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HEADER HYDROLASE 20-OCT-19 6T6Y
TITLE STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH
TITLE 2 BOTTROMYCIN A2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOTH;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. BC16019;
SOURCE 3 ORGANISM_TAXID: 1109705;
SOURCE 4 GENE: BOTH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2
KEYWDS BOTTROMYCIN, RIPP, EPIMERASE, ABH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KOEHNKE,A.SIKANDAR
REVDAT 1 15-JUL-20 6T6Y 0
JRNL AUTH A.SIKANDAR,L.FRANZ,S.ADAM,J.SANTOS-ABERTURAS,L.HORBAL,
JRNL AUTH 2 A.LUZHETSKYY,A.W.TRUMAN,O.V.KALININA,J.KOEHNKE
JRNL TITL THE BOTTROMYCIN EPIMERASE BOTH DEFINES A GROUP OF ATYPICAL
JRNL TITL 2 ALPHA / BETA-HYDROLASE-FOLD ENZYMES.
JRNL REF NAT.CHEM.BIOL. 2020
JRNL REFN ESSN 1552-4469
JRNL PMID 32601484
JRNL DOI 10.1038/S41589-020-0569-Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 68 352 2012
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 47297
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2373
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.7100 - 3.6000 0.99 2784 146 0.1715 0.1886
REMARK 3 2 3.6000 - 2.8600 1.00 2708 147 0.1510 0.1788
REMARK 3 3 2.8600 - 2.5000 0.98 2646 142 0.1468 0.1631
REMARK 3 4 2.5000 - 2.2700 0.99 2659 141 0.1428 0.1745
REMARK 3 5 2.2700 - 2.1100 1.00 2628 158 0.1407 0.1583
REMARK 3 6 2.1100 - 1.9800 1.00 2668 125 0.1395 0.1880
REMARK 3 7 1.9800 - 1.8800 0.99 2646 137 0.1461 0.1760
REMARK 3 8 1.8800 - 1.8000 0.99 2605 144 0.1547 0.1792
REMARK 3 9 1.8000 - 1.7300 0.99 2636 156 0.1630 0.1589
REMARK 3 10 1.7300 - 1.6700 0.99 2606 145 0.1633 0.1932
REMARK 3 11 1.6700 - 1.6200 1.00 2651 131 0.1686 0.1883
REMARK 3 12 1.6200 - 1.5700 1.00 2614 145 0.1682 0.1953
REMARK 3 13 1.5700 - 1.5300 0.99 2619 127 0.1900 0.2034
REMARK 3 14 1.5300 - 1.4900 0.99 2599 136 0.1959 0.2262
REMARK 3 15 1.4900 - 1.4600 0.99 2617 140 0.2050 0.2521
REMARK 3 16 1.4600 - 1.4300 0.99 2605 122 0.2201 0.2300
REMARK 3 17 1.4300 - 1.4000 0.99 2633 131 0.2282 0.2625
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.117
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.534
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.14
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 : 0.016 2045
REMARK 3 ANGLE : 1.426 2780
REMARK 3 CHIRALITY : 0.106 295
REMARK 3 PLANARITY : 0.013 375
REMARK 3 DIHEDRAL : 15.669 726
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9378 -3.9222 -6.2245
REMARK 3 T TENSOR
REMARK 3 T11: 0.1285 T22: 0.1314
REMARK 3 T33: 0.1159 T12: 0.0173
REMARK 3 T13: 0.0136 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.8450 L22: 5.4227
REMARK 3 L33: 2.2478 L12: 0.6881
REMARK 3 L13: -0.0078 L23: 0.4235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: -0.1179 S13: -0.0440
REMARK 3 S21: 0.0816 S22: -0.0423 S23: 0.1903
REMARK 3 S31: -0.0099 S32: -0.0828 S33: -0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9788 -13.2279 -13.5947
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1011
REMARK 3 T33: 0.1191 T12: 0.0210
REMARK 3 T13: -0.0011 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 2.1644 L22: 3.4254
REMARK 3 L33: 3.6959 L12: 0.0556
REMARK 3 L13: -0.6260 L23: -0.8614
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.0856 S13: -0.1821
REMARK 3 S21: 0.0402 S22: 0.0138 S23: 0.1627
REMARK 3 S31: 0.1085 S32: -0.0835 S33: -0.0034
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8758 -19.2874 -10.6163
REMARK 3 T TENSOR
REMARK 3 T11: 0.1508 T22: 0.1351
REMARK 3 T33: 0.1771 T12: -0.0432
REMARK 3 T13: -0.0200 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.7185 L22: 3.2490
REMARK 3 L33: 5.0642 L12: -1.1239
REMARK 3 L13: -0.4715 L23: -0.0774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0534 S12: 0.0388 S13: -0.2721
REMARK 3 S21: 0.1626 S22: 0.1062 S23: 0.0795
REMARK 3 S31: 0.5483 S32: -0.4885 S33: 0.0256
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7344 2.5973 -15.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1224 T22: 0.1060
REMARK 3 T33: 0.1166 T12: 0.0184
REMARK 3 T13: -0.0038 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 6.2584 L22: 4.4716
REMARK 3 L33: 5.4417 L12: 1.8443
REMARK 3 L13: -2.7810 L23: -2.8462
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: 0.1579 S13: 0.2484
REMARK 3 S21: -0.1084 S22: 0.0867 S23: 0.0085
REMARK 3 S31: -0.0589 S32: -0.0791 S33: -0.0333
