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HEADER HYDROLASE 03-OCT-19 6T0I
TITLE THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH THE ALDOTETRAURONIC ACID XUX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE;
SOURCE 3 ORGANISM_TAXID: 107709;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 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 6T0I 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH THE ALDOTETRAURONIC ACID XUX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.53 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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 42107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4168
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 32.4900 - 4.7600 0.98 1403 160 0.1642 0.1977
REMARK 3 2 4.7600 - 3.7800 0.99 1421 154 0.1138 0.1363
REMARK 3 3 3.7800 - 3.3100 0.98 1406 158 0.1236 0.1532
REMARK 3 4 3.3100 - 3.0000 0.98 1392 158 0.1292 0.1472
REMARK 3 5 3.0000 - 2.7900 0.98 1396 156 0.1356 0.1673
REMARK 3 6 2.7900 - 2.6200 0.98 1401 154 0.1284 0.1640
REMARK 3 7 2.6200 - 2.4900 0.86 1242 140 0.1418 0.2074
REMARK 3 8 2.4900 - 2.3800 0.69 968 110 0.1446 0.1867
REMARK 3 9 2.3800 - 2.2900 0.81 1167 121 0.1368 0.1583
REMARK 3 10 2.2900 - 2.2100 0.85 1210 140 0.1487 0.2064
REMARK 3 11 2.2100 - 2.1400 0.88 1269 130 0.1511 0.1975
REMARK 3 12 2.1400 - 2.0800 0.88 1263 143 0.1540 0.2291
REMARK 3 13 2.0800 - 2.0300 0.89 1263 145 0.1673 0.2235
REMARK 3 14 2.0300 - 1.9800 0.90 1291 140 0.1629 0.2019
REMARK 3 15 1.9800 - 1.9300 0.91 1291 142 0.1680 0.2248
REMARK 3 16 1.9300 - 1.8900 0.90 1280 144 0.2021 0.2324
REMARK 3 17 1.8900 - 1.8500 0.90 1312 145 0.1870 0.2193
REMARK 3 18 1.8500 - 1.8200 0.92 1294 141 0.2002 0.2580
REMARK 3 19 1.8200 - 1.7900 0.91 1317 147 0.2137 0.2523
REMARK 3 20 1.7900 - 1.7600 0.92 1306 140 0.2434 0.2756
REMARK 3 21 1.7600 - 1.7300 0.91 1313 140 0.2554 0.2853
REMARK 3 22 1.7300 - 1.7000 0.93 1310 144 0.2776 0.3233
REMARK 3 23 1.7000 - 1.6800 0.91 1304 153 0.2931 0.3325
REMARK 3 24 1.6800 - 1.6500 0.92 1350 133 0.3358 0.3974
REMARK 3 25 1.6500 - 1.6300 0.92 1300 145 0.3731 0.3883
REMARK 3 26 1.6300 - 1.6100 0.91 1290 147 0.3854 0.4110
REMARK 3 27 1.6100 - 1.5900 0.93 1335 138 0.3380 0.3615
REMARK 3 28 1.5900 - 1.5700 0.91 1308 148 0.3393 0.3408
REMARK 3 29 1.5700 - 1.5500 0.92 1317 137 0.3875 0.3904
REMARK 3 30 1.5500 - 1.5300 0.15 220 15 0.8076 0.8522
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) : 0.266
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.871
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.33
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 : 0.010 3299
REMARK 3 ANGLE : 1.159 4474
REMARK 3 CHIRALITY : 0.063 473
REMARK 3 PLANARITY : 0.008 590
REMARK 3 DIHEDRAL : 21.291 1196
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 6T0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42551
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 32.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04434
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 1.33000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.720
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
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 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 ALA A 33
REMARK 465 TYR A 34
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 OE1 GLN A 64 HH22 ARG A 73 1.54
REMARK 500 O4B XYP A 502 C2B XYP A 503 2.17
REMARK 500 C4B XYP A 502 C1B XYP A 503 2.19
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 VAL A 70 -72.19 -125.09
REMARK 500 ASP A 150 105.30 -28.05
REMARK 500 SER A 267 -124.16 58.13
REMARK 500 SER A 267 -119.73 42.47
REMARK 500 HIS A 328 35.59 -144.97
REMARK 500 ASP A 356 57.73 -90.38
REMARK 500 ASP A 360 71.40 59.78
REMARK 500 LYS A 427 -39.34 -159.33
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 506 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 250 O
REMARK 620 2 GLU A 251 O 75.2
REMARK 620 3 ASP A 253 O 82.7 109.1
REMARK 620 4 VAL A 256 O 104.0 171.0 79.5
REMARK 620 5 HOH A 790 O 108.4 88.9 161.0 82.9
REMARK 620 6 HOH A 838 O 148.6 79.1 89.0 104.2 88.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 93.2
REMARK 620 3 HOH A 771 O 101.9 95.3
REMARK 620 4 HOH A 622 O 84.1 81.9 173.5
