HEADER HYDROLASE/HYDROLASE INHIBITOR 16-SEP-15 5DRP
TITLE STRUCTURE OF THE AALPXC/LPC-023 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-3-O-[3-HYDROXYMYRISTOYL] N-ACETYLGLUCOSAMINE
COMPND 3 DEACETYLASE;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: UDP-3-O-ACYL-GLCNAC DEACETYLASE;
COMPND 6 EC: 3.5.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS (STRAIN VF5);
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: LPXC, ENVA, AQ_1772;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS LPXC, INHIBITOR, LIPID A, GRAM-NEGATIVE BACTERIA, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NAJEEB,C.-J.LEE,P.ZHOU
REVDAT 4 27-SEP-23 5DRP 1 LINK
REVDAT 3 11-DEC-19 5DRP 1 REMARK
REVDAT 2 20-SEP-17 5DRP 1 REMARK
REVDAT 1 09-MAR-16 5DRP 0
JRNL AUTH C.J.LEE,X.LIANG,Q.WU,J.NAJEEB,J.ZHAO,R.GOPALASWAMY,
JRNL AUTH 2 M.TITECAT,F.SEBBANE,N.LEMAITRE,E.J.TOONE,P.ZHOU
JRNL TITL DRUG DESIGN FROM THE CRYPTIC INHIBITOR ENVELOPE.
JRNL REF NAT COMMUN V. 7 10638 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 26912110
JRNL DOI 10.1038/NCOMMS10638
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.050
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 40333
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 2008
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 34.8142 - 4.5494 0.99 2758 145 0.1403 0.1548
REMARK 3 2 4.5494 - 3.6122 0.99 2786 142 0.1316 0.1704
REMARK 3 3 3.6122 - 3.1560 0.99 2778 150 0.1563 0.1721
REMARK 3 4 3.1560 - 2.8676 0.98 2756 143 0.1757 0.2518
REMARK 3 5 2.8676 - 2.6621 0.98 2711 146 0.1719 0.1971
REMARK 3 6 2.6621 - 2.5052 0.98 2749 143 0.1705 0.2043
REMARK 3 7 2.5052 - 2.3798 0.98 2749 149 0.1658 0.2116
REMARK 3 8 2.3798 - 2.2762 0.98 2722 139 0.1615 0.1993
REMARK 3 9 2.2762 - 2.1886 0.97 2729 133 0.1639 0.2265
REMARK 3 10 2.1886 - 2.1131 0.97 2747 151 0.1666 0.2098
REMARK 3 11 2.1131 - 2.0470 0.97 2737 145 0.1693 0.2175
REMARK 3 12 2.0470 - 1.9885 0.97 2654 130 0.1742 0.2371
REMARK 3 13 1.9885 - 1.9362 0.96 2719 151 0.1774 0.2205
REMARK 3 14 1.9362 - 1.8889 0.97 2730 141 0.1881 0.2195
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.91
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 : 0.006 4451
REMARK 3 ANGLE : 0.991 5996
REMARK 3 CHIRALITY : 0.040 653
REMARK 3 PLANARITY : 0.004 767
REMARK 3 DIHEDRAL : 12.668 1643
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7043 38.3730 -11.1298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2218 T22: 0.3672
REMARK 3 T33: 0.2315 T12: 0.0815
REMARK 3 T13: -0.0099 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 2.2722 L22: 2.8649
REMARK 3 L33: 2.1286 L12: -0.5929
REMARK 3 L13: -0.0871 L23: 0.0438
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.1593 S13: 0.2579
REMARK 3 S21: -0.0576 S22: 0.0064 S23: 0.2482
REMARK 3 S31: -0.2001 S32: -0.3999 S33: 0.0077
