HEADER TRANSFERASE 12-JUL-11 3ZTS
TITLE HEXAGONAL FORM P6122 OF THE AQUIFEX AEOLICUS NUCLEOSIDE DIPHOSPHATE
TITLE 2 KINASE (FINAL STAGE OF RADIATION DAMAGE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: NDK, NDP KINASE, NUCLEOSIDE-2-P KINASE;
COMPND 5 EC: 2.7.4.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-21A
KEYWDS TRANSFERASE, DISULFIDE BRIDGE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.BOISSIER,F.GEORGESCAULD,L.MOYNIE,J.-W.DUPUY,C.SARGER,M.PODAR,
AUTHOR 2 I.LASCU,M.-F.GIRAUD,A.DAUTANT
REVDAT 3 20-DEC-23 3ZTS 1 SSBOND
REVDAT 2 23-MAY-12 3ZTS 1 JRNL
REVDAT 1 14-MAR-12 3ZTS 0
JRNL AUTH F.BOISSIER,F.GEORGESCAULD,L.MOYNIE,J.-W.DUPUY,C.SARGER,
JRNL AUTH 2 M.PODAR,L.LASCU,M.-F.GIRAUD,A.DAUTANT
JRNL TITL AN INTER-SUBUNIT DISULPHIDE BRIDGE STABILIZES THE TETRAMERIC
JRNL TITL 2 NUCLEOSIDE DIPHOSPHATE KINASE OF AQUIFEX AEOLICUS
JRNL REF PROTEINS V. 80 1658 2012
JRNL REFN ISSN 0887-3585
JRNL PMID 22467275
JRNL DOI 10.1002/PROT.24062
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.MOYNIE,M.GIRAUD,F.GEORGESCAULD,I.LASCU,A.DAUTANT
REMARK 1 TITL THE STRUCTURE OF THE ESCHERICHIA COLI NUCLEOSIDE DIPHOSPHATE
REMARK 1 TITL 2 KINASE REVEALS A NEW QUATERNARY ARCHITECTURE FOR THIS ENZYME
REMARK 1 TITL 3 FAMILY.
REMARK 1 REF PROTEINS V. 67 755 2007
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 17330300
REMARK 1 DOI 10.1002/PROT.21316
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.L.WILLIAMS,D.A.OREN,J.MUNOZ-DORADO,S.INOUYE,M.INOUYE,
REMARK 1 AUTH 2 E.ARNOLD
REMARK 1 TITL CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE
REMARK 1 TITL 2 DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE
REMARK 1 TITL 3 SUBSTRATE AT 2.0 A RESOLUTION.
REMARK 1 REF J.MOL.BIOL. V. 234 1230 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8263923
REMARK 1 DOI 10.1006/JMBI.1993.1673
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.570
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 3 NUMBER OF REFLECTIONS : 209779
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10560
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 51.3435 - 7.1405 0.71 5537 296 0.1909 0.2112
REMARK 3 2 7.1405 - 5.6700 0.80 6227 399 0.1977 0.2241
REMARK 3 3 5.6700 - 4.9539 0.81 6288 336 0.1673 0.1989
REMARK 3 4 4.9539 - 4.5013 0.81 6378 309 0.1382 0.1699
REMARK 3 5 4.5013 - 4.1788 0.82 6428 306 0.1326 0.1359
REMARK 3 6 4.1788 - 3.9325 0.84 6509 377 0.1583 0.1654
REMARK 3 7 3.9325 - 3.7356 0.84 6561 342 0.1508 0.1761
REMARK 3 8 3.7356 - 3.5731 0.84 6547 347 0.1714 0.1940
REMARK 3 9 3.5731 - 3.4355 0.84 6652 333 0.1800 0.2144
REMARK 3 10 3.4355 - 3.3170 0.84 6578 349 0.1791 0.2089
REMARK 3 11 3.3170 - 3.2133 0.85 6659 321 0.1784 0.1952
REMARK 3 12 3.2133 - 3.1215 0.85 6654 356 0.1944 0.2347
REMARK 3 13 3.1215 - 3.0393 0.85 6646 360 0.1924 0.2275
REMARK 3 14 3.0393 - 2.9652 0.85 6664 355 0.1906 0.2142
REMARK 3 15 2.9652 - 2.8978 0.86 6702 337 0.2054 0.2461
REMARK 3 16 2.8978 - 2.8361 0.86 6745 345 0.2066 0.2418
REMARK 3 17 2.8361 - 2.7794 0.86 6726 352 0.2047 0.2340
REMARK 3 18 2.7794 - 2.7269 0.86 6778 348 0.2008 0.2251
REMARK 3 19 2.7269 - 2.6782 0.87 6681 398 0.2103 0.2472
REMARK 3 20 2.6782 - 2.6328 0.86 6710 403 0.2099 0.2290
REMARK 3 21 2.6328 - 2.5904 0.87 6767 390 0.2101 0.2338
REMARK 3 22 2.5904 - 2.5505 0.87 6805 374 0.2186 0.2604
REMARK 3 23 2.5505 - 2.5130 0.87 6806 331 0.2245 0.2377
REMARK 3 24 2.5130 - 2.4776 0.87 6872 341 0.2416 0.2828
REMARK 3 25 2.4776 - 2.4441 0.88 6826 364 0.2551 0.3049
REMARK 3 26 2.4441 - 2.4124 0.88 6864 375 0.2570 0.2683
REMARK 3 27 2.4124 - 2.3822 0.88 6890 354 0.2503 0.2931
REMARK 3 28 2.3822 - 2.3535 0.88 6899 355 0.2457 0.2579
REMARK 3 29 2.3535 - 2.3262 0.88 6880 390 0.2568 0.2721
REMARK 3 30 2.3262 - 2.3000 0.88 6940 317 0.2594 0.3301
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 : 0.38
REMARK 3 B_SOL : 40.52
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12280
REMARK 3 B22 (A**2) : 1.12280
REMARK 3 B33 (A**2) : -2.24570
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 13699
REMARK 3 ANGLE : 0.943 18437
REMARK 3 CHIRALITY : 0.071 1991
REMARK 3 PLANARITY : 0.003 2438
REMARK 3 DIHEDRAL : 14.742 5235
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3414 -76.1266 -2.1520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0555 T22: 0.1053
REMARK 3 T33: 0.0760 T12: 0.0385
REMARK 3 T13: -0.0129 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.9840 L22: 0.7482
REMARK 3 L33: 0.4979 L12: -0.7151
REMARK 3 L13: -0.6249 L23: 0.3200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0847 S12: -0.1806 S13: -0.0998
REMARK 3 S21: 0.1645 S22: 0.0400 S23: 0.0118
REMARK 3 S31: 0.0736 S32: 0.0501 S33: 0.0172
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8812 -89.9696 7.5360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3566 T22: 0.4622
REMARK 3 T33: 0.3520 T12: 0.1605
REMARK 3 T13: 0.0960 T23: 0.1780
REMARK 3 L TENSOR
REMARK 3 L11: 0.0131 L22: 0.7586
REMARK 3 L33: 1.0785 L12: -0.0485
