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HEADER HYDROLASE 05-MAY-20 6WV1
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH GB AND HI-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS NERVE AGENT, ACETYLCHOLINESTERASE, TABUN, GA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.MCGUIRE,S.M.BESTER,S.D.PEGAN,J.J.HEIGHT
REVDAT 1 17-FEB-21 6WV1 0
JRNL AUTH J.R.MCGUIRE,S.M.BESTER,M.A.GUELTA,J.CHEUNG,C.LANGLEY,
JRNL AUTH 2 M.D.WINEMILLER,S.Y.BAE,V.FUNK,J.M.MYSLINSKI,S.D.PEGAN,
JRNL AUTH 3 J.J.HEIGHT
JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO THE INHIBITION OF
JRNL TITL 2 HUMAN ACETYLCHOLINESTERASE BY G-SERIES NERVE AGENTS AND
JRNL TITL 3 SUBSEQUENT REACTIVATION BY HI-6.
JRNL REF CHEM.RES.TOXICOL. 2021
JRNL REFN ISSN 0893-228X
JRNL PMID 33538594
JRNL DOI 10.1021/ACS.CHEMRESTOX.0C00406
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1-3660
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) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 83046
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4141
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 37.0150 - 7.3519 0.95 2737 153 0.1794 0.1899
REMARK 3 2 7.3519 - 5.8429 0.98 2695 144 0.1815 0.2106
REMARK 3 3 5.8429 - 5.1065 0.99 2672 170 0.1652 0.2067
REMARK 3 4 5.1065 - 4.6405 1.00 2688 130 0.1397 0.1383
REMARK 3 5 4.6405 - 4.3085 0.99 2657 135 0.1296 0.1552
REMARK 3 6 4.3085 - 4.0548 0.99 2650 154 0.1404 0.1822
REMARK 3 7 4.0548 - 3.8519 0.99 2643 132 0.1413 0.1770
REMARK 3 8 3.8519 - 3.6844 0.99 2681 124 0.1482 0.1607
REMARK 3 9 3.6844 - 3.5427 1.00 2633 121 0.1574 0.1890
REMARK 3 10 3.5427 - 3.4205 0.99 2656 137 0.1642 0.2120
REMARK 3 11 3.4205 - 3.3136 1.00 2638 150 0.1675 0.1960
REMARK 3 12 3.3136 - 3.2190 1.00 2587 157 0.1734 0.2093
REMARK 3 13 3.2190 - 3.1343 1.00 2624 145 0.1805 0.2267
REMARK 3 14 3.1343 - 3.0578 1.00 2590 137 0.1701 0.1894
REMARK 3 15 3.0578 - 2.9884 1.00 2633 136 0.1653 0.2042
REMARK 3 16 2.9884 - 2.9248 1.00 2667 139 0.1672 0.2078
REMARK 3 17 2.9248 - 2.8663 1.00 2640 105 0.1748 0.1951
REMARK 3 18 2.8663 - 2.8122 1.00 2626 118 0.1824 0.2175
REMARK 3 19 2.8122 - 2.7620 1.00 2582 163 0.1799 0.2492
REMARK 3 20 2.7620 - 2.7152 1.00 2668 154 0.1826 0.2255
REMARK 3 21 2.7152 - 2.6714 1.00 2545 117 0.1913 0.2228
REMARK 3 22 2.6714 - 2.6304 1.00 2643 158 0.1917 0.2322
REMARK 3 23 2.6304 - 2.5917 1.00 2608 126 0.1900 0.2625
REMARK 3 24 2.5917 - 2.5552 1.00 2567 156 0.1928 0.2440
REMARK 3 25 2.5552 - 2.5207 1.00 2633 143 0.2029 0.2537
REMARK 3 26 2.5207 - 2.4879 1.00 2560 126 0.1996 0.2670
REMARK 3 27 2.4879 - 2.4568 1.00 2689 101 0.2083 0.2768
REMARK 3 28 2.4568 - 2.4272 1.00 2586 158 0.2156 0.2415
REMARK 3 29 2.4272 - 2.3990 1.00 2634 120 0.2180 0.2685
REMARK 3 30 2.3990 - 2.3721 0.96 2473 132 0.2272 0.2843
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.03
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 : 0.005 8851
REMARK 3 ANGLE : 0.766 12115
REMARK 3 CHIRALITY : 0.048 1298
REMARK 3 PLANARITY : 0.006 1592
REMARK 3 DIHEDRAL : 4.252 7003
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 288 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.2345 23.2066 28.3107
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.5812
REMARK 3 T33: 0.4313 T12: 0.0598
REMARK 3 T13: -0.0169 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 4.1615 L22: 3.1338
REMARK 3 L33: 3.3719 L12: 2.4002
REMARK 3 L13: 0.8426 L23: -0.4794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: 0.0960 S13: 0.0276
