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HEADER HYDROLASE 18-OCT-19 6T6H
TITLE APO STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH
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 6T6H 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. 1.18 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) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 77123
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 3770
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 51.2600 - 3.5300 1.00 2964 141 0.1551 0.1479
REMARK 3 2 3.5300 - 2.8000 1.00 2853 134 0.1482 0.1412
REMARK 3 3 2.8000 - 2.4500 1.00 2806 152 0.1431 0.1550
REMARK 3 4 2.4500 - 2.2200 1.00 2811 131 0.1326 0.1642
REMARK 3 5 2.2200 - 2.0600 1.00 2786 155 0.1407 0.1505
REMARK 3 6 2.0600 - 1.9400 1.00 2788 140 0.1384 0.1575
REMARK 3 7 1.9400 - 1.8400 1.00 2775 143 0.1453 0.1746
REMARK 3 8 1.8400 - 1.7600 1.00 2784 141 0.1507 0.1495
REMARK 3 9 1.7600 - 1.7000 1.00 2803 131 0.1536 0.1556
REMARK 3 10 1.7000 - 1.6400 1.00 2767 142 0.1512 0.1864
REMARK 3 11 1.6400 - 1.5900 1.00 2754 136 0.1548 0.1601
REMARK 3 12 1.5900 - 1.5400 1.00 2778 128 0.1627 0.1734
REMARK 3 13 1.5400 - 1.5000 1.00 2765 154 0.1645 0.2228
REMARK 3 14 1.5000 - 1.4600 1.00 2756 145 0.1688 0.1777
REMARK 3 15 1.4600 - 1.4300 1.00 2745 126 0.1745 0.2426
REMARK 3 16 1.4300 - 1.4000 0.99 2738 141 0.1818 0.1913
REMARK 3 17 1.4000 - 1.3700 1.00 2757 139 0.1861 0.2261
REMARK 3 18 1.3700 - 1.3500 0.99 2719 176 0.1914 0.2159
REMARK 3 19 1.3500 - 1.3200 0.99 2721 142 0.1945 0.1999
REMARK 3 20 1.3200 - 1.3000 0.99 2718 155 0.2005 0.2158
REMARK 3 21 1.3000 - 1.2800 0.99 2714 148 0.2015 0.2063
REMARK 3 22 1.2800 - 1.2600 0.98 2688 132 0.2008 0.2248
REMARK 3 23 1.2600 - 1.2400 0.97 2671 125 0.2147 0.2229
REMARK 3 24 1.2400 - 1.2200 0.96 2632 131 0.2154 0.2138
REMARK 3 25 1.2200 - 1.2100 0.94 2618 138 0.2336 0.2446
REMARK 3 26 1.2100 - 1.1900 0.94 2560 146 0.2407 0.2622
REMARK 3 27 1.1900 - 1.1800 0.69 1882 98 0.2488 0.2504
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) : 0.101
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.669
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.86
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 : 0.011 1987
REMARK 3 ANGLE : 1.139 2694
REMARK 3 CHIRALITY : 0.092 285
REMARK 3 PLANARITY : 0.010 363
REMARK 3 DIHEDRAL : 14.284 714
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7441 -3.9336 -6.2540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.0910
REMARK 3 T33: 0.0772 T12: 0.0152
REMARK 3 T13: 0.0113 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.6972 L22: 2.5361
REMARK 3 L33: 1.5475 L12: 1.1712
REMARK 3 L13: -0.0702 L23: 0.1553
REMARK 3 S TENSOR
REMARK 3 S11: -0.0081 S12: -0.1170 S13: -0.0444
REMARK 3 S21: 0.0732 S22: -0.0107 S23: 0.1566
REMARK 3 S31: -0.0117 S32: -0.0190 S33: 0.0348
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0130 -15.7428 -12.3032
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.0927
REMARK 3 T33: 0.0872 T12: 0.0127
REMARK 3 T13: 0.0098 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.3323 L22: 3.4726
REMARK 3 L33: 4.2965 L12: -0.0402
REMARK 3 L13: -0.0842 L23: -2.1056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0205 S12: -0.0955 S13: -0.0780
REMARK 3 S21: 0.0712 S22: 0.0766 S23: 0.1271
REMARK 3 S31: 0.1017 S32: -0.1105 S33: -0.0631
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5188 -1.6394 -9.8105
REMARK 3 T TENSOR
REMARK 3 T11: 0.0946 T22: 0.0668
REMARK 3 T33: 0.0736 T12: 0.0177
REMARK 3 T13: 0.0048 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 1.5362 L22: 2.6471
REMARK 3 L33: 4.3368 L12: 0.1559
REMARK 3 L13: -0.0304 L23: -2.4218
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: -0.0184 S13: 0.0401
REMARK 3 S21: 0.0578 S22: -0.0776 S23: -0.0480
REMARK 3 S31: 0.0288 S32: 0.1352 S33: 0.0705
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6361 -10.6808 -14.5533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0849 T22: 0.0968
