8 4578 3069 4362 -524 1476 -50 N ATOM 1023 N LYS B 9 31.873 -5.490 -9.105 1.00 25.47 N ANISOU 1023 N LYS B 9 2411 2713 4554 95 -96 542 N ATOM 1024 CA LYS B 9 33.073 -5.128 -8.359 1.00 28.41 C ANISOU 1024 CA LYS B 9 2531 3029 5235 168 -384 670 C ATOM 1025 C LYS B 9 32.727 -4.436 -7.047 1.00 32.53 C ANISOU 1025 C LYS B 9 3165 3646 5547 259 -857 626 C ATOM 1026 O LYS B 9 33.450 -4.589 -6.056 1.00 33.17 O ANISOU 1026 O LYS B 9 3132 3701 5772 374 -1135 732 O ATOM 1027 CB LYS B 9 33.966 -4.227 -9.207 1.00 36.55 C ANISOU 1027 CB LYS B 9 3343 3978 6564 29 -368 726 C ATOM 1028 CG LYS B 9 34.431 -4.845 -10.511 1.00 42.90 C ANISOU 1028 CG LYS B 9 4045 4707 7550 -20 134 779 C ATOM 1029 CD LYS B 9 35.582 -4.037 -11.098 1.00 54.72 C ANISOU 1029 CD LYS B 9 5225 6139 9428 -119 140 934 C ATOM 1030 CE LYS B 9 35.653 -4.169 -12.612 1.00 59.34 C ANISOU 1030 CE LYS B 9 5833 6711 10001 -202 644 934 C ATOM 1031 NZ LYS B 9 35.756 -5.586 -13.061 1.00 58.94 N ANISOU 1031 NZ LYS B 9 5840 6600 9956 -58 1094 912 N ATOM 1032 N SER B 10 31.628 -3.677 -7.021 1.00 27.21 N ANISOU 1032 N SER B 10 2732 3083 4525 230 -957 471 N ATOM 1033 CA SER B 10 31.245 -2.940 -5.821 1.00 28.53 C ANISOU 1033 CA SER B 10 3059 3340 4441 360 -1374 392 C ATOM 1034 C SER B 10 30.865 -3.877 -4.682 1.00 31.06 C ANISOU 1034 C SER B 10 3487 3776 4539 559 -1398 459 C ATOM 1035 O SER B 10 31.207 -3.619 -3.522 1.00 30.97 O ANISOU 1035 O SER B 10 3529 3795 4445 705 -1761 475 O ATOM 1036 CB SER B 10 30.085 -1.993 -6.129 1.00 30.83 C ANISOU 1036 CB SER B 10 3572 3721 4422 323 -1406 220 C ATOM 1037 OG SER B 10 30.461 -1.021 -7.088 1.00 35.00 O ANISOU 1037 OG SER B 10 4016 4134 5148 140 -1442 185 O ATOM 1038 N THR B 11 30.156 -4.963 -4.979 1.00 27.60 N ANISOU 1038 N THR B 11 3099 3393 3994 560 -1040 512 N ATOM 1039 CA THR B 11 29.773 -5.866 -3.897 1.00 30.50 C ANISOU 1039 CA THR B 11 3554 3869 4166 734 -1052 628 C ATOM 1040 C THR B 11 30.919 -6.755 -3.437 1.00 28.56 C ANISOU 1040 C THR B 11 3125 3505 4222 806 -1101 811 C ATOM 1041 O THR B 11 30.920 -7.202 -2.285 1.00 30.11 O ANISOU 1041 O THR B 11 3387 3783 4272 972 -1269 928 O ATOM 1042 CB THR B 11 28.615 -6.771 -4.319 1.00 27.57 C ANISOU 1042 CB THR B 11 3278 3566 3631 686 -693 666 C ATOM 1043 OG1 THR B 11 29.082 -7.723 -5.291 1.00 24.87 O ANISOU 1043 OG1 THR B 11 2816 3041 3594 565 -393 719 O ATOM 1044 CG2 THR B 11 27.464 -5.954 -4.875 1.00 24.17 C ANISOU 1044 CG2 THR B 11 2982 3247 2954 604 -636 519 C ATOM 1045 N GLY B 12 31.883 -7.040 -4.308 1.00 21.26 N ANISOU 1045 N GLY B 12 2457 3497 2123 738 597 468 N ATOM 1046 CA GLY B 12 32.879 -8.044 -4.016 1.00 23.33 C ANISOU 1046 CA GLY B 12 2695 3695 2475 691 634 343 C ATOM 1047 C GLY B 12 32.418 -9.474 -4.200 1.00 20.39 C ANISOU 1047 C GLY B 12 2200 3393 2156 779 632 249 C ATOM 1048 O GLY B 12 33.188 -10.395 -3.926 1.00 25.69 O ANISOU 1048 O GLY B 12 2837 3979 2944 781 649 134 O ATOM 1049 N GLY B 13 31.185 -9.694 -4.655 1.00 23.15 N ANISOU 1049 N GLY B 13 2505 3790 2499 785 496 264 N ATOM 1050 CA GLY B 13 30.725 -11.043 -4.943 1.00 25.78 C ANISOU 1050 CA GLY B 13 2792 4034 2971 735 320 124 C ATOM 1051 C GLY B 13 30.151 -11.747 -3.728 1.00 19.08 C ANISOU 1051 C GLY B 13 1803 3049 2396 660 257 232 C ATOM 1052 O GLY B 13 30.473 -11.390 -2.594 1.00 20.74 O ANISOU 1052 O GLY B 13 1968 3227 2685 663 378 369 O HETATM 1053 N KCR B 14 29.293 -12.735 -3.969 1.00 21.34 N ANISOU 1053 N KCR B 