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5032 -5.3236 -4.9495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1495 T22: 0.1276
REMARK 3 T33: 0.1239 T12: 0.0264
REMARK 3 T13: -0.0143 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 3.8517 L22: 3.0329
REMARK 3 L33: 5.9376 L12: 0.2503
REMARK 3 L13: -1.0286 L23: -1.7273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: -0.2392 S13: 0.0177
REMARK 3 S21: 0.2075 S22: -0.1288 S23: -0.0774
REMARK 3 S31: 0.0982 S32: 0.2248 S33: 0.0960
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8612 -6.5847 -21.9076
REMARK 3 T TENSOR
REMARK 3 T11: 0.1470 T22: 0.1470
REMARK 3 T33: 0.1453 T12: 0.0190
REMARK 3 T13: 0.0224 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.4691 L22: 1.3407
REMARK 3 L33: 0.8327 L12: -0.5394
REMARK 3 L13: 0.2438 L23: -0.3709
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: 0.1991 S13: 0.0647
REMARK 3 S21: -0.1826 S22: -0.0681 S23: -0.1369
REMARK 3 S31: 0.0150 S32: 0.0811 S33: 0.0502
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1011 -9.5140 -27.6512
REMARK 3 T TENSOR
REMARK 3 T11: 0.1358 T22: 0.1737
REMARK 3 T33: 0.1413 T12: 0.0051
REMARK 3 T13: -0.0062 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 3.6913 L22: 7.0636
REMARK 3 L33: 4.2010 L12: -1.7292
REMARK 3 L13: 0.4071 L23: 1.9455
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.2431 S13: -0.1863
REMARK 3 S21: -0.2927 S22: -0.0035 S23: 0.1887
REMARK 3 S31: 0.0971 S32: -0.0479 S33: 0.0480
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.6262 -3.6574 -16.3111
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1763
REMARK 3 T33: 0.1878 T12: 0.0089
REMARK 3 T13: 0.0137 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 2.7225 L22: 3.0701
REMARK 3 L33: 1.7950 L12: -1.8512
REMARK 3 L13: 1.2107 L23: -1.1976
REMARK 3 S TENSOR
REMARK 3 S11: -0.0817 S12: -0.0833 S13: 0.2479
REMARK 3 S21: 0.0109 S22: 0.0269 S23: -0.3847
REMARK 3 S31: 0.0119 S32: 0.0656 S33: 0.0323
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6161 -19.7282 -22.0473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1603 T22: 0.1527
REMARK 3 T33: 0.1775 T12: 0.0315
REMARK 3 T13: 0.0278 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 3.0331 L22: 2.0183
REMARK 3 L33: 1.8086 L12: 0.2826
REMARK 3 L13: 0.4341 L23: 0.4629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0695 S12: 0.1604 S13: -0.0740
REMARK 3 S21: -0.0706 S22: 0.1129 S23: -0.1683
REMARK 3 S31: 0.0897 S32: 0.1717 S33: -0.0546
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6174 -23.2955 -19.8960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.1156
REMARK 3 T33: 0.1595 T12: 0.0161
REMARK 3 T13: 0.0094 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 4.0364 L22: 5.2324
REMARK 3 L33: 2.6557 L12: 0.9615
REMARK 3 L13: -1.7099 L23: -3.3310
REMARK 3 S TENSOR
REMARK 3 S11: -0.0524 S12: 0.0417 S13: -0.2241
REMARK 3 S21: -0.1651 S22: -0.0105 S23: 0.0154
REMARK 3 S31: 0.1830 S32: 0.0627 S33: 0.0815
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 6T6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104929.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-18
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972420
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47303
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6T6H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.49300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.05450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.71000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.49300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.05450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.71000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.49300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.05450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.71000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.49300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.05450
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.71000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 402 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 435 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 449 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 517 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 580 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 593 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 594 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 596 LIES ON A SPECIAL POSITION.
