HEADER STRUCTURAL PROTEIN 15-MAY-20 6X02 TITLE NUP84-NUP133 (AA521-1157) FROM S. CEREVISIAE BOUND BY VHH-SAN8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOPORIN NUP84; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NUCLEAR PORE PROTEIN NUP84; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NUCLEOPORIN NUP133; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: NUCLEAR PORE PROTEIN NUP133; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: VHH-SAN8; COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 / SOURCE 3 S288C); SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 5 ORGANISM_TAXID: 559292; SOURCE 6 STRAIN: ATCC 204508 / S288C; SOURCE 7 GENE: NUP84, YDL116W; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 / SOURCE 12 S288C); SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 14 ORGANISM_TAXID: 559292; SOURCE 15 STRAIN: ATCC 204508 / S288C; SOURCE 16 GENE: NUP133, RAT3, YKR082W, YKR402; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 21 ORGANISM_TAXID: 30538; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS STRUCTURAL PROTEIN, NUCLEOPORIN, NANOBODY EXPDTA X-RAY DIFFRACTION AUTHOR S.A.NORDEEN,T.U.SCHWARTZ REVDAT 1 09-DEC-20 6X02 0 JRNL AUTH S.A.NORDEEN,D.L.TURMAN,T.U.SCHWARTZ JRNL TITL YEAST NUP84-NUP133 COMPLEX STRUCTURE DETAILS FLEXIBILITY AND JRNL TITL 2 REVEALS CONSERVATION OF THE MEMBRANE ANCHORING ALPS MOTIF. JRNL REF NAT COMMUN V. 11 6060 2020 JRNL REFN ESSN 2041-1723 JRNL PMID 33247142 JRNL DOI 10.1038/S41467-020-19885-5 REMARK 2 REMARK 2 RESOLUTION. 6.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18_3845 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 6.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 103.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 13453 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.315 REMARK 3 R VALUE (WORKING SET) : 0.314 REMARK 3 FREE R VALUE : 0.324 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.030 REMARK 3 FREE R VALUE TEST SET COUNT : 1350 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1103.3800 - 13.7400 0.99 1337 151 0.3569 0.3406 REMARK 3 2 13.7300 - 10.9100 0.99 1236 139 0.2689 0.2851 REMARK 3 3 10.9100 - 9.5300 0.99 1231 135 0.2359 0.2431 REMARK 3 4 9.5300 - 8.6600 1.00 1222 135 0.2563 0.3141 REMARK 3 5 8.6600 - 8.0400 1.00 1192 135 0.3190 0.3504 REMARK 3 6 8.0400 - 7.5700 1.00 1240 136 0.3813 0.4081 REMARK 3 7 7.5700 - 7.1900 1.00 1174 131 0.4068 0.4523 REMARK 3 8 7.1900 - 6.8700 1.00 1227 131 0.4223 0.4286 REMARK 3 9 6.8700 - 6.6100 1.00 1174 137 0.4321 0.4470 REMARK 3 10 6.6100 - 6.3800 0.89 1070 120 0.4679 0.4815 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL 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) : 1.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.812 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 614.5 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 574.6 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 : 0.003 6653 REMARK 3 ANGLE : 0.840 9266 REMARK 3 CHIRALITY : 0.048 1299 REMARK 3 PLANARITY : 0.004 1328 REMARK 3 DIHEDRAL : 4.314 1328 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 25 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.6746 10.5650 40.6575 REMARK 3 T TENSOR REMARK 3 T11: 6.9729 T22: 6.0731 REMARK 3 T33: 10.0669 T12: 2.0572 REMARK 3 T13: -1.9460 T23: -4.1998 REMARK 3 L TENSOR REMARK 3 L11: 0.1110 L22: 0.1443 REMARK 3 L33: 0.0330 L12: -0.1161 REMARK 3 L13: 0.0431 L23: -0.0271 REMARK 3 S TENSOR REMARK 3 S11: 0.0760 S12: -0.6069 S13: -0.4544 REMARK 3 S21: -0.4847 S22: -0.1517 S23: 0.0797 REMARK 3 S31: 0.3252 S32: -0.3826 S33: -0.1324 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.9777 2.7336 53.4818 REMARK 3 T TENSOR REMARK 3 T11: 2.5143 T22: 4.0971 REMARK 3 T33: 6.4102 T12: 2.1018 REMARK 3 T13: -2.3312 T23: -0.4821 REMARK 3 L TENSOR REMARK 3 L11: -0.0038 L22: 0.4516 REMARK 3 L33: 0.8066 L12: 0.0077 REMARK 3 L13: -0.0358 L23: -0.5402 REMARK 3 S TENSOR REMARK 3 S11: 0.1748 S12: 0.8281 S13: -0.1229 REMARK 3 S21: -0.4206 S22: -0.7377 S23: 0.3676 REMARK 3 S31: -0.1091 S32: 0.0602 S33: -0.3905 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 205 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.2173 35.3199 53.2310 REMARK 3 T TENSOR REMARK 3 T11: 5.3186 T22: 7.8399 REMARK 3 T33: 6.9181 T12: -1.9416 REMARK 3 T13: 0.6718 T23: -4.0547 REMARK 3 L TENSOR REMARK 3 L11: 1.0286 L22: 2.2780 REMARK 3 L33: 0.6695 L12: -0.1674 REMARK 3 L13: 0.4873 L23: 0.6776 REMARK 3 S TENSOR REMARK 3 S11: 1.1953 S12: -1.4792 S13: -0.0137 REMARK 3 S21: -4.9235 S22: -1.7611 S23: -1.0244 REMARK 3 S31: -1.0077 S32: 3.3919 S33: 1.4921 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9892 46.8169 61.6962 REMARK 3 T TENSOR REMARK 3 T11: 7.9559 T22: 9.0338 REMARK 3 T33: 5.8871 T12: 2.0992 REMARK 3 T13: -3.9343 T23: -5.6251 REMARK 3 L TENSOR REMARK 3 L11: 2.8545 L22: 2.1350 REMARK 3 L33: 1.6827 L12: -0.9244 REMARK 3 L13: -1.1328 L23: -1.1938 REMARK 3 S TENSOR REMARK 3 S11: -0.8805 S12: -2.0120 S13: 0.8900 REMARK 3 S21: 0.1603 S22: -0.5345 S23: 1.5018 REMARK 3 S31: -1.3605 S32: 1.2927 S33: -3.5802 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 315 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5121 50.5421 75.5932 REMARK 3 T TENSOR REMARK 3 T11: 13.6081 T22: 13.5568 REMARK 3 T33: 7.1119 T12: -0.2077 REMARK 3 T13: 1.2964 T23: -0.3023 REMARK 3 L TENSOR REMARK 3 L11: 0.0126 L22: 0.0107 REMARK 3 L33: 0.0169 L12: -0.0035 REMARK 3 L13: -0.0128 L23: 0.0122 REMARK 3 S TENSOR REMARK 3 S11: -0.5355 S12: 0.2690 S13: 0.6833 REMARK 3 S21: -0.1324 S22: -0.1246 S23: 0.3794 REMARK 3 S31: -0.1474 S32: 0.0568 S33: -0.3494 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 323 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.5903 41.7812 61.5880 REMARK 3 T TENSOR REMARK 3 T11: 6.7227 T22: 3.7442 REMARK 3 T33: 11.5212 T12: -1.7114 REMARK 3 T13: 1.9566 T23: -1.5567 REMARK 3 L TENSOR REMARK 3 L11: 0.0574 L22: 1.8804 REMARK 3 L33: 0.9240 L12: -0.1513 REMARK 3 L13: 0.1535 L23: 0.0983 REMARK 3 S TENSOR REMARK 3 S11: 0.1507 S12: -0.4293 S13: 0.0213 REMARK 3 S21: 1.2503 S22: -0.1437 S23: 0.5480 REMARK 3 S31: -2.2821 S32: 0.4961 S33: 0.4039 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 324 THROUGH 339 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7143 36.1679 44.6878 REMARK 3 T TENSOR REMARK 3 T11: 6.3455 T22: 5.5672 REMARK 3 T33: 3.5993 T12: 1.3961 REMARK 3 T13: -2.1527 T23: 1.3172 REMARK 3 L TENSOR REMARK 3 L11: 1.4622 L22: 2.1587 REMARK 3 L33: 0.0541 L12: -0.4068 REMARK 3 L13: -0.0690 L23: 0.3258 REMARK 3 S TENSOR REMARK 3 S11: 0.3763 S12: 1.0695 S13: 1.0188 REMARK 3 S21: -2.6676 S22: -2.2585 S23: -2.0402 REMARK 3 S31: -0.3602 S32: 0.7322 S33: -0.0932 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 344 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.9999 27.9332 41.2059 REMARK 3 T TENSOR REMARK 3 T11: 9.6414 T22: 3.2835 REMARK 3 T33: 8.3222 T12: 0.8592 REMARK 3 T13: -1.0208 T23: 2.7889 REMARK 3 L TENSOR REMARK 3 L11: 1.7196 L22: 0.1571 REMARK 3 L33: 0.2639 L12: -0.2518 REMARK 3 L13: -0.6015 L23: 0.0073 REMARK 3 S TENSOR REMARK 3 S11: 0.4015 S12: 0.0502 S13: 0.1913 REMARK 3 S21: 0.1771 S22: 0.2043 S23: -0.1727 REMARK 3 S31: -0.0285 S32: -0.1760 S33: 0.2208 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 345 THROUGH 352 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.7897 23.5859 49.6480 REMARK 3 T TENSOR REMARK 3 T11: 4.6849 T22: 4.4613 REMARK 3 T33: 6.8968 T12: 0.5643 REMARK 3 T13: 1.3896 T23: -4.4489 REMARK 3 L TENSOR REMARK 3 L11: 0.9402 L22: 0.0723 REMARK 3 L33: 0.0426 L12: -0.2042 REMARK 3 L13: -0.2110 L23: 0.0376 REMARK 3 S TENSOR REMARK 3 S11: -0.4008 S12: -0.3085 S13: 0.0540 REMARK 3 S21: 0.1863 S22: 0.0869 S23: 0.0211 REMARK 3 S31: -0.1041 S32: -0.3630 S33: -1.6539 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 353 THROUGH 368 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8166 18.0055 35.4001 REMARK 3 T TENSOR REMARK 3 T11: 5.4356 T22: 5.4992 REMARK 3 T33: 8.4393 T12: 5.0159 REMARK 3 T13: -1.7026 T23: 2.4357 REMARK 3 L TENSOR REMARK 3 L11: 1.1055 L22: 1.4446 REMARK 3 L33: 0.9983 L12: 0.6825 REMARK 3 L13: -0.2876 L23: -1.1354 REMARK 3 S TENSOR REMARK 3 S11: 0.1340 S12: -0.2873 S13: 0.7985 REMARK 3 S21: -2.1898 S22: -0.2121 S23: 1.1505 REMARK 3 S31: -0.3075 S32: -0.7224 S33: 0.6793 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 419 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2216 9.6958 44.6054 REMARK 3 T TENSOR REMARK 3 T11: 7.0365 T22: 8.9332 REMARK 3 T33: 9.5284 T12: -1.9877 REMARK 3 T13: 3.9180 T23: -3.3192 REMARK 3 L TENSOR REMARK 3 L11: 0.5529 L22: 0.7775 REMARK 3 L33: 0.6528 L12: -0.6678 REMARK 3 L13: 0.5679 L23: -0.6957 REMARK 3 S TENSOR REMARK 3 S11: 4.0168 S12: -0.6822 S13: -4.0697 REMARK 3 S21: -3.9653 S22: 0.0436 S23: 2.7750 REMARK 3 S31: 1.1650 S32: -3.6438 S33: 2.3197 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 420 THROUGH 450 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1644 -1.9830 40.1624 REMARK 3 T TENSOR REMARK 3 T11: 4.3251 T22: 5.2271 REMARK 3 T33: 6.8095 T12: -0.4084 REMARK 3 T13: 0.0170 T23: -0.0783 REMARK 3 L TENSOR REMARK 3 L11: 0.0572 L22: 0.3672 REMARK 3 L33: 0.1915 L12: -0.1651 REMARK 3 L13: 0.0557 L23: 0.0215 REMARK 3 S TENSOR REMARK 3 S11: 4.3456 S12: -0.1737 S13: -0.4885 REMARK 3 S21: 0.4302 S22: 5.0911 S23: 2.7621 REMARK 3 S31: -2.9883 S32: -0.4493 S33: 0.0000 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 451 THROUGH 491 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.4806 -12.4813 34.0875 REMARK 3 T TENSOR REMARK 3 T11: 5.6251 T22: 5.0207 REMARK 3 T33: 2.5847 T12: 1.9238 REMARK 3 T13: -0.0540 T23: -1.0803 REMARK 3 L TENSOR REMARK 3 L11: 0.2875 L22: 0.8813 REMARK 3 L33: 0.3958 L12: 0.6363 REMARK 3 L13: 0.0759 L23: -0.0401 REMARK 3 S TENSOR REMARK 3 S11: -1.5633 S12: -3.0135 S13: -0.5197 REMARK 3 S21: 1.6347 S22: -0.9622 S23: -2.0843 REMARK 3 S31: -0.3049 S32: 1.0781 S33: -0.0566 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 492 THROUGH 511 