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HEADER HYDROLASE 21-DEC-24 9HUC
TITLE THE GLUCURONYL ESTERASE OTCE15A FROM OPITUTUS TERRAE IN COMPLEX WITH A
TITLE 2 HEPTASACCHARIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: 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 GLUCUROYL ESTERASE, OPITUTUS TERRAE, LIGNOCELLULOSE, CARBOHYDRATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.OESTBERG,L.LO LEGGIO,A.ZAGHINI,S.MAZURKEWICH,J.LARSBRINK
REVDAT 1 14-JAN-26 9HUC 0
JRNL AUTH A.ZAGHINI,E.B.OESTBERG,S.BANERJEE,S.MAZURKEWICH,L.YU,
JRNL AUTH 2 P.DUPREE,J.LARSBRINK,L.LO LEGGIO
JRNL TITL INTERACTION OF A GLUCURONYL ESTERASE WITH COMPLEX FRAGMENTS
JRNL TITL 2 OF THE PLANT CELL WALL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0403
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 14772
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.152
REMARK 3 FREE R VALUE TEST SET COUNT : 761
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3055
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.98100
REMARK 3 B22 (A**2) : 2.42100
REMARK 3 B33 (A**2) : -0.44100
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): 0.832
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.299
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.231
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.239
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3274 ; 0.005 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2970 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4490 ; 1.343 ; 1.661
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6818 ; 0.473 ; 1.576
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 406 ; 7.092 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 36 ; 6.174 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 454 ;15.781 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 486 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3978 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 814 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 733 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 31 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1601 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.151 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.162 ; 0.200
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): 1600 ; 2.171 ; 3.507
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1600 ; 2.170 ; 3.508
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2005 ; 3.413 ; 6.297
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2006 ; 3.417 ; 6.300
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1674 ; 2.627 ; 3.908
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1675 ; 2.626 ; 3.912
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2483 ; 4.249 ; 7.060
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2484 ; 4.249 ; 7.064
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9HUC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-24.
REMARK 100 THE DEPOSITION ID IS D_1292144167.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.03285
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14772
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 38.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 4.567
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.59
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: OTCE15A MIXED 3:1 WITH RESERVOIR
REMARK 280 CONTAINING 0.10 M CARBOXYLIC ACIDS (0.2M SODIUM FORMATE; 0.2M
REMARK 280 AMMONIUM ACETATE; 0.2M SODIUM CITRATE TRIBASIC DIHYDRATE; 0.2M
REMARK 280 POTASSIUM SODIUM TARTRATE TETRAHYDRATE; 0.2M SODIUM OXAMATE),
REMARK 280 0.1 M BUFFER SYSTEM 1, PH 6.5 (IMIDAZOLE; MES MONOHYDRATE (ACID))
REMARK 280 , 37.50 % V/V, PRECIPITANT MIX 4 (25% V/V MPD; 25% PEG 1000; 25%
REMARK 280 W/V PEG 3350). SOLID OLIGOSACCHARIDE ADDED TO THE DROP AND
REMARK 280 SOAKED FOR 15 MIN., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
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 25.38500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.31000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.71500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.31000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.38500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.71500
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 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ARG A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 SER A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 PHE A 12
REMARK 465 THR A 13
REMARK 465 LEU A 14
REMARK 465 THR A 15
REMARK 465 SER A 16
REMARK 465 MET A 17
REMARK 465 GLN A 18
REMARK 465 ALA A 19
REMARK 465 THR A 20
REMARK 465 SER A 21
REMARK 465 ARG A 22
REMARK 465 PRO A 23
REMARK 465 ALA A 24
REMARK 465 ARG A 25
REMARK 465 LEU A 26
REMARK 465 ASP A 27
REMARK 465 ASP A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 PRO A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 429
REMARK 465 LEU A 430
REMARK 465 PRO A 431
REMARK 465 ALA A 432
REMARK 465 ARG A 433
REMARK 465 GLU A 434
REMARK 465 PRO A 435
REMARK 465 GLN A 436
REMARK 465 ARG A 437
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 427 CG CD CE NZ
REMARK 470 SER A 428 OG
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 -72.76 -114.18
REMARK 500 ASP A 150 107.16 -51.87
REMARK 500 SER A 267 -114.26 49.94
REMARK 500 HIS A 328 43.31 -151.88
REMARK 500 ASP A 360 72.27 54.71
REMARK 500 LYS A 427 178.35 80.50
