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HEADER HYDROLASE 09-SEP-22 8GU4
TITLE POLY(ETHYLENE TEREPHTHALATE) HYDROLASE (ISPETASE)-LINKER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /
SOURCE 3 TISTR 2288 / 201-F6);
SOURCE 4 ORGANISM_TAXID: 1547922;
SOURCE 5 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 6 GENE: ISF6_4831;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, LYASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.J.XIAO,Z.F.WANG
REVDAT 1 30-NOV-22 8GU4 0
JRNL AUTH Z.CHEN,R.DUAN,Y.XIAO,Y.WEI,H.ZHANG,X.SUN,S.WANG,Y.CHENG,
JRNL AUTH 2 X.WANG,S.TONG,Y.YAO,C.ZHU,H.YANG,Y.WANG,Z.WANG
JRNL TITL BIODEGRADATION OF HIGHLY CRYSTALLIZED POLY(ETHYLENE
JRNL TITL 2 TEREPHTHALATE) THROUGH CELL SURFACE CODISPLAY OF BACTERIAL
JRNL TITL 3 PETASE AND HYDROPHOBIN.
JRNL REF NAT COMMUN V. 13 7138 2022
JRNL REFN ESSN 2041-1723
JRNL PMID 36414665
JRNL DOI 10.1038/S41467-022-34908-Z
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19_4092
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 37913
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1818
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 27.9500 - 3.5300 1.00 2989 156 0.1300 0.1389
REMARK 3 2 3.5200 - 2.8000 1.00 2876 136 0.1471 0.2111
REMARK 3 3 2.8000 - 2.4500 1.00 2835 141 0.1642 0.1842
REMARK 3 4 2.4400 - 2.2200 0.99 2808 140 0.1643 0.2027
REMARK 3 5 2.2200 - 2.0600 0.99 2788 149 0.1607 0.1934
REMARK 3 6 2.0600 - 1.9400 0.98 2772 135 0.1642 0.1961
REMARK 3 7 1.9400 - 1.8400 0.99 2775 122 0.1641 0.1837
REMARK 3 8 1.8400 - 1.7600 0.99 2744 132 0.1649 0.1975
REMARK 3 9 1.7600 - 1.7000 0.98 2762 129 0.1670 0.2209
REMARK 3 10 1.7000 - 1.6400 0.98 2711 150 0.1695 0.2080
REMARK 3 11 1.6400 - 1.5900 0.98 2721 140 0.1702 0.1937
REMARK 3 12 1.5900 - 1.5400 0.97 2685 146 0.1818 0.2024
REMARK 3 13 1.5400 - 1.5000 0.95 2629 142 0.2076 0.2694
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.05
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0135 13.4802 -3.8723
REMARK 3 T TENSOR
REMARK 3 T11: 0.2085 T22: 0.1567
REMARK 3 T33: 0.2241 T12: 0.0552
REMARK 3 T13: 0.0420 T23: 0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 0.7279 L22: 0.6456
REMARK 3 L33: 0.2598 L12: 0.0634
REMARK 3 L13: -0.1610 L23: 0.3644
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: 0.1931 S13: 0.2847
REMARK 3 S21: -0.0305 S22: 0.1345 S23: 0.1465
REMARK 3 S31: -0.2650 S32: -0.2303 S33: -0.0103
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9206 -0.5889 9.6757
REMARK 3 T TENSOR
REMARK 3 T11: 0.0864 T22: 0.0857
REMARK 3 T33: 0.0631 T12: 0.0047
REMARK 3 T13: 0.0241 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.8253 L22: 1.4076
REMARK 3 L33: 1.6826 L12: -0.3303
REMARK 3 L13: 0.2386 L23: 0.0871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.0776 S13: 0.1468
REMARK 3 S21: 0.1894 S22: 0.0320 S23: 0.0035
REMARK 3 S31: -0.1129 S32: -0.1212 S33: -0.0223
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0256 -4.8639 2.0061
REMARK 3 T TENSOR
REMARK 3 T11: 0.0650 T22: 0.0767
REMARK 3 T33: 0.0650 T12: -0.0018
REMARK 3 T13: -0.0043 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.0719 L22: 1.6394
REMARK 3 L33: 0.9653 L12: -0.4762
REMARK 3 L13: -0.2340 L23: -0.1135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0100 S13: 0.0622
REMARK 3 S21: 0.0630 S22: 0.0123 S23: -0.0537
REMARK 3 S31: -0.0462 S32: 0.0839 S33: -0.0050
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2995 -11.0702 3.4177
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.0836
REMARK 3 T33: 0.0806 T12: -0.0147
REMARK 3 T13: -0.0061 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.5195 L22: 1.1527
REMARK 3 L33: 1.6190 L12: -0.7121
REMARK 3 L13: -0.6917 L23: 0.4217
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: 0.0349 S13: -0.0133
REMARK 3 S21: 0.0707 S22: 0.0060 S23: 0.0584
REMARK 3 S31: 0.0970 S32: -0.1220 S33: 0.0175
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0856 0.2150 8.6854
REMARK 3 T TENSOR
REMARK 3 T11: 0.1020 T22: 0.1414
REMARK 3 T33: 0.1220 T12: 0.0132
REMARK 3 T13: 0.0214 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.0724 L22: 0.9873
REMARK 3 L33: 3.4277 L12: -0.1569
REMARK 3 L13: 0.4067 L23: -0.3206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0335 S12: -0.0698 S13: 0.1605
REMARK 3 S21: 0.1871 S22: 0.0741 S23: 0.1674
REMARK 3 S31: -0.1620 S32: -0.3032 S33: -0.0519
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1457 -3.5354 -11.7849
REMARK 3 T TENSOR
REMARK 3 T11: 0.0783 T22: 0.0890
REMARK 3 T33: 0.0829 T12: -0.0019
REMARK 3 T13: -0.0002 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.6234 L22: 0.6896
REMARK 3 L33: 1.0992 L12: -0.0185
REMARK 3 L13: -0.1797 L23: -0.0566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: 0.1040 S13: 0.0565
REMARK 3 S21: -0.0644 S22: -0.0024 S23: -0.0274
REMARK 3 S31: -0.0375 S32: -0.0048 S33: -0.0363
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7185 6.1488 -20.8334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.1559
REMARK 3 T33: 0.1238 T12: 0.0087
REMARK 3 T13: 0.0280 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 3.1420 L22: 1.3674
REMARK 3 L33: 0.5553 L12: -0.5259