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9276 -17.3822 15.2106 REMARK 3 T TENSOR REMARK 3 T11: 6.5874 T22: 2.8203 REMARK 3 T33: 6.2199 T12: 1.4537 REMARK 3 T13: -3.1192 T23: 2.8427 REMARK 3 L TENSOR REMARK 3 L11: 3.3207 L22: 4.6770 REMARK 3 L33: 1.6690 L12: -3.7157 REMARK 3 L13: -2.3141 L23: 2.4811 REMARK 3 S TENSOR REMARK 3 S11: 1.2254 S12: 2.7017 S13: -0.3901 REMARK 3 S21: -0.7227 S22: -0.5019 S23: 3.2672 REMARK 3 S31: -0.9658 S32: -1.1858 S33: -4.5747 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 512 THROUGH 603 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.6734 -29.7065 27.7809 REMARK 3 T TENSOR REMARK 3 T11: 4.0082 T22: 2.6360 REMARK 3 T33: 6.0060 T12: 2.6072 REMARK 3 T13: -1.8271 T23: -0.1221 REMARK 3 L TENSOR REMARK 3 L11: 6.0481 L22: 2.3488 REMARK 3 L33: 2.0292 L12: -0.5381 REMARK 3 L13: 2.8804 L23: 5.0901 REMARK 3 S TENSOR REMARK 3 S11: -0.2227 S12: -6.0465 S13: -3.5400 REMARK 3 S21: 2.9830 S22: -2.7153 S23: -3.1442 REMARK 3 S31: 2.5883 S32: -7.0395 S33: -0.6546 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 604 THROUGH 657 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.9199 -41.0019 14.1315 REMARK 3 T TENSOR REMARK 3 T11: 1.7292 T22: 5.5621 REMARK 3 T33: 6.8837 T12: 0.0024 REMARK 3 T13: -0.8764 T23: 1.2483 REMARK 3 L TENSOR REMARK 3 L11: 1.4945 L22: 4.2083 REMARK 3 L33: 2.2921 L12: 2.5935 REMARK 3 L13: -2.1698 L23: -3.0447 REMARK 3 S TENSOR REMARK 3 S11: -2.1891 S12: 2.1670 S13: 3.0810 REMARK 3 S21: 0.4952 S22: 1.4488 S23: -1.8852 REMARK 3 S31: -1.6609 S32: 1.4425 S33: -2.0571 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 658 THROUGH 726 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9791 -44.2271 1.3777 REMARK 3 T TENSOR REMARK 3 T11: 2.7296 T22: 2.9574 REMARK 3 T33: 4.4737 T12: 0.6374 REMARK 3 T13: -1.1320 T23: -1.1595 REMARK 3 L TENSOR REMARK 3 L11: 1.2745 L22: 0.6198 REMARK 3 L33: 0.6257 L12: 1.2353 REMARK 3 L13: 0.8152 L23: 0.5000 REMARK 3 S TENSOR REMARK 3 S11: -1.6482 S12: -0.2486 S13: -0.7880 REMARK 3 S21: -0.5963 S22: 2.2302 S23: 1.2638 REMARK 3 S31: 0.3380 S32: 4.1742 S33: 0.0014 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 549 THROUGH 593 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9113 -57.4229 -70.3453 REMARK 3 T TENSOR REMARK 3 T11: 7.1317 T22: 9.3729 REMARK 3 T33: 1.8843 T12: 1.9146 REMARK 3 T13: 5.6824 T23: 2.3760 REMARK 3 L TENSOR REMARK 3 L11: 0.0679 L22: 4.9027 REMARK 3 L33: 0.2249 L12: -0.6210 REMARK 3 L13: 0.1576 L23: -0.7630 REMARK 3 S TENSOR REMARK 3 S11: -1.3664 S12: 1.1204 S13: -2.4729 REMARK 3 S21: -0.8834 S22: 1.5722 S23: 2.0107 REMARK 3 S31: -2.9604 S32: 3.8930 S33: 2.1590 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 594 THROUGH 626 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.3629 -71.4011 -60.2463 REMARK 3 T TENSOR REMARK 3 T11: 8.4896 T22: 3.4181 REMARK 3 T33: 3.2492 T12: 1.8085 REMARK 3 T13: -0.4685 T23: 2.5967 REMARK 3 L TENSOR REMARK 3 L11: 1.7264 L22: 0.0095 REMARK 3 L33: 0.1234 L12: -0.1551 REMARK 3 L13: -0.4512 L23: 0.0802 REMARK 3 S TENSOR REMARK 3 S11: -2.4063 S12: -1.2407 S13: -4.2447 REMARK 3 S21: 0.9803 S22: 1.4106 S23: 1.2584 REMARK 3 S31: 2.3809 S32: 3.1314 S33: 0.0779 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 627 THROUGH 661 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.7303 -73.9983 -55.9919 REMARK 3 T TENSOR REMARK 3 T11: 5.3008 T22: -1.8318 REMARK 3 T33: 2.7327 T12: -0.8416 REMARK 3 T13: 2.0474 T23: -2.4563 REMARK 3 L TENSOR REMARK 3 L11: 2.2830 L22: 2.7518 REMARK 3 L33: 4.4328 L12: -1.0117 REMARK 3 L13: -3.0438 L23: 2.2749 REMARK 3 S TENSOR REMARK 3 S11: -2.4322 S12: 2.3673 S13: -2.3690 REMARK 3 S21: -4.6371 S22: -1.6629 S23: 0.9410 REMARK 3 S31: 2.3153 S32: -1.3418 S33: -1.9717 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 662 THROUGH 715 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.0414 -59.1679 -54.5746 REMARK 3 T TENSOR REMARK 3 T11: 7.3423 T22: 0.0206 REMARK 3 T33: 3.0771 T12: -1.5029 REMARK 3 T13: 0.3650 T23: -1.9914 REMARK 3 L TENSOR REMARK 3 L11: 1.8327 L22: 1.2017 REMARK 3 L33: 0.6985 L12: 0.8231 REMARK 3 L13: 1.5276 L23: -0.7484 REMARK 3 S TENSOR REMARK 3 S11: 3.1910 S12: -2.2905 S13: -4.5972 REMARK 3 S21: -7.2910 S22: -0.3354 S23: -4.2172 REMARK 3 S31: 2.6772 S32: 0.4007 S33: -0.0584 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 716 THROUGH 768 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.2223 -58.9396 -43.2665 REMARK 3 T TENSOR REMARK 3 T11: 9.5288 T22: 4.0391 REMARK 3 T33: 3.9369 T12: 0.0235 REMARK 3 T13: -0.0952 T23: 0.6422 REMARK 3 L TENSOR REMARK 3 L11: 2.0101 L22: 3.5866 REMARK 3 L33: 9.3499 L12: -5.0185 REMARK 3 L13: -3.4879 L23: 4.8591 REMARK 3 S TENSOR REMARK 3 S11: -1.0892 S12: -3.7360 S13: 4.8734 REMARK 3 S21: -0.1451 S22: 0.5377 S23: -0.5812 REMARK 3 S31: 0.5990 S32: 5.5400 S33: 0.2713 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 769 THROUGH 1123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.0842 -66.7991 -7.0128 REMARK 3 T TENSOR REMARK 3 T11: 2.5168 T22: 3.7439 REMARK 3 T33: 4.6405 T12: -0.5242 REMARK 3 T13: 0.0615 T23: 0.3606 REMARK 3 L TENSOR REMARK 3 L11: -0.2867 L22: 6.1941 REMARK 3 L33: 2.0451 L12: 4.9180 REMARK 3 L13: -2.1852 L23: -3.5547 REMARK 3 S TENSOR REMARK 3 S11: 1.6489 S12: -0.6913 S13: -0.4038 REMARK 3 S21: 0.6358 S22: -1.8409 S23: 0.2838 REMARK 3 S31: 0.3737 S32: 0.8566 S33: -0.0202 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1124 THROUGH 1157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.1672 -83.3982 23.9421 REMARK 3 T TENSOR REMARK 3 T11: 3.0932 T22: 8.7690 REMARK 3 T33: -0.5300 T12: -1.5097 REMARK 3 T13: 1.1090 T23: 5.6349 REMARK 3 L TENSOR REMARK 3 L11: 1.2927 L22: 0.2205 REMARK 3 L33: 1.9441 L12: 0.3869 REMARK 3 L13: 3.9322 L23: 0.9394 REMARK 3 S TENSOR REMARK 3 S11: -2.5530 S12: -3.4082 S13: 0.2219 REMARK 3 S21: 0.8485 S22: -3.7922 S23: 0.3325 REMARK 3 S31: -4.2432 S32: -3.2781 S33: -27.9894 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 31.4597 21.4867 64.9910 REMARK 3 T TENSOR REMARK 3 T11: 7.9995 T22: 10.1893 REMARK 3 T33: 5.9607 T12: 4.4568 REMARK 3 T13: -2.0362 T23: -0.7411 REMARK 3 L TENSOR REMARK 3 L11: 2.5059 L22: 1.5794 REMARK 3 L33: 2.7400 L12: 1.8981 REMARK 3 L13: -2.5009 L23: -2.0344 REMARK 3 S TENSOR REMARK 3 S11: 1.6091 S12: -3.4071 S13: -4.8470 REMARK 3 S21: -0.4949 S22: -1.3486 S23: -6.9402 REMARK 3 S31: 0.9315 S32: -1.2554 S33: 4.8954 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 6X02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1000249125. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-AUG-19; 15-OCT-19 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 24-ID-C; 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791; 1.2141 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL; PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M; PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13539 REMARK 200 RESOLUTION RANGE HIGH (A) : 6.400 REMARK 200 RESOLUTION RANGE LOW (A) : 103.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 24.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 55.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.38 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 6.63 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 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: PHENIX, SHELXCD REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 8,000, 30% ETHYLENE GLYCOL, REMARK 280 0.1M IMIDAZOLE TITRATED WITH MES PH 6.5, 15MM SODIUM NITRATE, REMARK 280 15MM SODIUM PHOSPHATE DIBASIC, 15MM AMMONIUM SULFATE, VAPOR REMARK 280 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 36.12850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 148.68750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 143.82500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 148.68750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.12850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 143.82500 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 MET A 1 REMARK 465 GLU A 2 REMARK 465 LEU A 3 REMARK 465 SER A 4 REMARK 465 PRO A 5 REMARK 465 THR A 6 REMARK 465 ASN A 27 REMARK 465 ASN A 28 REMARK 465 GLU A 29 REMARK 465 GLN A 30 REMARK 465 ASN A 31 REMARK 465 PRO A 32 REMARK 465 ILE A 33 REMARK 465 GLU A 93 REMARK 465 MET A 94 REMARK 465 GLU A 95 REMARK 465 LEU A 96 REMARK 465 HIS A 97 REMARK 465 PRO A 98 REMARK 465 TYR A 99 REMARK 465 ASN A 100 REMARK 465 SER A 101 REMARK 465 ARG A 102 REMARK 465 GLY A 103 REMARK 465 LEU A 104 REMARK 465 PHE A 105 REMARK 465 GLU A 106 REMARK 465 LYS A 107 REMARK 465 LYS A 108 REMARK 465 LEU A 109 REMARK 465 MET A 110 REMARK 465 GLN A 111 REMARK 465 ILE A 148 REMARK 465 THR A 149 REMARK 465 SER A 150 REMARK 465 GLY A 151 REMARK 465 GLY A 152 REMARK 465 LEU A 153 REMARK 465 LYS A 154 REMARK 465 SER A 155 REMARK 465 CYS A 156 REMARK 465 ASP A 157 REMARK 465 LEU A 158 REMARK 465 ASP A 159 REMARK 465 PHE A 160 REMARK 465 PRO A 161 REMARK 465 LEU A 162 REMARK 465 ARG A 163 REMARK 465 GLU A 164 REMARK 465 ASN A 165 REMARK 465 THR A 166 REMARK 465 GLN A 226 REMARK 465 ILE A 227 REMARK 465 ALA A 228 REMARK 465 ASN A 229 REMARK 465 GLU A 230 REMARK 465 PHE A 231 REMARK 465 ASN A 232 REMARK 465 THR A 233 REMARK 465 GLN A 234 REMARK 465 GLN A 235 REMARK 465 GLY A 236 REMARK 465 ILE A 237 REMARK 465 LYS A 238 REMARK 465 VAL A 369 REMARK 465 VAL A 370 REMARK 465 LYS A 371 REMARK 465 GLY A 372 REMARK 465 THR A 373 REMARK 465 GLU A 374 REMARK 465 ALA A 375 REMARK 465 SER A 376 REMARK 465 ASN A 377 REMARK 465 ASP A 378 REMARK 465 ILE A 379 REMARK 465 ILE A 380 REMARK 465 MET B 515 REMARK 465 ALA B 516 REMARK 465 ASP B 517 REMARK 465 PRO B 518 REMARK 465 ARG B 690 REMARK 465 TYR B 691 REMARK 465 GLU B 692 REMARK 465 LEU B 693 REMARK 465 LEU B 694 REMARK 465 GLU B 695 REMARK 465 LEU B 696 REMARK 465 ASP B 697 REMARK 465 PRO B 698 REMARK 465 MET B 699 REMARK 465 GLU B 700 REMARK 465 VAL B 701 REMARK 465 ASP B 702 REMARK 465 THR B 703 REMARK 465 SER B 704 REMARK 465 LYS B 705 REMARK 465 LEU B 706 REMARK 465 LYS B 855 REMARK 