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HEADER VIRAL PROTEIN 04-MAY-24 8ZE6
TITLE CRYSTAL STRUCTURE OF MJHKU4R-COV-1 RBD BOUND TO MJDPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: B, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SPIKE GLYCOPROTEIN;
COMPND 7 CHAIN: C, A;
COMPND 8 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: SEQUENCE REFERENCE FOR SOURCE ORGANISM PANGOLIN
COMPND 11 CORONAVIRUS HKU4 IS NOT AVAILABLE IN UNIPROT AT THE TIME OF
COMPND 12 BIOCURATION. CURRENT SEQUENCE REFERENCE IS FROM UNIPROT ID
COMPND 13 A0AAE8ZFM2.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MANIS JAVANICA;
SOURCE 3 ORGANISM_TAXID: 9974;
SOURCE 4 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 274590;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: PANGOLIN CORONAVIRUS HKU4;
SOURCE 8 ORGANISM_TAXID: 3027597;
SOURCE 9 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 274590
KEYWDS VIRUS PROTEIN AND RECEPTOR COMPLEX, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YANG,Z.LI,Y.XU,S.ZHANG
REVDAT 1 30-OCT-24 8ZE6 0
JRNL AUTH M.YANG,Z.LI,Y.XU,S.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF MJHKU4R-COV-1 RBD BOUND TO MJDPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 66672
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3342
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 47.4900 - 7.7900 0.97 2664 136 0.2016 0.2187
REMARK 3 2 7.7800 - 6.1800 0.99 2660 149 0.2331 0.2823
REMARK 3 3 6.1800 - 5.4000 0.99 2674 139 0.2176 0.2309
REMARK 3 4 5.4000 - 4.9100 0.99 2642 162 0.1976 0.2031
REMARK 3 5 4.9100 - 4.5600 0.99 2646 144 0.1897 0.2226
REMARK 3 6 4.5600 - 4.2900 0.99 2658 129 0.1915 0.1994
REMARK 3 7 4.2900 - 4.0700 0.99 2626 127 0.2158 0.2603
REMARK 3 8 4.0700 - 3.9000 0.99 2663 146 0.2179 0.2765
REMARK 3 9 3.9000 - 3.7500 0.99 2630 164 0.2392 0.2755
REMARK 3 10 3.7500 - 3.6200 0.99 2631 146 0.2357 0.2733
REMARK 3 11 3.6200 - 3.5000 0.99 2638 125 0.2550 0.2755
REMARK 3 12 3.5000 - 3.4000 0.99 2689 128 0.2687 0.3111
REMARK 3 13 3.4000 - 3.3200 0.99 2634 133 0.2844 0.3452
REMARK 3 14 3.3200 - 3.2300 0.99 2605 154 0.2974 0.3560
REMARK 3 15 3.2300 - 3.1600 0.99 2659 125 0.2941 0.3325
REMARK 3 16 3.1600 - 3.0900 0.99 2659 139 0.2946 0.3405
REMARK 3 17 3.0900 - 3.0300 0.99 2646 125 0.3097 0.3527
REMARK 3 18 3.0300 - 2.9700 0.99 2637 129 0.3138 0.3791
REMARK 3 19 2.9700 - 2.9200 0.99 2607 144 0.3302 0.3744
REMARK 3 20 2.9200 - 2.8700 0.99 2620 157 0.3223 0.3685
REMARK 3 21 2.8700 - 2.8300 0.98 2641 124 0.3290 0.3569
REMARK 3 22 2.8300 - 2.7800 0.99 2624 125 0.3420 0.3597
REMARK 3 23 2.7800 - 2.7400 0.98 2615 139 0.3485 0.3655
REMARK 3 24 2.7400 - 2.7000 0.96 2562 153 0.3603 0.4002
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 15699
REMARK 3 ANGLE : 0.482 21342
REMARK 3 CHIRALITY : 0.049 2310
REMARK 3 PLANARITY : 0.004 2708
REMARK 3 DIHEDRAL : 14.985 5648
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 27
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6120 105.6043 92.0975
REMARK 3 T TENSOR
REMARK 3 T11: 0.3503 T22: 0.3806
REMARK 3 T33: 0.4508 T12: -0.0040
REMARK 3 T13: 0.0520 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.9501 L22: 0.9022
REMARK 3 L33: 2.5763 L12: 0.9327
REMARK 3 L13: -0.1242 L23: -0.3342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0740 S12: -0.1847 S13: 0.0467
REMARK 3 S21: -0.0746 S22: -0.0519 S23: 0.0412
REMARK 3 S31: 0.2271 S32: -0.1641 S33: 0.0117
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.0947 112.5981 110.7656
REMARK 3 T TENSOR
REMARK 3 T11: 0.3086 T22: 0.2927
REMARK 3 T33: 0.4060 T12: -0.0063
REMARK 3 T13: 0.0612 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.0156 L22: 1.2712
REMARK 3 L33: 1.4087 L12: 0.4355
REMARK 3 L13: 0.0752 L23: -0.1970
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.1404 S13: -0.0561
REMARK 3 S21: -0.0354 S22: 0.0705 S23: -0.1310
REMARK 3 S31: -0.0416 S32: 0.1438 S33: -0.0613
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 318 THROUGH 766 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5349 123.2402 108.9750
REMARK 3 T TENSOR
REMARK 3 T11: 0.4140 T22: 0.4203
REMARK 3 T33: 0.5033 T12: 0.0639
REMARK 3 T13: 0.0510 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 0.6684 L22: 0.3882
REMARK 3 L33: 1.5341 L12: 0.0604
REMARK 3 L13: 0.0020 L23: -0.0134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0153 S13: 0.0997
REMARK 3 S21: -0.0065 S22: 0.0204 S23: 0.0908
REMARK 3 S31: -0.2375 S32: -0.3689 S33: -0.0307
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 388 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.9058 123.8682 59.4062
REMARK 3 T TENSOR
REMARK 3 T11: 0.7576 T22: 1.8959
REMARK 3 T33: 1.2096 T12: -0.1842
REMARK 3 T13: 0.1214 T23: -0.2862
REMARK 3 L TENSOR
REMARK 3 L11: 1.0104 L22: 0.1417
REMARK 3 L33: 0.1469 L12: 0.1912
REMARK 3 L13: -0.2696 L23: -0.1397
REMARK 3 S TENSOR
REMARK 3 S11: -0.4539 S12: 0.1684 S13: -0.6732
REMARK 3 S21: -0.0528 S22: -0.3358 S23: 0.6662
REMARK 3 S31: 0.6669 S32: -1.2680 S33: 0.6718
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 408 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.4043 115.0904 58.1451
