HEADER TRANSFERASE 28-MAR-14 4CVN
TITLE STRUCTURE OF THE FAP7-RPS14 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ADENYLATE KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AK, ATP-AMP TRANSPHOSPHORYLASE, AFAP7;
COMPND 5 EC: 2.7.4.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 SYNONYM: ARPS14;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS ABYSSI GE5;
SOURCE 3 ORGANISM_TAXID: 272844;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: PYROCOCCUS ABYSSI GE5;
SOURCE 11 ORGANISM_TAXID: 272844;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS TRANSFERASE, RIBOSOME BIOGENESIS, RNP ASSEMBLY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LOCH,M.BLAUD,S.RETY,S.LEBARON,P.DESCHAMPS,J.BAREILLE,J.JOMBART,
AUTHOR 2 J.ROBERT-PAGANIN,L.DELBOS,F.CHARDON,E.ZHANG,C.CHARENTON,D.TOLLERVEY,
AUTHOR 3 N.LEULLIOT
REVDAT 1 28-MAY-14 4CVN 0
JRNL AUTH J.LOCH,M.BLAUD,S.RETY,S.LEBARON,P.DESCHAMPS,J.BAREILLE,
JRNL AUTH 2 J.JOMBART,J.ROBERT-PAGANIN,L.DELBOS,F.CHARDON,E.ZHANG,
JRNL AUTH 3 C.CHARENTON,D.TOLLERVEY,N.LEULLIOT
JRNL TITL RNA MIMICRY BY THE FAP7 ADENYLATE KINASE IN RIBOSOME
JRNL TITL 2 BIOGENESIS
JRNL REF PLOS BIOL. V. 12 01860 2014
JRNL REFN ISSN 1544-9173
JRNL PMID 24823650
JRNL DOI 10.1371/JOURNAL.PBIO.1001860
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.121
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.766
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.00
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.46
REMARK 3 NUMBER OF REFLECTIONS : 82650
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1741
REMARK 3 R VALUE (WORKING SET) : 0.1721
REMARK 3 FREE R VALUE : 0.2125
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4132
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 44.7759 - 6.5848 0.99 2668 140 0.1647 0.1620
REMARK 3 2 6.5848 - 5.2291 1.00 2635 139 0.1774 0.1844
REMARK 3 3 5.2291 - 4.5689 1.00 2662 140 0.1440 0.1798
REMARK 3 4 4.5689 - 4.1514 1.00 2606 137 0.1332 0.1733
REMARK 3 5 4.1514 - 3.8541 1.00 2655 140 0.1484 0.1929
REMARK 3 6 3.8541 - 3.6269 1.00 2628 138 0.1548 0.2185
REMARK 3 7 3.6269 - 3.4454 1.00 2622 138 0.1627 0.1898
REMARK 3 8 3.4454 - 3.2954 1.00 2639 139 0.1762 0.1985
REMARK 3 9 3.2954 - 3.1686 1.00 2625 138 0.1754 0.2596
REMARK 3 10 3.1686 - 3.0593 1.00 2612 138 0.1851 0.2238
REMARK 3 11 3.0593 - 2.9637 1.00 2636 139 0.1899 0.2572
REMARK 3 12 2.9637 - 2.8790 1.00 2628 138 0.1858 0.2184
REMARK 3 13 2.8790 - 2.8032 1.00 2624 138 0.1907 0.2497
REMARK 3 14 2.8032 - 2.7348 1.00 2652 140 0.1827 0.2268
REMARK 3 15 2.7348 - 2.6726 1.00 2595 136 0.1829 0.2420
REMARK 3 16 2.6726 - 2.6158 1.00 2632 139 0.1886 0.2431
REMARK 3 17 2.6158 - 2.5635 1.00 2653 139 0.1950 0.2502
REMARK 3 18 2.5635 - 2.5151 1.00 2626 139 0.1877 0.2742
REMARK 3 19 2.5151 - 2.4702 1.00 2597 136 0.1973 0.2353
REMARK 3 20 2.4702 - 2.4283 1.00 2641 139 0.1877 0.2415
REMARK 3 21 2.4283 - 2.3891 1.00 2592 137 0.1890 0.2725
REMARK 3 22 2.3891 - 2.3524 1.00 2620 138 0.1958 0.2748
REMARK 3 23 2.3524 - 2.3178 1.00 2640 138 0.1992 0.2501
REMARK 3 24 2.3178 - 2.2851 1.00 2622 138 0.2034 0.2329
REMARK 3 25 2.2851 - 2.2543 1.00 2590 137 0.2113 0.2575
REMARK 3 26 2.2543 - 2.2250 1.00 2616 137 0.2129 0.2711
REMARK 3 27 2.2250 - 2.1972 1.00 2658 140 0.2122 0.2535
REMARK 3 28 2.1972 - 2.1707 1.00 2607 138 0.2168 0.2699
REMARK 3 29 2.1707 - 2.1455 1.00 2623 138 0.2299 0.2835
REMARK 3 30 2.1455 - 2.1214 0.88 2314 121 0.2517 0.2905
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.23
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.11
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 : 0.008 9392
REMARK 3 ANGLE : 1.285 12710
REMARK 3 CHIRALITY : 0.087 1456
REMARK 3 PLANARITY : 0.007 1621
REMARK 3 DIHEDRAL : 13.928 3567
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 51
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 0 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9876 88.8754 11.7414
REMARK 3 T TENSOR
REMARK 3 T11: 0.5378 T22: 0.3862
REMARK 3 T33: 0.2637 T12: 0.0485
REMARK 3 T13: 0.0826 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 3.4698 L22: 5.4620
REMARK 3 L33: 4.9157 L12: 1.2821
REMARK 3 L13: -1.7426 L23: -1.9013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0410 S12: -0.3706 S13: 0.1021
REMARK 3 S21: 0.6112 S22: 0.2371 S23: 0.2307
REMARK 3 S31: -0.1252 S32: -0.2445 S33: -0.3231
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 25 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5893 82.9144 15.4291
REMARK 3 T TENSOR
REMARK 3 T11: 0.8285 T22: 0.4395
REMARK 3 T33: 0.1579 T12: 0.1095
REMARK 3 T13: 0.0521 T23: 0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 6.3686 L22: 3.7064
REMARK 3 L33: 3.9783 L12: -1.0002
REMARK 3 L13: -1.6370 L23: 0.1216
REMARK 3 S TENSOR
REMARK 3 S11: -0.2923 S12: -0.7201 S13: -0.1173
REMARK 3 S21: 1.3627 S22: 0.5479 S23: -0.2912
REMARK 3 S31: -0.2896 S32: -0.2052 S33: -0.0570
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 38 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0653 82.2375 8.1649
REMARK 3 T TENSOR
REMARK 3 T11: 0.9380 T22: 0.8855
REMARK 3 T33: 0.7017 T12: -0.0502
REMARK 3 T13: -0.2336 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 5.3448 L22: 5.2412
REMARK 3 L33: 4.8634 L12: 5.3044
REMARK 3 L13: -5.1689 L23: -5.1113
REMARK 3 S TENSOR
REMARK 3 S11: 0.3453 S12: -1.0743 S13: -0.3771
REMARK 3 S21: 0.9751 S22: -0.3114 S23: -0.9014
REMARK 3 S31: -0.2286 S32: 2.1009 S33: 0.1255
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 52 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7286 74.5077 10.9274
REMARK 3 T TENSOR
REMARK 3 T11: 0.7569 T22: 0.3549
REMARK 3 T33: 0.4073 T12: -0.0229
REMARK 3 T13: 0.1312 T23: 0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 2.8504 L22: 7.5607
REMARK 3 L33: 8.4749 L12: -0.7874
REMARK 3 L13: -4.4812 L23: -1.8038
REMARK 3 S TENSOR
REMARK 3 S11: -0.9652 S12: -0.6397 S13: -0.5814
REMARK 3 S21: 0.5917 S22: 0.3263 S23: -0.1877
REMARK 3 S31: 0.9492 S32: 0.0313 S33: 0.5215
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 72 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7965 84.7748 3.8315
REMARK 3 T TENSOR
REMARK 3 T11: 0.4759 T22: 0.2895
REMARK 3 T33: 0.2460 T12: -0.0113
REMARK 3 T13: 0.0801 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.6097 L22: 4.7033
REMARK 3 L33: 5.3847 L12: 1.1372
REMARK 3 L13: -0.5269 L23: -4.5379
REMARK 3 S TENSOR
REMARK 3 S11: -0.1228 S12: -0.2050 S13: -0.1620
REMARK 3 S21: 0.5333 S22: 0.1142 S23: 0.2551
REMARK 3 S31: 0.3187 S32: -0.2527 S33: 0.1270
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 90 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8186 103.7151 5.0544
REMARK 3 T TENSOR
REMARK 3 T11: 0.7166 T22: 0.3344
REMARK 3 T33: 0.3899 T12: 0.0358
REMARK 3 T13: -0.1254 T23: -0.0802
REMARK 3 L TENSOR
REMARK 3 L11: 2.9312 L22: 5.1386
REMARK 3 L33: 5.5877 L12: 1.7233
