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HEADER HYDROLASE 12-APR-23 8J17
TITLE CRYSTAL STRUCTURE OF ISPETASE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ISPETASE, 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;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS POLYETHYLENE TEREPHTHALATE (PET), ISPETASE, PET DEGRADATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.D.YIN,Y.X.WANG
REVDAT 1 29-NOV-23 8J17 0
JRNL AUTH Q.YIN,J.ZHANG,S.MA,T.GU,M.WANG,S.YOU,S.YE,R.SU,Y.WANG,W.QI
JRNL TITL EFFICIENT POLYETHYLENE TEREPHTHALATE BIODEGRADATION BY AN
JRNL TITL 2 ENGINEERED IDEONELLA SAKAIENSIS PETASE WITH A FIXED
JRNL TITL 3 SUBSTRATE-BINDING W156 RESIDUE
JRNL REF GREEN CHEM 2013
JRNL REFN ISSN 1463-9262
JRNL DOI 10.1039/D3GC03663D
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 71705
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 3529
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 40.9200 - 5.7600 0.99 2934 142 0.1599 0.1882
REMARK 3 2 5.7500 - 4.5700 1.00 2810 149 0.1402 0.1555
REMARK 3 3 4.5700 - 3.9900 1.00 2771 145 0.1313 0.1688
REMARK 3 4 3.9900 - 3.6300 1.00 2759 152 0.1378 0.1762
REMARK 3 5 3.6300 - 3.3700 1.00 2751 156 0.1632 0.2210
REMARK 3 6 3.3700 - 3.1700 1.00 2719 154 0.1806 0.2000
REMARK 3 7 3.1700 - 3.0100 1.00 2758 139 0.1911 0.2256
REMARK 3 8 3.0100 - 2.8800 1.00 2725 122 0.1991 0.2710
REMARK 3 9 2.8800 - 2.7700 1.00 2708 138 0.2076 0.2638
REMARK 3 10 2.7700 - 2.6700 1.00 2734 145 0.1938 0.2483
REMARK 3 11 2.6700 - 2.5900 1.00 2731 133 0.1931 0.2115
REMARK 3 12 2.5900 - 2.5200 1.00 2697 135 0.1871 0.2553
REMARK 3 13 2.5200 - 2.4500 1.00 2742 132 0.1955 0.2305
REMARK 3 14 2.4500 - 2.3900 1.00 2682 120 0.1862 0.2489
REMARK 3 15 2.3900 - 2.3400 1.00 2770 128 0.1905 0.2517
REMARK 3 16 2.3400 - 2.2900 1.00 2654 152 0.1915 0.2392
REMARK 3 17 2.2900 - 2.2400 1.00 2747 131 0.2076 0.2539
REMARK 3 18 2.2400 - 2.2000 1.00 2681 135 0.2138 0.2613
REMARK 3 19 2.2000 - 2.1600 1.00 2719 146 0.2247 0.2834
REMARK 3 20 2.1600 - 2.1200 1.00 2680 138 0.2383 0.2790
REMARK 3 21 2.1200 - 2.0900 1.00 2675 156 0.2448 0.2941
REMARK 3 22 2.0900 - 2.0600 1.00 2687 150 0.2700 0.3444
REMARK 3 23 2.0600 - 2.0300 1.00 2653 140 0.2802 0.2795
REMARK 3 24 2.0300 - 2.0000 1.00 2713 141 0.3084 0.3409
REMARK 3 25 2.0000 - 1.9700 0.99 2676 150 0.3309 0.3543
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) : 0.216
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.907
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.91
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 5908
REMARK 3 ANGLE : 0.824 8054
REMARK 3 CHIRALITY : 0.054 888
REMARK 3 PLANARITY : 0.006 1066
REMARK 3 DIHEDRAL : 16.461 2092
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 8J17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1300037008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL10U2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71765
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 58.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES-NAOH, 1.7M MGSO4, PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 81.84500
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 81.84500
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 26.28000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 116.90000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.28000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 116.90000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 81.84500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.28000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.90000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 81.84500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.28000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 116.90000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 B 474 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 MET A -2