REMARK 3 S21: -0.3577 S22: -0.3486 S23: -0.0988
REMARK 3 S31: 0.0942 S32: 0.7833 S33: 0.2243
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 289 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 106.4092 36.6867 21.9355
REMARK 3 T TENSOR
REMARK 3 T11: 0.3162 T22: 0.5189
REMARK 3 T33: 0.3032 T12: -0.0264
REMARK 3 T13: -0.0415 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.5157 L22: 2.5785
REMARK 3 L33: 2.3492 L12: -1.4193
REMARK 3 L13: -0.6781 L23: -0.1649
REMARK 3 S TENSOR
REMARK 3 S11: 0.2075 S12: 0.2983 S13: -0.0527
REMARK 3 S21: -0.0230 S22: -0.2697 S23: -0.1600
REMARK 3 S31: -0.0461 S32: 0.1120 S33: 0.0481
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 116.6924 52.5243 11.7972
REMARK 3 T TENSOR
REMARK 3 T11: 0.4082 T22: 0.4876
REMARK 3 T33: 0.3554 T12: -0.1282
REMARK 3 T13: -0.0166 T23: 0.1267
REMARK 3 L TENSOR
REMARK 3 L11: 1.2638 L22: 1.5917
REMARK 3 L33: 3.5841 L12: 0.2400
REMARK 3 L13: 0.6959 L23: -0.2157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0400 S12: -0.0704 S13: 0.0489
REMARK 3 S21: 0.0127 S22: -0.1660 S23: -0.3820
REMARK 3 S31: -0.6328 S32: 0.6354 S33: 0.0984
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.8312 50.4828 30.7716
REMARK 3 T TENSOR
REMARK 3 T11: 0.3944 T22: 0.3285
REMARK 3 T33: 0.3266 T12: -0.0702
REMARK 3 T13: -0.0129 T23: 0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 1.7640 L22: 0.9984
REMARK 3 L33: 3.5467 L12: -0.3380
REMARK 3 L13: -1.3378 L23: -0.2699
REMARK 3 S TENSOR
REMARK 3 S11: 0.1375 S12: 0.0842 S13: 0.3436
REMARK 3 S21: 0.1616 S22: -0.1034 S23: -0.0341
REMARK 3 S31: -0.7125 S32: 0.4125 S33: -0.0339
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 91.7609 51.5437 33.0154
REMARK 3 T TENSOR
REMARK 3 T11: 0.2655 T22: 0.3197
REMARK 3 T33: 0.2892 T12: 0.0432
REMARK 3 T13: 0.0121 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.5178 L22: 2.3904
REMARK 3 L33: 5.4224 L12: -0.5583
REMARK 3 L13: 0.3698 L23: -0.0134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: 0.0949 S13: 0.2702
REMARK 3 S21: 0.0989 S22: -0.0473 S23: 0.1854
REMARK 3 S31: -0.6115 S32: -0.5977 S33: 0.0088
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.2896 48.9342 14.3672
REMARK 3 T TENSOR
REMARK 3 T11: 0.3776 T22: 0.3634
REMARK 3 T33: 0.3188 T12: 0.0256
REMARK 3 T13: -0.0270 T23: 0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 1.5032 L22: 0.2233
REMARK 3 L33: 3.9942 L12: 0.5770
REMARK 3 L13: -0.3694 L23: -0.2093
REMARK 3 S TENSOR
REMARK 3 S11: -0.1183 S12: 0.2642 S13: 0.2739
REMARK 3 S21: -0.0806 S22: 0.0347 S23: 0.0718
REMARK 3 S31: -0.3498 S32: -0.1185 S33: 0.0557
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9370 37.2131 45.6943
REMARK 3 T TENSOR
REMARK 3 T11: 0.3984 T22: 0.3792
REMARK 3 T33: 0.2743 T12: -0.0145
REMARK 3 T13: -0.0995 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 5.1031 L22: 2.3928
REMARK 3 L33: 4.0523 L12: 0.9763
REMARK 3 L13: -0.4612 L23: -0.0208
REMARK 3 S TENSOR
REMARK 3 S11: 0.1147 S12: -0.2371 S13: 0.0169
REMARK 3 S21: 0.2767 S22: 0.0339 S23: -0.3328
REMARK 3 S31: -0.6900 S32: 0.2944 S33: -0.1440
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5774 33.2408 34.2901
REMARK 3 T TENSOR
REMARK 3 T11: 0.2140 T22: 0.3606
REMARK 3 T33: 0.2417 T12: 0.0121
REMARK 3 T13: -0.0332 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.0727 L22: 1.8495
REMARK 3 L33: 3.3415 L12: 0.3357
