| 7c72-pdb | HEADER HYDROLASE 22-MAY-20 7C72
TITLE STRUCTURE OF A MYCOBACTERIUM TUBERCULOSIS PUROMYCIN-HYDROLYZING
TITLE 2 PEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: CNE19725.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS PROLYL OLIGOPEPTIDASE, HYDROLASE, TUBERCULOSIS, ACYL AMINOPEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.RUIZ-CARRILLO,Y.H.ZHAO,Q.FENG,X.ZHOU,Y.ZHANG,J.JIANG,M.LUKMAN
REVDAT 1 24-MAR-21 7C72 0
JRNL AUTH Y.ZHAO,Q.FENG,X.ZHOU,Y.ZHANG,M.LUKMAN,J.JIANG,
JRNL AUTH 2 D.RUIZ-CARRILLO
JRNL TITL MYCOBACTERIUM TUBERCULOSIS PUROMYCIN HYDROLASE DISPLAYS A
JRNL TITL 2 PROLYL OLIGOPEPTIDASE FOLD AND AN ACYL AMINOPEPTIDASE
JRNL TITL 3 ACTIVITY.
JRNL REF PROTEINS 2021
JRNL REFN ESSN 1097-0134
JRNL PMID 33426726
JRNL DOI 10.1002/PROT.26044
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.564
REMARK 3 FREE R VALUE TEST SET COUNT : 2004
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 46.4897 - 7.2221 1.00 3954 144 0.1424 0.1808
REMARK 3 2 7.2221 - 5.7358 1.00 3876 147 0.1923 0.2531
REMARK 3 3 5.7358 - 5.0117 1.00 3892 147 0.1572 0.1929
REMARK 3 4 5.0117 - 4.5539 1.00 3871 144 0.1495 0.1916
REMARK 3 5 4.5539 - 4.2278 1.00 3885 149 0.1547 0.1999
REMARK 3 6 4.2278 - 3.9786 1.00 3858 140 0.1747 0.2023
REMARK 3 7 3.9786 - 3.7795 1.00 3886 144 0.1814 0.2349
REMARK 3 8 3.7795 - 3.6150 1.00 3836 141 0.2045 0.2244
REMARK 3 9 3.6150 - 3.4759 1.00 3887 136 0.2128 0.2591
REMARK 3 10 3.4759 - 3.3560 1.00 3834 144 0.2291 0.2599
REMARK 3 11 3.3560 - 3.2511 1.00 3886 144 0.2495 0.2794
REMARK 3 12 3.2511 - 3.1582 1.00 3850 140 0.2912 0.3236
REMARK 3 13 3.1582 - 3.0751 1.00 3885 148 0.3122 0.3789
REMARK 3 14 3.0751 - 3.0000 1.00 3831 136 0.3401 0.3562
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.436
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.753
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 111.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 134.9
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 10367
REMARK 3 ANGLE : 1.222 14180
REMARK 3 CHIRALITY : 0.064 1508
REMARK 3 PLANARITY : 0.008 1889
REMARK 3 DIHEDRAL : 10.242 6057
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 4:51)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0536 -65.1576 1.1872
REMARK 3 T TENSOR
REMARK 3 T11: 1.0327 T22: 0.8482
REMARK 3 T33: 1.2984 T12: 0.1406
REMARK 3 T13: -0.3005 T23: 0.0960
REMARK 3 L TENSOR
REMARK 3 L11: 3.8803 L22: 7.0286
REMARK 3 L33: 1.5124 L12: 3.0737
REMARK 3 L13: 0.4849 L23: 3.0309
REMARK 3 S TENSOR
REMARK 3 S11: -0.2706 S12: -0.3546 S13: 0.9999
REMARK 3 S21: 0.0757 S22: -0.1475 S23: 1.1182
REMARK 3 S31: -0.5776 S32: -0.2769 S33: 0.6231
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 52:107)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3200 -84.0893 -1.2971
REMARK 3 T TENSOR
REMARK 3 T11: 0.7528 T22: 0.6326
REMARK 3 T33: 0.8210 T12: -0.0157
REMARK 3 T13: -0.0822 T23: -0.1343
REMARK 3 L TENSOR
REMARK 3 L11: 8.9594 L22: 7.9486
REMARK 3 L33: 8.5708 L12: -1.9587
REMARK 3 L13: 0.8478 L23: -0.9541
REMARK 3 S TENSOR
REMARK 3 S11: 0.1973 S12: 0.1014 S13: 0.6238
REMARK 3 S21: -0.1697 S22: -0.2515 S23: 1.2856
REMARK 3 S31: 0.2863 S32: -1.3444 S33: 0.1583
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 108:124)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.1757 -92.3853 4.2975
REMARK 3 T TENSOR
REMARK 3 T11: 1.0971 T22: 1.0392
REMARK 3 T33: 1.2080 T12: -0.0139
REMARK 3 T13: 0.1488 T23: -0.1189
REMARK 3 L TENSOR
REMARK 3 L11: 3.4786 L22: 4.3761
REMARK 3 L33: 3.5018 L12: -3.2684
REMARK 3 L13: 2.3056 L23: -3.6567
REMARK 3 S TENSOR
REMARK 3 S11: 0.2970 S12: -2.1257 S13: 1.6033
REMARK 3 S21: 0.1556 S22: 0.0268 S23: -0.2642
REMARK 3 S31: 0.8946 S32: -2.4621 S33: -0.1747
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 125:153)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6855 -96.5332 0.3538
REMARK 3 T TENSOR
REMARK 3 T11: 0.7818 T22: 0.6682
REMARK 3 T33: 0.9316 T12: -0.0897
REMARK 3 T13: 0.0107 T23: -0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 4.8516 L22: 7.4731
REMARK 3 L33: 8.0822 L12: -4.1451
REMARK 3 L13: 2.8274 L23: -7.5092
REMARK 3 S TENSOR
REMARK 3 S11: 0.2454 S12: 0.1188 S13: -0.3878
REMARK 3 S21: 0.3041 S22: -0.1108 S23: 0.2983
REMARK 3 S31: 1.4055 S32: -0.6100 S33: -0.1430
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 169:184)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6308 -98.2332 6.4036
REMARK 3 T TENSOR
REMARK 3 T11: 0.8166 T22: 0.4906
REMARK 3 T33: 0.7704 T12: -0.0303
REMARK 3 T13: -0.0596 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 7.4593 L22: 7.4576
REMARK 3 L33: 3.2605 L12: -2.1927
REMARK 3 L13: 2.5401 L23: -1.8885
REMARK 3 S TENSOR
REMARK 3 S11: -0.3081 S12: -1.3710 S13: 0.4528
REMARK 3 S21: 1.0594 S22: -0.1285 S23: 0.6530
REMARK 3 S31: 0.6114 S32: -0.5272 S33: 0.4826
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 185:251)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6701 -99.0421 -7.2261
REMARK 3 T TENSOR
REMARK 3 T11: 0.7309 T22: 0.5143
REMARK 3 T33: 0.6557 T12: 0.0228
REMARK 3 T13: -0.0714 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 8.2451 L22: 4.7005
REMARK 3 L33: 2.4060 L12: 1.0413
REMARK 3 L13: -1.3520 L23: 0.5813
REMARK 3 S TENSOR
REMARK 3 S11: -0.0674 S12: -0.1636 S13: -0.5349
REMARK 3 S21: 0.1771 S22: -0.3271 S23: 0.1601
REMARK 3 S31: 0.4122 S32: -0.3600 S33: 0.4031
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 252:277)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7008 -90.5890 -17.3713
