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HEADER HYDROLASE 17-DEC-17 6FAT
TITLE THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM
TITLE 2 OXYSPORUM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;
SOURCE 3 ORGANISM_COMMON: FUSARIUM VASCULAR WILT;
SOURCE 4 ORGANISM_TAXID: 5507;
SOURCE 5 GENE: FAEC;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS FERULIC ACID ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DIMAROGONA,E.D.CHRYSINA
REVDAT 1 30-JAN-19 6FAT 0
JRNL AUTH M.DIMAROGONA,E.D.CHRYSINA
JRNL TITL THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM
JRNL TITL 2 OXYSPORUM.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.MOUKOULI,E.TOPAKAS,P.CHRISTAKOPOULOS
REMARK 1 TITL CLONING, CHARACTERIZATION AND FUNCTIONAL EXPRESSION OF AN
REMARK 1 TITL 2 ALKALITOLERANT TYPE C FERULOYL ESTERASE FROM FUSARIUM
REMARK 1 TITL 3 OXYSPORUM.
REMARK 1 REF APPL. MICROBIOL. BIOTECHNOL. V. 79 245 2008
REMARK 1 REFN ISSN 0175-7598
REMARK 1 PMID 18414848
REMARK 1 DOI 10.1007/S00253-008-1432-3
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 102.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 49493
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 : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2634
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3638
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7910
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 407
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 2.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.373
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.218
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.882
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8600 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7454 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11731 ; 1.072 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17324 ; 0.862 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1056 ;17.770 ; 5.398
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 380 ;34.272 ;24.132
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1222 ;11.272 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;13.997 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1316 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9357 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1753 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4068 ; 0.565 ; 3.532
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4067 ; 0.565 ; 3.531
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5077 ; 1.051 ; 5.296
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5078 ; 1.051 ; 5.297
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4532 ; 0.437 ; 3.665
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4532 ; 0.437 ; 3.665
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6654 ; 0.807 ; 5.482
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9554 ; 1.994 ;41.463
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9497 ; 1.926 ;41.417
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 6FAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200008019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2395
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 102.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 0.0950
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3WMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) PEG400, 0.1M TRIS-HCL PH 8.5
REMARK 280 BUFFER, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.73350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLN A 544
REMARK 465 LYS A 545
REMARK 465 LEU A 546
