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HEADER HYDROLASE 27-JAN-25 9I50
TITLE CRYSTAL STRUCTURE OF FERULOYL ESTERASE FROM FUSARIUM OXYSPORUM G122S
TITLE 2 VARIANT
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;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;
SOURCE 3 ORGANISM_TAXID: 5507;
SOURCE 4 GENE: FAEC;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS PLASTIC DEGRADING ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.KARAMPA,M.DIMAROGONA,E.TOPAKAS,K.MAKRYNIOTIS,E.NIKOLAIVITS
REVDAT 1 01-APR-26 9I50 0
JRNL AUTH P.KARAMPA,K.MAKRYNIOTIS,T.I.SOUSANI,E.TOPAKAS,V.DASKALAKIS,
JRNL AUTH 2 M.DIMAROGONA
JRNL TITL STRUCTURAL INSIGHTS INTO AN ENGINEERED FERULOYL ESTERASE
JRNL TITL 2 WITH IMPROVED MHET DEGRADING PROPERTIES.
JRNL REF FEBS LETT. 2026
JRNL REFN ISSN 0014-5793
JRNL PMID 41797379
JRNL DOI 10.1002/1873-3468.70322
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 114.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 107314
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) : 0.162
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.067
REMARK 3 FREE R VALUE TEST SET COUNT : 5438
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
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) : 7532
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 388
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7914
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 614
REMARK 3 SOLVENT ATOMS : 606
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.49000
REMARK 3 B22 (A**2) : -3.10200
REMARK 3 B33 (A**2) : 0.00600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.86900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8857 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 7896 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12067 ; 1.582 ; 1.883
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18343 ; 0.559 ; 1.808
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1032 ; 6.830 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 44 ; 9.857 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1273 ;13.125 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1386 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10109 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2026 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1724 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 45 ; 0.215 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4432 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 524 ; 0.140 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.142 ; 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): 4107 ; 2.169 ; 3.356
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4107 ; 2.168 ; 3.356
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5146 ; 2.948 ; 6.027
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5147 ; 2.949 ; 6.028
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4750 ; 3.200 ; 3.817
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4751 ; 3.200 ; 3.818
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6921 ; 4.764 ; 6.815
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6922 ; 4.764 ; 6.815
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 36 A 577
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0722 -12.2206 -13.4412
REMARK 3 T TENSOR
REMARK 3 T11: 0.0420 T22: 0.0253
REMARK 3 T33: 0.0275 T12: 0.0123
REMARK 3 T13: 0.0156 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.8895 L22: 0.6762
REMARK 3 L33: 0.9405 L12: 0.2580
REMARK 3 L13: -0.3944 L23: -0.1992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.0443 S13: -0.0527
REMARK 3 S21: 0.0940 S22: 0.0279 S23: 0.0824
REMARK 3 S31: 0.0827 S32: -0.0471 S33: -0.0415
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6687 10.8356 -41.9311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0160 T22: 0.0152
REMARK 3 T33: 0.0196 T12: 0.0039
REMARK 3 T13: 0.0039 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.8445 L22: 0.7932
REMARK 3 L33: 0.8047 L12: 0.3659
REMARK 3 L13: -0.4262 L23: -0.3463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0168 S12: -0.0209 S13: 0.0565
REMARK 3 S21: -0.0012 S22: -0.0331 S23: -0.0629
REMARK 3 S31: -0.0759 S32: 0.0537 S33: 0.0163
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 9I50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1292144891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 8.0.016
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107339
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 114.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 10.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 114.0
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.02900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 41.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 8.0.016
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% (V/V) PEG400, 0.1M TRIS-HCL PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 44.63050
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, C, D, E
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, F, G
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 MET A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 THR A 6
REMARK 465 ASP A 7
REMARK 465 ILE A 8
