| content |
HEADER HYDROLASE 23-FEB-17 5X6S
TITLE ACETYL XYLAN ESTERASE FROM ASPERGILLUS AWAMORI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLXYLAN ESTERASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 30-304;
COMPND 5 EC: 3.1.1.72;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS AWAMORI;
SOURCE 3 ORGANISM_COMMON: BLACK KOJI MOLD;
SOURCE 4 ORGANISM_TAXID: 105351;
SOURCE 5 GENE: AXEA, ACEA;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA
KEYWDS ALPHA/BETA-HYDROLASE, ESTRASE_PHB, CAZY CE1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOMIYA,T.KOSEKI,S.FUSHINOBU
REVDAT 1 23-AUG-17 5X6S 0
JRNL AUTH D.KOMIYA,A.HORI,T.ISHIDA,K.IGARASHI,M.SAMEJIMA,T.KOSEKI,
JRNL AUTH 2 S.FUSHINOBU
JRNL TITL CRYSTAL STRUCTURE AND SUBSTRATE SPECIFICITY MODIFICATION OF
JRNL TITL 2 ACETYL XYLAN ESTERASE FROM ASPERGILLUS LUCHUENSIS
JRNL REF APPL. ENVIRON. MICROBIOL. 2017
JRNL REFN ESSN 1098-5336
JRNL PMID 28802264
JRNL DOI 10.1128/AEM.01251-17
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.KOSEKI,S.FURUSE,K.IWANO,H.SAKAI,H.MATSUZAWA
REMARK 1 TITL AN ASPERGILLUS AWAMORI ACETYLESTERASE: PURIFICATION OF THE
REMARK 1 TITL 2 ENZYME, AND CLONING AND SEQUENCING OF THE GENE
REMARK 1 REF BIOCHEM. J. V.T 2) 485 1997
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 9291122
REMARK 1 DOI 10.1042/BJ3260485
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.KOSEKI,Y.MIWA,S.FUSHINOBU,K.HASHIZUME
REMARK 1 TITL BIOCHEMICAL CHARACTERIZATION OF RECOMBINANT ACETYL XYLAN
REMARK 1 TITL 2 ESTERASE FROM ASPERGILLUS AWAMORI EXPRESSED IN PICHIA
REMARK 1 TITL 3 PASTORIS: MUTATIONAL ANALYSIS OF CATALYTIC RESIDUES
REMARK 1 REF BIOCHIM. BIOPHYS. ACTA V.1749 7 2005
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 15848131
REMARK 1 DOI 10.1016/J.BBAPAP.2005.01.009
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 42045
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2238
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3047
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4148
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
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): 0.133
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4376 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3715 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5996 ; 1.522 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8591 ; 3.865 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 546 ; 6.129 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;36.061 ;24.894
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 564 ;12.223 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ; 7.467 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5078 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1042 ; 0.018 ; 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): 2190 ; 1.150 ; 2.114
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2189 ; 1.139 ; 2.113
