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HEADER HYDROLASE 12-OCT-17 6EQG
TITLE CRYSTAL STRUCTURE OF A POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE
TITLE 2 FROM IDEONELLA SAKAIENSIS IN SPACEGROUP P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PETASE;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41
KEYWDS PETASE, PET DEGRADATION, A/B HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.AUSTIN,M.D.ALLEN,C.W.JOHNSON,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 25-APR-18 6EQG 0
JRNL AUTH H.P.AUSTIN,M.D.ALLEN,B.DONOHOE,N.RORRER,F.KEARNS,R.SILVEIRA,
JRNL AUTH 2 B.POLLARD,G.DOMINICK,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,
JRNL AUTH 3 A.WAGNER,W.MICHENER,A.AMORE,M.SKAF,M.CROWLEY,A.THORNE,
JRNL AUTH 4 C.JOHNSON,H.WOODCOCK,J.MCGEEHAN,G.T.BECKHAM
JRNL TITL CHARACTERIZATION AND ENGINEERING OF A PLASTIC-DEGRADING
JRNL TITL 2 AROMATIC POLYESTERASE
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1718804115
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 68954
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 3550
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 46.4719 - 5.2591 0.98 2759 152 0.1639 0.1626
REMARK 3 2 5.2591 - 4.1751 0.99 2708 133 0.1254 0.1354
REMARK 3 3 4.1751 - 3.6476 0.98 2688 134 0.1195 0.1334
REMARK 3 4 3.6476 - 3.3142 0.98 2635 145 0.1319 0.1474
REMARK 3 5 3.3142 - 3.0767 0.99 2698 134 0.1399 0.1834
REMARK 3 6 3.0767 - 2.8953 0.98 2623 164 0.1436 0.1950
REMARK 3 7 2.8953 - 2.7504 0.98 2638 145 0.1452 0.1824
REMARK 3 8 2.7504 - 2.6306 0.98 2683 117 0.1502 0.2005
REMARK 3 9 2.6306 - 2.5294 0.98 2621 143 0.1480 0.1498
REMARK 3 10 2.5294 - 2.4421 0.98 2581 148 0.1545 0.2159
REMARK 3 11 2.4421 - 2.3657 0.98 2638 155 0.1593 0.1940
REMARK 3 12 2.3657 - 2.2981 0.98 2585 151 0.1515 0.1861
REMARK 3 13 2.2981 - 2.2376 0.98 2640 132 0.1510 0.1971
REMARK 3 14 2.2376 - 2.1830 0.98 2578 148 0.1497 0.1936
REMARK 3 15 2.1830 - 2.1334 0.97 2605 137 0.1541 0.2305
REMARK 3 16 2.1334 - 2.0880 0.97 2590 140 0.1577 0.2250
REMARK 3 17 2.0880 - 2.0462 0.97 2609 135 0.1670 0.2103
REMARK 3 18 2.0462 - 2.0076 0.97 2627 124 0.1730 0.2154
REMARK 3 19 2.0076 - 1.9718 0.97 2586 134 0.1696 0.1938
REMARK 3 20 1.9718 - 1.9383 0.97 2565 154 0.1740 0.2362
REMARK 3 21 1.9383 - 1.9071 0.97 2615 133 0.1824 0.2100
REMARK 3 22 1.9071 - 1.8777 0.96 2551 148 0.1997 0.2311
REMARK 3 23 1.8777 - 1.8501 0.97 2540 146 0.2010 0.2248
REMARK 3 24 1.8501 - 1.8241 0.97 2579 154 0.2177 0.2610
REMARK 3 25 1.8241 - 1.7994 0.93 2462 144 0.2451 0.2867
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.003 5950
REMARK 3 ANGLE : 0.598 8119
REMARK 3 CHIRALITY : 0.045 896
REMARK 3 PLANARITY : 0.004 1071
REMARK 3 DIHEDRAL : 2.483 4376
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 6EQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68988
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.53700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6EQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 0.1 M BIS-TRIS, PH 5.5
REMARK 280 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.19050
REMARK 290 SMTRY3 2 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 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 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 MET A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 LEU A 18
REMARK 465 MET A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 GLN A 28
REMARK 465 LEU A 291
REMARK 465 GLU A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PHE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 MET B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 18
REMARK 465 MET B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLN B 28
REMARK 465 LEU B 291
REMARK 465 GLU B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 PHE C 3
REMARK 465 PRO C 4
REMARK 465 ARG C 5
REMARK 465 ALA C 6
REMARK 465 SER C 7
REMARK 465 ARG C 8
REMARK 465 LEU C 9
REMARK 465 MET C 10
REMARK 465 GLN C 11
REMARK 465 ALA C 12
REMARK 465 ALA C 13
REMARK 465 VAL C 14
REMARK 465 LEU C 15
REMARK 465 GLY C 16
REMARK 465 GLY C 17
REMARK 465 LEU C 18
REMARK 465 MET C 19
REMARK 465 ALA C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 ALA C 24
REMARK 465 ALA C 25
REMARK 465 THR C 26
REMARK 465 ALA C 27
REMARK 465 GLN C 28
REMARK 465 GLU C 292
REMARK 465 HIS C 293
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