REMARK 3 L13: -0.0092 L23: -0.6954
REMARK 3 S TENSOR
REMARK 3 S11: -0.0707 S12: -0.2240 S13: -0.0783
REMARK 3 S21: 0.2156 S22: 0.4654 S23: 0.2715
REMARK 3 S31: -0.0640 S32: -0.1662 S33: -0.2085
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND (RESSEQ 2:51 OR RESSEQ 58:142)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9443 -69.4394 -23.9541
REMARK 3 T TENSOR
REMARK 3 T11: 0.0588 T22: 0.0083
REMARK 3 T33: 0.0542 T12: 0.0438
REMARK 3 T13: -0.0016 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.5474 L22: 0.9101
REMARK 3 L33: 1.0920 L12: -0.0963
REMARK 3 L13: 0.3835 L23: -0.5177
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.0370 S13: -0.0223
REMARK 3 S21: -0.1694 S22: -0.0534 S23: -0.0512
REMARK 3 S31: -0.0911 S32: 0.1589 S33: 0.0328
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9776 -72.6558 -33.8481
REMARK 3 T TENSOR
REMARK 3 T11: 0.7306 T22: 0.5509
REMARK 3 T33: 0.0509 T12: -0.0960
REMARK 3 T13: 0.1972 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.2035 L22: 1.3444
REMARK 3 L33: 4.0273 L12: -0.3134
REMARK 3 L13: 0.5977 L23: 0.4792
REMARK 3 S TENSOR
REMARK 3 S11: 0.1279 S12: 0.2613 S13: 0.1450
REMARK 3 S21: -0.7094 S22: 0.3293 S23: -0.1584
REMARK 3 S31: -0.1028 S32: -0.3256 S33: -0.3642
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN C AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9027 -95.7219 -2.8993
REMARK 3 T TENSOR
REMARK 3 T11: 0.0799 T22: 0.1078
REMARK 3 T33: 0.0841 T12: 0.0664
REMARK 3 T13: -0.0025 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.4356 L22: 0.8067
REMARK 3 L33: 0.6347 L12: -0.8930
REMARK 3 L13: 0.7311 L23: -0.1848
REMARK 3 S TENSOR
REMARK 3 S11: -0.0687 S12: -0.0968 S13: -0.0493
REMARK 3 S21: 0.0683 S22: 0.0069 S23: -0.0235
REMARK 3 S31: 0.0410 S32: 0.0716 S33: 0.0218
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN C AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.6739 -81.5881 6.2452
REMARK 3 T TENSOR
REMARK 3 T11: 0.3978 T22: 0.4301
REMARK 3 T33: 0.3756 T12: 0.2214
REMARK 3 T13: -0.2173 T23: -0.1935
REMARK 3 L TENSOR
REMARK 3 L11: 0.0955 L22: 0.0150
REMARK 3 L33: 0.1562 L12: 0.0289
REMARK 3 L13: 0.1200 L23: 0.0337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0538 S12: -0.0583 S13: 0.0376
REMARK 3 S21: 0.0552 S22: 0.1759 S23: -0.0457
REMARK 3 S31: -0.1048 S32: 0.0175 S33: -0.0100
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN D AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8209-103.0582 -23.6576
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.0603
REMARK 3 T33: 0.0753 T12: 0.0372
REMARK 3 T13: -0.0070 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.6786 L22: 1.0438
REMARK 3 L33: 1.1539 L12: -0.3846
REMARK 3 L13: -0.1002 L23: 0.8503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: 0.1027 S13: -0.0365
REMARK 3 S21: -0.0365 S22: -0.0571 S23: 0.0760
REMARK 3 S31: 0.2140 S32: -0.0108 S33: 0.0251
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN D AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1172 -99.9990 -32.5828
REMARK 3 T TENSOR
REMARK 3 T11: 0.4329 T22: 0.4571
REMARK 3 T33: 0.2085 T12: 0.1031
REMARK 3 T13: -0.1347 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.0082 L22: 1.2012
REMARK 3 L33: 2.4193 L12: 0.0908
REMARK 3 L13: 0.1305 L23: 1.6951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1607 S12: -0.1320 S13: 0.0024
REMARK 3 S21: -0.1697 S22: 0.3919 S23: 0.0497
REMARK 3 S31: -0.6006 S32: 0.0777 S33: -0.0718
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN E AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1885 -50.8329 -16.2428
REMARK 3 T TENSOR
REMARK 3 T11: 0.0167 T22: 0.0913
REMARK 3 T33: 0.0779 T12: -0.0080
REMARK 3 T13: 0.0068 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.0958 L22: 0.4017
REMARK 3 L33: 0.9844 L12: 0.6277
REMARK 3 L13: 0.6368 L23: 0.3775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: -0.1187 S13: 0.1063
REMARK 3 S21: -0.0199 S22: -0.0540 S23: 0.0557
REMARK 3 S31: -0.0893 S32: -0.0471 S33: 0.0216
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN E AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2291 -40.3956 -6.3900
REMARK 3 T TENSOR
REMARK 3 T11: 0.4275 T22: 0.5396
REMARK 3 T33: 0.2549 T12: -0.0264
REMARK 3 T13: 0.0531 T23: -0.1218
REMARK 3 L TENSOR
REMARK 3 L11: 0.6225 L22: 0.2758
REMARK 3 L33: 1.3404 L12: -0.2550
REMARK 3 L13: -0.8957 L23: 0.4461
REMARK 3 S TENSOR
REMARK 3 S11: 0.3879 S12: -0.2538 S13: 0.1110
REMARK 3 S21: -0.0736 S22: -0.1841 S23: 0.0522
REMARK 3 S31: -0.6324 S32: 0.1426 S33: -0.1873
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN F AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4594 -64.3750 -37.9422
REMARK 3 T TENSOR
REMARK 3 T11: 0.0057 T22: 0.0623
REMARK 3 T33: 0.0304 T12: 0.0242
REMARK 3 T13: -0.0153 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.5439 L22: 0.7817
REMARK 3 L33: 0.4020 L12: 0.3991
REMARK 3 L13: -0.1782 L23: 0.1630
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: 0.0567 S13: 0.1014
