HEADER LIGASE 28-JUN-16 5KNL
TITLE CRYSTAL STRUCTURE OF S. POMBE UBIQUITIN E1 (UBA1) IN COMPLEX WITH
TITLE 2 UBC15 AND UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: POLY(A)+ RNA TRANSPORT PROTEIN 3;
COMPND 5 EC: 6.2.1.45;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UBIQUITIN;
COMPND 9 CHAIN: B, E;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 15;
COMPND 14 CHAIN: C, F;
COMPND 15 SYNONYM: E2 UBIQUITIN-CONJUGATING ENZYME 15,UBIQUITIN CARRIER PROTEIN
COMPND 16 15,UBIQUITIN-PROTEIN LIGASE 15;
COMPND 17 EC: 2.3.2.23;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC
SOURCE 3 24843);
SOURCE 4 ORGANISM_COMMON: FISSION YEAST;
SOURCE 5 ORGANISM_TAXID: 284812;
SOURCE 6 STRAIN: 972 / ATCC 24843;
SOURCE 7 GENE: PTR3, SPBC1604.21C, SPBC211.09;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSMT3;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 14 ORGANISM_COMMON: YEAST;
SOURCE 15 ORGANISM_TAXID: 84753;
SOURCE 16 GENE: PAN0_008C3613;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-28;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC
SOURCE 23 24843);
SOURCE 24 ORGANISM_COMMON: FISSION YEAST;
SOURCE 25 ORGANISM_TAXID: 284812;
SOURCE 26 STRAIN: 972 / ATCC 24843;
SOURCE 27 GENE: UBC15, SPBC1105.09;
SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 30 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PET-29
KEYWDS UBIQUITIN, E1, E2, UBA1, UBC15, CONFORMATIONAL CHANGE, THIOESTER,
KEYWDS 2 ADENYLATION, THIOESTER TRANSFER (TRANSTHIOESTERIFICATION), ATP-
KEYWDS 3 BINDING, UBIQUITIN E2 BINDING, UBIQUITINATION, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.OLSEN,Z.LV,L.YUAN,K.WILLIAMS
REVDAT 5 27-SEP-23 5KNL 1 REMARK
REVDAT 4 25-DEC-19 5KNL 1 REMARK
REVDAT 3 20-SEP-17 5KNL 1 REMARK
REVDAT 2 01-MAR-17 5KNL 1 JRNL
REVDAT 1 15-FEB-17 5KNL 0
JRNL AUTH Z.LV,K.A.RICKMAN,L.YUAN,K.WILLIAMS,S.P.SELVAM,A.N.WOOSLEY,
JRNL AUTH 2 P.H.HOWE,B.OGRETMEN,A.SMOGORZEWSKA,S.K.OLSEN
JRNL TITL S. POMBE UBA1-UBC15 STRUCTURE REVEALS A NOVEL REGULATORY
JRNL TITL 2 MECHANISM OF UBIQUITIN E2 ACTIVITY.
JRNL REF MOL. CELL V. 65 699 2017
JRNL REFN ISSN 1097-4164
JRNL PMID 28162934
JRNL DOI 10.1016/J.MOLCEL.2017.01.008
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.530
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 108284
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10828
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 28.3162 - 7.7172 0.97 3254 362 0.1437 0.1629
REMARK 3 2 7.7172 - 6.1460 0.98 3311 368 0.1562 0.1980
REMARK 3 3 6.1460 - 5.3751 0.98 3288 366 0.1647 0.2104
REMARK 3 4 5.3751 - 4.8864 0.98 3273 362 0.1476 0.1854
REMARK 3 5 4.8864 - 4.5377 0.99 3307 368 0.1410 0.1787
REMARK 3 6 4.5377 - 4.2711 0.99 3321 369 0.1523 0.1801
REMARK 3 7 4.2711 - 4.0579 0.99 3287 366 0.1607 0.1953
REMARK 3 8 4.0579 - 3.8817 0.99 3328 368 0.1680 0.2004
REMARK 3 9 3.8817 - 3.7326 0.98 3292 366 0.1902 0.2233
REMARK 3 10 3.7326 - 3.6040 0.99 3303 368 0.1955 0.2527
REMARK 3 11 3.6040 - 3.4916 0.98 3300 366 0.1995 0.2374
REMARK 3 12 3.4916 - 3.3919 0.98 3269 363 0.2182 0.2659
REMARK 3 13 3.3919 - 3.3028 0.98 3314 369 0.2304 0.2685
REMARK 3 14 3.3028 - 3.2223 0.98 3292 365 0.2452 0.2639
REMARK 3 15 3.2223 - 3.1491 0.97 3233 360 0.2551 0.3043
REMARK 3 16 3.1491 - 3.0822 0.97 3279 363 0.2645 0.2937
REMARK 3 17 3.0822 - 3.0206 0.97 3277 365 0.2657 0.2971
REMARK 3 18 3.0206 - 2.9637 0.97 3238 359 0.2846 0.3248
REMARK 3 19 2.9637 - 2.9108 0.96 3239 361 0.2924 0.3232
REMARK 3 20 2.9108 - 2.8615 0.96 3194 354 0.2924 0.3288
REMARK 3 21 2.8615 - 2.8154 0.96 3229 359 0.2893 0.3214
REMARK 3 22 2.8154 - 2.7721 0.96 3217 357 0.2928 0.3490
REMARK 3 23 2.7721 - 2.7314 0.96 3220 359 0.2995 0.3439
REMARK 3 24 2.7314 - 2.6929 0.96 3215 357 0.3117 0.3319
REMARK 3 25 2.6929 - 2.6566 0.95 3118 346 0.3110 0.3387
REMARK 3 26 2.6566 - 2.6221 0.95 3295 366 0.3274 0.3551
REMARK 3 27 2.6221 - 2.5893 0.95 3145 350 0.3260 0.3517
REMARK 3 28 2.5893 - 2.5582 0.95 3176 353 0.3418 0.3858
REMARK 3 29 2.5582 - 2.5284 0.93 3175 352 0.3542 0.3859
REMARK 3 30 2.5284 - 2.5001 0.93 3067 341 0.3546 0.3781
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.780
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 : 0.003 19751
REMARK 3 ANGLE : 0.699 26745
REMARK 3 CHIRALITY : 0.027 2965
REMARK 3 PLANARITY : 0.003 3482
REMARK 3 DIHEDRAL : 11.994 7409
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 39
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 14 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1116 -95.7338 1.2257
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.1747
REMARK 3 T33: 0.3464 T12: 0.0229
REMARK 3 T13: -0.0741 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.2355 L22: 0.0711
REMARK 3 L33: 0.2071 L12: 0.0016
REMARK 3 L13: -0.0206 L23: 0.1096
REMARK 3 S TENSOR
REMARK 3 S11: 0.1853 S12: -0.1692 S13: -0.3904
REMARK 3 S21: 0.1198 S22: -0.0142 S23: -0.2145
REMARK 3 S31: 0.1228 S32: 0.1822 S33: 0.7179
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5963 -96.9714 0.7390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2962 T22: 0.8976
REMARK 3 T33: 0.5949 T12: 0.0648
REMARK 3 T13: -0.0709 T23: -0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 0.0187 L22: 0.0024
REMARK 3 L33: 0.0029 L12: -0.0039
REMARK 3 L13: 0.0054 L23: 0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0606 S12: -0.0300 S13: -0.0318
REMARK 3 S21: -0.0247 S22: -0.0595 S23: -0.0645
REMARK 3 S31: -0.0076 S32: -0.0844 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8735-112.4070 -3.6621
REMARK 3 T TENSOR
REMARK 3 T11: 0.2831 T22: 0.1824
REMARK 3 T33: 0.5918 T12: 0.0447
REMARK 3 T13: -0.1682 T23: 0.1144
REMARK 3 L TENSOR
REMARK 3 L11: 0.0644 L22: 0.1329
REMARK 3 L33: 0.4494 L12: -0.0362
REMARK 3 L13: 0.1252 L23: -0.0334
REMARK 3 S TENSOR
REMARK 3 S11: 0.1383 S12: -0.0474 S13: -0.2366
REMARK 3 S21: 0.0038 S22: -0.0167 S23: 0.0247
REMARK 3 S31: 0.2701 S32: -0.1921 S33: 0.1250
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 538 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1154 -95.0603 -19.6930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0828 T22: 0.1952
REMARK 3 T33: 0.2652 T12: 0.0453
REMARK 3 T13: 0.0474 T23: -0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 0.2698 L22: 0.1998
REMARK 3 L33: 0.4332 L12: 0.0542
REMARK 3 L13: 0.3072 L23: -0.0733
REMARK 3 S TENSOR
REMARK 3 S11: 0.1189 S12: 0.1092 S13: -0.2884
REMARK 3 S21: -0.1904 S22: 0.0879 S23: -0.1898
REMARK 3 S31: 0.1871 S32: 0.3602 S33: 1.2561
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 539 THROUGH 753 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4906 -67.0306 -16.9409
REMARK 3 T TENSOR
REMARK 3 T11: 0.2382 T22: 0.0361
REMARK 3 T33: 0.0176 T12: 0.2023
REMARK 3 T13: 0.0597 T23: -0.1939
REMARK 3 L TENSOR
REMARK 3 L11: 0.2699 L22: 0.2131
REMARK 3 L33: 0.1135 L12: -0.1950
REMARK 3 L13: 0.0366 L23: -0.0157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: -0.0069 S13: 0.1621
REMARK 3 S21: 0.0219 S22: 0.0433 S23: -0.1832
REMARK 3 S31: -0.1874 S32: -0.1419 S33: -0.1705
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 754 THROUGH 855 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1755 -61.5856 -14.0224
REMARK 3 T TENSOR
REMARK 3 T11: 0.2936 T22: 0.1431
REMARK 3 T33: 0.2714 T12: 0.0813
