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HEADER HYDROLASE 20-NOV-13 4CG2
TITLE STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
TITLE 2 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
TITLE 3 THERMOBIFIDA FUSCA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.74;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: S-O LINK BEWEEN S130 UND PMS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 2021;
SOURCE 4 STRAIN: KW3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET DEGRADATION, HYDROLASE, ALPHA BETA FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ROTH,R.WEI,T.OESER,J.THEN,C.FOELLNER,W.ZIMMERMANN, N.STRAETER
REVDAT 1 25-JUN-14 4CG2 0
JRNL AUTH C.ROTH,R.WEI,T.OESER,J.THEN,C.FOLLNER,W.ZIMMERMANN,N.STRATER
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
JRNL TITL 2 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
JRNL TITL 3 THERMOBIFIDA FUSCA.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2014
JRNL REFN ESSN 1432-0614
JRNL PMID 24728714
JRNL DOI 10.1007/S00253-014-5672-0
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.437
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.503
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.29
REMARK 3 NUMBER OF REFLECTIONS : 43606
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1406
REMARK 3 R VALUE (WORKING SET) : 0.1380
REMARK 3 FREE R VALUE : 0.1661
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3940
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 19.5049 - 4.3487 1.00 1497 149 0.1458 0.1693
REMARK 3 2 4.3487 - 3.4579 1.00 1497 121 0.1149 0.1438
REMARK 3 3 3.4579 - 3.0227 1.00 1421 168 0.1363 0.1481
REMARK 3 4 3.0227 - 2.7471 1.00 1442 131 0.1366 0.1947
REMARK 3 5 2.7471 - 2.5507 1.00 1430 149 0.1250 0.1569
REMARK 3 6 2.5507 - 2.4006 1.00 1440 141 0.1219 0.1383
REMARK 3 7 2.4006 - 2.2805 1.00 1444 130 0.1178 0.1571
REMARK 3 8 2.2805 - 2.1814 1.00 1423 153 0.1139 0.1303
REMARK 3 9 2.1814 - 2.0975 1.00 1412 131 0.1188 0.1334
REMARK 3 10 2.0975 - 2.0252 1.00 1459 130 0.1252 0.1339
REMARK 3 11 2.0252 - 1.9620 1.00 1408 133 0.1244 0.1563
REMARK 3 12 1.9620 - 1.9059 1.00 1445 141 0.1230 0.1550
REMARK 3 13 1.9059 - 1.8558 1.00 1410 156 0.1287 0.1627
REMARK 3 14 1.8558 - 1.8105 1.00 1405 142 0.1283 0.1364
REMARK 3 15 1.8105 - 1.7694 1.00 1417 147 0.1319 0.1666
REMARK 3 16 1.7694 - 1.7318 1.00 1396 146 0.1462 0.1700
REMARK 3 17 1.7318 - 1.6972 1.00 1408 120 0.1408 0.1487
REMARK 3 18 1.6972 - 1.6652 1.00 1456 134 0.1492 0.1899
REMARK 3 19 1.6652 - 1.6354 1.00 1428 131 0.1530 0.1979
REMARK 3 20 1.6354 - 1.6077 1.00 1397 140 0.1595 0.2022
REMARK 3 21 1.6077 - 1.5818 1.00 1437 132 0.1667 0.2111
REMARK 3 22 1.5818 - 1.5575 1.00 1382 151 0.1687 0.1939
REMARK 3 23 1.5575 - 1.5346 0.99 1394 134 0.1774 0.2199
REMARK 3 24 1.5346 - 1.5130 0.99 1439 151 0.1916 0.2433
REMARK 3 25 1.5130 - 1.4925 1.00 1409 144 0.2035 0.2199
REMARK 3 26 1.4925 - 1.4732 0.99 1392 149 0.2167 0.2453
REMARK 3 27 1.4732 - 1.4547 1.00 1378 170 0.2267 0.2480
REMARK 3 28 1.4547 - 1.4372 0.86 1200 116 0.2813 0.3360
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) : 0.14
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.07
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.7
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 : 0.008 2121
REMARK 3 ANGLE : 1.260 2910
REMARK 3 CHIRALITY : 0.072 321
REMARK 3 PLANARITY : 0.008 376
REMARK 3 DIHEDRAL : 11.752 775
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 1:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0113 36.7760 11.3800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0855
REMARK 3 T33: 0.0640 T12: -0.0048
REMARK 3 T13: 0.0017 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0028 L22: -0.0003
REMARK 3 L33: 0.0010 L12: 0.0010
REMARK 3 L13: 0.0017 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: 0.0130 S13: -0.0069
REMARK 3 S21: 0.0119 S22: 0.0157 S23: 0.0530
REMARK 3 S31: -0.0122 S32: -0.0128 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 14:26)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8736 43.1148 -0.1492
REMARK 3 T TENSOR
REMARK 3 T11: 0.0248 T22: 0.0779
REMARK 3 T33: 0.0581 T12: 0.0240
