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HEADER HYDROLASE 12-OCT-17 6EQE
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF A POLYETHYLENE TEREPHTHALATE
TITLE 2 DEGRADING HYDROLASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
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 6EQE 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. 0.92 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) : 0.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 154294
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.101
REMARK 3 R VALUE (WORKING SET) : 0.100
REMARK 3 FREE R VALUE : 0.110
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 8053
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 27.5254 - 2.8577 1.00 5216 274 0.1279 0.1307
REMARK 3 2 2.8577 - 2.2685 1.00 5045 260 0.1015 0.1144
REMARK 3 3 2.2685 - 1.9819 1.00 4980 246 0.0900 0.0896
REMARK 3 4 1.9819 - 1.8007 1.00 4936 283 0.0845 0.0991
REMARK 3 5 1.8007 - 1.6717 1.00 4928 288 0.0822 0.0916
REMARK 3 6 1.6717 - 1.5731 1.00 4857 302 0.0752 0.0926
REMARK 3 7 1.5731 - 1.4943 1.00 4879 285 0.0745 0.0891
REMARK 3 8 1.4943 - 1.4293 1.00 4890 266 0.0732 0.0926
REMARK 3 9 1.4293 - 1.3743 1.00 4892 268 0.0771 0.0868
REMARK 3 10 1.3743 - 1.3268 1.00 4883 266 0.0766 0.0853
REMARK 3 11 1.3268 - 1.2854 1.00 4819 304 0.0748 0.0868
REMARK 3 12 1.2854 - 1.2486 1.00 4830 309 0.0749 0.0821
REMARK 3 13 1.2486 - 1.2158 1.00 4901 246 0.0734 0.0818
REMARK 3 14 1.2158 - 1.1861 1.00 4860 253 0.0773 0.0948
REMARK 3 15 1.1861 - 1.1591 1.00 4879 239 0.0812 0.0947
REMARK 3 16 1.1591 - 1.1345 1.00 4852 259 0.0822 0.0948
REMARK 3 17 1.1345 - 1.1118 1.00 4876 229 0.0829 0.0916
REMARK 3 18 1.1118 - 1.0908 1.00 4886 252 0.0928 0.1087
REMARK 3 19 1.0908 - 1.0713 1.00 4798 277 0.0987 0.1147
REMARK 3 20 1.0713 - 1.0531 1.00 4851 265 0.1017 0.1146
REMARK 3 21 1.0531 - 1.0362 1.00 4814 294 0.1159 0.1231
REMARK 3 22 1.0362 - 1.0202 1.00 4836 269 0.1213 0.1327
REMARK 3 23 1.0202 - 1.0052 1.00 4832 249 0.1316 0.1282
REMARK 3 24 1.0052 - 0.9910 1.00 4853 272 0.1503 0.1681
REMARK 3 25 0.9910 - 0.9777 0.99 4778 284 0.1780 0.1878
REMARK 3 26 0.9777 - 0.9650 0.99 4831 247 0.1866 0.2078
REMARK 3 27 0.9650 - 0.9529 1.00 4801 269 0.1856 0.2062
REMARK 3 28 0.9529 - 0.9414 1.00 4830 266 0.1972 0.2159
REMARK 3 29 0.9414 - 0.9305 1.00 4848 231 0.1969 0.2242
REMARK 3 30 0.9305 - 0.9200 0.99 4760 301 0.2152 0.2337
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) : 0.070
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 9.460
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 : 0.007 2174
REMARK 3 ANGLE : 1.104 2997
REMARK 3 CHIRALITY : 0.093 332
REMARK 3 PLANARITY : 0.010 396
REMARK 3 DIHEDRAL : 12.676 837
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 6EQE 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_1200007045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I23
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2398
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 12M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 154417
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.920
REMARK 200 RESOLUTION RANGE LOW (A) : 84.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 31.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M MES, PH 6.0 20% PEG
REMARK 280 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 25.55700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.27250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.69400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.27250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.55700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.69400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
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 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 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 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 A 519 O HOH A 523 2.08
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 ASN A 73 35.33 -146.25
REMARK 500 THR A 88 -12.79 75.21
REMARK 500 SER A 160 -120.21 65.27
REMARK 500 SER A 214 -82.35 -132.27
REMARK 500 SER A 214 -86.09 -129.79
REMARK 500 SER A 214 -85.41 -130.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 123 0.10 SIDE CHAIN
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 791 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A 793 DISTANCE = 7.00 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 193 OG
REMARK 620 2 HOH A 662 O 100.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 204 OE1
REMARK 620 2 ASN A 233 OD1 78.1
REMARK 620 3 HOH A 643 O 145.3 67.6
REMARK 620 4 HOH A 401 O 119.6 58.0 43.4
REMARK 620 5 HOH A 417 O 85.8 81.5 93.5 51.3
REMARK 620 N 1 2 3 4
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 CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EQD RELATED DB: PDB
REMARK 900 INITAL STRUCTURE OF PETASE
DBREF1 6EQE A 1 290 UNP PETH_IDESA
DBREF2 6EQE A A0A0K8P6T7 1 290
SEQADV 6EQE LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQE HIS A 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
HET CL A 301 1
HET CL A 302 1
HET NA A 303 1
HET NA A 304 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 NA 2(NA 1+)
FORMUL 6 HOH *393(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 PHE A 106 1 11
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
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 GLY A 158 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
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 ASP A 283 N GLU A 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.05
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.05
LINK OG SER A 193 NA NA A 303 1555 1555 2.71
LINK OE1 GLU A 204 NA NA A 304 1555 1555 2.38
LINK OD1 ASN A 233 NA NA A 304 1555 1555 2.37
LINK NA NA A 303 O HOH A 662 1555 1555 2.68
LINK NA NA A 304 O HOH A 643 1555 1555 3.08
LINK NA NA A 304 O HOH A 401 1555 1555 2.03
LINK NA NA A 304 O HOH A 417 1555 1555 2.52
SITE 1 AC1 4 TYR A 87 ARG A 132 SER A 160 MET A 161
SITE 1 AC2 3 SER A 207 HIS A 237 HOH A 773
SITE 1 AC3 5 ASN A 190 PHE A 191 SER A 193 HIS A 293
SITE 2 AC3 5 HOH A 662
SITE 1 AC4 5 GLU A 204 ASN A 233 HOH A 401 HOH A 417
SITE 2 AC4 5 HOH A 643
CRYST1 51.114 51.388 84.545 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 0.019564 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019460 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011828 0.00000
TER 4200 HIS A 293
MASTER 367 0 4 9 9 0 6 6 2349 1 14 23
END |