REMARK 3 T13: -0.0500 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 0.0457 L22: 0.2616
REMARK 3 L33: 0.0700 L12: -0.0075
REMARK 3 L13: 0.0500 L23: -0.0410
REMARK 3 S TENSOR
REMARK 3 S11: -0.1696 S12: -0.0953 S13: 0.2169
REMARK 3 S21: -0.0402 S22: 0.0010 S23: -0.2519
REMARK 3 S31: -0.1802 S32: -0.0775 S33: -0.1776
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 856 THROUGH 1012 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4136 -92.0513 -44.8619
REMARK 3 T TENSOR
REMARK 3 T11: 0.4434 T22: 0.2907
REMARK 3 T33: 0.1577 T12: 0.0837
REMARK 3 T13: -0.0312 T23: -0.1028
REMARK 3 L TENSOR
REMARK 3 L11: 0.2478 L22: 0.0508
REMARK 3 L33: 0.0284 L12: 0.0426
REMARK 3 L13: -0.0023 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: 0.1480 S12: 0.3134 S13: -0.1439
REMARK 3 S21: -0.1566 S22: -0.0101 S23: -0.1054
REMARK 3 S31: 0.1178 S32: -0.0021 S33: 0.3920
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3831-106.9410 -13.2167
REMARK 3 T TENSOR
REMARK 3 T11: 0.3150 T22: 0.1436
REMARK 3 T33: 0.3964 T12: -0.1668
REMARK 3 T13: -0.0564 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 0.0143 L22: 0.0524
REMARK 3 L33: 0.0125 L12: 0.0255
REMARK 3 L13: 0.0035 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: 0.0017 S13: -0.0248
REMARK 3 S21: 0.0261 S22: -0.0326 S23: -0.0020
REMARK 3 S31: 0.0089 S32: 0.0124 S33: -0.0413
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1274-115.2908 -24.5958
REMARK 3 T TENSOR
REMARK 3 T11: 0.7130 T22: 0.7509
REMARK 3 T33: 0.7321 T12: -0.0812
REMARK 3 T13: -0.1072 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 0.0002
REMARK 3 L33: 0.0038 L12: 0.0002
REMARK 3 L13: -0.0012 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: -0.0052 S13: 0.0034
REMARK 3 S21: -0.0090 S22: -0.0042 S23: 0.0025
REMARK 3 S31: 0.0008 S32: 0.0007 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6510-104.0922 -22.9983
REMARK 3 T TENSOR
REMARK 3 T11: 0.4143 T22: 0.4123
REMARK 3 T33: 0.7060 T12: -0.0199
REMARK 3 T13: 0.0300 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 0.0011 L22: 0.0031
REMARK 3 L33: 0.0013 L12: 0.0002
REMARK 3 L13: -0.0013 L23: -0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: -0.0012 S13: -0.0187
REMARK 3 S21: 0.0148 S22: 0.0252 S23: -0.0014
REMARK 3 S31: -0.0146 S32: -0.0092 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0080 -98.7682 -23.6359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3302 T22: 0.1775
REMARK 3 T33: 0.4331 T12: 0.0474
REMARK 3 T13: -0.0802 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.0024 L22: 0.0006
REMARK 3 L33: -0.0001 L12: 0.0010
REMARK 3 L13: -0.0008 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0223 S13: -0.0103
REMARK 3 S21: 0.0212 S22: -0.0148 S23: 0.0041
REMARK 3 S31: -0.0352 S32: -0.0395 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1845-110.6601 -27.4678
REMARK 3 T TENSOR
REMARK 3 T11: 0.4408 T22: 0.2603
REMARK 3 T33: 0.4425 T12: 0.0392
REMARK 3 T13: -0.1328 T23: -0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: 0.0025
REMARK 3 L33: 0.0034 L12: 0.0007
REMARK 3 L13: 0.0005 L23: -0.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: 0.0011 S13: -0.0334
REMARK 3 S21: -0.0389 S22: -0.0177 S23: -0.0375
REMARK 3 S31: 0.0249 S32: 0.0005 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5100-117.8618 -21.0536
REMARK 3 T TENSOR
REMARK 3 T11: 0.5825 T22: 0.1303
REMARK 3 T33: 0.4897 T12: 0.0121
REMARK 3 T13: -0.1713 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 0.0069 L22: 0.0488
REMARK 3 L33: 0.0377 L12: 0.0083
REMARK 3 L13: -0.0154 L23: -0.0330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: -0.0079 S13: -0.0456
REMARK 3 S21: 0.0082 S22: -0.0063 S23: 0.0175
REMARK 3 S31: -0.0036 S32: -0.0116 S33: -0.0063
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4862 -98.5564 -18.9881
REMARK 3 T TENSOR
REMARK 3 T11: 0.2312 T22: 0.2662
REMARK 3 T33: 0.3639 T12: 0.0029
REMARK 3 T13: -0.1023 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.0108 L22: 0.0036
REMARK 3 L33: 0.0039 L12: -0.0033
REMARK 3 L13: 0.0081 L23: -0.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: -0.0205 S13: 0.0119
REMARK 3 S21: 0.0345 S22: 0.0579 S23: -0.0149
REMARK 3 S31: 0.0464 S32: -0.0200 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2656 -87.7243 -43.0175
REMARK 3 T TENSOR
REMARK 3 T11: 0.5073 T22: 0.3490
REMARK 3 T33: 0.3511 T12: -0.0372
REMARK 3 T13: -0.0204 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0093
REMARK 3 L33: 0.0074 L12: -0.0037
REMARK 3 L13: -0.0015 L23: 0.0105
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.0240 S13: -0.0110
REMARK 3 S21: -0.0302 S22: 0.0224 S23: 0.0200
REMARK 3 S31: 0.0251 S32: 0.0931 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7831 -80.2019 -46.4155
REMARK 3 T TENSOR
REMARK 3 T11: 0.4284 T22: 0.3466
REMARK 3 T33: 0.3293 T12: -0.0442
REMARK 3 T13: -0.0275 T23: 0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 0.0034 L22: 0.0021
REMARK 3 L33: 0.0064 L12: -0.0015
REMARK 3 L13: -0.0047 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0369 S12: 0.0001 S13: 0.0115
REMARK 3 S21: -0.0245 S22: -0.0393 S23: -0.0695
REMARK 3 S31: -0.0620 S32: -0.0144 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 37 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3075 -75.5568 -34.0142
REMARK 3 T TENSOR
REMARK 3 T11: 0.2070 T22: 0.4030
REMARK 3 T33: 0.1850 T12: -0.0118
REMARK 3 T13: -0.0180 T23: 0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 0.0044 L22: 0.4166
REMARK 3 L33: 0.0191 L12: -0.0234
REMARK 3 L13: -0.0041 L23: 0.0915
REMARK 3 S TENSOR
REMARK 3 S11: 0.1185 S12: -0.0305 S13: -0.0820
REMARK 3 S21: -0.0863 S22: 0.0387 S23: -0.1227
REMARK 3 S31: -0.0440 S32: -0.2267 S33: 0.0526
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 100 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2189 -87.7669 -14.9433
REMARK 3 T TENSOR
REMARK 3 T11: 1.0040 T22: 0.8538
REMARK 3 T33: 0.8534 T12: 0.1247
REMARK 3 T13: 0.1293 T23: -0.0749
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 0.0009
REMARK 3 L33: 0.0072 L12: 0.0010
REMARK 3 L13: 0.0002 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: 0.0107 S13: 0.0021
REMARK 3 S21: 0.0332 S22: 0.0176 S23: -0.0150
REMARK 3 S31: -0.0089 S32: 0.0020 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 110 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3026 -84.6867 -33.2910
REMARK 3 T TENSOR
REMARK 3 T11: 0.4034 T22: 0.5011
REMARK 3 T33: 0.3271 T12: -0.0621
REMARK 3 T13: -0.0642 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 0.0052 L22: 0.0073
REMARK 3 L33: 0.0106 L12: 0.0058
REMARK 3 L13: -0.0031 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: -0.0304 S13: 0.0028
REMARK 3 S21: 0.0021 S22: 0.0210 S23: 0.0361
REMARK 3 S31: 0.0597 S32: 0.0421 S33: 0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 130 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7435 -70.4846 -22.3641
REMARK 3 T TENSOR
REMARK 3 T11: 0.2454 T22: 0.5161
REMARK 3 T33: 0.1323 T12: -0.0489
REMARK 3 T13: 0.0067 T23: 0.0698
REMARK 3 L TENSOR
REMARK 3 L11: 0.0227 L22: 0.0096
REMARK 3 L33: 0.0499 L12: 0.0112
REMARK 3 L13: 0.0321 L23: 0.0118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: -0.0177 S13: 0.0109
REMARK 3 S21: 0.0625 S22: 0.0273 S23: 0.0165
REMARK 3 S31: -0.0341 S32: 0.0061 S33: 0.0047