REMARK 3 T TENSOR
REMARK 3 T11: 0.8431 T22: 0.7216
REMARK 3 T33: 0.8554 T12: 0.0668
REMARK 3 T13: 0.0368 T23: 0.0944
REMARK 3 L TENSOR
REMARK 3 L11: 4.7067 L22: 8.6980
REMARK 3 L33: 5.3471 L12: -3.9159
REMARK 3 L13: 4.3068 L23: -4.4207
REMARK 3 S TENSOR
REMARK 3 S11: -0.3113 S12: 1.3326 S13: -0.1160
REMARK 3 S21: -0.7830 S22: -0.1747 S23: -0.3476
REMARK 3 S31: 0.6475 S32: 1.2810 S33: 0.3928
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 278:289)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8339 -89.8381 -20.2350
REMARK 3 T TENSOR
REMARK 3 T11: 1.1196 T22: 0.9982
REMARK 3 T33: 0.7909 T12: 0.2053
REMARK 3 T13: -0.1073 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 4.7126 L22: 6.7497
REMARK 3 L33: 5.9367 L12: 5.4326
REMARK 3 L13: 4.5474 L23: 6.0537
REMARK 3 S TENSOR
REMARK 3 S11: 0.2692 S12: 0.6288 S13: -0.2049
REMARK 3 S21: 0.2731 S22: 0.0465 S23: -1.4596
REMARK 3 S31: 0.4526 S32: -0.3573 S33: -0.3967
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 290:310)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8971 -81.9103 -15.0166
REMARK 3 T TENSOR
REMARK 3 T11: 0.8400 T22: 0.8688
REMARK 3 T33: 1.1763 T12: 0.1334
REMARK 3 T13: -0.1633 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 4.8166 L22: 3.6121
REMARK 3 L33: 9.3200 L12: -0.6353
REMARK 3 L13: -2.0868 L23: -1.2452
REMARK 3 S TENSOR
REMARK 3 S11: -0.2793 S12: 0.1771 S13: 0.5090
REMARK 3 S21: 0.4847 S22: -0.0828 S23: -0.9390
REMARK 3 S31: 0.1395 S32: 1.4759 S33: 0.2612
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 311:346)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6492 -77.0058 -22.9785
REMARK 3 T TENSOR
REMARK 3 T11: 0.8507 T22: 1.0171
REMARK 3 T33: 1.1111 T12: 0.1258
REMARK 3 T13: -0.2904 T23: 0.2645
REMARK 3 L TENSOR
REMARK 3 L11: 8.1077 L22: 6.4959
REMARK 3 L33: 7.5632 L12: 2.9694
REMARK 3 L13: -1.7450 L23: 3.4409
REMARK 3 S TENSOR
REMARK 3 S11: -0.1778 S12: 1.1971 S13: 1.3215
REMARK 3 S21: -0.6902 S22: -0.1447 S23: 0.3790
REMARK 3 S31: -0.8937 S32: 0.4813 S33: 0.5798
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 347:391)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5975 -70.2253 -15.3301
REMARK 3 T TENSOR
REMARK 3 T11: 0.7638 T22: 0.7998
REMARK 3 T33: 0.9546 T12: 0.0838
REMARK 3 T13: -0.3059 T23: 0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 7.4740 L22: 3.4571
REMARK 3 L33: 3.5914 L12: -2.9278
REMARK 3 L13: -5.1502 L23: 1.4453
REMARK 3 S TENSOR
REMARK 3 S11: 0.1281 S12: 0.3318 S13: 0.6798
REMARK 3 S21: -0.5189 S22: -0.2866 S23: 0.3275
REMARK 3 S31: -0.1156 S32: -0.7424 S33: 0.1422
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 392:408)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5626 -55.5769 -4.2064
REMARK 3 T TENSOR
REMARK 3 T11: 1.1501 T22: 0.9768
REMARK 3 T33: 1.4747 T12: 0.0111
REMARK 3 T13: -0.4163 T23: 0.0898
REMARK 3 L TENSOR
REMARK 3 L11: 7.8715 L22: 8.2693
REMARK 3 L33: 7.4950 L12: -2.0308
REMARK 3 L13: 1.4599 L23: 0.1298
REMARK 3 S TENSOR
REMARK 3 S11: 0.5958 S12: 0.6359 S13: 0.5180
REMARK 3 S21: -0.4529 S22: -0.4056 S23: 1.0109
REMARK 3 S31: -0.5581 S32: -0.0584 S33: 0.1889
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 409:416)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3708 -65.8484 -4.2259
REMARK 3 T TENSOR
REMARK 3 T11: 1.4896 T22: 1.4331
REMARK 3 T33: 1.7976 T12: -0.0747
REMARK 3 T13: 0.0534 T23: 0.5357
REMARK 3 L TENSOR
REMARK 3 L11: 9.3214 L22: 8.0996
REMARK 3 L33: 9.3678 L12: -8.5880
REMARK 3 L13: 4.3070 L23: -3.1950
REMARK 3 S TENSOR
REMARK 3 S11: -0.5305 S12: 3.0243 S13: 2.5983
REMARK 3 S21: -1.1854 S22: -3.1187 S23: -2.2375
REMARK 3 S31: -0.1617 S32: 2.5155 S33: 2.5522
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 417:447)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3355 -54.0967 2.0588
REMARK 3 T TENSOR
REMARK 3 T11: 0.9884 T22: 0.8496
REMARK 3 T33: 1.5346 T12: -0.0232
REMARK 3 T13: -0.3556 T23: 0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 2.0145 L22: 4.7196
REMARK 3 L33: 5.9401 L12: -2.8996
REMARK 3 L13: -2.2992 L23: 4.8012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.0332 S13: 1.1688
REMARK 3 S21: -1.4740 S22: 0.1102 S23: -0.1248
REMARK 3 S31: -0.8933 S32: -0.4413 S33: -0.1617
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 448:551)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4167 -66.0723 4.9447
REMARK 3 T TENSOR
REMARK 3 T11: 0.7258 T22: 0.6133
REMARK 3 T33: 1.1378 T12: -0.0299
REMARK 3 T13: -0.4201 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.9911 L22: 5.8805
REMARK 3 L33: 3.3194 L12: -1.4755
REMARK 3 L13: -2.7697 L23: 1.5375
REMARK 3 S TENSOR
REMARK 3 S11: -0.2560 S12: 0.4711 S13: 0.6409
REMARK 3 S21: -0.4368 S22: 0.0641 S23: 0.1038
REMARK 3 S31: -0.3710 S32: 0.1287 S33: 0.1707
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 552:576)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2403 -86.5396 10.6826
REMARK 3 T TENSOR
REMARK 3 T11: 0.9513 T22: 0.7438
REMARK 3 T33: 0.7654 T12: 0.1778
REMARK 3 T13: -0.3041 T23: 0.0734
REMARK 3 L TENSOR
REMARK 3 L11: 9.2387 L22: 6.3959
REMARK 3 L33: 8.4086 L12: 1.5615
REMARK 3 L13: -6.9076 L23: 2.4756
REMARK 3 S TENSOR
REMARK 3 S11: -0.4971 S12: -0.8524 S13: -0.6982
REMARK 3 S21: 0.1317 S22: -0.0840 S23: -0.6182
REMARK 3 S31: 1.3447 S32: 0.1149 S33: 0.5175
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN A AND RESID 577:587)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3977 -82.5809 15.5760