REMARK 3 L13: 0.7039 L23: 0.5056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.5514 S13: 1.2536
REMARK 3 S21: 1.1295 S22: -0.3408 S23: -0.2375
REMARK 3 S31: -1.1455 S32: -0.0187 S33: 0.2232
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESID 104 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0562 99.6631 -2.6444
REMARK 3 T TENSOR
REMARK 3 T11: 0.4326 T22: 0.2579
REMARK 3 T33: 0.3428 T12: -0.0336
REMARK 3 T13: -0.0428 T23: 0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 2.1001 L22: 7.4283
REMARK 3 L33: 7.1534 L12: 0.5293
REMARK 3 L13: 1.6227 L23: 1.8091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: 0.0584 S13: 0.0827
REMARK 3 S21: 0.1953 S22: -0.2675 S23: -0.8257
REMARK 3 S31: -0.5402 S32: 0.4583 S33: 0.1679
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESID 116 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7361 88.6983 -1.1078
REMARK 3 T TENSOR
REMARK 3 T11: 0.4065 T22: 0.2572
REMARK 3 T33: 0.2202 T12: 0.0023
REMARK 3 T13: 0.0537 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 6.2535 L22: 3.3696
REMARK 3 L33: 5.7372 L12: 0.6021
REMARK 3 L13: -1.4035 L23: -2.3105
REMARK 3 S TENSOR
REMARK 3 S11: -0.1039 S12: 0.0345 S13: -0.1383
REMARK 3 S21: 0.3718 S22: 0.3870 S23: 0.2431
REMARK 3 S31: -0.0372 S32: -0.4460 S33: -0.2530
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESID 140 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0870 91.9938 11.1790
REMARK 3 T TENSOR
REMARK 3 T11: 0.6019 T22: 0.6531
REMARK 3 T33: 0.5609 T12: 0.1579
REMARK 3 T13: 0.2886 T23: 0.1114
REMARK 3 L TENSOR
REMARK 3 L11: 3.9849 L22: 4.0238
REMARK 3 L33: 8.3529 L12: 3.9070
REMARK 3 L13: 0.7016 L23: -0.9151
REMARK 3 S TENSOR
REMARK 3 S11: -0.2462 S12: -0.5371 S13: 0.5600
REMARK 3 S21: 1.2540 S22: 0.1701 S23: 1.7537
REMARK 3 S31: -0.3935 S32: -1.5842 S33: -0.0682
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESID 153 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9288 98.6040 -5.1227
REMARK 3 T TENSOR
REMARK 3 T11: 0.2910 T22: 0.2429
REMARK 3 T33: 0.3031 T12: 0.0445
REMARK 3 T13: -0.0338 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 5.5500 L22: 1.0729
REMARK 3 L33: 6.3953 L12: 1.5625
REMARK 3 L13: -2.9915 L23: -2.2027
REMARK 3 S TENSOR
REMARK 3 S11: -0.1332 S12: -0.0023 S13: -0.3048
REMARK 3 S21: 0.0014 S22: 0.1209 S23: -0.0515
REMARK 3 S31: -0.2263 S32: -0.4195 S33: -0.1015
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESID 0 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8540 75.3376 31.2719
REMARK 3 T TENSOR
REMARK 3 T11: 0.3714 T22: 0.3787
REMARK 3 T33: 0.2572 T12: -0.0554
REMARK 3 T13: 0.0989 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 7.7264 L22: 5.3744
REMARK 3 L33: 6.5836 L12: 0.2683
REMARK 3 L13: 4.7484 L23: 1.6101
REMARK 3 S TENSOR
REMARK 3 S11: 0.2401 S12: 0.6346 S13: -0.2428
REMARK 3 S21: -0.5633 S22: -0.0817 S23: -0.1383
REMARK 3 S31: 0.4532 S32: 0.0268 S33: -0.1350
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESID 25 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8169 83.5385 27.4018
REMARK 3 T TENSOR
REMARK 3 T11: 0.4242 T22: 0.5456
REMARK 3 T33: 0.2321 T12: 0.0383
REMARK 3 T13: 0.0572 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 3.6358 L22: 9.3201
REMARK 3 L33: 6.6190 L12: -3.6843
REMARK 3 L13: 1.2786 L23: 4.1515
REMARK 3 S TENSOR
REMARK 3 S11: 0.3761 S12: 0.4477 S13: 0.2967
REMARK 3 S21: -1.3560 S22: -0.1955 S23: -0.6865
REMARK 3 S31: -0.0627 S32: -0.0155 S33: -0.1368
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESID 38 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7768 91.2840 34.2457
REMARK 3 T TENSOR
REMARK 3 T11: 0.2969 T22: 0.5136
REMARK 3 T33: 0.3475 T12: 0.0355
REMARK 3 T13: -0.0049 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 4.7905 L22: 8.4048
REMARK 3 L33: 3.7186 L12: 6.5368
REMARK 3 L13: 4.3349 L23: 5.6118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0647 S12: -0.1167 S13: 0.6564
REMARK 3 S21: -0.6042 S22: -0.5122 S23: 0.7622
REMARK 3 S31: -0.4118 S32: -0.8151 S33: 0.4959
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESID 64 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9841 78.0293 35.6215
REMARK 3 T TENSOR
REMARK 3 T11: 0.2599 T22: 0.4821
REMARK 3 T33: 0.3033 T12: -0.0999
REMARK 3 T13: 0.0041 T23: -0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 2.7106 L22: 5.2730
REMARK 3 L33: 4.7996 L12: -1.8271
REMARK 3 L13: -0.3952 L23: 0.2861
REMARK 3 S TENSOR
REMARK 3 S11: 0.2608 S12: 0.1325 S13: -0.3899
REMARK 3 S21: -0.3179 S22: -0.3241 S23: 0.4937
REMARK 3 S31: 0.1697 S32: -0.7947 S33: 0.0764
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESID 90 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8997 84.4511 41.2512
REMARK 3 T TENSOR
REMARK 3 T11: 0.2400 T22: 0.5270
REMARK 3 T33: 0.3785 T12: -0.0489
REMARK 3 T13: 0.0559 T23: 0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 3.8222 L22: 2.2844
REMARK 3 L33: 2.4282 L12: 1.6207
REMARK 3 L13: -2.2644 L23: -2.0690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: 0.5278 S13: 0.1901
REMARK 3 S21: -0.1873 S22: 0.0060 S23: -0.5208
REMARK 3 S31: 0.0325 S32: 0.5528 S33: 0.0120
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESID 116 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2899 73.8387 44.1298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2823 T22: 0.3195
REMARK 3 T33: 0.2072 T12: -0.0908
REMARK 3 T13: 0.0378 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 4.4774 L22: 7.8018
REMARK 3 L33: 7.6402 L12: -0.1252
REMARK 3 L13: 1.8162 L23: 2.0096
REMARK 3 S TENSOR
REMARK 3 S11: 0.3681 S12: 0.0193 S13: -0.0958
REMARK 3 S21: 0.0643 S22: -0.0692 S23: 0.1709
REMARK 3 S31: 0.5352 S32: -0.5017 S33: -0.3269
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESID 140 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9004 65.0041 32.1340
REMARK 3 T TENSOR
REMARK 3 T11: 0.5454 T22: 0.4214
REMARK 3 T33: 0.4420 T12: 0.0015
REMARK 3 T13: -0.0732 T23: -0.1503
REMARK 3 L TENSOR
REMARK 3 L11: 1.2569 L22: 7.8440
REMARK 3 L33: 9.6192 L12: 0.9151
REMARK 3 L13: -0.6935 L23: -3.3509
REMARK 3 S TENSOR
REMARK 3 S11: 0.6184 S12: 1.2017 S13: -1.8249
REMARK 3 S21: -0.8957 S22: -0.1192 S23: -0.5258
REMARK 3 S31: 1.6791 S32: -0.3816 S33: -0.0989
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND (RESID 153 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2944 73.7537 48.3021
REMARK 3 T TENSOR
REMARK 3 T11: 0.2194 T22: 0.3177
REMARK 3 T33: 0.3717 T12: -0.0081
REMARK 3 T13: 0.0327 T23: 0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 0.3888 L22: 5.2984
REMARK 3 L33: 5.4939 L12: 0.9363
REMARK 3 L13: 1.4748 L23: 2.1706
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: 0.0479 S13: 0.2984
REMARK 3 S21: -0.0015 S22: 0.2110 S23: 0.1881
REMARK 3 S31: 0.5098 S32: 0.1823 S33: -0.1312
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN C AND (RESID 1 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8992 115.8240 21.4122