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 149 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2569 -62.9477 -39.1769
REMARK 3 T TENSOR
REMARK 3 T11: 0.3560 T22: 0.6089
REMARK 3 T33: 0.3156 T12: 0.0062
REMARK 3 T13: -0.0907 T23: 0.0724
REMARK 3 L TENSOR
REMARK 3 L11: 0.0041 L22: 0.0016
REMARK 3 L33: 0.0021 L12: 0.0028
REMARK 3 L13: 0.0015 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: -0.0207 S13: 0.0130
REMARK 3 S21: -0.0579 S22: -0.0131 S23: 0.0234
REMARK 3 S31: -0.0423 S32: -0.0241 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 14 THROUGH 538 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9818 -65.7939 21.7614
REMARK 3 T TENSOR
REMARK 3 T11: 0.1379 T22: 0.1562
REMARK 3 T33: 0.1030 T12: -0.0529
REMARK 3 T13: 0.0226 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 0.3246 L22: 0.3403
REMARK 3 L33: 0.4139 L12: -0.1698
REMARK 3 L13: 0.1631 L23: 0.0848
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: 0.0975 S13: 0.0028
REMARK 3 S21: 0.0065 S22: -0.0162 S23: 0.0205
REMARK 3 S31: -0.0854 S32: 0.1362 S33: -0.0784
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 539 THROUGH 752 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1227 -97.5585 45.6358
REMARK 3 T TENSOR
REMARK 3 T11: 0.2322 T22: 0.1728
REMARK 3 T33: 0.2382 T12: -0.0916
REMARK 3 T13: -0.0879 T23: 0.0846
REMARK 3 L TENSOR
REMARK 3 L11: 0.1146 L22: 0.3387
REMARK 3 L33: 0.3016 L12: 0.1119
REMARK 3 L13: 0.0270 L23: -0.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.0901 S12: -0.0654 S13: -0.1395
REMARK 3 S21: 0.0055 S22: 0.0394 S23: 0.0430
REMARK 3 S31: 0.1669 S32: -0.0121 S33: 0.6186
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 753 THROUGH 904 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6186 -87.3677 38.4328
REMARK 3 T TENSOR
REMARK 3 T11: 0.2498 T22: 0.1093
REMARK 3 T33: 0.1812 T12: -0.1240
REMARK 3 T13: -0.0279 T23: 0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 0.1153 L22: 0.1418
REMARK 3 L33: 0.2189 L12: 0.0353
REMARK 3 L13: 0.0014 L23: 0.0348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.0102 S13: -0.0645
REMARK 3 S21: 0.0848 S22: 0.0909 S23: 0.0660
REMARK 3 S31: 0.0270 S32: 0.0480 S33: 0.3349
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 905 THROUGH 1012 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9891 -76.5963 61.2158
REMARK 3 T TENSOR
REMARK 3 T11: 0.3817 T22: 0.6111
REMARK 3 T33: 0.2782 T12: -0.1172
REMARK 3 T13: -0.1151 T23: 0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 0.4266 L22: 0.1418
REMARK 3 L33: 0.1181 L12: -0.2332
REMARK 3 L13: -0.2124 L23: 0.1291
REMARK 3 S TENSOR
REMARK 3 S11: -0.2059 S12: -0.2819 S13: 0.0427
REMARK 3 S21: 0.2529 S22: 0.0081 S23: -0.0157
REMARK 3 S31: -0.1165 S32: 0.1594 S33: -0.1328
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 7 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7592 -54.4906 43.8018
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.2515
REMARK 3 T33: 0.2697 T12: -0.0072
REMARK 3 T13: -0.0715 T23: -0.2271
REMARK 3 L TENSOR
REMARK 3 L11: 0.0195 L22: 0.0344
REMARK 3 L33: 0.0305 L12: 0.0257
REMARK 3 L13: 0.0227 L23: 0.0318
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: -0.0052 S13: 0.0130
REMARK 3 S21: -0.0021 S22: 0.0018 S23: 0.0059
REMARK 3 S31: -0.0098 S32: -0.0293 S33: 0.0130
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2561 -60.4368 43.5742
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.3568
REMARK 3 T33: 0.2852 T12: 0.0027
REMARK 3 T13: -0.0123 T23: -0.1939
REMARK 3 L TENSOR
REMARK 3 L11: 0.0025 L22: 0.0034
REMARK 3 L33: 0.0027 L12: 0.0027
REMARK 3 L13: -0.0029 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.0401 S13: 0.0303
REMARK 3 S21: -0.0108 S22: -0.0028 S23: 0.0272
REMARK 3 S31: 0.0321 S32: -0.0398 S33: -0.0025
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 17 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0251 -49.2472 55.4067
REMARK 3 T TENSOR
REMARK 3 T11: 0.9612 T22: 0.9698
REMARK 3 T33: 0.9097 T12: -0.0093
REMARK 3 T13: 0.0830 T23: -0.2115
REMARK 3 L TENSOR
REMARK 3 L11: 0.0376 L22: 0.0001
REMARK 3 L33: 0.0028 L12: -0.0019
REMARK 3 L13: 0.0060 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.0038 S13: -0.0030
REMARK 3 S21: 0.0103 S22: -0.0091 S23: 0.0092
REMARK 3 S31: 0.0049 S32: -0.0075 S33: -0.0003
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 23 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2412 -60.4127 54.1890
REMARK 3 T TENSOR
REMARK 3 T11: 0.7269 T22: 0.8561
REMARK 3 T33: 0.6305 T12: 0.0000
REMARK 3 T13: 0.1558 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0005
REMARK 3 L33: 0.0023 L12: -0.0003
REMARK 3 L13: -0.0007 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.0148 S13: -0.0250
REMARK 3 S21: 0.0145 S22: 0.0094 S23: 0.0213
REMARK 3 S31: -0.0123 S32: -0.0368 S33: -0.0000
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 34 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9651 -65.7329 49.2372
REMARK 3 T TENSOR
REMARK 3 T11: 0.3738 T22: 0.4140
REMARK 3 T33: 0.2288 T12: -0.1974
REMARK 3 T13: 0.1153 T23: -0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 0.0038 L22: 0.0005
REMARK 3 L33: 0.0014 L12: 0.0009
REMARK 3 L13: -0.0012 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: -0.0319 S13: 0.0059
REMARK 3 S21: -0.0075 S22: 0.0094 S23: 0.0287
REMARK 3 S31: -0.0044 S32: -0.0354 S33: -0.0000
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 45 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2474 -53.9625 48.1197
REMARK 3 T TENSOR
REMARK 3 T11: 0.3351 T22: 0.0952
REMARK 3 T33: 0.2633 T12: 0.0170
REMARK 3 T13: -0.0072 T23: -0.1292
REMARK 3 L TENSOR
REMARK 3 L11: 0.0042 L22: 0.0123
REMARK 3 L33: 0.0003 L12: -0.0072
REMARK 3 L13: 0.0008 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.0018 S13: 0.0190
REMARK 3 S21: -0.0023 S22: 0.0052 S23: -0.0068
REMARK 3 S31: -0.0120 S32: 0.0033 S33: 0.0239
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 57 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2521 -47.0006 45.9584
REMARK 3 T TENSOR
REMARK 3 T11: 0.7696 T22: 0.4247
REMARK 3 T33: 0.5875 T12: 0.0876
REMARK 3 T13: -0.3340 T23: -0.1575
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0053
REMARK 3 L33: 0.0029 L12: -0.0002
REMARK 3 L13: 0.0023 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: 0.0041 S13: -0.0119
REMARK 3 S21: 0.0496 S22: -0.0056 S23: -0.0026
REMARK 3 S31: -0.0214 S32: -0.0194 S33: 0.0000
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 66 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8747 -58.8424 41.6438
REMARK 3 T TENSOR
REMARK 3 T11: 0.3262 T22: 0.3654
REMARK 3 T33: 0.3611 T12: 0.0708
REMARK 3 T13: -0.0163 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.0029 L22: 0.0244
REMARK 3 L33: 0.0040 L12: -0.0065
REMARK 3 L13: 0.0017 L23: -0.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.0305 S13: -0.0060
REMARK 3 S21: 0.0032 S22: -0.0288 S23: 0.0056
REMARK 3 S31: -0.0212 S32: -0.0109 S33: -0.0001
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 71 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5557 -73.9550 38.5870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2834 T22: 0.2884
REMARK 3 T33: 0.1708 T12: -0.0621
REMARK 3 T13: 0.1150 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.0025 L22: 0.1059
