6t6z-pdb | HEADER HYDROLASE 20-OCT-19 6T6Z
TITLE STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH A
TITLE 2 BOTTROMYCIN A2 DERIVATIVE
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 6T6Z 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. 1.70 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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 26135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1295
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 44.5200 - 3.5400 0.97 2874 138 0.1636 0.1980
REMARK 3 2 3.5400 - 2.8100 1.00 2808 143 0.1617 0.1864
REMARK 3 3 2.8100 - 2.4500 1.00 2795 132 0.1543 0.1881
REMARK 3 4 2.4500 - 2.2300 0.99 2765 132 0.1538 0.1965
REMARK 3 5 2.2300 - 2.0700 0.99 2719 156 0.1599 0.2218
REMARK 3 6 2.0700 - 1.9500 0.99 2730 154 0.1704 0.2082
REMARK 3 7 1.9500 - 1.8500 0.99 2694 158 0.2043 0.2627
REMARK 3 8 1.8500 - 1.7700 0.99 2753 132 0.2272 0.2363
REMARK 3 9 1.7700 - 1.7000 0.99 2702 150 0.2460 0.2880
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) : 0.164
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.92
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 2046
REMARK 3 ANGLE : 0.902 2780
REMARK 3 CHIRALITY : 0.050 295
REMARK 3 PLANARITY : 0.005 375
REMARK 3 DIHEDRAL : 12.304 1175
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): -27.7555 -3.8806 -6.2233
REMARK 3 T TENSOR
REMARK 3 T11: 0.1561 T22: 0.1652
REMARK 3 T33: 0.1278 T12: 0.0112
REMARK 3 T13: 0.0051 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.3944 L22: 3.3659
REMARK 3 L33: 1.3787 L12: 0.2384
REMARK 3 L13: -0.1579 L23: 0.1049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: -0.1792 S13: 0.0265
REMARK 3 S21: 0.0359 S22: -0.1452 S23: 0.3105
REMARK 3 S31: 0.0106 S32: -0.0877 S33: 0.0428
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0501 -15.5603 -12.3766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.1322
REMARK 3 T33: 0.1345 T12: 0.0072
REMARK 3 T13: -0.0020 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.5810 L22: 1.9633
REMARK 3 L33: 4.4047 L12: -0.4252
REMARK 3 L13: 0.3534 L23: -0.4866
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.0819 S13: -0.0917
REMARK 3 S21: -0.0125 S22: 0.0435 S23: 0.1105
REMARK 3 S31: 0.1752 S32: -0.1897 S33: -0.0459
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5874 2.5500 -15.8516
REMARK 3 T TENSOR
REMARK 3 T11: 0.1298 T22: 0.1300
REMARK 3 T33: 0.1465 T12: 0.0223
REMARK 3 T13: -0.0263 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 3.0310 L22: 6.6735
REMARK 3 L33: 4.8294 L12: 2.9480
REMARK 3 L13: -3.7866 L23: -3.1493
REMARK 3 S TENSOR
REMARK 3 S11: -0.1053 S12: 0.1591 S13: 0.2872
REMARK 3 S21: -0.1767 S22: 0.1903 S23: 0.2981
REMARK 3 S31: 0.1172 S32: -0.1116 S33: -0.0759
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2862 -5.2158 -4.9256
REMARK 3 T TENSOR
REMARK 3 T11: 0.1544 T22: 0.1246
REMARK 3 T33: 0.1148 T12: 0.0183
REMARK 3 T13: -0.0171 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 3.9761 L22: 2.5396
REMARK 3 L33: 5.9075 L12: -0.2123
REMARK 3 L13: -0.7882 L23: -1.4922
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: -0.2512 S13: -0.0590
REMARK 3 S21: 0.2334 S22: -0.1773 S23: -0.0192
REMARK 3 S31: 0.0251 S32: 0.2222 S33: 0.1191
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6864 -10.6230 -14.5746
REMARK 3 T TENSOR
REMARK 3 T11: 0.1102 T22: 0.1070
REMARK 3 T33: 0.1450 T12: 0.0175
REMARK 3 T13: -0.0047 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.1621 L22: 1.7251
REMARK 3 L33: 1.3750 L12: -0.4518
REMARK 3 L13: 0.2981 L23: -0.2157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0090 S13: 0.0285
REMARK 3 S21: -0.0809 S22: 0.0072 S23: -0.1677
REMARK 3 S31: -0.0091 S32: 0.1091 S33: 0.0352
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6798 -0.2538 -33.1633
REMARK 3 T TENSOR
REMARK 3 T11: 0.2180 T22: 0.2594
REMARK 3 T33: 0.1458 T12: 0.0231
REMARK 3 T13: 0.0129 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 2.1144 L22: 2.8225
REMARK 3 L33: 1.2820 L12: -0.0349
REMARK 3 L13: 0.5324 L23: 0.2771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0604 S12: 0.5460 S13: 0.1967
REMARK 3 S21: -0.3767 S22: -0.0849 S23: 0.0459
REMARK 3 S31: -0.0019 S32: 0.3570 S33: 0.0696
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8469 -9.5128 -27.6583
REMARK 3 T TENSOR
REMARK 3 T11: 0.1512 T22: 0.1576
REMARK 3 T33: 0.1547 T12: -0.0031
REMARK 3 T13: 0.0159 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.9908 L22: 7.5983
REMARK 3 L33: 3.8933 L12: -2.4395
REMARK 3 L13: 0.2514 L23: 3.2458
REMARK 3 S TENSOR
REMARK 3 S11: 0.1041 S12: 0.1534 S13: -0.0227
REMARK 3 S21: -0.2104 S22: -0.1260 S23: -0.0960
REMARK 3 S31: 0.0653 S32: -0.0378 S33: -0.0011
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4015 -3.5786 -16.3239
REMARK 3 T TENSOR
REMARK 3 T11: 0.1540 T22: 0.1668
REMARK 3 T33: 0.1457 T12: -0.0135
REMARK 3 T13: 0.0030 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 2.8903 L22: 3.1665
REMARK 3 L33: 2.7581 L12: -2.2074
REMARK 3 L13: 1.7265 L23: -2.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.1188 S12: -0.0971 S13: 0.2491
REMARK 3 S21: 0.1575 S22: 0.0094 S23: -0.3714
REMARK 3 S31: -0.1875 S32: 0.1929 S33: 0.1053
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3558 -19.6314 -22.0102
REMARK 3 T TENSOR
REMARK 3 T11: 0.1314 T22: 0.1327
REMARK 3 T33: 0.1549 T12: 0.0355
REMARK 3 T13: 0.0066 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 2.6249 L22: 1.6057
REMARK 3 L33: 2.0895 L12: 0.9337