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2394 46.5570 -1.5294
REMARK 3 T TENSOR
REMARK 3 T11: 0.3456 T22: 0.3691
REMARK 3 T33: 0.4075 T12: 0.0542
REMARK 3 T13: 0.0123 T23: -0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 4.3039 L22: 3.3551
REMARK 3 L33: 8.5470 L12: -1.3432
REMARK 3 L13: 3.9936 L23: -2.0947
REMARK 3 S TENSOR
REMARK 3 S11: -0.5667 S12: -0.1264 S13: 0.7487
REMARK 3 S21: 0.3888 S22: -0.0130 S23: -0.5238
REMARK 3 S31: -0.6127 S32: 0.0816 S33: 0.5630
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9996 31.8030 -3.4003
REMARK 3 T TENSOR
REMARK 3 T11: 0.2203 T22: 0.3905
REMARK 3 T33: 0.2585 T12: 0.0320
REMARK 3 T13: -0.0548 T23: -0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 2.7049 L22: 4.5321
REMARK 3 L33: 3.2018 L12: -0.8661
REMARK 3 L13: 0.9822 L23: 2.8057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: -0.0753 S13: 0.1039
REMARK 3 S21: 0.2414 S22: 0.1946 S23: -0.4198
REMARK 3 S31: 0.2054 S32: 0.4029 S33: -0.1848
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9688 23.6544 -6.9818
REMARK 3 T TENSOR
REMARK 3 T11: 0.2475 T22: 0.3603
REMARK 3 T33: 0.1639 T12: 0.0452
REMARK 3 T13: 0.0257 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 3.0694 L22: 3.1727
REMARK 3 L33: 3.1440 L12: 0.4649
REMARK 3 L13: -0.7266 L23: -0.7363
REMARK 3 S TENSOR
REMARK 3 S11: -0.1837 S12: 0.1266 S13: 0.0480
REMARK 3 S21: 0.2079 S22: 0.2108 S23: 0.0933
REMARK 3 S31: 0.2296 S32: -0.4043 S33: -0.0062
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4869 18.5042 -7.2794
REMARK 3 T TENSOR
REMARK 3 T11: 0.2718 T22: 0.2840
REMARK 3 T33: 0.2582 T12: -0.0591
REMARK 3 T13: 0.0396 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 6.4068 L22: 3.5305
REMARK 3 L33: 3.3014 L12: -0.2610
REMARK 3 L13: 0.1632 L23: -2.7178
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: 0.0125 S13: -0.4690
REMARK 3 S21: 0.1021 S22: 0.1565 S23: 0.4117
REMARK 3 S31: 0.3433 S32: -0.2581 S33: -0.2020
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 207 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9124 15.7803 -11.5880
REMARK 3 T TENSOR
REMARK 3 T11: 0.2709 T22: 0.2507
REMARK 3 T33: 0.2662 T12: 0.0718
REMARK 3 T13: 0.0088 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 5.7805 L22: 4.8412
REMARK 3 L33: 6.7419 L12: 3.4384
REMARK 3 L13: -0.7093 L23: -0.0391
REMARK 3 S TENSOR
REMARK 3 S11: -0.2360 S12: -0.1486 S13: -0.2721
REMARK 3 S21: 0.0984 S22: 0.3606 S23: -0.3110
REMARK 3 S31: 0.6563 S32: 0.0947 S33: -0.0389
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6449 38.4879 -1.2258
REMARK 3 T TENSOR
REMARK 3 T11: 0.1979 T22: 0.2839
REMARK 3 T33: 0.1879 T12: 0.0533
REMARK 3 T13: -0.0359 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 2.9927 L22: 3.4487
REMARK 3 L33: 2.7884 L12: -0.3023
REMARK 3 L13: -0.3881 L23: -0.0891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0322 S12: -0.2411 S13: 0.3221