REMARK 3 T TENSOR
REMARK 3 T11: 0.8518 T22: 0.5975
REMARK 3 T33: 0.7218 T12: -0.0568
REMARK 3 T13: -0.3940 T23: 0.1067
REMARK 3 L TENSOR
REMARK 3 L11: 1.2082 L22: 4.4476
REMARK 3 L33: 6.4401 L12: 1.2026
REMARK 3 L13: -2.2416 L23: 0.6417
REMARK 3 S TENSOR
REMARK 3 S11: -0.3832 S12: 0.3832 S13: 0.5267
REMARK 3 S21: -0.4362 S22: -0.0371 S23: 0.1372
REMARK 3 S31: -1.4010 S32: -0.3611 S33: 0.4256
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN C AND (RESID 38 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3179 100.7633 10.3326
REMARK 3 T TENSOR
REMARK 3 T11: 0.8528 T22: 0.8078
REMARK 3 T33: 0.6999 T12: -0.2575
REMARK 3 T13: -0.1978 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 9.1320 L22: 3.6890
REMARK 3 L33: 4.0359 L12: -1.3563
REMARK 3 L13: 3.3473 L23: 2.6403
REMARK 3 S TENSOR
REMARK 3 S11: 0.3839 S12: 0.5374 S13: -1.4914
REMARK 3 S21: -1.3772 S22: 0.0371 S23: 0.4422
REMARK 3 S31: 0.2593 S32: 0.3162 S33: -0.0769
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN C AND (RESID 52 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5814 115.8944 13.6187
REMARK 3 T TENSOR
REMARK 3 T11: 1.1304 T22: 0.8845
REMARK 3 T33: 0.6884 T12: -0.3643
REMARK 3 T13: -0.2259 T23: 0.2128
REMARK 3 L TENSOR
REMARK 3 L11: 8.9219 L22: 4.4243
REMARK 3 L33: 7.1743 L12: -3.1151
REMARK 3 L13: -0.8020 L23: -1.2041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: 0.3640 S13: 1.1437
REMARK 3 S21: -1.0849 S22: 0.1403 S23: -0.6364
REMARK 3 S31: -1.3433 S32: 1.1730 S33: -0.1191
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN C AND (RESID 72 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6843 107.1985 33.3001
REMARK 3 T TENSOR
REMARK 3 T11: 0.5466 T22: 0.5755
REMARK 3 T33: 0.4993 T12: 0.0245
REMARK 3 T13: -0.2231 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 3.0124 L22: 4.5899
REMARK 3 L33: 4.7266 L12: -0.2919
REMARK 3 L13: -0.2942 L23: -2.3768
REMARK 3 S TENSOR
REMARK 3 S11: -0.4419 S12: 0.2279 S13: 0.3166
REMARK 3 S21: -0.0667 S22: 0.2859 S23: 0.4759
REMARK 3 S31: -0.8879 S32: -0.4357 S33: 0.1513
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN D AND (RESID 1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6903 48.6904 18.5386
REMARK 3 T TENSOR
REMARK 3 T11: 0.6975 T22: 0.7230
REMARK 3 T33: 1.3381 T12: -0.1939
REMARK 3 T13: -0.6003 T23: 0.5484
REMARK 3 L TENSOR
REMARK 3 L11: 1.7493 L22: 0.0488
REMARK 3 L33: 4.0657 L12: -0.0822
REMARK 3 L13: 0.9359 L23: 0.1727
REMARK 3 S TENSOR
REMARK 3 S11: 0.4178 S12: -0.6852 S13: -0.5811
REMARK 3 S21: 1.1927 S22: -0.5951 S23: -1.5711
REMARK 3 S31: 0.1519 S32: 0.7927 S33: 0.1678
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN D AND (RESID 25 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8854 50.4495 28.6842
REMARK 3 T TENSOR
REMARK 3 T11: 1.5577 T22: 1.2452
REMARK 3 T33: 1.0328 T12: -0.5657
REMARK 3 T13: -1.1772 T23: 0.7464
REMARK 3 L TENSOR
REMARK 3 L11: 1.8688 L22: 1.5212
REMARK 3 L33: 3.3851 L12: -0.7513
REMARK 3 L13: 1.2969 L23: -0.9968
REMARK 3 S TENSOR
REMARK 3 S11: -0.2884 S12: -0.7054 S13: 0.3666
REMARK 3 S21: 0.7018 S22: -0.4658 S23: -0.7439
REMARK 3 S31: 0.3805 S32: 0.4593 S33: -0.0106
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN D AND (RESID 38 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5806 58.1348 24.7656
REMARK 3 T TENSOR
REMARK 3 T11: 1.5540 T22: 0.9143
REMARK 3 T33: 1.0010 T12: -0.5603
REMARK 3 T13: -1.0150 T23: 0.2227
REMARK 3 L TENSOR
REMARK 3 L11: 4.9475 L22: 0.8264
REMARK 3 L33: 0.2093 L12: -0.2293
REMARK 3 L13: -0.1121 L23: 0.2036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: -1.2955 S13: 0.6841
REMARK 3 S21: 2.5122 S22: -0.8073 S23: -1.2706
REMARK 3 S31: -0.5322 S32: 0.6843 S33: 0.2299
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN D AND (RESID 90 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0647 42.0073 12.1268
REMARK 3 T TENSOR
REMARK 3 T11: 0.4276 T22: 0.2783
REMARK 3 T33: 0.4716 T12: -0.0395
REMARK 3 T13: -0.1129 T23: 0.1268
REMARK 3 L TENSOR
REMARK 3 L11: 6.9330 L22: 8.1672
REMARK 3 L33: 9.1371 L12: 4.2591
REMARK 3 L13: -4.5975 L23: -6.2154
REMARK 3 S TENSOR
REMARK 3 S11: -0.3495 S12: -0.1538 S13: -0.2897
REMARK 3 S21: 0.1224 S22: -0.4337 S23: -1.1286
REMARK 3 S31: 0.6894 S32: 0.6523 S33: 0.7334
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN D AND (RESID 104 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3262 49.9863 12.0577
REMARK 3 T TENSOR
REMARK 3 T11: 0.5207 T22: 0.2595
REMARK 3 T33: 0.3696 T12: -0.0526
REMARK 3 T13: -0.1352 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 7.1121 L22: 4.2821
REMARK 3 L33: 5.8520 L12: 5.3667
REMARK 3 L13: -4.1063 L23: -4.1891
REMARK 3 S TENSOR
REMARK 3 S11: 0.1581 S12: -0.3784 S13: 0.4152
REMARK 3 S21: 0.6243 S22: -0.3816 S23: -0.2456
REMARK 3 S31: -0.4923 S32: 0.3491 S33: 0.2599
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN D AND (RESID 116 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0410 57.5552 10.5232
REMARK 3 T TENSOR
REMARK 3 T11: 0.6792 T22: 0.6938
REMARK 3 T33: 1.1913 T12: -0.1879
REMARK 3 T13: -0.6990 T23: 0.5290
REMARK 3 L TENSOR
REMARK 3 L11: 1.4095 L22: 0.3983
REMARK 3 L33: 2.8225 L12: -0.0430
REMARK 3 L13: -0.5566 L23: -1.0397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.7438 S13: 0.0102
REMARK 3 S21: 1.7446 S22: -1.2687 S23: -1.7435
REMARK 3 S31: -0.0741 S32: 1.2912 S33: 0.2387
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN D AND (RESID 140 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9228 47.7895 10.5634
REMARK 3 T TENSOR
REMARK 3 T11: 0.5477 T22: 1.0656
REMARK 3 T33: 1.5554 T12: 0.0001
REMARK 3 T13: -0.2718 T23: 0.6169
REMARK 3 L TENSOR
REMARK 3 L11: 4.4625 L22: 2.7335
REMARK 3 L33: 5.2238 L12: 2.7289
REMARK 3 L13: 2.9666 L23: 3.0958
REMARK 3 S TENSOR
REMARK 3 S11: 0.1356 S12: 0.6351 S13: -0.6797
REMARK 3 S21: 0.2604 S22: 0.1679 S23: -1.6188
REMARK 3 S31: 0.1519 S32: 1.3891 S33: -0.1398
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN D AND (RESID 154 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6196 59.2779 6.4279
REMARK 3 T TENSOR
REMARK 3 T11: 0.5645 T22: 0.9940
REMARK 3 T33: 1.7024 T12: -0.7077
REMARK 3 T13: -0.3254 T23: 0.7940
REMARK 3 L TENSOR
REMARK 3 L11: 1.3048 L22: 0.9082
REMARK 3 L33: 0.3929 L12: -0.3742
REMARK 3 L13: -0.6491 L23: 0.5238
REMARK 3 S TENSOR
REMARK 3 S11: 0.9756 S12: -0.4344 S13: 0.8426
REMARK 3 S21: 0.3644 S22: -0.8639 S23: -1.1786
REMARK 3 S31: -0.5542 S32: 0.7954 S33: 0.0194
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN D AND (RESID 164 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1961 48.9898 1.7854
REMARK 3 T TENSOR
REMARK 3 T11: 0.4797 T22: 0.2263
REMARK 3 T33: 0.4286 T12: -0.0890
REMARK 3 T13: -0.0775 T23: 0.0802
REMARK 3 L TENSOR
REMARK 3 L11: 3.3338 L22: 5.7698
REMARK 3 L33: 5.2632 L12: 1.4339
REMARK 3 L13: 0.1120 L23: -0.7372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0952 S12: 0.2881 S13: -0.1969