REMARK 3 L33: 0.0077 L12: -0.0173
REMARK 3 L13: -0.0043 L23: 0.0284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: -0.0351 S13: -0.0071
REMARK 3 S21: -0.0114 S22: -0.0414 S23: -0.0126
REMARK 3 S31: 0.0065 S32: 0.0047 S33: -0.0230
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5611 -76.9674 60.9253
REMARK 3 T TENSOR
REMARK 3 T11: 0.4484 T22: 0.5619
REMARK 3 T33: 0.3815 T12: -0.1263
REMARK 3 T13: -0.0036 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 0.0084 L22: 0.0046
REMARK 3 L33: 0.0022 L12: 0.0053
REMARK 3 L13: 0.0035 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: 0.0149 S13: -0.0350
REMARK 3 S21: 0.0181 S22: -0.0585 S23: 0.0188
REMARK 3 S31: 0.0358 S32: 0.0076 S33: -0.0000
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 18 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0690 -84.9293 69.9861
REMARK 3 T TENSOR
REMARK 3 T11: 0.3808 T22: 0.3894
REMARK 3 T33: 0.2231 T12: -0.0445
REMARK 3 T13: -0.0674 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 0.0031 L22: 0.0034
REMARK 3 L33: 0.0001 L12: -0.0032
REMARK 3 L13: -0.0000 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: -0.0294 S13: -0.0299
REMARK 3 S21: -0.0249 S22: 0.0682 S23: -0.0081
REMARK 3 S31: 0.0385 S32: -0.0265 S33: 0.0001
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 37 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0352 -90.5561 67.5231
REMARK 3 T TENSOR
REMARK 3 T11: 0.3377 T22: 0.5577
REMARK 3 T33: 0.3486 T12: -0.0829
REMARK 3 T13: -0.0224 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 0.0375 L22: 0.0343
REMARK 3 L33: 0.0196 L12: -0.0026
REMARK 3 L13: 0.0085 L23: 0.0265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0138 S12: -0.1892 S13: -0.0649
REMARK 3 S21: -0.0351 S22: 0.0562 S23: -0.0029
REMARK 3 S31: -0.0676 S32: -0.0530 S33: 0.0012
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 95 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9486 -82.8869 65.6124
REMARK 3 T TENSOR
REMARK 3 T11: 0.3574 T22: 0.5004
REMARK 3 T33: 0.3850 T12: 0.0266
REMARK 3 T13: -0.0013 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.0044 L22: 0.0031
REMARK 3 L33: 0.0053 L12: -0.0024
REMARK 3 L13: -0.0058 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: -0.1398 S13: 0.0542
REMARK 3 S21: 0.0040 S22: -0.0102 S23: 0.0648
REMARK 3 S31: 0.0144 S32: -0.0599 S33: 0.0000
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 139 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8788-101.7495 76.5807
REMARK 3 T TENSOR
REMARK 3 T11: 0.3903 T22: 0.8332
REMARK 3 T33: 0.5057 T12: -0.2242
REMARK 3 T13: -0.0208 T23: 0.2391
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0707
REMARK 3 L33: 0.0054 L12: -0.0169
REMARK 3 L13: -0.0067 L23: 0.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.0856 S13: -0.0406
REMARK 3 S21: 0.1267 S22: -0.0548 S23: -0.0526
REMARK 3 S31: 0.0608 S32: -0.1738 S33: -0.0030
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 5KNL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 8.0-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108289
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 4II2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.0-8.5, 0.3-0.4 M
REMARK 280 LITHIUM SULFATE, 15-18% W/V POLYETHYLENE GLYCOL 8000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 SER A 12
REMARK 465 ASN A 13
REMARK 465 GLY A 764
REMARK 465 ILE A 765
REMARK 465 LYS A 766
REMARK 465 ILE A 767
REMARK 465 GLN A 768
REMARK 465 VAL A 769
REMARK 465 ASN A 770
REMARK 465 GLU A 771
REMARK 465 ASN A 772
REMARK 465 GLU A 773
REMARK 465 GLU A 774
REMARK 465 ALA A 775
REMARK 465 PRO A 776
REMARK 465 GLU A 777
REMARK 465 THR A 778
REMARK 465 ALA A 779
REMARK 465 ALA A 780
REMARK 465 ASN A 781
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 HIS C 172
REMARK 465 HIS C 173
REMARK 465 HIS C 174
REMARK 465 HIS C 175
REMARK 465 SER D 12
REMARK 465 GLY D 764
REMARK 465 ILE D 765
REMARK 465 LYS D 766
REMARK 465 ILE D 767
REMARK 465 GLN D 768
REMARK 465 VAL D 769
REMARK 465 ASN D 770
REMARK 465 GLU D 771
REMARK 465 ASN D 772
REMARK 465 GLU D 773
REMARK 465 GLU D 774
REMARK 465 ALA D 775
REMARK 465 PRO D 776
REMARK 465 GLU D 777
REMARK 465 THR D 778
REMARK 465 ALA D 779
REMARK 465 ALA D 780
REMARK 465 ASN D 781
REMARK 465 LYS D 782
REMARK 465 ASP D 783
REMARK 465 LYS D 784
REMARK 465 GLN D 785
REMARK 465 GLU D 786
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 ASP F 100
REMARK 465 LYS F 101
REMARK 465 TYR F 102
REMARK 465 GLY F 103
REMARK 465 TYR F 104
REMARK 465 GLU F 105
REMARK 465 ASP F 106
REMARK 465 ALA F 107
REMARK 465 GLY F 108
REMARK 465 HIS F 172
REMARK 465 HIS F 173
REMARK 465 HIS F 174
REMARK 465 HIS F 175
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 LYS A 782 CG CD CE NZ
REMARK 470 HIS C 170 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 171 CG ND1 CD2 CE1 NE2
REMARK 470 ASP F 99 CG OD1 OD2
REMARK 470 HIS F 171 CG ND1 CD2 CE1 NE2
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 HG CYS A 593 SG CYS C 90 1.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 16 93.55 -65.19
REMARK 500 LYS A 46 -158.95 -86.80
REMARK 500 ASP A 68 85.68 -161.86
REMARK 500 SER A 79 -15.45 -155.79
REMARK 500 ASP A 176 -8.04 -154.12
REMARK 500 GLU A 198 109.94 -51.10
REMARK 500 GLU A 214 18.60 59.50
REMARK 500 ASP A 281 108.93 -160.32
REMARK 500 HIS A 305 28.45 -143.01
REMARK 500 SER A 375 19.40 59.42
REMARK 500 PHE A 377 149.73 74.74
REMARK 500 ASP A 463 118.09 -168.32
REMARK 500 PHE A 521 57.65 -100.41
REMARK 500 ALA A 535 50.45 -141.58
REMARK 500 LEU A 562 103.70 -163.06
REMARK 500 LEU A 575 -62.90 -142.06
REMARK 500 ASN A 597 -20.34 -142.23
REMARK 500 LYS A 618 -59.41 -139.60
REMARK 500 THR A 640 51.39 -117.75
REMARK 500 VAL A 656 -52.23 -133.97
REMARK 500 ASN A 679 -76.23 -131.35
REMARK 500 SER A 696 49.59 -74.10
REMARK 500 THR A 697 11.61 -147.83
REMARK 500 ASP A 743 107.67 -54.17
REMARK 500 ASP A 783 95.11 -161.98
REMARK 500 GLU A 786 75.04 -60.40
REMARK 500 LYS A 788 47.37 -93.72
REMARK 500 MET A 906 103.53 -168.23
REMARK 500 GLU A 938 -32.27 -134.11
REMARK 500 ALA A 998 70.52 -60.72
REMARK 500 ASN A 999 -34.62 -156.93
REMARK 500 PRO A1006 153.33 -48.02
REMARK 500 ARG B 33 28.72 -150.82
REMARK 500 GLU B 34 -32.01 -156.55
REMARK 500 PRO C 2 -177.89 -67.20
REMARK 500 GLN C 18 35.91 -91.78
REMARK 500 LYS C 19 -60.97 -123.80
REMARK 500 ASN C 20 70.79 -118.66
REMARK 500 ASP C 47 -24.95 72.10
REMARK 500 ASP C 99 -154.05 -73.03
REMARK 500 ASP C 100 159.12 69.64
REMARK 500 ARG C 110 -146.02 -90.72
REMARK 500 ASN C 148 72.46 -152.30
REMARK 500 HIS C 170 75.95 -62.75
REMARK 500 THR D 14 76.59 -118.03
REMARK 500 ASP D 16 92.01 -66.83
REMARK 500 ASP D 68 85.41 -161.60
REMARK 500 SER D 79 -16.56 -155.78
REMARK 500 ASP D 176 -8.41 -153.80
REMARK 500 GLU D 214 18.82 59.65
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER F 135 PRO F 136 -30.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 201
DBREF 5KNL A 13 1012 UNP O94609 UBA1_SCHPO 13 1012
DBREF1 5KNL B 1 76 UNP A0A081CFF0_PSEA2
DBREF2 5KNL B A0A081CFF0 30 105
DBREF 5KNL C 1 167 UNP Q9Y818 UBC15_SCHPO 1 167
DBREF 5KNL D 13 1012 UNP O94609 UBA1_SCHPO 13 1012
DBREF1 5KNL E 1 76 UNP A0A081CFF0_PSEA2
DBREF2 5KNL E A0A081CFF0 30 105
DBREF 5KNL F 1 167 UNP Q9Y818 UBC15_SCHPO 1 167
SEQADV 5KNL SER A 12 UNP O94609 EXPRESSION TAG