REMARK 465 GLN A -1
REMARK 465 LEU A 262
REMARK 465 GLU A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 MET B -2
REMARK 465 GLN B -1
REMARK 465 LEU B 262
REMARK 465 GLU B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 MET C -2
REMARK 465 GLN C -1
REMARK 465 LEU C 262
REMARK 465 GLU C 263
REMARK 465 HIS C 264
REMARK 465 HIS C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
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 SER A 131 -119.69 65.47
REMARK 500 ALA A 180 75.00 -116.99
REMARK 500 SER A 185 -82.97 -126.28
REMARK 500 SER B 131 -117.36 61.69
REMARK 500 SER B 185 -82.86 -130.70
REMARK 500 SER C 131 -117.67 63.95
REMARK 500 SER C 185 -78.06 -124.96
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 621 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A 622 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A 623 DISTANCE = 6.75 ANGSTROMS
DBREF1 8J17 A -1 261 UNP PETH_IDESA
DBREF2 8J17 A A0A0K8P6T7 28 290
DBREF1 8J17 B -1 261 UNP PETH_IDESA
DBREF2 8J17 B A0A0K8P6T7 28 290
DBREF1 8J17 C -1 261 UNP PETH_IDESA
DBREF2 8J17 C A0A0K8P6T7 28 290
SEQADV 8J17 MET A -2 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8J17 PRO A 92 UNP A0A0K8P6T SER 121 VARIANT
SEQADV 8J17 ALA A 157 UNP A0A0K8P6T ASP 186 VARIANT
SEQADV 8J17 LEU A 262 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 GLU A 263 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS A 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 MET B -2 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8J17 PRO B 92 UNP A0A0K8P6T SER 121 VARIANT
SEQADV 8J17 ALA B 157 UNP A0A0K8P6T ASP 186 VARIANT
SEQADV 8J17 LEU B 262 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 GLU B 263 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS B 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 MET C -2 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8J17 PRO C 92 UNP A0A0K8P6T SER 121 VARIANT
SEQADV 8J17 ALA C 157 UNP A0A0K8P6T ASP 186 VARIANT
SEQADV 8J17 LEU C 262 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 GLU C 263 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J17 HIS C 269 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO PRO SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ALA SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 B 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 B 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 B 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 B 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 B 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 B 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 B 272 ASP GLN PRO PRO SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 B 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 B 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 B 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 B 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 B 272 ALA PRO TRP ALA SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 B 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 B 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 B 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 B 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 B 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 B 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 B 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 B 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 C 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 C 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 C 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 C 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 C 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 C 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 C 272 ASP GLN PRO PRO SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 C 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 C 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 C 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 C 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 C 272 ALA PRO TRP ALA SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 C 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 C 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 C 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 C 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 C 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 C 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 C 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 C 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 4 HOH *761(H2 O)
HELIX 1 AA1 THR A 10 ALA A 16 1 7
HELIX 2 AA2 ARG A 61 LYS A 66 5 6
HELIX 3 AA3 TRP A 67 SER A 74 1 8
HELIX 4 AA4 GLN A 90 GLY A 110 1 21
HELIX 5 AA5 SER A 131 ASN A 144 1 14
HELIX 6 AA6 SER A 185 MET A 193 1 9
HELIX 7 AA7 ASN A 217 ASP A 234 1 18
HELIX 8 AA8 ASP A 236 ARG A 238 5 3
HELIX 9 AA9 TYR A 239 GLU A 245 1 7
HELIX 10 AB1 THR B 10 ALA B 16 1 7
HELIX 11 AB2 ARG B 61 LYS B 66 1 6
HELIX 12 AB3 TRP B 67 SER B 74 1 8
HELIX 13 AB4 GLN B 90 GLY B 110 1 21
HELIX 14 AB5 SER B 131 ASN B 144 1 14
HELIX 15 AB6 PRO B 181 SER B 184 5 4
HELIX 16 AB7 SER B 185 MET B 193 1 9
HELIX 17 AB8 ASN B 217 ASP B 234 1 18
HELIX 18 AB9 ASP B 236 ARG B 238 5 3
HELIX 19 AC1 TYR B 239 GLU B 245 1 7
HELIX 20 AC2 THR C 10 ALA C 16 1 7
HELIX 21 AC3 ARG C 61 LYS C 66 5 6
HELIX 22 AC4 TRP C 67 SER C 74 1 8
HELIX 23 AC5 GLN C 90 GLY C 110 1 21
HELIX 24 AC6 SER C 131 ASN C 144 1 14
HELIX 25 AC7 SER C 185 MET C 193 1 9
HELIX 26 AC8 ASN C 217 ASP C 234 1 18
HELIX 27 AC9 ASP C 236 ARG C 238 5 3
HELIX 28 AD1 TYR C 239 GLU C 245 1 7
SHEET 1 AA1 6 VAL A 23 THR A 27 0
SHEET 2 AA1 6 ALA A 36 PRO A 42 -1 O VAL A 39 N PHE A 26
SHEET 3 AA1 6 VAL A 78 ASP A 83 -1 O VAL A 79 N TYR A 40
SHEET 4 AA1 6 VAL A 49 VAL A 55 1 N ILE A 52 O ILE A 80
SHEET 5 AA1 6 VAL A 120 TRP A 130 1 O ASP A 121 N VAL A 49
SHEET 6 AA1 6 ALA A 149 GLN A 153 1 O GLN A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 CYS A 174 0
SHEET 2 AA2 3 LYS A 198 ILE A 203 1 O GLN A 199 N ILE A 171
SHEET 3 AA2 3 VAL A 252 ALA A 258 -1 O ARG A 256 N PHE A 200
SHEET 1 AA3 6 VAL B 23 THR B 27 0
SHEET 2 AA3 6 ALA B 36 PRO B 42 -1 O VAL B 39 N PHE B 26
SHEET 3 AA3 6 VAL B 78 ASP B 83 -1 O VAL B 79 N TYR B 40
SHEET 4 AA3 6 VAL B 49 VAL B 55 1 N ILE B 54 O ILE B 80
SHEET 5 AA3 6 VAL B 120 GLY B 129 1 O ASP B 121 N VAL B 49
SHEET 6 AA3 6 ALA B 149 ALA B 150 1 O ALA B 149 N VAL B 127
SHEET 1 AA4 3 THR B 169 CYS B 174 0
SHEET 2 AA4 3 LYS B 198 ILE B 203 1 O ILE B 203 N ALA B 173
SHEET 3 AA4 3 VAL B 252 ALA B 258 -1 O ARG B 256 N PHE B 200
SHEET 1 AA5 6 THR C 22 THR C 27 0
SHEET 2 AA5 6 ALA C 36 THR C 43 -1 O VAL C 39 N PHE C 26
SHEET 3 AA5 6 VAL C 78 ASP C 83 -1 O VAL C 79 N TYR C 40
SHEET 4 AA5 6 VAL C 49 VAL C 55 1 N ILE C 52 O ILE C 80
SHEET 5 AA5 6 VAL C 120 TRP C 130 1 O ASP C 121 N VAL C 49
SHEET 6 AA5 6 ALA C 149 GLN C 153 1 O GLN C 153 N GLY C 129
SHEET 1 AA6 3 THR C 169 CYS C 174 0
SHEET 2 AA6 3 LYS C 198 ILE C 203 1 O GLN C 199 N ILE C 171
SHEET 3 AA6 3 VAL C 252 ALA C 258 -1 O ARG C 256 N PHE C 200
SSBOND 1 CYS A 174 CYS A 210 1555 1555 2.04
SSBOND 2 CYS A 244 CYS A 260 1555 1555 2.04
SSBOND 3 CYS B 174 CYS B 210 1555 1555 2.03
SSBOND 4 CYS B 244 CYS B 260 1555 1555 2.05
SSBOND 5 CYS C 174 CYS C 210 1555 1555 2.06
SSBOND 6 CYS C 244 CYS C 260 1555 1555 2.07
CRYST1 52.560 233.800 163.690 90.00 90.00 90.00 C 2 2 21 24
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 0.019026 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006109 0.00000
TER 1924 SER A 261
TER 3848 SER B 261
TER 5772 SER C 261
MASTER 325 0 0 28 27 0 0 6 6530 3 12 63
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