REMARK 3 S21: 0.3492 S22: 0.2070 S23: -0.1402
REMARK 3 S31: -0.1686 S32: 0.0055 S33: -0.1495
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6264 25.2522 21.3965
REMARK 3 T TENSOR
REMARK 3 T11: 0.1991 T22: 0.3765
REMARK 3 T33: 0.2267 T12: -0.0412
REMARK 3 T13: -0.0193 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 2.2638 L22: 0.7745
REMARK 3 L33: 2.5417 L12: -0.2371
REMARK 3 L13: -0.3745 L23: -0.2915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: 0.2018 S13: -0.0722
REMARK 3 S21: -0.0994 S22: 0.0508 S23: 0.1130
REMARK 3 S31: -0.0221 S32: -0.4562 S33: -0.1132
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9099 28.2038 33.9630
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.2599
REMARK 3 T33: 0.1422 T12: -0.0067
REMARK 3 T13: -0.0030 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 4.7397 L22: 7.0352
REMARK 3 L33: 6.0179 L12: 0.9275
REMARK 3 L13: -2.0841 L23: 0.6463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.3281 S13: -0.0408
REMARK 3 S21: 0.2248 S22: 0.0061 S23: -0.1344
REMARK 3 S31: 0.0941 S32: 0.1079 S33: 0.0134
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5655 24.5090 17.2795
REMARK 3 T TENSOR
REMARK 3 T11: 0.1542 T22: 0.2844
REMARK 3 T33: 0.1549 T12: -0.0209
REMARK 3 T13: -0.0133 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 2.8132 L22: 2.3271
REMARK 3 L33: 1.5398 L12: -0.6683
REMARK 3 L13: -0.1871 L23: -0.3755
REMARK 3 S TENSOR
REMARK 3 S11: 0.1263 S12: 0.3634 S13: -0.1386
REMARK 3 S21: -0.0738 S22: -0.1240 S23: 0.0960
REMARK 3 S31: 0.0179 S32: -0.1684 S33: -0.0219
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 117 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7820 41.5391 22.2312
REMARK 3 T TENSOR
REMARK 3 T11: 0.3762 T22: 0.2308
REMARK 3 T33: 0.4005 T12: -0.0291
REMARK 3 T13: 0.0287 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 5.9051 L22: 1.4171
REMARK 3 L33: 4.2216 L12: 0.5097
REMARK 3 L13: 2.0324 L23: 0.8328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1268 S12: -0.0984 S13: 1.2380
REMARK 3 S21: -0.0042 S22: -0.1251 S23: -0.1264
REMARK 3 S31: -0.5547 S32: 0.1116 S33: 0.2448
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4593 19.1193 24.0674
REMARK 3 T TENSOR
REMARK 3 T11: 0.2288 T22: 0.2326
REMARK 3 T33: 0.1918 T12: 0.0042
REMARK 3 T13: 0.0099 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 4.5338 L22: 3.6264
REMARK 3 L33: 1.9021 L12: 0.6071
REMARK 3 L13: -0.2816 L23: -1.0218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0506 S12: -0.2236 S13: -0.3665
REMARK 3 S21: 0.2102 S22: -0.1264 S23: -0.1120
REMARK 3 S31: 0.0428 S32: 0.1589 S33: 0.0526
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 207 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4330 11.2565 19.3613
REMARK 3 T TENSOR
REMARK 3 T11: 0.2945 T22: 0.3036
REMARK 3 T33: 0.5022 T12: 0.0345