14 2028 3262 2816 577 60 177 N HETATM 1054 CA KCR B 14 28.675 -13.457 -2.910 1.00 19.03 C ANISOU 1054 CA KCR B 14 1601 2852 2776 472 -9 302 C HETATM 1055 CB KCR B 14 27.677 -14.466 -3.457 1.00 21.34 C ANISOU 1055 CB KCR B 14 1838 3076 3193 352 -254 230 C HETATM 1056 CG KCR B 14 26.519 -13.866 -4.227 1.00 22.93 C ANISOU 1056 CG KCR B 14 1979 3455 3278 341 -364 271 C HETATM 1057 CD KCR B 14 25.463 -14.905 -4.572 1.00 24.91 C ANISOU 1057 CD KCR B 14 2134 3636 3693 180 -628 228 C HETATM 1058 CE KCR B 14 24.354 -14.366 -5.452 1.00 26.96 C ANISOU 1058 CE KCR B 14 2324 4086 3833 175 -775 249 C HETATM 1059 NZ KCR B 14 23.437 -13.596 -4.683 1.00 25.82 N ANISOU 1059 NZ KCR B 14 1973 4089 3747 181 -706 502 N HETATM 1060 CH KCR B 14 23.103 -12.280 -5.098 1.00 27.78 C ANISOU 1060 CH KCR B 14 2221 4539 3796 328 -648 585 C HETATM 1061 OH KCR B 14 23.614 -11.816 -6.100 1.00 30.02 O ANISOU 1061 OH KCR B 14 2686 4872 3848 423 -656 465 O HETATM 1062 CX KCR B 14 22.127 -11.465 -4.273 1.00 25.19 C ANISOU 1062 CX KCR B 14 1670 4361 3541 377 -569 825 C HETATM 1063 CY KCR B 14 21.741 -10.207 -4.588 1.00 25.12 C ANISOU 1063 CY KCR B 14 1657 4511 3377 542 -529 913 C HETATM 1064 CH3 KCR B 14 20.741 -9.473 -3.708 1.00 25.39 C ANISOU 1064 CH3 KCR B 14 1594 4573 3481 571 -407 1040 C HETATM 1065 C KCR B 14 29.710 -14.205 -2.070 1.00 18.44 C ANISOU 1065 C KCR B 14 1549 2601 2855 469 51 277 C HETATM 1066 O KCR B 14 30.849 -14.543 -2.522 1.00 18.61 O ANISOU 1066 O KCR B 14 1675 2561 2837 547 89 94 O ATOM 1067 N ALA B 15 29.336 -14.485 -0.823 1.00 18.02 N ANISOU 1067 N ALA B 15 1390 2480 2978 386 61 466 N ATOM 1068 CA ALA B 15 30.099 -15.390 0.036 1.00 18.05 C ANISOU 1068 CA ALA B 15 1405 2291 3162 359 56 479 C ATOM 1069 C ALA B 15 30.181 -16.791 -0.595 1.00 20.25 C ANISOU 1069 C ALA B 15 1741 2353 3601 312 -146 292 C ATOM 1070 O ALA B 15 29.385 -17.111 -1.474 1.00 21.82 O ANISOU 1070 O ALA B 15 1941 2556 3796 251 -298 195 O ATOM 1071 CB ALA B 15 29.452 -15.445 1.406 1.00 18.94 C ANISOU 1071 CB ALA B 15 1398 2401 3399 253 85 741 C ATOM 1072 N PRO B 16 31.131 -17.620 -0.154 1.00 20.66 N ANISOU 1072 N PRO B 16 1846 2206 3798 347 -168 234 N ATOM 1073 CA PRO B 16 31.332 -18.924 -0.803 1.00 23.07 C ANISOU 1073 CA PRO B 16 2238 2269 4258 344 -361 16 C ATOM 1074 C PRO B 16 30.065 -19.767 -0.791 1.00 25.94 C ANISOU 1074 C PRO B 16 2555 2496 4805 143 -582 87 C ATOM 1075 O PRO B 16 29.280 -19.739 0.159 1.00 24.89 O ANISOU 1075 O PRO B 16 2302 2381 4772 -6 -584 354 O ATOM 1076 CB PRO B 16 32.442 -19.568 0.035 1.00 23.13 C ANISOU 1076 CB PRO B 16 2275 2083 4429 417 -344 32 C ATOM 1077 CG PRO B 16 33.231 -18.400 0.538 1.00 20.65 C ANISOU 1077 CG PRO B 16 1924 1980 3944 518 -111 126 C ATOM 1078 CD PRO B 16 32.185 -17.346 0.840 1.00 19.19 C ANISOU 1078 CD PRO B 16 1658 2009 3624 423 -25 330 C ATOM 1079 N ARG B 17 29.898 -20.546 -1.867 1.00 29.58 N ANISOU 1079 N ARG B 17 3112 2824 5302 134 -770 -164 N ATOM 1080 CA ARG B 17 28.627 -21.209 -2.150 1.00 35.30 C ANISOU 1080 CA ARG B 17 3794 3456 6163 -75 -1006 -138 C ATOM 1081 C ARG B 17 28.178 -22.114 -1.006 1.00 31.22 C ANISOU 1081 C ARG B 17 3207 2709 5946 -273 -1118 100 C ATOM 1082 O ARG B 17 26.989 -22.155 -0.668 1.00 31.69 O ANISOU 1082 O ARG B 17 3122 2828 6093 -485 -1196 305 O ATOM 1083 CB ARG B 17 28.760 -22.014 -3.442 1.00 44.84 C ANISOU 1083 CB ARG B 17 5164 4509 7364 -36 -1205 -493 C ATOM 1084 CG ARG B 17 