REMARK 465 ILE A 547
REMARK 465 SER A 548
REMARK 465 GLU A 549
REMARK 465 GLU A 550
REMARK 465 ASP A 551
REMARK 465 LEU A 552
REMARK 465 ASN A 553
REMARK 465 SER A 554
REMARK 465 ALA A 555
REMARK 465 VAL A 556
REMARK 465 ASP A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 GLN B 544
REMARK 465 LYS B 545
REMARK 465 LEU B 546
REMARK 465 ILE B 547
REMARK 465 SER B 548
REMARK 465 GLU B 549
REMARK 465 GLU B 550
REMARK 465 ASP B 551
REMARK 465 LEU B 552
REMARK 465 ASN B 553
REMARK 465 SER B 554
REMARK 465 ALA B 555
REMARK 465 VAL B 556
REMARK 465 ASP B 557
REMARK 465 HIS B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 HIS B 562
REMARK 465 HIS B 563
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 170 -39.06 -143.06
REMARK 500 SER A 201 -111.26 62.36
REMARK 500 ALA A 225 55.26 36.15
REMARK 500 ALA A 227 38.08 -83.44
REMARK 500 ASP A 270 -80.15 -77.17
REMARK 500 LYS A 302 -68.39 -145.87
REMARK 500 PHE A 317 35.84 -93.06
REMARK 500 ASN A 383 72.47 39.73
REMARK 500 CYS A 453 -46.98 73.26
REMARK 500 LYS A 472 51.95 -119.54
REMARK 500 LYS A 527 -52.21 -161.21
REMARK 500 TYR B 170 -33.81 -147.84
REMARK 500 SER B 201 -112.93 67.00
REMARK 500 ALA B 225 54.12 33.05
REMARK 500 ALA B 227 40.43 -82.38
REMARK 500 ASP B 270 -80.73 -80.28
REMARK 500 PHE B 317 34.57 -91.36
REMARK 500 CYS B 453 -39.38 74.67
REMARK 500 LYS B 527 -61.47 -128.62
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 B 897 DISTANCE = 6.82 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 CA A 613 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 270 OD1
REMARK 620 2 ASP A 274 OD1 105.3
REMARK 620 3 ASP A 274 OD2 84.9 46.3
REMARK 620 4 VAL A 276 O 90.0 81.8 123.4
REMARK 620 5 ASP A 278 OD1 96.4 149.6 159.6 77.0
REMARK 620 6 ILE A 280 O 70.9 123.1 77.3 151.3 83.9
REMARK 620 7 HOH A 745 O 154.4 86.2 87.1 114.5 83.0 83.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 622 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 270 OD1
REMARK 620 2 ASP B 274 OD1 110.6
REMARK 620 3 ASP B 274 OD2 92.3 46.2
REMARK 620 4 VAL B 276 O 87.2 82.8 124.9
REMARK 620 5 ASP B 278 OD1 89.0 151.1 158.1 76.9
REMARK 620 6 ILE B 280 O 68.4 124.2 78.1 148.1 82.2
REMARK 620 7 HOH B 799 O 152.2 89.9 88.8 114.6 80.2 84.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through BMA A 603 bound to ASN A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through BMA A 607 bound to ASN A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 608 through MAN A 612 bound to ASN A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 601 through NAG B 602 bound to ASN B 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 101
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 800 604 through MAN B 610 bound to ASN B 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 611 through MAN B 621 bound to ASN B 362
DBREF1 6FAT A 36 563 UNP A0A1D3S5H0_FUSOX
DBREF2 6FAT A A0A1D3S5H0 36 563
DBREF1 6FAT B 36 563 UNP A0A1D3S5H0_FUSOX
DBREF2 6FAT B A0A1D3S5H0 36 563
SEQRES 1 A 528 ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU
SEQRES 2 A 528 LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL
SEQRES 3 A 528 PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO
SEQRES 4 A 528 THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE
SEQRES 5 A 528 CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER
SEQRES 6 A 528 ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR
SEQRES 7 A 528 GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY
SEQRES 8 A 528 CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE
SEQRES 9 A 528 GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY
SEQRES 10 A 528 THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL
SEQRES 11 A 528 GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL
SEQRES 12 A 528 LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS
SEQRES 13 A 528 HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY
SEQRES 14 A 528 ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP
SEQRES 15 A 528 PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE
SEQRES 16 A 528 ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE
SEQRES 17 A 528 THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU
SEQRES 18 A 528 GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS
SEQRES 19 A 528 ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU
SEQRES 20 A 528 ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL
SEQRES 21 A 528 CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO
SEQRES 22 A 528 GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR
SEQRES 23 A 528 GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO
SEQRES 24 A 528 GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN
SEQRES 25 A 528 PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE
SEQRES 26 A 528 TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO
SEQRES 27 A 528 ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN
SEQRES 28 A 528 VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS
SEQRES 29 A 528 ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP
SEQRES 30 A 528 GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN
SEQRES 31 A 528 HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU
SEQRES 32 A 528 ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY
SEQRES 33 A 528 HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN
SEQRES 34 A 528 ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN
SEQRES 35 A 528 VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN
SEQRES 36 A 528 ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY
SEQRES 37 A 528 ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS
SEQRES 38 A 528 ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN
SEQRES 39 A 528 TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU
SEQRES 40 A 528 GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA
SEQRES 41 A 528 VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 528 ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU
SEQRES 2 B 528 LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL
SEQRES 3 B 528 PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO
SEQRES 4 B 528 THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE
SEQRES 5 B 528 CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER
SEQRES 6 B 528 ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR
SEQRES 7 B 528 GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY
SEQRES 8 B 528 CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE
SEQRES 9 B 528 GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY
SEQRES 10 B 528 THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL
SEQRES 11 B 528 GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL
SEQRES 12 B 528 LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS
SEQRES 13 B 528 HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY
SEQRES 14 B 528 ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP
SEQRES 15 B 528 PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE
SEQRES 16 B 528 ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE
SEQRES 17 B 528 THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU
SEQRES 18 B 528 GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS
SEQRES 19 B 528 ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU
SEQRES 20 B 528 ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL
SEQRES 21 B 528 CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO
SEQRES 22 B 528 GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR
SEQRES 23 B 528 GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO
SEQRES 24 B 528 GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN
SEQRES 25 B 528 PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE
SEQRES 26 B 528 TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO
SEQRES 27 B 528 ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN
SEQRES 28 B 528 VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS
SEQRES 29 B 528 ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP
SEQRES 30 B 528 GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN
SEQRES 31 B 528 HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU
SEQRES 32 B 528 ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY
SEQRES 33 B 528 HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN
SEQRES 34 B 528 ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN
SEQRES 35 B 528 VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN
SEQRES 36 B 528 ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY
SEQRES 37 B 528 ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS
SEQRES 38 B 528 ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN
SEQRES 39 B 528 TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU
SEQRES 40 B 528 GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA
SEQRES 41 B 528 VAL ASP HIS HIS HIS HIS HIS HIS
MODRES 6FAT CYS A 41 CYS S
MODRES 6FAT CYS A 76 CYS S
MODRES 6FAT CYS A 200 CYS S
MODRES 6FAT CYS A 269 CYS S
MODRES 6FAT CYS A 296 CYS S
MODRES 6FAT CYS A 516 CYS S
MODRES 6FAT CYS A 88 CYS S
MODRES 6FAT CYS A 127 CYS S
MODRES 6FAT CYS A 453 CYS S
MODRES 6FAT CYS A 287 CYS S
MODRES 6FAT CYS A 304 CYS S
MODRES 6FAT CYS A 538 CYS S
MODRES 6FAT CYS B 41 CYS S
MODRES 6FAT CYS B 76 CYS S
MODRES 6FAT CYS B 200 CYS S
MODRES 6FAT CYS B 269 CYS S
MODRES 6FAT CYS B 296 CYS S
MODRES 6FAT CYS B 516 CYS S
MODRES 6FAT CYS B 88 CYS S
MODRES 6FAT CYS B 127 CYS S
MODRES 6FAT CYS B 453 CYS S
MODRES 6FAT CYS B 287 CYS S
MODRES 6FAT CYS B 304 CYS S
MODRES 6FAT CYS B 538 CYS S
HET NAG A 601 14
HET NAG A 602 14
HET BMA A 603 11
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET BMA A 607 11
HET NAG A 608 14
HET NAG A 609 14
HET BMA A 610 11
HET MAN A 611 11
HET MAN A 612 11
HET CA A 613 1
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET BMA B 606 11
HET MAN B 607 11
HET MAN B 608 11
HET MAN B 609 11
HET MAN B 610 11
HET NAG B 611 14
HET NAG B 612 14
HET BMA B 613 11
HET MAN B 614 11
HET MAN B 615 11
HET MAN B 616 11
HET MAN B 617 11
HET MAN B 618 11
HET MAN B 619 11
HET MAN B 620 11
HET MAN B 621 11
HET CA B 622 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM CA CALCIUM ION
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 3 BMA 5(C6 H12 O6)
FORMUL 6 MAN 14(C6 H12 O6)
FORMUL 7 CA 2(CA 2+)
FORMUL 13 HOH *357(H2 O)
HELIX 1 AA1 ASP A 36 LEU A 48 1 13
HELIX 2 AA2 GLN A 129 PHE A 139 1 11
HELIX 3 AA3 ALA A 155 TYR A 159 5 5
HELIX 4 AA4 ASN A 161 TYR A 170 1 10
HELIX 5 AA5 TYR A 170 GLY A 189 1 20
HELIX 6 AA6 SER A 201 PHE A 214 1 14
HELIX 7 AA7 ARG A 229 GLY A 245 1 17
HELIX 8 AA8 SER A 254 ASP A 270 1 17
HELIX 9 AA9 ASP A 270 GLY A 275 1 6
HELIX 10 AB1 ARG A 290 VAL A 295 5 6
HELIX 11 AB2 THR A 306 PHE A 317 1 12
HELIX 12 AB3 ASN A 323 GLY A 325 5 3
HELIX 13 AB4 GLY A 339 ILE A 344 1 6
HELIX 14 AB5 PHE A 349 VAL A 359 1 11
HELIX 15 AB6 ASP A 367 ILE A 371 5 5
HELIX 16 AB7 GLY A 372 ASN A 383 1 12
HELIX 17 AB8 PRO A 384 VAL A 387 5 4
HELIX 18 AB9 LEU A 394 ARG A 400 1 7
HELIX 19 AC1 SER A 416 GLY A 432 1 17