SEQADV 5KNL MET B -19 UNP A0A081CFF INITIATING METHIONINE
SEQADV 5KNL GLY B -18 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER B -17 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER B -16 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -15 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -14 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -13 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -12 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -11 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B -10 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER B -9 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER B -8 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL GLY B -7 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL LEU B -6 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL VAL B -5 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL PRO B -4 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL ARG B -3 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL GLY B -2 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER B -1 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS B 0 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL ARG B 6 UNP A0A081CFF LYS 35 ENGINEERED MUTATION
SEQADV 5KNL ARG B 11 UNP A0A081CFF LYS 40 ENGINEERED MUTATION
SEQADV 5KNL ARG B 27 UNP A0A081CFF LYS 56 ENGINEERED MUTATION
SEQADV 5KNL ARG B 29 UNP A0A081CFF LYS 58 ENGINEERED MUTATION
SEQADV 5KNL ARG B 33 UNP A0A081CFF LYS 62 ENGINEERED MUTATION
SEQADV 5KNL ARG B 48 UNP A0A081CFF LYS 77 ENGINEERED MUTATION
SEQADV 5KNL ALA B 57 UNP A0A081CFF SER 86 ENGINEERED MUTATION
SEQADV 5KNL ARG B 63 UNP A0A081CFF LYS 92 ENGINEERED MUTATION
SEQADV 5KNL LEU C 168 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL GLU C 169 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 170 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 171 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 172 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 173 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 174 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS C 175 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL SER D 12 UNP O94609 EXPRESSION TAG
SEQADV 5KNL MET E -19 UNP A0A081CFF INITIATING METHIONINE
SEQADV 5KNL GLY E -18 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER E -17 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER E -16 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -15 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -14 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -13 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -12 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -11 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E -10 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER E -9 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER E -8 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL GLY E -7 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL LEU E -6 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL VAL E -5 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL PRO E -4 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL ARG E -3 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL GLY E -2 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL SER E -1 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL HIS E 0 UNP A0A081CFF EXPRESSION TAG
SEQADV 5KNL ARG E 6 UNP A0A081CFF LYS 35 ENGINEERED MUTATION
SEQADV 5KNL ARG E 11 UNP A0A081CFF LYS 40 ENGINEERED MUTATION
SEQADV 5KNL ARG E 27 UNP A0A081CFF LYS 56 ENGINEERED MUTATION
SEQADV 5KNL ARG E 29 UNP A0A081CFF LYS 58 ENGINEERED MUTATION
SEQADV 5KNL ARG E 33 UNP A0A081CFF LYS 62 ENGINEERED MUTATION
SEQADV 5KNL ARG E 48 UNP A0A081CFF LYS 77 ENGINEERED MUTATION
SEQADV 5KNL ALA E 57 UNP A0A081CFF SER 86 ENGINEERED MUTATION
SEQADV 5KNL ARG E 63 UNP A0A081CFF LYS 92 ENGINEERED MUTATION
SEQADV 5KNL LEU F 168 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL GLU F 169 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 170 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 171 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 172 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 173 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 174 UNP Q9Y818 EXPRESSION TAG
SEQADV 5KNL HIS F 175 UNP Q9Y818 EXPRESSION TAG
SEQRES 1 A 1001 SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU
SEQRES 2 A 1001 TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN
SEQRES 3 A 1001 SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL
SEQRES 4 A 1001 GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER
SEQRES 5 A 1001 VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP
SEQRES 6 A 1001 LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY
SEQRES 7 A 1001 VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU
SEQRES 8 A 1001 LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU
SEQRES 9 A 1001 SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL
SEQRES 10 A 1001 THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP
SEQRES 11 A 1001 PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP
SEQRES 12 A 1001 SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY
SEQRES 13 A 1001 GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO
SEQRES 14 A 1001 LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL
SEQRES 15 A 1001 VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN
SEQRES 16 A 1001 GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO
SEQRES 17 A 1001 GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS
SEQRES 18 A 1001 GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU
SEQRES 19 A 1001 GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS
SEQRES 20 A 1001 VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER
SEQRES 21 A 1001 LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS
SEQRES 22 A 1001 MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA
SEQRES 23 A 1001 LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO
SEQRES 24 A 1001 ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU
SEQRES 25 A 1001 PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL
SEQRES 26 A 1001 GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN
SEQRES 27 A 1001 ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY
SEQRES 28 A 1001 GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER
SEQRES 29 A 1001 LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER
SEQRES 30 A 1001 LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU
SEQRES 31 A 1001 THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE
SEQRES 32 A 1001 ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER
SEQRES 33 A 1001 LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS
SEQRES 34 A 1001 GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR
SEQRES 35 A 1001 GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER
SEQRES 36 A 1001 ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG
SEQRES 37 A 1001 PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER
SEQRES 38 A 1001 THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS
SEQRES 39 A 1001 ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU
SEQRES 40 A 1001 GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU
SEQRES 41 A 1001 VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR
SEQRES 42 A 1001 VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU
SEQRES 43 A 1001 GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL
SEQRES 44 A 1001 VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN
SEQRES 45 A 1001 ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS
SEQRES 46 A 1001 ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA
SEQRES 47 A 1001 ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP
SEQRES 48 A 1001 ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU
SEQRES 49 A 1001 THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU
SEQRES 50 A 1001 GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU
SEQRES 51 A 1001 SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE
SEQRES 52 A 1001 ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE
SEQRES 53 A 1001 ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO
SEQRES 54 A 1001 PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER
SEQRES 55 A 1001 PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL
SEQRES 56 A 1001 ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS
SEQRES 57 A 1001 SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA
SEQRES 58 A 1001 GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE
SEQRES 59 A 1001 LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR
SEQRES 60 A 1001 ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA
SEQRES 61 A 1001 ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG
SEQRES 62 A 1001 LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN
SEQRES 63 A 1001 HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG
SEQRES 64 A 1001 ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS
SEQRES 65 A 1001 THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS
SEQRES 66 A 1001 THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU
SEQRES 67 A 1001 LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU
SEQRES 68 A 1001 TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE
SEQRES 69 A 1001 THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL
SEQRES 70 A 1001 ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN
SEQRES 71 A 1001 LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE
SEQRES 72 A 1001 GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER
SEQRES 73 A 1001 GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS
SEQRES 74 A 1001 LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU
SEQRES 75 A 1001 VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG
SEQRES 76 A 1001 LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN
SEQRES 77 A 1001 GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU
SEQRES 1 B 96 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 96 LEU VAL PRO ARG GLY SER HIS MET GLN ILE PHE VAL ARG
SEQRES 3 B 96 THR LEU THR GLY ARG THR ILE THR LEU GLU VAL GLU SER
SEQRES 4 B 96 SER ASP THR ILE ASP ASN VAL ARG ALA ARG ILE GLN ASP
SEQRES 5 B 96 ARG GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 6 B 96 ALA GLY ARG GLN LEU GLU ASP GLY ARG THR LEU ALA ASP
SEQRES 7 B 96 TYR ASN ILE GLN ARG GLU SER THR LEU HIS LEU VAL LEU
SEQRES 8 B 96 ARG LEU ARG GLY GLY
SEQRES 1 C 175 MET PRO SER SER ALA SER GLU GLN LEU LEU ARG LYS GLN
SEQRES 2 C 175 LEU LYS GLU ILE GLN LYS ASN PRO PRO GLN GLY PHE SER
SEQRES 3 C 175 VAL GLY LEU VAL ASP ASP LYS SER ILE PHE GLU TRP GLU
SEQRES 4 C 175 VAL MET ILE ILE GLY PRO GLU ASP THR LEU TYR GLU GLY
SEQRES 5 C 175 GLY PHE PHE HIS ALA THR LEU SER PHE PRO GLN ASP TYR
SEQRES 6 C 175 PRO LEU MET PRO PRO LYS MET LYS PHE THR THR GLU ILE
SEQRES 7 C 175 TRP HIS PRO ASN VAL HIS PRO ASN GLY GLU VAL CYS ILE
SEQRES 8 C 175 SER ILE LEU HIS PRO PRO GLY ASP ASP LYS TYR GLY TYR
SEQRES 9 C 175 GLU ASP ALA GLY GLU ARG TRP LEU PRO VAL HIS SER PRO
SEQRES 10 C 175 GLU THR ILE LEU ILE SER VAL ILE SER MET LEU SER SER
SEQRES 11 C 175 PRO ASN ASP GLU SER PRO ALA ASN ILE ASP ALA ALA LYS
SEQRES 12 C 175 GLU PHE ARG GLU ASN PRO GLN GLU PHE LYS LYS ARG VAL
SEQRES 13 C 175 ARG ARG LEU VAL ARG ARG SER ILE GLU MET ILE LEU GLU
SEQRES 14 C 175 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 1001 SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU
SEQRES 2 D 1001 TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN
SEQRES 3 D 1001 SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL
SEQRES 4 D 1001 GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER
SEQRES 5 D 1001 VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP
SEQRES 6 D 1001 LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY
SEQRES 7 D 1001 VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU
SEQRES 8 D 1001 LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU
SEQRES 9 D 1001 SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL
SEQRES 10 D 1001 THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP
SEQRES 11 D 1001 PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP
SEQRES 12 D 1001 SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY
SEQRES 13 D 1001 GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO
SEQRES 14 D 1001 LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL
SEQRES 15 D 1001 VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN
SEQRES 16 D 1001 GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO
SEQRES 17 D 1001 GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS
SEQRES 18 D 1001 GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU
SEQRES 19 D 1001 GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS
SEQRES 20 D 1001 VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER
SEQRES 21 D 1001 LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS
SEQRES 22 D 1001 MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA
SEQRES 23 D 1001 LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO
SEQRES 24 D 1001 ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU
SEQRES 25 D 1001 PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL
SEQRES 26 D 1001 GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN
SEQRES 27 D 1001 ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY
SEQRES 28 D 1001 GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER
SEQRES 29 D 1001 LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER
SEQRES 30 D 1001 LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU
SEQRES 31 D 1001 THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE
SEQRES 32 D 1001 ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER
SEQRES 33 D 1001 LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS
SEQRES 34 D 1001 GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR
SEQRES 35 D 1001 GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER
SEQRES 36 D 1001 ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG
SEQRES 37 D 1001 PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER
SEQRES 38 D 1001 THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS
SEQRES 39 D 1001 ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU
SEQRES 40 D 1001 GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU
SEQRES 41 D 1001 VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR
SEQRES 42 D 1001 VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU
SEQRES 43 D 1001 GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL
SEQRES 44 D 1001 VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN
SEQRES 45 D 1001 ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS
SEQRES 46 D 1001 ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA
SEQRES 47 D 1001 ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP
SEQRES 48 D 1001 ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU
SEQRES 49 D 1001 THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU
SEQRES 50 D 1001 GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU
SEQRES 51 D 1001 SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE
SEQRES 52 D 1001 ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE
SEQRES 53 D 1001 ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO
SEQRES 54 D 1001 PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER
SEQRES 55 D 1001 PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL
SEQRES 56 D 1001 ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS
SEQRES 57 D 1001 SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA
SEQRES 58 D 1001 GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE
SEQRES 59 D 1001 LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR
SEQRES 60 D 1001 ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA
SEQRES 61 D 1001 ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG
SEQRES 62 D 1001 LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN
SEQRES 63 D 1001 HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG
SEQRES 64 D 1001 ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS
SEQRES 65 D 1001 THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS
SEQRES 66 D 1001 THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU
SEQRES 67 D 1001 LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU
SEQRES 68 D 1001 TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE
SEQRES 69 D 1001 THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL
SEQRES 70 D 1001 ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN
SEQRES 71 D 1001 LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE
SEQRES 72 D 1001 GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER
SEQRES 73 D 1001 GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS
SEQRES 74 D 1001 LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU
SEQRES 75 D 1001 VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG
SEQRES 76 D 1001 LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN
SEQRES 77 D 1001 GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU
SEQRES 1 E 96 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 96 LEU VAL PRO ARG GLY SER HIS MET GLN ILE PHE VAL ARG
SEQRES 3 E 96 THR LEU THR GLY ARG THR ILE THR LEU GLU VAL GLU SER
SEQRES 4 E 96 SER ASP THR ILE ASP ASN VAL ARG ALA ARG ILE GLN ASP
SEQRES 5 E 96 ARG GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 6 E 96 ALA GLY ARG GLN LEU GLU ASP GLY ARG THR LEU ALA ASP
SEQRES 7 E 96 TYR ASN ILE GLN ARG GLU SER THR LEU HIS LEU VAL LEU
SEQRES 8 E 96 ARG LEU ARG GLY GLY
SEQRES 1 F 175 MET PRO SER SER ALA SER GLU GLN LEU LEU ARG LYS GLN
SEQRES 2 F 175 LEU LYS GLU ILE GLN LYS ASN PRO PRO GLN GLY PHE SER
SEQRES 3 F 175 VAL GLY LEU VAL ASP ASP LYS SER ILE PHE GLU TRP GLU
SEQRES 4 F 175 VAL MET ILE ILE GLY PRO GLU ASP THR LEU TYR GLU GLY
SEQRES 5 F 175 GLY PHE PHE HIS ALA THR LEU SER PHE PRO GLN ASP TYR
SEQRES 6 F 175 PRO LEU MET PRO PRO LYS MET LYS PHE THR THR GLU ILE
SEQRES 7 F 175 TRP HIS PRO ASN VAL HIS PRO ASN GLY GLU VAL CYS ILE
SEQRES 8 F 175 SER ILE LEU HIS PRO PRO GLY ASP ASP LYS TYR GLY TYR
SEQRES 9 F 175 GLU ASP ALA GLY GLU ARG TRP LEU PRO VAL HIS SER PRO
SEQRES 10 F 175 GLU THR ILE LEU ILE SER VAL ILE SER MET LEU SER SER
SEQRES 11 F 175 PRO ASN ASP GLU SER PRO ALA ASN ILE ASP ALA ALA LYS
SEQRES 12 F 175 GLU PHE ARG GLU ASN PRO GLN GLU PHE LYS LYS ARG VAL
SEQRES 13 F 175 ARG ARG LEU VAL ARG ARG SER ILE GLU MET ILE LEU GLU
SEQRES 14 F 175 HIS HIS HIS HIS HIS HIS
HET SO4 A1101 5
HET SO4 A1102 5
HET SO4 A1103 5
HET SO4 A1104 5
HET SO4 B 101 5
HET SO4 D1101 5
HET SO4 D1102 5
HET SO4 D1103 5
HET SO4 F 201 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 9(O4 S 2-)
FORMUL 16 HOH *94(H2 O)
HELIX 1 AA1 ASP A 16 GLY A 28 1 13
HELIX 2 AA2 GLY A 28 SER A 36 1 9
HELIX 3 AA3 LYS A 46 GLY A 60 1 15
HELIX 4 AA4 ARG A 73 SER A 79 5 7
HELIX 5 AA5 THR A 84 ILE A 88 5 5
HELIX 6 AA6 PRO A 91 GLU A 102 1 12
HELIX 7 AA7 SER A 116 PHE A 123 5 8
HELIX 8 AA8 SER A 132 ASN A 146 1 15
HELIX 9 AA9 GLY A 220 GLY A 224 5 5
HELIX 10 AB1 SER A 267 LEU A 272 1 6
HELIX 11 AB2 ASP A 281 MET A 285 5 5
HELIX 12 AB3 MET A 286 ALA A 304 1 19
HELIX 13 AB4 ASN A 314 LEU A 332 1 19
HELIX 14 AB5 ASP A 339 GLN A 349 1 11
HELIX 15 AB6 LEU A 354 SER A 375 1 22
HELIX 16 AB7 LEU A 389 LEU A 392 5 4
HELIX 17 AB8 TYR A 410 GLY A 418 1 9
HELIX 18 AB9 GLY A 418 SER A 427 1 10
HELIX 19 AC1 GLY A 436 GLY A 450 1 15
HELIX 20 AC2 GLU A 468 ARG A 474 5 7
HELIX 21 AC3 ARG A 479 VAL A 483 5 5
HELIX 22 AC4 LEU A 486 ASN A 499 1 14
HELIX 23 AC5 PRO A 500 THR A 503 5 4
HELIX 24 AC6 GLY A 514 GLU A 518 5 5
HELIX 25 AC7 GLY A 522 LYS A 528 1 7
HELIX 26 AC8 ASN A 538 PHE A 552 1 15
HELIX 27 AC9 SER A 578 SER A 582 5 5
HELIX 28 AD1 PRO A 591 PHE A 598 1 8
HELIX 29 AD2 ARG A 601 LYS A 618 1 18
HELIX 30 AD3 LYS A 618 SER A 630 1 13
HELIX 31 AD4 ASN A 632 THR A 640 1 9
HELIX 32 AD5 ASN A 643 VAL A 656 1 14
HELIX 33 AD6 SER A 662 ASN A 679 1 18
HELIX 34 AD7 ASN A 679 PHE A 689 1 11
HELIX 35 AD8 ASN A 718 GLY A 737 1 20
HELIX 36 AD9 ASP A 743 GLY A 753 1 11
HELIX 37 AE1 ILE A 790 LEU A 794 5 5
HELIX 38 AE2 PRO A 796 VAL A 801 5 6
HELIX 39 AE3 HIS A 818 TYR A 834 1 17
HELIX 40 AE4 ASP A 840 GLY A 849 1 10
HELIX 41 AE5 MET A 855 ASP A 875 1 21
HELIX 42 AE6 LYS A 879 TYR A 883 5 5
HELIX 43 AE7 THR A 926 ASP A 932 1 7
HELIX 44 AE8 ASP A 932 GLU A 937 1 6
HELIX 45 AE9 PRO A 958 LEU A 966 1 9
HELIX 46 AF1 LYS A 969 THR A 978 1 10
HELIX 47 AF2 THR B 22 ASP B 32 1 11
HELIX 48 AF3 PRO B 37 GLN B 41 5 5
HELIX 49 AF4 LEU B 56 ASN B 60 5 5
HELIX 50 AF5 SER C 4 GLN C 18 1 15
HELIX 51 AF6 ILE C 91 HIS C 95 5 5
HELIX 52 AF7 SER C 116 SER C 130 1 15
HELIX 53 AF8 ASN C 138 ASN C 148 1 11
HELIX 54 AF9 ASN C 148 LEU C 168 1 21
HELIX 55 AG1 ASP D 16 GLY D 28 1 13
HELIX 56 AG2 GLY D 28 SER D 36 1 9
HELIX 57 AG3 LYS D 46 GLY D 60 1 15
HELIX 58 AG4 ARG D 73 SER D 79 5 7
HELIX 59 AG5 THR D 84 ILE D 88 5 5
HELIX 60 AG6 PRO D 91 GLU D 102 1 12
HELIX 61 AG7 SER D 116 PHE D 123 5 8
HELIX 62 AG8 SER D 132 ASN D 146 1 15
HELIX 63 AG9 SER D 267 LEU D 272 1 6
HELIX 64 AH1 ASP D 281 MET D 285 5 5
HELIX 65 AH2 MET D 286 ALA D 304 1 19
HELIX 66 AH3 ASN D 314 LEU D 332 1 19
HELIX 67 AH4 ASP D 339 GLN D 349 1 11
HELIX 68 AH5 LEU D 354 SER D 375 1 22
HELIX 69 AH6 LEU D 389 LEU D 392 5 4
HELIX 70 AH7 TYR D 410 GLY D 418 1 9
HELIX 71 AH8 GLY D 418 SER D 427 1 10
HELIX 72 AH9 GLY D 436 GLY D 450 1 15
HELIX 73 AI1 GLU D 468 ARG D 474 5 7
HELIX 74 AI2 ARG D 479 VAL D 483 5 5
HELIX 75 AI3 LEU D 486 ASN D 499 1 14
HELIX 76 AI4 PRO D 500 THR D 503 5 4
HELIX 77 AI5 GLY D 514 GLU D 518 5 5
HELIX 78 AI6 GLY D 522 LYS D 528 1 7
HELIX 79 AI7 ASN D 538 PHE D 552 1 15
HELIX 80 AI8 SER D 578 SER D 582 5 5
HELIX 81 AI9 PRO D 591 PHE D 598 1 8
HELIX 82 AJ1 ARG D 601 LYS D 618 1 18
HELIX 83 AJ2 LYS D 618 SER D 630 1 13