REMARK 3 T TENSOR
REMARK 3 T11: 1.2614 T22: 1.0926
REMARK 3 T33: 1.2308 T12: 0.2546
REMARK 3 T13: -0.4052 T23: -0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 5.4189 L22: 5.9590
REMARK 3 L33: 5.0579 L12: -5.6848
REMARK 3 L13: -1.1241 L23: 1.0324
REMARK 3 S TENSOR
REMARK 3 S11: -1.0468 S12: -1.4586 S13: 0.7613
REMARK 3 S21: 1.2449 S22: 0.5196 S23: -1.6544
REMARK 3 S31: 0.1966 S32: 1.7888 S33: 0.0920
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN A AND RESID 588:640)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9776 -72.2448 21.3027
REMARK 3 T TENSOR
REMARK 3 T11: 0.9263 T22: 0.6523
REMARK 3 T33: 1.0037 T12: 0.1224
REMARK 3 T13: -0.2466 T23: -0.1394
REMARK 3 L TENSOR
REMARK 3 L11: 4.9853 L22: 5.9306
REMARK 3 L33: 7.1239 L12: 1.9925
REMARK 3 L13: 0.9351 L23: 1.6333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.3623 S13: -0.0099
REMARK 3 S21: 0.5380 S22: -0.0947 S23: 0.3737
REMARK 3 S31: 0.2918 S32: -0.2112 S33: -0.0150
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN A AND RESID 641:668)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7484 -58.1923 15.3551
REMARK 3 T TENSOR
REMARK 3 T11: 1.1144 T22: 0.8764
REMARK 3 T33: 1.7072 T12: 0.1805
REMARK 3 T13: -0.3058 T23: -0.2785
REMARK 3 L TENSOR
REMARK 3 L11: 3.5018 L22: 5.5145
REMARK 3 L33: 3.8157 L12: -3.7774
REMARK 3 L13: -1.4450 L23: -0.5586
REMARK 3 S TENSOR
REMARK 3 S11: -0.1764 S12: -1.3082 S13: 2.1717
REMARK 3 S21: -0.8894 S22: -0.5695 S23: 0.9675
REMARK 3 S31: -1.1483 S32: -0.5783 S33: 0.4811
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN A AND RESID 669:675)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1990 -58.3432 26.4198
REMARK 3 T TENSOR
REMARK 3 T11: 1.0829 T22: 1.3333
REMARK 3 T33: 1.0744 T12: 0.0888
REMARK 3 T13: -0.4439 T23: -0.3954
REMARK 3 L TENSOR
REMARK 3 L11: 2.5344 L22: 9.8918
REMARK 3 L33: 1.4685 L12: -2.4512
REMARK 3 L13: -0.8755 L23: -2.1100
REMARK 3 S TENSOR
REMARK 3 S11: 1.9954 S12: 0.6829 S13: -0.8980
REMARK 3 S21: -0.9722 S22: -0.7865 S23: 2.5677
REMARK 3 S31: 0.3753 S32: -1.1893 S33: -1.3284
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN B AND RESID 4:27)
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3398 -54.7675 -14.6689
REMARK 3 T TENSOR
REMARK 3 T11: 1.3313 T22: 1.1223
REMARK 3 T33: 1.1487 T12: 0.3601
REMARK 3 T13: -0.3583 T23: -0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 2.5637 L22: 4.0434
REMARK 3 L33: 3.3934 L12: 1.4200
REMARK 3 L13: -0.5573 L23: -3.1861
REMARK 3 S TENSOR
REMARK 3 S11: -0.9620 S12: -0.6755 S13: 0.0492
REMARK 3 S21: 1.3128 S22: 0.1427 S23: -1.4716
REMARK 3 S31: -0.9021 S32: -1.0138 S33: 1.2865
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN B AND RESID 28:48)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9236 -56.0587 -34.9392
REMARK 3 T TENSOR
REMARK 3 T11: 0.9825 T22: 1.7331
REMARK 3 T33: 1.8501 T12: 0.0732
REMARK 3 T13: -0.2633 T23: 0.7287
REMARK 3 L TENSOR
REMARK 3 L11: 8.3641 L22: 7.4378
REMARK 3 L33: 8.0557 L12: -1.8084
REMARK 3 L13: -3.3675 L23: 0.1836
REMARK 3 S TENSOR
REMARK 3 S11: -0.2240 S12: 0.3226 S13: 1.8495
REMARK 3 S21: 0.0604 S22: -0.7877 S23: -1.1506
REMARK 3 S31: 0.7299 S32: 0.8425 S33: 0.5322
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN B AND RESID 49:87)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5948 -51.4556 -37.5735
REMARK 3 T TENSOR
REMARK 3 T11: 0.9092 T22: 1.6691
REMARK 3 T33: 1.8799 T12: -0.1565
REMARK 3 T13: -0.1901 T23: 0.5768
REMARK 3 L TENSOR
REMARK 3 L11: 2.0605 L22: 5.9259
REMARK 3 L33: 7.1470 L12: -3.5033
REMARK 3 L13: -0.9437 L23: 0.8267
REMARK 3 S TENSOR
REMARK 3 S11: -0.4202 S12: -0.2071 S13: 0.3099
REMARK 3 S21: -0.1542 S22: 0.1801 S23: -0.5654
REMARK 3 S31: 0.0383 S32: 1.1186 S33: -0.0369
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN B AND RESID 88:112)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3006 -49.3685 -42.1518
REMARK 3 T TENSOR
REMARK 3 T11: 1.3530 T22: 2.0294
REMARK 3 T33: 2.1875 T12: -0.0391
REMARK 3 T13: 0.0978 T23: 0.8321
REMARK 3 L TENSOR
REMARK 3 L11: 5.0749 L22: 0.5474
REMARK 3 L33: 5.4344 L12: 0.1701
REMARK 3 L13: 2.6065 L23: 1.2272
REMARK 3 S TENSOR
REMARK 3 S11: 0.2575 S12: 1.0921 S13: 0.7272
REMARK 3 S21: -1.7220 S22: -0.0581 S23: 0.1681
REMARK 3 S31: 0.2229 S32: 0.4646 S33: -0.1897
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN B AND RESID 113:140)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8986 -43.6165 -48.9270
REMARK 3 T TENSOR
REMARK 3 T11: 1.0755 T22: 2.2555
REMARK 3 T33: 2.8071 T12: 0.0494
REMARK 3 T13: 0.2677 T23: 1.1265
REMARK 3 L TENSOR
REMARK 3 L11: 6.7950 L22: 7.7162
REMARK 3 L33: 0.8559 L12: -7.2149
REMARK 3 L13: 2.3988 L23: -2.5703
REMARK 3 S TENSOR
REMARK 3 S11: 0.2962 S12: 0.2236 S13: 0.6335
REMARK 3 S21: -0.8573 S22: -1.0880 S23: -3.2464
REMARK 3 S31: -0.4369 S32: 1.7294 S33: 1.6600
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 141:184)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7381 -41.9459 -53.9384
REMARK 3 T TENSOR
REMARK 3 T11: 1.2392 T22: 2.1675
REMARK 3 T33: 2.1071 T12: 0.1895
REMARK 3 T13: 0.2677 T23: 1.2835
REMARK 3 L TENSOR
REMARK 3 L11: 5.6225 L22: 2.3776
REMARK 3 L33: 8.9478 L12: -1.0557
REMARK 3 L13: 6.9322 L23: -2.1903
REMARK 3 S TENSOR
REMARK 3 S11: 0.9067 S12: -1.4491 S13: -2.1447
REMARK 3 S21: -1.1457 S22: -1.1199 S23: -1.9801
REMARK 3 S31: 0.3481 S32: 0.6564 S33: 0.5690
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 185:198)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3821 -40.3963 -55.6073