REMARK 3 S21: 0.0201 S22: -0.2513 S23: -0.6207
REMARK 3 S31: 0.4511 S32: -0.1909 S33: 0.2431
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN E AND (RESID 11 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8688 83.8703 61.6080
REMARK 3 T TENSOR
REMARK 3 T11: 0.1723 T22: 0.2812
REMARK 3 T33: 0.4306 T12: -0.0152
REMARK 3 T13: 0.0334 T23: 0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 5.2500 L22: 4.3095
REMARK 3 L33: 8.2514 L12: 1.1087
REMARK 3 L13: 2.1295 L23: 1.5786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.1221 S13: 0.1723
REMARK 3 S21: -0.3069 S22: -0.0037 S23: -0.9609
REMARK 3 S31: -0.6518 S32: 0.3081 S33: 0.0218
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN E AND (RESID 38 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6054 69.8227 61.7188
REMARK 3 T TENSOR
REMARK 3 T11: 0.2484 T22: 0.2603
REMARK 3 T33: 0.3579 T12: 0.0575
REMARK 3 T13: 0.0190 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 3.7754 L22: 9.2479
REMARK 3 L33: 5.0326 L12: 6.0374
REMARK 3 L13: -2.8677 L23: -3.6111
REMARK 3 S TENSOR
REMARK 3 S11: -0.3322 S12: -0.1626 S13: -0.3610
REMARK 3 S21: -0.5917 S22: 0.0901 S23: -0.7221
REMARK 3 S31: 0.5899 S32: 0.1806 S33: 0.2226
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN E AND (RESID 57 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0666 80.0470 67.8806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2676 T22: 0.3688
REMARK 3 T33: 0.3497 T12: 0.0033
REMARK 3 T13: -0.0623 T23: 0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 5.7070 L22: 1.7999
REMARK 3 L33: 3.4186 L12: 0.0645
REMARK 3 L13: 1.6830 L23: 1.9401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0325 S12: -0.3875 S13: -0.1243
REMARK 3 S21: 0.6579 S22: 0.0032 S23: -0.5670
REMARK 3 S31: 0.1521 S32: 0.4803 S33: 0.0209
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN E AND (RESID 86 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7595 77.7895 64.2647
REMARK 3 T TENSOR
REMARK 3 T11: 0.3758 T22: 0.5070
REMARK 3 T33: 0.5786 T12: -0.1593
REMARK 3 T13: 0.0069 T23: 0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 3.4957 L22: 6.0881
REMARK 3 L33: 2.6259 L12: 2.6354
REMARK 3 L13: 0.9684 L23: 0.6246
REMARK 3 S TENSOR
REMARK 3 S11: 0.3436 S12: -0.1546 S13: -0.4075
REMARK 3 S21: 0.2890 S22: 0.0513 S23: 1.0868
REMARK 3 S31: 1.2848 S32: -1.2467 S33: -0.2409
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN E AND (RESID 108 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7160 90.3796 53.9817
REMARK 3 T TENSOR
REMARK 3 T11: 0.2064 T22: 0.2679
REMARK 3 T33: 0.3291 T12: -0.0803
REMARK 3 T13: -0.0001 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 4.9130 L22: 2.5321
REMARK 3 L33: 8.5395 L12: -1.8197
REMARK 3 L13: 5.3211 L23: -2.9567
REMARK 3 S TENSOR
REMARK 3 S11: -0.2786 S12: 0.3269 S13: 0.3360
REMARK 3 S21: 0.0238 S22: -0.0352 S23: -0.0071
REMARK 3 S31: -0.3924 S32: 0.0509 S33: 0.5213
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN E AND (RESID 132 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0772 91.4807 46.5877
REMARK 3 T TENSOR
REMARK 3 T11: 0.8081 T22: 0.6869
REMARK 3 T33: 1.0329 T12: 0.0305
REMARK 3 T13: 0.1671 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 7.8824 L22: 2.5160
REMARK 3 L33: 2.9087 L12: -0.4403
REMARK 3 L13: 3.2177 L23: 1.8407
REMARK 3 S TENSOR
REMARK 3 S11: 0.1511 S12: -1.2541 S13: 1.9866
REMARK 3 S21: 2.8758 S22: 0.3033 S23: 1.8903
REMARK 3 S31: -0.1680 S32: -1.3578 S33: -0.0652
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN F AND (RESID 12 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6464 56.9288 -0.7689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3251 T22: 0.3338
REMARK 3 T33: 0.3706 T12: -0.0347
REMARK 3 T13: -0.0270 T23: 0.1655
REMARK 3 L TENSOR
REMARK 3 L11: 6.5737 L22: 5.4592
REMARK 3 L33: 4.6869 L12: 0.4794
REMARK 3 L13: -0.2922 L23: -0.7839
REMARK 3 S TENSOR
REMARK 3 S11: -0.1511 S12: 0.0235 S13: -0.2847
REMARK 3 S21: 0.3668 S22: 0.0591 S23: 0.1088
REMARK 3 S31: 0.0559 S32: -0.3220 S33: 0.0379
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN F AND (RESID 38 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9683 59.8768 -8.2786
REMARK 3 T TENSOR
REMARK 3 T11: 0.2822 T22: 0.2406
REMARK 3 T33: 0.3472 T12: 0.0507
REMARK 3 T13: -0.0219 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 7.5239 L22: 9.0398
REMARK 3 L33: 6.2454 L12: 4.5860
REMARK 3 L13: -3.7574 L23: -3.5836
REMARK 3 S TENSOR
REMARK 3 S11: -0.0801 S12: -0.3374 S13: -0.5955
REMARK 3 S21: -0.1488 S22: -0.3494 S23: -0.9531
REMARK 3 S31: 0.4208 S32: 0.4158 S33: 0.3615
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN F AND (RESID 57 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5069 64.0225 -9.9044
REMARK 3 T TENSOR
REMARK 3 T11: 0.3558 T22: 0.4036
REMARK 3 T33: 0.3366 T12: -0.0538
REMARK 3 T13: -0.0734 T23: 0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 9.0789 L22: 6.6353
REMARK 3 L33: 3.1083 L12: 6.3228
REMARK 3 L13: -1.5100 L23: -2.2425
REMARK 3 S TENSOR
REMARK 3 S11: -0.2663 S12: 0.9067 S13: 0.7597
REMARK 3 S21: -0.6462 S22: 0.4278 S23: 0.6818
REMARK 3 S31: 0.2545 S32: -0.4443 S33: -0.1358
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN F AND (RESID 74 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8374 64.9888 2.9445
REMARK 3 T TENSOR
REMARK 3 T11: 0.4066 T22: 0.2422
REMARK 3 T33: 0.4018 T12: 0.0270
REMARK 3 T13: 0.0272 T23: 0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 8.5628 L22: 6.8263
REMARK 3 L33: 6.9921 L12: 1.5163
REMARK 3 L13: 2.2674 L23: -0.7853
REMARK 3 S TENSOR
REMARK 3 S11: -0.1806 S12: -0.4762 S13: 0.5722
REMARK 3 S21: 0.7845 S22: 0.1838 S23: 0.1639
REMARK 3 S31: -0.7846 S32: -0.5765 S33: -0.0134
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN F AND (RESID 108 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2778 59.2892 11.2891
REMARK 3 T TENSOR
REMARK 3 T11: 0.6279 T22: 0.4889
REMARK 3 T33: 0.4685 T12: -0.0983
REMARK 3 T13: -0.0954 T23: 0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 9.4137 L22: 6.7746
REMARK 3 L33: 4.0331 L12: -3.8736
REMARK 3 L13: 5.0062 L23: -5.1219
REMARK 3 S TENSOR
REMARK 3 S11: 0.2175 S12: -1.3978 S13: 0.1777
REMARK 3 S21: 0.9868 S22: -0.0198 S23: -0.3348
REMARK 3 S31: 0.1636 S32: -1.0913 S33: -0.4252
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN G AND (RESID 11 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7577 87.6488 45.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.2063 T22: 0.4515
REMARK 3 T33: 0.4433 T12: -0.0790
REMARK 3 T13: 0.0280 T23: -0.0670
REMARK 3 L TENSOR
REMARK 3 L11: 4.4195 L22: 2.2626
REMARK 3 L33: 5.2208 L12: -0.3143
REMARK 3 L13: 1.0957 L23: -0.0476
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: 0.1719 S13: -0.4161
REMARK 3 S21: -0.1178 S22: -0.0767 S23: 0.5338
REMARK 3 S31: 0.3222 S32: -0.6836 S33: 0.1335