29.992 -22.904 -3.452 1.00 50.30 C ANISOU 1084 CG ARG B 17 6010 4927 8176 119 -1227 -707 C ATOM 1085 CD ARG B 17 30.096 -23.753 -4.701 1.00 56.30 C ANISOU 1085 CD ARG B 17 6947 5518 8926 176 -1425 -1090 C ATOM 1086 NE ARG B 17 31.032 -24.853 -4.499 1.00 62.17 N ANISOU 1086 NE ARG B 17 7819 5917 9887 297 -1504 -1260 N ATOM 1087 CZ ARG B 17 31.497 -25.633 -5.468 1.00 70.14 C ANISOU 1087 CZ ARG B 17 9008 6748 10893 433 -1630 -1644 C ATOM 1088 NH1 ARG B 17 31.121 -25.432 -6.725 1.00 72.80 N ANISOU 1088 NH1 ARG B 17 9430 7239 10993 448 -1689 -1898 N ATOM 1089 NH2 ARG B 17 32.345 -26.611 -5.181 1.00 73.98 N ANISOU 1089 NH2 ARG B 17 9598 6904 11606 571 -1702 -1781 N ATOM 1090 N LYS B 18 29.107 -22.857 -0.405 1.00 31.29 N ANISOU 1090 N LYS B 18 3309 2463 6118 -212 -1133 91 N ATOM 1091 CA LYS B 18 28.730 -23.789 0.651 1.00 32.87 C ANISOU 1091 CA LYS B 18 3476 2416 6598 -410 -1260 335 C ATOM 1092 C LYS B 18 28.362 -23.076 1.941 1.00 30.97 C ANISOU 1092 C LYS B 18 3072 2384 6311 -498 -1075 704 C ATOM 1093 O LYS B 18 27.768 -23.694 2.831 1.00 32.43 O ANISOU 1093 O LYS B 18 3190 2451 6680 -711 -1155 965 O ATOM 1094 CB LYS B 18 29.859 -24.787 0.905 1.00 34.21 C ANISOU 1094 CB LYS B 18 3805 2236 6956 -291 -1351 224 C ATOM 1095 CG LYS B 18 30.085 -25.743 -0.247 1.00 37.06 C ANISOU 1095 CG LYS B 18 4341 2323 7417 -224 -1572 -141 C ATOM 1096 CD LYS B 18 31.122 -26.795 0.093 1.00 49.04 C ANISOU 1096 CD LYS B 18 6006 3463 9165 -90 -1682 -235 C ATOM 1097 CE LYS B 18 31.216 -27.835 -1.010 1.00 58.60 C ANISOU 1097 CE LYS B 18 7390 4458 10418 -24 -1886 -594 C ATOM 1098 NZ LYS B 18 31.485 -27.201 -2.329 1.00 61.73 N ANISOU 1098 NZ LYS B 18 7843 5010 10601 157 -1822 -963 N ATOM 1099 N GLN B 19 28.704 -21.799 2.061 1.00 28.08 N ANISOU 1099 N GLN B 19 2651 2321 5696 -345 -831 729 N ATOM 1100 CA GLN B 19 28.308 -21.010 3.216 1.00 27.63 C ANISOU 1100 CA GLN B 19 2455 2487 5557 -403 -646 1034 C ATOM 1101 C GLN B 19 26.995 -20.262 2.997 1.00 26.35 C ANISOU 1101 C GLN B 19 2120 2599 5293 -500 -600 1136 C ATOM 1102 O GLN B 19 26.395 -19.805 3.973 1.00 34.32 O ANISOU 1102 O GLN B 19 2987 3780 6272 -579 -472 1396 O ATOM 1103 CB GLN B 19 29.440 -20.044 3.603 1.00 24.72 C ANISOU 1103 CB GLN B 19 2135 2261 4997 -189 -425 1012 C ATOM 1104 CG GLN B 19 30.762 -20.746 3.964 1.00 24.10 C ANISOU 1104 CG GLN B 19 2179 1945 5032 -81 -468 943 C ATOM 1105 CD GLN B 19 31.919 -19.782 4.146 1.00 25.74 C ANISOU 1105 CD GLN B 19 2414 2311 5054 118 -272 883 C ATOM 1106 OE1 GLN B 19 31.783 -18.738 4.785 1.00 24.73 O ANISOU 1106 OE1 GLN B 19 2225 2408 4763 122 -101 1034 O ATOM 1107 NE2 GLN B 19 33.066 -20.119 3.562 1.00 24.30 N ANISOU 1107 NE2 GLN B 19 2320 2014 4900 285 -299 651 N ATOM 1108 N LEU B 20 26.535 -20.146 1.750 1.00 27.04 N ANISOU 1108 N LEU B 20 2212 2740 5320 -485 -705 936 N ATOM 1109 CA LEU B 20 25.295 -19.441 1.442 1.00 27.58 C ANISOU 1109 CA LEU B 20 2104 3071 5304 -551 -693 1023 C ATOM 1110 C LEU B 20 24.080 -20.233 1.920 1.00 36.53 C ANISOU 1110 C LEU B 20 3058 4161 6658 -832 -836 1232 C ATOM 1111 O LEU B 20 24.119 -21.457 2.101 1.00 32.14 O ANISOU 1111 O LEU B 20 2561 3322 6331 -1000 -1014 1250 O ATOM 1112 CB LEU B 20 25.161 -19.209 -0.068 1.00 27.77 C ANISOU 1112 CB LEU B 20 2199 3152 5200 -471 -809 755 C ATOM 1113 CG LEU B 20 26.203 -18.341 -0.799 1.00 27.43 C ANISOU 1113 CG LEU B 20 2314 3205 4902 -220 -671 549 C ATOM 1114 CD1 LEU B 20 25.962 -18.383 -2.307 1.00 27.92 C ANISOU 1114 CD1 LEU B 20 2460 3305 4844 -188 -829 297 C ATOM 1115 CD2 LEU B 20 26.206 -16.890 -0.300 1.00 24.87 C ANISOU 1115 CD2 LEU B 20 1920 3147 4383 -94 -426 702 C ATOM 1116 N ALA B 21 22.979 -19.511 2.106 1.00 34.32 N ANISOU 1116 N ALA B 21 2593 4165 6282 -860 -748 1378 N ATOM 1117 CA ALA B 21 21.736 -20.137 2.523 1.00 39.40 C ANISOU 1117 CA ALA B 21 3148 4832 6989 -1044 -816 1522 C ATOM 1118 C ALA B 21 21.173 -20.998 1.398 1.00 45.84 C ANISOU 1118 C ALA B 21 3937 5505 7975 -1222 -1120 1380 C ATOM 1119 O ALA B 21 21.330 -20.694 0.212 1.00 38.02 O ANISOU 1119 O ALA B 21 2952 4538 6956 -1165 -1255 1171 O ATOM 1120 CB ALA B 21 20.714 -19.069 2.908 1.00 43.44 C ANISOU 1120 CB ALA B 21 3531 5675 7299 -954 -631 1627 C ATOM 1121 N THR B 22 20.508 -22.084 1.782 1.00 48.53 N ANISOU 1121 N THR B 22 4268 5706 8467 -1431 -1242 1484 N ATOM 1122 CA THR B 22 19.956 -23.020 0.810 1.00 54.53 C ANISOU 1122 CA THR B 22 5044 6294 9383 -1615 -1543 1343 C ATOM 1123 C THR B 22 18.655 -22.496 0.209 1.00 59.89 C ANISOU 1123 C THR B 22 5522 7253 9979 -1664 -1583 1349 C ATOM 1124 O THR B 22 18.047 -21.564 0.736 1.00 59.96 O ANISOU 1124 O THR B 22 5374 7563 9843 -1572 -1369 1495 O ATOM 1125 CB THR B 22 19.706 -24.403 1.441 1.00 62.20 C ANISOU 1125 CB THR B 22 6084 7004 10546 -1823 -1665 1463 C ATOM 1126 OG1 THR B 22 18.808 -24.271 2.549 1.00 69.86 O ANISOU 1126 OG1 THR B 22 6891 8191 11461 -1899 -1494 1743 O ATOM 1127 CG2 THR B 22 21.013 -25.017 1.922 1.00 56.32 C ANISOU 1127 CG2 THR B 22 5557 5950 9892 -1750 -1671 1431 C TER 1128 THR B 22 HETATM 1129 ZN ZN A 401 15.521 5.467 -12.972 1.00 21.21 ZN HETATM 1130 ZN ZN A 402 17.286 -3.163 -24.036 1.00 18.51 ZN HETATM 1131 ZN ZN A 403 25.258 -8.103 4.364 1.00 12.76 ZN HETATM 1132 ZN ZN A 404 18.130 -12.207 -8.884 1.00 11.53 ZN HETATM 1133 O HOH A 501 24.919 -0.605 -27.343 1.00 52.78 O HETATM 1134 O HOH A 502 24.725 2.137 -28.307 1.00 47.53 O HETATM 1135 O HOH A 503 14.901 8.405 -28.610 1.00 30.23 O HETATM 1136 O HOH A 504 14.104 -0.916 -26.597 1.00 38.43 O HETATM 1137 O HOH A 505 15.635 4.238 -27.668 1.00 44.22 O HETATM 1138 O HOH A 506 10.539 2.687 0.104 1.00 40.03 O HETATM 1139 O HOH A 507 5.995 -1.896 -18.846 1.00 42.89 O HETATM 1140 O HOH A 508 0.512 -6.946 -7.308 1.00 23.92 O HETATM 1141 O HOH A 509 16.823 5.356 -19.977 1.00 25.22 O HETATM 1142 O HOH A 510 11.481 -3.210 -15.479 1.00 30.97 O HETATM 1143 O HOH A 511 13.707 3.675 -24.525 1.00 35.43 O HETATM 1144 O HOH A 512 18.182 -7.671 16.872 1.00 56.43 O HETATM 1145 O HOH A 513 24.497 -0.971 -22.551 1.00 26.20 O HETATM 1146 O HOH A 514 19.151 -11.627 -27.043 1.00 26.51 O HETATM 1147 O HOH A 515 10.494 -21.086 3.553 1.00 28.54 O HETATM 1148 O HOH A 516 16.352 -4.886 10.858 1.00 25.68 O HETATM 1149 O HOH A 517 12.415 -17.850 2.763 1.00 21.27 O HETATM 1150 O HOH A 518 13.125 -18.305 -3.201 1.00 43.76 O HETATM 1151 O HOH A 519 27.960 3.356 -3.439 1.00 48.77 O HETATM 1152 O HOH A 520 19.007 -13.077 13.212 1.00 48.87 O HETATM 1153 O HOH A 521 15.318 -2.902 -15.378 1.00 14.04 O HETATM 1154 O HOH A 522 7.887 -2.015 -9.918 1.00 25.60 O HETATM 1155 O HOH A 523 12.516 -5.760 -17.830 1.00 27.52 O HETATM 1156 O HOH A 524 21.763 8.235 -4.398 1.00 48.70 O HETATM 1157 O HOH A 525 24.620 4.723 -13.358 1.00 21.90 O HETATM 1158 O HOH A 526 26.508 -11.130 -9.226 1.00 26.82 O HETATM 1159 O HOH A 527 26.919 -4.405 5.891 1.00 18.15 O