REMARK 3 L13: 0.9294 L23: -0.0505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0839 S12: -0.0915 S13: -0.0288
REMARK 3 S21: 0.0503 S22: 0.0875 S23: -0.0360
REMARK 3 S31: -0.2665 S32: -0.0066 S33: -0.0251
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1594 17.3977 33.3145
REMARK 3 T TENSOR
REMARK 3 T11: 0.2636 T22: 0.6110
REMARK 3 T33: 0.3996 T12: -0.0594
REMARK 3 T13: -0.0265 T23: 0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 2.0514 L22: 2.4531
REMARK 3 L33: 3.2421 L12: 0.1526
REMARK 3 L13: 0.7843 L23: -0.6996
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: -0.0354 S13: -0.3121
REMARK 3 S21: -0.0934 S22: 0.0118 S23: 0.0863
REMARK 3 S31: 0.4664 S32: -0.9343 S33: 0.0123
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0046 34.5595 19.3717
REMARK 3 T TENSOR
REMARK 3 T11: 0.3474 T22: 0.5250
REMARK 3 T33: 0.3730 T12: 0.0221
REMARK 3 T13: -0.1260 T23: 0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 1.8239 L22: 1.0368
REMARK 3 L33: 2.2064 L12: 1.3502
REMARK 3 L13: 0.0020 L23: 0.0289
REMARK 3 S TENSOR
REMARK 3 S11: -0.1268 S12: 0.0375 S13: 0.1673
REMARK 3 S21: -0.0166 S22: 0.1611 S23: 0.1652
REMARK 3 S31: -0.2087 S32: -0.2982 S33: -0.0683
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7773 10.3314 8.7263
REMARK 3 T TENSOR
REMARK 3 T11: 0.5584 T22: 0.4757
REMARK 3 T33: 0.4481 T12: 0.1205
REMARK 3 T13: -0.0925 T23: -0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 3.1174 L22: 2.0831
REMARK 3 L33: 3.2284 L12: 0.4380
REMARK 3 L13: 1.8056 L23: 0.2564
REMARK 3 S TENSOR
REMARK 3 S11: 0.2989 S12: -0.3135 S13: -0.6615
REMARK 3 S21: 0.3736 S22: 0.2110 S23: -0.5445
REMARK 3 S31: 0.6342 S32: 0.4629 S33: -0.3829
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 367 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1017 18.0501 2.9588
REMARK 3 T TENSOR
REMARK 3 T11: 0.3739 T22: 0.4529
REMARK 3 T33: 0.3090 T12: 0.0581
REMARK 3 T13: -0.0722 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.2435 L22: 1.8914
REMARK 3 L33: 3.5891 L12: -0.1942
REMARK 3 L13: -0.0134 L23: 1.1340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1500 S12: -0.0124 S13: -0.1344
REMARK 3 S21: 0.0010 S22: -0.1106 S23: -0.1248
REMARK 3 S31: 0.2414 S32: 0.2924 S33: -0.1275
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9713 30.7267 16.3689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3465 T22: 0.5943
REMARK 3 T33: 0.3299 T12: -0.0817
REMARK 3 T13: -0.0293 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 1.8636 L22: 1.8609
REMARK 3 L33: 1.6000 L12: 0.2374
REMARK 3 L13: 0.0043 L23: 0.3552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0694 S12: 0.1055 S13: -0.2385
REMARK 3 S21: -0.1948 S22: 0.2149 S23: -0.2267
REMARK 3 S31: -0.0688 S32: 0.4329 S33: -0.1035
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.6921 41.9826 14.1274
REMARK 3 T TENSOR
REMARK 3 T11: 0.4892 T22: 0.5953
REMARK 3 T33: 0.4217 T12: -0.2650
REMARK 3 T13: -0.0435 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 2.0567 L22: 1.4741
REMARK 3 L33: 2.4463 L12: -0.8880
REMARK 3 L13: 1.6361 L23: -0.3998
REMARK 3 S TENSOR
REMARK 3 S11: -0.1962 S12: 0.5763 S13: 0.4268
REMARK 3 S21: -0.0922 S22: -0.0074 S23: -0.3123
REMARK 3 S31: -0.5922 S32: 0.6481 S33: 0.0960
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9826 32.3478 5.0155
REMARK 3 T TENSOR
REMARK 3 T11: 0.3702 T22: 0.5148
REMARK 3 T33: 0.2302 T12: -0.0696
REMARK 3 T13: -0.0371 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 2.5787 L22: 2.3007
REMARK 3 L33: 2.1607 L12: 0.8093
