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HEADER HYDROLASE 02-OCT-19 6SZO
TITLE THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH D-GALACTURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE PB90-1;
SOURCE 3 ORGANISM_TAXID: 452637;
SOURCE 4 GENE: OTER_0116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, COMPLEX, BIOMASS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 27-NOV-19 6SZO 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH D-GALACTURONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 16672
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) : 0.154
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.490
REMARK 3 FREE R VALUE TEST SET COUNT : 1249
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 44.7400 - 4.5700 0.97 1721 136 0.1726 0.2381
REMARK 3 2 4.5700 - 3.6300 0.98 1731 145 0.1306 0.1779
REMARK 3 3 3.6300 - 3.1700 0.98 1722 146 0.1331 0.1837
REMARK 3 4 3.1700 - 2.8800 0.98 1736 139 0.1349 0.1967
REMARK 3 5 2.8800 - 2.6700 0.97 1715 135 0.1532 0.2360
REMARK 3 6 2.6700 - 2.5200 0.97 1711 132 0.1716 0.2532
REMARK 3 7 2.5200 - 2.3900 0.97 1711 132 0.1784 0.2745
REMARK 3 8 2.3900 - 2.2900 0.96 1710 143 0.1874 0.3295
REMARK 3 9 2.2900 - 2.2000 0.95 1666 141 0.1955 0.2782
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.242
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.546
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.10
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 : 0.012 3020
REMARK 3 ANGLE : 1.262 4036
REMARK 3 CHIRALITY : 0.063 414
REMARK 3 PLANARITY : 0.009 520
REMARK 3 DIHEDRAL : 24.172 1088
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 6SZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104623.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9891
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.198
REMARK 200 RESOLUTION RANGE LOW (A) : 44.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.08127
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47980
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472
REMARK 200 STARTING MODEL: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION E8: 0.12 M ETHYLENE
REMARK 280 GLYCOLS (0.3M DIETHYLENE GLYCOL; 0.3M TRIETHYLENE GLYCOL; 0.3M
REMARK 280 TETRAETHYLENE GLYCOL; 0.3M PENTAETHYLENE GLYCOL), 0.1 M BUFFER
REMARK 280 SYSTEM 2 PH 7.5 (SODIUM HEPES; MOPS), AND 50 % V/V PRECIPITANT
REMARK 280 MIX 4 (25% V/V MPD; 25% PEG 1000; 25% W/V PEG 3350), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 7910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 92.0 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 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLU A 24
REMARK 465 ASN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 PHE A 28
REMARK 465 GLN A 29
REMARK 465 GLY A 30
REMARK 465 HIS A 31
REMARK 465 SER A 32
REMARK 465 HIS A 148
REMARK 465 THR A 149
REMARK 465 ASP A 150
REMARK 465 PRO A 151
REMARK 465 ALA A 152
REMARK 465 ILE A 153
REMARK 465 ALA A 154
REMARK 465 LEU A 155
REMARK 465 SER A 156
REMARK 465 ALA A 157
REMARK 465 ARG A 158
REMARK 465 TRP A 159
REMARK 465 ILE A 160
REMARK 465 PRO A 161
REMARK 465 ALA A 162
REMARK 465 GLU A 163
REMARK 465 ALA A 164
REMARK 465 PRO A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 ALA A 168
REMARK 465 ASN A 169
REMARK 465 HIS A 170
REMARK 465 ARG A 171
REMARK 465 ALA A 172
REMARK 465 THR A 173
REMARK 465 GLU A 174
REMARK 465 ALA A 175
REMARK 465 ALA A 176
REMARK 465 ARG A 177
REMARK 465 GLY A 178
REMARK 465 SER A 179
REMARK 465 ASP A 180
REMARK 465 LEU A 220
REMARK 465 ASP A 221
REMARK 465 ALA A 222
REMARK 465 ALA A 223
REMARK 465 ALA A 224
REMARK 465 GLY A 225
REMARK 465 SER A 428
REMARK 465 ALA A 429
REMARK 465 LEU A 430
REMARK 465 PRO A 431
REMARK 465 ALA A 432
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 OD2 ASP A 207 HH11 ARG A 268 1.51
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 TYR A 34 69.37 -164.86
REMARK 500 VAL A 70 -67.72 -122.55
REMARK 500 ALA A 92 39.58 -140.97