HETATM 1160 O HOH A 528 26.547 9.193 -30.850 1.00 23.88 O HETATM 1161 O HOH A 529 20.492 -7.437 16.357 1.00 44.01 O HETATM 1162 O HOH A 530 15.156 -12.551 -24.857 1.00 40.22 O HETATM 1163 O HOH A 531 10.869 5.376 -11.233 1.00 36.50 O HETATM 1164 O HOH A 532 28.314 0.298 2.606 1.00 39.46 O HETATM 1165 O HOH A 533 34.514 5.033 -32.441 1.00 40.94 O HETATM 1166 O HOH A 534 11.408 2.148 -24.550 1.00 37.82 O HETATM 1167 O HOH A 535 23.344 -16.685 1.996 1.00 21.02 O HETATM 1168 O HOH A 536 25.728 10.608 -16.520 1.00 23.54 O HETATM 1169 O HOH A 537 22.457 -2.974 -8.777 1.00 21.69 O HETATM 1170 O HOH A 538 18.485 9.468 -19.358 1.00 36.90 O HETATM 1171 O HOH A 539 30.868 5.825 -16.862 1.00 41.97 O HETATM 1172 O HOH A 540 27.021 -12.975 -15.343 1.00 37.97 O HETATM 1173 O HOH A 541 12.517 -6.705 -5.301 1.00 13.95 O HETATM 1174 O HOH A 542 5.917 -1.259 -7.270 1.00 42.77 O HETATM 1175 O HOH A 543 4.436 -8.712 -16.841 1.00 47.31 O HETATM 1176 O HOH A 544 12.870 11.212 -20.367 1.00 55.71 O HETATM 1177 O HOH A 545 8.289 -1.155 0.429 1.00 25.84 O HETATM 1178 O HOH A 546 31.241 -11.866 0.242 1.00 17.15 O HETATM 1179 O HOH A 547 13.374 -7.530 3.702 1.00 20.26 O HETATM 1180 O HOH A 548 22.512 6.137 -6.200 1.00 34.45 O HETATM 1181 O HOH A 549 15.329 -18.720 -4.379 1.00 48.05 O HETATM 1182 O HOH A 550 22.245 -7.191 -25.176 1.00 42.04 O HETATM 1183 O HOH A 551 10.770 -14.630 -12.180 1.00 39.30 O HETATM 1184 O HOH A 552 27.049 9.196 -23.451 1.00 18.50 O HETATM 1185 O HOH A 553 13.223 -9.745 2.174 1.00 18.03 O HETATM 1186 O HOH A 554 19.970 -14.522 0.036 1.00 15.03 O HETATM 1187 O HOH A 555 16.653 -11.747 7.976 1.00 18.38 O HETATM 1188 O HOH A 556 25.599 -3.242 -6.032 1.00 19.61 O HETATM 1189 O HOH A 557 25.620 1.849 1.440 1.00 32.83 O HETATM 1190 O HOH A 558 19.573 8.643 -23.148 1.00 22.98 O HETATM 1191 O HOH A 559 15.098 -11.660 -14.752 1.00 23.89 O HETATM 1192 O HOH A 560 11.737 -11.581 -3.752 1.00 18.25 O HETATM 1193 O HOH A 561 19.590 0.110 4.867 1.00 20.73 O HETATM 1194 O HOH A 562 14.571 -3.928 -13.004 1.00 15.89 O HETATM 1195 O HOH A 563 18.965 -7.526 -26.659 1.00 57.78 O HETATM 1196 O HOH A 564 -0.642 -11.626 -11.635 1.00 32.83 O HETATM 1197 O HOH A 565 17.028 7.407 -5.477 1.00 32.92 O HETATM 1198 O HOH A 566 31.251 -7.888 11.220 1.00 58.15 O HETATM 1199 O HOH A 567 8.869 -20.481 -2.830 1.00 33.27 O HETATM 1200 O HOH A 568 14.599 8.103 -2.220 1.00 26.93 O HETATM 1201 O HOH A 569 32.459 7.009 -21.534 1.00 39.43 O HETATM 1202 O HOH A 570 11.189 -6.321 -12.319 1.00 19.01 O HETATM 1203 O HOH A 571 7.518 -13.865 -12.075 1.00 37.89 O HETATM 1204 O HOH A 572 14.691 -7.897 6.087 1.00 16.27 O HETATM 1205 O HOH A 573 7.928 3.681 -11.142 1.00 35.70 O HETATM 1206 O HOH A 574 21.176 9.557 -29.873 1.00 35.71 O HETATM 1207 O HOH A 575 17.422 -1.556 4.702 1.00 18.28 O HETATM 1208 O HOH A 576 -4.718 -6.343 -10.288 1.00 54.15 O HETATM 1209 O HOH A 577 14.491 -1.308 -9.608 1.00 18.04 O HETATM 1210 O HOH A 578 12.569 -1.639 5.079 1.00 36.35 O HETATM 1211 O HOH A 579 21.707 -10.148 -27.706 1.00 30.04 O HETATM 1212 O HOH A 580 29.451 10.005 -22.502 1.00 21.04 O HETATM 1213 O HOH A 581 18.872 2.180 -30.900 1.00 38.60 O HETATM 1214 O HOH A 582 17.142 -19.712 -3.034 1.00 37.72 O HETATM 1215 O HOH A 583 15.849 -3.461 -10.601 1.00 13.46 O HETATM 1216 O HOH A 584 11.868 -10.921 -14.832 1.00 30.53 O HETATM 1217 O HOH A 585 12.134 -6.467 11.150 1.00 45.52 O HETATM 