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN G AND (RESID 48 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6694 104.4220 51.0305
REMARK 3 T TENSOR
REMARK 3 T11: 0.4707 T22: 0.3756
REMARK 3 T33: 0.4818 T12: -0.0189
REMARK 3 T13: -0.1416 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 6.5661 L22: 5.6213
REMARK 3 L33: 2.0052 L12: 0.2167
REMARK 3 L13: -1.8651 L23: 0.3060
REMARK 3 S TENSOR
REMARK 3 S11: -0.6000 S12: 0.8791 S13: 1.1674
REMARK 3 S21: -0.4229 S22: -0.2665 S23: 0.1168
REMARK 3 S31: -1.5051 S32: 0.2925 S33: 0.6110
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN G AND (RESID 57 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5970 89.0444 52.2275
REMARK 3 T TENSOR
REMARK 3 T11: 0.1891 T22: 0.2880
REMARK 3 T33: 0.3259 T12: 0.0400
REMARK 3 T13: -0.0108 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 6.4949 L22: 9.9274
REMARK 3 L33: 5.4440 L12: 7.5729
REMARK 3 L13: 1.8391 L23: 0.3388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1259 S12: 0.0692 S13: -0.3415
REMARK 3 S21: 0.5998 S22: -0.0353 S23: -0.1896
REMARK 3 S31: -0.0693 S32: -0.2752 S33: 0.0120
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN G AND (RESID 74 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4415 88.9224 39.5505
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.4507
REMARK 3 T33: 0.3402 T12: -0.0766
REMARK 3 T13: 0.0010 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 3.8888 L22: 7.2510
REMARK 3 L33: 8.5126 L12: -1.3622
REMARK 3 L13: 1.5044 L23: -4.0839
REMARK 3 S TENSOR
REMARK 3 S11: -0.1549 S12: 0.6892 S13: 0.0207
REMARK 3 S21: -0.5461 S22: -0.2141 S23: -0.3796
REMARK 3 S31: -0.0788 S32: 0.5261 S33: 0.4510
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN G AND (RESID 108 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1279 89.8312 30.4752
REMARK 3 T TENSOR
REMARK 3 T11: 0.4143 T22: 0.6875
REMARK 3 T33: 0.4070 T12: -0.0375
REMARK 3 T13: -0.0577 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 3.6625 L22: 7.9003
REMARK 3 L33: 3.1325 L12: -1.2088
REMARK 3 L13: 2.6300 L23: -3.9885
REMARK 3 S TENSOR
REMARK 3 S11: -0.3303 S12: 0.6835 S13: 0.0818
REMARK 3 S21: -1.5066 S22: 0.3659 S23: 0.1859
REMARK 3 S31: 0.5618 S32: -0.7333 S33: -0.1142
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN H AND (RESID 12 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9081 104.5878 -18.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2576 T22: 0.1638
REMARK 3 T33: 0.2475 T12: -0.0099
REMARK 3 T13: -0.0352 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 4.3853 L22: 5.1669
REMARK 3 L33: 5.5392 L12: -0.1668
REMARK 3 L13: 0.5994 L23: 1.0844
REMARK 3 S TENSOR
REMARK 3 S11: -0.1962 S12: 0.0369 S13: 0.4273
REMARK 3 S21: 0.0121 S22: 0.0981 S23: -0.4438
REMARK 3 S31: -0.4089 S32: 0.3072 S33: 0.1228
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN H AND (RESID 48 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2191 99.7259 -23.5745
REMARK 3 T TENSOR
REMARK 3 T11: 0.2595 T22: 0.2880
REMARK 3 T33: 0.2513 T12: 0.0474
REMARK 3 T13: -0.0202 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 8.7252 L22: 3.7990
REMARK 3 L33: 2.9505 L12: 4.0930
REMARK 3 L13: -0.5133 L23: 0.9842
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: 0.2493 S13: 0.2848
REMARK 3 S21: 0.0831 S22: 0.0219 S23: 0.5436
REMARK 3 S31: -0.1214 S32: -0.4556 S33: -0.0222
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN H AND (RESID 74 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0809 97.7363 -22.1167
REMARK 3 T TENSOR
REMARK 3 T11: 0.2040 T22: 0.1918
REMARK 3 T33: 0.3104 T12: 0.0001
REMARK 3 T13: 0.0424 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 4.5626 L22: 4.9722
REMARK 3 L33: 7.4113 L12: 2.1247
REMARK 3 L13: -1.4433 L23: -3.2350
REMARK 3 S TENSOR
REMARK 3 S11: -0.2938 S12: 0.0903 S13: -0.2161
REMARK 3 S21: -0.2495 S22: 0.0588 S23: 0.0237
REMARK 3 S31: 0.3150 S32: -0.0048 S33: 0.3062
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN H AND (RESID 108 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4886 92.3893 -9.6720
REMARK 3 T TENSOR
REMARK 3 T11: 0.3577 T22: 0.2121
REMARK 3 T33: 0.3035 T12: -0.0393
REMARK 3 T13: -0.0114 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.9600 L22: 6.1826
REMARK 3 L33: 4.6776 L12: -1.0373
REMARK 3 L13: 1.5654 L23: -5.4975
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0543 S13: -0.1732
REMARK 3 S21: 0.2244 S22: -0.1916 S23: -0.3634
REMARK 3 S31: 0.2173 S32: 0.4982 S33: 0.4630
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 4CVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-14.
REMARK 100 THE PDBE ID CODE IS EBI-60136.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
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) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 312402
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.12
REMARK 200 RESOLUTION RANGE LOW (A) : 80.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M TRIS-HCL PH
REMARK 280 8.5, 25 %(W/V) POLYETHYLENE GLYCOL 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 69.77500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -10
REMARK 465 LYS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 GLY A 179
REMARK 465 GLU A 180
REMARK 465 MET B -10
REMARK 465 LYS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
REMARK 465 ARG B 42
REMARK 465 GLU B 43
REMARK 465 VAL B 44
REMARK 465 ASP B 45
REMARK 465 GLY B 46
REMARK 465 GLU B 47
REMARK 465 GLU B 180
REMARK 465 MET C -10
REMARK 465 LYS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 ALA C -2
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 GLU C 180
REMARK 465 MET D -10
REMARK 465 LYS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 ALA D -2
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 CYS D 40
REMARK 465 GLY D 41
REMARK 465 ARG D 42
REMARK 465 GLU D 43
REMARK 465 VAL D 44
REMARK 465 ASP D 45
REMARK 465 GLY D 46
REMARK 465 GLU D 47
REMARK 465 VAL D 48
REMARK 465 LYS D 61
REMARK 465 GLU D 62
REMARK 465 LEU D 63
REMARK 465 LYS D 64
REMARK 465 ASP D 65
REMARK 465 GLU D 180
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLU E 3
REMARK 465 GLU E 4
REMARK 465 GLN E 5
REMARK 465 VAL E 6
REMARK 465 ASN E 7
REMARK 465 ILE E 8
REMARK 465 LYS E 9
REMARK 465 LYS E 10
REMARK 465 VAL E 137
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 GLU F 3
REMARK 465 GLU F 4
REMARK 465 GLN F 5
REMARK 465 VAL F 6
REMARK 465 ASN F 7
REMARK 465 ILE F 8
REMARK 465 LYS F 9
REMARK 465 LYS F 10
REMARK 465 LYS F 11
REMARK 465 GLY F 130
REMARK 465 GLY F 131
REMARK 465 ARG F 132
REMARK 465 ARG F 133
REMARK 465 GLY F 134
REMARK 465 ARG F 135
REMARK 465 ARG F 136
REMARK 465 VAL F 137
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLU G 3
REMARK 465 GLU G 4
REMARK 465 GLN G 5
REMARK 465 VAL G 6
REMARK 465 ASN G 7
REMARK 465 ILE G 8
REMARK 465 LYS G 9
REMARK 465 LYS G 10
REMARK 465 GLY G 131
REMARK 465 ARG G 132
REMARK 465 ARG G 133