465 LYS B 856 REMARK 465 LEU B 857 REMARK 465 ASN B 858 REMARK 465 ASP B 859 REMARK 465 LEU B 860 REMARK 465 ILE B 861 REMARK 465 PHE B 862 REMARK 465 ARG B 863 REMARK 465 PHE B 864 REMARK 465 PRO B 865 REMARK 465 LEU B 932 REMARK 465 LEU B 933 REMARK 465 VAL B 934 REMARK 465 GLU B 935 REMARK 465 LYS B 936 REMARK 465 ASP B 937 REMARK 465 ASN B 938 REMARK 465 LEU B 939 REMARK 465 ASP B 940 REMARK 465 ARG C 27 REMARK 465 THR C 28 REMARK 465 PHE C 29 REMARK 465 THR C 30 REMARK 465 SER C 31 REMARK 465 TYR C 32 REMARK 465 ALA C 33 REMARK 465 MET C 34 REMARK 465 GLY C 35 REMARK 465 ALA C 50 REMARK 465 ILE C 51 REMARK 465 SER C 52 REMARK 465 ARG C 53 REMARK 465 LEU C 54 REMARK 465 ALA C 55 REMARK 465 SER C 56 REMARK 465 GLY C 57 REMARK 465 THR C 58 REMARK 465 LEU C 99 REMARK 465 GLN C 100 REMARK 465 ALA C 101 REMARK 465 LEU C 102 REMARK 465 ARG C 103 REMARK 465 PHE C 104 REMARK 465 SER C 105 REMARK 465 LEU C 106 REMARK 465 PRO C 107 REMARK 465 ILE C 108 REMARK 465 ALA C 109 REMARK 465 MET C 110 REMARK 465 ALA C 111 REMARK 465 THR C 112 REMARK 465 MET C 113 REMARK 465 LYS C 114 REMARK 465 ASN C 115 REMARK 465 GLY C 116 REMARK 465 ARG C 117 REMARK 465 ALA C 118 REMARK 465 ASP C 119 REMARK 465 SER C 120 REMARK 465 TRP C 121 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 TYR A 7 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN A 8 CG CD OE1 NE2 REMARK 470 THR A 9 OG1 CG2 REMARK 470 GLU A 10 CG CD OE1 OE2 REMARK 470 ARG A 11 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 12 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR A 13 OG1 CG2 REMARK 470 LYS A 14 CG CD CE NZ REMARK 470 PHE A 15 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 16 OG REMARK 470 ASP A 17 CG OD1 OD2 REMARK 470 THR A 18 OG1 CG2 REMARK 470 LEU A 19 CG CD1 CD2 REMARK 470 LYS A 20 CG CD CE NZ REMARK 470 GLU A 21 CG CD OE1 OE2 REMARK 470 PHE A 22 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 23 CG CD CE NZ REMARK 470 ILE A 24 CG1 CG2 CD1 REMARK 470 GLU A 25 CG CD OE1 OE2 REMARK 470 GLN A 26 CG CD OE1 NE2 REMARK 470 ASP A 34 CG OD1 OD2 REMARK 470 PRO A 35 CG CD REMARK 470 PHE A 36 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN A 37 CG OD1 ND2 REMARK 470 ILE A 38 CG1 CG2 CD1 REMARK 470 ILE A 39 CG1 CG2 CD1 REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 41 CG CD OE1 OE2 REMARK 470 PHE A 42 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2 REMARK 470 SER A 44 OG REMARK 470 GLN A 48 CG CD OE1 NE2 REMARK 470 LEU A 49 CG CD1 CD2 REMARK 470 LEU A 51 CG CD1 CD2 REMARK 470 ASP A 52 CG OD1 OD2 REMARK 470 LEU A 53 CG CD1 CD2 REMARK 470 ASN A 55 CG OD1 ND2 REMARK 470 SER A 56 OG REMARK 470 ASP A 58 CG OD1 OD2 REMARK 470 GLU A 59 CG CD OE1 OE2 REMARK 470 SER A 60 OG REMARK 470 ASN A 61 CG OD1 ND2 REMARK 470 VAL A 62 CG1 CG2 REMARK 470 ILE A 63 CG1 CG2 CD1 REMARK 470 SER A 64 OG REMARK 470 SER A 65 OG REMARK 470 LYS A 66 CG CD CE NZ REMARK 470 ASP A 67 CG OD1 OD2 REMARK 470 TRP A 68 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 68 CZ3 CH2 REMARK 470 GLU A 69 CG CD OE1 OE2 REMARK 470 LEU A 70 CG CD1 CD2 REMARK 470 GLU A 71 CG CD OE1 OE2 REMARK 470 ARG A 73 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 74 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TRP A 75 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 75 CZ3 CH2 REMARK 470 HIS A 76 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 77 CG CD1 CD2 REMARK 470 VAL A 78 CG1 CG2 REMARK 470 GLU A 79 CG CD OE1 OE2 REMARK 470 LEU A 80 CG CD1 CD2 REMARK 470 LEU A 81 CG CD1 CD2 REMARK 470 LEU A 82 CG CD1 CD2 REMARK 470 VAL A 83 CG1 CG2 REMARK 470 PHE A 84 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 85 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 86 CG OD1 ND2 REMARK 470 ASP A 88 CG OD1 OD2 REMARK 470 LEU A 89 CG CD1 CD2 REMARK 470 ASP A 90 CG OD1 OD2 REMARK 470 LEU A 91 CG CD1 CD2 REMARK 470 ASP A 92 CG OD1 OD2 REMARK 470 ASP A 112 CG OD1 OD2 REMARK 470 ASN A 113 CG OD1 ND2 REMARK 470 LYS A 114 CG CD CE NZ REMARK 470 GLN A 115 CG CD OE1 NE2 REMARK 470 LEU A 116 CG CD1 CD2 REMARK 470 TYR A 117 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN A 118 CG CD OE1 NE2 REMARK 470 ILE A 119 CG1 CG2 CD1 REMARK 470 TRP A 120 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 120 CZ3 CH2 REMARK 470 ILE A 121 CG1 CG2 CD1 REMARK 470 VAL A 122 CG1 CG2 REMARK 470 MET A 123 CG SD CE REMARK 470 VAL A 124 CG1 CG2 REMARK 470 TRP A 125 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 125 CZ3 CH2 REMARK 470 LEU A 126 CG CD1 CD2 REMARK 470 LYS A 127 CG CD CE NZ REMARK 470 GLU A 128 CG CD OE1 OE2 REMARK 470 ASN A 129 CG OD1 ND2 REMARK 470 THR A 130 OG1 CG2 REMARK 470 TYR A 131 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 132 CG1 CG2 REMARK 470 MET A 133 CG SD CE REMARK 470 GLU A 134 CG CD OE1 OE2 REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2 REMARK 470 PRO A 136 CG CD REMARK 470 LYS A 137 CG CD CE NZ REMARK 470 ASN A 138 CG OD1 ND2 REMARK 470 VAL A 139 CG1 CG2 REMARK 470 PRO A 140 CG CD REMARK 470 THR A 141 OG1 CG2 REMARK 470 SER A 142 OG REMARK 470 LYS A 143 CG CD CE NZ REMARK 470 TRP A 144 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 144 CZ3 CH2 REMARK 470 LEU A 145 CG CD1 CD2 REMARK 470 ASN A 146 CG OD1 ND2 REMARK 470 SER A 147 OG REMARK 470 ASN A 167 CG OD1 ND2 REMARK 470 VAL A 168 CG1 CG2 REMARK 470 LEU A 169 CG CD1 CD2 REMARK 470 ASP A 170 CG OD1 OD2 REMARK 470 VAL A 171 CG1 CG2 REMARK 470 LYS A 172 CG CD CE NZ REMARK 470 ASP A 173 CG OD1 OD2 REMARK 470 LYS A 174 CG CD CE NZ REMARK 470 GLU A 175 CG CD OE1 OE2 REMARK 470 GLU A 176 CG CD OE1 OE2 REMARK 470 ASP A 177 CG OD1 OD2 REMARK 470 HIS A 178 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 179 CG1 CG2 CD1 REMARK 470 PHE A 180 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 181 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 182 CG CD CE NZ REMARK 470 TYR A 183 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE A 184 CG1 CG2 CD1 REMARK 470 TYR A 185 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 186 CG CD OE1 OE2 REMARK 470 LEU A 187 CG CD1 CD2 REMARK 470 ILE A 188 CG1 CG2 CD1 REMARK 470 LEU A 189 CG CD1 CD2 REMARK 470 ILE A 193 CG1 CG2 CD1 REMARK 470 ASP A 194 CG OD1 OD2 REMARK 470 GLU A 195 CG CD OE1 OE2 REMARK 470 LEU A 197 CG CD1 CD2 REMARK 470 GLU A 198 CG CD OE1 OE2 REMARK 470 GLU A 199 CG CD OE1 OE2 REMARK 470 LYS A 201 CG CD CE NZ REMARK 470 LEU A 202 CG CD1 CD2 REMARK 470 SER A 203 OG REMARK 470 ASP A 204 CG OD1 OD2 REMARK 470 ASN A 205 CG OD1 ND2 REMARK 470 ILE A 206 CG1 CG2 CD1 REMARK 470 SER A 207 OG REMARK 470 ILE A 208 CG1 CG2 CD1 REMARK 470 CYS A 209 SG REMARK 470 MET A 210 CG SD CE REMARK 470 ILE A 211 CG1 CG2 CD1 REMARK 470 LEU A 212 CG CD1 CD2 REMARK 470 CYS A 213 SG REMARK 470 ILE A 215 CG1 CG2 CD1 REMARK 470 GLN A 216 CG CD OE1 NE2 REMARK 470 GLU A 217 CG CD OE1 OE2 REMARK 470 TYR A 218 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 219 CG CD1 CD2 REMARK 470 ASN A 220 CG OD1 ND2 REMARK 470 PRO A 221 CG CD REMARK 470 VAL A 222 CG1 CG2 REMARK 470 ILE A 223 CG1 CG2 CD1 REMARK 470 ASP A 224 CG OD1 OD2 REMARK 470 THR A 225 OG1 CG2 REMARK 470 LYS A 239 CG CD CE NZ REMARK 470 HIS A 240 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 241 OG REMARK 470 LEU A 242 CG CD1 CD2 REMARK 470 TRP A 243 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 243 CZ3 CH2 REMARK 470 ARG A 244 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 245 CG CD NE CZ NH1 NH2 REMARK 470 THR A 246 OG1 CG2 REMARK 470 VAL A 247 CG1 CG2 REMARK 470 TYR A 248 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 249 OG REMARK 470 LEU A 250 CG CD1 CD2 REMARK 470 SER A 251 OG REMARK 470 GLN A 252 CG CD OE1 NE2 REMARK 470 GLN A 253 CG CD OE1 NE2 REMARK 470 LEU A 256 CG CD1 CD2 REMARK 470 ASP A 257 CG OD1 OD2 REMARK 470 PRO A 258 CG CD REMARK 470 TYR A 259 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 260 CG CD OE1 OE2 REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 263 CG1 CG2 CD1 REMARK 470 TYR A 264 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 265 OG REMARK 470 TYR A 266 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 267 CG CD1 CD2 REMARK 470 SER A 268 OG REMARK 470 ILE A 271 CG1 CG2 CD1 REMARK 470 PRO A 272 CG CD REMARK 470 ASN A 273 CG OD1 ND2 REMARK 470 GLN A 274 CG CD OE1 NE2 REMARK 470 GLU A 275 CG CD OE1 OE2 REMARK 470 VAL A 276 CG1 CG2 REMARK 470 LEU A 277 CG CD1 CD2 REMARK 470 GLN A 278 CG CD OE1 NE2 REMARK 470 TYR A 279 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 280 OG REMARK 470 ASP A 281 CG OD1 OD2 REMARK 470 TRP A 282 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 282 CZ3 CH2 REMARK 470 GLU A 283 CG CD OE1 OE2 REMARK 470 SER A 284 OG REMARK 470 ASP A 285 CG OD1 OD2 REMARK 470 LEU A 286 CG CD1 CD2 REMARK 470 HIS A 287 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 288 CG1 CG2 CD1 REMARK 470 HIS A 289 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 290 CG CD1 CD2 REMARK 470 ASN A 291 CG OD1 ND2 REMARK 470 GLN A 292 CG CD OE1 NE2 REMARK 470 ILE A 293 CG1 CG2 CD1 REMARK 470 LEU A 294 CG CD1 CD2 REMARK 470 GLN A 295 CG CD OE1 NE2 REMARK 470 THR A 296 OG1 CG2 REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 ILE A 298 CG1 CG2 CD1 REMARK 470 GLU A 299 CG CD OE1 OE2 REMARK 470 ASN A 300 CG OD1 ND2 REMARK 470 TYR A 301 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 302 CG CD1 CD2 REMARK 470 LEU A 303 CG CD1 CD2 REMARK 470 GLU A 304 CG CD OE1 OE2 REMARK 470 ASN A 305 CG OD1 ND2 REMARK 470 ASN A 306 CG OD1 ND2 REMARK 470 GLN A 307 CG CD OE1 NE2 REMARK 470 VAL A 308 CG1 CG2 REMARK 470 THR A 310 OG1 CG2 REMARK 470 ASP A 311 CG OD1 OD2 REMARK 470 GLU A 312 CG CD OE1 OE2 REMARK 470 LEU A 313 CG CD1 CD2 REMARK 470 ILE A 314 CG1 CG2 CD1 REMARK 470 LEU A 315 CG CD1 CD2 REMARK 470 PRO A 316 CG CD REMARK 470 LEU A 317 CG CD1 CD2 REMARK 470 PRO A 318 CG CD REMARK 470 SER A 319 OG REMARK 470 HIS A 320 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 322 CG CD1 CD2 REMARK 470 THR A 323 OG1 CG2 REMARK 470 VAL A 324 CG1 CG2 REMARK 