REMARK 3 S21: -0.0066 S22: -0.0083 S23: 0.1520
REMARK 3 S31: -0.0323 S32: -0.1007 S33: 0.0656
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN F AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7739 -75.3231 -47.5719
REMARK 3 T TENSOR
REMARK 3 T11: 0.3545 T22: 0.3269
REMARK 3 T33: 0.1477 T12: 0.0835
REMARK 3 T13: -0.1070 T23: -0.1179
REMARK 3 L TENSOR
REMARK 3 L11: 3.2513 L22: 0.2971
REMARK 3 L33: 6.2013 L12: -0.6177
REMARK 3 L13: -4.2185 L23: 0.6158
REMARK 3 S TENSOR
REMARK 3 S11: 0.6369 S12: 0.3760 S13: -0.2892
REMARK 3 S21: 0.0081 S22: -0.2639 S23: -0.1074
REMARK 3 S31: -0.5406 S32: -0.5886 S33: -0.1367
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN G AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1615 -65.6265 -16.4720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: 0.1364
REMARK 3 T33: 0.0613 T12: -0.0065
REMARK 3 T13: -0.0019 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.9972 L22: 0.2714
REMARK 3 L33: 0.6338 L12: 0.4389
REMARK 3 L13: -0.4676 L23: -0.0771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0331 S12: -0.1906 S13: -0.0095
REMARK 3 S21: 0.0883 S22: -0.0034 S23: 0.0157
REMARK 3 S31: 0.1548 S32: -0.0634 S33: 0.0111
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN G AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0049 -76.6422 -7.4678
REMARK 3 T TENSOR
REMARK 3 T11: 0.4757 T22: 0.5018
REMARK 3 T33: 0.0856 T12: -0.0410
REMARK 3 T13: -0.0652 T23: 0.1063
REMARK 3 L TENSOR
REMARK 3 L11: 1.1084 L22: 0.3755
REMARK 3 L33: 0.9418 L12: -0.0588
REMARK 3 L13: -0.6367 L23: 0.4949
REMARK 3 S TENSOR
REMARK 3 S11: 0.2164 S12: -0.7793 S13: -0.1884
REMARK 3 S21: -0.1763 S22: -0.1474 S23: 0.0319
REMARK 3 S31: -0.5822 S32: 0.0526 S33: -0.0628
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN H AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5376 -50.8171 -37.4012
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: 0.0907
REMARK 3 T33: 0.0609 T12: 0.0236
REMARK 3 T13: 0.0053 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.5312 L22: 0.8896
REMARK 3 L33: 0.3510 L12: -0.1096
REMARK 3 L13: 0.3676 L23: -0.3502
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: -0.0064 S13: -0.0783
REMARK 3 S21: 0.0015 S22: -0.0440 S23: -0.1776
REMARK 3 S31: 0.0557 S32: 0.1027 S33: 0.0097
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN H AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8267 -39.4580 -46.4888
REMARK 3 T TENSOR
REMARK 3 T11: 0.2735 T22: 0.5298
REMARK 3 T33: 0.2718 T12: 0.0011
REMARK 3 T13: 0.0385 T23: 0.1648
REMARK 3 L TENSOR
REMARK 3 L11: 0.0460 L22: 0.4079
REMARK 3 L33: 6.9605 L12: -0.1274
REMARK 3 L13: -0.5258 L23: 1.6847
REMARK 3 S TENSOR
REMARK 3 S11: -0.0824 S12: 0.1823 S13: 0.0922
REMARK 3 S21: -0.0048 S22: 0.1936 S23: 0.0512
REMARK 3 S31: -0.3699 S32: 1.0944 S33: 0.0234
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN I AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2294 -50.7719 39.9636
REMARK 3 T TENSOR
REMARK 3 T11: 0.0659 T22: 0.1534
REMARK 3 T33: 0.1230 T12: -0.0274
REMARK 3 T13: -0.0012 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.5257 L22: 0.5024
REMARK 3 L33: 0.8946 L12: 0.4857
REMARK 3 L13: 0.4136 L23: 0.5489
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: -0.1085 S13: -0.0376
REMARK 3 S21: 0.1236 S22: -0.0105 S23: -0.0397
REMARK 3 S31: -0.0427 S32: 0.1481 S33: 0.0123
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN I AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1129 -40.3203 49.6641
REMARK 3 T TENSOR
REMARK 3 T11: 0.3972 T22: 0.5555
REMARK 3 T33: 0.2482 T12: -0.0518
REMARK 3 T13: 0.0775 T23: -0.1495
REMARK 3 L TENSOR
REMARK 3 L11: 0.1959 L22: 0.0206
REMARK 3 L33: 2.5055 L12: 0.0403
REMARK 3 L13: -0.2871 L23: -0.1978
REMARK 3 S TENSOR
REMARK 3 S11: -0.0940 S12: -0.2310 S13: 0.1275
REMARK 3 S21: 0.0066 S22: -0.0586 S23: 0.0292
REMARK 3 S31: 0.3754 S32: -0.6835 S33: 0.2235
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN J AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5759 -64.3073 18.2263
REMARK 3 T TENSOR
REMARK 3 T11: -0.0034 T22: 0.1334
REMARK 3 T33: 0.0959 T12: 0.0209
REMARK 3 T13: 0.0044 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.9080 L22: 0.7039
REMARK 3 L33: 1.2459 L12: -0.7520
REMARK 3 L13: -0.4845 L23: 0.1715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0040 S12: 0.0716 S13: -0.1584
REMARK 3 S21: 0.0634 S22: -0.0726 S23: 0.0684
REMARK 3 S31: 0.2408 S32: 0.0482 S33: 0.0653
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN J AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0580 -75.1275 8.3677
REMARK 3 T TENSOR
REMARK 3 T11: 0.6377 T22: 0.8064
REMARK 3 T33: 0.0818 T12: 0.0146
REMARK 3 T13: -0.0807 T23: -0.1950
REMARK 3 L TENSOR
REMARK 3 L11: 1.4719 L22: 0.4596
REMARK 3 L33: 4.4375 L12: 0.1557
REMARK 3 L13: -1.7543 L23: -1.1829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2785 S12: 0.5073 S13: -0.2461
REMARK 3 S21: -0.0101 S22: -0.0875 S23: -0.1331
REMARK 3 S31: -0.5526 S32: -1.4597 S33: -0.0250