REMARK 500 HIS A 145 38.79 -96.74
REMARK 500 GLN A 182 -31.80 113.66
REMARK 500 LYS A 183 124.25 -26.30
REMARK 500 GLN A 227 -160.94 -176.38
REMARK 500 ALA A 267 -125.46 53.98
REMARK 500 HIS A 328 43.57 -146.43
REMARK 500 ASP A 360 79.30 65.18
REMARK 500 HIS A 408 127.56 -39.36
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 MG A 506 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 95.6
REMARK 620 3 HOH A 641 O 93.2 95.9
REMARK 620 4 HOH A 689 O 163.9 83.0 102.9
REMARK 620 5 HOH A 637 O 91.3 153.9 108.8 83.4
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 GTR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 538
DBREF 6SZO A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6SZO MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6SZO GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZO ALA A 267 UNP B1ZMF4 SER 267 ENGINEERED MUTATION
SEQRES 1 A 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 A 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 A 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 A 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 A 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 A 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 A 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 A 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 A 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 A 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 A 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 A 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 A 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 A 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 A 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 A 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 A 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 A 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 A 421 SER ARG VAL ALA VAL HIS GLY HIS ALA ARG LEU GLY LYS
SEQRES 21 A 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 A 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 A 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 A 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 A 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 A 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 A 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 A 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 A 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 A 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 A 421 HIS ILE ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP
SEQRES 32 A 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 A 421 SER ALA LEU PRO ALA
HET GTR A 501 22
HET DMS A 502 10
HET DMS A 503 10
HET DMS A 504 10
HET DMS A 505 10
HET MG A 506 1
HET EDO A 507 10
HET EDO A 508 10
HET EDO A 509 10
HET EDO A 510 10
HET EDO A 511 10
HET EDO A 512 10
HET EDO A 513 10
HET EDO A 514 10
HET EDO A 515 10
HET EDO A 516 10
HET EDO A 517 10
HET EDO A 518 10
HET EDO A 519 10
HET EDO A 520 10
HET EDO A 521 10
HET EDO A 522 10
HET EDO A 523 10
HET EDO A 524 10
HET EDO A 525 10
HET EDO A 526 10
HET EDO A 527 10
HET EDO A 528 10
HET EDO A 529 10
HET EDO A 530 10
HET PEG A 531 17
HET PEG A 532 17
HET PEG A 533 17
HET PEG A 534 17
HET PGE A 535 24
HET PGE A 536 24
HET PGE A 537 24
HET PGE A 538 24
HETNAM GTR BETA-D-GALACTOPYRANURONIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN GTR GALACTURONIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 GTR C6 H10 O7
FORMUL 3 DMS 4(C2 H6 O S)
FORMUL 7 MG MG 2+
FORMUL 8 EDO 24(C2 H6 O2)
FORMUL 32 PEG 4(C4 H10 O3)
FORMUL 36 PGE 4(C6 H14 O4)
FORMUL 40 HOH *122(H2 O)
HELIX 1 AA1 ASP A 50 ARG A 57 1 8
HELIX 2 AA2 ARG A 57 VAL A 70 1 14
HELIX 3 AA3 LEU A 94 GLY A 96 5 3
HELIX 4 AA4 ASN A 124 ALA A 128 1 5
HELIX 5 AA5 GLY A 143 HIS A 145 5 3
HELIX 6 AA6 THR A 146 VAL A 147 1 2
HELIX 7 AA7 GLN A 182 TRP A 184 1 3
HELIX 8 AA8 PRO A 185 ARG A 192 1 8
HELIX 9 AA9 GLY A 202 LEU A 204 5 3