470 GLN A 325 CG CD OE1 NE2 REMARK 470 GLU A 326 CG CD OE1 OE2 REMARK 470 VAL A 327 CG1 CG2 REMARK 470 LEU A 328 CG CD1 CD2 REMARK 470 ASN A 329 CG OD1 ND2 REMARK 470 ARG A 330 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 331 CG1 CG2 REMARK 470 SER A 333 OG REMARK 470 ARG A 334 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 335 CG ND1 CD2 CE1 NE2 REMARK 470 PRO A 336 CG CD REMARK 470 SER A 337 OG REMARK 470 GLU A 338 CG CD OE1 OE2 REMARK 470 SER A 339 OG REMARK 470 GLU A 340 CG CD OE1 OE2 REMARK 470 HIS A 341 CG ND1 CD2 CE1 NE2 REMARK 470 PRO A 342 CG CD REMARK 470 ILE A 343 CG1 CG2 CD1 REMARK 470 ARG A 344 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 345 CG1 CG2 REMARK 470 LEU A 346 CG CD1 CD2 REMARK 470 MET A 347 CG SD CE REMARK 470 SER A 349 OG REMARK 470 VAL A 350 CG1 CG2 REMARK 470 ILE A 351 CG1 CG2 CD1 REMARK 470 LEU A 352 CG CD1 CD2 REMARK 470 ASP A 353 CG OD1 OD2 REMARK 470 SER A 354 OG REMARK 470 LEU A 355 CG CD1 CD2 REMARK 470 PRO A 356 CG CD REMARK 470 SER A 357 OG REMARK 470 VAL A 358 CG1 CG2 REMARK 470 ILE A 359 CG1 CG2 CD1 REMARK 470 HIS A 360 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 361 OG REMARK 470 SER A 362 OG REMARK 470 VAL A 363 CG1 CG2 REMARK 470 GLU A 364 CG CD OE1 OE2 REMARK 470 MET A 365 CG SD CE REMARK 470 LEU A 366 CG CD1 CD2 REMARK 470 LEU A 367 CG CD1 CD2 REMARK 470 ASP A 368 CG OD1 OD2 REMARK 470 ASP A 381 CG OD1 OD2 REMARK 470 LYS A 382 CG CD CE NZ REMARK 470 PRO A 383 CG CD REMARK 470 TYR A 384 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 385 CG CD1 CD2 REMARK 470 LEU A 386 CG CD1 CD2 REMARK 470 ARG A 387 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 388 CG1 CG2 CD1 REMARK 470 VAL A 389 CG1 CG2 REMARK 470 THR A 390 OG1 CG2 REMARK 470 HIS A 391 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 392 CG CD1 CD2 REMARK 470 ILE A 394 CG1 CG2 CD1 REMARK 470 CYS A 395 SG REMARK 470 LEU A 396 CG CD1 CD2 REMARK 470 ASP A 397 CG OD1 OD2 REMARK 470 ILE A 398 CG1 CG2 CD1 REMARK 470 ILE A 399 CG1 CG2 CD1 REMARK 470 ASN A 400 CG OD1 ND2 REMARK 470 PRO A 401 CG CD REMARK 470 SER A 403 OG REMARK 470 VAL A 404 CG1 CG2 REMARK 470 GLU A 405 CG CD OE1 OE2 REMARK 470 GLU A 406 CG CD OE1 OE2 REMARK 470 VAL A 407 CG1 CG2 REMARK 470 ASP A 408 CG OD1 OD2 REMARK 470 LYS A 409 CG CD CE NZ REMARK 470 SER A 410 OG REMARK 470 LYS A 411 CG CD CE NZ REMARK 470 LEU A 412 CG CD1 CD2 REMARK 470 ILE A 413 CG1 CG2 CD1 REMARK 470 THR A 414 OG1 CG2 REMARK 470 THR A 415 OG1 CG2 REMARK 470 TYR A 416 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE A 417 CG1 CG2 CD1 REMARK 470 SER A 418 OG REMARK 470 LEU A 419 CG CD1 CD2 REMARK 470 LEU A 420 CG CD1 CD2 REMARK 470 LYS A 421 CG CD CE NZ REMARK 470 LEU A 422 CG CD1 CD2 REMARK 470 GLN A 423 CG CD OE1 NE2 REMARK 470 LEU A 425 CG CD1 CD2 REMARK 470 TYR A 426 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 427 CG CD OE1 OE2 REMARK 470 ASN A 428 CG OD1 ND2 REMARK 470 ILE A 429 CG1 CG2 CD1 REMARK 470 PRO A 430 CG CD REMARK 470 ILE A 431 CG1 CG2 CD1 REMARK 470 TYR A 432 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR A 434 OG1 CG2 REMARK 470 PHE A 435 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 436 CG CD1 CD2 REMARK 470 ASN A 437 CG OD1 ND2 REMARK 470 GLU A 438 CG CD OE1 OE2 REMARK 470 SER A 439 OG REMARK 470 ASP A 440 CG OD1 OD2 REMARK 470 CYS A 441 SG REMARK 470 LEU A 442 CG CD1 CD2 REMARK 470 GLU A 443 CG CD OE1 OE2 REMARK 470 CYS A 445 SG REMARK 470 SER A 446 OG REMARK 470 PHE A 447 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 448 CG1 CG2 CD1 REMARK 470 LEU A 449 CG CD1 CD2 REMARK 470 SER A 450 OG REMARK 470 SER A 451 OG REMARK 470 LEU A 452 CG CD1 CD2 REMARK 470 GLU A 453 CG CD OE1 OE2 REMARK 470 ASP A 454 CG OD1 OD2 REMARK 470 PRO A 455 CG CD REMARK 470 GLN A 456 CG CD OE1 NE2 REMARK 470 VAL A 457 CG1 CG2 REMARK 470 ARG A 458 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 459 CG CD CE NZ REMARK 470 LYS A 460 CG CD CE NZ REMARK 470 GLN A 461 CG CD OE1 NE2 REMARK 470 ILE A 462 CG1 CG2 CD1 REMARK 470 GLU A 463 CG CD OE1 OE2 REMARK 470 THR A 464 OG1 CG2 REMARK 470 ILE A 465 CG1 CG2 CD1 REMARK 470 ASN A 466 CG OD1 ND2 REMARK 470 PHE A 467 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 468 CG CD1 CD2 REMARK 470 ARG A 469 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 470 CG CD1 CD2 REMARK 470 PRO A 471 CG CD REMARK 470 SER A 473 OG REMARK 470 ASN A 474 CG OD1 ND2 REMARK 470 ILE A 475 CG1 CG2 CD1 REMARK 470 LEU A 476 CG CD1 CD2 REMARK 470 ARG A 477 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2 REMARK 470 THR A 479 OG1 CG2 REMARK 470 THR A 480 OG1 CG2 REMARK 470 GLN A 481 CG CD OE1 NE2 REMARK 470 ARG A 482 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 483 CG1 CG2 REMARK 470 PHE A 484 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 485 CG OD1 OD2 REMARK 470 GLU A 486 CG CD OE1 OE2 REMARK 470 THR A 487 OG1 CG2 REMARK 470 GLU A 488 CG CD OE1 OE2 REMARK 470 GLN A 489 CG CD OE1 NE2 REMARK 470 GLU A 490 CG CD OE1 OE2 REMARK 470 TYR A 491 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 492 OG REMARK 470 PRO A 493 CG CD REMARK 470 SER A 494 OG REMARK 470 ASN A 495 CG OD1 ND2 REMARK 470 GLU A 496 CG CD OE1 OE2 REMARK 470 ILE A 497 CG1 CG2 CD1 REMARK 470 SER A 498 OG REMARK 470 ILE A 499 CG1 CG2 CD1 REMARK 470 SER A 500 OG REMARK 470 PHE A 501 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 502 CG OD1 OD2 REMARK 470 VAL A 503 CG1 CG2 REMARK 470 ASN A 504 CG OD1 ND2 REMARK 470 ASN A 505 CG OD1 ND2 REMARK 470 ILE A 506 CG1 CG2 CD1 REMARK 470 ASP A 507 CG OD1 OD2 REMARK 470 MET A 508 CG SD CE REMARK 470 HIS A 509 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 510 CG CD1 CD2 REMARK 470 ILE A 511 CG1 CG2 CD1 REMARK 470 TYR A 512 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 514 CG1 CG2 REMARK 470 GLU A 515 CG CD OE1 OE2 REMARK 470 TRP A 516 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 516 CZ3 CH2 REMARK 470 LEU A 517 CG CD1 CD2 REMARK 470 ILE A 518 CG1 CG2 CD1 REMARK 470 GLU A 519 CG CD OE1 OE2 REMARK 470 LYS A 521 CG CD CE NZ REMARK 470 LEU A 522 CG CD1 CD2 REMARK 470 TYR A 523 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 524 CG1 CG2 REMARK 470 ASP A 525 CG OD1 OD2 REMARK 470 VAL A 527 CG1 CG2 REMARK 470 HIS A 528 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 529 OG REMARK 470 ILE A 530 CG1 CG2 CD1 REMARK 470 ILE A 531 CG1 CG2 CD1 REMARK 470 LEU A 533 CG CD1 CD2 REMARK 470 SER A 534 OG REMARK 470 ARG A 535 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 536 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 537 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 538 CG CD1 CD2 REMARK 470 LEU A 539 CG CD1 CD2 REMARK 470 ASN A 540 CG OD1 ND2 REMARK 470 ARG A 542 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 543 CG1 CG2 REMARK 470 LYS A 544 CG CD CE NZ REMARK 470 LEU A 546 CG CD1 CD2 REMARK 470 GLU A 547 CG CD OE1 OE2 REMARK 470 GLN A 548 CG CD OE1 NE2 REMARK 470 PHE A 549 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET A 550 CG SD CE REMARK 470 GLU A 551 CG CD OE1 OE2 REMARK 470 ARG A 552 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 553 CG OD1 ND2 REMARK 470 ASN A 554 CG OD1 ND2 REMARK 470 ILE A 555 CG1 CG2 CD1 REMARK 470 GLU A 557 CG CD OE1 OE2 REMARK 470 ILE A 558 CG1 CG2 CD1 REMARK 470 CYS A 559 SG REMARK 470 LYS A 560 CG CD CE NZ REMARK 470 ASN A 561 CG OD1 ND2 REMARK 470 TYR A 562 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 563 CG CD OE1 OE2 REMARK 470 LEU A 564 CG CD1 CD2 REMARK 470 GLU A 565 CG CD OE1 OE2 REMARK 470 LYS A 566 CG CD CE NZ REMARK 470 ILE A 567 CG1 CG2 CD1 REMARK 470 ASP A 569 CG OD1 OD2 REMARK 470 ASN A 570 CG OD1 ND2 REMARK 470 ILE A 571 CG1 CG2 CD1 REMARK 470 SER A 572 OG REMARK 470 LYS A 573 CG CD CE NZ REMARK 470 ASP A 574 CG OD1 OD2 REMARK 470 GLU A 575 CG CD OE1 OE2 REMARK 470 ASN A 576 CG OD1 ND2 REMARK 470 GLU A 577 CG CD OE1 OE2 REMARK 470 ASP A 578 CG OD1 OD2 REMARK 470 GLN A 579 CG CD OE1 NE2 REMARK 470 PHE A 580 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 581 CG CD1 CD2 REMARK 470 GLU A 582 CG CD OE1 OE2 REMARK 470 GLU A 583 CG CD OE1 OE2 REMARK 470 ILE A 584 CG1 CG2 CD1 REMARK 470 THR A 585 OG1 CG2 REMARK 470 GLN A 586 CG CD OE1 NE2 REMARK 470 TYR A 587 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 588 CG CD OE1 OE2 REMARK 470 HIS A 589 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 590 CG CD1 CD2 REMARK 470 ILE A 591 CG1 CG2 CD1 REMARK 470 LYS A 592 CG CD CE NZ REMARK 470 ILE A 594 CG1 CG2 CD1 REMARK 470 ARG A 595 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 596 CG CD OE1 OE2 REMARK 470 TYR A 597 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 598 CG CD OE1 OE2 REMARK 470 GLU A 599 CG CD OE1 OE2 REMARK 470 TRP A 600 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 600 CZ3 CH2 REMARK 470 GLN A 601 CG CD OE1 NE2 REMARK 470 LYS A 602 CG CD CE NZ REMARK 470 SER A 603 OG REMARK 470 VAL A 604 CG1 CG2 REMARK 470 SER A 605 OG REMARK 470 LEU A 606 CG CD1 CD2 REMARK 470 LEU A 607 CG CD1 CD2 REMARK 470 SER A 608 OG REMARK 470 SER A 609 OG REMARK 470 GLU A 610 CG CD OE1 OE2 REMARK 470 SER A 611 OG REMARK 470 ASN A 612 CG OD1 ND2 REMARK 470 ILE A 613 CG1 CG2 CD1 REMARK 470 PRO A 614 CG CD REMARK 470 THR A 615 OG1 CG2 REMARK 470 LEU A 616 CG CD1 CD2 REMARK 470 ILE A 617 CG1 CG2 CD1 REMARK 470 GLU A 618 CG CD OE1 OE2 REMARK 470 LYS A 619 CG CD CE NZ REMARK 470 LEU A 620 CG CD1 CD2 REMARK 470 GLN A 621 CG CD OE1 NE2 REMARK 470 PHE A 623 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 624 OG REMARK 470 LYS A 625 CG CD CE NZ REMARK 470 ASP A 626 CG OD1 OD2 REMARK 470 THR A 627 OG1 CG2 REMARK 470 PHE A 628 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 629 CG CD OE1 OE2 REMARK 470 LEU A 630 CG CD1 CD2 REMARK 470 ILE A 631 CG1 CG2 CD1 REMARK 470 LYS A 632 CG CD CE NZ REMARK 470 THR A 633 OG1 CG2 REMARK 470 PHE A 634 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 635 CG CD1 CD2 REMARK 470 VAL A 636 CG1 CG2 REMARK 470 ASP A 637 CG OD1 OD2 REMARK 470 LEU A 638 