REMARK 3 T33: 0.1077 T12: 0.0154
REMARK 3 T13: -0.0090 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.4321 L22: 1.5969
REMARK 3 L33: 1.6176 L12: -0.2169
REMARK 3 L13: -0.6587 L23: -0.0991
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: -0.0538 S13: 0.0690
REMARK 3 S21: -0.0436 S22: 0.0078 S23: -0.1448
REMARK 3 S31: -0.0561 S32: 0.1195 S33: 0.0023
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6872 -0.3868 -33.2764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1818 T22: 0.2035
REMARK 3 T33: 0.0968 T12: -0.0123
REMARK 3 T13: 0.0204 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 2.3057 L22: 7.0128
REMARK 3 L33: 1.7289 L12: 2.2793
REMARK 3 L13: 1.8681 L23: 2.2265
REMARK 3 S TENSOR
REMARK 3 S11: -0.1195 S12: 0.4222 S13: 0.0268
REMARK 3 S21: -0.3337 S22: 0.1162 S23: -0.1325
REMARK 3 S31: -0.0667 S32: 0.2196 S33: 0.0007
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9101 -9.8067 -27.6895
REMARK 3 T TENSOR
REMARK 3 T11: 0.0868 T22: 0.1033
REMARK 3 T33: 0.0858 T12: -0.0195
REMARK 3 T13: 0.0091 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 4.5981 L22: 8.5722
REMARK 3 L33: 6.8824 L12: -5.0558
REMARK 3 L13: -1.6872 L23: 5.8872
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: 0.1187 S13: -0.1075
REMARK 3 S21: -0.2498 S22: -0.0289 S23: -0.0325
REMARK 3 S31: 0.0641 S32: -0.0119 S33: 0.0571
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0490 -8.5153 -18.8353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1113 T22: 0.1363
REMARK 3 T33: 0.1185 T12: 0.0070
REMARK 3 T13: 0.0025 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.7748 L22: 1.5996
REMARK 3 L33: 0.0591 L12: -0.5363
REMARK 3 L13: -0.0289 L23: -0.1992
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: -0.0636 S13: 0.0679
REMARK 3 S21: 0.0164 S22: 0.0508 S23: -0.2191
REMARK 3 S31: -0.0175 S32: 0.0571 S33: 0.0079
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3209 -20.0752 -21.4381
REMARK 3 T TENSOR
REMARK 3 T11: 0.1172 T22: 0.1026
REMARK 3 T33: 0.1371 T12: 0.0295
REMARK 3 T13: 0.0199 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.9531 L22: 1.1426
REMARK 3 L33: 2.0900 L12: 0.6787
REMARK 3 L13: 0.3606 L23: 0.2792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0264 S13: -0.0561
REMARK 3 S21: -0.0062 S22: 0.0501 S23: -0.1615
REMARK 3 S31: 0.0860 S32: 0.1727 S33: -0.0513
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2639 -23.4094 -19.5801
REMARK 3 T TENSOR
REMARK 3 T11: 0.1442 T22: 0.0784
REMARK 3 T33: 0.1045 T12: 0.0181
REMARK 3 T13: 0.0031 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 2.7463 L22: 2.9189
REMARK 3 L33: 7.2961 L12: 0.4977
REMARK 3 L13: -1.5391 L23: -2.7887
REMARK 3 S TENSOR
REMARK 3 S11: -0.1579 S12: -0.0055 S13: -0.1344
REMARK 3 S21: -0.0720 S22: 0.0785 S23: -0.0183
REMARK 3 S31: 0.1845 S32: -0.1468 S33: 0.0747
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 6T6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-16
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77123
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.170
REMARK 200 RESOLUTION RANGE LOW (A) : 51.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.63400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
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 33.34150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.06650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.34950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.34150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.06650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.34950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.34150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.06650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.34950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.34150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.06650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.34950