REMARK 465 GLY G 134
REMARK 465 ARG G 135
REMARK 465 ARG G 136
REMARK 465 VAL G 137
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 GLU H 3
REMARK 465 GLU H 4
REMARK 465 GLN H 5
REMARK 465 VAL H 6
REMARK 465 ASN H 7
REMARK 465 ILE H 8
REMARK 465 LYS H 9
REMARK 465 LYS H 10
REMARK 465 LYS H 11
REMARK 465 GLY H 87
REMARK 465 GLY H 88
REMARK 465 LYS H 92
REMARK 465 THR H 93
REMARK 465 PRO H 94
REMARK 465 GLY H 95
REMARK 465 VAL H 137
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 OH TYR A 57 OD2 ASP F 117 2.04
REMARK 500 O GLY A 149 OG SER A 153 2.18
REMARK 500 NH2 ARG A 157 O HOH A 2061 2.15
REMARK 500 NZ LYS B 38 OE1 GLU B 62 2.16
REMARK 500 NH2 ARG B 98 OH TYR B 174 2.16
REMARK 500 NH2 ARG B 100 O3B ADP B 1001 2.13
REMARK 500 OE2 GLU C 95 OH TYR C 174 1.99
REMARK 500 NH1 ARG C 157 O HOH C 2022 2.03
REMARK 500 OE2 GLU C 166 O HOH C 2032 2.08
REMARK 500 OE2 GLU D 166 O HOH D 2047 1.99
REMARK 500 OD1 ASP E 53 O HOH E 2029 2.06
REMARK 500 OE2 GLU E 69 O HOH E 2032 2.14
REMARK 500 NZ LYS E 90 O HOH E 2027 2.07
REMARK 500 NZ LYS G 92 O HOH G 2038 2.12
REMARK 500 O HOH C 2027 O HOH C 2028 2.18
REMARK 500 O HOH D 2047 O HOH D 2048 2.04
REMARK 500 O HOH E 2029 O HOH E 2030 1.95
REMARK 500 O HOH E 2050 O HOH B 2064 2.14
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 C 45 61.16 39.07
REMARK 500 LEU C 175 -78.97 -80.42
REMARK 500 ARG C 176 -137.44 174.23
REMARK 500 LEU C 177 -9.45 98.71
REMARK 500 ASP E 124 145.76 177.10
REMARK 500 LYS F 90 -70.61 -77.17
REMARK 500 ASP H 124 147.39 177.79
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 A 153 GLY A 154 -31.87
REMARK 500 SER B 153 GLY B 154 -33.20
REMARK 500 SER D 153 GLY D 154 -32.51
REMARK 500 HIS E 123 ASP E 124 124.12
REMARK 500 HIS F 123 ASP F 124 121.31
REMARK 500 HIS G 123 ASP G 124 125.38
REMARK 500 HIS H 123 ASP H 124 121.39
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 F2004 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH F2035 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH F2045 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH H2018 DISTANCE = 6.56 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 14 OG1
REMARK 620 2 ADP A1001 O1B 95.0
REMARK 620 3 HOH A2012 O 89.9 100.4
REMARK 620 4 HOH A2013 O 84.4 177.7 81.8
REMARK 620 5 HOH A2049 O 171.9 93.0 87.4 87.7
REMARK 620 6 HOH A2014 O 93.9 91.2 167.4 86.6 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 14 OG1
REMARK 620 2 HOH B2006 O 82.4
REMARK 620 3 HOH B2007 O 80.7 80.6
REMARK 620 4 ADP B1001 O1B 92.5 173.6 102.5
REMARK 620 5 HOH B2008 O 86.3 86.9 163.0 88.9
REMARK 620 6 HOH B2053 O 167.7 86.3 92.9 99.1 97.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2004 O
REMARK 620 2 THR C 14 OG1 81.4
REMARK 620 3 ADP C1001 O2B 148.5 88.9
REMARK 620 4 HOH C2005 O 98.3 99.6 112.9
REMARK 620 5 HOH C2006 O 72.7 81.5 76.2 170.8
REMARK 620 6 HOH C2041 O 87.5 160.3 92.2 98.1 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D1001 O2B
REMARK 620 2 THR D 14 OG1 107.4
REMARK 620 3 HOH D2004 O 166.1 86.2
REMARK 620 4 HOH D2005 O 88.3 107.0 84.9
REMARK 620 5 HOH D2006 O 101.4 89.4 81.1 157.7
REMARK 620 6 HOH D2026 O 89.2 162.1 77.7 79.6 80.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CW7 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE FAP7-RPS14 COMPLEX IN COMPLEX WITH
REMARK 900 ATP
DBREF 4CVN A 1 180 UNP Q9UZK4 KAD6_PYRAB 1 180
DBREF 4CVN B 1 180 UNP Q9UZK4 KAD6_PYRAB 1 180
DBREF 4CVN C 1 180 UNP Q9UZK4 KAD6_PYRAB 1 180
DBREF 4CVN D 1 180 UNP Q9UZK4 KAD6_PYRAB 1 180
DBREF 4CVN E 1 137 UNP P62010 RS11_PYRAB 1 137
DBREF 4CVN F 1 137 UNP P62010 RS11_PYRAB 1 137
DBREF 4CVN G 1 137 UNP P62010 RS11_PYRAB 1 137
DBREF 4CVN H 1 137 UNP P62010 RS11_PYRAB 1 137
SEQADV 4CVN MET A -10 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN LYS A -9 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -8 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -7 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -6 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -5 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -4 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS A -3 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN ALA A -2 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET A -1 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN GLY A 0 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET B -10 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN LYS B -9 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -8 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -7 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -6 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -5 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -4 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS B -3 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN ALA B -2 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET B -1 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN GLY B 0 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET C -10 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN LYS C -9 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -8 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -7 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -6 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -5 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -4 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS C -3 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN ALA C -2 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET C -1 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN GLY C 0 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET D -10 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN LYS D -9 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -8 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -7 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -6 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -5 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -4 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN HIS D -3 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN ALA D -2 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN MET D -1 UNP Q9UZK4 EXPRESSION TAG
SEQADV 4CVN GLY D 0 UNP Q9UZK4 EXPRESSION TAG
SEQRES 1 A 191 MET LYS HIS HIS HIS HIS HIS HIS ALA MET GLY MET LEU
SEQRES 2 A 191 ILE ALA ILE THR GLY THR PRO GLY VAL GLY LYS THR THR
SEQRES 3 A 191 ILE ALA LYS LEU LEU ALA GLU LYS LEU GLY TYR GLU TYR
SEQRES 4 A 191 VAL ASN LEU ARG ASP PHE ALA LEU GLU LYS GLY CYS GLY
SEQRES 5 A 191 ARG GLU VAL ASP GLY GLU VAL GLU VAL GLU ILE ASP GLU
SEQRES 6 A 191 LEU ALA TYR PHE VAL GLU LYS GLU LEU LYS ASP ARG ASN
SEQRES 7 A 191 VAL VAL LEU ASP GLY HIS LEU SER HIS LEU MET PRO VAL
SEQRES 8 A 191 ASP LEU VAL VAL VAL LEU ARG ALA HIS PRO ARG ILE ILE
SEQRES 9 A 191 GLY GLU ARG LEU ARG GLU ARG GLY TYR SER LYS GLU LYS