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 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 VAL A 1
REMARK 465 ARG A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 ASN A 5
REMARK 465 GLY A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 ARG A 9
REMARK 465 GLU A 263
REMARK 465 GLY A 264
REMARK 465 GLY A 265
REMARK 465 HIS A 266
REMARK 465 GLY A 267
REMARK 465 THR A 268
REMARK 465 GLY A 269
REMARK 465 ASP A 270
REMARK 465 ALA A 271
REMARK 465 PRO A 272
REMARK 465 ALA A 273
REMARK 465 GLU A 274
REMARK 465 ALA A 275
REMARK 465 ARG A 276
REMARK 465 THR A 277
REMARK 465 THR A 278
REMARK 465 GLY A 279
REMARK 465 ASP A 280
REMARK 465 ALA A 281
REMARK 465 PRO A 282
REMARK 465 ALA A 283
REMARK 465 GLU A 284
REMARK 465 ALA A 285
REMARK 465 ARG A 286
REMARK 465 ALA A 287
REMARK 465 SER A 288
REMARK 465 GLY A 289
REMARK 465 THR A 290
REMARK 465 GLY A 291
REMARK 465 VAL A 292
REMARK 465 VAL A 293
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 H ASP A 59 O HOH A 409 1.47
REMARK 500 O HOH A 562 O HOH A 576 1.90
REMARK 500 O HOH A 602 O HOH A 617 1.95
REMARK 500 OE1 GLU A 252 O HOH A 401 1.95
REMARK 500 O HOH A 504 O HOH A 516 2.02
REMARK 500 OD1 ASP A 11 O HOH A 403 2.03
REMARK 500 N ARG A 10 O HOH A 404 2.04
REMARK 500 O HOH A 409 O HOH A 601 2.05
REMARK 500 O HOH A 526 O HOH A 570 2.06
REMARK 500 OD1 ASP A 55 O HOH A 405 2.11
REMARK 500 O HOH A 519 O HOH A 612 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 617 O HOH A 617 4555 1.26
REMARK 500 O HOH A 530 O HOH A 564 2455 1.98
REMARK 500 O HOH A 554 O HOH A 612 8544 2.07
REMARK 500 O HOH A 457 O HOH A 491 8544 2.08
REMARK 500 OE1 GLU A 80 NH2 ARG A 249 7454 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 178 CB CYS A 178 SG -0.105
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 ALA A 42 41.25 -98.05
REMARK 500 VAL A 76 -70.98 -123.31
REMARK 500 PHE A 109 -125.64 58.21
REMARK 500 HIS A 195 62.75 -116.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 45 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MQH A 301
DBREF 6T6Y A 2 293 UNP K4MHV9 K4MHV9_9ACTN 2 293
SEQADV 6T6Y HIS A -16 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -15 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -14 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -13 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -12 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -11 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y SER A -10 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y SER A -9 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y GLY A -8 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y LEU A -7 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y VAL A -6 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y PRO A -5 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y ARG A -4 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y GLY A -3 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y SER A -2 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y HIS A -1 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y MET A 0 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Y VAL A 1 UNP K4MHV9 EXPRESSION TAG