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2734 ; 1.577 ; 3.164
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2735 ; 1.582 ; 3.164
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2186 ; 1.835 ; 2.244
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2186 ; 1.835 ; 2.244
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3263 ; 2.517 ; 3.323
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5255 ; 3.898 ;26.248
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5143 ; 3.689 ;25.703
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 : NULL
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 5X6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300003016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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-6A
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44285
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 87.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-22.5% PEG 8000, 0.1M MES-NAOH (PH
REMARK 280 5.0), 0.2M CALCIUM ACETATE, 5% MPD, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 87.07550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.27306
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.90267
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 87.07550
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 50.27306
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 16.90267
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 87.07550
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 50.27306
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.90267
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.54613
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 33.80533
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 100.54613
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 33.80533
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 100.54613
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 33.80533
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
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 SER A 1
REMARK 465 SER B 1
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 13 56.24 -152.79
REMARK 500 THR A 41 -4.94 71.48
REMARK 500 SER A 119 -119.92 54.45
REMARK 500 SER A 143 68.91 61.78
REMARK 500 TYR A 151 132.00 -34.46
REMARK 500 ASN B 13 58.81 -154.50
REMARK 500 ASN B 26 51.82 -90.41
REMARK 500 THR B 41 -4.58 66.36
REMARK 500 SER B 119 -123.50 56.11
REMARK 500 SER B 143 66.02 63.92
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 669 DISTANCE = 6.54 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 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 30 OD1
REMARK 620 2 HOH A 488 O 86.3
REMARK 620 3 HOH B 588 O 128.9 77.6
REMARK 620 4 HOH B 433 O 85.6 168.4 114.0
REMARK 620 5 HOH A 604 O 87.8 83.3 136.3 88.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 134 O