REMARK 3 T TENSOR
REMARK 3 T11: 0.5436 T22: 1.9358
REMARK 3 T33: 1.5681 T12: -0.2494
REMARK 3 T13: 0.0634 T23: -0.1716
REMARK 3 L TENSOR
REMARK 3 L11: 4.0486 L22: 0.3056
REMARK 3 L33: 0.8271 L12: 0.0941
REMARK 3 L13: 1.7679 L23: 0.1699
REMARK 3 S TENSOR
REMARK 3 S11: 0.2106 S12: 0.4773 S13: -1.0158
REMARK 3 S21: -0.3398 S22: 0.0461 S23: 0.6106
REMARK 3 S31: 0.4946 S32: -1.3060 S33: -0.1174
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 419 THROUGH 434 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.4911 122.1453 45.2099
REMARK 3 T TENSOR
REMARK 3 T11: 0.9342 T22: 2.0962
REMARK 3 T33: 1.0980 T12: 0.3450
REMARK 3 T13: -0.3093 T23: -0.1673
REMARK 3 L TENSOR
REMARK 3 L11: 4.4009 L22: 0.1087
REMARK 3 L33: 0.0084 L12: -0.6823
REMARK 3 L13: 0.1484 L23: -0.0268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.8504 S13: 0.5041
REMARK 3 S21: -0.1540 S22: -0.3722 S23: 0.1709
REMARK 3 S31: -0.1422 S32: -0.6080 S33: 0.3758
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 435 THROUGH 447 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.0288 109.7410 46.5595
REMARK 3 T TENSOR
REMARK 3 T11: 1.1306 T22: 1.4180
REMARK 3 T33: 1.7809 T12: -0.2062
REMARK 3 T13: -0.4338 T23: -0.4906
REMARK 3 L TENSOR
REMARK 3 L11: 1.7561 L22: 0.4135
REMARK 3 L33: 0.0237 L12: -0.8503
REMARK 3 L13: -0.1733 L23: 0.0810
REMARK 3 S TENSOR
REMARK 3 S11: 0.2316 S12: 0.3431 S13: -0.7059
REMARK 3 S21: -0.4120 S22: -0.3186 S23: 0.9243
REMARK 3 S31: 0.2521 S32: -1.1482 S33: 0.0886
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 448 THROUGH 463 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.6899 122.7565 51.6277
REMARK 3 T TENSOR
REMARK 3 T11: 0.4393 T22: 1.1246
REMARK 3 T33: 0.7137 T12: 0.0812
REMARK 3 T13: -0.0441 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 4.8249 L22: 5.9269
REMARK 3 L33: 4.2524 L12: -0.3506
REMARK 3 L13: 2.2242 L23: 2.0908
REMARK 3 S TENSOR
REMARK 3 S11: 0.1505 S12: -0.0356 S13: -0.3862
REMARK 3 S21: -0.5027 S22: -0.2572 S23: 1.1238
REMARK 3 S31: -0.1906 S32: -0.8278 S33: 0.2812
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 464 THROUGH 503 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2257 122.3969 51.9739
REMARK 3 T TENSOR
REMARK 3 T11: 0.4904 T22: 1.0166
REMARK 3 T33: 0.6621 T12: -0.0865
REMARK 3 T13: 0.0632 T23: -0.0821
REMARK 3 L TENSOR
REMARK 3 L11: 5.3168 L22: 7.6166
REMARK 3 L33: 3.9489 L12: -3.7585
REMARK 3 L13: 0.1583 L23: -0.3354
REMARK 3 S TENSOR
REMARK 3 S11: 0.3429 S12: 0.2416 S13: -0.5834
REMARK 3 S21: -0.6794 S22: -0.3850 S23: 1.0851
REMARK 3 S31: 0.3673 S32: -1.2471 S33: -0.0400
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 504 THROUGH 537 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6483 120.0172 64.7593
REMARK 3 T TENSOR
REMARK 3 T11: 0.5945 T22: 0.5502
REMARK 3 T33: 0.5585 T12: 0.0193
REMARK 3 T13: 0.1230 T23: -0.1399
REMARK 3 L TENSOR
REMARK 3 L11: 6.7934 L22: 2.4816
REMARK 3 L33: 3.9773 L12: 1.1774
REMARK 3 L13: 2.9035 L23: 0.2418
REMARK 3 S TENSOR
REMARK 3 S11: 0.2903 S12: -0.0751 S13: -0.6126
REMARK 3 S21: 0.3913 S22: 0.0236 S23: 0.0323
REMARK 3 S31: 0.7287 S32: -0.4317 S33: -0.1486
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 538 THROUGH 560 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6608 126.0207 70.7866
REMARK 3 T TENSOR
REMARK 3 T11: 0.6579 T22: 0.5032
REMARK 3 T33: 0.6221 T12: -0.0004
REMARK 3 T13: 0.0850 T23: -0.1582
REMARK 3 L TENSOR
REMARK 3 L11: 3.8120 L22: 2.6630
REMARK 3 L33: 7.6820 L12: 2.9623
REMARK 3 L13: -1.5017 L23: -2.7610
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.2745 S13: 0.2590
REMARK 3 S21: -0.5391 S22: -0.3510 S23: -0.0518
REMARK 3 S31: 0.2128 S32: 0.0067 S33: 0.4741
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 561 THROUGH 588 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1664 123.0204 55.3887
REMARK 3 T TENSOR
REMARK 3 T11: 0.5064 T22: 0.6593
REMARK 3 T33: 0.5786 T12: 0.0805
REMARK 3 T13: -0.0163 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 5.4163 L22: 1.8769
REMARK 3 L33: 4.5364 L12: 0.3199
REMARK 3 L13: 1.1123 L23: -0.3895
REMARK 3 S TENSOR
REMARK 3 S11: -0.3535 S12: 0.8746 S13: 0.4295
REMARK 3 S21: -0.1275 S22: 0.3143 S23: 0.6153
REMARK 3 S31: -0.3055 S32: -0.8335 S33: 0.1163
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 40 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2093 155.2139 49.0062
REMARK 3 T TENSOR
REMARK 3 T11: 0.5634 T22: 0.5230
REMARK 3 T33: 0.5387 T12: -0.0634
REMARK 3 T13: 0.0752 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.9028 L22: 0.3266
REMARK 3 L33: 2.2952 L12: 0.2250
REMARK 3 L13: 1.1095 L23: 0.7773
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: 0.1141 S13: 0.0018
REMARK 3 S21: -0.0897 S22: 0.0117 S23: -0.1166
REMARK 3 S31: -0.1998 S32: 0.2655 S33: 0.0653
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 131 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9858 152.3802 51.4089
REMARK 3 T TENSOR
REMARK 3 T11: 0.3876 T22: 0.4479
REMARK 3 T33: 0.5077 T12: 0.0576
REMARK 3 T13: 0.0529 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.8237 L22: 2.0714
REMARK 3 L33: 1.8642 L12: 0.5151
REMARK 3 L13: -0.4286 L23: -0.4431