REMARK 3 T TENSOR
REMARK 3 T11: 1.2567 T22: 1.9008
REMARK 3 T33: 2.3941 T12: -0.0205
REMARK 3 T13: 0.3737 T23: 0.4495
REMARK 3 L TENSOR
REMARK 3 L11: 4.9235 L22: 5.3495
REMARK 3 L33: 8.2335 L12: -5.0797
REMARK 3 L13: 6.3067 L23: -6.3139
REMARK 3 S TENSOR
REMARK 3 S11: -1.2410 S12: -1.8158 S13: 0.7340
REMARK 3 S21: -0.1345 S22: 0.8525 S23: -2.0467
REMARK 3 S31: -0.4092 S32: 0.2215 S33: 1.7885
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 199:239)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8890 -45.7537 -58.3014
REMARK 3 T TENSOR
REMARK 3 T11: 1.7144 T22: 2.1289
REMARK 3 T33: 1.5908 T12: 0.6093
REMARK 3 T13: -0.0192 T23: 0.6512
REMARK 3 L TENSOR
REMARK 3 L11: 9.3827 L22: 3.4328
REMARK 3 L33: 4.2769 L12: -2.7733
REMARK 3 L13: 0.3811 L23: 1.8822
REMARK 3 S TENSOR
REMARK 3 S11: -0.1250 S12: 0.5831 S13: 0.6149
REMARK 3 S21: -1.8041 S22: -0.3073 S23: -0.3184
REMARK 3 S31: 1.3557 S32: 1.7211 S33: 0.6033
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 240:262)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3529 -48.5233 -63.4305
REMARK 3 T TENSOR
REMARK 3 T11: 1.8345 T22: 2.2005
REMARK 3 T33: 1.1269 T12: 0.4148
REMARK 3 T13: -0.1053 T23: 0.7466
REMARK 3 L TENSOR
REMARK 3 L11: 2.6823 L22: 2.7599
REMARK 3 L33: 0.1715 L12: 1.4445
REMARK 3 L13: -0.3955 L23: 0.2384
REMARK 3 S TENSOR
REMARK 3 S11: 0.1598 S12: -0.0154 S13: -0.6493
REMARK 3 S21: -0.6296 S22: -1.1918 S23: -0.6564
REMARK 3 S31: -0.9658 S32: 2.0384 S33: 0.5280
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 263:308)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2793 -57.8753 -57.4254
REMARK 3 T TENSOR
REMARK 3 T11: 1.7614 T22: 1.7960
REMARK 3 T33: 1.1676 T12: 0.4553
REMARK 3 T13: -0.3912 T23: 0.1032
REMARK 3 L TENSOR
REMARK 3 L11: 2.1824 L22: 3.2315
REMARK 3 L33: 2.4917 L12: 1.2625
REMARK 3 L13: -1.5930 L23: -2.4113
REMARK 3 S TENSOR
REMARK 3 S11: 0.2826 S12: 1.3704 S13: -0.0707
REMARK 3 S21: -1.8280 S22: -0.7102 S23: 0.1426
REMARK 3 S31: 0.5269 S32: 0.2124 S33: 0.3463
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN B AND RESID 309:315)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4688 -59.3753 -50.2059
REMARK 3 T TENSOR
REMARK 3 T11: 1.5244 T22: 2.3694
REMARK 3 T33: 0.6767 T12: 1.6109
REMARK 3 T13: -0.9111 T23: 0.4032
REMARK 3 L TENSOR
REMARK 3 L11: 1.8496 L22: 5.0056
REMARK 3 L33: 0.2597 L12: 0.7116
REMARK 3 L13: -0.6333 L23: 0.2650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: -0.7669 S13: -0.1858
REMARK 3 S21: -0.8538 S22: 0.7673 S23: 1.5742
REMARK 3 S31: -0.4094 S32: -1.6265 S33: 0.3804
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN B AND RESID 316:371)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8698 -66.9347 -44.6214
REMARK 3 T TENSOR
REMARK 3 T11: 1.3526 T22: 1.1255
REMARK 3 T33: 1.2631 T12: 0.3977
REMARK 3 T13: -0.3340 T23: 0.0785
REMARK 3 L TENSOR
REMARK 3 L11: 2.4107 L22: 6.0469
REMARK 3 L33: 9.8504 L12: 2.0930
REMARK 3 L13: 0.2099 L23: 3.2892
REMARK 3 S TENSOR
REMARK 3 S11: 0.0452 S12: 0.4294 S13: -0.1480
REMARK 3 S21: -1.1361 S22: -0.4257 S23: -0.0606
REMARK 3 S31: 1.5242 S32: 0.4007 S33: 0.2396
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN B AND RESID 372:403)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6656 -66.0645 -29.0811
REMARK 3 T TENSOR
REMARK 3 T11: 0.9164 T22: 1.0792
REMARK 3 T33: 1.4571 T12: 0.2109
REMARK 3 T13: -0.3852 T23: 0.2104
REMARK 3 L TENSOR
REMARK 3 L11: 4.5079 L22: 5.6915
REMARK 3 L33: 6.3551 L12: -1.6254
REMARK 3 L13: -2.0573 L23: -4.1911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.9024 S13: -1.0914
REMARK 3 S21: -0.5771 S22: -1.0676 S23: -0.3878
REMARK 3 S31: -0.0947 S32: 1.1607 S33: 0.7904
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN B AND RESID 404:425)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.8638 -55.4274 -32.7012
REMARK 3 T TENSOR
REMARK 3 T11: 1.0312 T22: 1.0850
REMARK 3 T33: 1.4307 T12: 0.1746
REMARK 3 T13: -0.2671 T23: -0.1032
REMARK 3 L TENSOR
REMARK 3 L11: 8.0100 L22: 8.1666
REMARK 3 L33: 9.6950 L12: 4.3369
REMARK 3 L13: 1.8723 L23: -1.7812
REMARK 3 S TENSOR
REMARK 3 S11: -0.5534 S12: -0.4852 S13: -0.7938
REMARK 3 S21: -0.4944 S22: 0.2272 S23: 0.2390
REMARK 3 S31: 0.0002 S32: -1.3783 S33: 0.2086
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN B AND RESID 426:571)
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1379 -44.9712 -30.5917
REMARK 3 T TENSOR
REMARK 3 T11: 0.8758 T22: 0.9289
REMARK 3 T33: 1.2211 T12: 0.1267
REMARK 3 T13: -0.4544 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.7809 L22: 4.7938
REMARK 3 L33: 4.7943 L12: -0.9547
REMARK 3 L13: 0.7797 L23: -1.7216
REMARK 3 S TENSOR
REMARK 3 S11: -0.4477 S12: 0.0723 S13: 0.3120
REMARK 3 S21: -0.1179 S22: 0.2937 S23: -0.0600
REMARK 3 S31: -0.2778 S32: -0.1417 S33: 0.2255
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: (CHAIN B AND RESID 572:605)
REMARK 3 ORIGIN FOR THE GROUP (A): -46.5768 -28.9942 -33.5932
REMARK 3 T TENSOR
REMARK 3 T11: 1.5525 T22: 0.9406
REMARK 3 T33: 1.5304 T12: 0.1658
REMARK 3 T13: -0.7175 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 4.1894 L22: 0.7577
REMARK 3 L33: 7.1582 L12: -0.9477
REMARK 3 L13: 2.1588 L23: -2.3654
REMARK 3 S TENSOR
REMARK 3 S11: -0.1867 S12: -0.4194 S13: 0.7626
REMARK 3 S21: 1.1720 S22: -0.0469 S23: -0.8435
REMARK 3 S31: -1.9623 S32: -0.6024 S33: 0.2615