HELIX 20 AC2 SER A 434 ASP A 439 1 6
HELIX 21 AC3 GLU A 473 ASN A 476 5 4
HELIX 22 AC4 ASN A 477 GLY A 489 1 13
HELIX 23 AC5 ASN A 502 ALA A 504 5 3
HELIX 24 AC6 ASN A 532 ASP A 534 5 3
HELIX 25 AC7 PHE B 37 LEU B 48 1 12
HELIX 26 AC8 GLN B 129 PHE B 139 1 11
HELIX 27 AC9 ALA B 155 TYR B 159 5 5
HELIX 28 AD1 ASN B 161 TYR B 170 1 10
HELIX 29 AD2 TYR B 170 GLY B 189 1 20
HELIX 30 AD3 SER B 201 PHE B 214 1 14
HELIX 31 AD4 PRO B 215 PHE B 218 5 4
HELIX 32 AD5 ARG B 229 GLY B 245 1 17
HELIX 33 AD6 SER B 254 ASP B 270 1 17
HELIX 34 AD7 ASP B 270 GLY B 275 1 6
HELIX 35 AD8 ASP B 283 CYS B 287 5 5
HELIX 36 AD9 ARG B 290 VAL B 295 5 6
HELIX 37 AE1 THR B 306 PHE B 317 1 12
HELIX 38 AE2 ASN B 323 GLY B 325 5 3
HELIX 39 AE3 PHE B 349 VAL B 359 1 11
HELIX 40 AE4 GLY B 372 ASN B 383 1 12
HELIX 41 AE5 PRO B 384 VAL B 387 5 4
HELIX 42 AE6 LEU B 394 GLY B 401 1 8
HELIX 43 AE7 SER B 416 GLY B 432 1 17
HELIX 44 AE8 SER B 434 ASP B 439 1 6
HELIX 45 AE9 GLU B 473 ASN B 476 5 4
HELIX 46 AF1 ASN B 477 GLU B 488 1 12
HELIX 47 AF2 ASN B 502 ALA B 504 5 3
HELIX 48 AF3 ASN B 532 ASP B 534 5 3
SHEET 1 AA1 9 THR A 53 VAL A 61 0
SHEET 2 AA1 9 ILE A 87 GLY A 97 -1 O ARG A 89 N GLU A 59
SHEET 3 AA1 9 SER A 100 PRO A 109 -1 O LEU A 102 N VAL A 94
SHEET 4 AA1 9 ALA A 142 GLY A 145 -1 O THR A 143 N TRP A 107
SHEET 5 AA1 9 PHE A 116 THR A 119 1 N THR A 119 O VAL A 144
SHEET 6 AA1 9 SER A 195 CYS A 200 1 O LEU A 198 N SER A 118
SHEET 7 AA1 9 GLY A 220 GLY A 224 1 O GLY A 224 N GLY A 199
SHEET 8 AA1 9 LYS A 403 GLY A 409 1 O ILE A 405 N ILE A 221
SHEET 9 AA1 9 TYR A 442 VAL A 447 1 O PHE A 445 N HIS A 406
SHEET 1 AA2 2 ASN A 66 THR A 68 0
SHEET 2 AA2 2 SER A 80 ILE A 82 -1 O THR A 81 N ILE A 67
SHEET 1 AA3 2 LEU A 320 TYR A 321 0
SHEET 2 AA3 2 TYR A 327 TYR A 329 -1 O TYR A 329 N LEU A 320
SHEET 1 AA4 2 THR A 494 TYR A 500 0
SHEET 2 AA4 2 VAL A 509 CYS A 516 -1 O VAL A 511 N ARG A 499
SHEET 1 AA5 2 ARG A 521 TRP A 524 0
SHEET 2 AA5 2 TRP A 536 GLU A 539 -1 O LYS A 537 N VAL A 523
SHEET 1 AA6 9 THR B 53 VAL B 61 0
SHEET 2 AA6 9 ILE B 87 GLY B 97 -1 O ARG B 89 N GLU B 59
SHEET 3 AA6 9 SER B 100 PRO B 109 -1 O LEU B 102 N VAL B 94
SHEET 4 AA6 9 ALA B 142 ALA B 146 -1 O THR B 143 N TRP B 107
SHEET 5 AA6 9 PHE B 116 THR B 119 1 N LEU B 117 O ALA B 142
SHEET 6 AA6 9 SER B 195 CYS B 200 1 O TYR B 196 N PHE B 116
SHEET 7 AA6 9 GLY B 220 GLY B 224 1 O GLY B 224 N GLY B 199
SHEET 8 AA6 9 LYS B 403 GLY B 409 1 O ILE B 405 N ILE B 221
SHEET 9 AA6 9 TYR B 442 VAL B 447 1 O PHE B 445 N HIS B 406
SHEET 1 AA7 2 ASN B 66 THR B 68 0
SHEET 2 AA7 2 SER B 80 ILE B 82 -1 O THR B 81 N ILE B 67
SHEET 1 AA8 2 LEU B 320 TYR B 321 0
SHEET 2 AA8 2 TYR B 327 TYR B 329 -1 O TYR B 329 N LEU B 320
SHEET 1 AA9 2 THR B 494 TYR B 500 0
SHEET 2 AA9 2 VAL B 509 CYS B 516 -1 O GLU B 510 N ARG B 499
SHEET 1 AB1 2 ARG B 521 TRP B 524 0
SHEET 2 AB1 2 TRP B 536 GLU B 539 -1 O GLU B 539 N ARG B 521
SSBOND 1 CYS A 41 CYS A 88 1555 1555 2.04
SSBOND 2 CYS A 76 CYS A 127 1555 1555 2.03
SSBOND 3 CYS A 200 CYS A 453 1555 1555 2.04
SSBOND 4 CYS A 269 CYS A 287 1555 1555 2.04
SSBOND 5 CYS A 296 CYS A 304 1555 1555 2.03
SSBOND 6 CYS A 516 CYS A 538 1555 1555 2.03
SSBOND 7 CYS B 41 CYS B 88 1555 1555 2.04
SSBOND 8 CYS B 76 CYS B 127 1555 1555 2.03
SSBOND 9 CYS B 200 CYS B 453 1555 1555 2.04
SSBOND 10 CYS B 269 CYS B 287 1555 1555 2.04
SSBOND 11 CYS B 296 CYS B 304 1555 1555 2.04
SSBOND 12 CYS B 516 CYS B 538 1555 1555 2.03
LINK ND2 ASN A 66 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 101 C1 NAG A 604 1555 1555 1.45
LINK ND2 ASN A 151 C1 NAG A 605 1555 1555 1.44
LINK OD1 ASP A 270 CA CA A 613 1555 1555 2.32
LINK OD1 ASP A 274 CA CA A 613 1555 1555 2.33