REMARK 3 S TENSOR
REMARK 3 S11: -0.1247 S12: 0.4270 S13: 0.1279
REMARK 3 S21: -0.2302 S22: -0.0046 S23: -0.0616
REMARK 3 S31: 0.2484 S32: -0.0521 S33: 0.0937
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 222 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1118 154.1961 73.2089
REMARK 3 T TENSOR
REMARK 3 T11: 0.3677 T22: 0.2892
REMARK 3 T33: 0.3913 T12: 0.0373
REMARK 3 T13: 0.0612 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.3306 L22: 0.6013
REMARK 3 L33: 1.0701 L12: 0.3153
REMARK 3 L13: -0.0748 L23: 0.4829
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: -0.1135 S13: 0.1491
REMARK 3 S21: 0.1518 S22: -0.1367 S23: 0.1454
REMARK 3 S31: 0.0448 S32: 0.0139 S33: 0.1392
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 265 THROUGH 388 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1695 129.5775 57.7057
REMARK 3 T TENSOR
REMARK 3 T11: 0.5783 T22: 0.3825
REMARK 3 T33: 0.5025 T12: -0.0419
REMARK 3 T13: 0.1241 T23: -0.0724
REMARK 3 L TENSOR
REMARK 3 L11: 1.4975 L22: 0.6489
REMARK 3 L33: 0.8625 L12: -0.0621
REMARK 3 L13: 0.1635 L23: 0.0870
REMARK 3 S TENSOR
REMARK 3 S11: -0.1953 S12: 0.1948 S13: -0.1796
REMARK 3 S21: -0.1096 S22: 0.0604 S23: 0.0062
REMARK 3 S31: 0.1285 S32: -0.0921 S33: 0.1040
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 389 THROUGH 456 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7888 125.4045 53.6116
REMARK 3 T TENSOR
REMARK 3 T11: 0.6325 T22: 0.4003
REMARK 3 T33: 0.6205 T12: 0.0952
REMARK 3 T13: 0.1606 T23: -0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 2.8307 L22: 0.4265
REMARK 3 L33: 2.1597 L12: 0.3360
REMARK 3 L13: -0.5018 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.4387 S12: -0.0254 S13: -0.4596
REMARK 3 S21: 0.1254 S22: 0.1805 S23: -0.3470
REMARK 3 S31: 0.4202 S32: 0.1422 S33: 0.1441
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 457 THROUGH 503 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9758 140.7495 47.0080
REMARK 3 T TENSOR
REMARK 3 T11: 0.4216 T22: 0.5297
REMARK 3 T33: 0.4495 T12: 0.0164
REMARK 3 T13: 0.0759 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.0748 L22: 1.0398
REMARK 3 L33: 2.9754 L12: 0.9529
REMARK 3 L13: 0.1721 L23: 0.4317
REMARK 3 S TENSOR
REMARK 3 S11: -0.1397 S12: 0.4644 S13: -0.3191
REMARK 3 S21: -0.1070 S22: 0.2046 S23: -0.0100
REMARK 3 S31: -0.0833 S32: 0.5573 S33: -0.0058
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 504 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1014 139.0198 79.9423
REMARK 3 T TENSOR
REMARK 3 T11: 0.3749 T22: 0.4444
REMARK 3 T33: 0.4387 T12: 0.0989
REMARK 3 T13: 0.0475 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.7796 L22: 0.9709
REMARK 3 L33: 1.0516 L12: 0.3765
REMARK 3 L13: 0.0098 L23: -0.2207
REMARK 3 S TENSOR
REMARK 3 S11: -0.0150 S12: -0.0720 S13: -0.2517
REMARK 3 S21: 0.0801 S22: -0.0890 S23: -0.1323
REMARK 3 S31: 0.1306 S32: 0.3305 S33: 0.1068
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 698 THROUGH 767 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2462 155.7598 83.3871
REMARK 3 T TENSOR
REMARK 3 T11: 0.4301 T22: 0.3977
REMARK 3 T33: 0.4425 T12: 0.0332
REMARK 3 T13: 0.0377 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 1.8034 L22: 1.5788
REMARK 3 L33: 1.9946 L12: -0.2116
REMARK 3 L13: -0.7275 L23: -0.5594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: -0.0994 S13: 0.0242
REMARK 3 S21: 0.0245 S22: 0.1036 S23: -0.1495
REMARK 3 S31: 0.0034 S32: 0.3738 S33: -0.0874
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 390 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.1544 140.7744 131.7949
REMARK 3 T TENSOR
REMARK 3 T11: 0.6913 T22: 1.9649
REMARK 3 T33: 1.1318 T12: -0.2390
REMARK 3 T13: -0.0597 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 2.5714 L22: 2.3066
REMARK 3 L33: 0.3855 L12: -2.1963
REMARK 3 L13: -0.7659 L23: 0.3894
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.2544 S13: -0.3123
REMARK 3 S21: 0.3032 S22: -0.0459 S23: -1.3103
REMARK 3 S31: -0.5304 S32: 1.3423 S33: 0.0309
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 105.1873 142.1002 118.0066
REMARK 3 T TENSOR
REMARK 3 T11: 0.7966 T22: 2.2051
REMARK 3 T33: 1.0933 T12: -0.0846
REMARK 3 T13: 0.2345 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 9.3331 L22: 1.6434
REMARK 3 L33: 2.5671 L12: -3.9087
REMARK 3 L13: 3.4093 L23: -1.3244
REMARK 3 S TENSOR
REMARK 3 S11: 0.3429 S12: -0.6493 S13: -0.6531
REMARK 3 S21: 0.0068 S22: 0.1988 S23: 0.1943
REMARK 3 S31: -0.0084 S32: 1.1530 S33: -0.5642
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 439 THROUGH 448 )
REMARK 3 ORIGIN FOR THE GROUP (A): 109.5405 152.9733 126.1572
REMARK 3 T TENSOR
REMARK 3 T11: 1.0070 T22: 1.9119
REMARK 3 T33: 1.5124 T12: -0.5315
REMARK 3 T13: -0.2084 T23: -0.2986
REMARK 3 L TENSOR
REMARK 3 L11: 0.0584 L22: 1.3870
REMARK 3 L33: 0.1782 L12: 0.1955
REMARK 3 L13: -0.1019 L23: -0.3149
REMARK 3 S TENSOR
REMARK 3 S11: 0.5176 S12: -0.2919 S13: 0.5714
REMARK 3 S21: 0.7226 S22: -0.6035 S23: -1.1203
REMARK 3 S31: -0.3091 S32: 0.6003 S33: -0.0300
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 449 THROUGH 492 )