REMARK 3 T13: 0.0868 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 2.3203 L22: 7.5216
REMARK 3 L33: 7.6004 L12: -0.9263
REMARK 3 L13: 1.1796 L23: -2.5043
REMARK 3 S TENSOR
REMARK 3 S11: 0.1002 S12: 0.3309 S13: -0.7683
REMARK 3 S21: -0.4905 S22: -0.3440 S23: -0.5214
REMARK 3 S31: 0.7318 S32: 0.4810 S33: 0.2579
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8575 31.2346 22.7883
REMARK 3 T TENSOR
REMARK 3 T11: 0.1652 T22: 0.1792
REMARK 3 T33: 0.1700 T12: -0.0310
REMARK 3 T13: 0.0008 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 3.1374 L22: 2.7594
REMARK 3 L33: 2.3742 L12: -0.6777
REMARK 3 L13: -0.8264 L23: 0.6266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0342 S12: -0.1169 S13: 0.2418
REMARK 3 S21: 0.0278 S22: 0.0426 S23: -0.0541
REMARK 3 S31: -0.2450 S32: 0.1630 S33: -0.0227
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 253 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6366 39.0529 31.9441
REMARK 3 T TENSOR
REMARK 3 T11: 0.3384 T22: 0.3567
REMARK 3 T33: 0.2848 T12: -0.1082
REMARK 3 T13: 0.0513 T23: -0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 4.9876 L22: 2.3816
REMARK 3 L33: 5.2554 L12: -2.8853
REMARK 3 L13: 0.2393 L23: -1.9286
REMARK 3 S TENSOR
REMARK 3 S11: 0.0886 S12: -0.2970 S13: 0.5269
REMARK 3 S21: 0.6270 S22: -0.0229 S23: -0.0201
REMARK 3 S31: -0.7646 S32: 0.0308 S33: -0.0423
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 5DRP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213627.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-15
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 : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43313
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 3P3C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M AMMONIUM CHLORIDE, 11.8%
REMARK 280 PEG3350, 10% 1,3-PROPANEDIOL., PH 7.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 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 1
REMARK 465 LEU A 269
REMARK 465 THR A 270
REMARK 465 ARG A 271
REMARK 465 ASP A 272
REMARK 465 LEU A 273
REMARK 465 PRO A 274
REMARK 465 MET B 1
REMARK 465 LEU B 269
REMARK 465 THR B 270
REMARK 465 ARG B 271
REMARK 465 ASP B 272
REMARK 465 LEU B 273
REMARK 465 PRO B 274
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 LYS A 32 CD CE NZ
REMARK 470 GLU A 33 CD OE1 OE2
REMARK 470 GLU A 187 CG CD OE1 OE2
REMARK 470 LYS A 268 CG CD CE NZ
REMARK 470 GLU B 135 CG CD OE1 OE2
REMARK 470 GLU B 187 CG CD OE1 OE2
REMARK 470 LYS B 268 CG CD CE NZ
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 O HOH B 582 O HOH B 621 2.11
REMARK 500 O HOH B 572 O HOH B 577 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 56 18.89 -140.65
REMARK 500 THR A 71 62.51 63.87
REMARK 500 LEU A 99 -122.14 53.74
REMARK 500 ASP A 134 89.76 -159.93
REMARK 500 LYS A 156 42.62 -79.78
REMARK 500 ASN A 157 -159.65 -150.03
REMARK 500 THR B 6 -163.53 -128.03