LINK OD2 ASP A 274 CA CA A 613 1555 1555 3.01
LINK O VAL A 276 CA CA A 613 1555 1555 2.33
LINK OD1 ASP A 278 CA CA A 613 1555 1555 2.32
LINK O ILE A 280 CA CA A 613 1555 1555 2.32
LINK ND2 ASN A 362 C1 NAG A 608 1555 1555 1.44
LINK ND2 ASN B 66 C1 NAG B 601 1555 1555 1.45
LINK ND2 ASN B 101 C1 NAG B 603 1555 1555 1.44
LINK ND2 ASN B 151 C1 NAG B 604 1555 1555 1.44
LINK OD1 ASP B 270 CA CA B 622 1555 1555 2.32
LINK OD1 ASP B 274 CA CA B 622 1555 1555 2.33
LINK OD2 ASP B 274 CA CA B 622 1555 1555 3.01
LINK O VAL B 276 CA CA B 622 1555 1555 2.33
LINK OD1 ASP B 278 CA CA B 622 1555 1555 2.32
LINK O ILE B 280 CA CA B 622 1555 1555 2.33
LINK ND2 ASN B 362 C1 NAG B 611 1555 1555 1.44
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.44
LINK O4 NAG A 602 C1 BMA A 603 1555 1555 1.44
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.44
LINK O4 NAG A 606 C1 BMA A 607 1555 1555 1.45
LINK O4 NAG A 608 C1 NAG A 609 1555 1555 1.45
LINK O4 NAG A 609 C1 BMA A 610 1555 1555 1.44
LINK O6 BMA A 610 C1 MAN A 611 1555 1555 1.45
LINK O3 MAN A 611 C1 MAN A 612 1555 1555 1.45
LINK CA CA A 613 O HOH A 745 1555 1555 2.50
LINK O4 NAG B 601 C1 NAG B 602 1555 1555 1.44
LINK O4 NAG B 604 C1 NAG B 605 1555 1555 1.44
LINK O4 NAG B 605 C1 BMA B 606 1555 1555 1.44
LINK O3 BMA B 606 C1 MAN B 608 1555 1555 1.44
LINK O6 BMA B 606 C1 MAN B 607 1555 1555 1.44
LINK O2 MAN B 608 C1 MAN B 609 1555 1555 1.44
LINK O2 MAN B 609 C1 MAN B 610 1555 1555 1.44
LINK O4 NAG B 611 C1 NAG B 612 1555 1555 1.44
LINK O4 NAG B 612 C1 BMA B 613 1555 1555 1.44
LINK O3 BMA B 613 C1 MAN B 618 1555 1555 1.44
LINK O6 BMA B 613 C1 MAN B 614 1555 1555 1.44
LINK O3 MAN B 614 C1 MAN B 615 1555 1555 1.44
LINK O6 MAN B 614 C1 MAN B 616 1555 1555 1.45
LINK O2 MAN B 616 C1 MAN B 617 1555 1555 1.45
LINK O2 MAN B 618 C1 MAN B 620 1555 1555 1.44
LINK O6 MAN B 618 C1 MAN B 619 1555 1555 1.46
LINK O2 MAN B 620 C1 MAN B 621 1555 1555 1.44
LINK CA CA B 622 O HOH B 799 1555 1555 2.41
CISPEP 1 THR A 77 PRO A 78 0 1.27
CISPEP 2 TYR A 518 PRO A 519 0 8.49
CISPEP 3 THR B 77 PRO B 78 0 0.52
CISPEP 4 TYR B 518 PRO B 519 0 8.57
SITE 1 AC1 6 ASP A 270 ASP A 274 VAL A 276 ASP A 278
SITE 2 AC1 6 ILE A 280 HOH A 745
SITE 1 AC2 6 ASP B 270 ASP B 274 VAL B 276 ASP B 278
SITE 2 AC2 6 ILE B 280 HOH B 799
SITE 1 AC3 3 ASN A 66 SER A 80 HOH A 785
SITE 1 AC4 5 PHE A 93 LYS A 99 ASN A 101 VAL A 164
SITE 2 AC4 5 LYS A 298
SITE 1 AC5 7 TRP A 56 PHE A 57 ASP A 71 ASN A 72
SITE 2 AC5 7 GLU A 105 ASN A 151 HOH A 790
SITE 1 AC6 17 ILE A 360 TRP A 361 ASN A 362 LYS A 378
SITE 2 AC6 17 VAL A 382 ASN A 383 PRO A 384 PHE A 385
SITE 3 AC6 17 ASN A 386 HOH A 720 HOH A 730 LYS B 194
SITE 4 AC6 17 ARG B 400 LYS B 403 GLU B 440 GLY B 489
SITE 5 AC6 17 HOH B 832
SITE 1 AC7 5 ASN B 66 THR B 68 SER B 80 ILE B 82
SITE 2 AC7 5 HOH B 714
SITE 1 AC8 4 ASN B 101 GLY B 149 VAL B 164 HOH B 756
SITE 1 AC9 10 TRP B 56 PHE B 57 ASP B 71 ASN B 101
SITE 2 AC9 10 THR B 103 GLU B 105 ASN B 151 HOH B 760
SITE 3 AC9 10 HOH B 816 HOH B 857
SITE 1 AD1 24 SER B 162 ILE B 360 TRP B 361 ASN B 362
SITE 2 AD1 24 LYS B 378 SER B 380 GLU B 381 VAL B 382
SITE 3 AD1 24 ASN B 383 PRO B 384 ASN B 386 GLU B 388
SITE 4 AD1 24 TRP B 390 GLU B 391 HOH B 706 HOH B 722
SITE 5 AD1 24 HOH B 738 HOH B 745 HOH B 780 HOH B 790
SITE 6 AD1 24 HOH B 793 HOH B 800 HOH B 818 HOH B 827
CRYST1 67.536 87.467 106.565 90.00 106.18 90.00 P 1 21 1 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 0.014807 0.000000 0.004295 0.00000
SCALE2 0.000000 0.011433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009771 0.00000
TER 3956 GLU A 543
TER 7915 GLU B 543
MASTER 416 0 35 48 34 0 26 6 8674 2 455 82
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