| content |
HEADER HYDROLASE 20-NOV-13 4CG1
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
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 4CG1 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. 1.40 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) : 1.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.251
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.83
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.17
REMARK 3 NUMBER OF REFLECTIONS : 91150
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1360
REMARK 3 R VALUE (WORKING SET) : 0.1356
REMARK 3 FREE R VALUE : 0.1563
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1907
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 41.2687 - 3.3737 0.98 6329 139 0.1316 0.1216
REMARK 3 2 3.3737 - 2.6780 0.99 6441 131 0.1281 0.1656
REMARK 3 3 2.6780 - 2.3395 0.99 6383 105 0.1155 0.1515
REMARK 3 4 2.3395 - 2.1256 0.99 6457 137 0.1073 0.1231
REMARK 3 5 2.1256 - 1.9732 0.99 6363 154 0.1106 0.1258
REMARK 3 6 1.9732 - 1.8569 0.98 6421 146 0.1137 0.1518
REMARK 3 7 1.8569 - 1.7639 0.99 6324 156 0.1259 0.1492
REMARK 3 8 1.7639 - 1.6871 0.98 6382 142 0.1332 0.1511
REMARK 3 9 1.6871 - 1.6222 0.98 6404 119 0.1521 0.1749
REMARK 3 10 1.6222 - 1.5662 0.98 6370 125 0.1611 0.1962
REMARK 3 11 1.5662 - 1.5172 0.98 6337 160 0.1732 0.2261
REMARK 3 12 1.5172 - 1.4739 0.98 6357 149 0.1859 0.2309
REMARK 3 13 1.4739 - 1.4350 0.98 6344 113 0.2066 0.2255
REMARK 3 14 1.4350 - 1.4000 0.97 6331 131 0.2290 0.2652
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) : 14.54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.1
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 : 0.007 2114
REMARK 3 ANGLE : 1.209 2902
REMARK 3 CHIRALITY : 0.074 325
REMARK 3 PLANARITY : 0.008 378
REMARK 3 DIHEDRAL : 11.292 774
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.3515 44.4283 5.8105
REMARK 3 T TENSOR
REMARK 3 T11: 0.0482 T22: 0.0658
REMARK 3 T33: 0.0961 T12: 0.0014
REMARK 3 T13: 0.0019 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0780 L22: 0.1233
REMARK 3 L33: 0.1999 L12: -0.0696
REMARK 3 L13: -0.0795 L23: 0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0713 S12: 0.0783 S13: 0.0722
REMARK 3 S21: -0.0398 S22: -0.0256 S23: 0.0977
REMARK 3 S31: -0.0783 S32: -0.0794 S33: 0.0220
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 40 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2419 43.9828 3.5730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0495 T22: 0.0466
REMARK 3 T33: 0.0510 T12: 0.0069
REMARK 3 T13: 0.0094 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.0576 L22: 0.1794
REMARK 3 L33: 0.0607 L12: 0.0823
REMARK 3 L13: 0.0216 L23: 0.0799
REMARK 3 S TENSOR
REMARK 3 S11: 0.0210 S12: 0.0590 S13: 0.0984
REMARK 3 S21: -0.0515 S22: -0.0097 S23: 0.0216
REMARK 3 S31: -0.0559 S32: -0.0204 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 93 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.4820 43.5222 11.8446
REMARK 3 T TENSOR
REMARK 3 T11: 0.0596 T22: 0.0499
REMARK 3 T33: 0.0591 T12: -0.0024
REMARK 3 T13: 0.0087 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0206 L22: 0.0217
REMARK 3 L33: 0.0197 L12: 0.0187
REMARK 3 L13: -0.0084 L23: 0.0072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: -0.0316 S13: 0.0527
REMARK 3 S21: 0.0530 S22: -0.0270 S23: -0.0427
REMARK 3 S31: -0.0506 S32: 0.0337 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 110 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3023 46.0769 12.8536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0613 T22: 0.0402
REMARK 3 T33: 0.0459 T12: -0.0014
REMARK 3 T13: 0.0078 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0850 L22: 0.0890
REMARK 3 L33: 0.0207 L12: 0.0801
REMARK 3 L13: 0.0433 L23: 0.0280
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0005 S13: 0.0451
REMARK 3 S21: 0.0073 S22: -0.0202 S23: 0.0666
REMARK 3 S31: 0.0052 S32: 0.0210 S33: -0.0011
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 131 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8747 26.5526 7.6868
REMARK 3 T TENSOR
REMARK 3 T11: 0.0542 T22: 0.0384
REMARK 3 T33: 0.0243 T12: 0.0023
REMARK 3 T13: -0.0022 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.2163 L22: 0.1045
REMARK 3 L33: 0.0514 L12: -0.0216
REMARK 3 L13: -0.0254 L23: 0.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: -0.0014 S13: -0.0588
REMARK 3 S21: 0.0061 S22: -0.0216 S23: -0.0163
REMARK 3 S31: 0.0301 S32: 0.0251 S33: 0.0012
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 204 THROUGH 230 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5941 31.4422 0.4025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.0719
REMARK 3 T33: 0.0320 T12: 0.0219
REMARK 3 T13: -0.0262 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.0267 L22: 0.4227
REMARK 3 L33: 0.1718 L12: -0.0408
REMARK 3 L13: -0.0566 L23: 0.1205
REMARK 3 S TENSOR
REMARK 3 S11: 0.0469 S12: 0.1071 S13: -0.0634
REMARK 3 S21: -0.0746 S22: -0.0598 S23: 0.1649
REMARK 3 S31: 0.0768 S32: -0.0789 S33: -0.0545