CG CD1 CD2 REMARK 470 THR A 639 OG1 CG2 REMARK 470 SER A 640 OG REMARK 470 SER A 641 OG REMARK 470 ASN A 642 CG OD1 ND2 REMARK 470 PHE A 643 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 645 CG OD1 OD2 REMARK 470 SER A 646 OG REMARK 470 ASP A 648 CG OD1 OD2 REMARK 470 TYR A 649 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 650 CG CD OE1 OE2 REMARK 470 ILE A 651 CG1 CG2 CD1 REMARK 470 LEU A 652 CG CD1 CD2 REMARK 470 TYR A 653 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 654 CG CD OE1 OE2 REMARK 470 ILE A 655 CG1 CG2 CD1 REMARK 470 ARG A 656 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 658 CG CD1 CD2 REMARK 470 TYR A 659 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR A 660 OG1 CG2 REMARK 470 PRO A 661 CG CD REMARK 470 PHE A 662 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 663 CG CD1 CD2 REMARK 470 LEU A 664 CG CD1 CD2 REMARK 470 MET A 665 CG SD CE REMARK 470 GLU A 666 CG CD OE1 OE2 REMARK 470 LEU A 667 CG CD1 CD2 REMARK 470 HIS A 668 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 669 CG CD CE NZ REMARK 470 LYS A 670 CG CD CE NZ REMARK 470 LEU A 671 CG CD1 CD2 REMARK 470 VAL A 672 CG1 CG2 REMARK 470 GLU A 673 CG CD OE1 OE2 REMARK 470 LYS A 676 CG CD CE NZ REMARK 470 LEU A 677 CG CD1 CD2 REMARK 470 LEU A 678 CG CD1 CD2 REMARK 470 LYS A 679 CG CD CE NZ REMARK 470 ILE A 680 CG1 CG2 CD1 REMARK 470 PRO A 681 CG CD REMARK 470 LYS A 682 CG CD CE NZ REMARK 470 PHE A 683 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 684 CG1 CG2 CD1 REMARK 470 SER A 685 OG REMARK 470 GLU A 686 CG CD OE1 OE2 REMARK 470 LEU A 688 CG CD1 CD2 REMARK 470 PHE A 690 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR A 691 OG1 CG2 REMARK 470 SER A 692 OG REMARK 470 LEU A 693 CG CD1 CD2 REMARK 470 VAL A 694 CG1 CG2 REMARK 470 ASN A 696 CG OD1 ND2 REMARK 470 GLU A 697 CG CD OE1 OE2 REMARK 470 ASN A 698 CG OD1 ND2 REMARK 470 ASP A 699 CG OD1 OD2 REMARK 470 LYS A 700 CG CD CE NZ REMARK 470 ILE A 701 CG1 CG2 CD1 REMARK 470 TYR A 702 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 703 CG CD1 CD2 REMARK 470 LEU A 704 CG CD1 CD2 REMARK 470 PHE A 705 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN A 706 CG CD OE1 NE2 REMARK 470 SER A 707 OG REMARK 470 SER A 708 OG REMARK 470 LYS A 710 CG CD CE NZ REMARK 470 LEU A 711 CG CD1 CD2 REMARK 470 LYS A 712 CG CD CE NZ REMARK 470 GLU A 713 CG CD OE1 OE2 REMARK 470 TYR A 714 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 715 CG CD1 CD2 REMARK 470 ASP A 716 CG OD1 OD2 REMARK 470 LEU A 717 CG CD1 CD2 REMARK 470 VAL A 718 CG1 CG2 REMARK 470 ARG A 720 CG CD NE CZ NH1 NH2 REMARK 470 THR A 721 OG1 CG2 REMARK 470 THR A 723 OG1 CG2 REMARK 470 LEU A 724 CG CD1 CD2 REMARK 470 SER A 725 OG REMARK 470 ASN A 726 CG OD1 ND2 REMARK 470 PHE B 520 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 521 OG REMARK 470 LEU B 522 CG CD1 CD2 REMARK 470 ASP B 523 CG OD1 OD2 REMARK 470 GLN B 524 CG CD OE1 NE2 REMARK 470 GLU B 525 CG CD OE1 OE2 REMARK 470 SER B 526 OG REMARK 470 ILE B 527 CG1 CG2 CD1 REMARK 470 GLU B 528 CG CD OE1 OE2 REMARK 470 HIS B 529 CG ND1 CD2 CE1 NE2 REMARK 470 ASP B 530 CG OD1 OD2 REMARK 470 LEU B 531 CG CD1 CD2 REMARK 470 LYS B 532 CG CD CE NZ REMARK 470 LEU B 533 CG CD1 CD2 REMARK 470 THR B 534 OG1 CG2 REMARK 470 SER B 535 OG REMARK 470 GLU B 536 CG CD OE1 OE2 REMARK 470 GLU B 537 CG CD OE1 OE2 REMARK 470 ILE B 538 CG1 CG2 CD1 REMARK 470 PHE B 539 CG CD1 CD2 CE1 CE2 CZ REMARK 470 HIS B 540 CG ND1 CD2 CE1 NE2 REMARK 470 SER B 541 OG REMARK 470 ASN B 542 CG OD1 ND2 REMARK 470 LYS B 544 CG CD CE NZ REMARK 470 TYR B 545 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE B 546 CG1 CG2 CD1 REMARK 470 PRO B 547 CG CD REMARK 470 PRO B 548 CG CD REMARK 470 MET B 549 CG SD CE REMARK 470 LEU B 550 CG CD1 CD2 REMARK 470 ASN B 551 CG OD1 ND2 REMARK 470 THR B 552 OG1 CG2 REMARK 470 LEU B 553 CG CD1 CD2 REMARK 470 GLN B 555 CG CD OE1 NE2 REMARK 470 HIS B 556 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 557 CG CD1 CD2 REMARK 470 SER B 558 OG REMARK 470 VAL B 559 CG1 CG2 REMARK 470 ARG B 560 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 561 CG CD CE NZ REMARK 470 GLU B 562 CG CD OE1 OE2 REMARK 470 PHE B 563 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 564 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN B 565 CG CD OE1 NE2 REMARK 470 ASN B 566 CG OD1 ND2 REMARK 470 PHE B 567 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B 568 CG CD1 CD2 REMARK 470 THR B 569 OG1 CG2 REMARK 470 PHE B 570 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL B 571 CG1 CG2 REMARK 470 LYS B 573 CG CD CE NZ REMARK 470 ASN B 574 CG OD1 ND2 REMARK 470 PHE B 575 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 576 CG OD1 ND2 REMARK 470 TYR B 577 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 578 CG CD CE NZ REMARK 470 ILE B 579 CG1 CG2 CD1 REMARK 470 SER B 580 OG REMARK 470 PRO B 581 CG CD REMARK 470 GLU B 582 CG CD OE1 OE2 REMARK 470 LEU B 583 CG CD1 CD2 REMARK 470 LYS B 584 CG CD CE NZ REMARK 470 LEU B 585 CG CD1 CD2 REMARK 470 ASP B 586 CG OD1 OD2 REMARK 470 LEU B 587 CG CD1 CD2 REMARK 470 ILE B 588 CG1 CG2 CD1 REMARK 470 GLU B 589 CG CD OE1 OE2 REMARK 470 LYS B 590 CG CD CE NZ REMARK 470 PHE B 591 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B 592 CG CD OE1 OE2 REMARK 470 ILE B 593 CG1 CG2 CD1 REMARK 470 LEU B 594 CG CD1 CD2 REMARK 470 ASN B 595 CG OD1 ND2 REMARK 470 CYS B 596 SG REMARK 470 CYS B 597 SG REMARK 470 ILE B 598 CG1 CG2 CD1 REMARK 470 LYS B 599 CG CD CE NZ REMARK 470 PHE B 600 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 601 CG OD1 ND2 REMARK 470 SER B 602 OG REMARK 470 ILE B 603 CG1 CG2 CD1 REMARK 470 ILE B 604 CG1 CG2 CD1 REMARK 470 ARG B 605 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 606 CG CD OE1 NE2 REMARK 470 SER B 607 OG REMARK 470 ASP B 608 CG OD1 OD2 REMARK 470 VAL B 609 CG1 CG2 REMARK 470 LEU B 610 CG CD1 CD2 REMARK 470 ASN B 611 CG OD1 ND2 REMARK 470 ASP B 612 CG OD1 OD2 REMARK 470 ILE B 613 CG1 CG2 CD1 REMARK 470 TRP B 614 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 614 CZ3 CH2 REMARK 470 GLU B 615 CG CD OE1 OE2 REMARK 470 LYS B 616 CG CD CE NZ REMARK 470 THR B 617 OG1 CG2 REMARK 470 LEU B 618 CG CD1 CD2 REMARK 470 SER B 619 OG REMARK 470 ASN B 620 CG OD1 ND2 REMARK 470 TYR B 621 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN B 622 CG OD1 ND2 REMARK 470 LEU B 623 CG CD1 CD2 REMARK 470 THR B 624 OG1 CG2 REMARK 470 GLN B 625 CG CD OE1 NE2 REMARK 470 ASN B 626 CG OD1 ND2 REMARK 470 GLU B 627 CG CD OE1 OE2 REMARK 470 HIS B 628 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 629 CG CD1 CD2 REMARK 470 THR B 630 OG1 CG2 REMARK 470 THR B 631 OG1 CG2 REMARK 470 LYS B 632 CG CD CE NZ REMARK 470 THR B 633 OG1 CG2 REMARK 470 VAL B 634 CG1 CG2 REMARK 470 VAL B 635 CG1 CG2 REMARK 470 ILE B 636 CG1 CG2 CD1 REMARK 470 ASN B 637 CG OD1 ND2 REMARK 470 SER B 638 OG REMARK 470 PRO B 639 CG CD REMARK 470 ASP B 640 CG OD1 OD2 REMARK 470 VAL B 641 CG1 CG2 REMARK 470 PHE B 642 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO B 643 CG CD REMARK 470 VAL B 644 CG1 CG2 REMARK 470 ILE B 645 CG1 CG2 CD1 REMARK 470 PHE B 646 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 647 CG CD CE NZ REMARK 470 GLN B 648 CG CD OE1 NE2 REMARK 470 PHE B 649 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B 650 CG CD1 CD2 REMARK 470 ASN B 651 CG OD1 ND2 REMARK 470 HIS B 652 CG ND1 CD2 CE1 NE2 REMARK 470 VAL B 653 CG1 CG2 REMARK 470 VAL B 654 CG1 CG2 REMARK 470 PHE B 655 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL B 656 CG1 CG2 REMARK 470 LEU B 657 CG CD1 CD2 REMARK 470 PHE B 658 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO B 659 CG CD REMARK 470 SER B 660 OG REMARK 470 GLN B 661 CG CD OE1 NE2 REMARK 470 ASN B 662 CG OD1 ND2 REMARK 470 GLN B 663 CG CD OE1 NE2 REMARK 470 ASN B 664 CG OD1 ND2 REMARK 470 PHE B 665 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 666 CG CD CE NZ REMARK 470 LEU B 667 CG CD1 CD2 REMARK 470 ASN B 668 CG OD1 ND2 REMARK 470 VAL B 669 CG1 CG2 REMARK 470 THR B 670 OG1 CG2 REMARK 470 ASN B 671 CG OD1 ND2 REMARK 470 LEU B 672 CG CD1 CD2 REMARK 470 ILE B 673 CG1 CG2 CD1 REMARK 470 ASN B 674 CG OD1 ND2 REMARK 470 LEU B 675 CG CD1 CD2 REMARK 470 CYS B 676 SG REMARK 470 PHE B 677 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 678 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP B 679 CG OD1 OD2 REMARK 470 ILE B 681 CG1 CG2 CD1 REMARK 470 LEU B 682 CG CD1 CD2 REMARK 470 GLU B 683 CG CD OE1 OE2 REMARK 470 GLU B 684 CG CD OE1 OE2 REMARK 470 GLU B 686 CG CD OE1 OE2 REMARK 470 LYS B 687 CG CD CE NZ REMARK 470 THR B 688 OG1 CG2 REMARK 470 ILE B 689 CG1 CG2 CD1 REMARK 470 PRO B 707 CG CD REMARK 470 TRP B 708 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 708 CZ3 CH2 REMARK 470 PHE B 709 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE B 710 CG1 CG2 CD1 REMARK 470 ASN B 711 CG OD1 ND2 REMARK 470 PHE B 712 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP B 713 CG OD1 OD2 REMARK 470 TYR B 714 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 715 CG CD1 CD2 REMARK 470 ASN B 716 CG OD1 ND2 REMARK 470 CYS B 717 SG REMARK 470 ILE B 718 CG1 CG2 CD1 REMARK 470 ASN B 719 CG OD1 ND2 REMARK 470 GLN B 720 CG CD OE1 NE2 REMARK 470 CYS B 721 SG REMARK 470 PHE B 722 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 723 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP B 724 CG OD1 OD2 REMARK 470 PHE B 725 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 726 OG1 CG2 REMARK 470 PHE B 727 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS B 729 SG REMARK 470 GLU B 730 CG CD OE1 OE2 REMARK 470 GLU B 731 CG CD OE1 OE2 REMARK 470 GLU B 732 CG CD OE1 OE2 REMARK 470 SER B 734 OG REMARK 470 LEU B 735 CG CD1 CD2 REMARK 470 ASP B 736 CG OD1 OD2 REMARK 470 SER B 737 OG REMARK 470 TYR B 738 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 739 CG CD CE NZ REMARK 470 GLU B 740 CG CD OE1 OE2 REMARK 470 LEU B 742 CG CD1 CD2 REMARK 470 LEU B 743 CG CD1 CD2 REMARK 470 LYS B 744 