1218 O HOH A 586 26.558 5.077 -32.713 1.00 54.92 O HETATM 1219 O HOH A 587 22.891 1.030 5.651 1.00 41.55 O HETATM 1220 O HOH A 588 27.230 6.116 -10.685 1.00 29.87 O HETATM 1221 O HOH A 589 10.140 -18.592 -4.781 1.00 23.89 O HETATM 1222 O HOH A 590 16.814 -1.215 8.197 1.00 22.04 O HETATM 1223 O HOH A 591 22.003 2.674 2.535 1.00 29.19 O HETATM 1224 O HOH A 592 15.101 2.187 3.472 1.00 27.26 O HETATM 1225 O HOH A 593 12.198 -4.415 -3.599 1.00 15.81 O HETATM 1226 O HOH A 594 21.081 -0.092 9.431 1.00 39.09 O HETATM 1227 O HOH A 595 23.489 9.631 -0.324 1.00 47.72 O HETATM 1228 O HOH A 596 -2.431 -4.329 -8.368 1.00 55.63 O HETATM 1229 O HOH A 597 13.021 -4.699 1.329 1.00 23.84 O HETATM 1230 O HOH A 598 23.696 4.157 -4.625 1.00 26.34 O HETATM 1231 O HOH A 599 5.350 -7.289 -8.762 1.00 21.46 O HETATM 1232 O HOH A 600 30.033 -3.554 3.038 1.00 31.15 O HETATM 1233 O HOH A 601 2.913 -5.900 -8.184 1.00 24.58 O HETATM 1234 O HOH A 602 12.985 -9.549 -24.426 1.00 52.87 O HETATM 1235 O HOH A 603 22.660 -7.486 -6.904 1.00 15.96 O HETATM 1236 O HOH A 604 12.510 -2.559 -11.376 1.00 21.67 O HETATM 1237 O HOH A 605 11.429 -7.981 8.062 1.00 32.27 O HETATM 1238 O HOH A 606 31.866 7.624 -14.398 1.00 37.60 O HETATM 1239 O HOH A 607 17.288 3.932 3.156 1.00 27.44 O HETATM 1240 O HOH A 608 27.554 -9.380 -21.690 1.00 42.80 O HETATM 1241 O HOH A 609 25.100 8.972 -27.868 1.00 27.40 O HETATM 1242 O HOH A 610 26.656 0.576 -5.647 1.00 40.38 O HETATM 1243 O HOH A 611 21.889 9.995 -20.737 1.00 43.59 O HETATM 1244 O HOH A 612 12.399 -5.654 -14.736 1.00 26.83 O HETATM 1245 O HOH A 613 23.340 6.238 -30.394 1.00 42.67 O HETATM 1246 O HOH A 614 22.315 -13.342 -16.133 1.00 30.43 O HETATM 1247 O HOH A 615 19.666 8.625 -5.817 1.00 42.89 O HETATM 1248 O HOH A 616 24.739 -0.008 10.185 1.00 41.11 O HETATM 1249 O HOH A 617 12.125 -11.159 7.914 1.00 38.83 O HETATM 1250 O HOH A 618 31.755 3.855 -23.803 1.00 35.51 O HETATM 1251 O HOH A 619 10.512 -15.757 -10.180 1.00 53.61 O HETATM 1252 O HOH A 620 25.588 -12.420 -22.339 1.00 37.16 O HETATM 1253 O HOH A 621 11.912 -4.364 5.421 1.00 46.85 O HETATM 1254 O HOH A 622 16.189 -8.549 -27.821 1.00 52.93 O HETATM 1255 O HOH A 623 14.849 12.286 -26.773 1.00 47.79 O HETATM 1256 O HOH A 624 33.569 0.188 -1.167 1.00 59.65 O HETATM 1257 O HOH A 625 21.222 -13.051 13.583 1.00 46.68 O HETATM 1258 O HOH A 626 25.717 -10.262 -17.821 1.00 42.64 O HETATM 1259 O HOH A 627 13.467 -2.589 11.303 1.00 52.16 O HETATM 1260 O HOH A 628 25.187 -2.374 -24.619 1.00 61.35 O HETATM 1261 O HOH A 629 15.596 -5.393 13.366 1.00 43.15 O HETATM 1262 O HOH A 630 14.405 8.344 -6.069 1.00 46.31 O HETATM 1263 O HOH A 631 17.837 7.535 -21.235 1.00 28.73 O HETATM 1264 O HOH A 632 8.162 7.868 -7.591 1.00 53.67 O HETATM 1265 O HOH A 633 14.250 1.597 -27.270 1.00 40.60 O HETATM 1266 O HOH A 634 13.164 -5.648 -1.261 1.00 20.75 O HETATM 1267 O HOH A 635 20.319 12.102 -17.327 1.00 43.66 O HETATM 1268 O HOH A 636 11.452 -8.963 -17.650 1.00 46.81 O HETATM 1269 O HOH A 637 22.995 -17.915 -4.093 1.00 46.13 O HETATM 1270 O HOH A 638 14.593 -0.025 6.987 1.00 36.02 O HETATM 1271 O HOH A 639 17.587 -16.212 8.612 1.00 40.80 O HETATM 1272 O HOH A 640 26.267 4.954 -3.192 1.00 52.49 O HETATM 1273 O HOH A 641 21.195 0.576 12.525 1.00 49.03 O HETATM 1274 O HOH A 642 5.714 -3.481 -9.198 1.00 47.23 O HETATM 1275 O HOH A 643 32.155 -7.783 8.918 1.00 34.60 O HETATM 1276 O HOH A 644 