REMARK 500 SER B 59 165.66 59.15
REMARK 500 THR B 71 61.95 64.95
REMARK 500 LEU B 99 -121.84 52.72
REMARK 500 GLN B 117 -133.86 -97.82
REMARK 500 ASN B 118 -57.62 -123.70
REMARK 500 GLU B 135 105.86 -51.17
REMARK 500 ASN B 157 -164.43 -161.96
REMARK 500 ASP B 209 28.18 -141.77
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 5EP B 402
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 74 NE2
REMARK 620 2 HIS A 226 NE2 98.0
REMARK 620 3 ASP A 230 OD1 97.2 98.6
REMARK 620 4 5EP A 402 O01 118.3 85.8 143.4
REMARK 620 5 5EP A 402 O04 99.5 161.3 85.7 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 74 NE2
REMARK 620 2 HIS B 226 NE2 100.4
REMARK 620 3 ASP B 230 OD1 95.9 96.8
REMARK 620 4 5EP B 402 O01 112.3 90.5 149.1
REMARK 620 5 5EP B 402 O04 98.5 159.5 89.1 74.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5EP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5EP B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DRO RELATED DB: PDB
REMARK 900 RELATED ID: 5DRQ RELATED DB: PDB
REMARK 900 RELATED ID: 5DRR RELATED DB: PDB
DBREF 5DRP A 1 274 UNP O67648 LPXC_AQUAE 1 274
DBREF 5DRP B 1 274 UNP O67648 LPXC_AQUAE 1 274
SEQADV 5DRP ALA A 181 UNP O67648 CYS 181 ENGINEERED MUTATION
SEQADV 5DRP ALA B 181 UNP O67648 CYS 181 ENGINEERED MUTATION
SEQRES 1 A 274 MET GLY LEU GLU LYS THR VAL LYS GLU LYS LEU SER PHE
SEQRES 2 A 274 GLU GLY VAL GLY ILE HIS THR GLY GLU TYR SER LYS LEU
SEQRES 3 A 274 ILE ILE HIS PRO GLU LYS GLU GLY THR GLY ILE ARG PHE
SEQRES 4 A 274 PHE LYS ASN GLY VAL TYR ILE PRO ALA ARG HIS GLU PHE
SEQRES 5 A 274 VAL VAL HIS THR ASN HIS SER THR ASP LEU GLY PHE LYS
SEQRES 6 A 274 GLY GLN ARG ILE LYS THR VAL GLU HIS ILE LEU SER VAL
SEQRES 7 A 274 LEU HIS LEU LEU GLU ILE THR ASN VAL THR ILE GLU VAL
SEQRES 8 A 274 ILE GLY ASN GLU ILE PRO ILE LEU ASP GLY SER GLY TRP
SEQRES 9 A 274 GLU PHE TYR GLU ALA ILE ARG LYS ASN ILE LEU ASN GLN
SEQRES 10 A 274 ASN ARG GLU ILE ASP TYR PHE VAL VAL GLU GLU PRO ILE
SEQRES 11 A 274 ILE VAL GLU ASP GLU GLY ARG LEU ILE LYS ALA GLU PRO
SEQRES 12 A 274 SER ASP THR LEU GLU VAL THR TYR GLU GLY GLU PHE LYS
SEQRES 13 A 274 ASN PHE LEU GLY ARG GLN LYS PHE THR PHE VAL GLU GLY
SEQRES 14 A 274 ASN GLU GLU GLU ILE VAL LEU ALA ARG THR PHE ALA PHE
SEQRES 15 A 274 ASP TRP GLU ILE GLU HIS ILE LYS LYS VAL GLY LEU GLY
SEQRES 16 A 274 LYS GLY GLY SER LEU LYS ASN THR LEU VAL LEU GLY LYS
SEQRES 17 A 274 ASP LYS VAL TYR ASN PRO GLU GLY LEU ARG TYR GLU ASN
SEQRES 18 A 274 GLU PRO VAL ARG HIS LYS VAL PHE ASP LEU ILE GLY ASP
SEQRES 19 A 274 LEU TYR LEU LEU GLY SER PRO VAL LYS GLY LYS PHE TYR
SEQRES 20 A 274 SER PHE ARG GLY GLY HIS SER LEU ASN VAL LYS LEU VAL
SEQRES 21 A 274 LYS GLU LEU ALA LYS LYS GLN LYS LEU THR ARG ASP LEU
SEQRES 22 A 274 PRO
SEQRES 1 B 274 MET GLY LEU GLU LYS THR VAL LYS GLU LYS LEU SER PHE
SEQRES 2 B 274 GLU GLY VAL GLY ILE HIS THR GLY GLU TYR SER LYS LEU