REMARK 3 T13: -0.0250 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0084
REMARK 3 L33: 0.0026 L12: -0.0024
REMARK 3 L13: 0.0023 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.0380 S13: 0.0120
REMARK 3 S21: -0.0090 S22: -0.0085 S23: 0.0007
REMARK 3 S31: 0.0091 S32: -0.0049 S33: 0.0043
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 27:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.2501 47.2910 4.5512
REMARK 3 T TENSOR
REMARK 3 T11: 0.0373 T22: -0.0424
REMARK 3 T33: 0.0148 T12: -0.0116
REMARK 3 T13: 0.0381 T23: 0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 0.0073 L22: 0.0059
REMARK 3 L33: 0.0110 L12: 0.0066
REMARK 3 L13: -0.0140 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: 0.0158 S13: 0.0698
REMARK 3 S21: -0.0432 S22: -0.0179 S23: -0.0116
REMARK 3 S31: -0.0504 S32: -0.0099 S33: -0.0338
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 70:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1460 43.4130 3.5219
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: 0.0350
REMARK 3 T33: 0.0347 T12: 0.0074
REMARK 3 T13: 0.0050 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: 0.0032
REMARK 3 L33: 0.0033 L12: 0.0001
REMARK 3 L13: -0.0014 L23: 0.0041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0180 S13: 0.0129
REMARK 3 S21: -0.0252 S22: -0.0180 S23: -0.0349
REMARK 3 S31: -0.0441 S32: -0.0007 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 89:113)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7915 44.6557 10.2736
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.0425
REMARK 3 T33: 0.0583 T12: -0.0044
REMARK 3 T13: 0.0091 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.0019 L22: 0.0044
REMARK 3 L33: 0.0024 L12: 0.0039
REMARK 3 L13: -0.0003 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.0023 S13: 0.0208
REMARK 3 S21: 0.0119 S22: -0.0196 S23: -0.0204
REMARK 3 S31: -0.0260 S32: 0.0233 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 114:240)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7897 30.3085 6.8245
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0492
REMARK 3 T33: 0.0370 T12: 0.0026
REMARK 3 T13: -0.0043 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.0810 L22: 0.0630
REMARK 3 L33: 0.0283 L12: 0.0196
REMARK 3 L13: 0.0001 L23: -0.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: 0.0204 S13: -0.0297
REMARK 3 S21: 0.0045 S22: -0.0365 S23: 0.0141
REMARK 3 S31: -0.0028 S32: 0.0031 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 241:245)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6643 18.9502 4.5628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0623 T22: 0.0625
REMARK 3 T33: 0.0909 T12: -0.0187
REMARK 3 T13: -0.0130 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0036
REMARK 3 L33: 0.0008 L12: 0.0012
REMARK 3 L13: 0.0006 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: 0.0039 S13: 0.0013
REMARK 3 S21: -0.0013 S22: 0.0003 S23: 0.0019
REMARK 3 S31: 0.0008 S32: -0.0013 S33: -0.0033
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 248:253)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8304 20.1811 -6.5986
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.1187
REMARK 3 T33: 0.1051 T12: -0.0207
REMARK 3 T13: -0.0295 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0001
REMARK 3 L33: 0.0001 L12: 0.0000
REMARK 3 L13: 0.0001 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: 0.0044 S13: -0.0010
REMARK 3 S21: -0.0054 S22: 0.0000 S23: 0.0013
REMARK 3 S31: 0.0022 S32: -0.0038 S33: 0.0021
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 254:263)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8622 20.1893 11.0611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0512 T22: 0.0212
REMARK 3 T33: 0.0870 T12: -0.0114
REMARK 3 T13: 0.0018 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: 0.0033
REMARK 3 L33: 0.0010 L12: 0.0003
REMARK 3 L13: 0.0011 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: -0.0064 S13: 0.0057
REMARK 3 S21: 0.0030 S22: -0.0031 S23: 0.0019
REMARK 3 S31: -0.0005 S32: -0.0021 S33: -0.0045
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 4CG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-13.