REMARK 620 2 GLU B 134 O 167.6
REMARK 620 3 HOH B 551 O 88.7 90.1
REMARK 620 4 HOH A 607 O 80.8 101.3 168.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 30 OD1
REMARK 620 2 HOH A 445 O 92.8
REMARK 620 3 HOH A 570 O 80.0 76.7
REMARK 620 4 HOH A 627 O 138.7 113.9 76.6
REMARK 620 5 HOH B 524 O 86.2 164.0 118.7 76.1
REMARK 620 6 HOH B 575 O 82.8 83.6 153.0 128.9 80.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 48 O
REMARK 620 2 SER B 51 O 75.1
REMARK 620 3 SER B 51 OG 89.7 66.0
REMARK 620 4 TYR B 66 OH 114.9 169.8 110.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 301 through NAG A 302 bound to ASN A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 301 through NAG B 302 bound to ASN B 161
DBREF 5X6S A 1 275 UNP Q92194 AXE1_ASPAW 30 304
DBREF 5X6S B 1 275 UNP Q92194 AXE1_ASPAW 30 304
SEQRES 1 A 275 SER GLY SER LEU GLN GLN VAL THR ASP PHE GLY ASP ASN
SEQRES 2 A 275 PRO THR ASN VAL GLY MET TYR ILE TYR VAL PRO ASN ASN
SEQRES 3 A 275 LEU ALA SER ASN PRO GLY ILE VAL VAL ALA ILE HIS TYR
SEQRES 4 A 275 CYS THR GLY THR GLY PRO GLY TYR TYR GLY ASP SER PRO
SEQRES 5 A 275 TYR ALA THR LEU SER GLU GLN TYR GLY PHE ILE VAL ILE
SEQRES 6 A 275 TYR PRO SER SER PRO TYR SER GLY GLY CYS TRP ASP VAL
SEQRES 7 A 275 SER SER GLN ALA THR LEU THR HIS ASN GLY GLY GLY ASN
SEQRES 8 A 275 SER ASN SER ILE ALA ASN MET VAL THR TRP THR ILE SER
SEQRES 9 A 275 LYS TYR GLY ALA ASP SER SER LYS VAL PHE VAL THR GLY
SEQRES 10 A 275 SER SER SER GLY ALA MET MET THR ASN VAL MET ALA ALA
SEQRES 11 A 275 THR TYR PRO GLU LEU PHE ALA ALA ALA THR VAL TYR SER
SEQRES 12 A 275 GLY VAL SER ALA GLY CYS PHE TYR SER ASN THR ASN GLN
SEQRES 13 A 275 VAL ASP GLY TRP ASN SER THR CYS ALA GLN GLY ASP VAL
SEQRES 14 A 275 ILE THR THR PRO GLU HIS TRP ALA SER ILE ALA GLU ALA
SEQRES 15 A 275 MET TYR SER GLY TYR SER GLY SER ARG PRO ARG MET GLN
SEQRES 16 A 275 ILE TYR HIS GLY SER ILE ASP THR THR LEU TYR PRO GLN
SEQRES 17 A 275 ASN TYR TYR GLU THR CYS LYS GLN TRP ALA GLY VAL PHE
SEQRES 18 A 275 GLY TYR ASP TYR SER ALA PRO GLU LYS THR GLU ALA ASN
SEQRES 19 A 275 THR PRO GLN THR ASN TYR GLU THR THR ILE TRP GLY ASP
SEQRES 20 A 275 SER LEU GLN GLY ILE PHE ALA THR GLY VAL GLY HIS THR
SEQRES 21 A 275 VAL PRO ILE HIS GLY ASP LYS ASP MET GLU TRP PHE GLY
SEQRES 22 A 275 PHE ALA
SEQRES 1 B 275 SER GLY SER LEU GLN GLN VAL THR ASP PHE GLY ASP ASN
SEQRES 2 B 275 PRO THR ASN VAL GLY MET TYR ILE TYR VAL PRO ASN ASN
SEQRES 3 B 275 LEU ALA SER ASN PRO GLY ILE VAL VAL ALA ILE HIS TYR
SEQRES 4 B 275 CYS THR GLY THR GLY PRO GLY TYR TYR GLY ASP SER PRO
SEQRES 5 B 275 TYR ALA THR LEU SER GLU GLN TYR GLY PHE ILE VAL ILE
SEQRES 6 B 275 TYR PRO SER SER PRO TYR SER GLY GLY CYS TRP ASP VAL
SEQRES 7 B 275 SER SER GLN ALA THR LEU THR HIS ASN GLY GLY GLY ASN
SEQRES 8 B 275 SER ASN SER ILE ALA ASN MET VAL THR TRP THR ILE SER
SEQRES 9 B 275 LYS TYR GLY ALA ASP SER SER LYS VAL PHE VAL THR GLY