SEQRES 3 B 274 ILE ILE HIS PRO GLU LYS GLU GLY THR GLY ILE ARG PHE
SEQRES 4 B 274 PHE LYS ASN GLY VAL TYR ILE PRO ALA ARG HIS GLU PHE
SEQRES 5 B 274 VAL VAL HIS THR ASN HIS SER THR ASP LEU GLY PHE LYS
SEQRES 6 B 274 GLY GLN ARG ILE LYS THR VAL GLU HIS ILE LEU SER VAL
SEQRES 7 B 274 LEU HIS LEU LEU GLU ILE THR ASN VAL THR ILE GLU VAL
SEQRES 8 B 274 ILE GLY ASN GLU ILE PRO ILE LEU ASP GLY SER GLY TRP
SEQRES 9 B 274 GLU PHE TYR GLU ALA ILE ARG LYS ASN ILE LEU ASN GLN
SEQRES 10 B 274 ASN ARG GLU ILE ASP TYR PHE VAL VAL GLU GLU PRO ILE
SEQRES 11 B 274 ILE VAL GLU ASP GLU GLY ARG LEU ILE LYS ALA GLU PRO
SEQRES 12 B 274 SER ASP THR LEU GLU VAL THR TYR GLU GLY GLU PHE LYS
SEQRES 13 B 274 ASN PHE LEU GLY ARG GLN LYS PHE THR PHE VAL GLU GLY
SEQRES 14 B 274 ASN GLU GLU GLU ILE VAL LEU ALA ARG THR PHE ALA PHE
SEQRES 15 B 274 ASP TRP GLU ILE GLU HIS ILE LYS LYS VAL GLY LEU GLY
SEQRES 16 B 274 LYS GLY GLY SER LEU LYS ASN THR LEU VAL LEU GLY LYS
SEQRES 17 B 274 ASP LYS VAL TYR ASN PRO GLU GLY LEU ARG TYR GLU ASN
SEQRES 18 B 274 GLU PRO VAL ARG HIS LYS VAL PHE ASP LEU ILE GLY ASP
SEQRES 19 B 274 LEU TYR LEU LEU GLY SER PRO VAL LYS GLY LYS PHE TYR
SEQRES 20 B 274 SER PHE ARG GLY GLY HIS SER LEU ASN VAL LYS LEU VAL
SEQRES 21 B 274 LYS GLU LEU ALA LYS LYS GLN LYS LEU THR ARG ASP LEU
SEQRES 22 B 274 PRO
HET ZN A 401 1
HET 5EP A 402 29
HET ZN B 401 1
HET 5EP B 402 28
HET CL B 403 1
HET DMS B 404 4
HETNAM ZN ZINC ION
HETNAM 5EP N~2~-{4-[4-(4-AMINOPHENYL)BUTA-1,3-DIYN-1-YL]BENZOYL}-
HETNAM 2 5EP N-HYDROXY-L-ISOLEUCINAMIDE
HETNAM CL CHLORIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 5EP 2(C23 H23 N3 O3)
FORMUL 7 CL CL 1-
FORMUL 8 DMS C2 H6 O S
FORMUL 9 HOH *259(H2 O)
HELIX 1 AA1 ARG A 49 GLU A 51 5 3
HELIX 2 AA2 VAL A 72 LEU A 82 1 11
HELIX 3 AA3 GLY A 103 LYS A 112 1 10
HELIX 4 AA4 ASN A 170 ILE A 174 5 5
HELIX 5 AA5 GLU A 185 VAL A 192 1 8
HELIX 6 AA6 ASN A 221 TYR A 236 1 16
HELIX 7 AA7 LEU A 237 GLY A 239 5 3
HELIX 8 AA8 GLY A 252 LYS A 268 1 17
HELIX 9 AA9 ARG B 49 GLU B 51 5 3
HELIX 10 AB1 VAL B 72 LEU B 82 1 11
HELIX 11 AB2 GLY B 103 LYS B 112 1 10
HELIX 12 AB3 ASN B 170 ILE B 174 5 5
HELIX 13 AB4 ASP B 183 VAL B 192 1 10
HELIX 14 AB5 ASN B 221 TYR B 236 1 16
HELIX 15 AB6 LEU B 237 GLY B 239 5 3
HELIX 16 AB7 GLY B 252 GLN B 267 1 16
SHEET 1 AA1 2 LEU A 3 VAL A 7 0
SHEET 2 AA1 2 ILE A 114 GLU A 120 -1 O ARG A 119 N GLU A 4
SHEET 1 AA2 5 LEU A 11 VAL A 16 0
SHEET 2 AA2 5 TYR A 23 PRO A 30 -1 O ILE A 28 N LEU A 11
SHEET 3 AA2 5 VAL A 87 ILE A 92 -1 O THR A 88 N HIS A 29
SHEET 4 AA2 5 ILE A 37 LYS A 41 1 N PHE A 40 O VAL A 91
SHEET 5 AA2 5 VAL A 44 PRO A 47 -1 O ILE A 46 N PHE A 39
SHEET 1 AA3 3 VAL A 53 HIS A 55 0
SHEET 2 AA3 3 ASP A 61 PHE A 64 -1 O ASP A 61 N HIS A 55
SHEET 3 AA3 3 GLN A 67 ILE A 69 -1 O ILE A 69 N LEU A 62
SHEET 1 AA4 2 PHE A 124 VAL A 125 0
SHEET 2 AA4 2 VAL A 242 LYS A 243 1 O LYS A 243 N PHE A 124