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN K AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1826 -65.7584 39.2731
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: 0.1414
REMARK 3 T33: 0.1194 T12: -0.0395
REMARK 3 T13: 0.0249 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.6294 L22: 0.7246
REMARK 3 L33: 1.0363 L12: 0.6098
REMARK 3 L13: -0.5062 L23: -0.7673
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: -0.1189 S13: -0.0419
REMARK 3 S21: 0.0489 S22: -0.0499 S23: -0.0988
REMARK 3 S31: -0.0301 S32: -0.0887 S33: 0.0262
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN K AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0788 -76.7112 48.4414
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.6766
REMARK 3 T33: 0.3579 T12: -0.1906
REMARK 3 T13: -0.0530 T23: 0.2455
REMARK 3 L TENSOR
REMARK 3 L11: 1.4122 L22: 0.0918
REMARK 3 L33: 7.2692 L12: 0.2738
REMARK 3 L13: -2.4166 L23: -0.4870
REMARK 3 S TENSOR
REMARK 3 S11: 0.2072 S12: -0.6921 S13: -0.1232
REMARK 3 S21: 0.0933 S22: -0.0956 S23: 0.0712
REMARK 3 S31: -0.7775 S32: 0.5044 S33: -0.0647
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN L AND (RESSEQ 2:51 OR RESSEQ 58:142))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2931 -50.7623 18.5478
REMARK 3 T TENSOR
REMARK 3 T11: 0.0523 T22: 0.1378
REMARK 3 T33: 0.0941 T12: -0.0008
REMARK 3 T13: -0.0093 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.7882 L22: 0.7184
REMARK 3 L33: 1.3605 L12: -0.4209
REMARK 3 L13: 0.4221 L23: -0.4521
REMARK 3 S TENSOR
REMARK 3 S11: -0.1091 S12: 0.0938 S13: 0.0359
REMARK 3 S21: -0.0292 S22: 0.0482 S23: 0.1796
REMARK 3 S31: -0.1775 S32: -0.2339 S33: 0.0339
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN L AND RESSEQ 52:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5886 -39.3295 9.5800
REMARK 3 T TENSOR
REMARK 3 T11: 0.6567 T22: 0.5144
REMARK 3 T33: 0.4507 T12: 0.1541
REMARK 3 T13: 0.1692 T23: 0.2799
REMARK 3 L TENSOR
REMARK 3 L11: 0.2962 L22: 0.3209
REMARK 3 L33: 5.4765 L12: -0.3010
REMARK 3 L13: 0.9467 L23: -0.8422
REMARK 3 S TENSOR
REMARK 3 S11: 0.2598 S12: 0.1551 S13: 0.0924
REMARK 3 S21: -0.0873 S22: -0.0059 S23: 0.0642
REMARK 3 S31: 0.9116 S32: 0.1903 S33: -0.0453
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN B AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 565
REMARK 3 RMSD : 0.025
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN C AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 563
REMARK 3 RMSD : 0.035
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN D AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 564
REMARK 3 RMSD : 0.035
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN E AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 565
REMARK 3 RMSD : 0.029
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN F AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 563
REMARK 3 RMSD : 0.024
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN G AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 564
REMARK 3 RMSD : 0.035
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN H AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 563
REMARK 3 RMSD : 0.028
REMARK 3 NCS OPERATOR : 8
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN I AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 564
REMARK 3 RMSD : 0.032
REMARK 3 NCS OPERATOR : 9
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN J AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 565
REMARK 3 RMSD : 0.028
REMARK 3 NCS OPERATOR : 10
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN K AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 563
REMARK 3 RMSD : 0.036
REMARK 3 NCS OPERATOR : 11
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 2:142 AND BACKBONE
REMARK 3 SELECTION : CHAIN L AND RESID 2:142 AND BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 565
REMARK 3 RMSD : 0.031
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 SELECTION : CHAIN B AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 543
REMARK 3 RMSD : 0.058
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 SELECTION : CHAIN E AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 543
REMARK 3 RMSD : 0.091
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 SELECTION : CHAIN F AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 539
REMARK 3 RMSD : 0.052
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 SELECTION : CHAIN I AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 538
REMARK 3 RMSD : 0.065
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 SELECTION : CHAIN J AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 543
REMARK 3 RMSD : 0.065
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 SELECTION : CHAIN D AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 529
REMARK 3 RMSD : 0.057
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN C AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 SELECTION : CHAIN G AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 529