REMARK 3 L13: 1.4875 L23: 0.7235
REMARK 3 S TENSOR
REMARK 3 S11: 0.2091 S12: -0.3152 S13: -0.0872
REMARK 3 S21: -0.1839 S22: -0.2307 S23: -0.0497
REMARK 3 S31: -0.3605 S32: 0.3510 S33: 0.0152
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.9210 31.3406 53.8321
REMARK 3 T TENSOR
REMARK 3 T11: 0.3582 T22: 0.3763
REMARK 3 T33: 0.3109 T12: -0.1338
REMARK 3 T13: -0.0224 T23: 0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 1.8306 L22: 3.3734
REMARK 3 L33: 1.9740 L12: -1.4530
REMARK 3 L13: -0.6876 L23: 0.7336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0830 S12: -0.2968 S13: -0.1042
REMARK 3 S21: 0.6712 S22: -0.0297 S23: -0.0455
REMARK 3 S31: 0.2054 S32: 0.0601 S33: 0.1068
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 110.9922 34.1095 44.0319
REMARK 3 T TENSOR
REMARK 3 T11: 0.2779 T22: 0.3996
REMARK 3 T33: 0.3057 T12: -0.1337
REMARK 3 T13: -0.0354 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 1.0995 L22: 1.6399
REMARK 3 L33: 2.0062 L12: -0.2532
REMARK 3 L13: -0.2124 L23: -0.0915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: -0.1263 S13: 0.0321
REMARK 3 S21: 0.2968 S22: -0.0837 S23: -0.2378
REMARK 3 S31: -0.1732 S32: 0.4849 S33: 0.0485
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 108.8270 33.4400 37.1745
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.3365
REMARK 3 T33: 0.3274 T12: -0.1027
REMARK 3 T13: -0.0045 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.8366 L22: 1.7887
REMARK 3 L33: 2.3661 L12: -1.7285
REMARK 3 L13: -0.8866 L23: 1.1700
REMARK 3 S TENSOR
REMARK 3 S11: 0.0395 S12: -0.0273 S13: 0.0032
REMARK 3 S21: 0.2297 S22: -0.0335 S23: -0.0566
REMARK 3 S31: 0.0968 S32: 0.1554 S33: -0.0186
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.6035 30.1270 31.1112
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.3224
REMARK 3 T33: 0.3441 T12: -0.0915
REMARK 3 T13: -0.0157 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.5367 L22: 1.1184
REMARK 3 L33: 2.2127 L12: -0.6269
REMARK 3 L13: 0.2398 L23: -0.0083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0944 S12: 0.1571 S13: -0.1125
REMARK 3 S21: 0.0048 S22: -0.1171 S23: 0.1569
REMARK 3 S31: 0.1075 S32: -0.1055 S33: 0.0234
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 6WV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1000249039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83198
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
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: PHENIX 1.17.1-3660
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, KNO3, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 107.92000
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 215.84000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 215.84000
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 107.92000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 52.09150
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -90.22512
REMARK 350 BIOMT3 2 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 GLY A 2
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 THR B 543
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 203 P1 UCJ B 604 1.12
REMARK 500 OG SER A 203 P1 UCJ A 607 1.30
REMARK 500 ND2 ASN A 265 C1 NAG A 604 1.64
REMARK 500 OG SER B 203 O1 UCJ B 604 1.70
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 GLU B 285 O - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 GLU B 285 O - C - N ANGL. DEV. = -17.9 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 PHE A 47 -2.26 69.83