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESID 231 THROUGH 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6743 23.4223 6.7650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0764 T22: 0.0614
REMARK 3 T33: 0.1262 T12: -0.0133
REMARK 3 T13: -0.0157 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.1116 L22: 0.2004
REMARK 3 L33: 0.0111 L12: -0.1021
REMARK 3 L13: -0.0324 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0067 S12: 0.0689 S13: -0.1259
REMARK 3 S21: -0.0433 S22: -0.0167 S23: 0.2068
REMARK 3 S31: 0.0583 S32: -0.0634 S33: 0.0078
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 4CG1 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-59032.
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 : 14.2
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118918
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.30
REMARK 200 RESOLUTION RANGE LOW (A) : 41.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.8
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : 0.64
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.50
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 (%): 49.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
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 58.33750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 58.33750
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.86450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.33750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 8.93225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.33750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.79675
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.33750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.33750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.86450
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 58.33750
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 26.79675
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 58.33750
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 8.93225
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 A2036 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2209 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 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 O ARG A 31 O HOH A 2096 2.20
REMARK 500 HD1 HIS A 156 H ASN A 158 1.35
REMARK 500 O HOH A 2076 O HOH A 2083 2.19
REMARK 500 O HOH A 2085 O HOH A 2086 2.14
REMARK 500 O HOH A 2178 O HOH A 2180 2.02
REMARK 500 O HOH A 2184 O HOH A 2195 2.15
REMARK 500 O HOH A 2324 O HOH A 2325 2.09
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 2167 O HOH A 2317 1554 2.18
REMARK 500 O HOH A 2180 O HOH A 2268 4564 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 61 -2.85 73.70
REMARK 500 SER A 130 -119.14 60.67
REMARK 500 THR A 153 56.99 35.49
REMARK 500 HIS A 184 -82.98 -124.77
REMARK 500 PRO A 244 48.29 -84.03
REMARK 500 GLU A 251 -59.84 -126.60
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CG2 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 4CG1 A 1 261 UNP E5BBQ3 E5BBQ3_THEFU 1 261
SEQADV 4CG1 TYR A 262 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 PRO A 263 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 ASN A 264 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 SER A 265 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 SER A 266 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 SER A 267 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 VAL A 268 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 ASP A 269 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 LYS A 270 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 LEU A 271 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 ALA A 272 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 ALA A 273 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 ALA A 274 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 LEU A 275 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 GLU A 276 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 HIS A 277 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 HIS A 278 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 HIS A 279 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 HIS A 280 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 HIS A 281 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG1 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 SO4 A1264 5
HET SO4 A1265 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 3 HOH *340(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 2.05
CISPEP 1 CYS A 241 PRO A 242 0 4.96
CISPEP 2 CYS A 259 PRO A 260 0 13.65
SITE 1 AC1 9 VAL A 24 ARG A 46 ARG A 256 SER A 257
SITE 2 AC1 9 HOH A2074 HOH A2274 HOH A2334 HOH A2335
SITE 3 AC1 9 HOH A2339
SITE 1 AC2 7 SER A 30 ARG A 31 LEU A 32 ARG A 46
SITE 2 AC2 7 ARG A 256 HOH A2077 HOH A2340
CRYST1 116.675 116.675 35.729 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 0.008571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027988 0.00000
TER 4082 PRO A 263
MASTER 436 0 2 11 9 0 5 6 4431 1 12 22
END |