REMARK 3 RMSD : 0.060
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN C AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 SELECTION : CHAIN H AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 536
REMARK 3 RMSD : 0.092
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN C AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 SELECTION : CHAIN K AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 536
REMARK 3 RMSD : 0.053
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN C AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 SELECTION : CHAIN L AND SIDECHAIN AND RESSEQ 2:142
REMARK 3 AND NOT (RESSEQ 96 OR RESSEQ 100 OR
REMARK 3 RESSEQ 114)
REMARK 3 ATOM PAIRS NUMBER : 534
REMARK 3 RMSD : 0.063
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IN THE SSBOND CARDS: THE FIRST ATOM
REMARK 3 BELONGS TO THE ALTERNATE CONFORMER A (WITH OCCUPANCY Q1). THE
REMARK 3 SECOND ONE BELONGS TO THE ALTERNATE CONFORMER B (WITH OCCUPANCY
REMARK 3 Q2). ABS(Q1 - Q2)*100 IS THE PERCENTAGE OF CYS133 NOT INVOLVED
REMARK 3 IN THE DISULFIDE BRIDGE.
REMARK 4
REMARK 4 3ZTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1290046253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : KIRKPATRICK BAEZ
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110849
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 52.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: PDB ENTRY 3ZTO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG 3350, 0.2 M NACL, 0.1 M BIS
REMARK 280 -TRIS PH 5.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.24367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 164.48733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 123.36550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 205.60917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.12183
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.24367
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 164.48733
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 205.60917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 123.36550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 41.12183
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2069 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2095 LIES ON A SPECIAL POSITION.
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 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 MET G 1
REMARK 465 MET H 1
REMARK 465 MET I 1
REMARK 465 MET J 1
REMARK 465 MET K 1
REMARK 465 MET L 1
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 ARG E 85 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG E 85 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG H 85 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG H 85 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 113 -146.33 -144.87
REMARK 500 ALA A 118 -40.87 72.23
REMARK 500 TYR B 51 30.61 -97.52
REMARK 500 ASP B 113 -147.07 -145.53
REMARK 500 ALA B 118 -41.08 72.70
REMARK 500 ASP C 113 -147.21 -145.82
REMARK 500 ALA C 118 -43.10 73.91
REMARK 500 ASP D 113 -147.30 -145.17
REMARK 500 ALA D 118 -42.05 75.54
REMARK 500 TYR E 51 31.39 -99.98
REMARK 500 ASP E 113 -146.32 -144.70
REMARK 500 ALA E 118 -39.68 74.05
REMARK 500 TYR F 51 30.02 -96.52
REMARK 500 ASP F 113 -145.13 -144.64
REMARK 500 ALA F 118 -41.52 73.22
REMARK 500 ASP G 113 -146.06 -143.29
REMARK 500 ALA G 118 -42.71 74.74
REMARK 500 TYR H 51 30.55 -99.14
REMARK 500 ASP H 113 -146.25 -144.85
REMARK 500 ALA H 118 -41.20 73.98
REMARK 500 TYR I 51 31.70 -99.82
REMARK 500 ASP I 113 -147.03 -145.68
REMARK 500 ALA I 118 -41.92 72.63
REMARK 500 TYR J 51 30.93 -97.64
REMARK 500 ASP J 113 -145.98 -145.21
REMARK 500 ALA J 118 -40.91 72.92
REMARK 500 ASP K 113 -145.54 -145.01
REMARK 500 ALA K 118 -42.03 75.02
REMARK 500 ASP L 113 -146.62 -146.31
REMARK 500 ALA L 118 -42.31 76.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2024 DISTANCE = 5.89 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZTR RELATED DB: PDB
REMARK 900 HEXAGONAL FORM P6122 OF THE AQUIFEX AEOLICUS NUCLEOSIDE DIPHOSPHATE
REMARK 900 KINASE (FIRST STAGE OF RADIATION DAMAGE)
REMARK 900 RELATED ID: 3ZTQ RELATED DB: PDB
REMARK 900 HEXAGONAL CRYSTAL FORM P61 OF THE AQUIFEX AEOLICUS NUCLEOSIDE
REMARK 900 DIPHOSPHATE KINASE
REMARK 900 RELATED ID: 3ZTP RELATED DB: PDB
REMARK 900 ORTHORHOMBIC CRYSTAL FORM P21212 OF THE AQUIFEX AEOLICUS NUCLEOSIDE
REMARK 900 DIPHOSPHATE KINASE
REMARK 900 RELATED ID: 3ZTO RELATED DB: PDB
REMARK 900 ORTHORHOMBIC CRYSTAL FORM C222 OF THE AQUIFEX AEOLICUS NUCLEOSIDE
REMARK 900 DIPHOSPHATE KINASE
DBREF 3ZTS A 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS B 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS C 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS D 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS E 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS F 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS G 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS H 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS I 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS J 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS K 1 142 UNP O67528 NDK_AQUAE 1 142