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 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 NH1 ARG A 199 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 401 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 533 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 550 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 567 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 637 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 638 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 652 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 712 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 O HOH A 663 O HOH A 688 1.87
REMARK 500 O HOH A 582 O HOH A 653 1.89
REMARK 500 O HOH A 450 O HOH A 630 1.90
REMARK 500 O HOH A 435 O HOH A 476 1.91
REMARK 500 O HOH A 632 O HOH A 665 1.94
REMARK 500 O HOH A 537 O HOH A 622 1.95
REMARK 500 O HOH A 423 O HOH A 527 1.96
REMARK 500 O HOH A 605 O HOH A 654 2.03
REMARK 500 O HOH A 708 O HOH A 716 2.06
REMARK 500 O HOH A 601 O HOH A 635 2.07
REMARK 500 O HOH A 510 O HOH A 563 2.11
REMARK 500 O HOH A 661 O HOH A 702 2.13
REMARK 500 N ARG A 10 O HOH A 402 2.14
REMARK 500 O HOH A 421 O HOH A 671 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 434 O HOH A 446 4555 1.59
REMARK 500 O HOH A 413 O HOH A 635 2455 1.94
REMARK 500 O HOH A 662 O HOH A 673 8544 2.05
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 42.94 -95.72
REMARK 500 VAL A 76 -74.23 -127.90
REMARK 500 PHE A 109 -125.39 56.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 717 DISTANCE = 6.19 ANGSTROMS
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 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 37 O
REMARK 620 2 LEU A 65 O 104.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 305
DBREF 6T6H A 2 293 UNP K4MHV9 K4MHV9_9ACTN 2 293
SEQADV 6T6H HIS A -16 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -15 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -14 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -13 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -12 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -11 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H SER A -10 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H SER A -9 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H GLY A -8 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H LEU A -7 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H VAL A -6 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H PRO A -5 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H ARG A -4 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H GLY A -3 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H SER A -2 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H HIS A -1 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H MET A 0 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6H 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 SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET NA A 305 1
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 NA NA 1+
FORMUL 7 HOH *317(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 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 SER A 130
SHEET 8 AA1 8 HIS A 234 VAL A 238 1 O HIS A 234 N LEU A 212
LINK O LEU A 37 NA NA A 305 1555 1555 2.73
LINK O LEU A 65 NA NA A 305 1555 1555 2.75
SITE 1 AC1 5 ARG A 85 HIS A 195 ARG A 200 HOH A 588
SITE 2 AC1 5 HOH A 599
SITE 1 AC2 7 HIS A 195 ARG A 249 ARG A 255 HOH A 421
SITE 2 AC2 7 HOH A 443 HOH A 532 HOH A 564
SITE 1 AC3 10 ARG A 46 ARG A 180 ASP A 182 PRO A 183
SITE 2 AC3 10 GLY A 184 HOH A 479 HOH A 484 HOH A 487
SITE 3 AC3 10 HOH A 530 HOH A 569
SITE 1 AC4 6 ARG A 18 ARG A 86 HOH A 405 HOH A 407
SITE 2 AC4 6 HOH A 428 HOH A 438
SITE 1 AC5 5 LEU A 37 VAL A 38 HIS A 39 TRP A 48
SITE 2 AC5 5 LEU A 65
CRYST1 66.683 80.133 88.699 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 0.014996 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011274 0.00000
TER 3814 ALA A 262
MASTER 565 0 5 13 8 0 11 6 2267 1 23 24
END |