REMARK 100 THE PDBE ID CODE IS EBI-59040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43954
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.44
REMARK 200 RESOLUTION RANGE LOW (A) : 19.50
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 16.3
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 13.4
REMARK 200 R MERGE FOR SHELL (I) : 1.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JFR
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 58.29550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 58.29550
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.79050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.29550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 8.89525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.29550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.68575
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.29550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.29550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.79050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 58.29550
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 26.68575
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 58.29550
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 8.89525
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 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 A2092 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 ASP A 246
REMARK 465 GLY A 247
REMARK 465 ASN A 264
REMARK 465 SER A 265
REMARK 465 SER A 266
REMARK 465 SER A 267
REMARK 465 VAL A 268
REMARK 465 ASP A 269
REMARK 465 LYS A 270
REMARK 465 LEU A 271
REMARK 465 ALA A 272
REMARK 465 ALA A 273
REMARK 465 ALA A 274
REMARK 465 LEU A 275
REMARK 465 GLU A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG A SER A 25 O HOH A 2075 2.15
REMARK 500 O ARG A 31 O HOH A 2097 2.09
REMARK 500 O ALA A 34 O HOH A 2097 2.18
REMARK 500 HE ARG A 110 O HOH A 2107 1.56
REMARK 500 O1SB PMS A 1130 O HOH A 2212 2.03
REMARK 500 O HOH A 2017 O HOH A 2038 2.17
REMARK 500 O HOH A 2073 O HOH A 2081 2.11
REMARK 500 O HOH A 2087 O HOH A 2088 2.09
REMARK 500 O HOH A 2102 O HOH A 2122 2.00
REMARK 500 O HOH A 2122 O HOH A 2212 1.91
REMARK 500 O HOH A 2129 O HOH A 2221 2.16
REMARK 500 O HOH A 2193 O HOH A 2194 2.11
REMARK 500 O HOH A 2217 O HOH A 2218 2.10
REMARK 500 O HOH A 2225 O HOH A 2228 2.08
REMARK 500 O HOH A 2225 O HOH A 2227 2.16
REMARK 500 O HOH A 2286 O HOH A 2323 2.19
REMARK 500 O HOH A 2304 O HOH A 2329 2.04
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 61 -3.62 71.82
REMARK 500 SER A 130 -118.01 57.76
REMARK 500 THR A 153 56.62 36.08
REMARK 500 HIS A 184 -83.65 -125.53
REMARK 500 PRO A 244 49.47 -81.50
REMARK 500 GLU A 251 -58.11 -126.26
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 SO4 A1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1267
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CG1 RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
REMARK 900 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
REMARK 900 THERMOBIFIDA FUSCA
REMARK 900 RELATED ID: 4CG3 RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
REMARK 900 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
REMARK 900 THERMOBIFIDA FUSCA
DBREF 4CG2 A 1 261 UNP E5BBQ3 E5BBQ3_THEFU 1 261
SEQADV 4CG2 TYR A 262 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 PRO A 263 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 ASN A 264 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 SER A 265 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 SER A 266 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 SER A 267 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 VAL A 268 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 ASP A 269 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 LYS A 270 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 LEU A 271 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 ALA A 272 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 