DBREF 3ZTS L 1 142 UNP O67528 NDK_AQUAE 1 142
SEQRES 1 A 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 A 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 A 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 A 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 A 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 A 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 A 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 A 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 A 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 A 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 A 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 B 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 B 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 B 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 B 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 B 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 B 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 B 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 B 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 B 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 B 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 B 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 C 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 C 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 C 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 C 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 C 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 C 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 C 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 C 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 C 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 C 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 C 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 D 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 D 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 D 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 D 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 D 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 D 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 D 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 D 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 D 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 D 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 D 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 E 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 E 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 E 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 E 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 E 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 E 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 E 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 E 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 E 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 E 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 E 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 F 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 F 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 F 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 F 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 F 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 F 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 F 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 F 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 F 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 F 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 F 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 G 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 G 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 G 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 G 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 G 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 G 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 G 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 G 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 G 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 G 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 G 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 H 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 H 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 H 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 H 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 H 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 H 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 H 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 H 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 H 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 H 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 H 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 I 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 I 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 I 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 I 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 I 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 I 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 I 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 I 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 I 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 I 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 I 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 J 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 J 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 J 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 J 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 J 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 J 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 J 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 J 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 J 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 J 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 J 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 K 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 K 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 K 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 K 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 K 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 K 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 K 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 K 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 K 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 K 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 K 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
SEQRES 1 L 142 MET ALA VAL GLU ARG THR LEU ILE ILE VAL LYS PRO ASP
SEQRES 2 L 142 ALA MET GLU LYS GLY ALA LEU GLY LYS ILE LEU ASP ARG
SEQRES 3 L 142 PHE ILE GLN GLU GLY PHE GLN ILE LYS ALA LEU LYS MET
SEQRES 4 L 142 PHE ARG PHE THR PRO GLU LYS ALA GLY GLU PHE TYR TYR
SEQRES 5 L 142 VAL HIS ARG GLU ARG PRO PHE PHE GLN GLU LEU VAL GLU
SEQRES 6 L 142 PHE MET SER SER GLY PRO VAL VAL ALA ALA VAL LEU GLU
SEQRES 7 L 142 GLY GLU ASP ALA ILE LYS ARG VAL ARG GLU ILE ILE GLY
SEQRES 8 L 142 PRO THR ASP SER GLU GLU ALA ARG LYS VAL ALA PRO ASN
SEQRES 9 L 142 SER ILE ARG ALA GLN PHE GLY THR ASP LYS GLY LYS ASN
SEQRES 10 L 142 ALA ILE HIS ALA SER ASP SER PRO GLU SER ALA GLN TYR
SEQRES 11 L 142 GLU ILE CYS PHE ILE PHE SER GLY LEU GLU ILE VAL
FORMUL 13 HOH *1092(H2 O)
HELIX 1 1 LYS A 11 LYS A 17 1 7
HELIX 2 2 ALA A 19 GLU A 30 1 12
HELIX 3 3 THR A 43 TYR A 51 1 9
HELIX 4 4 TYR A 52 ARG A 55 5 4
HELIX 5 5 PHE A 59 SER A 68 1 10
HELIX 6 6 ASP A 81 GLY A 91 1 11
HELIX 7 7 ASP A 94 ALA A 102 1 9
HELIX 8 8 SER A 105 GLY A 111 1 7
HELIX 9 9 SER A 124 PHE A 136 1 13
HELIX 10 10 SER A 137 ILE A 141 5 5
HELIX 11 11 LYS B 11 LYS B 17 1 7
HELIX 12 12 ALA B 19 GLU B 30 1 12
HELIX 13 13 THR B 43 TYR B 51 1 9
HELIX 14 14 TYR B 52 ARG B 55 5 4
HELIX 15 15 PHE B 59 SER B 68 1 10
HELIX 16 16 ASP B 81 GLY B 91 1 11
HELIX 17 17 ASP B 94 ALA B 102 1 9
HELIX 18 18 SER B 105 GLY B 111 1 7
HELIX 19 19 SER B 124 PHE B 136 1 13
HELIX 20 20 SER B 137 ILE B 141 5 5
HELIX 21 21 LYS C 11 LYS C 17 1 7
HELIX 22 22 ALA C 19 GLU C 30 1 12
HELIX 23 23 THR C 43 TYR C 51 1 9
HELIX 24 24 TYR C 52 ARG C 55 5 4
HELIX 25 25 PHE C 59 SER C 68 1 10
HELIX 26 26 ASP C 81 GLY C 91 1 11
HELIX 27 27 ASP C 94 ALA C 102 1 9
HELIX 28 28 SER C 105 GLY C 111 1 7
HELIX 29 29 SER C 124 PHE C 136 1 13
HELIX 30 30 SER C 137 ILE C 141 5 5
HELIX 31 31 LYS D 11 LYS D 17 1 7
HELIX 32 32 ALA D 19 GLU D 30 1 12
HELIX 33 33 THR D 43 TYR D 51 1 9
HELIX 34 34 TYR D 52 ARG D 55 5 4
HELIX 35 35 PHE D 59 SER D 68 1 10
HELIX 36 36 ASP D 81 GLY D 91 1 11
HELIX 37 37 ASP D 94 ALA D 102 1 9
HELIX 38 38 SER D 105 GLY D 111 1 7
HELIX 39 39 SER D 124 PHE D 136 1 13
HELIX 40 40 SER D 137 ILE D 141 5 5
HELIX 41 41 LYS E 11 LYS E 17 1 7
HELIX 42 42 ALA E 19 GLU E 30 1 12
HELIX 43 43 THR E 43 TYR E 51 1 9
HELIX 44 44 TYR E 52 ARG E 55 5 4
HELIX 45 45 PHE E 59 SER E 68 1 10
HELIX 46 46 ASP E 81 GLY E 91 1 11
HELIX 47 47 ASP E 94 ALA E 102 1 9
HELIX 48 48 SER E 105 GLY E 111 1 7
HELIX 49 49 SER E 124 PHE E 136 1 13
HELIX 50 50 SER E 137 ILE E 141 5 5
HELIX 51 51 LYS F 11 LYS F 17 1 7
HELIX 52 52 ALA F 19 GLU F 30 1 12
HELIX 53 53 THR F 43 TYR F 51 1 9
HELIX 54 54 TYR F 52 ARG F 55 5 4
HELIX 55 55 PHE F 59 SER F 68 1 10
HELIX 56 56 ASP F 81 GLY F 91 1 11
HELIX 57 57 ASP F 94 ALA F 102 1 9
HELIX 58 58 SER F 105 GLY F 111 1 7
HELIX 59 59 SER F 124 PHE F 136 1 13