SEQRES 10 B 275 SER SER SER GLY ALA MET MET THR ASN VAL MET ALA ALA
SEQRES 11 B 275 THR TYR PRO GLU LEU PHE ALA ALA ALA THR VAL TYR SER
SEQRES 12 B 275 GLY VAL SER ALA GLY CYS PHE TYR SER ASN THR ASN GLN
SEQRES 13 B 275 VAL ASP GLY TRP ASN SER THR CYS ALA GLN GLY ASP VAL
SEQRES 14 B 275 ILE THR THR PRO GLU HIS TRP ALA SER ILE ALA GLU ALA
SEQRES 15 B 275 MET TYR SER GLY TYR SER GLY SER ARG PRO ARG MET GLN
SEQRES 16 B 275 ILE TYR HIS GLY SER ILE ASP THR THR LEU TYR PRO GLN
SEQRES 17 B 275 ASN TYR TYR GLU THR CYS LYS GLN TRP ALA GLY VAL PHE
SEQRES 18 B 275 GLY TYR ASP TYR SER ALA PRO GLU LYS THR GLU ALA ASN
SEQRES 19 B 275 THR PRO GLN THR ASN TYR GLU THR THR ILE TRP GLY ASP
SEQRES 20 B 275 SER LEU GLN GLY ILE PHE ALA THR GLY VAL GLY HIS THR
SEQRES 21 B 275 VAL PRO ILE HIS GLY ASP LYS ASP MET GLU TRP PHE GLY
SEQRES 22 B 275 PHE ALA
MODRES 5X6S NAG A 301 NAG -D
MODRES 5X6S NAG A 302 NAG -D
MODRES 5X6S NAG B 301 NAG -D
MODRES 5X6S NAG B 302 NAG -D
HET NAG A 301 14
HET NAG A 302 14
HET MES A 303 12
HET NA A 304 1
HET NA A 305 1
HET NAG B 301 14
HET NAG B 302 14
HET MES B 303 12
HET MES B 304 12
HET NA B 305 1
HET NA B 306 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM NA SODIUM ION
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 MES 3(C6 H13 N O4 S)
FORMUL 5 NA 4(NA 1+)
FORMUL 12 HOH *510(H2 O)
HELIX 1 AA1 THR A 43 ASP A 50 1 8
HELIX 2 AA2 PRO A 52 GLY A 61 1 10
HELIX 3 AA3 GLY A 90 GLY A 107 1 18
HELIX 4 AA4 SER A 119 TYR A 132 1 14
HELIX 5 AA5 PRO A 133 PHE A 136 5 4
HELIX 6 AA6 ASN A 161 GLN A 166 1 6
HELIX 7 AA7 THR A 172 MET A 183 1 12
HELIX 8 AA8 PRO A 207 GLY A 222 1 16
HELIX 9 AA9 HIS A 264 GLY A 273 1 10
HELIX 10 AB1 THR B 43 ASP B 50 1 8
HELIX 11 AB2 PRO B 52 GLY B 61 1 10
HELIX 12 AB3 GLY B 90 GLY B 107 1 18
HELIX 13 AB4 SER B 119 TYR B 132 1 14
HELIX 14 AB5 PRO B 133 PHE B 136 5 4
HELIX 15 AB6 ASN B 161 GLN B 166 1 6
HELIX 16 AB7 THR B 172 ALA B 182 1 11
HELIX 17 AB8 MET B 183 SER B 185 5 3
HELIX 18 AB9 PRO B 207 GLY B 222 1 16
HELIX 19 AC1 HIS B 264 GLY B 273 1 10
SHEET 1 AA110 SER A 3 VAL A 7 0
SHEET 2 AA110 GLY A 18 VAL A 23 -1 O ILE A 21 N GLN A 5
SHEET 3 AA110 ILE A 63 SER A 68 -1 O TYR A 66 N TYR A 20
SHEET 4 AA110 ILE A 33 ILE A 37 1 N ALA A 36 O ILE A 65
SHEET 5 AA110 VAL A 113 SER A 118 1 O THR A 116 N ILE A 37
SHEET 6 AA110 ALA A 138 TYR A 142 1 O TYR A 142 N GLY A 117
SHEET 7 AA110 ARG A 193 GLY A 199 1 O TYR A 197 N VAL A 141
SHEET 8 AA110 LEU A 249 ALA A 254 1 O ILE A 252 N ILE A 196
SHEET 9 AA110 TYR A 240 GLY A 246 -1 N THR A 243 O GLY A 251
SHEET 10 AA110 LYS A 230 GLU A 232 -1 N GLU A 232 O THR A 242
SHEET 1 AA210 SER B 3 VAL B 7 0
SHEET 2 AA210 GLY B 18 VAL B 23 -1 O MET B 19 N VAL B 7
SHEET 3 AA210 ILE B 63 SER B 68 -1 O TYR B 66 N TYR B 20
SHEET 4 AA210 ILE B 33 ILE B 37 1 N VAL B 34 O ILE B 65
SHEET 5 AA210 VAL B 113 SER B 118 1 O PHE B 114 N VAL B 35
SHEET 6 AA210 ALA B 138 TYR B 142 1 O TYR B 142 N GLY B 117