CG CD CE NZ REMARK 470 ILE B 745 CG1 CG2 CD1 REMARK 470 VAL B 746 CG1 CG2 REMARK 470 LYS B 747 CG CD CE NZ REMARK 470 ILE B 748 CG1 CG2 CD1 REMARK 470 LEU B 749 CG CD1 CD2 REMARK 470 TYR B 750 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR B 751 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN B 752 CG CD OE1 NE2 REMARK 470 PHE B 753 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 754 CG OD1 ND2 REMARK 470 GLN B 755 CG CD OE1 NE2 REMARK 470 PHE B 756 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 757 CG CD CE NZ REMARK 470 ILE B 758 CG1 CG2 CD1 REMARK 470 TRP B 759 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 759 CZ3 CH2 REMARK 470 ILE B 760 CG1 CG2 CD1 REMARK 470 ASN B 761 CG OD1 ND2 REMARK 470 THR B 762 OG1 CG2 REMARK 470 GLN B 763 CG CD OE1 NE2 REMARK 470 PRO B 764 CG CD REMARK 470 VAL B 765 CG1 CG2 REMARK 470 LYS B 766 CG CD CE NZ REMARK 470 SER B 767 OG REMARK 470 VAL B 768 CG1 CG2 REMARK 470 ASN B 769 CG OD1 ND2 REMARK 470 ASN B 771 CG OD1 ND2 REMARK 470 ASP B 772 CG OD1 OD2 REMARK 470 ASN B 773 CG OD1 ND2 REMARK 470 PHE B 774 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE B 775 CG1 CG2 CD1 REMARK 470 ASN B 776 CG OD1 ND2 REMARK 470 ILE B 777 CG1 CG2 CD1 REMARK 470 ASN B 778 CG OD1 ND2 REMARK 470 ASN B 779 CG OD1 ND2 REMARK 470 LEU B 780 CG CD1 CD2 REMARK 470 TYR B 781 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP B 782 CG OD1 OD2 REMARK 470 ASP B 783 CG OD1 OD2 REMARK 470 ASN B 784 CG OD1 ND2 REMARK 470 HIS B 785 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 786 CG CD1 CD2 REMARK 470 ASP B 787 CG OD1 OD2 REMARK 470 TRP B 788 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 788 CZ3 CH2 REMARK 470 ASN B 789 CG OD1 ND2 REMARK 470 HIS B 790 CG ND1 CD2 CE1 NE2 REMARK 470 VAL B 791 CG1 CG2 REMARK 470 LEU B 792 CG CD1 CD2 REMARK 470 CYS B 793 SG REMARK 470 LYS B 794 CG CD CE NZ REMARK 470 VAL B 795 CG1 CG2 REMARK 470 ASN B 796 CG OD1 ND2 REMARK 470 LEU B 797 CG CD1 CD2 REMARK 470 LYS B 798 CG CD CE NZ REMARK 470 GLU B 799 CG CD OE1 OE2 REMARK 470 GLN B 800 CG CD OE1 NE2 REMARK 470 CYS B 801 SG REMARK 470 ILE B 802 CG1 CG2 CD1 REMARK 470 GLN B 803 CG CD OE1 NE2 REMARK 470 ILE B 804 CG1 CG2 CD1 REMARK 470 GLU B 806 CG CD OE1 OE2 REMARK 470 PHE B 807 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 808 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 809 CG CD CE NZ REMARK 470 ASP B 810 CG OD1 OD2 REMARK 470 LEU B 811 CG CD1 CD2 REMARK 470 SER B 812 OG REMARK 470 LEU B 814 CG CD1 CD2 REMARK 470 VAL B 815 CG1 CG2 REMARK 470 GLN B 816 CG CD OE1 NE2 REMARK 470 THR B 817 OG1 CG2 REMARK 470 LEU B 818 CG CD1 CD2 REMARK 470 GLN B 819 CG CD OE1 NE2 REMARK 470 THR B 820 OG1 CG2 REMARK 470 LEU B 821 CG CD1 CD2 REMARK 470 ASP B 822 CG OD1 OD2 REMARK 470 GLN B 823 CG CD OE1 NE2 REMARK 470 ASN B 824 CG OD1 ND2 REMARK 470 ASP B 825 CG OD1 OD2 REMARK 470 SER B 826 OG REMARK 470 THR B 827 OG1 CG2 REMARK 470 THR B 828 OG1 CG2 REMARK 470 VAL B 829 CG1 CG2 REMARK 470 SER B 830 OG REMARK 470 LEU B 831 CG CD1 CD2 REMARK 470 TYR B 832 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 833 CG CD OE1 OE2 REMARK 470 THR B 834 OG1 CG2 REMARK 470 PHE B 835 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 836 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 837 CG OD1 ND2 REMARK 470 GLU B 838 CG CD OE1 OE2 REMARK 470 PHE B 839 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO B 840 CG CD REMARK 470 LYS B 841 CG CD CE NZ REMARK 470 GLU B 842 CG CD OE1 OE2 REMARK 470 PHE B 843 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 844 OG REMARK 470 PHE B 845 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 846 OG1 CG2 REMARK 470 LEU B 847 CG CD1 CD2 REMARK 470 PHE B 848 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B 849 CG CD OE1 OE2 REMARK 470 TYR B 850 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 851 CG CD1 CD2 REMARK 470 ILE B 852 CG1 CG2 CD1 REMARK 470 LYS B 853 CG CD CE NZ REMARK 470 HIS B 854 CG ND1 CD2 CE1 NE2 REMARK 470 GLN B 866 CG CD OE1 NE2 REMARK 470 GLN B 867 CG CD OE1 NE2 REMARK 470 HIS B 868 CG ND1 CD2 CE1 NE2 REMARK 470 ASP B 869 CG OD1 OD2 REMARK 470 VAL B 870 CG1 CG2 REMARK 470 LEU B 871 CG CD1 CD2 REMARK 470 ILE B 872 CG1 CG2 CD1 REMARK 470 GLN B 873 CG CD OE1 NE2 REMARK 470 PHE B 874 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 875 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN B 876 CG CD OE1 NE2 REMARK 470 GLU B 877 CG CD OE1 OE2 REMARK 470 SER B 878 OG REMARK 470 PRO B 880 CG CD REMARK 470 LYS B 881 CG CD CE NZ REMARK 470 TYR B 882 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS B 884 CG ND1 CD2 CE1 NE2 REMARK 470 VAL B 885 CG1 CG2 REMARK 470 TRP B 887 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 887 CZ3 CH2 REMARK 470 ILE B 888 CG1 CG2 CD1 REMARK 470 GLN B 889 CG CD OE1 NE2 REMARK 470 GLN B 890 CG CD OE1 NE2 REMARK 470 ILE B 891 CG1 CG2 CD1 REMARK 470 LEU B 892 CG CD1 CD2 REMARK 470 ASP B 893 CG OD1 OD2 REMARK 470 SER B 895 OG REMARK 470 TYR B 896 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP B 898 CG OD1 OD2 REMARK 470 MET B 900 CG SD CE REMARK 470 ASN B 901 CG OD1 ND2 REMARK 470 THR B 902 OG1 CG2 REMARK 470 LEU B 903 CG CD1 CD2 REMARK 470 LYS B 904 CG CD CE NZ REMARK 470 ASN B 905 CG OD1 ND2 REMARK 470 ILE B 906 CG1 CG2 CD1 REMARK 470 THR B 907 OG1 CG2 REMARK 470 VAL B 908 CG1 CG2 REMARK 470 ASP B 909 CG OD1 OD2 REMARK 470 ASP B 910 CG OD1 OD2 REMARK 470 SER B 911 OG REMARK 470 LYS B 912 CG CD CE NZ REMARK 470 LYS B 913 CG CD CE NZ REMARK 470 GLU B 915 CG CD OE1 OE2 REMARK 470 SER B 916 OG REMARK 470 LEU B 917 CG CD1 CD2 REMARK 470 SER B 918 OG REMARK 470 GLU B 919 CG CD OE1 OE2 REMARK 470 CYS B 920 SG REMARK 470 GLU B 921 CG CD OE1 OE2 REMARK 470 LEU B 922 CG CD1 CD2 REMARK 470 HIS B 923 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 924 CG CD1 CD2 REMARK 470 ASN B 925 CG OD1 ND2 REMARK 470 VAL B 926 CG1 CG2 REMARK 470 LYS B 928 CG CD CE NZ REMARK 470 LEU B 929 CG CD1 CD2 REMARK 470 SER B 930 OG REMARK 470 SER B 931 OG REMARK 470 ILE B 941 CG1 CG2 CD1 REMARK 470 ASN B 942 CG OD1 ND2 REMARK 470 THR B 943 OG1 CG2 REMARK 470 LEU B 944 CG CD1 CD2 REMARK 470 ARG B 945 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 946 CG CD CE NZ REMARK 470 ILE B 947 CG1 CG2 CD1 REMARK 470 GLN B 948 CG CD OE1 NE2 REMARK 470 TYR B 949 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN B 950 CG OD1 ND2 REMARK 470 LEU B 951 CG CD1 CD2 REMARK 470 ASP B 952 CG OD1 OD2 REMARK 470 THR B 953 OG1 CG2 REMARK 470 ILE B 954 CG1 CG2 CD1 REMARK 470 ASP B 955 CG OD1 OD2 REMARK 470 GLU B 957 CG CD OE1 OE2 REMARK 470 LYS B 958 CG CD CE NZ REMARK 470 ASN B 959 CG OD1 ND2 REMARK 470 ILE B 960 CG1 CG2 CD1 REMARK 470 SER B 961 OG REMARK 470 ASN B 962 CG OD1 ND2 REMARK 470 LYS B 963 CG CD CE NZ REMARK 470 LEU B 964 CG CD1 CD2 REMARK 470 LYS B 965 CG CD CE NZ REMARK 470 LYS B 966 CG CD CE NZ REMARK 470 GLU B 968 CG CD OE1 OE2 REMARK 470 VAL B 969 CG1 CG2 REMARK 470 GLN B 970 CG CD OE1 NE2 REMARK 470 ILE B 971 CG1 CG2 CD1 REMARK 470 CYS B 972 SG REMARK 470 LYS B 973 CG CD CE NZ REMARK 470 ARG B 974 CG CD NE CZ NH1 NH2 REMARK 470 PHE B 975 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 976 CG CD CE NZ REMARK 470 ASN B 977 CG OD1 ND2 REMARK 470 SER B 979 OG REMARK 470 ILE B 980 CG1 CG2 CD1 REMARK 470 ARG B 981 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 982 CG CD OE1 OE2 REMARK 470 VAL B 983 CG1 CG2 REMARK 470 PHE B 984 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 985 CG OD1 ND2 REMARK 470 ILE B 986 CG1 CG2 CD1 REMARK 470 LEU B 987 CG CD1 CD2 REMARK 470 VAL B 988 CG1 CG2 REMARK 470 GLU B 989 CG CD OE1 OE2 REMARK 470 GLU B 990 CG CD OE1 OE2 REMARK 470 LEU B 991 CG CD1 CD2 REMARK 470 LYS B 992 CG CD CE NZ REMARK 470 SER B 993 OG REMARK 470 THR B 994 OG1 CG2 REMARK 470 THR B 995 OG1 CG2 REMARK 470 VAL B 996 CG1 CG2 REMARK 470 VAL B 997 CG1 CG2 REMARK 470 ASN B 998 CG OD1 ND2 REMARK 470 LEU B 999 CG CD1 CD2 REMARK 470 SER B1000 OG REMARK 470 ASP B1001 CG OD1 OD2 REMARK 470 LEU B1002 CG CD1 CD2 REMARK 470 VAL B1003 CG1 CG2 REMARK 470 GLU B1004 CG CD OE1 OE2 REMARK 470 LEU B1005 CG CD1 CD2 REMARK 470 TYR B1006 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER B1007 OG REMARK 470 MET B1008 CG SD CE REMARK 470 LEU B1009 CG CD1 CD2 REMARK 470 ASP B1010 CG OD1 OD2 REMARK 470 ASP B1011 CG OD1 OD2 REMARK 470 GLU B1012 CG CD OE1 OE2 REMARK 470 GLU B1013 CG CD OE1 OE2 REMARK 470 SER B1014 OG REMARK 470 LEU B1015 CG CD1 CD2 REMARK 470 PHE B1016 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE B1017 CG1 CG2 CD1 REMARK 470 PRO B1018 CG CD REMARK 470 LEU B1019 CG CD1 CD2 REMARK 470 ARG B1020 CG CD NE CZ NH1 NH2 REMARK 470 ILE B1021 CG1 CG2 CD1 REMARK 470 LEU B1022 CG CD1 CD2 REMARK 470 SER B1023 OG REMARK 470 VAL B1024 CG1 CG2 REMARK 470 ASP B1025 CG OD1 OD2 REMARK 470 ASP B1027 CG OD1 OD2 REMARK 470 LEU B1028 CG CD1 CD2 REMARK 470 LEU B1029 CG CD1 CD2 REMARK 470 ASN B1030 CG OD1 ND2 REMARK 470 PHE B1031 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B1032 CG CD OE1 OE2 REMARK 470 VAL B1033 CG1 CG2 REMARK 470 LYS B1034 CG CD CE NZ REMARK 470 LYS B1035 CG CD CE NZ REMARK 470 PHE B1036 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B1037 CG CD1 CD2 REMARK 470 ASN B1038 CG OD1 ND2 REMARK 470 LEU B1040 CG CD1 CD2 REMARK 470 VAL B1041 CG1 CG2 REMARK 470 TRP B1042 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B1042 CZ3 CH2 REMARK 470 ARG B1043 CG CD NE CZ NH1 NH2 REMARK 470 ARG B1044 CG CD NE CZ NH1 NH2 REMARK 470 ILE B1045 CG1 CG2 CD1 REMARK 470 VAL B1046 CG1 CG2 REMARK 470 LEU B1047 CG CD1 CD2 REMARK 470 LEU B1048 CG CD1 CD2 REMARK 470 ASN B1049 CG OD1 ND2 REMARK 470 SER B1051 OG REMARK 470 ASN B1052 CG OD1 ND2 REMARK 470 GLU B1053 CG CD OE1 OE2 REMARK 470 ASP B1055 CG OD1 OD2 REMARK 470 LYS B1056 CG CD CE NZ REMARK 470 LEU B1057 CG CD1 CD2 REMARK 470 LEU B1058 CG CD1 CD2 REMARK 470 GLN B1059 CG CD OE1 NE2 REMARK 470 HIS B1060 CG ND1 CD2 CE1 NE2 REMARK 470 ILE B1061 CG1 CG2 CD1 REMARK 470 VAL B1062 CG1 CG2 REMARK 470 LYS B1063 CG CD