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: (CHAIN B AND RESID 606:615)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5405 -27.7908 -28.3524
REMARK 3 T TENSOR
REMARK 3 T11: 2.0373 T22: 2.0648
REMARK 3 T33: 2.4914 T12: -0.5406
REMARK 3 T13: -0.7539 T23: 0.3493
REMARK 3 L TENSOR
REMARK 3 L11: 6.5200 L22: 3.8043
REMARK 3 L33: 5.2238 L12: 4.3736
REMARK 3 L13: -5.6186 L23: -4.3532
REMARK 3 S TENSOR
REMARK 3 S11: 0.5191 S12: 0.1694 S13: 2.2934
REMARK 3 S21: -1.5902 S22: 1.4231 S23: 0.4286
REMARK 3 S31: -1.6857 S32: 2.4442 S33: -1.4592
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN B AND RESID 616:632)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.3760 -27.0675 -19.1539
REMARK 3 T TENSOR
REMARK 3 T11: 2.2471 T22: 0.8795
REMARK 3 T33: 2.2191 T12: 0.0335
REMARK 3 T13: -0.6213 T23: -0.0938
REMARK 3 L TENSOR
REMARK 3 L11: 6.0415 L22: 5.5658
REMARK 3 L33: 6.9800 L12: -1.6983
REMARK 3 L13: 3.6584 L23: -5.9610
REMARK 3 S TENSOR
REMARK 3 S11: -1.0387 S12: -0.3686 S13: 2.6867
REMARK 3 S21: 3.4121 S22: 0.3581 S23: -0.8125
REMARK 3 S31: -2.6442 S32: -0.1231 S33: 1.4472
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: (CHAIN B AND RESID 633:667)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6245 -41.7059 -16.4614
REMARK 3 T TENSOR
REMARK 3 T11: 2.0379 T22: 1.4515
REMARK 3 T33: 1.8135 T12: 0.1210
REMARK 3 T13: -0.9738 T23: -0.0880
REMARK 3 L TENSOR
REMARK 3 L11: 7.0268 L22: 6.4237
REMARK 3 L33: 8.5408 L12: 1.2076
REMARK 3 L13: -3.1314 L23: -3.2408
REMARK 3 S TENSOR
REMARK 3 S11: -1.2500 S12: -0.4914 S13: 1.6814
REMARK 3 S21: 1.1881 S22: 0.2296 S23: -0.7201
REMARK 3 S31: -1.7857 S32: -0.0055 S33: 0.5205
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: (CHAIN B AND RESID 668:675)
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3731 -35.2680 -8.4340
REMARK 3 T TENSOR
REMARK 3 T11: 2.1592 T22: 0.9964
REMARK 3 T33: 1.1766 T12: 0.2459
REMARK 3 T13: -0.4648 T23: -0.3081
REMARK 3 L TENSOR
REMARK 3 L11: 1.9714 L22: 0.8193
REMARK 3 L33: 7.8316 L12: 1.2318
REMARK 3 L13: -2.8048 L23: -2.2229
REMARK 3 S TENSOR
REMARK 3 S11: 2.6924 S12: 1.8946 S13: -0.9815
REMARK 3 S21: -2.5364 S22: -2.6949 S23: 1.8501
REMARK 3 S31: 2.9112 S32: 4.0398 S33: -0.9294
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 5 THROUGH 26 OR
REMARK 3 RESID 28 THROUGH 56 OR RESID 58 THROUGH
REMARK 3 71 OR RESID 73 OR RESID 75 THROUGH 86 OR
REMARK 3 RESID 88 THROUGH 89 OR RESID 91 THROUGH
REMARK 3 112 OR RESID 114 THROUGH 119 OR RESID 121
REMARK 3 THROUGH 136 OR RESID 139 THROUGH 146 OR
REMARK 3 RESID 177 THROUGH 199 OR RESID 201
REMARK 3 THROUGH 242 OR RESID 244 THROUGH 247 OR
REMARK 3 RESID 249 THROUGH 254 OR RESID 256
REMARK 3 THROUGH 266 OR RESID 268 THROUGH 291 OR
REMARK 3 RESID 293 THROUGH 384 OR RESID 386
REMARK 3 THROUGH 390 OR RESID 392 THROUGH 394 OR
REMARK 3 RESID 397 THROUGH 413 OR RESID 415
REMARK 3 THROUGH 433 OR RESID 435 THROUGH 490 OR
REMARK 3 RESID 492 THROUGH 568 OR RESID 570
REMARK 3 THROUGH 579 OR RESID 581 THROUGH 614 OR
REMARK 3 RESID 617 THROUGH 621 OR RESID 624
REMARK 3 THROUGH 640 OR RESID 642 THROUGH 660 OR
REMARK 3 RESID 662 THROUGH 671 OR RESID 673
REMARK 3 THROUGH 675))
REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 5 THROUGH 26 OR
REMARK 3 RESID 28 THROUGH 56 OR RESID 58 THROUGH
REMARK 3 71 OR RESID 73 OR RESID 75 THROUGH 86 OR
REMARK 3 RESID 88 THROUGH 89 OR RESID 91 THROUGH
REMARK 3 112 OR RESID 114 THROUGH 119 OR RESID 121
REMARK 3 THROUGH 136 OR RESID 139 THROUGH 146 OR
REMARK 3 RESID 177 THROUGH 199 OR RESID 201
REMARK 3 THROUGH 242 OR RESID 244 THROUGH 247 OR
REMARK 3 RESID 249 THROUGH 254 OR RESID 256
REMARK 3 THROUGH 266 OR RESID 268 THROUGH 291 OR
REMARK 3 RESID 293 THROUGH 384 OR RESID 386
REMARK 3 THROUGH 390 OR RESID 392 THROUGH 394 OR
REMARK 3 RESID 397 THROUGH 413 OR RESID 415
REMARK 3 THROUGH 433 OR RESID 435 THROUGH 490 OR
REMARK 3 RESID 492 THROUGH 568 OR RESID 570
REMARK 3 THROUGH 579 OR RESID 581 THROUGH 614 OR
REMARK 3 RESID 617 THROUGH 621 OR RESID 624
REMARK 3 THROUGH 640 OR RESID 642 THROUGH 660 OR
REMARK 3 RESID 662 THROUGH 671 OR RESID 673
REMARK 3 THROUGH 675))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7C72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1300016197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X CDTE 1M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56249
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 19.50
REMARK 200 R MERGE (I) : 0.24070
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.50
REMARK 200 R MERGE FOR SHELL (I) : 3.35800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 3AZO
REMARK 200
REMARK 200 REMARK: DIAMOND SHAPED CRYSTALS WITH A HEXAGONAL SYMMETRY
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 7, 2.4 M DL
REMARK 280 -MALIC ACID PH 7.0 20 % (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 287.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
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 73.15500
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 73.15500
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 73.15500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ALA A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 154
REMARK 465 PRO A 155
REMARK 465 PRO A 156
REMARK 465 PRO A 157
REMARK 465 ALA A 158
REMARK 465 GLU A 159
REMARK 465 GLY A 160
REMARK 465 GLU A 161
REMARK 465 GLU A 162
REMARK 465 GLY A 163
REMARK 465 ALA A 164
REMARK 465 PRO A 165
REMARK 465 ALA A 166
REMARK 465 SER A 167
REMARK 465 GLU A 168