ALA A 273 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 ALA A 274 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 LEU A 275 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 GLU A 276 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 277 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 278 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 279 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 280 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 281 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG2 HIS A 282 UNP E5BBQ3 EXPRESSION TAG
SEQRES 1 A 282 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 A 282 LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 A 282 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 A 282 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 A 282 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 A 282 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 A 282 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 A 282 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 A 282 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 A 282 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 A 282 MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG
SEQRES 12 A 282 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 A 282 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 A 282 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 A 282 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 282 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 A 282 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 A 282 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 A 282 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 A 282 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 A 282 PHE TYR PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA
SEQRES 22 A 282 ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET PMS A1130 10
HET SO4 A1264 5
HET SO4 A1265 5
HET SO4 A1266 5
HET SO4 A1267 5
HETNAM PMS PHENYLMETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 2 PMS C7 H8 O3 S
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 4 HOH *338(H2 O)
HELIX 1 1 THR A 11 ALA A 17 1 7
HELIX 2 2 THR A 63 SER A 66 5 4
HELIX 3 3 ILE A 67 SER A 76 1 10
HELIX 4 4 GLN A 92 ARG A 110 1 19
HELIX 5 5 SER A 112 SER A 117 1 6
HELIX 6 6 SER A 130 ARG A 143 1 14
HELIX 7 7 HIS A 184 LEU A 192 1 9
HELIX 8 8 PHE A 209 ILE A 213 5 5
HELIX 9 9 ASN A 215 ASP A 231 1 17
HELIX 10 10 ASP A 233 ARG A 235 5 3
HELIX 11 11 TYR A 236 CYS A 241 1 6
SHEET 1 AA 6 VAL A 24 VAL A 29 0
SHEET 2 AA 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA 6 VAL A 80 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA 6 TYR A 51 SER A 57 1 O GLY A 52 N VAL A 80
SHEET 5 AA 6 ILE A 119 HIS A 129 1 N ASP A 120 O TYR A 51
SHEET 6 AA 6 ALA A 148 LEU A 152 1 O ALA A 148 N VAL A 126
SHEET 1 AB 3 THR A 168 ALA A 173 0
SHEET 2 AB 3 LYS A 198 LEU A 203 1 O ALA A 199 N ILE A 170
SHEET 3 AB 3 VAL A 252 SER A 257 -1 N GLU A 253 O GLU A 202
SSBOND 1 CYS A 241 CYS A 259 1555 1555 2.06
LINK OG BSER A 130 S BPMS A1130 1555 1555 1.50
CISPEP 1 CYS A 241 PRO A 242 0 4.54
CISPEP 2 CYS A 259 PRO A 260 0 12.69
SITE 1 AC1 9 SER A 30 ARG A 31 LEU A 32 ARG A 46
SITE 2 AC1 9 ARG A 256 HOH A2075 HOH A2271 HOH A2331
SITE 3 AC1 9 HOH A2332
SITE 1 AC2 6 ALA A 17 ARG A 18 HOH A2002 HOH A2057
SITE 2 AC2 6 HOH A2333 HOH A2334
SITE 1 AC3 10 ALA A 34 PRO A 193 SER A 194 SER A 195
SITE 2 AC3 10 HOH A2097 HOH A2111 HOH A2270 HOH A2280
SITE 3 AC3 10 HOH A2336 HOH A2337
SITE 1 AC4 8 VAL A 24 ARG A 46 ARG A 256 SER A 257
SITE 2 AC4 8 HOH A2072 HOH A2267 HOH A2320 HOH A2328
CRYST1 116.591 116.591 35.581 90.00 90.00 90.00 I 41 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 0.008577 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028105 0.00000
TER 4047 PRO A 263
MASTER 478 0 5 11 9 0 10 6 4414 1 33 22
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