HELIX 84 AJ3 ASN D 632 THR D 640 1 9
HELIX 85 AJ4 ASN D 643 VAL D 656 1 14
HELIX 86 AJ5 SER D 662 ASN D 679 1 18
HELIX 87 AJ6 ASN D 679 PHE D 689 1 11
HELIX 88 AJ7 ASN D 718 GLY D 737 1 20
HELIX 89 AJ8 ASP D 743 GLY D 753 1 11
HELIX 90 AJ9 PRO D 796 VAL D 801 5 6
HELIX 91 AK1 HIS D 818 TYR D 834 1 17
HELIX 92 AK2 ASP D 840 GLY D 849 1 10
HELIX 93 AK3 MET D 855 ASP D 875 1 21
HELIX 94 AK4 LYS D 879 TYR D 883 5 5
HELIX 95 AK5 THR D 926 ASP D 932 1 7
HELIX 96 AK6 PRO D 958 LEU D 966 1 9
HELIX 97 AK7 LYS D 969 THR D 978 1 10
HELIX 98 AK8 THR E 22 ASP E 32 1 11
HELIX 99 AK9 PRO E 37 GLN E 41 5 5
HELIX 100 AL1 LEU E 56 ASN E 60 5 5
HELIX 101 AL2 SER F 4 GLN F 18 1 15
HELIX 102 AL3 ILE F 91 HIS F 95 5 5
HELIX 103 AL4 SER F 116 SER F 130 1 15
HELIX 104 AL5 ASN F 138 ASN F 148 1 11
HELIX 105 AL6 ASN F 148 LEU F 168 1 21
SHEET 1 AA1 7 VAL A 109 VAL A 111 0
SHEET 2 AA1 7 SER A 63 TYR A 67 1 N LEU A 66 O SER A 110
SHEET 3 AA1 7 ASN A 39 ILE A 43 1 N ILE A 42 O THR A 65
SHEET 4 AA1 7 CYS A 125 VAL A 128 1 O VAL A 127 N LEU A 41
SHEET 5 AA1 7 ALA A 149 ARG A 156 1 O ILE A 151 N VAL A 128
SHEET 6 AA1 7 PHE A 159 ASP A 165 -1 O PHE A 163 N ALA A 152
SHEET 7 AA1 7 TYR A 383 ASP A 387 -1 O PHE A 386 N GLY A 160
SHEET 1 AA2 2 PHE A 170 CYS A 172 0
SHEET 2 AA2 2 THR A 261 ILE A 263 -1 O ILE A 263 N PHE A 170
SHEET 1 AA3 7 ARG A 227 LYS A 228 0
SHEET 2 AA3 7 PHE A 209 THR A 213 -1 N VAL A 210 O ARG A 227
SHEET 3 AA3 7 VAL A 253 VAL A 257 -1 O VAL A 257 N PHE A 209
SHEET 4 AA3 7 THR A 182 THR A 189 -1 N GLY A 183 O PHE A 254
SHEET 5 AA3 7 VAL A 193 MET A 196 -1 O THR A 195 N ALA A 186
SHEET 6 AA3 7 THR A 236 SER A 238 -1 O PHE A 237 N VAL A 194
SHEET 7 AA3 7 GLU A 230 VAL A 231 -1 N GLU A 230 O SER A 238
SHEET 1 AA4 5 ARG A 227 LYS A 228 0
SHEET 2 AA4 5 PHE A 209 THR A 213 -1 N VAL A 210 O ARG A 227
SHEET 3 AA4 5 VAL A 253 VAL A 257 -1 O VAL A 257 N PHE A 209
SHEET 4 AA4 5 THR A 182 THR A 189 -1 N GLY A 183 O PHE A 254
SHEET 5 AA4 5 ALA A 248 TYR A 250 -1 O GLY A 249 N ILE A 188
SHEET 1 AA5 8 ILE A 506 TYR A 509 0
SHEET 2 AA5 8 HIS A 458 THR A 462 1 N VAL A 461 O TYR A 509
SHEET 3 AA5 8 SER A 429 VAL A 433 1 N LEU A 432 O SER A 460
SHEET 4 AA5 8 LEU A 531 ASN A 534 1 O THR A 533 N PHE A 431
SHEET 5 AA5 8 LEU A 556 LEU A 562 1 O LEU A 557 N ASN A 534
SHEET 6 AA5 8 LYS A 565 VAL A 571 -1 O GLN A 569 N GLU A 558
SHEET 7 AA5 8 ASN A 885 ASN A 889 -1 O PHE A 888 N GLY A 566
SHEET 8 AA5 8 LEU A 894 SER A 898 -1 O SER A 898 N ASN A 885
SHEET 1 AA6 2 LYS A 905 VAL A 908 0
SHEET 2 AA6 2 LYS A 911 ASP A 914 -1 O LYS A 911 N VAL A 908
SHEET 1 AA7 5 ARG A 919 PRO A 923 0
SHEET 2 AA7 5 PHE A1007 LYS A1011 1 O CYS A1009 N TYR A 920
SHEET 3 AA7 5 HIS A 988 ASP A 997 -1 N LEU A 989 O ILE A1010
SHEET 4 AA7 5 LEU A 940 SER A 947 -1 N SER A 946 O GLU A 992
SHEET 5 AA7 5 SER A 950 ALA A 954 -1 O TYR A 953 N LEU A 945
SHEET 1 AA8 4 ARG A 919 PRO A 923 0
SHEET 2 AA8 4 PHE A1007 LYS A1011 1 O CYS A1009 N TYR A 920
SHEET 3 AA8 4 HIS A 988 ASP A 997 -1 N LEU A 989 O ILE A1010
SHEET 4 AA8 4 ASP A1002 GLU A1004 -1 O VAL A1003 N CYS A 995
SHEET 1 AA9 5 THR B 12 GLU B 16 0
SHEET 2 AA9 5 GLN B 2 THR B 7 -1 N VAL B 5 O ILE B 13
SHEET 3 AA9 5 SER B 65 VAL B 70 1 O LEU B 67 N PHE B 4
SHEET 4 AA9 5 ARG B 42 PHE B 45 -1 N ARG B 42 O VAL B 70
SHEET 5 AA9 5 ARG B 48 GLN B 49 -1 O ARG B 48 N PHE B 45
SHEET 1 AB1 4 PHE C 25 ASP C 31 0
SHEET 2 AB1 4 SER C 34 ILE C 43 -1 O GLU C 39 N GLY C 28
SHEET 3 AB1 4 PHE C 54 SER C 60 -1 O PHE C 55 N ILE C 42
SHEET 4 AB1 4 LYS C 71 PHE C 74 -1 O LYS C 71 N SER C 60
SHEET 1 AB2 7 VAL D 109 VAL D 111 0
SHEET 2 AB2 7 SER D 63 TYR D 67 1 N LEU D 66 O SER D 110
SHEET 3 AB2 7 ASN D 39 ILE D 43 1 N ILE D 42 O THR D 65
SHEET 4 AB2 7 CYS D 125 VAL D 128 1 O VAL D 127 N LEU D 41
SHEET 5 AB2 7 ALA D 149 ARG D 156 1 O ILE D 151 N VAL D 126
SHEET 6 AB2 7 PHE D 159 ASP D 165 -1 O PHE D 159 N ARG D 156
SHEET 7 AB2 7 TYR D 383 ASP D 387 -1 O PHE D 384 N ILE D 162
SHEET 1 AB3 2 PHE D 170 CYS D 172 0
SHEET 2 AB3 2 THR D 261 ILE D 263 -1 O ILE D 263 N PHE D 170
SHEET 1 AB4 7 ARG D 227 LYS D 228 0
SHEET 2 AB4 7 PHE D 209 THR D 213 -1 N VAL D 210 O ARG D 227
SHEET 3 AB4 7 VAL D 253 GLN D 256 -1 O THR D 255 N LYS D 211
SHEET 4 AB4 7 THR D 182 THR D 189 -1 N GLY D 183 O PHE D 254
SHEET 5 AB4 7 VAL D 193 MET D 196 -1 O THR D 195 N ALA D 186
SHEET 6 AB4 7 THR D 236 SER D 238 -1 O PHE D 237 N VAL D 194
SHEET 7 AB4 7 GLU D 230 VAL D 231 -1 N GLU D 230 O SER D 238
SHEET 1 AB5 5 ARG D 227 LYS D 228 0
SHEET 2 AB5 5 PHE D 209 THR D 213 -1 N VAL D 210 O ARG D 227
SHEET 3 AB5 5 VAL D 253 GLN D 256 -1 O THR D 255 N LYS D 211
SHEET 4 AB5 5 THR D 182 THR D 189 -1 N GLY D 183 O PHE D 254
SHEET 5 AB5 5 ALA D 248 TYR D 250 -1 O GLY D 249 N ILE D 188
SHEET 1 AB6 8 ILE D 506 TYR D 509 0
SHEET 2 AB6 8 HIS D 458 THR D 462 1 N VAL D 461 O TYR D 509
SHEET 3 AB6 8 SER D 429 VAL D 433 1 N LEU D 432 O SER D 460
SHEET 4 AB6 8 LEU D 531 ASN D 534 1 O THR D 533 N PHE D 431
SHEET 5 AB6 8 LEU D 556 LEU D 562 1 O LEU D 557 N ASN D 534
SHEET 6 AB6 8 LYS D 565 VAL D 571 -1 O GLN D 569 N GLU D 558
SHEET 7 AB6 8 ASN D 885 ASN D 889 -1 O PHE D 888 N GLY D 566
SHEET 8 AB6 8 LEU D 894 SER D 898 -1 O SER D 898 N ASN D 885
SHEET 1 AB7 2 LYS D 905 VAL D 908 0
SHEET 2 AB7 2 LYS D 911 ASP D 914 -1 O LYS D 911 N VAL D 908
SHEET 1 AB8 5 TYR D 920 PRO D 923 0
SHEET 2 AB8 5 ILE D1008 LYS D1011 1 O CYS D1009 N TYR D 920
SHEET 3 AB8 5 HIS D 988 ASP D 997 -1 N LEU D 989 O ILE D1010
SHEET 4 AB8 5 LEU D 940 SER D 947 -1 N SER D 946 O GLU D 992
SHEET 5 AB8 5 SER D 950 ALA D 954 -1 O TYR D 953 N LEU D 945
SHEET 1 AB9 4 TYR D 920 PRO D 923 0
SHEET 2 AB9 4 ILE D1008 LYS D1011 1 O CYS D1009 N TYR D 920
SHEET 3 AB9 4 HIS D 988 ASP D 997 -1 N LEU D 989 O ILE D1010
SHEET 4 AB9 4 ASP D1002 GLU D1004 -1 O VAL D1003 N CYS D 995
SHEET 1 AC1 5 THR E 12 GLU E 16 0
SHEET 2 AC1 5 GLN E 2 THR E 7 -1 N VAL E 5 O ILE E 13
SHEET 3 AC1 5 THR E 66 VAL E 70 1 O LEU E 67 N PHE E 4
SHEET 4 AC1 5 ARG E 42 PHE E 45 -1 N ARG E 42 O VAL E 70
SHEET 5 AC1 5 ARG E 48 GLN E 49 -1 O ARG E 48 N PHE E 45
SHEET 1 AC2 4 PHE F 25 ASP F 31 0
SHEET 2 AC2 4 SER F 34 ILE F 43 -1 O GLU F 39 N GLY F 28
SHEET 3 AC2 4 PHE F 54 SER F 60 -1 O PHE F 55 N ILE F 42
SHEET 4 AC2 4 LYS F 71 PHE F 74 -1 O LYS F 71 N SER F 60
SSBOND 1 CYS A 593 CYS C 90 1555 1555 2.04
SSBOND 2 CYS D 593 CYS F 90 1555 1555 2.03
CISPEP 1 LYS A 381 GLN A 382 0 0.57
CISPEP 2 ASP A 783 LYS A 784 0 3.78
CISPEP 3 TYR C 65 PRO C 66 0 5.45
CISPEP 4 PRO C 97 GLY C 98 0 4.91
CISPEP 5 ASP C 100 LYS C 101 0 -2.23
CISPEP 6 LYS D 381 GLN D 382 0 0.94
CISPEP 7 TYR F 65 PRO F 66 0 5.11
SITE 1 AC1 2 HIS A 29 GLU A 30
SITE 1 AC2 5 PHE A 590 ARG A 601 HIS A 604 ASP C 100
SITE 2 AC2 5 ARG C 110
SITE 1 AC3 5 ARG A 601 ILE A 602 GLU A 603 LYS A 843
SITE 2 AC3 5 LYS C 101
SITE 1 AC4 3 ARG A 22 ASN A 471 ARG A 474
SITE 1 AC5 3 ARG A 201 ARG B 29 ARG B 33
SITE 1 AC6 3 GLY D 28 HIS D 29 GLU D 30
SITE 1 AC7 2 ARG D 610 LYS D 850
SITE 1 AC8 2 ARG D 22 ARG D 474
SITE 1 AC9 5 PHE D 590 ARG D 601 HIS D 604 ASP F 99
SITE 2 AC9 5 ARG F 110
CRYST1 77.111 82.238 135.376 102.10 95.78 90.86 P 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012968 0.000194 0.001386 0.00000
SCALE2 0.000000 0.012161 0.002642 0.00000
SCALE3 0.000000 0.000000 0.007598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