REMARK 465 GLY A 676
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ALA B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 GLY B 147
REMARK 465 HIS B 148
REMARK 465 ILE B 149
REMARK 465 ALA B 150
REMARK 465 ALA B 151
REMARK 465 PRO B 152
REMARK 465 PRO B 153
REMARK 465 GLU B 154
REMARK 465 PRO B 155
REMARK 465 PRO B 156
REMARK 465 PRO B 157
REMARK 465 ALA B 158
REMARK 465 GLU B 159
REMARK 465 GLY B 160
REMARK 465 GLU B 161
REMARK 465 GLU B 162
REMARK 465 GLY B 163
REMARK 465 ALA B 164
REMARK 465 PRO B 165
REMARK 465 ALA B 166
REMARK 465 SER B 167
REMARK 465 GLU B 168
REMARK 465 GLU B 169
REMARK 465 PRO B 170
REMARK 465 ALA B 171
REMARK 465 VAL B 172
REMARK 465 THR B 173
REMARK 465 GLY B 676
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 OG SER B 97 OH TYR B 132 1.83
REMARK 500 OH TYR A 349 OE2 GLU B 395 1.97
REMARK 500 OG SER A 97 OH TYR A 132 2.04
REMARK 500 O GLY B 524 N GLY B 528 2.09
REMARK 500 OE2 GLU B 636 N ARG B 641 2.13
REMARK 500 OD1 ASP A 20 NH2 ARG A 23 2.14
REMARK 500 NH1 ARG B 196 O GLY B 242 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 153 C - N - CA ANGL. DEV. = 11.1 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 ARG A 72 109.20 -163.52
REMARK 500 HIS A 76 13.23 55.21
REMARK 500 GLU A 77 -11.84 66.22
REMARK 500 GLN A 102 -2.99 66.58
REMARK 500 THR A 139 13.94 54.64
REMARK 500 ASP A 265 -175.76 -172.02
REMARK 500 SER A 268 143.36 -170.76
REMARK 500 ASP A 274 30.11 -96.20
REMARK 500 HIS A 287 -56.35 -123.18
REMARK 500 TYR A 295 73.02 37.80
REMARK 500 GLU A 395 87.35 -68.42
REMARK 500 PHE A 414 48.21 -91.45
REMARK 500 ARG A 491 14.92 58.23
REMARK 500 VAL A 495 -61.83 -126.10
REMARK 500 PRO A 576 78.58 -57.21
REMARK 500 VAL A 608 -61.50 -93.64
REMARK 500 PRO A 611 -6.65 -59.19
REMARK 500 ASP A 623 -12.57 72.21
REMARK 500 ARG B 25 59.36 -92.28
REMARK 500 LEU B 65 91.66 67.74
REMARK 500 GLN B 66 -169.27 -77.84
REMARK 500 HIS B 76 13.74 56.38
REMARK 500 GLU B 77 -11.13 67.81
REMARK 500 GLN B 102 -1.93 65.61
REMARK 500 PRO B 112 47.59 -82.40
REMARK 500 LEU B 120 104.92 -56.01
REMARK 500 ASP B 137 38.88 -140.01
REMARK 500 THR B 139 15.79 54.33
REMARK 500 ASP B 191 106.97 -160.67
REMARK 500 ALA B 200 -166.37 -76.40
REMARK 500 ASP B 241 -169.98 -102.18
REMARK 500 LEU B 259 -7.15 -148.36
REMARK 500 ASP B 265 -175.18 -172.11
REMARK 500 SER B 268 147.34 -171.11
REMARK 500 HIS B 287 -54.09 -122.03
REMARK 500 TYR B 295 70.82 36.27
REMARK 500 GLU B 395 75.94 50.25
REMARK 500 ASN B 398 126.11 -172.43
REMARK 500 ARG B 491 19.99 50.39
REMARK 500 VAL B 495 -61.67 -127.50
REMARK 500 PHE B 548 63.76 39.45
REMARK 500 VAL B 608 -60.96 -94.73
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 ASN A 223 HIS A 224 -135.38
REMARK 500 ASN B 223 HIS B 224 -140.49
REMARK 500 GLU B 395 LEU B 396 148.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 703
DBREF 7C72 A -19 676 PDB 7C72 7C72 -19 676
DBREF 7C72 B -19 676 PDB 7C72 7C72 -19 676
SEQRES 1 A 696 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 696 LEU VAL PRO ALA GLY SER HIS MET THR ALA ARG ALA THR
SEQRES 3 A 696 LEU PRO TYR GLY SER TRP PRO SER PRO ILE SER ALA ALA
SEQRES 4 A 696 ASP VAL ALA ARG ALA ARG LEU ARG LEU SER PHE PRO THR
SEQRES 5 A 696 VAL ALA GLY ASP ASP VAL TRP TRP GLN GLU THR ARG PRO
SEQRES 6 A 696 GLU GLU ASP GLY ARG THR THR VAL ILE HIS LEU ARG GLY
SEQRES 7 A 696 GLY HIS ARG THR GLU LEU LEU GLN ALA PRO TRP ASP ALA
SEQRES 8 A 696 ARG THR ARG VAL HIS GLU TYR GLY GLY ARG SER TYR LEU
SEQRES 9 A 696 PRO ILE ARG THR ALA GLU GLY TRP SER VAL VAL PHE SER
SEQRES 10 A 696 ASN TYR ASP ASP GLN ARG LEU HIS ARG LEU ASP GLU GLY
SEQRES 11 A 696 ASP PRO LYS PRO TYR PRO LEU THR PRO LEU PRO ALA VAL
SEQRES 12 A 696 PRO ALA GLY LEU ARG TYR ALA ASP TYR VAL LEU SER PRO
SEQRES 13 A 696 ASP GLY THR GLU VAL TRP CYS VAL CYS GLU GLY HIS ILE
SEQRES 14 A 696 ALA ALA PRO PRO GLU PRO PRO PRO ALA GLU GLY GLU GLU
SEQRES 15 A 696 GLY ALA PRO ALA SER GLU GLU PRO ALA VAL THR GLY ILE
SEQRES 16 A 696 ARG ARG ALA ILE VAL ALA ILE PRO LEU ASP GLY ARG ALA
SEQRES 17 A 696 ALA GLU ASP ALA GLY ALA ILE ARG GLU LEU VAL ALA GLY
SEQRES 18 A 696 ALA GLN PHE TYR ALA SER PRO ALA PRO SER PRO GLY GLY
SEQRES 19 A 696 GLY HIS LEU ALA TRP VAL GLN TRP ASN HIS PRO ARG MET
SEQRES 20 A 696 PRO TRP ASP GLY THR GLU VAL ARG VAL ALA ALA VAL GLU
SEQRES 21 A 696 ASP GLY ARG THR VAL ALA PRO ARG THR VAL LYS GLY GLY
SEQRES 22 A 696 LEU LYS GLU SER ALA LEU ALA PRO LEU TRP ARG ASP GLU
SEQRES 23 A 696 GLU SER LEU TYR VAL ILE SER ASP TRP PRO GLY TRP TRP
SEQRES 24 A 696 ASN ILE TYR GLN VAL GLY LEU HIS GLY GLU SER PRO GLN
SEQRES 25 A 696 ALA LEU TYR PRO ALA GLU GLU GLU PHE ALA GLY PRO LEU
SEQRES 26 A 696 TRP GLN LEU GLY GLY MET PRO TYR ALA LEU LEU GLY ASP
SEQRES 27 A 696 GLY ARG LEU ALA VAL LEU HIS GLY GLU GLY ASP LEU ARG
SEQRES 28 A 696 LEU GLY VAL TYR ASP PRO GLU THR LEU ASP LEU VAL ASP
SEQRES 29 A 696 LEU GLU VAL PRO TYR GLU HIS TRP ALA THR GLN LEU SER
SEQRES 30 A 696 ALA ASP GLY THR THR VAL VAL GLY ILE GLY GLY GLY PRO
SEQRES 31 A 696 ASP LEU PRO ALA SER VAL VAL ARG VAL ASP THR THR THR
SEQRES 32 A 696 GLY ARG VAL GLU GLY LEU ARG ARG GLU LEU ALA GLU LEU
SEQRES 33 A 696 PRO ASN VAL ALA TYR LEU SER ARG PRO ARG ALA GLU ARG
SEQRES 34 A 696 LEU ASP GLY PRO PHE GLY ARG PRO VAL HIS ALA TYR VAL
SEQRES 35 A 696 PHE PRO PRO THR ASN PRO GLU ALA ALA ALA PRO GLU GLY
SEQRES 36 A 696 GLU LEU PRO PRO TYR VAL VAL PHE VAL HIS GLY GLY PRO
SEQRES 37 A 696 THR GLY ARG VAL SER THR VAL LEU ASP LEU GLU ARG VAL