REMARK 500 ALA A 62 68.13 -100.58
REMARK 500 ALA A 167 73.70 -151.82
REMARK 500 SER A 203 -126.84 58.04
REMARK 500 ASP A 306 -81.75 -94.72
REMARK 500 VAL A 407 -64.17 -124.20
REMARK 500 ASN A 464 50.46 -97.28
REMARK 500 ASP A 514 -167.17 -160.04
REMARK 500 PHE B 47 -3.98 78.90
REMARK 500 ALA B 62 50.46 -111.73
REMARK 500 TYR B 77 79.65 -113.80
REMARK 500 SER B 203 -129.44 55.58
REMARK 500 ASP B 306 -86.66 -103.49
REMARK 500 VAL B 407 -61.42 -128.49
REMARK 500 ASP B 514 -159.45 -158.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU B 285 29.47
REMARK 500 GLU B 285 29.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 604
REMARK 610 UCJ A 607
REMARK 610 UCJ B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6WUV RELATED DB: PDB
REMARK 900 RELATED ID: 6WUY RELATED DB: PDB
REMARK 900 RELATED ID: 6WUZ RELATED DB: PDB
DBREF 6WV1 A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6WV1 B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET FUC D 3 10
HET NAG A 604 14
HET 7PE A 605 21
HET NAG A 606 14
HET UCJ A 607 7
HET HI6 A 608 21
HET UCJ B 604 7
HET HI6 B 605 42
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM 7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)
HETNAM 2 7PE ETHOXY)ETHANOL
HETNAM UCJ PROPAN-2-YL HYDROGEN (S)-METHYLPHOSPHONATE
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN 7PE POLYETHYLENE GLYCOL FRAGMENT
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN 2 HI6 PYRIDINIUM DIMETHYLETHER
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 6 7PE C14 H30 O7
FORMUL 8 UCJ 2(C4 H11 O3 P)
FORMUL 9 HI6 2(C14 H16 N4 O3 2+)
FORMUL 12 HOH *413(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 MET A 241 GLY A 256 1 16
HELIX 12 AB3 ASN A 265 THR A 275 1 11
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 ALA A 318 1 8
HELIX 16 AB7 GLY A 335 GLY A 342 5 8
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 PHE A 535 1 11
HELIX 26 AC8 PHE A 535 ALA A 542 1 8
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 MET B 241 VAL B 255 1 15
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
HELIX 41 AE5 THR B 311 ALA B 318 1 8
HELIX 42 AE6 GLY B 335 GLY B 342 5 8
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 PHE B 535 ALA B 542 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 2 VAL A 239 GLY A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA611 ILE B 20 THR B 24 0
SHEET 2 AA611 GLY B 27 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA611 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA611 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA611 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA611 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA7 2 VAL B 68 CYS B 69 0
SHEET 2 AA7 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA8 2 VAL B 239 GLY B 240 0
SHEET 2 AA8 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.02
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 4.02
CISPEP 2 CYS A 257 PRO A 258 0 -4.16
CISPEP 3 TYR B 105 PRO B 106 0 0.46
CISPEP 4 PRO B 258 PRO B 259 0 -12.86
CRYST1 104.183 104.183 323.760 90.00 90.00 120.00 P 31 2 1 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 0.009598 0.005542 0.000000 0.00000
SCALE2 0.000000 0.011083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003089 0.00000
TER 4184 ALA A 542
TER 8366 ALA B 542
MASTER 640 0 13 52 36 0 0 6 8859 2 217 84
END |