| content |
HEADER HYDROLASE 02-AUG-24 9J07
TITLE ACETYL XYLAN ESTERASE B FROM ASPERGILLUS ORYZAE (AOAXEB), APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE RIB40;
SOURCE 3 ORGANISM_TAXID: 510516;
SOURCE 4 GENE: AO090005000945;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZB
KEYWDS ACETYL XYLAN ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.YAMADA,T.KOSEKI,S.FUSHINOBU
REVDAT 1 05-FEB-25 9J07 0
JRNL AUTH C.YAMADA,T.KATO,Y.SHIONO,T.KOSEKI,S.FUSHINOBU
JRNL TITL IDENTIFICATION AND STRUCTURAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 ACETYL XYLAN ESTERASE FROM ASPERGILLUS ORYZAE.
JRNL REF FEBS J. 2025
JRNL REFN ISSN 1742-464X
JRNL PMID 39876052
JRNL DOI 10.1111/FEBS.17420
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1562
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2139
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.50000
REMARK 3 B33 (A**2) : 0.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2449 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2156 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3342 ; 1.669 ; 1.680
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5003 ; 1.444 ; 1.600
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 302 ; 7.291 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;32.373 ;22.520
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 347 ;12.361 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;21.518 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 314 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2832 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 576 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1199 ; 1.543 ; 1.597
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1198 ; 1.540 ; 1.593
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1498 ; 2.267 ; 2.386
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1499 ; 2.267 ; 2.391
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1250 ; 2.472 ; 1.883
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1251 ; 2.471 ; 1.884
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1843 ; 3.776 ; 2.728
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2856 ; 5.341 ;20.461
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2763 ; 5.174 ;19.866
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 9J07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-21
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31605
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 47.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.85900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM FLUORIDE, 20% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 28.80700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.70850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.76450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.70850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.80700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.76450
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 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 LYS A 2
REMARK 465 PHE A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 VAL A 6
REMARK 465 ILE A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 THR A 10
REMARK 465 THR A 11
REMARK 465 THR A 12
REMARK 465 ALA A 13
REMARK 465 GLY A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 SER A 17
REMARK 465 ALA A 18
REMARK 465 SER A 318
REMARK 465 GLU A 319
REMARK 465 ASP A 320
REMARK 465 ASN A 321
REMARK 465 GLN A 322
REMARK 465 SER A 323
REMARK 465 GLU A 324
REMARK 465 ALA A 325
REMARK 465 ARG A 326
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 81 CD GLU A 81 OE1 0.071
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 GLN A 111 133.65 -36.35
REMARK 500 ARG A 142 57.24 -140.52
REMARK 500 SER A 149 -113.27 60.56
REMARK 500 GLU A 226 -164.99 -122.79
REMARK 500 THR A 297 -159.51 -124.85
REMARK 500
REMARK 500 REMARK: NULL
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 K A 405 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 295 O
REMARK 620 2 GLY A 296 O 64.9