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 B 559 O HOH B 565 1.78
REMARK 500 O HOH A 684 O HOH A 692 1.91
REMARK 500 O HOH C 431 O HOH C 465 1.97
REMARK 500 O HOH A 601 O HOH A 683 1.97
REMARK 500 O HOH C 582 O HOH C 681 1.97
REMARK 500 O HOH A 623 O HOH A 718 1.99
REMARK 500 O HOH A 517 O HOH A 576 2.00
REMARK 500 O HOH C 638 O HOH C 689 2.01
REMARK 500 O HOH C 586 O HOH C 635 2.02
REMARK 500 O HOH A 618 O HOH A 671 2.02
REMARK 500 O HOH A 662 O HOH A 691 2.02
REMARK 500 O HOH C 507 O HOH C 534 2.03
REMARK 500 O HOH B 564 O HOH B 612 2.06
REMARK 500 O HOH C 544 O HOH C 592 2.07
REMARK 500 O HOH A 706 O HOH A 732 2.07
REMARK 500 O HOH C 431 O HOH C 648 2.08
REMARK 500 O HOH C 571 O HOH C 573 2.08
REMARK 500 O HOH C 417 O HOH C 641 2.09
REMARK 500 OG SER B 188 O HOH B 401 2.10
REMARK 500 O HOH A 648 O HOH A 678 2.10
REMARK 500 O HOH A 559 O HOH A 667 2.13
REMARK 500 O HOH B 783 O HOH B 787 2.14
REMARK 500 O HOH C 438 O HOH C 540 2.14
REMARK 500 O HOH C 494 O HOH C 578 2.15
REMARK 500 O HOH A 693 O HOH A 704 2.17
REMARK 500 O HOH B 617 O HOH B 694 2.19
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 C 569 O HOH C 627 2353 1.77
REMARK 500 O HOH B 744 O HOH B 767 2544 1.90
REMARK 500 O HOH A 676 O HOH C 381 2453 2.17
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 SER A 160 -118.36 60.19
REMARK 500 SER A 214 -74.50 -128.97
REMARK 500 THR B 88 -0.36 68.58
REMARK 500 SER B 160 -117.53 60.71
REMARK 500 SER B 214 -79.97 -135.69
REMARK 500 SER C 160 -117.23 62.47
REMARK 500 SER C 214 -81.43 -138.53
REMARK 500 SER C 214 -80.66 -139.01
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 775 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH C 690 DISTANCE = 5.86 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EQD RELATED DB: PDB
REMARK 900 ORIGINAL S-SAD PETASE
DBREF1 6EQG A 1 290 UNP PETH_IDESA
DBREF2 6EQG A A0A0K8P6T7 1 290
DBREF1 6EQG B 1 290 UNP PETH_IDESA
DBREF2 6EQG B A0A0K8P6T7 1 290
DBREF1 6EQG C 1 290 UNP PETH_IDESA
DBREF2 6EQG C A0A0K8P6T7 1 290
SEQADV 6EQG LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG LEU C 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG GLU C 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQG HIS C 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 A 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 A 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 A 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 A 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 A 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 A 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 A 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 A 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 A 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 A 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 A 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 A 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 A 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 A 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 A 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 A 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 A 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 A 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 A 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 A 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 A 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 A 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 B 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 B 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 B 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 B 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 B 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 B 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 B 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 B 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 B 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 B 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 B 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 B 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 B 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 B 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 B 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 B 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 