8.897 7.890 -5.364 1.00 59.09 O HETATM 1277 O HOH A 645 16.962 8.352 2.188 1.00 32.29 O HETATM 1278 O HOH A 646 27.293 9.428 -26.222 1.00 18.56 O HETATM 1279 O HOH A 647 11.996 -7.904 -1.045 1.00 22.22 O HETATM 1280 O HOH A 648 33.541 -0.781 -3.815 1.00 68.56 O HETATM 1281 O HOH A 649 10.069 5.920 -3.579 1.00 49.05 O HETATM 1282 O HOH A 650 10.881 -8.102 -15.451 1.00 31.84 O HETATM 1283 O HOH A 651 6.368 4.814 -4.245 1.00 49.55 O HETATM 1284 O HOH A 652 23.188 -12.314 -19.787 1.00 36.88 O HETATM 1285 O HOH A 653 18.810 -20.038 -5.169 1.00 47.89 O HETATM 1286 O HOH A 654 16.415 -2.436 11.005 1.00 35.63 O HETATM 1287 O HOH A 655 19.699 2.651 3.752 1.00 27.86 O HETATM 1288 O HOH A 656 22.647 3.124 -30.269 1.00 44.94 O HETATM 1289 O HOH A 657 10.503 -9.266 -2.940 1.00 20.93 O HETATM 1290 O HOH A 658 29.067 -2.552 5.641 1.00 29.34 O HETATM 1291 O HOH A 659 9.045 5.171 -1.344 1.00 52.47 O HETATM 1292 O HOH A 660 13.754 -11.693 4.109 1.00 21.73 O HETATM 1293 O HOH A 661 28.475 2.324 0.244 1.00 51.91 O HETATM 1294 O HOH A 662 16.535 6.238 4.413 1.00 30.69 O HETATM 1295 O HOH A 663 15.621 -13.258 9.859 1.00 32.65 O HETATM 1296 O HOH A 664 14.361 -19.661 3.133 1.00 43.60 O HETATM 1297 O HOH A 665 13.231 -20.916 -1.736 1.00 54.35 O HETATM 1298 O HOH A 666 17.542 -5.566 -27.207 1.00 35.19 O HETATM 1299 O HOH A 667 31.273 0.163 2.317 1.00 43.11 O HETATM 1300 O HOH A 668 15.540 10.549 -30.267 1.00 55.88 O HETATM 1301 O HOH A 669 12.035 7.751 -2.724 1.00 43.55 O HETATM 1302 O HOH A 670 33.377 -5.549 7.456 1.00 36.81 O HETATM 1303 O HOH A 671 28.225 4.925 -8.436 1.00 45.23 O HETATM 1304 O HOH A 672 31.328 -2.553 7.029 1.00 41.27 O HETATM 1305 O HOH A 673 25.550 2.291 3.795 1.00 56.44 O HETATM 1306 O HOH A 674 18.743 0.517 7.529 1.00 32.77 O HETATM 1307 O HOH A 675 11.130 -4.287 2.750 1.00 51.59 O HETATM 1308 O HOH A 676 14.543 -10.720 6.483 1.00 18.71 O HETATM 1309 O HOH A 677 14.925 9.128 0.488 1.00 33.29 O HETATM 1310 O HOH A 678 23.202 -4.711 -6.623 1.00 20.86 O HETATM 1311 O HOH A 679 12.702 -14.018 8.751 1.00 39.10 O HETATM 1312 O HOH A 680 15.516 -3.142 14.558 1.00 49.92 O HETATM 1313 O HOH A 681 5.092 1.668 -20.819 1.00 52.47 O HETATM 1314 O HOH A 682 16.543 -18.959 7.456 1.00 47.52 O HETATM 1315 O HOH A 683 20.330 4.072 6.001 1.00 40.76 O HETATM 1316 O HOH A 684 13.835 6.546 4.968 1.00 46.36 O HETATM 1317 O HOH A 685 17.759 3.013 7.585 1.00 45.36 O HETATM 1318 O HOH A 686 10.122 8.506 -0.001 1.00 49.96 O HETATM 1319 O HOH A 687 12.673 8.570 2.601 1.00 52.23 O HETATM 1320 O HOH B 101 24.425 -9.620 -6.894 1.00 29.03 O HETATM 1321 O HOH B 102 29.745 -6.171 -0.327 1.00 20.96 O HETATM 1322 O HOH B 103 31.143 -1.521 -17.470 1.00 46.34 O HETATM 1323 O HOH B 104 32.633 -0.827 -8.906 1.00 41.17 O HETATM 1324 O HOH B 105 31.152 -8.892 -0.275 1.00 15.78 O HETATM 1325 O HOH B 106 27.189 -20.403 6.486 1.00 34.60 O HETATM 1326 O HOH B 107 22.650 -12.895 -8.396 1.00 22.03 O HETATM 1327 O HOH B 108 30.542 -18.727 7.217 1.00 29.38 O HETATM 1328 O HOH B 109 27.449 -9.230 -6.886 1.00 35.83 O HETATM 1329 O HOH B 110 22.786 -10.596 -17.328 1.00 32.29 O HETATM 1330 O HOH B 111 33.077 -13.198 -3.407 1.00 24.98 O HETATM 1331 O HOH B 112 28.767 -0.018 -9.033 1.00 53.48 O HETATM 1332 O HOH B 113 35.926 -10.041 -4.118 1.00 19.99 O HETATM 1333 O HOH B 114 32.981 -9.164 -7.581 1.00 28.31 O HETATM 1334 O HOH B 115 35.730 -6.104 -5.520 1.00 22.57 O HETATM 