REMARK 620 3 PGE A 401 O1 72.3 129.6
REMARK 620 4 PGE A 401 O2 84.8 93.9 55.8
REMARK 620 5 PGE A 401 O4 136.4 74.9 151.2 115.1
REMARK 620 6 PGE A 401 O3 122.2 76.2 107.5 56.2 59.0
REMARK 620 7 HOH A 607 O 84.0 77.0 124.3 167.8 70.8 127.6
REMARK 620 N 1 2 3 4 5 6
DBREF 9J07 A 1 326 UNP Q2UR69 Q2UR69_ASPOR 1 326
SEQRES 1 A 326 MET LYS PHE LEU SER VAL ILE LEU LEU THR THR THR ALA
SEQRES 2 A 326 GLY LEU ALA SER ALA ALA GLY SER ALA GLY CYS GLY GLN
SEQRES 3 A 326 PRO LEU PRO PRO SER GLN ASN PRO GLY GLY SER SER TYR
SEQRES 4 A 326 GLY VAL ASN PHE THR LEU SER ALA GLY THR GLN ARG PHE
SEQRES 5 A 326 TYR ARG ILE HIS ILE PRO SER ASN TYR ASN VAL ASN THR
SEQRES 6 A 326 PRO THR PRO LEU ILE PHE SER PHE HIS GLY ARG GLY LYS
SEQRES 7 A 326 THR ALA GLU SER GLN GLU LYS LEU SER GLN PHE SER ASN
SEQRES 8 A 326 GLU ASP TRP ASN PRO ASP ALA ILE ALA VAL TYR PRO GLN
SEQRES 9 A 326 GLY LEU ASN LYS GLU TRP GLN GLY ASP PRO HIS SER LYS
SEQRES 10 A 326 ASP VAL ASP ASP ILE ALA PHE THR MET GLU MET LEU ASP
SEQRES 11 A 326 TYR PHE GLN GLU LYS PHE CYS ILE ASP SER THR ARG VAL
SEQRES 12 A 326 TYR ALA ALA GLY LYS SER ASN GLY GLY GLY PHE THR ASN
SEQRES 13 A 326 LEU LEU ALA CYS ASP PRO THR ALA SER THR ARG ILE ALA
SEQRES 14 A 326 ALA PHE ALA PRO VAL SER GLY ALA TYR TYR GLN ASP VAL
SEQRES 15 A 326 SER GLU GLU ALA CYS HIS PRO THR THR VAL PRO ILE LYS
SEQRES 16 A 326 CYS SER PRO GLY ARG PRO SER ILE PRO ILE LEU GLU PHE
SEQRES 17 A 326 HIS GLY THR ALA ASP LYS THR ILE PRO TYR GLY GLY GLY
SEQRES 18 A 326 GLY ARG ARG GLY GLU CYS LEU PRO SER ILE PRO HIS PHE
SEQRES 19 A 326 VAL ARG GLU TRP SER LYS ARG LEU GLY TYR GLY LEU HIS
SEQRES 20 A 326 ASN THR THR LYS GLU LEU TYR ASP GLY ASN VAL GLN GLU
SEQRES 21 A 326 TYR GLN TYR GLY ASN GLY ASP ASN ARG GLY ILE VAL THR
SEQRES 22 A 326 HIS TYR ARG ILE GLY GLY LEU GLY HIS ASP TRP PRO SER
SEQRES 23 A 326 VAL ARG PRO ASN SER ASP ASN PRO ASN GLY THR TYR LEU
SEQRES 24 A 326 ASP ALA THR PRO ILE ILE VAL LYS PHE PHE LYS GLN TRP
SEQRES 25 A 326 VAL LEU PRO GLY SER SER GLU ASP ASN GLN SER GLU ALA
SEQRES 26 A 326 ARG
HET PGE A 401 10
HET NAG A 402 14
HET NAG A 403 14
HET NAG A 404 14
HET K A 405 1
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM K POTASSIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 PGE C6 H14 O4
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 6 K K 1+
FORMUL 7 HOH *323(H2 O)
HELIX 1 AA1 THR A 79 GLN A 88 1 10
HELIX 2 AA2 GLY A 105 GLU A 109 5 5
HELIX 3 AA3 ASP A 120 PHE A 136 1 17
HELIX 4 AA4 SER A 149 CYS A 160 1 12
HELIX 5 AA5 THR A 163 ARG A 167 5 5
HELIX 6 AA6 SER A 230 LEU A 242 1 13
HELIX 7 AA7 ASP A 300 TRP A 312 1 13
SHEET 1 AA1 6 TYR A 39 THR A 44 0
SHEET 2 AA1 6 GLN A 50 HIS A 56 -1 O ARG A 51 N PHE A 43
SHEET 3 AA1 6 ILE A 99 PRO A 103 -1 O ALA A 100 N HIS A 56
SHEET 4 AA1 6 THR A 67 PHE A 73 1 N ILE A 70 O VAL A 101
SHEET 5 AA1 6 ILE A 138 LYS A 148 1 O TYR A 144 N PHE A 71
SHEET 6 AA1 6 ALA A 170 VAL A 174 1 O VAL A 174 N GLY A 147
SHEET 1 AA2 4 ILE A 205 GLY A 210 0
SHEET 2 AA2 4 VAL A 272 ILE A 277 1 O THR A 273 N ILE A 205
SHEET 3 AA2 4 VAL A 258 TYR A 263 -1 N TYR A 261 O HIS A 274
SHEET 4 AA2 4 ASN A 248 LEU A 253 -1 N LEU A 253 O VAL A 258
SHEET 1 AA3 2 GLY A 221 ARG A 223 0
SHEET 2 AA3 2 GLU A 226 LEU A 228 -1 O GLU A 226 N ARG A 223
SSBOND 1 CYS A 24 CYS A 137 1555 1555 2.03
SSBOND 2 CYS A 160 CYS A 196 1555 1555 2.05
SSBOND 3 CYS A 187 CYS A 227 1555 1555 2.05
LINK ND2 ASN A 42 C1 NAG A 403 1555 1555 1.44
LINK ND2 ASN A 248 C1 NAG A 404 1555 1555 1.43
LINK ND2 ASN A 295 C1 NAG A 402 1555 1555 1.44
LINK O ASN A 295 K K A 405 1555 1555 2.70
LINK O GLY A 296 K K A 405 1555 1555 3.06
LINK O1 PGE A 401 K K A 405 1555 1555 3.14
LINK O2 PGE A 401 K K A 405 1555 1555 3.00
LINK O4 PGE A 401 K K A 405 1555 1555 2.82
LINK O3 PGE A 401 K K A 405 1555 1555 2.95
LINK K K A 405 O HOH A 607 1555 1555 2.99
CRYST1 57.614 63.529 83.417 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 0.017357 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015741 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011988 0.00000
TER 2319 SER A 317
MASTER 328 0 5 7 12 0 0 6 2688 1 66 26
END |