SHEET 1 AA5 5 ILE A 130 GLU A 133 0
SHEET 2 AA5 5 LEU A 138 GLU A 142 -1 O ILE A 139 N VAL A 132
SHEET 3 AA5 5 LYS A 245 PHE A 249 -1 O PHE A 249 N LEU A 138
SHEET 4 AA5 5 GLU A 148 GLU A 154 1 N GLU A 148 O PHE A 246
SHEET 5 AA5 5 ARG A 161 VAL A 167 -1 O PHE A 166 N VAL A 149
SHEET 1 AA6 2 PHE A 180 PHE A 182 0
SHEET 2 AA6 2 LEU A 204 LEU A 206 1 O LEU A 206 N ALA A 181
SHEET 1 AA7 2 LEU B 3 VAL B 7 0
SHEET 2 AA7 2 ILE B 114 GLU B 120 -1 O GLN B 117 N GLU B 4
SHEET 1 AA8 5 LEU B 11 VAL B 16 0
SHEET 2 AA8 5 TYR B 23 PRO B 30 -1 O LEU B 26 N PHE B 13
SHEET 3 AA8 5 VAL B 87 ILE B 92 -1 O THR B 88 N HIS B 29
SHEET 4 AA8 5 ILE B 37 LYS B 41 1 N ARG B 38 O ILE B 89
SHEET 5 AA8 5 VAL B 44 PRO B 47 -1 O ILE B 46 N PHE B 39
SHEET 1 AA9 3 VAL B 53 VAL B 54 0
SHEET 2 AA9 3 ASP B 61 PHE B 64 -1 O ASP B 61 N VAL B 54
SHEET 3 AA9 3 GLN B 67 ILE B 69 -1 O ILE B 69 N LEU B 62
SHEET 1 AB1 2 PHE B 124 VAL B 125 0
SHEET 2 AB1 2 VAL B 242 LYS B 243 1 O LYS B 243 N PHE B 124
SHEET 1 AB2 5 ILE B 130 ASP B 134 0
SHEET 2 AB2 5 ARG B 137 GLU B 142 -1 O ALA B 141 N ILE B 130
SHEET 3 AB2 5 LYS B 245 PHE B 249 -1 O PHE B 249 N LEU B 138
SHEET 4 AB2 5 GLU B 148 PHE B 155 1 N THR B 150 O SER B 248
SHEET 5 AB2 5 GLY B 160 VAL B 167 -1 O GLN B 162 N GLY B 153
SHEET 1 AB3 2 PHE B 180 PHE B 182 0
SHEET 2 AB3 2 LEU B 204 LEU B 206 1 O LEU B 206 N ALA B 181
LINK NE2 HIS A 74 ZN ZN A 401 1555 1555 2.10
LINK NE2 HIS A 226 ZN ZN A 401 1555 1555 2.09
LINK OD1 ASP A 230 ZN ZN A 401 1555 1555 1.99
LINK ZN ZN A 401 O01 5EP A 402 1555 1555 2.05
LINK ZN ZN A 401 O04 5EP A 402 1555 1555 2.19
LINK NE2 HIS B 74 ZN ZN B 401 1555 1555 2.01
LINK NE2 HIS B 226 ZN ZN B 401 1555 1555 2.05
LINK OD1 ASP B 230 ZN ZN B 401 1555 1555 2.02
LINK ZN ZN B 401 O01 5EP B 402 1555 1555 2.13
LINK ZN ZN B 401 O04 5EP B 402 1555 1555 2.28
SITE 1 AC1 4 HIS A 74 HIS A 226 ASP A 230 5EP A 402
SITE 1 AC2 15 HIS A 58 GLU A 73 HIS A 74 ARG A 119
SITE 2 AC2 15 THR A 179 PHE A 180 GLY A 198 SER A 199
SITE 3 AC2 15 LEU A 200 THR A 203 HIS A 226 ASP A 230
SITE 4 AC2 15 HIS A 253 ZN A 401 HOH A 537
SITE 1 AC3 4 HIS B 74 HIS B 226 ASP B 230 5EP B 402
SITE 1 AC4 19 HIS B 19 GLU B 73 HIS B 74 GLU B 128
SITE 2 AC4 19 THR B 179 PHE B 180 ALA B 181 ILE B 189
SITE 3 AC4 19 LYS B 190 GLY B 195 GLY B 198 SER B 199
SITE 4 AC4 19 THR B 203 HIS B 226 ASP B 230 ZN B 401
SITE 5 AC4 19 CL B 403 DMS B 404 HOH B 580
SITE 1 AC5 4 SER B 59 5EP B 402 DMS B 404 HOH B 590
SITE 1 AC6 9 SER B 59 THR B 60 GLU B 73 ASP B 234
SITE 2 AC6 9 HIS B 253 ASN B 256 5EP B 402 CL B 403
SITE 3 AC6 9 HOH B 571
CRYST1 45.657 50.419 61.730 80.26 71.71 88.90 P 1 2
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 0.021902 -0.000421 -0.007275 0.00000
SCALE2 0.000000 0.019837 -0.003461 0.00000
SCALE3 0.000000 0.000000 0.017319 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