REMARK 3 ORIGIN FOR THE GROUP (A): 93.1696 141.6539 119.2341
REMARK 3 T TENSOR
REMARK 3 T11: 0.6721 T22: 1.1467
REMARK 3 T33: 0.6629 T12: -0.1966
REMARK 3 T13: 0.1012 T23: -0.0953
REMARK 3 L TENSOR
REMARK 3 L11: 5.1249 L22: 4.0087
REMARK 3 L33: 4.5651 L12: -1.0317
REMARK 3 L13: 0.1433 L23: -0.7613
REMARK 3 S TENSOR
REMARK 3 S11: -0.3037 S12: -0.0117 S13: 0.0560
REMARK 3 S21: -0.2324 S22: 0.0448 S23: -0.9201
REMARK 3 S31: -0.4190 S32: 1.8366 S33: 0.1575
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 493 THROUGH 503 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.4574 125.3704 128.0288
REMARK 3 T TENSOR
REMARK 3 T11: 1.0478 T22: 1.5787
REMARK 3 T33: 1.1762 T12: 0.0984
REMARK 3 T13: -0.0849 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 1.7596
REMARK 3 L33: 0.9805 L12: 0.5054
REMARK 3 L13: -0.2144 L23: 0.5754
REMARK 3 S TENSOR
REMARK 3 S11: -0.1847 S12: -0.4862 S13: -1.0311
REMARK 3 S21: 0.3841 S22: 0.2042 S23: -1.3380
REMARK 3 S31: 0.4981 S32: 1.9770 S33: -0.0608
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 504 THROUGH 569 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.1980 137.8489 126.7693
REMARK 3 T TENSOR
REMARK 3 T11: 0.4265 T22: 0.5103
REMARK 3 T33: 0.4393 T12: -0.0889
REMARK 3 T13: 0.0007 T23: 0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 5.6285 L22: 4.3595
REMARK 3 L33: 3.8416 L12: -0.2444
REMARK 3 L13: -0.1443 L23: 1.8183
REMARK 3 S TENSOR
REMARK 3 S11: -0.1673 S12: -0.4441 S13: -0.0947
REMARK 3 S21: 0.1318 S22: 0.2046 S23: -0.0161
REMARK 3 S31: -0.2518 S32: 0.5948 S33: -0.0572
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 570 THROUGH 590 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.3357 142.9410 125.1741
REMARK 3 T TENSOR
REMARK 3 T11: 0.7871 T22: 1.7402
REMARK 3 T33: 1.0325 T12: 0.0815
REMARK 3 T13: 0.1025 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.2353 L22: 1.9812
REMARK 3 L33: 3.0611 L12: 2.2139
REMARK 3 L13: -0.0090 L23: -0.1046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: 0.5486 S13: -0.2029
REMARK 3 S21: -0.0088 S22: 0.9514 S23: -0.5991
REMARK 3 S31: -0.5685 S32: 0.6347 S33: -1.0823
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 8ZE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1300047545.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 30, 2023
REMARK 200 DATA SCALING SOFTWARE : XDS JUN 30, 2023
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66775
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM TARTRATE DIBASIC (PH
REMARK 280 7.0) AND 12% (WT/VOL) PEG 3350., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
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 60.72000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, E, F, 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 APPLY THE FOLLOWING TO CHAINS: C, D, H, I, J
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 38.78406
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -60.72000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 213.57868
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 ARG B 40
REMARK 465 GLU B 767
REMARK 465 THR C 589
REMARK 465 ASN C 590
REMARK 465 ASP A 388
REMARK 465 LYS A 389
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU D 97 CG CD OE1 OE2
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 ND2 ASN B 92 O5 NAG B 802 2.06
REMARK 500 O LYS D 123 OG SER D 127 2.09
REMARK 500 O LYS B 123 OG SER B 127 2.13
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 SER B 64 -168.33 -162.35
REMARK 500 HIS B 66 17.57 -142.40
REMARK 500 ASP B 96 16.45 57.26
REMARK 500 TRP B 124 -161.87 57.43
REMARK 500 GLU B 146 71.39 58.24
REMARK 500 HIS B 162 35.58 -144.60
REMARK 500 VAL B 193 -65.81 -131.83
REMARK 500 ASP B 200 -152.89 -88.85
REMARK 500 VAL B 207 -61.22 -100.22
REMARK 500 ALA B 213 43.29 -142.82
REMARK 500 ASP B 230 49.13 -107.39
REMARK 500 SER B 242 -152.64 59.76
REMARK 500 PHE B 357 -50.71 -131.19
REMARK 500 VAL B 401 43.85 -87.26
REMARK 500 THR B 411 -164.97 -110.47
REMARK 500 LYS B 423 14.38 56.71
REMARK 500 ASN B 450 76.82 -151.77
REMARK 500 SER B 486 -71.70 -66.39
REMARK 500 TYR B 547 -60.86 -126.81
REMARK 500 THR B 557 55.06 -118.92
REMARK 500 ASN B 562 -157.30 -123.43
REMARK 500 ARG B 596 17.66 56.42
REMARK 500 ARG B 597 53.32 -143.39
REMARK 500 LEU B 601 -57.32 64.45
REMARK 500 ASN B 615 0.86 -68.54
REMARK 500 SER B 630 -112.63 57.65
REMARK 500 ASP B 678 -102.16 -127.59
REMARK 500 SER B 686 50.28 -95.36
REMARK 500 ASN B 710 -76.71 -98.92
REMARK 500 ASP B 739 -161.95 -77.81
REMARK 500 LYS C 389 -158.52 -88.85
REMARK 500 PHE C 431 69.11 -156.07
REMARK 500 ALA C 440 3.86 -69.15
REMARK 500 ASN C 476 -76.05 -141.65
REMARK 500 THR C 497 35.32 -91.52
REMARK 500 CYS C 510 79.41 -152.52
REMARK 500 GLU C 557 35.72 -87.79
REMARK 500 SER D 64 -157.41 -157.33
REMARK 500 PRO D 109 12.28 -68.74
REMARK 500 TRP D 124 -164.25 61.76
REMARK 500 GLU D 146 83.41 56.50
REMARK 500 HIS D 162 32.46 -141.02
REMARK 500 VAL D 193 -63.17 -128.32
REMARK 500 ASP D 230 46.14 -108.06
REMARK 500 SER D 242 -156.51 59.24
REMARK 500 PRO D 255 99.55 -59.37
REMARK 500 LYS D 423 17.62 59.27
REMARK 500 ASN D 450 85.64 -151.28
REMARK 500 TYR D 547 -50.36 -120.36