SEQRES 38 A 696 TYR PHE THR SER ARG GLY ILE GLY VAL ILE ASP VAL ASN
SEQRES 39 A 696 TYR GLY GLY SER THR GLY TYR GLY ARG ALA TYR ARG GLU
SEQRES 40 A 696 ARG LEU ARG ARG GLN TRP GLY VAL VAL ASP VAL GLU ASP
SEQRES 41 A 696 ALA ILE ALA ALA ALA GLN ALA LEU VAL ASP GLY GLY ILE
SEQRES 42 A 696 ALA ASP PRO ALA ARG LEU ALA ILE ARG GLY GLY SER ALA
SEQRES 43 A 696 GLY GLY TRP THR THR LEU ALA ALA ILE THR GLN THR ASP
SEQRES 44 A 696 VAL PHE LYS ALA ALA THR SER TYR PHE GLY ILE SER ASP
SEQRES 45 A 696 LEU GLN SER PHE ALA GLU ALA THR HIS ASP PHE GLU SER
SEQRES 46 A 696 GLN TYR LEU PHE GLY LEU ILE GLY PRO LEU PRO GLY PHE
SEQRES 47 A 696 GLU ARG ALA TYR GLU GLU ARG SER PRO LEU ARG HIS ALA
SEQRES 48 A 696 ASP ARG THR ALA CYS PRO VAL LEU LEU LEU GLN GLY LEU
SEQRES 49 A 696 ASN ASP PRO VAL VAL PRO PRO ASP GLN SER GLU ARG PHE
SEQRES 50 A 696 ALA LEU ALA LEU ALA ASP LYS LYS MET PRO TYR ALA TYR
SEQRES 51 A 696 LEU THR PHE GLU GLY GLU SER HIS GLY PHE ARG LYS ALA
SEQRES 52 A 696 GLY THR VAL VAL ARG SER LEU GLU ALA GLU LEU ALA PHE
SEQRES 53 A 696 TYR GLY GLN THR LEU GLY PHE GLU PRO ARG GLY VAL GLU
SEQRES 54 A 696 PRO ILE ASN LEU THR VAL GLY
SEQRES 1 B 696 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 696 LEU VAL PRO ALA GLY SER HIS MET THR ALA ARG ALA THR
SEQRES 3 B 696 LEU PRO TYR GLY SER TRP PRO SER PRO ILE SER ALA ALA
SEQRES 4 B 696 ASP VAL ALA ARG ALA ARG LEU ARG LEU SER PHE PRO THR
SEQRES 5 B 696 VAL ALA GLY ASP ASP VAL TRP TRP GLN GLU THR ARG PRO
SEQRES 6 B 696 GLU GLU ASP GLY ARG THR THR VAL ILE HIS LEU ARG GLY
SEQRES 7 B 696 GLY HIS ARG THR GLU LEU LEU GLN ALA PRO TRP ASP ALA
SEQRES 8 B 696 ARG THR ARG VAL HIS GLU TYR GLY GLY ARG SER TYR LEU
SEQRES 9 B 696 PRO ILE ARG THR ALA GLU GLY TRP SER VAL VAL PHE SER
SEQRES 10 B 696 ASN TYR ASP ASP GLN ARG LEU HIS ARG LEU ASP GLU GLY
SEQRES 11 B 696 ASP PRO LYS PRO TYR PRO LEU THR PRO LEU PRO ALA VAL
SEQRES 12 B 696 PRO ALA GLY LEU ARG TYR ALA ASP TYR VAL LEU SER PRO
SEQRES 13 B 696 ASP GLY THR GLU VAL TRP CYS VAL CYS GLU GLY HIS ILE
SEQRES 14 B 696 ALA ALA PRO PRO GLU PRO PRO PRO ALA GLU GLY GLU GLU
SEQRES 15 B 696 GLY ALA PRO ALA SER GLU GLU PRO ALA VAL THR GLY ILE
SEQRES 16 B 696 ARG ARG ALA ILE VAL ALA ILE PRO LEU ASP GLY ARG ALA
SEQRES 17 B 696 ALA GLU ASP ALA GLY ALA ILE ARG GLU LEU VAL ALA GLY
SEQRES 18 B 696 ALA GLN PHE TYR ALA SER PRO ALA PRO SER PRO GLY GLY
SEQRES 19 B 696 GLY HIS LEU ALA TRP VAL GLN TRP ASN HIS PRO ARG MET
SEQRES 20 B 696 PRO TRP ASP GLY THR GLU VAL ARG VAL ALA ALA VAL GLU
SEQRES 21 B 696 ASP GLY ARG THR VAL ALA PRO ARG THR VAL LYS GLY GLY
SEQRES 22 B 696 LEU LYS GLU SER ALA LEU ALA PRO LEU TRP ARG ASP GLU
SEQRES 23 B 696 GLU SER LEU TYR VAL ILE SER ASP TRP PRO GLY TRP TRP
SEQRES 24 B 696 ASN ILE TYR GLN VAL GLY LEU HIS GLY GLU SER PRO GLN
SEQRES 25 B 696 ALA LEU TYR PRO ALA GLU GLU GLU PHE ALA GLY PRO LEU
SEQRES 26 B 696 TRP GLN LEU GLY GLY MET PRO TYR ALA LEU LEU GLY ASP
SEQRES 27 B 696 GLY ARG LEU ALA VAL LEU HIS GLY GLU GLY ASP LEU ARG
SEQRES 28 B 696 LEU GLY VAL TYR ASP PRO GLU THR LEU ASP LEU VAL ASP
SEQRES 29 B 696 LEU GLU VAL PRO TYR GLU HIS TRP ALA THR GLN LEU SER
SEQRES 30 B 696 ALA ASP GLY THR THR VAL VAL GLY ILE GLY GLY GLY PRO
SEQRES 31 B 696 ASP LEU PRO ALA SER VAL VAL ARG VAL ASP THR THR THR
SEQRES 32 B 696 GLY ARG VAL GLU GLY LEU ARG ARG GLU LEU ALA GLU LEU
SEQRES 33 B 696 PRO ASN VAL ALA TYR LEU SER ARG PRO ARG ALA GLU ARG
SEQRES 34 B 696 LEU ASP GLY PRO PHE GLY ARG PRO VAL HIS ALA TYR VAL
SEQRES 35 B 696 PHE PRO PRO THR ASN PRO GLU ALA ALA ALA PRO GLU GLY
SEQRES 36 B 696 GLU LEU PRO PRO TYR VAL VAL PHE VAL HIS GLY GLY PRO
SEQRES 37 B 696 THR GLY ARG VAL SER THR VAL LEU ASP LEU GLU ARG VAL
SEQRES 38 B 696 TYR PHE THR SER ARG GLY ILE GLY VAL ILE ASP VAL ASN
SEQRES 39 B 696 TYR GLY GLY SER THR GLY TYR GLY ARG ALA TYR ARG GLU
SEQRES 40 B 696 ARG LEU ARG ARG GLN TRP GLY VAL VAL ASP VAL GLU ASP
SEQRES 41 B 696 ALA ILE ALA ALA ALA GLN ALA LEU VAL ASP GLY GLY ILE
SEQRES 42 B 696 ALA ASP PRO ALA ARG LEU ALA ILE ARG GLY GLY SER ALA
SEQRES 43 B 696 GLY GLY TRP THR THR LEU ALA ALA ILE THR GLN THR ASP
SEQRES 44 B 696 VAL PHE LYS ALA ALA THR SER TYR PHE GLY ILE SER ASP
SEQRES 45 B 696 LEU GLN SER PHE ALA GLU ALA THR HIS ASP PHE GLU SER
SEQRES 46 B 696 GLN TYR LEU PHE GLY LEU ILE GLY PRO LEU PRO GLY PHE
SEQRES 47 B 696 GLU ARG ALA TYR GLU GLU ARG SER PRO LEU ARG HIS ALA
SEQRES 48 B 696 ASP ARG THR ALA CYS PRO VAL LEU LEU LEU GLN GLY LEU
SEQRES 49 B 696 ASN ASP PRO VAL VAL PRO PRO ASP GLN SER GLU ARG PHE
SEQRES 50 B 696 ALA LEU ALA LEU ALA ASP LYS LYS MET PRO TYR ALA TYR
SEQRES 51 B 696 LEU THR PHE GLU GLY GLU SER HIS GLY PHE ARG LYS ALA
SEQRES 52 B 696 GLY THR VAL VAL ARG SER LEU GLU ALA GLU LEU ALA PHE
SEQRES 53 B 696 TYR GLY GLN THR LEU GLY PHE GLU PRO ARG GLY VAL GLU
SEQRES 54 B 696 PRO ILE ASN LEU THR VAL GLY
HET GOL A 701 14
HET MLT A 702 13
HET GOL A 703 14
HETNAM GOL GLYCEROL
HETNAM MLT D-MALATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 MLT C4 H6 O5
HELIX 1 AA1 SER A 17 ALA A 24 1 8
HELIX 2 AA2 PRO A 45 ASP A 48 5 4
HELIX 3 AA3 ARG A 74 TYR A 78 5 5
HELIX 4 AA4 ASP A 191 ILE A 195 5 5
HELIX 5 AA5 ASP A 457 SER A 465 1 9
HELIX 6 AA6 GLY A 482 ARG A 488 1 7
HELIX 7 AA7 VAL A 495 GLY A 511 1 17
HELIX 8 AA8 GLY A 524 THR A 538 1 15
HELIX 9 AA9 ASP A 552 THR A 560 1 9
HELIX 10 AB1 HIS A 561 GLN A 566 5 6
HELIX 11 AB2 TYR A 567 ILE A 572 1 6
HELIX 12 AB3 PHE A 578 SER A 586 1 9
HELIX 13 AB4 PRO A 587 THR A 594 5 8
HELIX 14 AB5 PRO A 611 ALA A 622 1 12