1335 O HOH B 116 33.663 -16.671 4.950 1.00 16.05 O HETATM 1336 O HOH B 117 29.504 -17.742 -4.213 1.00 30.59 O HETATM 1337 O HOH B 118 31.739 -20.166 -4.036 1.00 43.22 O HETATM 1338 O HOH B 119 23.949 -18.726 5.067 1.00 25.50 O HETATM 1339 O HOH B 120 26.748 -26.407 2.684 1.00 51.19 O HETATM 1340 O HOH B 121 24.649 -22.495 -2.381 1.00 40.37 O HETATM 1341 O HOH B 122 25.985 -0.804 -7.521 1.00 24.29 O HETATM 1342 O HOH B 123 29.066 -13.614 -6.774 1.00 26.79 O HETATM 1343 O HOH B 124 33.647 -25.065 -2.277 1.00 40.39 O HETATM 1344 O HOH B 125 32.903 -16.778 -2.883 1.00 31.02 O HETATM 1345 O HOH B 126 15.902 -21.678 -1.695 1.00 42.98 O HETATM 1346 O HOH B 127 20.232 -21.905 5.215 1.00 41.29 O HETATM 1347 O HOH B 128 34.710 -23.883 -4.704 1.00 45.63 O HETATM 1348 O HOH B 129 29.796 2.421 -8.594 1.00 44.19 O HETATM 1349 O HOH B 130 34.023 -8.494 -10.437 1.00 44.47 O HETATM 1350 O HOH B 131 33.088 -13.912 0.643 1.00 17.97 O HETATM 1351 O HOH B 132 33.400 -22.141 -2.703 1.00 41.25 O HETATM 1352 O HOH B 133 34.168 -13.541 -6.139 1.00 49.80 O HETATM 1353 O HOH B 134 35.587 -8.643 -6.568 1.00 24.73 O HETATM 1354 O HOH B 135 34.579 -15.109 -1.211 1.00 22.06 O HETATM 1355 O HOH B 136 33.975 -0.542 -11.146 1.00 44.27 O HETATM 1356 O HOH B 137 36.043 -26.749 -3.432 1.00 40.21 O HETATM 1357 O HOH B 138 24.198 -22.440 6.499 1.00 45.85 O HETATM 1358 O HOH B 139 29.186 -11.145 -8.187 1.00 25.54 O HETATM 1359 O HOH B 140 22.132 -20.754 6.194 1.00 41.35 O HETATM 1360 O HOH B 141 31.823 -11.245 -9.180 1.00 32.42 O HETATM 1361 O HOH B 142 37.985 -4.788 -6.860 1.00 38.91 O CONECT 130 1131 CONECT 155 1131 CONECT 300 1132 CONECT 319 1132 CONECT 351 1131 CONECT 373 1131 CONECT 525 1132 CONECT 548 1132 CONECT 570 1130 CONECT 588 1130 CONECT 691 1129 CONECT 711 1129 CONECT 752 1130 CONECT 778 1130 CONECT 923 1129 CONECT 946 1129 CONECT 1051 1053 CONECT 1053 1051 1054 CONECT 1054 1053 1055 1065 CONECT 1055 1054 1056 CONECT 1056 1055 1057 CONECT 1057 1056 1058 CONECT 1058 1057 1059 CONECT 1059 1058 1060 CONECT 1060 1059 1061 1062 CONECT 1061 1060 CONECT 1062 1060 1063 CONECT 1063 1062 1064 CONECT 1064 1063 CONECT 1065 1054 1066 1067 CONECT 1066 1065 CONECT 1067 1065 CONECT 1129 691 711 923 946 CONECT 1130 570 588 752 778 CONECT 1131 130 155 351 373 CONECT 1132 300 319 525 548 MASTER 483 0 5 7 5 0 4 6 1332 2 36 13 END
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Related entries of code: 5b78
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
3v43
RCSB PDB
PDBbind
112aa, >3V43_1|Chain... at 98%
5b75
RCSB PDB
PDBbind
131aa, >5B75_1|Chain... *
5b76
RCSB PDB
PDBbind
131aa, >5B76_1|Chain... at 100%
5b77
RCSB PDB
PDBbind
131aa, >5B77_1|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
5b76
RCSB PDB
PDBbind
histone H3 crotonylation at K14, H3(1-25)K14cr
Entry Information
PDB ID
5b78
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
MOZ double PHD finger mutant-S210D/N235R
Ligand Name
histone H3 crotonylation at K14, H3(1-25)K14cr
EC.Number
E.C.2.3.1.48
Resolution
1.4(Å)
Affinity (Kd/Ki/IC50)
Kd=1.88uM
Release Year
2016
Protein/NA Sequence
Check fasta file
Primary Reference
(2016) Nat.Chem.Biol. Vol. 12: pp. 1111-1118
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q92794
K7EMV3
Entrez Gene ID
NCBI Entrez Gene ID:
7994
ASD
Information of known allosteric effects of PDB entries
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