SEQRES 10 A 191 ILE GLY GLU ASN VAL GLU ALA GLU LEU VAL ASP ALA ILE
SEQRES 11 A 191 LEU ILE GLU ALA ILE ASP GLU HIS GLU ASN VAL ILE GLU
SEQRES 12 A 191 VAL ASP THR THR ASN LYS THR PRO GLU GLU ILE VAL GLU
SEQRES 13 A 191 GLU ILE ILE GLY LEU ILE LYS SER GLY VAL LYS ARG ARG
SEQRES 14 A 191 VAL GLY ILE VAL ASP TRP SER GLU VAL TYR ASP GLU ILE
SEQRES 15 A 191 ILE PRO TYR LEU ARG LEU GLY GLY GLU
SEQRES 1 B 191 MET LYS HIS HIS HIS HIS HIS HIS ALA MET GLY MET LEU
SEQRES 2 B 191 ILE ALA ILE THR GLY THR PRO GLY VAL GLY LYS THR THR
SEQRES 3 B 191 ILE ALA LYS LEU LEU ALA GLU LYS LEU GLY TYR GLU TYR
SEQRES 4 B 191 VAL ASN LEU ARG ASP PHE ALA LEU GLU LYS GLY CYS GLY
SEQRES 5 B 191 ARG GLU VAL ASP GLY GLU VAL GLU VAL GLU ILE ASP GLU
SEQRES 6 B 191 LEU ALA TYR PHE VAL GLU LYS GLU LEU LYS ASP ARG ASN
SEQRES 7 B 191 VAL VAL LEU ASP GLY HIS LEU SER HIS LEU MET PRO VAL
SEQRES 8 B 191 ASP LEU VAL VAL VAL LEU ARG ALA HIS PRO ARG ILE ILE
SEQRES 9 B 191 GLY GLU ARG LEU ARG GLU ARG GLY TYR SER LYS GLU LYS
SEQRES 10 B 191 ILE GLY GLU ASN VAL GLU ALA GLU LEU VAL ASP ALA ILE
SEQRES 11 B 191 LEU ILE GLU ALA ILE ASP GLU HIS GLU ASN VAL ILE GLU
SEQRES 12 B 191 VAL ASP THR THR ASN LYS THR PRO GLU GLU ILE VAL GLU
SEQRES 13 B 191 GLU ILE ILE GLY LEU ILE LYS SER GLY VAL LYS ARG ARG
SEQRES 14 B 191 VAL GLY ILE VAL ASP TRP SER GLU VAL TYR ASP GLU ILE
SEQRES 15 B 191 ILE PRO TYR LEU ARG LEU GLY GLY GLU
SEQRES 1 C 191 MET LYS HIS HIS HIS HIS HIS HIS ALA MET GLY MET LEU
SEQRES 2 C 191 ILE ALA ILE THR GLY THR PRO GLY VAL GLY LYS THR THR
SEQRES 3 C 191 ILE ALA LYS LEU LEU ALA GLU LYS LEU GLY TYR GLU TYR
SEQRES 4 C 191 VAL ASN LEU ARG ASP PHE ALA LEU GLU LYS GLY CYS GLY
SEQRES 5 C 191 ARG GLU VAL ASP GLY GLU VAL GLU VAL GLU ILE ASP GLU
SEQRES 6 C 191 LEU ALA TYR PHE VAL GLU LYS GLU LEU LYS ASP ARG ASN
SEQRES 7 C 191 VAL VAL LEU ASP GLY HIS LEU SER HIS LEU MET PRO VAL
SEQRES 8 C 191 ASP LEU VAL VAL VAL LEU ARG ALA HIS PRO ARG ILE ILE
SEQRES 9 C 191 GLY GLU ARG LEU ARG GLU ARG GLY TYR SER LYS GLU LYS
SEQRES 10 C 191 ILE GLY GLU ASN VAL GLU ALA GLU LEU VAL ASP ALA ILE
SEQRES 11 C 191 LEU ILE GLU ALA ILE ASP GLU HIS GLU ASN VAL ILE GLU
SEQRES 12 C 191 VAL ASP THR THR ASN LYS THR PRO GLU GLU ILE VAL GLU
SEQRES 13 C 191 GLU ILE ILE GLY LEU ILE LYS SER GLY VAL LYS ARG ARG
SEQRES 14 C 191 VAL GLY ILE VAL ASP TRP SER GLU VAL TYR ASP GLU ILE
SEQRES 15 C 191 ILE PRO TYR LEU ARG LEU GLY GLY GLU
SEQRES 1 D 191 MET LYS HIS HIS HIS HIS HIS HIS ALA MET GLY MET LEU
SEQRES 2 D 191 ILE ALA ILE THR GLY THR PRO GLY VAL GLY LYS THR THR
SEQRES 3 D 191 ILE ALA LYS LEU LEU ALA GLU LYS LEU GLY TYR GLU TYR
SEQRES 4 D 191 VAL ASN LEU ARG ASP PHE ALA LEU GLU LYS GLY CYS GLY
SEQRES 5 D 191 ARG GLU VAL ASP GLY GLU VAL GLU VAL GLU ILE ASP GLU
SEQRES 6 D 191 LEU ALA TYR PHE VAL GLU LYS GLU LEU LYS ASP ARG ASN
SEQRES 7 D 191 VAL VAL LEU ASP GLY HIS LEU SER HIS LEU MET PRO VAL
SEQRES 8 D 191 ASP LEU VAL VAL VAL LEU ARG ALA HIS PRO ARG ILE ILE
SEQRES 9 D 191 GLY GLU ARG LEU ARG GLU ARG GLY TYR SER LYS GLU LYS
SEQRES 10 D 191 ILE GLY GLU ASN VAL GLU ALA GLU LEU VAL ASP ALA ILE
SEQRES 11 D 191 LEU ILE GLU ALA ILE ASP GLU HIS GLU ASN VAL ILE GLU
SEQRES 12 D 191 VAL ASP THR THR ASN LYS THR PRO GLU GLU ILE VAL GLU
SEQRES 13 D 191 GLU ILE ILE GLY LEU ILE LYS SER GLY VAL LYS ARG ARG
SEQRES 14 D 191 VAL GLY ILE VAL ASP TRP SER GLU VAL TYR ASP GLU ILE
SEQRES 15 D 191 ILE PRO TYR LEU ARG LEU GLY GLY GLU
SEQRES 1 E 137 MET SER GLU GLU GLN VAL ASN ILE LYS LYS LYS GLU LYS
SEQRES 2 E 137 TRP GLY ILE ALA HIS ILE TYR SER SER TYR ASN ASN THR
SEQRES 3 E 137 ILE ILE HIS ILE THR ASP ILE THR GLY ALA GLU THR ILE
SEQRES 4 E 137 SER ARG TRP SER GLY GLY MET VAL VAL LYS ALA ASP ARG
SEQRES 5 E 137 ASP GLU PRO SER PRO TYR ALA ALA MET LEU ALA ALA ARG
SEQRES 6 E 137 ARG ALA ALA GLU GLU ALA LEU GLU LYS GLY ILE VAL GLY
SEQRES 7 E 137 VAL HIS ILE ARG VAL ARG ALA PRO GLY GLY SER LYS SER
SEQRES 8 E 137 LYS THR PRO GLY PRO GLY ALA GLN ALA ALA ILE ARG ALA
SEQRES 9 E 137 LEU ALA ARG ALA GLY LEU LYS ILE GLY ARG VAL GLU ASP
SEQRES 10 E 137 VAL THR PRO ILE PRO HIS ASP GLY THR ARG PRO LYS GLY
SEQRES 11 E 137 GLY ARG ARG GLY ARG ARG VAL
SEQRES 1 F 137 MET SER GLU GLU GLN VAL ASN ILE LYS LYS LYS GLU LYS
SEQRES 2 F 137 TRP GLY ILE ALA HIS ILE TYR SER SER TYR ASN ASN THR
SEQRES 3 F 137 ILE ILE HIS ILE THR ASP ILE THR GLY ALA GLU THR ILE
SEQRES 4 F 137 SER ARG TRP SER GLY GLY MET VAL VAL LYS ALA ASP ARG
SEQRES 5 F 137 ASP GLU PRO SER PRO TYR ALA ALA MET LEU ALA ALA ARG
SEQRES 6 F 137 ARG ALA ALA GLU GLU ALA LEU GLU LYS GLY ILE VAL GLY
SEQRES 7 F 137 VAL HIS ILE ARG VAL ARG ALA PRO GLY GLY SER LYS SER
SEQRES 8 F 137 LYS THR PRO GLY PRO GLY ALA GLN ALA ALA ILE ARG ALA
SEQRES 9 F 137 LEU ALA ARG ALA GLY LEU LYS ILE GLY ARG VAL GLU ASP
SEQRES 10 F 137 VAL THR PRO ILE PRO HIS ASP GLY THR ARG PRO LYS GLY
SEQRES 11 F 137 GLY ARG ARG GLY ARG ARG VAL
SEQRES 1 G 137 MET SER GLU GLU GLN VAL ASN ILE LYS LYS LYS GLU LYS
SEQRES 2 G 137 TRP GLY ILE ALA HIS ILE TYR SER SER TYR ASN ASN THR
SEQRES 3 G 137 ILE ILE HIS ILE THR ASP ILE THR GLY ALA GLU THR ILE
SEQRES 4 G 137 SER ARG TRP SER GLY GLY MET VAL VAL LYS ALA ASP ARG
SEQRES 5 G 137 ASP GLU PRO SER PRO TYR ALA ALA MET LEU ALA ALA ARG
SEQRES 6 G 137 ARG ALA ALA GLU GLU ALA LEU GLU LYS GLY ILE VAL GLY
SEQRES 7 G 137 VAL HIS ILE ARG VAL ARG ALA PRO GLY GLY SER LYS SER
SEQRES 8 G 137 LYS THR PRO GLY PRO GLY ALA GLN ALA ALA ILE ARG ALA
SEQRES 9 G 137 LEU ALA ARG ALA GLY LEU LYS ILE GLY ARG VAL GLU ASP
SEQRES 10 G 137 VAL THR PRO ILE PRO HIS ASP GLY THR ARG PRO LYS GLY
SEQRES 11 G 137 GLY ARG ARG GLY ARG ARG VAL
SEQRES 1 H 137 MET SER GLU GLU GLN VAL ASN ILE LYS LYS LYS GLU LYS
SEQRES 2 H 137 TRP GLY ILE ALA HIS ILE TYR SER SER TYR ASN ASN THR
SEQRES 3 H 137 ILE ILE HIS ILE THR ASP ILE THR GLY ALA GLU THR ILE
SEQRES 4 H 137 SER ARG TRP SER GLY GLY MET VAL VAL LYS ALA ASP ARG
SEQRES 5 H 137 ASP GLU PRO SER PRO TYR ALA ALA MET LEU ALA ALA ARG
SEQRES 6 H 137 ARG ALA ALA GLU GLU ALA LEU GLU LYS GLY ILE VAL GLY
SEQRES 7 H 137 VAL HIS ILE ARG VAL ARG ALA PRO GLY GLY SER LYS SER
SEQRES 8 H 137 LYS THR PRO GLY PRO GLY ALA GLN ALA ALA ILE ARG ALA
SEQRES 9 H 137 LEU ALA ARG ALA GLY LEU LYS ILE GLY ARG VAL GLU ASP
SEQRES 10 H 137 VAL THR PRO ILE PRO HIS ASP GLY THR ARG PRO LYS GLY
SEQRES 11 H 137 GLY ARG ARG GLY ARG ARG VAL
HET ADP A1001 27
HET MG A1002 1
HET ADP B1001 27
HET MG B1002 1
HET ADP C1001 27
HET MG C1002 1
HET ADP D1001 27
HET MG D1002 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 9 ADP 4(C10 H15 N5 O10 P2)
FORMUL 10 MG 4(MG 2+)
FORMUL 11 HOH *508(H2 O)
HELIX 1 1 GLY A 12 GLY A 25 1 14
HELIX 2 2 LEU A 31 LYS A 38 1 8
HELIX 3 3 GLU A 51 LEU A 63 1 13
HELIX 4 4 LEU A 74 MET A 78 5 5
HELIX 5 5 HIS A 89 GLY A 101 1 13
HELIX 6 6 SER A 103 VAL A 116 1 14
HELIX 7 7 ASP A 117 HIS A 127 1 11
HELIX 8 8 THR A 139 SER A 153 1 15
HELIX 9 9 ASP A 163 GLU A 166 5 4
HELIX 10 10 VAL A 167 ILE A 172 1 6