HELIX 15 AB6 LYS A 642 GLY A 662 1 21
HELIX 16 AB7 SER B 17 ALA B 24 1 8
HELIX 17 AB8 PRO B 45 ASP B 48 5 4
HELIX 18 AB9 ARG B 74 TYR B 78 5 5
HELIX 19 AC1 ASP B 191 ILE B 195 5 5
HELIX 20 AC2 ASN B 398 LEU B 402 5 5
HELIX 21 AC3 ASP B 457 SER B 465 1 9
HELIX 22 AC4 GLY B 482 ARG B 488 1 7
HELIX 23 AC5 VAL B 495 GLY B 511 1 17
HELIX 24 AC6 GLY B 524 THR B 538 1 15
HELIX 25 AC7 ASP B 552 GLU B 558 1 7
HELIX 26 AC8 GLN B 566 ILE B 572 1 7
HELIX 27 AC9 PHE B 578 SER B 586 1 9
HELIX 28 AD1 PRO B 587 THR B 594 5 8
HELIX 29 AD2 PRO B 610 LYS B 624 1 15
HELIX 30 AD3 LYS B 642 THR B 660 1 19
SHEET 1 AA1 4 SER A 29 ALA A 34 0
SHEET 2 AA1 4 ASP A 37 THR A 43 -1 O ASP A 37 N ALA A 34
SHEET 3 AA1 4 THR A 51 ARG A 57 -1 O THR A 52 N GLU A 42
SHEET 4 AA1 4 HIS A 60 GLU A 63 -1 O THR A 62 N HIS A 55
SHEET 1 AA2 4 TYR A 83 THR A 88 0
SHEET 2 AA2 4 GLY A 91 SER A 97 -1 O SER A 93 N ILE A 86
SHEET 3 AA2 4 LEU A 104 ASP A 108 -1 O HIS A 105 N PHE A 96
SHEET 4 AA2 4 TYR A 115 PRO A 116 -1 O TYR A 115 N ARG A 106
SHEET 1 AA3 4 LEU A 127 LEU A 134 0
SHEET 2 AA3 4 VAL A 141 ALA A 150 -1 O TRP A 142 N VAL A 133
SHEET 3 AA3 4 VAL A 172 ILE A 182 -1 O VAL A 180 N CYS A 143
SHEET 4 AA3 4 ARG A 196 ALA A 200 -1 O VAL A 199 N ILE A 179
SHEET 1 AA4 4 PHE A 204 PRO A 210 0
SHEET 2 AA4 4 HIS A 216 TRP A 222 -1 O ALA A 218 N ALA A 209
SHEET 3 AA4 4 GLU A 233 GLU A 240 -1 O ALA A 237 N LEU A 217
SHEET 4 AA4 4 ARG A 243 GLY A 252 -1 O LYS A 251 N VAL A 234
SHEET 1 AA5 4 ALA A 258 ASP A 265 0
SHEET 2 AA5 4 SER A 268 SER A 273 -1 O TYR A 270 N LEU A 262
SHEET 3 AA5 4 ASN A 280 VAL A 284 -1 O TYR A 282 N VAL A 271
SHEET 4 AA5 4 GLN A 292 LEU A 294 -1 O GLN A 292 N GLN A 283
SHEET 1 AA6 4 TYR A 313 LEU A 315 0
SHEET 2 AA6 4 LEU A 321 HIS A 325 -1 O ALA A 322 N ALA A 314
SHEET 3 AA6 4 ARG A 331 TYR A 335 -1 O ARG A 331 N HIS A 325
SHEET 4 AA6 4 LEU A 342 ASP A 344 -1 O VAL A 343 N VAL A 334
SHEET 1 AA7 3 HIS A 351 TRP A 352 0
SHEET 2 AA7 3 THR A 362 GLY A 368 -1 O GLY A 368 N HIS A 351
SHEET 3 AA7 3 SER A 357 ASP A 359 -1 N SER A 357 O VAL A 364
SHEET 1 AA8 4 HIS A 351 TRP A 352 0
SHEET 2 AA8 4 THR A 362 GLY A 368 -1 O GLY A 368 N HIS A 351
SHEET 3 AA8 4 SER A 375 ASP A 380 -1 O VAL A 379 N VAL A 363
SHEET 4 AA8 4 VAL A 386 ARG A 391 -1 O GLU A 387 N ARG A 378
SHEET 1 AA9 8 ARG A 406 ASP A 411 0
SHEET 2 AA9 8 PRO A 417 PHE A 423 -1 O VAL A 422 N ARG A 406
SHEET 3 AA9 8 GLY A 469 ASN A 474 -1 O VAL A 470 N PHE A 423
SHEET 4 AA9 8 TYR A 440 VAL A 444 1 N PHE A 443 O ILE A 471
SHEET 5 AA9 8 LEU A 519 GLY A 523 1 O ALA A 520 N VAL A 442
SHEET 6 AA9 8 ALA A 543 TYR A 547 1 O TYR A 547 N GLY A 523
SHEET 7 AA9 8 VAL A 598 GLY A 603 1 O LEU A 599 N SER A 546
SHEET 8 AA9 8 TYR A 628 PHE A 633 1 O LEU A 631 N LEU A 600
SHEET 1 AB1 4 ARG B 27 ALA B 34 0
SHEET 2 AB1 4 ASP B 37 THR B 43 -1 O ASP B 37 N ALA B 34
SHEET 3 AB1 4 THR B 51 ARG B 57 -1 O LEU B 56 N VAL B 38
SHEET 4 AB1 4 HIS B 60 LEU B 64 -1 O THR B 62 N HIS B 55
SHEET 1 AB2 4 TYR B 83 THR B 88 0
SHEET 2 AB2 4 GLY B 91 SER B 97 -1 O SER B 93 N ILE B 86
SHEET 3 AB2 4 LEU B 104 LEU B 107 -1 O HIS B 105 N PHE B 96
SHEET 4 AB2 4 TYR B 115 PRO B 116 -1 O TYR B 115 N ARG B 106
SHEET 1 AB3 4 ARG B 128 LEU B 134 0
SHEET 2 AB3 4 GLU B 140 GLU B 146 -1 O VAL B 144 N ALA B 130
SHEET 3 AB3 4 ALA B 178 PRO B 183 -1 O VAL B 180 N CYS B 143
SHEET 4 AB3 4 ARG B 196 GLU B 197 -1 O ARG B 196 N ALA B 181
SHEET 1 AB4 4 PHE B 204 PRO B 210 0
SHEET 2 AB4 4 HIS B 216 TRP B 222 -1 O ALA B 218 N ALA B 209
SHEET 3 AB4 4 GLU B 233 VAL B 239 -1 O ALA B 237 N LEU B 217
SHEET 4 AB4 4 THR B 244 GLY B 252 -1 O VAL B 250 N VAL B 234
SHEET 1 AB5 4 LEU B 262 ASP B 265 0
SHEET 2 AB5 4 SER B 268 SER B 273 -1 O SER B 268 N ARG B 264
SHEET 3 AB5 4 ASN B 280 VAL B 284 -1 O TYR B 282 N VAL B 271
SHEET 4 AB5 4 GLN B 292 LEU B 294 -1 O GLN B 292 N GLN B 283
SHEET 1 AB6 4 TYR B 313 LEU B 315 0
SHEET 2 AB6 4 LEU B 321 HIS B 325 -1 O ALA B 322 N ALA B 314
SHEET 3 AB6 4 ARG B 331 TYR B 335 -1 O GLY B 333 N VAL B 323
SHEET 4 AB6 4 LEU B 342 ASP B 344 -1 O VAL B 343 N VAL B 334
SHEET 1 AB7 3 HIS B 351 TRP B 352 0
SHEET 2 AB7 3 THR B 362 GLY B 369 -1 O GLY B 368 N HIS B 351
SHEET 3 AB7 3 SER B 357 ASP B 359 -1 N SER B 357 O VAL B 364
SHEET 1 AB8 4 HIS B 351 TRP B 352 0
SHEET 2 AB8 4 THR B 362 GLY B 369 -1 O GLY B 368 N HIS B 351
SHEET 3 AB8 4 LEU B 372 ASP B 380 -1 O LEU B 372 N GLY B 369
SHEET 4 AB8 4 VAL B 386 ARG B 391 -1 O GLU B 387 N ARG B 378
SHEET 1 AB9 8 ARG B 406 ASP B 411 0
SHEET 2 AB9 8 PRO B 417 PHE B 423 -1 O VAL B 422 N ARG B 406
SHEET 3 AB9 8 GLY B 469 ASN B 474 -1 O VAL B 470 N PHE B 423
SHEET 4 AB9 8 TYR B 440 VAL B 444 1 N PHE B 443 O ILE B 471
SHEET 5 AB9 8 LEU B 519 GLY B 523 1 O ALA B 520 N VAL B 442
SHEET 6 AB9 8 ALA B 543 TYR B 547 1 O THR B 545 N ILE B 521
SHEET 7 AB9 8 VAL B 598 GLY B 603 1 O LEU B 599 N SER B 546
SHEET 8 AB9 8 TYR B 628 PHE B 633 1 O LEU B 631 N LEU B 600
SITE 1 AC1 5 TRP A 229 ASP A 230 ARG A 486 GLU A 487
SITE 2 AC1 5 ARG A 490
SITE 1 AC2 7 LEU A 198 VAL A 199 ALA A 200 ARG A 235
SITE 2 AC2 7 THR A 244 PRO A 247 LYS A 255
SITE 1 AC3 3 LYS A 251 GLY A 252 GLU A 256
CRYST1 183.950 183.950 146.310 90.00 90.00 120.00 P 63 12
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 0.005436 0.003139 0.000000 0.00000
SCALE2 0.000000 0.006277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006835 0.00000
TER 5069 VAL A 675
TER 10057 VAL B 675
MASTER 1088 0 3 30 78 0 5 610076 2 41 108
END
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