REMARK 500 THR D 557 52.61 -98.52
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8ZE6 B 40 767 PDB 8ZE6 8ZE6 40 767
DBREF1 8ZE6 C 388 590 UNP A0AAE8ZFM2_9BETC
DBREF2 8ZE6 C A0AAE8ZFM2 388 590
DBREF 8ZE6 D 40 767 PDB 8ZE6 8ZE6 40 767
DBREF1 8ZE6 A 388 590 UNP A0AAE8ZFM2_9BETC
DBREF2 8ZE6 A A0AAE8ZFM2 388 590
SEQADV 8ZE6 ASP C 388 UNP A0AAE8ZFM SER 388 CONFLICT
SEQADV 8ZE6 ALA C 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 8ZE6 GLU C 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQADV 8ZE6 ASP A 388 UNP A0AAE8ZFM SER 388 CONFLICT
SEQADV 8ZE6 ALA A 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 8ZE6 GLU A 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQRES 1 B 728 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 B 728 PHE ARG VAL LYS PHE TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 B 728 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 B 728 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 B 728 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 B 728 TYR SER VAL SER PRO ASP GLY GLN PHE ILE LEU PHE GLU
SEQRES 7 B 728 TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 728 SER TYR ASP ILE TYR ASP LEU HIS LYS ARG GLN LEU ILE
SEQRES 9 B 728 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 B 728 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP HIS
SEQRES 11 B 728 ASN ASP ILE TYR ILE LYS LYS GLU PRO ASN LEU GLN SER
SEQRES 12 B 728 GLN ARG ILE THR TRP THR GLY LYS GLU ASP VAL ILE TYR
SEQRES 13 B 728 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 B 728 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 728 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 B 728 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 728 TYR PRO LYS THR MET GLN VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 B 728 ALA ALA ASN PRO THR VAL LYS LEU PHE VAL VAL ASN THR
SEQRES 19 B 728 ASP SER LEU ASN SER THR ALA ASN ALA THR SER VAL GLN
SEQRES 20 B 728 VAL VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 21 B 728 LEU CYS ASP VAL THR TRP VAL ASN GLU GLU ARG ILE SER
SEQRES 22 B 728 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL LEU
SEQRES 23 B 728 ALA ILE CYS ASP TYR ASP LYS PRO THR GLY ARG TRP ALA
SEQRES 24 B 728 SER HIS VAL ARG GLN GLN HIS ILE GLU SER SER THR THR
SEQRES 25 B 728 GLY TRP VAL GLY ARG PHE LYS PRO SER GLU PRO HIS PHE
SEQRES 26 B 728 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 B 728 LYS GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN VAL ASP
SEQRES 28 B 728 ARG GLU ASN CYS THR PHE ILE THR LYS GLY VAL TRP GLU
SEQRES 29 B 728 VAL ILE GLY ILE GLU ALA LEU THR SER ASP ASP LEU TYR
SEQRES 30 B 728 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 B 728 ASN LEU TYR LYS ILE GLN LEU ASN ASP HIS THR LYS VAL
SEQRES 32 B 728 THR CYS LEU SER CYS GLU LEU ASN THR GLU ARG CYS GLN
SEQRES 33 B 728 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 B 728 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 B 728 LEU HIS SER SER SER ASN ASP LYS GLU LEU ARG VAL LEU
SEQRES 36 B 728 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 37 B 728 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE TRP ASN
SEQRES 38 B 728 GLY ILE LYS LEU TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 B 728 PHE ASP LYS LEU LYS LYS TYR PRO LEU LEU ILE ASP VAL
SEQRES 40 B 728 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 B 728 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU LYS
SEQRES 42 B 728 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 B 728 GLN GLY ASP LYS ILE LEU HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 B 728 GLY THR LEU GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 B 728 GLN PHE THR ASN MET GLY PHE VAL ASP GLU LYS ARG ILE
SEQRES 46 B 728 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 B 728 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 B 728 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 B 728 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 B 728 GLU ASP ASN LEU GLU HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 B 728 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 B 728 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 B 728 SER ALA GLN ILE SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 54 B 728 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 B 728 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 B 728 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLU
SEQRES 1 C 203 ASP LYS GLU CYS ASP PHE THR PRO MET LEU VAL GLY VAL
SEQRES 2 C 203 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 3 C 203 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 4 C 203 MET VAL ASN GLU PHE SER CYS ASN GLY ILE SER PRO ASP
SEQRES 5 C 203 ALA ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP
SEQRES 6 C 203 TYR PHE ALA TYR PRO LEU SER MET ARG SER TYR ILE GLN
SEQRES 7 C 203 PRO GLY SER ALA GLY ASP ILE SER LEU TYR ASN TYR LYS
SEQRES 8 C 203 GLN SER PHE ALA ASN PRO THR CYS ARG VAL LEU ALA THR
SEQRES 9 C 203 ALA PRO ALA ASN LEU THR LEU THR LYS PRO SER ALA TYR
SEQRES 10 C 203 GLY TYR PHE GLN LYS CYS SER ARG VAL SER GLY GLU HIS