B 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 B 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 B 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 B 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 B 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 B 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 C 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 C 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 C 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 C 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 C 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 C 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 C 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 C 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 C 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 C 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 C 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 C 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 C 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 C 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 C 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 C 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 C 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 C 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 C 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 C 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 C 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 C 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET SO4 B 301 5
HET CL B 302 1
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 4 CL 2(CL 1-)
FORMUL 5 SO4 O4 S 2-
FORMUL 7 HOH *1153(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
HELIX 10 AB1 THR B 39 ALA B 45 1 7
HELIX 11 AB2 ARG B 90 LYS B 95 5 6
HELIX 12 AB3 TRP B 96 SER B 103 1 8
HELIX 13 AB4 GLN B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 PRO B 210 SER B 213 5 4
HELIX 16 AB7 SER B 214 MET B 222 1 9
HELIX 17 AB8 ASN B 246 ASP B 263 1 18
HELIX 18 AB9 ASP B 265 ARG B 267 5 3
HELIX 19 AC1 TYR B 268 GLU B 274 1 7
HELIX 20 AC2 THR C 39 ALA C 45 1 7
HELIX 21 AC3 ARG C 90 LYS C 95 5 6
HELIX 22 AC4 TRP C 96 SER C 103 1 8
HELIX 23 AC5 GLN C 119 GLY C 139 1 21
HELIX 24 AC6 SER C 160 ASN C 173 1 14
HELIX 25 AC7 PRO C 210 SER C 213 5 4
HELIX 26 AC8 SER C 214 MET C 222 1 9
HELIX 27 AC9 ASN C 246 ASP C 263 1 18
HELIX 28 AD1 ASP C 265 ARG C 267 5 3
HELIX 29 AD2 TYR C 268 GLU C 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SHEET 1 AA3 6 VAL B 52 THR B 56 0
SHEET 2 AA3 6 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA3 6 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA3 6 VAL B 78 VAL B 84 1 N GLY B 79 O VAL B 107
SHEET 5 AA3 6 VAL B 149 TRP B 159 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 GLN B 182 1 O GLN B 182 N GLY B 158
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O ILE B 232 N ALA B 202
SHEET 3 AA4 3 VAL B 281 ALA B 287 -1 O ARG B 285 N PHE B 229
SHEET 1 AA5 6 VAL C 52 THR C 56 0
SHEET 2 AA5 6 ALA C 65 PRO C 71 -1 O VAL C 68 N PHE C 55
SHEET 3 AA5 6 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA5 6 VAL C 78 VAL C 84 1 N GLY C 79 O VAL C 107
SHEET 5 AA5 6 VAL C 149 GLY C 158 1 O ASP C 150 N VAL C 78
SHEET 6 AA5 6 ALA C 178 ALA C 179 1 O ALA C 178 N VAL C 156
SHEET 1 AA6 3 THR C 198 CYS C 203 0
SHEET 2 AA6 3 LYS C 227 ILE C 232 1 O GLN C 228 N ILE C 200
SHEET 3 AA6 3 VAL C 281 ALA C 287 -1 O ARG C 285 N PHE C 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.04
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.04
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.04
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.04
SSBOND 5 CYS C 203 CYS C 239 1555 1555 2.04
SSBOND 6 CYS C 273 CYS C 289 1555 1555 2.04
SITE 1 AC1 4 TYR A 87 SER A 160 MET A 161 HOH A 544
SITE 1 AC2 5 GLN B 119 SER B 121 SER B 122 HOH B 491
SITE 2 AC2 5 HOH B 563
SITE 1 AC3 3 TYR B 87 SER B 160 MET B 161
CRYST1 69.149 46.381 119.581 90.00 93.19 90.00 P 1 21 1 6
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 0.014462 0.000000 0.000807 0.00000
SCALE2 0.000000 0.021561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008376 0.00000
TER 1926 SER A 290
TER 3860 SER B 290
TER 5803 LEU C 291
MASTER 443 0 3 29 27 0 4 6 6943 3 17 69
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