HELIX 10 AB1 ASP A 210 TRP A 219 5 10
HELIX 11 AB2 GLY A 234 ASP A 253 1 20
HELIX 12 AB3 ALA A 267 ASP A 280 1 14
HELIX 13 AB4 LEU A 298 ILE A 302 5 5
HELIX 14 AB5 THR A 306 PHE A 314 1 9
HELIX 15 AB6 ALA A 319 ASP A 326 5 8
HELIX 16 AB7 HIS A 328 LEU A 332 5 5
HELIX 17 AB8 ASP A 335 LEU A 342 1 8
HELIX 18 AB9 ASP A 356 ALA A 359 5 4
HELIX 19 AC1 ASP A 360 PHE A 378 1 19
HELIX 20 AC2 THR A 411 LYS A 427 1 17
SHEET 1 AA110 VAL A 83 ALA A 93 0
SHEET 2 AA110 ALA A 98 ARG A 106 -1 O ARG A 106 N VAL A 83
SHEET 3 AA110 SER A 115 PRO A 123 -1 O MET A 116 N VAL A 105
SHEET 4 AA110 ALA A 195 TYR A 200 -1 O VAL A 196 N TYR A 121
SHEET 5 AA110 ALA A 133 ASN A 140 1 N PRO A 134 O ALA A 195
SHEET 6 AA110 VAL A 256 HIS A 266 1 O ALA A 262 N VAL A 135
SHEET 7 AA110 LEU A 285 ASN A 289 1 O LEU A 285 N VAL A 263
SHEET 8 AA110 LEU A 348 ALA A 353 1 O TYR A 349 N SER A 288
SHEET 9 AA110 LEU A 399 ARG A 404 1 O ARG A 400 N VAL A 350
SHEET 10 AA110 SER A 395 GLY A 396 -1 N SER A 395 O TYR A 401
LINK O HIS A 303 MG MG A 506 1555 1555 2.34
LINK O GLU A 305 MG MG A 506 1555 1555 2.29
LINK MG MG A 506 O HOH A 641 1555 1555 2.47
LINK MG MG A 506 O HOH A 689 1555 1555 2.44
LINK MG MG A 506 O HOH A 637 1555 1555 2.39
CISPEP 1 ALA A 344 PRO A 345 0 -2.14
SITE 1 AC1 14 ALA A 267 ARG A 268 LYS A 271 SER A 291
SITE 2 AC1 14 GLU A 305 ILE A 310 PHE A 314 TRP A 358
SITE 3 AC1 14 HIS A 408 DMS A 502 HOH A 642 HOH A 645
SITE 4 AC1 14 HOH A 673 HOH A 687
SITE 1 AC2 5 HIS A 266 ALA A 267 ARG A 268 GTR A 501
SITE 2 AC2 5 DMS A 505
SITE 1 AC3 4 ALA A 43 PEG A 532 PGE A 536 HOH A 665
SITE 1 AC4 6 ARG A 129 GLU A 131 ASN A 311 THR A 312
SITE 2 AC4 6 ARG A 323 ASP A 326
SITE 1 AC5 4 TYR A 142 GLN A 182 DMS A 502 EDO A 527
SITE 1 AC6 5 HIS A 303 GLU A 305 HOH A 637 HOH A 641
SITE 2 AC6 5 HOH A 689
SITE 1 AC7 2 TYR A 34 LEU A 36
SITE 1 AC8 3 ARG A 51 ASN A 112 LEU A 377
SITE 1 AC9 5 GLU A 131 ARG A 132 GLN A 227 PRO A 254
SITE 2 AC9 5 HOH A 626
SITE 1 AD1 5 ALA A 97 PRO A 123 ASN A 124 ALA A 125
SITE 2 AD1 5 ALA A 191
SITE 1 AD2 5 TRP A 241 SER A 244 ARG A 245 GLN A 279
SITE 2 AD2 5 HOH A 605
SITE 1 AD3 3 PRO A 394 SER A 395 GLY A 396
SITE 1 AD4 3 ARG A 208 PRO A 209 ASP A 210
SITE 1 AD5 3 ASP A 207 ARG A 268 HOH A 693
SITE 1 AD6 3 ALA A 43 GLN A 413 PEG A 532
SITE 1 AD7 5 ASP A 44 PRO A 394 PHE A 417 PGE A 536
SITE 2 AD7 5 HOH A 644
SITE 1 AD8 4 ALA A 67 THR A 74 GLN A 279 HOH A 627
SITE 1 AD9 5 GLU A 251 THR A 252 ASP A 253 PRO A 254
SITE 2 AD9 5 HOH A 608
SITE 1 AE1 3 SER A 259 ASP A 281 HOH A 601
SITE 1 AE2 4 GLN A 380 THR A 381 GLY A 397 ALA A 398
SITE 1 AE3 5 LYS A 101 TYR A 249 THR A 252 ASP A 253
SITE 2 AE3 5 PRO A 254
SITE 1 AE4 3 ASP A 50 ARG A 51 ALA A 52
SITE 1 AE5 2 PRO A 345 GLN A 380
SITE 1 AE6 4 ARG A 129 GLU A 131 ARG A 260 LYS A 427
SITE 1 AE7 5 GLN A 182 TRP A 184 HIS A 266 MET A 410
SITE 2 AE7 5 DMS A 505
SITE 1 AE8 2 HIS A 56 ARG A 57
SITE 1 AE9 3 ASN A 124 HOH A 616 HOH A 676
SITE 1 AF1 2 ARG A 228 TRP A 233
SITE 1 AF2 6 ALA A 43 LEU A 65 ARG A 68 GLN A 188
SITE 2 AF2 6 ALA A 412 ALA A 416
SITE 1 AF3 5 ASP A 38 VAL A 41 ARG A 58 DMS A 503
SITE 2 AF3 5 EDO A 517
SITE 1 AF4 5 LYS A 85 THR A 104 ARG A 106 ASP A 355
SITE 2 AF4 5 HOH A 674
SITE 1 AF5 7 ASP A 110 ASP A 355 ASP A 356 ASP A 357
SITE 2 AF5 7 TRP A 358 PRO A 407 HIS A 408
SITE 1 AF6 9 ALA A 128 ARG A 129 ALA A 130 PRO A 209
SITE 2 AF6 9 GLN A 227 ARG A 228 PRO A 315 ARG A 320
SITE 3 AF6 9 ARG A 323
SITE 1 AF7 7 GLY A 45 ASN A 392 GLU A 393 PRO A 394
SITE 2 AF7 7 DMS A 503 EDO A 518 HOH A 665
SITE 1 AF8 5 PHE A 141 TYR A 200 GLY A 202 PRO A 206
SITE 2 AF8 5 ASP A 207
SITE 1 AF9 5 TYR A 34 GLU A 80 ARG A 301 HIS A 303
SITE 2 AF9 5 ARG A 362
CRYST1 44.626 46.138 50.195 63.65 86.79 71.17 P 1 1
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 0.022408 -0.007643 0.002451 0.00000
SCALE2 0.000000 0.022900 -0.011557 0.00000
SCALE3 0.000000 0.000000 0.022351 0.00000
TER 5433 LYS A 427
MASTER 462 0 38 20 10 0 58 6 3098 1 473 33
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