SEQRES 11 C 203 ASN SER VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU
SEQRES 12 C 203 TYR SER ILE CYS ARG SER PHE SER PRO TYR GLY PHE SER
SEQRES 13 C 203 GLU ASP GLY GLU VAL PHE ARG ARG GLN LEU THR GLN TYR
SEQRES 14 C 203 GLU GLY GLY GLY ILE LEU VAL GLY VAL GLY ALA LYS LEU
SEQRES 15 C 203 ALA MET THR ASP LYS LEU GLU MET GLY PHE ILE ILE SER
SEQRES 16 C 203 VAL GLN TYR GLY THR ASP THR ASN
SEQRES 1 D 728 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 D 728 PHE ARG VAL LYS PHE TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 D 728 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 D 728 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 D 728 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 D 728 TYR SER VAL SER PRO ASP GLY GLN PHE ILE LEU PHE GLU
SEQRES 7 D 728 TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR ALA
SEQRES 8 D 728 SER TYR ASP ILE TYR ASP LEU HIS LYS ARG GLN LEU ILE
SEQRES 9 D 728 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 D 728 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP HIS
SEQRES 11 D 728 ASN ASP ILE TYR ILE LYS LYS GLU PRO ASN LEU GLN SER
SEQRES 12 D 728 GLN ARG ILE THR TRP THR GLY LYS GLU ASP VAL ILE TYR
SEQRES 13 D 728 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 D 728 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 D 728 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 D 728 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 D 728 TYR PRO LYS THR MET GLN VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 D 728 ALA ALA ASN PRO THR VAL LYS LEU PHE VAL VAL ASN THR
SEQRES 19 D 728 ASP SER LEU ASN SER THR ALA ASN ALA THR SER VAL GLN
SEQRES 20 D 728 VAL VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 21 D 728 LEU CYS ASP VAL THR TRP VAL ASN GLU GLU ARG ILE SER
SEQRES 22 D 728 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL LEU
SEQRES 23 D 728 ALA ILE CYS ASP TYR ASP LYS PRO THR GLY ARG TRP ALA
SEQRES 24 D 728 SER HIS VAL ARG GLN GLN HIS ILE GLU SER SER THR THR
SEQRES 25 D 728 GLY TRP VAL GLY ARG PHE LYS PRO SER GLU PRO HIS PHE
SEQRES 26 D 728 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 D 728 LYS GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN VAL ASP
SEQRES 28 D 728 ARG GLU ASN CYS THR PHE ILE THR LYS GLY VAL TRP GLU
SEQRES 29 D 728 VAL ILE GLY ILE GLU ALA LEU THR SER ASP ASP LEU TYR
SEQRES 30 D 728 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 D 728 ASN LEU TYR LYS ILE GLN LEU ASN ASP HIS THR LYS VAL
SEQRES 32 D 728 THR CYS LEU SER CYS GLU LEU ASN THR GLU ARG CYS GLN
SEQRES 33 D 728 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 D 728 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 D 728 LEU HIS SER SER SER ASN ASP LYS GLU LEU ARG VAL LEU
SEQRES 36 D 728 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 37 D 728 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE TRP ASN
SEQRES 38 D 728 GLY ILE LYS LEU TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 D 728 PHE ASP LYS LEU LYS LYS TYR PRO LEU LEU ILE ASP VAL
SEQRES 40 D 728 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 D 728 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU LYS
SEQRES 42 D 728 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 D 728 GLN GLY ASP LYS ILE LEU HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 D 728 GLY THR LEU GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 D 728 GLN PHE THR ASN MET GLY PHE VAL ASP GLU LYS ARG ILE
SEQRES 46 D 728 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 D 728 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 D 728 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 D 728 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 D 728 GLU ASP ASN LEU GLU HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 D 728 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 D 728 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 D 728 SER ALA GLN ILE SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 54 D 728 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 D 728 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 D 728 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLU
SEQRES 1 A 203 ASP LYS GLU CYS ASP PHE THR PRO MET LEU VAL GLY VAL
SEQRES 2 A 203 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 3 A 203 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 4 A 203 MET VAL ASN GLU PHE SER CYS ASN GLY ILE SER PRO ASP
SEQRES 5 A 203 ALA ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP
SEQRES 6 A 203 TYR PHE ALA TYR PRO LEU SER MET ARG SER TYR ILE GLN
SEQRES 7 A 203 PRO GLY SER ALA GLY ASP ILE SER LEU TYR ASN TYR LYS
SEQRES 8 A 203 GLN SER PHE ALA ASN PRO THR CYS ARG VAL LEU ALA THR
SEQRES 9 A 203 ALA PRO ALA ASN LEU THR LEU THR LYS PRO SER ALA TYR
SEQRES 10 A 203 GLY TYR PHE GLN LYS CYS SER ARG VAL SER GLY GLU HIS
SEQRES 11 A 203 ASN SER VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU
SEQRES 12 A 203 TYR SER ILE CYS ARG SER PHE SER PRO TYR GLY PHE SER
SEQRES 13 A 203 GLU ASP GLY GLU VAL PHE ARG ARG GLN LEU THR GLN TYR
SEQRES 14 A 203 GLU GLY GLY GLY ILE LEU VAL GLY VAL GLY ALA LYS LEU