SHEET 7 AA210 ARG B 193 GLY B 199 1 O GLN B 195 N VAL B 141
SHEET 8 AA210 LEU B 249 ALA B 254 1 O ILE B 252 N ILE B 196
SHEET 9 AA210 TYR B 240 GLY B 246 -1 N THR B 243 O GLY B 251
SHEET 10 AA210 LYS B 230 GLU B 232 -1 N GLU B 232 O THR B 242
SSBOND 1 CYS A 40 CYS A 75 1555 1555 2.01
SSBOND 2 CYS A 149 CYS A 164 1555 1555 2.02
SSBOND 3 CYS B 40 CYS B 75 1555 1555 2.04
SSBOND 4 CYS B 149 CYS B 164 1555 1555 2.02
LINK OD1 ASN A 30 NA NA A 304 1555 1555 2.39
LINK O GLU A 134 NA NA A 305 1555 1555 2.94
LINK ND2 ASN A 161 C1 NAG A 301 1555 1555 1.44
LINK OD1 ASN B 30 NA NA B 306 1555 1555 2.32
LINK O TYR B 48 NA NA B 305 1555 1555 2.79
LINK O SER B 51 NA NA B 305 1555 1555 3.08
LINK OG SER B 51 NA NA B 305 1555 1555 2.82
LINK OH TYR B 66 NA NA B 305 1555 1555 2.72
LINK O GLU B 134 NA NA A 305 1555 1555 2.59
LINK ND2 ASN B 161 C1 NAG B 301 1555 1555 1.35
LINK O4 NAG A 301 C1 NAG A 302 1555 1555 1.42
LINK NA NA A 304 O HOH A 488 1555 1555 2.55
LINK NA NA A 304 O HOH B 588 1555 1555 2.53
LINK NA NA A 304 O HOH B 433 1555 1555 2.24
LINK NA NA A 304 O HOH A 604 1555 1555 2.37
LINK NA NA A 305 O HOH B 551 1555 1555 2.40
LINK NA NA A 305 O HOH A 607 1555 1555 2.00
LINK O4 NAG B 301 C1 NAG B 302 1555 1555 1.41
LINK NA NA B 306 O HOH A 445 1555 1555 2.38
LINK NA NA B 306 O HOH A 570 1555 1555 2.60
LINK NA NA B 306 O HOH A 627 1555 1555 2.50
LINK NA NA B 306 O HOH B 524 1555 1555 2.31
LINK NA NA B 306 O HOH B 575 1555 1555 2.53
CISPEP 1 THR A 235 PRO A 236 0 5.40
CISPEP 2 HIS A 259 THR A 260 0 -3.13
CISPEP 3 THR B 235 PRO B 236 0 5.30
CISPEP 4 HIS B 259 THR B 260 0 3.91
SITE 1 AC1 10 TYR A 48 GLY A 49 SER A 51 THR A 55
SITE 2 AC1 10 HOH A 403 HOH A 427 HOH A 439 HOH A 532
SITE 3 AC1 10 GLN B 6 TYR B 20
SITE 1 AC2 6 ASN A 30 HOH A 488 HOH A 604 ASP B 12
SITE 2 AC2 6 HOH B 433 HOH B 588
SITE 1 AC3 4 GLU A 134 HOH A 607 GLU B 134 HOH B 551
SITE 1 AC4 8 GLN A 6 TYR A 20 TYR B 48 GLY B 49
SITE 2 AC4 8 SER B 51 THR B 55 HOH B 461 HOH B 539
SITE 1 AC5 11 GLU A 232 ALA A 233 THR A 235 HOH A 440
SITE 2 AC5 11 GLN B 166 GLY B 167 ASP B 168 TYR B 206
SITE 3 AC5 11 PRO B 207 GLN B 208 HOH B 414
SITE 1 AC6 5 TYR B 48 SER B 51 TYR B 53 ALA B 54
SITE 2 AC6 5 TYR B 66
SITE 1 AC7 6 HOH A 445 HOH A 570 HOH A 627 ASN B 30
SITE 2 AC7 6 HOH B 524 HOH B 575
SITE 1 AC8 10 CYS A 149 TYR A 151 SER A 152 ASN A 153
SITE 2 AC8 10 ASN A 161 VAL A 169 HIS A 175 ILE A 179
SITE 3 AC8 10 HOH A 519 HOH A 600
SITE 1 AC9 14 CYS B 149 TYR B 151 SER B 152 ASN B 153
SITE 2 AC9 14 ASN B 161 VAL B 169 HIS B 175 ILE B 179
SITE 3 AC9 14 HOH B 401 HOH B 426 HOH B 499 HOH B 531
SITE 4 AC9 14 HOH B 535 HOH B 572
CRYST1 174.151 174.151 50.708 90.00 90.00 120.00 H 3 18
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 0.005742 0.003315 0.000000 0.00000
SCALE2 0.000000 0.006630 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019721 0.00000
TER 2075 ALA A 275
TER 4150 ALA B 275
MASTER 408 0 11 19 20 0 22 6 4754 2 127 44
END |