SEQRES 1 A 310 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 310 GLY SER HIS MET VAL ARG ASP GLY ASN GLY THR SER ARG
SEQRES 3 A 310 ARG ASP VAL PHE GLU VAL PHE SER ARG ASP GLY THR PRO
SEQRES 4 A 310 ILE ARG GLY PHE SER ARG PRO GLY PRO GLY GLU THR VAL
SEQRES 5 A 310 VAL LEU VAL HIS GLY VAL ALA MET ASP ARG ARG ILE TRP
SEQRES 6 A 310 ALA GLU SER GLY PHE LEU ASP ALA LEU PRO ASP ALA HIS
SEQRES 7 A 310 VAL LEU ALA LEU ASP LEU ARG GLY ARG GLY GLU SER GLY
SEQRES 8 A 310 ARG VAL GLY THR ALA GLU GLY HIS ALA LEU ARG ARG TYR
SEQRES 9 A 310 VAL GLU ASP VAL ARG ALA VAL LEU ASP ARG PHE GLY ARG
SEQRES 10 A 310 ALA ARG TYR SER LEU PHE GLY THR PHE PHE GLY GLY ARG
SEQRES 11 A 310 ILE ALA LEU GLN VAL ALA ALA VAL ASP THR ARG VAL ALA
SEQRES 12 A 310 ARG ALA PHE SER PHE CYS ALA HIS ALA GLU GLN VAL GLU
SEQRES 13 A 310 ILE PRO GLU ASP ALA VAL GLU GLU GLU ALA VAL ALA VAL
SEQRES 14 A 310 GLU GLY PRO GLY GLY HIS ALA TYR LEU ARG ASP HIS PHE
SEQRES 15 A 310 THR GLY ARG GLY ALA PRO PRO TRP MET VAL GLU ALA CYS
SEQRES 16 A 310 ALA ARG VAL ASP PRO GLY GLU LEU GLY ALA ALA THR ARG
SEQRES 17 A 310 GLY LEU LEU HIS GLY SER ASP ARG ARG THR GLU ARG GLY
SEQRES 18 A 310 HIS PRO ASP GLN GLU LEU VAL LEU ILE THR ALA ASP GLY
SEQRES 19 A 310 ASP ALA ASP LEU ALA PRO PHE HIS ALA GLY GLU ARG ARG
SEQRES 20 A 310 LEU GLY ALA HIS LEU TRP LEU VAL ASP ALA PRO THR ARG
SEQRES 21 A 310 ILE LYS ALA ALA GLY ARG LEU ALA GLU VAL GLY ARG ARG
SEQRES 22 A 310 VAL ALA GLY VAL LEU ALA GLU GLY GLY HIS GLY THR GLY
SEQRES 23 A 310 ASP ALA PRO ALA GLU ALA ARG THR THR GLY ASP ALA PRO
SEQRES 24 A 310 ALA GLU ALA ARG ALA SER GLY THR GLY VAL VAL
HET MQH A 301 120
HETNAM MQH BOTTROMYCIN A2
FORMUL 2 MQH C42 H62 N8 O7 S
FORMUL 3 HOH *225(H2 O)
HELIX 1 AA1 ARG A 46 SER A 51 1 6
HELIX 2 AA2 PHE A 53 LEU A 57 5 5
HELIX 3 AA3 ALA A 79 HIS A 82 5 4
HELIX 4 AA4 ALA A 83 GLY A 99 1 17
HELIX 5 AA5 PHE A 109 ASP A 122 1 14
HELIX 6 AA6 PRO A 141 GLY A 154 1 14
HELIX 7 AA7 GLY A 156 ARG A 168 1 13
HELIX 8 AA8 PRO A 171 CYS A 178 1 8
HELIX 9 AA9 ALA A 179 VAL A 181 5 3
HELIX 10 AB1 ASP A 182 LEU A 193 1 12
HELIX 11 AB2 LEU A 221 GLY A 232 1 12
HELIX 12 AB3 THR A 242 ALA A 247 1 6
HELIX 13 AB4 ARG A 249 ALA A 262 1 14
SHEET 1 AA1 8 ASP A 11 PHE A 16 0
SHEET 2 AA1 8 PRO A 22 ARG A 28 -1 O ILE A 23 N VAL A 15
SHEET 3 AA1 8 HIS A 61 LEU A 65 -1 O VAL A 62 N ARG A 28
SHEET 4 AA1 8 THR A 34 VAL A 38 1 N VAL A 35 O LEU A 63
SHEET 5 AA1 8 TYR A 103 THR A 108 1 O SER A 104 N VAL A 36
SHEET 6 AA1 8 VAL A 125 PHE A 131 1 O PHE A 131 N GLY A 107
SHEET 7 AA1 8 GLU A 209 ALA A 215 1 O VAL A 211 N ALA A 128
SHEET 8 AA1 8 HIS A 234 VAL A 238 1 O HIS A 234 N LEU A 212
SITE 1 AC1 11 PHE A 110 ARG A 113 PRO A 141 GLU A 148
SITE 2 AC1 11 HIS A 164 PHE A 165 MET A 174 THR A 190
SITE 3 AC1 11 LEU A 193 ILE A 244 HOH A 414
CRYST1 66.986 80.109 89.420 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014928 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011183 0.00000
TER 3836 ALA A 262
MASTER 569 0 1 13 8 0 3 6 2212 1 120 24
END |