REMARK 3 L13: 0.4850 L23: 0.7702
REMARK 3 S TENSOR
REMARK 3 S11: -0.0831 S12: 0.0702 S13: -0.0573
REMARK 3 S21: -0.0269 S22: 0.1289 S23: -0.1408
REMARK 3 S31: 0.1142 S32: 0.1714 S33: -0.0361
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2696 -23.1914 -19.7897
REMARK 3 T TENSOR
REMARK 3 T11: 0.1907 T22: 0.1265
REMARK 3 T33: 0.1585 T12: 0.0194
REMARK 3 T13: -0.0013 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 2.1429 L22: 3.0651
REMARK 3 L33: 8.0705 L12: 0.4297
REMARK 3 L13: -1.5500 L23: -2.9686
REMARK 3 S TENSOR
REMARK 3 S11: -0.2670 S12: 0.0190 S13: -0.1462
REMARK 3 S21: -0.2436 S22: -0.0309 S23: -0.2086
REMARK 3 S31: 0.5609 S32: -0.1441 S33: 0.2452
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 6T6Z 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_1292104927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-17
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 : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873130
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26141
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.77800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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 (%): 31.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78
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 33.35800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.76500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.51600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.35800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.76500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.51600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.35800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.76500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.51600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.35800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.76500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.51600
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: 10310 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 403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 496 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 498 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 503 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 559 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 595 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 602 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 639 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 HH22 ARG A 46 O HOH A 408 1.51
REMARK 500 N ARG A 10 O HOH A 401 1.92
REMARK 500 O HOH A 532 O HOH A 613 1.92
REMARK 500 O HOH A 487 O HOH A 605 2.06
REMARK 500 O HOH A 434 O HOH A 447 2.10
REMARK 500 OE2 GLU A 252 O HOH A 402 2.11
REMARK 500 O HOH A 404 O HOH A 589 2.12
REMARK 500 O HOH A 597 O HOH A 601 2.14
REMARK 500 O HOH A 464 O HOH A 487 2.16
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 441 O HOH A 486 4555 1.76
REMARK 500 O HOH A 619 O HOH A 626 8544 1.86
REMARK 500 O HOH A 591 O HOH A 608 2455 1.89
REMARK 500 O HOH A 521 O HOH A 521 3455 1.96
REMARK 500 O HOH A 584 O HOH A 613 8544 2.03
REMARK 500 O HOH A 584 O HOH A 627 8544 2.11
REMARK 500 O HOH A 424 O HOH A 521 4555 2.19
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 40.63 -96.61
REMARK 500 LEU A 57 78.98 -117.00
REMARK 500 VAL A 76 -70.32 -124.78
REMARK 500 PHE A 109 -122.67 56.97
REMARK 500 HIS A 195 59.07 -118.55
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 MRB A 301
DBREF 6T6Z A 2 293 UNP K4MHV9 K4MHV9_9ACTN 2 293
SEQADV 6T6Z HIS A -16 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -15 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -14 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -13 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -12 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -11 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z SER A -10 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z SER A -9 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z GLY A -8 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z LEU A -7 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z VAL A -6 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z PRO A -5 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z ARG A -4 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z GLY A -3 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z SER A -2 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z HIS A -1 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z MET A 0 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6Z 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 MRB A 301 121
HETNAM MRB BOTTROMYCIN A2 DERIVATIVE
FORMUL 2 MRB C42 H62 N8 O7 S2
FORMUL 3 HOH *246(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 PHE A 106 N VAL A 38
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 SER A 130
SHEET 8 AA1 8 HIS A 234 VAL A 238 1 O HIS A 234 N LEU A 212
SITE 1 AC1 15 PHE A 109 PHE A 110 ARG A 113 PRO A 141
SITE 2 AC1 15 GLU A 148 TYR A 160 LEU A 161 HIS A 164
SITE 3 AC1 15 PHE A 165 THR A 190 LEU A 193 SER A 197
SITE 4 AC1 15 HOH A 407 HOH A 531 HOH A 545
CRYST1 66.716 79.530 89.032 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 0.014989 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011232 0.00000
TER 3836 ALA A 262
MASTER 527 0 1 13 8 0 4 6 2234 1 121 24
END
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