REMARK 620 5 HOH A 815 O 159.3 87.4 98.6 75.5
REMARK 620 6 HOH A 682 O 86.0 154.9 109.4 73.1 84.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYP A
REMARK 800 501 through GCV A 504
DBREF 6T0I A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6T0I MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6T0I GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6T0I SER A 32 UNP B1ZMF4 EXPRESSION TAG
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 SER 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 XYP A 501 19
HET XYP A 502 15
HET XYP A 503 18
HET GCV A 504 24
HET MG A 505 1
HET K 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 PEG A 523 17
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 XYP 3(C5 H10 O5)
FORMUL 2 GCV C7 H12 O7
FORMUL 3 MG MG 2+
FORMUL 4 K K 1+
FORMUL 5 EDO 16(C2 H6 O2)
FORMUL 21 PEG C4 H10 O3
FORMUL 22 HOH *258(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 VAL A 147 5 5
HELIX 6 AA6 THR A 173 ARG A 177 5 5
HELIX 7 AA7 ASP A 180 TRP A 184 5 5
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 ALA A 214 5 5
HELIX 11 AB2 SER A 215 ASP A 221 1 7
HELIX 12 AB3 GLY A 234 ASP A 253 1 20
HELIX 13 AB4 SER A 267 ASP A 280 1 14
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 LEU A 426 1 16
SHEET 1 AA1 9 VAL A 83 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 ARG A 106 -1 O ARG A 106 N VAL A 83
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O LEU A 118 N VAL A 103
SHEET 4 AA1 9 ALA A 195 TYR A 200 -1 O THR A 198 N LEU A 119
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PRO A 134 O ALA A 195
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N LEU A 137
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O LEU A 285 N VAL A 263
SHEET 8 AA1 9 LEU A 348 ALA A 353 1 O TYR A 349 N SER A 288
SHEET 9 AA1 9 LEU A 399 ARG A 404 1 O ARG A 400 N VAL A 350
LINK O LEU A 250 K K A 506 1555 1555 2.75
LINK O GLU A 251 K K A 506 1555 1555 2.85
LINK O ASP A 253 K K A 506 1555 1555 2.65
LINK O VAL A 256 K K A 506 1555 1555 2.77
LINK O HIS A 303 MG MG A 505 1555 1555 2.22
LINK O GLU A 305 MG MG A 505 1555 1555 2.27
LINK O4B XYP A 501 C1B XYP A 502 1555 1555 1.37
LINK C2B XYP A 502 O1 GCV A 504 1555 1555 1.38
LINK O4B XYP A 502 C1B XYP A 503 1555 1555 1.38
LINK MG MG A 505 O HOH A 771 1555 1555 2.31
LINK MG MG A 505 O HOH A 622 1555 1555 2.62
LINK MG MG A 505 O HOH A 815 1555 1555 2.50
LINK MG MG A 505 O HOH A 682 1555 1555 2.27
LINK K K A 506 O HOH A 790 1555 1555 2.69
LINK K K A 506 O HOH A 838 1555 1555 3.03
CISPEP 1 ALA A 344 PRO A 345 0 4.47
SITE 1 AC1 6 HIS A 303 GLU A 305 HOH A 622 HOH A 682
SITE 2 AC1 6 HOH A 771 HOH A 815
SITE 1 AC2 6 LEU A 250 GLU A 251 ASP A 253 VAL A 256
SITE 2 AC2 6 HOH A 790 HOH A 838
SITE 1 AC3 4 GLU A 69 ALA A 412 HOH A 805 HOH A 814
SITE 1 AC4 6 ALA A 67 ARG A 73 THR A 74 GLN A 279
SITE 2 AC4 6 HOH A 658 HOH A 684
SITE 1 AC5 6 GLY A 81 ARG A 109 ARG A 362 VAL A 388
SITE 2 AC5 6 HOH A 629 HOH A 656
SITE 1 AC6 2 ASN A 392 PRO A 394
SITE 1 AC7 3 ALA A 43 GLN A 413 EDO A 519
SITE 1 AC8 2 SER A 395 GLY A 396
SITE 1 AC9 3 VAL A 86 THR A 87 GLU A 330
SITE 1 AD1 1 GLU A 131
SITE 1 AD2 6 ARG A 268 PHE A 314 XYP A 501 HOH A 699
SITE 2 AD2 6 HOH A 717 HOH A 786
SITE 1 AD3 5 HIS A 408 XYP A 502 XYP A 503 GCV A 504
SITE 2 AD3 5 HOH A 699
SITE 1 AD4 3 PRO A 79 GLU A 80 HOH A 604
SITE 1 AD5 3 LYS A 85 THR A 104 ARG A 106
SITE 1 AD6 8 ASP A 38 VAL A 41 GLY A 42 ALA A 43
SITE 2 AD6 8 ARG A 58 EDO A 511 HOH A 639 HOH A 774
SITE 1 AD7 3 THR A 74 GLY A 95 HOH A 636
SITE 1 AD8 3 HIS A 56 ARG A 57 ALA A 191
SITE 1 AD9 2 HOH A 767 HOH A 796
SITE 1 AE1 6 ALA A 152 ILE A 153 ALA A 154 LEU A 155
SITE 2 AE1 6 ARG A 177 HOH A 611
SITE 1 AE2 20 ALA A 52 GLN A 55 HIS A 56 SER A 267
SITE 2 AE2 20 ARG A 268 LYS A 271 SER A 291 GLU A 305
SITE 3 AE2 20 ILE A 310 VAL A 313 PHE A 314 TRP A 317
SITE 4 AE2 20 TRP A 358 PRO A 407 HIS A 408 EDO A 515
SITE 5 AE2 20 EDO A 516 HOH A 711 HOH A 744 HOH A 747
CRYST1 43.406 44.173 50.237 75.80 65.49 70.98 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 0.023038 -0.007940 -0.009567 0.00000
SCALE2 0.000000 0.023945 -0.003091 0.00000
SCALE3 0.000000 0.000000 0.022059 0.00000
TER 6084 PRO A 431
MASTER 385 0 23 20 9 0 32 6 3440 1 269 33
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