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 718 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 719 DISTANCE = 7.68 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 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 85.9
REMARK 620 3 HOH A 628 O 92.4 161.2
REMARK 620 4 HOH A 633 O 94.5 88.2 110.5
REMARK 620 5 HOH A 641 O 79.9 78.8 82.5 166.2
REMARK 620 6 HOH A 656 O 164.5 93.2 83.5 100.9 84.8
REMARK 620 N 1 2 3 4 5
DBREF 9HUC A 1 437 UNP B1ZMF4 B1ZMF4_OPITP 1 437
SEQRES 1 A 437 MET ARG ASN VAL LEU ALA ALA LEU SER LEU LEU PHE THR
SEQRES 2 A 437 LEU THR SER MET GLN ALA THR SER ARG PRO ALA ARG LEU
SEQRES 3 A 437 ASP ASP THR PRO PRO PRO ALA TYR THR LEU PRO ASP PRO
SEQRES 4 A 437 LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP ARG ALA
SEQRES 5 A 437 THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU GLN LEU
SEQRES 6 A 437 PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU GLY ARG
SEQRES 7 A 437 PRO GLU GLY MET VAL PHE LYS VAL THR THR MET GLU HIS
SEQRES 8 A 437 ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU VAL THR
SEQRES 9 A 437 VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER MET GLN
SEQRES 10 A 437 LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA ARG ALA
SEQRES 11 A 437 GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE TYR GLY
SEQRES 12 A 437 ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA LEU SER
SEQRES 13 A 437 ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY ALA ASN
SEQRES 14 A 437 HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP ALA GLN
SEQRES 15 A 437 LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY TYR ALA
SEQRES 16 A 437 VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO ASP ARG
SEQRES 17 A 437 PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP LEU ASP
SEQRES 18 A 437 ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA TRP GLY
SEQRES 19 A 437 ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG ALA LEU
SEQRES 20 A 437 ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA SER ARG
SEQRES 21 A 437 VAL ALA VAL HIS GLY HIS SER ARG LEU GLY LYS ALA ALA
SEQRES 22 A 437 LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA LEU VAL
SEQRES 23 A 437 ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA LEU SER
SEQRES 24 A 437 LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE ASN THR
SEQRES 25 A 437 VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG ARG TYR
SEQRES 26 A 437 ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN HIS GLU
SEQRES 27 A 437 LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR VAL ALA
SEQRES 28 A 437 SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG GLY GLU
SEQRES 29 A 437 PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE ARG LEU
SEQRES 30 A 437 PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL PRO ARG
SEQRES 31 A 437 VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR HIS ILE
SEQRES 32 A 437 ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP TRP ALA
SEQRES 33 A 437 PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS SER ALA
SEQRES 34 A 437 LEU PRO ALA ARG GLU PRO GLN ARG
HET XYP B 1 10
HET XYP B 2 9
HET XYP B 3 9
HET XYP B 4 9
HET AHR B 5 9
HET XYP B 6 9
HET GCV B 7 13
HET NA A 501 1
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM AHR ALPHA-L-ARABINOFURANOSE
HETNAM GCV 4-O-METHYL-ALPHA-D-GLUCOPYRANURONIC ACID
HETNAM NA SODIUM ION
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
HETSYN AHR ALPHA-L-ARABINOSE; L-ARABINOSE; ARABINOSE
HETSYN GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID; 4-O-METHYL-D-
HETSYN 2 GCV GLUCURONIC ACID; 4-O-METHYL-GLUCURONIC ACID
FORMUL 2 XYP 5(C5 H10 O5)
FORMUL 2 AHR C5 H10 O5
FORMUL 2 GCV C7 H12 O7
FORMUL 3 NA NA 1+
FORMUL 4 HOH *119(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 ASN A 124 ALA A 128 1 5
HELIX 4 AA4 GLY A 143 HIS A 148 5 6
HELIX 5 AA5 THR A 173 ARG A 177 5 5
HELIX 6 AA6 ASP A 180 TRP A 184 5 5
HELIX 7 AA7 PRO A 185 ARG A 192 1 8
HELIX 8 AA8 GLY A 202 LEU A 204 5 3
HELIX 9 AA9 ASP A 210 ALA A 214 5 5
HELIX 10 AB1 SER A 215 ASP A 221 1 7
HELIX 11 AB2 GLY A 234 THR A 252 1 19
HELIX 12 AB3 SER A 267 ASP A 280 1 14
HELIX 13 AB4 THR A 306 PHE A 314 1 9
HELIX 14 AB5 ALA A 319 ASP A 326 5 8
HELIX 15 AB6 HIS A 328 LEU A 332 5 5
HELIX 16 AB7 ASP A 335 LEU A 342 1 8
HELIX 17 AB8 ASP A 356 ALA A 359 5 4
HELIX 18 AB9 ASP A 360 PHE A 378 1 19
HELIX 19 AC1 THR A 411 LYS A 427 1 17
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 100 N GLU A 90
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O MET A 116 N VAL A 105
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 VAL A 135
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O ILE A 287 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 LEU A 348
LINK O4 XYP B 1 C1 XYP B 2 1555 1555 1.43
LINK O4 XYP B 2 C1 XYP B 3 1555 1555 1.44
LINK O2 XYP B 2 C1 GCV B 7 1555 1555 1.43
LINK O4 XYP B 3 C1 XYP B 4 1555 1555 1.45
LINK O3 XYP B 4 C1 AHR B 5 1555 1555 1.47
LINK O4 XYP B 4 C1 XYP B 6 1555 1555 1.47
LINK O HIS A 303 NA NA A 501 1555 1555 2.45
LINK O GLU A 305 NA NA A 501 1555 1555 2.54
LINK NA NA A 501 O HOH A 628 1555 1555 2.19
LINK NA NA A 501 O HOH A 633 1555 1555 2.44
LINK NA NA A 501 O HOH A 641 1555 1555 2.34
LINK NA NA A 501 O HOH A 656 1555 1555 2.62
CISPEP 1 ALA A 344 PRO A 345 0 1.20
CRYST1 50.770 65.430 118.620 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 0.019697 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015284 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008430 0.00000
TER 3105 SER A 428
MASTER 350 0 8 19 9 0 0 6 3243 1 76 34
END |