REMARK 3 L13: 0.4311 L23: -0.2555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0671 S12: 0.0158 S13: 0.1926
REMARK 3 S21: -0.1568 S22: -0.1164 S23: -0.1087
REMARK 3 S31: -0.0809 S32: 0.0066 S33: 0.0536
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 8GU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1300032143.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-22
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 : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97864
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37971
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 42.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 12.20
REMARK 200 R MERGE (I) : 0.20300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.75800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % W/V PEG 8000, 100 MM MES, SODIUM
REMARK 280 HYDROXIDE, PH 6.0 200 MM ZINC ACETATE, BATCH MODE, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 25.39500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.70000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.39500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.97000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 MET A 0
REMARK 465 GLY A 270
REMARK 465 GLY A 271
REMARK 465 GLY A 272
REMARK 465 SER A 273
REMARK 465 LEU A 274
REMARK 465 GLU A 275
REMARK 465 HIS 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 1 CG CD OE1 NE2
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 ASN A 46 45.27 -144.88
REMARK 500 THR A 61 -9.25 72.04
REMARK 500 SER A 133 -115.65 62.28
REMARK 500 SER A 187 -83.53 -128.65
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 693 DISTANCE = 5.95 ANGSTROMS
DBREF1 8GU4 A 1 263 UNP PETH_IDESA
DBREF2 8GU4 A A0A0K8P6T7 28 290
SEQADV 8GU4 MET A 0 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8GU4 GLY A 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 SER A 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 271 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLY A 272 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 SER A 273 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 LEU A 274 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 GLU A 275 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 276 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 277 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 278 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 279 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 280 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU4 HIS A 281 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 282 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 282 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 282 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 282 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 282 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 282 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 282 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 282 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 282 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 282 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 282 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 282 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 282 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 282 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 282 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 282 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 A 282 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 282 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 282 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 282 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 A 282 ALA ASN CYS SER GLY GLY GLY GLY SER GLY GLY GLY GLY
SEQRES 22 A 282 SER LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *393(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 ARG A 63 LYS A 68 5 6
HELIX 3 AA3 TRP A 69 SER A 76 1 8
HELIX 4 AA4 GLN A 92 GLY A 112 1 21
HELIX 5 AA5 SER A 133 ASN A 146 1 14
HELIX 6 AA6 SER A 187 MET A 195 1 9
HELIX 7 AA7 ASN A 219 ASP A 236 1 18
HELIX 8 AA8 ASP A 238 ARG A 240 5 3
HELIX 9 AA9 TYR A 241 GLU A 247 1 7
SHEET 1 AA1 6 VAL A 25 THR A 29 0
SHEET 2 AA1 6 ALA A 38 PRO A 44 -1 O VAL A 41 N PHE A 28
SHEET 3 AA1 6 VAL A 80 ASP A 85 -1 O VAL A 81 N TYR A 42
SHEET 4 AA1 6 VAL A 51 VAL A 57 1 N ILE A 54 O ILE A 82
SHEET 5 AA1 6 VAL A 122 GLY A 131 1 O ASP A 123 N VAL A 51
SHEET 6 AA1 6 ALA A 151 ALA A 152 1 O ALA A 151 N VAL A 129
SHEET 1 AA2 3 THR A 171 CYS A 176 0
SHEET 2 AA2 3 LYS A 200 ILE A 205 1 O GLN A 201 N ILE A 173
SHEET 3 AA2 3 VAL A 254 ALA A 260 -1 O ASP A 256 N GLU A 204
SSBOND 1 CYS A 176 CYS A 212 1555 1555 2.02
SSBOND 2 CYS A 246 CYS A 262 1555 1555 2.05
CRYST1 50.790 59.940 77.400 90.00 90.00 90.00 P 21 21 21 4
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 0.019689 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016683 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012920 0.00000
TER 1960 GLY A 269
MASTER 366 0 0 9 9 0 0 6 2349 1 4 22
END |