HELIX 60 60 SER F 137 ILE F 141 5 5
HELIX 61 61 LYS G 11 LYS G 17 1 7
HELIX 62 62 ALA G 19 GLU G 30 1 12
HELIX 63 63 THR G 43 TYR G 51 1 9
HELIX 64 64 TYR G 52 ARG G 55 5 4
HELIX 65 65 PHE G 59 SER G 68 1 10
HELIX 66 66 ASP G 81 GLY G 91 1 11
HELIX 67 67 ASP G 94 ALA G 102 1 9
HELIX 68 68 SER G 105 GLY G 111 1 7
HELIX 69 69 SER G 124 PHE G 136 1 13
HELIX 70 70 SER G 137 ILE G 141 5 5
HELIX 71 71 LYS H 11 LYS H 17 1 7
HELIX 72 72 ALA H 19 GLU H 30 1 12
HELIX 73 73 THR H 43 TYR H 51 1 9
HELIX 74 74 TYR H 52 ARG H 55 5 4
HELIX 75 75 PHE H 59 SER H 68 1 10
HELIX 76 76 ASP H 81 GLY H 91 1 11
HELIX 77 77 ASP H 94 ALA H 102 1 9
HELIX 78 78 SER H 105 GLY H 111 1 7
HELIX 79 79 SER H 124 PHE H 136 1 13
HELIX 80 80 SER H 137 ILE H 141 5 5
HELIX 81 81 LYS I 11 LYS I 17 1 7
HELIX 82 82 ALA I 19 GLU I 30 1 12
HELIX 83 83 THR I 43 TYR I 51 1 9
HELIX 84 84 TYR I 52 ARG I 55 5 4
HELIX 85 85 PHE I 59 SER I 68 1 10
HELIX 86 86 ASP I 81 GLY I 91 1 11
HELIX 87 87 ASP I 94 ALA I 102 1 9
HELIX 88 88 SER I 105 GLY I 111 1 7
HELIX 89 89 SER I 124 PHE I 136 1 13
HELIX 90 90 SER I 137 ILE I 141 5 5
HELIX 91 91 LYS J 11 LYS J 17 1 7
HELIX 92 92 ALA J 19 GLU J 30 1 12
HELIX 93 93 THR J 43 TYR J 51 1 9
HELIX 94 94 TYR J 52 ARG J 55 5 4
HELIX 95 95 PHE J 59 SER J 68 1 10
HELIX 96 96 ASP J 81 GLY J 91 1 11
HELIX 97 97 ASP J 94 ALA J 102 1 9
HELIX 98 98 SER J 105 GLY J 111 1 7
HELIX 99 99 SER J 124 PHE J 136 1 13
HELIX 100 100 SER J 137 ILE J 141 5 5
HELIX 101 101 LYS K 11 LYS K 17 1 7
HELIX 102 102 ALA K 19 GLU K 30 1 12
HELIX 103 103 THR K 43 TYR K 51 1 9
HELIX 104 104 TYR K 52 ARG K 55 5 4
HELIX 105 105 PHE K 59 SER K 68 1 10
HELIX 106 106 ASP K 81 GLY K 91 1 11
HELIX 107 107 ASP K 94 ALA K 102 1 9
HELIX 108 108 SER K 105 GLY K 111 1 7
HELIX 109 109 SER K 124 PHE K 136 1 13
HELIX 110 110 SER K 137 ILE K 141 5 5
HELIX 111 111 LYS L 11 LYS L 17 1 7
HELIX 112 112 ALA L 19 GLU L 30 1 12
HELIX 113 113 THR L 43 TYR L 51 1 9
HELIX 114 114 TYR L 52 ARG L 55 5 4
HELIX 115 115 PHE L 59 SER L 68 1 10
HELIX 116 116 ASP L 81 GLY L 91 1 11
HELIX 117 117 ASP L 94 ALA L 102 1 9
HELIX 118 118 SER L 105 GLY L 111 1 7
HELIX 119 119 SER L 124 PHE L 136 1 13
HELIX 120 120 SER L 137 ILE L 141 5 5
SHEET 1 AA 4 GLN A 33 PHE A 40 0
SHEET 2 AA 4 VAL A 72 GLU A 80 -1 O VAL A 72 N PHE A 40
SHEET 3 AA 4 VAL A 3 VAL A 10 -1 O GLU A 4 N GLY A 79
SHEET 4 AA 4 ILE A 119 ALA A 121 -1 O HIS A 120 N ILE A 9
SHEET 1 BA 4 GLN B 33 PHE B 40 0
SHEET 2 BA 4 VAL B 72 GLU B 80 -1 O VAL B 72 N PHE B 40
SHEET 3 BA 4 VAL B 3 VAL B 10 -1 O GLU B 4 N GLY B 79
SHEET 4 BA 4 ILE B 119 ALA B 121 -1 O HIS B 120 N ILE B 9
SHEET 1 CA 4 GLN C 33 PHE C 40 0
SHEET 2 CA 4 VAL C 72 GLU C 80 -1 O VAL C 72 N PHE C 40
SHEET 3 CA 4 VAL C 3 VAL C 10 -1 O GLU C 4 N GLY C 79
SHEET 4 CA 4 ILE C 119 ALA C 121 -1 O HIS C 120 N ILE C 9
SHEET 1 DA 4 GLN D 33 PHE D 40 0
SHEET 2 DA 4 VAL D 72 GLU D 80 -1 O VAL D 72 N PHE D 40
SHEET 3 DA 4 VAL D 3 VAL D 10 -1 O GLU D 4 N GLY D 79
SHEET 4 DA 4 ILE D 119 ALA D 121 -1 O HIS D 120 N ILE D 9
SHEET 1 EA 4 GLN E 33 PHE E 40 0
SHEET 2 EA 4 VAL E 72 GLU E 80 -1 O VAL E 72 N PHE E 40
SHEET 3 EA 4 VAL E 3 VAL E 10 -1 O GLU E 4 N GLY E 79
SHEET 4 EA 4 ILE E 119 ALA E 121 -1 O HIS E 120 N ILE E 9
SHEET 1 FA 4 GLN F 33 PHE F 40 0
SHEET 2 FA 4 VAL F 72 GLU F 80 -1 O VAL F 72 N PHE F 40
SHEET 3 FA 4 VAL F 3 VAL F 10 -1 O GLU F 4 N GLY F 79
SHEET 4 FA 4 ILE F 119 ALA F 121 -1 O HIS F 120 N ILE F 9
SHEET 1 GA 4 GLN G 33 PHE G 40 0
SHEET 2 GA 4 VAL G 72 GLU G 80 -1 O VAL G 72 N PHE G 40
SHEET 3 GA 4 VAL G 3 VAL G 10 -1 O GLU G 4 N GLY G 79
SHEET 4 GA 4 ILE G 119 ALA G 121 -1 O HIS G 120 N ILE G 9
SHEET 1 HA 4 GLN H 33 PHE H 40 0
SHEET 2 HA 4 VAL H 72 GLU H 80 -1 O VAL H 72 N PHE H 40
SHEET 3 HA 4 VAL H 3 VAL H 10 -1 O GLU H 4 N GLY H 79
SHEET 4 HA 4 ILE H 119 ALA H 121 -1 O HIS H 120 N ILE H 9
SHEET 1 IA 4 GLN I 33 PHE I 40 0
SHEET 2 IA 4 VAL I 72 GLU I 80 -1 O VAL I 72 N PHE I 40
SHEET 3 IA 4 VAL I 3 VAL I 10 -1 O GLU I 4 N GLY I 79
SHEET 4 IA 4 ILE I 119 ALA I 121 -1 O HIS I 120 N ILE I 9
SHEET 1 JA 4 GLN J 33 PHE J 40 0
SHEET 2 JA 4 VAL J 72 GLU J 80 -1 O VAL J 72 N PHE J 40
SHEET 3 JA 4 VAL J 3 VAL J 10 -1 O GLU J 4 N GLY J 79
SHEET 4 JA 4 ILE J 119 ALA J 121 -1 O HIS J 120 N ILE J 9
SHEET 1 KA 4 GLN K 33 PHE K 40 0
SHEET 2 KA 4 VAL K 72 GLU K 80 -1 O VAL K 72 N PHE K 40
SHEET 3 KA 4 VAL K 3 VAL K 10 -1 O GLU K 4 N GLY K 79
SHEET 4 KA 4 ILE K 119 ALA K 121 -1 O HIS K 120 N ILE K 9
SHEET 1 LA 4 GLN L 33 PHE L 40 0
SHEET 2 LA 4 VAL L 72 GLU L 80 -1 O VAL L 72 N PHE L 40
SHEET 3 LA 4 VAL L 3 VAL L 10 -1 O GLU L 4 N GLY L 79
SHEET 4 LA 4 ILE L 119 ALA L 121 -1 O HIS L 120 N ILE L 9
SSBOND 1 CYS A 133 CYS C 133 1555 1555 2.04
SSBOND 2 CYS I 133 CYS K 133 1555 1555 2.05
CRYST1 200.709 200.709 246.731 90.00 90.00 120.00 P 61 2 2 144
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 0.004982 0.002877 0.000000 0.00000
SCALE2 0.000000 0.005753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004053 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