HELIX 11 11 PRO A 173 LEU A 175 5 3
HELIX 12 12 GLY B 12 GLY B 25 1 14
HELIX 13 13 LEU B 31 LYS B 38 1 8
HELIX 14 14 GLU B 51 LYS B 64 1 14
HELIX 15 15 LEU B 74 MET B 78 5 5
HELIX 16 16 HIS B 89 GLY B 101 1 13
HELIX 17 17 SER B 103 VAL B 116 1 14
HELIX 18 18 ASP B 117 HIS B 127 1 11
HELIX 19 19 THR B 139 SER B 153 1 15
HELIX 20 20 ASP B 163 GLU B 166 5 4
HELIX 21 21 VAL B 167 ILE B 172 1 6
HELIX 22 22 PRO B 173 LEU B 175 5 3
HELIX 23 23 GLY C 12 GLY C 25 1 14
HELIX 24 24 LEU C 31 LYS C 38 1 8
HELIX 25 25 GLU C 51 LEU C 63 1 13
HELIX 26 26 LEU C 74 MET C 78 5 5
HELIX 27 27 HIS C 89 GLY C 101 1 13
HELIX 28 28 SER C 103 VAL C 116 1 14
HELIX 29 29 ASP C 117 HIS C 127 1 11
HELIX 30 30 THR C 139 GLY C 154 1 16
HELIX 31 31 ASP C 163 GLU C 166 5 4
HELIX 32 32 VAL C 167 ILE C 172 1 6
HELIX 33 33 PRO C 173 LEU C 175 5 3
HELIX 34 34 GLY D 12 GLY D 25 1 14
HELIX 35 35 LEU D 31 LYS D 38 1 8
HELIX 36 36 GLU D 51 GLU D 60 1 10
HELIX 37 37 LEU D 74 MET D 78 5 5
HELIX 38 38 HIS D 89 GLY D 101 1 13
HELIX 39 39 SER D 103 VAL D 116 1 14
HELIX 40 40 ASP D 117 HIS D 127 1 11
HELIX 41 41 THR D 139 SER D 153 1 15
HELIX 42 42 ASP D 163 GLU D 166 5 4
HELIX 43 43 VAL D 167 ILE D 172 1 6
HELIX 44 44 PRO D 173 LEU D 175 5 3
HELIX 45 45 GLY E 44 VAL E 48 1 5
HELIX 46 46 ALA E 50 GLU E 54 5 5
HELIX 47 47 SER E 56 LYS E 74 1 19
HELIX 48 48 PRO E 96 ALA E 108 1 13
HELIX 49 49 GLY E 131 ARG E 135 5 5
HELIX 50 50 GLY F 44 VAL F 48 1 5
HELIX 51 51 ALA F 50 GLU F 54 5 5
HELIX 52 52 SER F 56 LYS F 74 1 19
HELIX 53 53 PRO F 96 ALA F 108 1 13
HELIX 54 54 GLY G 44 VAL G 48 1 5
HELIX 55 55 ALA G 50 GLU G 54 5 5
HELIX 56 56 SER G 56 LYS G 74 1 19
HELIX 57 57 PRO G 96 ALA G 108 1 13
HELIX 58 58 GLY H 44 VAL H 48 1 5
HELIX 59 59 ALA H 50 GLU H 54 5 5
HELIX 60 60 SER H 56 LYS H 74 1 19
HELIX 61 61 PRO H 96 ALA H 108 1 13
HELIX 62 62 GLY H 131 ARG H 135 5 5
SHEET 1 AA 5 GLU A 27 ASN A 30 0
SHEET 2 AA 5 ASN A 67 ASP A 71 1 O ASN A 67 N GLU A 27
SHEET 3 AA 5 MET A 1 THR A 6 1 O MET A 1 N VAL A 68
SHEET 4 AA 5 LEU A 82 ARG A 87 1 O LEU A 82 N ALA A 4
SHEET 5 AA 5 VAL A 130 ASP A 134 1 O ILE A 131 N VAL A 85
SHEET 1 AB 2 ARG A 42 VAL A 44 0
SHEET 2 AB 2 GLU A 47 GLU A 49 -1 O GLU A 47 N VAL A 44
SHEET 1 BA 5 GLU B 27 ASN B 30 0
SHEET 2 BA 5 ASN B 67 ASP B 71 1 O ASN B 67 N GLU B 27
SHEET 3 BA 5 MET B 1 THR B 6 1 O MET B 1 N VAL B 68
SHEET 4 BA 5 LEU B 82 ARG B 87 1 O LEU B 82 N ALA B 4
SHEET 5 BA 5 VAL B 130 ASP B 134 1 O ILE B 131 N VAL B 85
SHEET 1 BB 2 GLU B 49 VAL B 50 0
SHEET 2 BB 2 ARG E 127 PRO E 128 1 O ARG E 127 N VAL B 50
SHEET 1 CA 5 GLU C 27 ASN C 30 0
SHEET 2 CA 5 VAL C 68 ASP C 71 1 O VAL C 69 N VAL C 29
SHEET 3 CA 5 LEU C 2 THR C 6 1 O ILE C 3 N LEU C 70
SHEET 4 CA 5 LEU C 82 ARG C 87 1 O LEU C 82 N ALA C 4
SHEET 5 CA 5 VAL C 130 ASP C 134 1 O ILE C 131 N VAL C 85
SHEET 1 CB 3 ARG C 42 VAL C 44 0
SHEET 2 CB 3 GLU C 47 VAL C 50 -1 O GLU C 47 N VAL C 44
SHEET 3 CB 3 THR G 126 PRO G 128 1 O ARG G 127 N VAL C 50
SHEET 1 DA 5 GLU D 27 ASN D 30 0
SHEET 2 DA 5 VAL D 68 ASP D 71 1 O VAL D 69 N VAL D 29
SHEET 3 DA 5 LEU D 2 THR D 6 1 O ILE D 3 N LEU D 70
SHEET 4 DA 5 LEU D 82 ARG D 87 1 O LEU D 82 N ALA D 4
SHEET 5 DA 5 VAL D 130 ASP D 134 1 O ILE D 131 N VAL D 85
SHEET 1 EA 5 THR E 38 SER E 43 0
SHEET 2 EA 5 THR E 26 ASP E 32 -1 O ILE E 28 N TRP E 42
SHEET 3 EA 5 TRP E 14 SER E 21 -1 O ILE E 16 N THR E 31
SHEET 4 EA 5 GLY E 78 ARG E 84 1 O GLY E 78 N GLY E 15
SHEET 5 EA 5 LYS E 111 ASP E 117 1 O LYS E 111 N VAL E 79
SHEET 1 FA 5 THR F 38 SER F 43 0
SHEET 2 FA 5 THR F 26 ASP F 32 -1 O ILE F 28 N TRP F 42
SHEET 3 FA 5 LYS F 13 SER F 21 -1 O ILE F 16 N THR F 31
SHEET 4 FA 5 ILE F 76 ARG F 84 1 N VAL F 77 O LYS F 13
SHEET 5 FA 5 LYS F 111 ASP F 117 1 O LYS F 111 N VAL F 79
SHEET 1 GA 5 THR G 38 SER G 43 0
SHEET 2 GA 5 THR G 26 ASP G 32 -1 O ILE G 28 N TRP G 42
SHEET 3 GA 5 LYS G 13 SER G 21 -1 O ILE G 16 N THR G 31
SHEET 4 GA 5 ILE G 76 ARG G 84 1 N VAL G 77 O LYS G 13
SHEET 5 GA 5 LYS G 111 ASP G 117 1 O LYS G 111 N VAL G 79
SHEET 1 HA 5 THR H 38 SER H 43 0
SHEET 2 HA 5 THR H 26 ASP H 32 -1 O ILE H 28 N TRP H 42
SHEET 3 HA 5 TRP H 14 SER H 21 -1 O ILE H 16 N THR H 31
SHEET 4 HA 5 GLY H 78 ARG H 84 1 O GLY H 78 N GLY H 15
SHEET 5 HA 5 LYS H 111 ASP H 117 1 O LYS H 111 N VAL H 79
LINK O1B ADP A1001 MG MG A1002 1555 1555 2.10
LINK MG MG A1002 OG1 THR A 14 1555 1555 2.12
LINK MG MG A1002 O HOH A2012 1555 1555 2.21
LINK MG MG A1002 O HOH A2013 1555 1555 2.07
LINK MG MG A1002 O HOH A2049 1555 1555 2.24
LINK MG MG A1002 O HOH A2014 1555 1555 2.13
LINK O1B ADP B1001 MG MG B1002 1555 1555 1.96
LINK MG MG B1002 OG1 THR B 14 1555 1555 2.22
LINK MG MG B1002 O HOH B2006 1555 1555 2.16
LINK MG MG B1002 O HOH B2007 1555 1555 2.20
LINK MG MG B1002 O HOH B2008 1555 1555 2.05
LINK MG MG B1002 O HOH B2053 1555 1555 2.19
LINK O2B ADP C1001 MG MG C1002 1555 1555 2.19
LINK MG MG C1002 O HOH C2004 1555 1555 2.22
LINK MG MG C1002 OG1 THR C 14 1555 1555 2.18
LINK MG MG C1002 O HOH C2005 1555 1555 2.05
LINK MG MG C1002 O HOH C2006 1555 1555 2.29
LINK MG MG C1002 O HOH C2041 1555 1555 1.92
LINK O2B ADP D1001 MG MG D1002 1555 1555 2.01
LINK MG MG D1002 O HOH D2004 1555 1555 1.99
LINK MG MG D1002 O HOH D2005 1555 1555 2.29
LINK MG MG D1002 O HOH D2006 1555 1555 2.24
LINK MG MG D1002 O HOH D2026 1555 1555 2.14
LINK MG MG D1002 OG1 THR D 14 1555 1555 1.96
CISPEP 1 ASP C 45 GLY C 46 0 -15.46
SITE 1 AC1 17 GLY A 10 VAL A 11 GLY A 12 LYS A 13
SITE 2 AC1 17 THR A 14 THR A 15 ARG A 96 ARG A 100
SITE 3 AC1 17 LYS A 138 PRO A 140 ILE A 143 MG A1002
SITE 4 AC1 17 HOH A2010 HOH A2014 HOH A2049 HOH A2074
SITE 5 AC1 17 HOH A2093
SITE 1 AC2 6 THR A 14 ADP A1001 HOH A2012 HOH A2013
SITE 2 AC2 6 HOH A2014 HOH A2049
SITE 1 AC3 15 GLY B 10 VAL B 11 GLY B 12 LYS B 13
SITE 2 AC3 15 THR B 14 THR B 15 ARG B 96 ARG B 100
SITE 3 AC3 15 LYS B 138 PRO B 140 ILE B 143 MG B1002
SITE 4 AC3 15 HOH B2004 HOH B2008 HOH B2053
SITE 1 AC4 6 THR B 14 ADP B1001 HOH B2006 HOH B2007
SITE 2 AC4 6 HOH B2008 HOH B2053
SITE 1 AC5 17 GLY C 10 VAL C 11 GLY C 12 LYS C 13
SITE 2 AC5 17 THR C 14 THR C 15 ARG C 96 ARG C 100
SITE 3 AC5 17 LYS C 138 THR C 139 PRO C 140 ILE C 143
SITE 4 AC5 17 MG C1002 HOH C2006 HOH C2039 HOH C2040
SITE 5 AC5 17 HOH C2041
SITE 1 AC6 6 THR C 14 ADP C1001 HOH C2004 HOH C2005
SITE 2 AC6 6 HOH C2006 HOH C2041
SITE 1 AC7 17 GLY D 10 VAL D 11 GLY D 12 LYS D 13
SITE 2 AC7 17 THR D 14 THR D 15 ARG D 96 ARG D 100
SITE 3 AC7 17 LYS D 138 THR D 139 PRO D 140 ILE D 143
SITE 4 AC7 17 MG D1002 HOH D2005 HOH D2026 HOH D2061
SITE 5 AC7 17 HOH D2062
SITE 1 AC8 6 THR D 14 ADP D1001 HOH D2004 HOH D2005
SITE 2 AC8 6 HOH D2006 HOH D2026
CRYST1 67.050 139.550 83.080 90.00 105.51 90.00 P 1 21 1 8
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 0.014914 0.000000 0.004139 0.00000
SCALE2 0.000000 0.007166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012491 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