CE NZ REMARK 470 ARG B1064 CG CD NE CZ NH1 NH2 REMARK 470 VAL B1065 CG1 CG2 REMARK 470 PHE B1066 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP B1067 CG OD1 OD2 REMARK 470 GLU B1068 CG CD OE1 OE2 REMARK 470 GLU B1069 CG CD OE1 OE2 REMARK 470 LEU B1070 CG CD1 CD2 REMARK 470 PRO B1071 CG CD REMARK 470 LYS B1072 CG CD CE NZ REMARK 470 ASN B1073 CG OD1 ND2 REMARK 470 ASN B1074 CG OD1 ND2 REMARK 470 ASP B1075 CG OD1 OD2 REMARK 470 PHE B1076 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO B1077 CG CD REMARK 470 LEU B1078 CG CD1 CD2 REMARK 470 PRO B1079 CG CD REMARK 470 SER B1080 OG REMARK 470 VAL B1081 CG1 CG2 REMARK 470 ASP B1082 CG OD1 OD2 REMARK 470 LEU B1083 CG CD1 CD2 REMARK 470 LEU B1084 CG CD1 CD2 REMARK 470 CYS B1085 SG REMARK 470 ASP B1086 CG OD1 OD2 REMARK 470 LYS B1087 CG CD CE NZ REMARK 470 SER B1088 OG REMARK 470 LEU B1089 CG CD1 CD2 REMARK 470 LEU B1090 CG CD1 CD2 REMARK 470 THR B1091 OG1 CG2 REMARK 470 PRO B1092 CG CD REMARK 470 GLU B1093 CG CD OE1 OE2 REMARK 470 TYR B1094 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE B1095 CG1 CG2 CD1 REMARK 470 SER B1096 OG REMARK 470 GLU B1097 CG CD OE1 OE2 REMARK 470 THR B1098 OG1 CG2 REMARK 470 TYR B1099 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG B1101 CG CD NE CZ NH1 NH2 REMARK 470 PHE B1102 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO B1103 CG CD REMARK 470 ILE B1104 CG1 CG2 CD1 REMARK 470 ASP B1105 CG OD1 OD2 REMARK 470 GLN B1106 CG CD OE1 NE2 REMARK 470 ASN B1107 CG OD1 ND2 REMARK 470 ILE B1109 CG1 CG2 CD1 REMARK 470 ARG B1110 CG CD NE CZ NH1 NH2 REMARK 470 GLU B1111 CG CD OE1 OE2 REMARK 470 GLU B1112 CG CD OE1 OE2 REMARK 470 ILE B1113 CG1 CG2 CD1 REMARK 470 TYR B1114 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B1115 CG CD OE1 OE2 REMARK 470 GLU B1116 CG CD OE1 OE2 REMARK 470 ILE B1117 CG1 CG2 CD1 REMARK 470 SER B1118 OG REMARK 470 GLN B1119 CG CD OE1 NE2 REMARK 470 VAL B1120 CG1 CG2 REMARK 470 GLU B1121 CG CD OE1 OE2 REMARK 470 THR B1122 OG1 CG2 REMARK 470 LEU B1123 CG CD1 CD2 REMARK 470 ASN B1124 CG OD1 ND2 REMARK 470 SER B1125 OG REMARK 470 ASP B1126 CG OD1 OD2 REMARK 470 ASN B1127 CG OD1 ND2 REMARK 470 SER B1128 OG REMARK 470 LEU B1129 CG CD1 CD2 REMARK 470 GLU B1130 CG CD OE1 OE2 REMARK 470 ILE B1131 CG1 CG2 CD1 REMARK 470 LYS B1132 CG CD CE NZ REMARK 470 LEU B1133 CG CD1 CD2 REMARK 470 HIS B1134 CG ND1 CD2 CE1 NE2 REMARK 470 SER B1135 OG REMARK 470 THR B1136 OG1 CG2 REMARK 470 ILE B1137 CG1 CG2 CD1 REMARK 470 SER B1139 OG REMARK 470 VAL B1140 CG1 CG2 REMARK 470 LYS B1142 CG CD CE NZ REMARK 470 GLU B1143 CG CD OE1 OE2 REMARK 470 LYS B1144 CG CD CE NZ REMARK 470 ASN B1145 CG OD1 ND2 REMARK 470 TYR B1146 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR B1147 OG1 CG2 REMARK 470 ILE B1148 CG1 CG2 CD1 REMARK 470 ASN B1149 CG OD1 ND2 REMARK 470 TYR B1150 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B1151 CG CD OE1 OE2 REMARK 470 THR B1152 OG1 CG2 REMARK 470 ASN B1153 CG OD1 ND2 REMARK 470 THR B1154 OG1 CG2 REMARK 470 VAL B1155 CG1 CG2 REMARK 470 GLU B1156 CG CD OE1 OE2 REMARK 470 TYR B1157 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 LEU C 2 CG CD1 CD2 REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 LEU C 4 CG CD1 CD2 REMARK 470 VAL C 5 CG1 CG2 REMARK 470 GLU C 6 CG CD OE1 OE2 REMARK 470 THR C 7 OG1 CG2 REMARK 470 LEU C 11 CG CD1 CD2 REMARK 470 VAL C 12 CG1 CG2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 SER C 17 OG REMARK 470 LEU C 18 CG CD1 CD2 REMARK 470 ARG C 19 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 20 CG CD1 CD2 REMARK 470 SER C 21 OG REMARK 470 CYS C 22 SG REMARK 470 VAL C 23 CG1 CG2 REMARK 470 SER C 25 OG REMARK 470 TRP C 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 36 CZ3 CH2 REMARK 470 PHE C 37 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG C 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 39 CG CD OE1 NE2 REMARK 470 PRO C 41 CG CD REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 GLU C 44 CG CD OE1 OE2 REMARK 470 ARG C 45 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 46 CG CD OE1 OE2 REMARK 470 PHE C 47 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL C 48 CG1 CG2 REMARK 470 ASP C 59 CG OD1 OD2 REMARK 470 TYR C 60 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP C 62 CG OD1 OD2 REMARK 470 SER C 63 OG REMARK 470 VAL C 64 CG1 CG2 REMARK 470 LYS C 65 CG CD CE NZ REMARK 470 ARG C 67 CG CD NE CZ NH1 NH2 REMARK 470 PHE C 68 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR C 69 OG1 CG2 REMARK 470 ILE C 70 CG1 CG2 CD1 REMARK 470 SER C 71 OG REMARK 470 ARG C 72 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 73 CG OD1 ND2 REMARK 470 ASN C 74 CG OD1 ND2 REMARK 470 ASP C 75 CG OD1 OD2 REMARK 470 LYS C 76 CG CD CE NZ REMARK 470 ASN C 77 CG OD1 ND2 REMARK 470 THR C 78 OG1 CG2 REMARK 470 VAL C 79 CG1 CG2 REMARK 470 TYR C 80 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU C 81 CG CD1 CD2 REMARK 470 GLN C 82 CG CD OE1 NE2 REMARK 470 MET C 83 CG SD CE REMARK 470 ASN C 84 CG OD1 ND2 REMARK 470 ASN C 85 CG OD1 ND2 REMARK 470 LEU C 86 CG CD1 CD2 REMARK 470 ILE C 87 CG1 CG2 CD1 REMARK 470 PRO C 88 CG CD REMARK 470 GLU C 89 CG CD OE1 OE2 REMARK 470 ASP C 90 CG OD1 OD2 REMARK 470 THR C 91 OG1 CG2 REMARK 470 VAL C 93 CG1 CG2 REMARK 470 TYR C 94 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR C 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS C 96 SG REMARK 470 GLN C 123 CG CD OE1 NE2 REMARK 470 THR C 125 OG1 CG2 REMARK 470 GLN C 126 CG CD OE1 NE2 REMARK 470 VAL C 127 CG1 CG2 REMARK 470 THR C 128 OG1 CG2 REMARK 470 VAL C 129 CG1 CG2 REMARK 470 SER C 130 OG REMARK 470 SER C 131 OG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ASN B 662 CB LYS B 666 1.83 REMARK 500 CB ASN C 73 O ASN C 77 1.84 REMARK 500 O GLU B 537 O SER B 541 1.94 REMARK 500 O ASN B 662 N LYS B 666 1.97 REMARK 500 O ILE A 298 CB LEU A 302 1.99 REMARK 500 O GLN B 663 N LEU B 667 2.08 REMARK 500 O LEU C 18 CB GLN C 82 2.18 REMARK 500 O ASN B 601 N ARG B 605 2.18 REMARK 500 O LEU B 657 O SER B 660 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO B 659 C - N - CA ANGL. DEV. = 34.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 86 -62.38 -137.56 REMARK 500 THR A 141 -79.09 -69.64 REMARK 500 TRP A 144 73.41 58.89 REMARK 500 ASP A 285 -17.88 -40.39 REMARK 500 VAL A 308 -39.82 -170.66 REMARK 500 ILE A 314 -55.17 -121.29 REMARK 500 ILE A 429 -32.79 -133.44 REMARK 500 THR A 434 59.89 -112.43 REMARK 500 LEU A 436 -110.06 55.98 REMARK 500 GLU A 443 -72.82 -118.52 REMARK 500 LEU A 449 20.68 -79.14 REMARK 500 LEU A 452 89.67 -65.89 REMARK 500 GLU A 453 -80.61 -112.35 REMARK 500 THR A 464 -156.56 -88.09 REMARK 500 LEU A 468 -160.80 -165.75 REMARK 500 ARG A 469 -113.88 57.70 REMARK 500 ASN A 495 35.26 -151.12 REMARK 500 LEU A 522 46.94 -96.16 REMARK 500 LEU A 538 -141.04 59.87 REMARK 500 ASN A 540 -143.21 60.39 REMARK 500 ASN A 554 51.08 -155.80 REMARK 500 ILE A 555 -164.68 -77.99 REMARK 500 LYS A 566 39.42 -88.37 REMARK 500 VAL A 604 -89.42 54.80 REMARK 500 LEU A 607 -14.15 69.14 REMARK 500 SER A 608 -127.20 61.24 REMARK 500 SER A 640 -150.59 62.62 REMARK 500 SER A 641 -73.53 -120.16 REMARK 500 LEU A 678 63.10 -65.42 REMARK 500 PHE A 683 -62.37 -92.36 REMARK 500 ALA A 695 33.02 -85.68 REMARK 500 TYR A 702 -111.45 52.24 REMARK 500 LEU A 703 53.27 -159.86 REMARK 500 LEU A 724 -36.51 -139.14 REMARK 500 SER B 541 138.04 -175.64 REMARK 500 LEU B 550 -131.29 55.28 REMARK 500 THR B 552 97.74 -32.84 REMARK 500 ALA B 572 34.88 -76.77 REMARK 500 ASN B 574 -109.28 55.79 REMARK 500 LYS B 578 -109.61 55.12 REMARK 500 ASP B 608 -78.03 64.50 REMARK 500 ASN B 626 21.33 -142.73 REMARK 500 GLU B 627 -123.16 53.64 REMARK 500 THR B 630 -132.87 57.07 REMARK 500 ASN B 664 -71.22 -62.69 REMARK 500 TYR B 714 74.60 -152.71 REMARK 500 LEU B 715 -39.34 -135.04 REMARK 500 ASP B 724 -63.20 -91.77 REMARK 500 GLU B 732 -127.93 57.04 REMARK 500 ASP B 736 106.45 -160.51 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 6X02 A 1 726 UNP P52891 NUP84_YEAST 1 726 DBREF 6X02 B 521 1157 UNP P36161 NU133_YEAST 521 1157 DBREF 6X02 C 1 131 PDB 6X02 6X02 1 131 SEQADV 6X02 MET B 515 UNP P36161 EXPRESSION TAG SEQADV 6X02 ALA B 516 UNP P36161 EXPRESSION TAG SEQADV 6X02 ASP B 517 UNP P36161 EXPRESSION TAG SEQADV 6X02 PRO B 518 UNP P36161 EXPRESSION TAG SEQADV 6X02 GLY B 519 UNP P36161 EXPRESSION TAG SEQADV 6X02 PHE B 520 UNP P36161 EXPRESSION TAG SEQADV 6X02 ILE B 1021 UNP P36161 LEU 1021 CONFLICT SEQADV 6X02 ASP B 1027 UNP P36161 ASN 1027 CONFLICT SEQRES 1 A 726 MET GLU LEU SER PRO THR TYR GLN THR GLU ARG PHE THR SEQRES 2 A 726 LYS PHE SER ASP THR LEU LYS GLU PHE LYS ILE GLU GLN SEQRES 3 A 726 ASN ASN GLU GLN ASN PRO ILE ASP PRO PHE ASN ILE ILE SEQRES 4 A 726 ARG GLU PHE ARG SER ALA ALA GLY GLN LEU ALA LEU ASP SEQRES 5 A 726 LEU ALA ASN SER GLY ASP GLU SER ASN VAL ILE SER SER SEQRES 6 A 726 LYS ASP TRP GLU LEU GLU ALA ARG PHE TRP HIS LEU VAL SEQRES 7 A 726 GLU LEU LEU LEU VAL PHE ARG ASN ALA ASP LEU ASP LEU SEQRES 8 A 726 ASP GLU MET GLU LEU HIS PRO TYR ASN SER ARG GLY LEU SEQRES 9 A 726 PHE GLU LYS LYS LEU MET GLN ASP ASN LYS GLN LEU TYR SEQRES 10 A 726 GLN ILE TRP ILE VAL MET VAL TRP LEU LYS GLU ASN THR SEQRES 11 A 726 TYR VAL MET GLU ARG PRO LYS ASN VAL PRO THR SER LYS SEQRES 12 A 726 TRP LEU ASN SER ILE THR SER GLY GLY LEU LYS SER CYS SEQRES 13 A 726 ASP LEU ASP PHE PRO LEU ARG GLU ASN THR ASN VAL LEU SEQRES 14 A 726 ASP VAL LYS ASP LYS GLU GLU ASP HIS ILE PHE PHE LYS SEQRES 15 A 726 TYR ILE TYR GLU LEU ILE LEU ALA GLY ALA ILE ASP GLU SEQRES 16 A 726 ALA LEU GLU GLU ALA LYS LEU SER ASP ASN ILE SER ILE SEQRES 17 A 726 CYS MET ILE LEU CYS GLY ILE GLN GLU TYR LEU ASN PRO SEQRES 18 A 726 VAL ILE ASP THR GLN ILE ALA ASN GLU PHE ASN THR GLN SEQRES 19 A 726 GLN GLY ILE LYS LYS HIS SER LEU TRP ARG ARG THR VAL SEQRES 20 A 726 TYR SER LEU SER GLN GLN ALA GLY LEU ASP PRO TYR GLU SEQRES 21 A 726 ARG ALA ILE TYR SER TYR LEU SER GLY ALA ILE PRO ASN SEQRES 22 A 726 GLN GLU VAL LEU GLN TYR SER ASP TRP GLU SER ASP LEU SEQRES 23 A 726 HIS ILE HIS