SEQRES 15 A 203 ALA MET THR ASP LYS LEU GLU MET GLY PHE ILE ILE SER
SEQRES 16 A 203 VAL GLN TYR GLY THR ASP THR ASN
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG B 801 14
HET NAG B 802 14
HET GOL B 803 6
HET NAG D 801 14
HET NAG D 802 14
HET NAG D 803 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAG 17(C8 H15 N O6)
FORMUL 13 GOL C3 H8 O3
FORMUL 17 HOH *157(H2 O)
HELIX 1 AA1 THR B 44 LYS B 50 1 7
HELIX 2 AA2 ASP B 200 GLU B 206 1 7
HELIX 3 AA3 GLU B 421 MET B 425 5 5
HELIX 4 AA4 LYS B 463 LYS B 466 5 4
HELIX 5 AA5 ASN B 497 LEU B 504 1 8
HELIX 6 AA6 ASN B 562 THR B 570 1 9
HELIX 7 AA7 GLY B 587 HIS B 592 1 6
HELIX 8 AA8 ALA B 593 ASN B 595 5 3
HELIX 9 AA9 LEU B 601 ASN B 615 1 15
HELIX 10 AB1 SER B 630 GLY B 641 1 12
HELIX 11 AB2 ARG B 658 TYR B 662 5 5
HELIX 12 AB3 ASP B 663 GLY B 672 1 10
HELIX 13 AB4 ASN B 679 SER B 686 1 8
HELIX 14 AB5 VAL B 688 VAL B 698 5 11
HELIX 15 AB6 HIS B 712 ALA B 726 1 15
HELIX 16 AB7 SER B 744 SER B 764 1 21
HELIX 17 AB8 PHE C 393 LEU C 397 5 5
HELIX 18 AB9 ASN C 418 PHE C 426 1 9
HELIX 19 AC1 PRO C 457 ILE C 464 5 8
HELIX 20 AC2 GLY C 470 ASN C 476 1 7
HELIX 21 AC3 GLY C 515 SER C 519 5 5
HELIX 22 AC4 SER C 532 PHE C 537 5 6
HELIX 23 AC5 THR D 44 LYS D 50 1 7
HELIX 24 AC6 GLU D 91 ASP D 96 1 6
HELIX 25 AC7 ASP D 200 GLU D 206 1 7
HELIX 26 AC8 ASP D 274 LEU D 276 5 3
HELIX 27 AC9 PRO D 290 LEU D 294 5 5
HELIX 28 AD1 GLU D 421 MET D 425 5 5
HELIX 29 AD2 LYS D 463 ALA D 465 5 3
HELIX 30 AD3 ASN D 497 LEU D 504 1 8
HELIX 31 AD4 ASN D 562 THR D 570 1 9
HELIX 32 AD5 GLY D 587 HIS D 592 1 6
HELIX 33 AD6 ALA D 593 ASN D 595 5 3
HELIX 34 AD7 THR D 600 ASN D 615 1 16
HELIX 35 AD8 SER D 630 GLY D 641 1 12
HELIX 36 AD9 ASP D 663 GLY D 672 1 10
HELIX 37 AE1 ASN D 679 SER D 686 1 8
HELIX 38 AE2 VAL D 688 VAL D 698 5 11
HELIX 39 AE3 HIS D 712 ALA D 726 1 15
HELIX 40 AE4 SER D 744 PHE D 763 1 20
HELIX 41 AE5 PHE A 393 VAL A 398 5 6
HELIX 42 AE6 GLN A 403 PHE A 407 5 5
HELIX 43 AE7 LEU A 422 PHE A 426 5 5
HELIX 44 AE8 PRO A 438 ARG A 443 5 6
HELIX 45 AE9 PRO A 457 ILE A 464 5 8
HELIX 46 AF1 GLY A 470 ASN A 476 1 7
HELIX 47 AF2 GLY A 515 SER A 519 5 5
HELIX 48 AF3 SER A 532 SER A 536 5 5
HELIX 49 AF4 THR A 554 GLY A 558 5 5
SHEET 1 AA1 4 LEU B 60 TRP B 62 0
SHEET 2 AA1 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 AA1 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 AA1 4 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 AA2 3 ASP B 104 VAL B 107 0
SHEET 2 AA2 3 PHE B 113 LYS B 123 -1 O GLU B 117 N ASP B 104
SHEET 3 AA2 3 SER B 127 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 1 AA3 4 TRP B 154 TRP B 157 0
SHEET 2 AA3 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 AA3 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AA3 4 GLN B 183 ARG B 184 -1 O GLN B 183 N ILE B 174
SHEET 1 AA4 3 ILE B 194 ASN B 196 0
SHEET 2 AA4 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AA4 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AA5 4 ILE B 194 ASN B 196 0
SHEET 2 AA5 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AA5 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AA5 4 SER B 284 GLN B 286 -1 O VAL B 285 N VAL B 270
SHEET 1 AA6 2 LEU B 235 PHE B 240 0
SHEET 2 AA6 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AA7 4 HIS B 298 ASN B 307 0
SHEET 2 AA7 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AA7 4 TYR B 322 TYR B 330 -1 O ALA B 326 N LEU B 313
SHEET 4 AA7 4 TRP B 337 SER B 348 -1 O HIS B 345 N LEU B 325
SHEET 1 AA8 4 HIS B 363 PHE B 364 0
SHEET 2 AA8 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AA8 4 LYS B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 AA8 4 CYS B 394 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 AA9 4 VAL B 404 LEU B 410 0
SHEET 2 AA9 4 ASP B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 AA9 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AA9 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AB1 4 TYR B 457 PHE B 461 0
SHEET 2 AB1 4 TYR B 468 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 AB1 4 TYR B 480 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 AB1 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AB2 8 LYS B 513 TRP B 519 0
SHEET 2 AB2 8 ILE B 522 ILE B 529 -1 O LEU B 524 N ILE B 517
SHEET 3 AB2 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 AB2 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AB2 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 AB2 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AB2 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 AB2 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AB3 2 LYS C 389 GLU C 390 0
SHEET 2 AB3 2 CYS C 415 ASN C 416 1 O ASN C 416 N LYS C 389
SHEET 1 AB4 3 LYS C 408 PHE C 412 0
SHEET 2 AB4 3 LEU C 449 ALA C 455 -1 O VAL C 451 N LEU C 410
SHEET 3 AB4 3 LEU C 575 VAL C 583 -1 O ILE C 580 N ASP C 452
SHEET 1 AB5 2 MET C 427 ASN C 434 0
SHEET 2 AB5 2 THR C 485 ALA C 492 -1 O LEU C 489 N ASN C 429
SHEET 1 AB6 4 VAL C 520 PRO C 523 0
SHEET 2 AB6 4 TYR C 504 SER C 514 -1 N SER C 514 O VAL C 520
SHEET 3 AB6 4 ILE C 561 LEU C 569 -1 O ALA C 567 N TYR C 506
SHEET 4 AB6 4 VAL C 548 GLN C 552 -1 N ARG C 551 O LEU C 562
SHEET 1 AB7 4 ARG D 61 TRP D 62 0
SHEET 2 AB7 4 GLU D 67 GLN D 72 -1 O LEU D 69 N ARG D 61
SHEET 3 AB7 4 ASN D 75 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AB7 4 SER D 86 LEU D 90 -1 O SER D 87 N LEU D 78
SHEET 1 AB8 4 ASP D 104 VAL D 107 0
SHEET 2 AB8 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AB8 4 TYR D 128 ASP D 136 -1 O TYR D 135 N ILE D 114
SHEET 4 AB8 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AB9 4 ASP D 104 VAL D 107 0
SHEET 2 AB9 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AB9 4 TYR D 128 ASP D 136 -1 O TYR D 135 N ILE D 114
SHEET 4 AB9 4 ILE D 148 THR D 152 -1 O THR D 152 N ALA D 130
SHEET 1 AC1 4 TRP D 154 TRP D 157 0
SHEET 2 AC1 4 LEU D 164 VAL D 167 -1 O VAL D 167 N TRP D 154
SHEET 3 AC1 4 ILE D 172 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AC1 4 GLN D 183 ARG D 184 -1 O GLN D 183 N ILE D 174
SHEET 1 AC2 3 ILE D 194 ASN D 196 0
SHEET 2 AC2 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AC2 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AC3 4 ILE D 194 ASN D 196 0
SHEET 2 AC3 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AC3 4 THR D 265 ASN D 272 -1 O LYS D 267 N GLN D 227
SHEET 4 AC3 4 SER D 284 GLN D 286 -1 O VAL D 285 N VAL D 270
SHEET 1 AC4 2 LEU D 235 PHE D 240 0
SHEET 2 AC4 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AC5 4 HIS D 298 ASN D 307 0
SHEET 2 AC5 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AC5 4 TYR D 322 TYR D 330 -1 O ALA D 326 N LEU D 313
SHEET 4 AC5 4 TRP D 337 SER D 348 -1 O ALA D 338 N ASP D 329
SHEET 1 AC6 4 HIS D 363 PHE D 364 0
SHEET 2 AC6 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AC6 4 LYS D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 AC6 4 CYS D 394 PHE D 396 -1 O THR D 395 N HIS D 386
SHEET 1 AC7 4 VAL D 404 LEU D 410 0
SHEET 2 AC7 4 ASP D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AC7 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AC7 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AC8 4 CYS D 454 PHE D 461 0
SHEET 2 AC8 4 TYR D 467 PRO D 475 -1 O GLY D 474 N GLN D 455
SHEET 3 AC8 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 AC8 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AC9 8 SER D 511 ILE D 518 0
SHEET 2 AC9 8 LYS D 523 LEU D 530 -1 O MET D 528 N LYS D 513
SHEET 3 AC9 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AC9 8 TYR D 540 VAL D 546 1 N ASP D 545 O ALA D 576
SHEET 5 AC9 8 VAL D 619 TRP D 629 1 O ASP D 620 N TYR D 540
SHEET 6 AC9 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AC9 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AC9 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SHEET 1 AD1 5 LYS A 408 PHE A 412 0
SHEET 2 AD1 5 LEU A 449 ALA A 455 -1 O VAL A 451 N LEU A 410
SHEET 3 AD1 5 GLU A 576 VAL A 583 -1 O SER A 582 N THR A 450
SHEET 4 AD1 5 THR A 485 THR A 491 -1 N VAL A 488 O PHE A 579
SHEET 5 AD1 5 MET A 427 GLU A 430 -1 N GLU A 430 O LEU A 489
SHEET 1 AD2 5 LYS A 408 PHE A 412 0
SHEET 2 AD2 5 LEU A 449 ALA A 455 -1 O VAL A 451 N LEU A 410
SHEET 3 AD2 5 GLU A 576 VAL A 583 -1 O SER A 582 N THR A 450
SHEET 4 AD2 5 THR A 485 THR A 491 -1 N VAL A 488 O PHE A 579
SHEET 5 AD2 5 CYS A 433 ASN A 434 -1 N ASN A 434 O THR A 485
SHEET 1 AD3 4 VAL A 520 PRO A 523 0
SHEET 2 AD3 4 TYR A 504 SER A 514 -1 N ARG A 512 O THR A 522
SHEET 3 AD3 4 ILE A 561 LEU A 569 -1 O VAL A 563 N SER A 511
SHEET 4 AD3 4 VAL A 548 GLN A 552 -1 N ARG A 551 O LEU A 562
SSBOND 1 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 2 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 3 CYS B 649 CYS B 762 1555 1555 2.03
SSBOND 4 CYS C 391 CYS C 415 1555 1555 2.03
SSBOND 5 CYS C 433 CYS C 486 1555 1555 2.03
SSBOND 6 CYS C 510 CYS C 534 1555 1555 2.03
SSBOND 7 CYS D 385 CYS D 394 1555 1555 2.03
SSBOND 8 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 9 CYS D 454 CYS D 472 1555 1555 2.03
SSBOND 10 CYS D 649 CYS D 762 1555 1555 2.03
SSBOND 11 CYS A 391 CYS A 415 1555 1555 2.03
SSBOND 12 CYS A 433 CYS A 486 1555 1555 2.03
SSBOND 13 CYS A 510 CYS A 534 1555 1555 2.03
LINK ND2 ASN B 85 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 92 C1 NAG B 802 1555 1555 1.42
LINK ND2 ASN B 229 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG G 1 1555 1555 1.46
LINK ND2 ASN D 85 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN D 92 C1 NAG D 801 1555 1555 1.44
LINK ND2 ASN D 150 C1 NAG D 802 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN D 281 C1 NAG D 803 1555 1555 1.44
LINK ND2 ASN D 321 C1 NAG J 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.42
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.43
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
CISPEP 1 GLY B 474 PRO B 475 0 2.40
CISPEP 2 GLY D 474 PRO D 475 0 2.70
CRYST1 96.532 121.440 110.624 90.00 105.13 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010359 0.000000 0.002801 0.00000
SCALE2 0.000000 0.008235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009364 0.00000
TER 5945 PRO B 766
TER 7510 ASP C 588
TER 13471 GLU D 767
TER 15034 ASN A 590
MASTER 718 0 18 49 118 0 0 615431 4 281 144
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