LEU ASN GLN ILE LEU GLN THR GLU ILE GLU SEQRES 24 A 726 ASN TYR LEU LEU GLU ASN ASN GLN VAL GLY THR ASP GLU SEQRES 25 A 726 LEU ILE LEU PRO LEU PRO SER HIS ALA LEU THR VAL GLN SEQRES 26 A 726 GLU VAL LEU ASN ARG VAL ALA SER ARG HIS PRO SER GLU SEQRES 27 A 726 SER GLU HIS PRO ILE ARG VAL LEU MET ALA SER VAL ILE SEQRES 28 A 726 LEU ASP SER LEU PRO SER VAL ILE HIS SER SER VAL GLU SEQRES 29 A 726 MET LEU LEU ASP VAL VAL LYS GLY THR GLU ALA SER ASN SEQRES 30 A 726 ASP ILE ILE ASP LYS PRO TYR LEU LEU ARG ILE VAL THR SEQRES 31 A 726 HIS LEU ALA ILE CYS LEU ASP ILE ILE ASN PRO GLY SER SEQRES 32 A 726 VAL GLU GLU VAL ASP LYS SER LYS LEU ILE THR THR TYR SEQRES 33 A 726 ILE SER LEU LEU LYS LEU GLN GLY LEU TYR GLU ASN ILE SEQRES 34 A 726 PRO ILE TYR ALA THR PHE LEU ASN GLU SER ASP CYS LEU SEQRES 35 A 726 GLU ALA CYS SER PHE ILE LEU SER SER LEU GLU ASP PRO SEQRES 36 A 726 GLN VAL ARG LYS LYS GLN ILE GLU THR ILE ASN PHE LEU SEQRES 37 A 726 ARG LEU PRO ALA SER ASN ILE LEU ARG ARG THR THR GLN SEQRES 38 A 726 ARG VAL PHE ASP GLU THR GLU GLN GLU TYR SER PRO SER SEQRES 39 A 726 ASN GLU ILE SER ILE SER PHE ASP VAL ASN ASN ILE ASP SEQRES 40 A 726 MET HIS LEU ILE TYR GLY VAL GLU TRP LEU ILE GLU GLY SEQRES 41 A 726 LYS LEU TYR VAL ASP ALA VAL HIS SER ILE ILE ALA LEU SEQRES 42 A 726 SER ARG ARG PHE LEU LEU ASN GLY ARG VAL LYS ALA LEU SEQRES 43 A 726 GLU GLN PHE MET GLU ARG ASN ASN ILE GLY GLU ILE CYS SEQRES 44 A 726 LYS ASN TYR GLU LEU GLU LYS ILE ALA ASP ASN ILE SER SEQRES 45 A 726 LYS ASP GLU ASN GLU ASP GLN PHE LEU GLU GLU ILE THR SEQRES 46 A 726 GLN TYR GLU HIS LEU ILE LYS GLY ILE ARG GLU TYR GLU SEQRES 47 A 726 GLU TRP GLN LYS SER VAL SER LEU LEU SER SER GLU SER SEQRES 48 A 726 ASN ILE PRO THR LEU ILE GLU LYS LEU GLN GLY PHE SER SEQRES 49 A 726 LYS ASP THR PHE GLU LEU ILE LYS THR PHE LEU VAL ASP SEQRES 50 A 726 LEU THR SER SER ASN PHE ALA ASP SER ALA ASP TYR GLU SEQRES 51 A 726 ILE LEU TYR GLU ILE ARG ALA LEU TYR THR PRO PHE LEU SEQRES 52 A 726 LEU MET GLU LEU HIS LYS LYS LEU VAL GLU ALA ALA LYS SEQRES 53 A 726 LEU LEU LYS ILE PRO LYS PHE ILE SER GLU ALA LEU ALA SEQRES 54 A 726 PHE THR SER LEU VAL ALA ASN GLU ASN ASP LYS ILE TYR SEQRES 55 A 726 LEU LEU PHE GLN SER SER GLY LYS LEU LYS GLU TYR LEU SEQRES 56 A 726 ASP LEU VAL ALA ARG THR ALA THR LEU SER ASN SEQRES 1 B 643 MET ALA ASP PRO GLY PHE SER LEU ASP GLN GLU SER ILE SEQRES 2 B 643 GLU HIS ASP LEU LYS LEU THR SER GLU GLU ILE PHE HIS SEQRES 3 B 643 SER ASN GLY LYS TYR ILE PRO PRO MET LEU ASN THR LEU SEQRES 4 B 643 GLY GLN HIS LEU SER VAL ARG LYS GLU PHE PHE GLN ASN SEQRES 5 B 643 PHE LEU THR PHE VAL ALA LYS ASN PHE ASN TYR LYS ILE SEQRES 6 B 643 SER PRO GLU LEU LYS LEU ASP LEU ILE GLU LYS PHE GLU SEQRES 7 B 643 ILE LEU ASN CYS CYS ILE LYS PHE ASN SER ILE ILE ARG SEQRES 8 B 643 GLN SER ASP VAL LEU ASN ASP ILE TRP GLU LYS THR LEU SEQRES 9 B 643 SER ASN TYR ASN LEU THR GLN ASN GLU HIS LEU THR THR SEQRES 10 B 643 LYS THR VAL VAL ILE ASN SER PRO ASP VAL PHE PRO VAL SEQRES 11 B 643 ILE PHE LYS GLN PHE LEU ASN HIS VAL VAL PHE VAL LEU SEQRES 12 B 643 PHE PRO SER GLN ASN GLN ASN PHE LYS LEU ASN VAL THR SEQRES 13 B 643 ASN LEU ILE ASN LEU CYS PHE TYR ASP GLY ILE LEU GLU SEQRES 14 B 643 GLU GLY GLU LYS THR ILE ARG TYR GLU LEU LEU GLU LEU SEQRES 15 B 643 ASP PRO MET GLU VAL ASP THR SER LYS LEU PRO TRP PHE SEQRES 16 B 643 ILE ASN PHE ASP TYR LEU ASN CYS ILE ASN GLN CYS PHE SEQRES 17 B 643 PHE ASP PHE THR PHE ALA CYS GLU GLU GLU GLY SER LEU SEQRES 18 B 643 ASP SER TYR LYS GLU GLY LEU LEU LYS ILE VAL LYS ILE SEQRES 19 B 643 LEU TYR TYR GLN PHE ASN GLN PHE LYS ILE TRP ILE ASN SEQRES 20 B 643 THR GLN PRO VAL LYS SER VAL ASN ALA ASN ASP ASN PHE SEQRES 21 B 643 ILE ASN ILE ASN ASN LEU TYR ASP ASP ASN HIS LEU ASP SEQRES 22 B 643 TRP ASN HIS VAL LEU CYS LYS VAL ASN LEU LYS GLU GLN SEQRES 23 B 643 CYS ILE GLN ILE ALA GLU PHE TYR LYS ASP LEU SER GLY SEQRES 24 B 643 LEU VAL GLN THR LEU GLN THR LEU ASP GLN ASN ASP SER SEQRES 25 B 643 THR THR VAL SER LEU TYR GLU THR PHE PHE ASN GLU PHE SEQRES 26 B 643 PRO LYS GLU PHE SER PHE THR LEU PHE GLU TYR LEU ILE SEQRES 27 B 643 LYS HIS LYS LYS LEU ASN ASP LEU ILE PHE ARG PHE PRO SEQRES 28 B 643 GLN GLN HIS ASP VAL LEU ILE GLN PHE PHE GLN GLU SER SEQRES 29 B 643 ALA PRO LYS TYR GLY HIS VAL ALA TRP ILE GLN GLN ILE SEQRES 30 B 643 LEU ASP GLY SER TYR ALA ASP ALA MET ASN THR LEU LYS SEQRES 31 B 643 ASN ILE THR VAL ASP ASP SER LYS LYS GLY GLU SER LEU SEQRES 32 B 643 SER GLU CYS GLU LEU HIS LEU ASN VAL ALA LYS LEU SER SEQRES 33 B 643 SER LEU LEU VAL GLU LYS ASP ASN LEU ASP ILE ASN THR SEQRES 34 B 643 LEU ARG LYS ILE GLN TYR ASN LEU ASP THR ILE ASP ALA SEQRES 35 B 643 GLU LYS ASN ILE SER ASN LYS LEU LYS LYS GLY GLU VAL SEQRES 36 B 643 GLN ILE CYS LYS ARG PHE LYS ASN GLY SER ILE ARG GLU SEQRES 37 B 643 VAL PHE ASN ILE LEU VAL GLU GLU LEU LYS SER THR THR SEQRES 38 B 643 VAL VAL ASN LEU SER ASP LEU VAL GLU LEU TYR SER MET SEQRES 39 B 643 LEU ASP ASP GLU GLU SER LEU PHE ILE PRO LEU ARG ILE SEQRES 40 B 643 LEU SER VAL ASP GLY ASP LEU LEU ASN PHE GLU VAL LYS SEQRES 41 B 643 LYS PHE LEU ASN ALA LEU VAL TRP ARG ARG ILE VAL LEU SEQRES 42 B 643 LEU ASN ALA SER ASN GLU GLY ASP LYS LEU LEU GLN HIS SEQRES 43 B 643 ILE VAL LYS ARG VAL PHE ASP GLU GLU LEU PRO LYS ASN SEQRES 44 B 643 ASN ASP PHE PRO LEU PRO SER VAL ASP LEU LEU CYS ASP SEQRES 45 B 643 LYS SER LEU LEU THR PRO GLU TYR ILE SER GLU THR TYR SEQRES 46 B 643 GLY ARG PHE PRO ILE ASP GLN ASN ALA ILE ARG GLU GLU SEQRES 47 B 643 ILE TYR GLU GLU ILE SER GLN VAL GLU THR LEU ASN SER SEQRES 48 B 643 ASP ASN SER LEU GLU ILE LYS LEU HIS SER THR ILE GLY SEQRES 49 B 643 SER VAL ALA LYS GLU LYS ASN TYR THR ILE ASN TYR GLU SEQRES 50 B 643 THR ASN THR VAL GLU TYR SEQRES 1 C 131 GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 C 131 ALA GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 C 131 ARG THR PHE THR SER TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 C 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 C 131 ARG LEU ALA SER GLY THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 C 131 GLY ARG PHE THR ILE SER ARG ASN ASN ASP LYS ASN THR SEQRES 7 C 131 VAL TYR LEU GLN MET ASN ASN LEU ILE PRO GLU ASP THR SEQRES 8 C 131 ALA VAL TYR TYR CYS ALA ALA LEU GLN ALA LEU ARG PHE SEQRES 9 C 131 SER LEU PRO ILE ALA MET ALA THR MET LYS ASN GLY ARG SEQRES 10 C 131 ALA ASP SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 C 131 SER HELIX 1 AA1 GLU A 10 GLN A 26 1 17 HELIX 2 AA2 PHE A 36 GLU A 41 1 6 HELIX 3 AA3 GLU A 41 LEU A 53 1 13 HELIX 4 AA4 ASP A 58 SER A 60 5 3 HELIX 5 AA5 ASN A 61 ARG A 85 1 25 HELIX 6 AA6 LEU A 116 GLU A 128 1 13 HELIX 7 AA7 LYS A 172 ILE A 188 1 17 HELIX 8 AA8 LEU A 189 GLY A 191 5 3 HELIX 9 AA9 ALA A 192 SER A 203 1 12 HELIX 10 AB1 ASN A 205 SER A 207 5 3 HELIX 11 AB2 ILE A 208 THR A 225 1 18 HELIX 12 AB3 ARG A 245 SER A 251 1 7 HELIX 13 AB4 ASP A 257 GLY A 269 1 13 HELIX 14 AB5 ASN A 273 LEU A 277 5 5 HELIX 15 AB6 GLU A 283 ASP A 285 5 3 HELIX 16 AB7 LEU A 286 ASN A 306 1 21 HELIX 17 AB8 THR A 323 HIS A 335 1 13 HELIX 18 AB9 HIS A 335 GLU A 340 1 6 HELIX 19 AC1 VAL A 345 VAL A 350 1 6 HELIX 20 AC2 LYS A 382 ASN A 400 1 19 HELIX 21 AC3 GLU A 405 LEU A 420 1 16 HELIX 22 AC4 ILE A 429 ALA A 433 5 5 HELIX 23 AC5 PHE A 447 SER A 451 5 5 HELIX 24 AC6 GLN A 456 ILE A 462 1 7 HELIX 25 AC7 ARG A 469 LEU A 476 1 8 HELIX 26 AC8 LEU A 476 GLN A 481 1 6 HELIX 27 AC9 ASP A 485 SER A 492 5 8 HELIX 28 AD1 ASP A 502 ASP A 507 1 6 HELIX 29 AD2 MET A 508 LEU A 510 5 3 HELIX 30 AD3 ILE A 511 LEU A 517 1 7 HELIX 31 AD4 ILE A 530 SER A 534 5 5 HELIX 32 AD5 ARG A 542 ASN A 553 1 12 HELIX 33 AD6 GLY A 556 LEU A 564 1 9 HELIX 34 AD7 GLU A 575 LYS A 602 1 28 HELIX 35 AD8 SER A 611 ASP A 637 1 27 HELIX 36 AD9 LEU A 638 SER A 640 5 3 HELIX 37 AE1 SER A 646 TYR A 659 1 14 HELIX 38 AE2 THR A 660 LYS A 669 1 10 HELIX 39 AE3 LYS A 670 VAL A 672 5 3 HELIX 40 AE4 GLU A 673 LEU A 677 5 5 HELIX 41 AE5 ILE A 680 PHE A 690 1 11 HELIX 42 AE6 LEU A 693 GLU A 697 5 5 HELIX 43 AE7 LEU A 711 ARG A 720 1 10 HELIX 44 AE8 THR A 721 LEU A 724 5 4 HELIX 45 AE9 PHE B 520 PHE B 539 1 20 HELIX 46 AF1 LEU B 553 ALA B 572 1 20 HELIX 47 AF2 ILE B 579 ILE B 593 1 15 HELIX 48 AF3 LEU B 594 ASP B 608 1 15 HELIX 49 AF4 ASP B 608 GLU B 627 1 20 HELIX 50 AF5 VAL B 641 LEU B 657 1 17 HELIX 51 AF6 GLN B 661 PHE B 677 1 17 HELIX 52 AF7 TRP B 708 ASP B 713 1 6 HELIX 53 AF8 CYS B 717 GLU B 730 1 14 HELIX 54 AF9 ASP B 736 VAL B 746 1 11 HELIX 55 AG1 LYS B 747 ALA B 770 1 24 HELIX 56 AG2 ILE B 775 GLU B 799 1 25 HELIX 57 AG3 GLN B 803 SER B 812 1 10 HELIX 58 AG4 VAL B 815 ASN B 824 1 10 HELIX 59 AG5 SER B 830 PHE B 839 1 10 HELIX 60 AG6 PRO B 840 GLU B 842 5 3 HELIX 61 AG7 SER B 844 GLU B 849 1 6 HELIX 62 AG8 TYR B 850 LYS B 853 5 4 HELIX 63 AG9 ASP B 869 LEU B 871 5 3 HELIX 64 AH1 ILE B 872 GLU B 877 1 6 HELIX 65 AH2 HIS B 884 GLN B 889 1 6 HELIX 66 AH3 SER B 895 ASP B 910 1 16 HELIX 67 AH4 GLU B 915 SER B 931 1 17 HELIX 68 AH5 ASN B 942 GLY B 967 1 26 HELIX 69 AH6 GLU B 982 SER B 993 1 12 HELIX 70 AH7 SER B 993 ASN B 998 1 6 HELIX 71 AH8 ASP B 1001 MET B 1008 1 8 HELIX 72 AH9 ASP B 1011 ILE B 1017 1 7 HELIX 73 AI1 ILE B 1017 ASP B 1025 1 9 HELIX 74 AI2 ASN B 1030 ASN B 1052 1 23 HELIX 75 AI3 LEU B 1057 GLU B 1068 1 12 HELIX 76 AI4 SER B 1080 CYS B 1085 1 6 HELIX 77 AI5 THR B 1091 TYR B 1099 1 9 HELIX 78 AI6 ASP B 1105 ASN B 1124 1 20 HELIX 79 AI7 ASN B 1127 ALA B 1141 1 15 HELIX 80 AI8 ILE C 87 THR C 91 5 5 SHEET 1 AA1 3 GLN C 3 THR C 7 0 SHEET 2 AA1 3 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA1 3 LEU C 81 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 1 AA2 5 GLY C 10 GLN C 13 0 SHEET 2 AA2 5 THR C 125 SER C 130 1 O THR C 128 N VAL C 12 SHEET 3 AA2 5 ALA C 92 TYR C 95 -1 N TYR C 94 O THR C 125 SHEET 4 AA2 5 PHE C 37 GLN C 39 -1 N GLN C 39 O VAL C 93 SHEET 5 AA2 5 GLU C 46 PHE C 47 -1 O GLU C 46 N ARG C 38 CRYST1 72.257 287.650 297.375 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 0.013839 0.000000 0.000000 0.00000 SCALE2 0.000000 0.003476 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003363 0.00000