REMARK 465 CYS A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 GLN A 12
REMARK 465 ASP A 13
REMARK 465 ASN A 14
REMARK 465 MET A 15
REMARK 465 ARG A 16
REMARK 465 PRO A 17
REMARK 465 THR A 18
REMARK 465 PHE A 19
REMARK 465 LEU A 20
REMARK 465 LEU A 21
REMARK 465 PHE A 22
REMARK 465 SER A 23
REMARK 465 GLY A 24
REMARK 465 LEU A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 27
REMARK 465 CYS A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 ALA A 31
REMARK 465 GLY A 32
REMARK 465 LYS A 33
REMARK 465 GLY A 34
REMARK 465 ASP A 35
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 SER B 1
REMARK 465 MET B 2
REMARK 465 ASP B 3
REMARK 465 THR B 4
REMARK 465 SER B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 ILE B 8
REMARK 465 CYS B 9
REMARK 465 LEU B 10
REMARK 465 PRO B 11
REMARK 465 GLN B 12
REMARK 465 ASP B 13
REMARK 465 ASN B 14
REMARK 465 MET B 15
REMARK 465 ARG B 16
REMARK 465 PRO B 17
REMARK 465 THR B 18
REMARK 465 PHE B 19
REMARK 465 LEU B 20
REMARK 465 LEU B 21
REMARK 465 PHE B 22
REMARK 465 SER B 23
REMARK 465 GLY B 24
REMARK 465 LEU B 25
REMARK 465 GLY B 26
REMARK 465 ALA B 27
REMARK 465 CYS B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 ALA B 31
REMARK 465 GLY B 32
REMARK 465 LYS B 33
REMARK 465 GLY B 34
REMARK 465 ASP B 35
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: 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 HH21 ARG B 513 O HOH B 708 1.59
REMARK 500 HO3 MAN G 8 O HOH B 759 1.59
REMARK 500 ND2 ASN B 362 C1 NAG G 1 1.72
REMARK 500 ND2 ASN A 151 C1 NAG D 1 1.74
REMARK 500 ND2 ASN B 151 C1 NAG F 1 1.75
REMARK 500 ND2 ASN A 66 C1 NAG C 1 1.76
REMARK 500 ND2 ASN B 101 C1 NAG B 601 1.80
REMARK 500 ND2 ASN A 362 C1 NAG E 1 1.82
REMARK 500 ND2 ASN A 101 C1 NAG A 601 1.85
REMARK 500 ND2 ASN B 66 C1 NAG B 609 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 229 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG B 513 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
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 ASN A 111 79.98 -100.05
REMARK 500 TYR A 170 -33.24 -152.86
REMARK 500 SER A 201 -128.31 77.23
REMARK 500 SER A 201 -128.31 84.67
REMARK 500 ALA A 225 55.39 35.54
REMARK 500 ALA A 227 42.28 -73.57
REMARK 500 ASP A 270 -94.43 -81.31
REMARK 500 LYS A 298 109.12 40.29
REMARK 500 LYS A 302 -92.88 -83.75
REMARK 500 ASN A 303 70.61 -107.05
REMARK 500 ASN A 383 62.58 38.37
REMARK 500 PHE A 441 -13.06 -142.95
REMARK 500 CYS A 453 -22.91 78.22
REMARK 500 LYS A 527 -48.50 -145.14
REMARK 500 TYR B 170 -29.06 -148.78
REMARK 500 SER B 201 -126.16 83.08
REMARK 500 SER B 201 -126.16 88.99
REMARK 500 ALA B 225 53.86 39.19
REMARK 500 ALA B 227 39.44 -73.24
REMARK 500 ASP B 270 -93.31 -86.24
REMARK 500 ASP B 439 -18.88 -48.98
REMARK 500 PHE B 441 -11.59 -146.66
REMARK 500 CYS B 453 -29.45 73.00
REMARK 500 LYS B 527 -57.73 -121.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 125 GLY A 126 135.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 229 0.15 SIDE CHAIN
REMARK 500 ARG A 290 0.09 SIDE CHAIN
REMARK 500 ARG B 229 0.11 SIDE CHAIN
REMARK 500 ARG B 513 0.12 SIDE CHAIN
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 982 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 984 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A 985 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A 988 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH B1016 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B1018 DISTANCE = 6.94 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG C 1
REMARK 610 NAG D 1
REMARK 610 NAG E 1
REMARK 610 NAG F 1
REMARK 610 NAG G 1
REMARK 610 NAG A 601
REMARK 610 NAG A 608
REMARK 610 NAG B 601
REMARK 610 NAG B 608
REMARK 610 NAG B 609
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 609 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 270 OD1
REMARK 620 2 ASP A 274 OD1 104.2
REMARK 620 3 ASP A 274 OD2 96.9 52.8
REMARK 620 4 VAL A 276 O 82.2 75.5 126.5
REMARK 620 5 ASP A 278 OD1 92.4 143.7 157.4 75.1
REMARK 620 6 ILE A 280 O 76.9 131.0 78.3 149.6 83.8
REMARK 620 7 HOH A 845 O 163.7 89.7 84.7 109.9 80.8 87.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 610 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 270 OD1
REMARK 620 2 ASP B 274 OD1 106.9
REMARK 620 3 ASP B 274 OD2 98.9 51.4
REMARK 620 4 VAL B 276 O 81.6 77.2 126.7
REMARK 620 5 ASP B 278 OD1 93.2 146.0 152.9 78.9
REMARK 620 6 ILE B 280 O 79.0 130.1 78.8 150.3 79.8
REMARK 620 7 HOH B 765 O 162.9 89.5 87.4 107.4 74.9 86.7
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FAT RELATED DB: PDB
REMARK 900 RELATED ID: 8BHH RELATED DB: PDB
DBREF1 9I50 A 1 563 UNP A0A1D3S5H0_FUSOX
DBREF2 9I50 A A0A1D3S5H0 1 563
DBREF1 9I50 B 1 563 UNP A0A1D3S5H0_FUSOX
DBREF2 9I50 B A0A1D3S5H0 1 563
SEQADV 9I50 SER A 122 UNP A0A1D3S5H GLY 122 ENGINEERED MUTATION
SEQADV 9I50 SER B 122 UNP A0A1D3S5H GLY 122 ENGINEERED MUTATION
SEQRES 1 A 563 SER MET ASP THR SER THR ASP ILE CYS LEU PRO GLN ASP
SEQRES 2 A 563 ASN MET ARG PRO THR PHE LEU LEU PHE SER GLY LEU GLY
SEQRES 3 A 563 ALA CYS ALA ALA ALA GLY LYS GLY ASP ASP PHE ALA ALA
SEQRES 4 A 563 LYS CYS ALA GLY PHE LYS THR SER LEU LYS LEU PRO ASN
SEQRES 5 A 563 THR LYS VAL TRP PHE THR GLU HIS VAL PRO ALA GLY LYS
SEQRES 6 A 563 ASN ILE THR PHE PRO ASP ASN HIS PRO THR CYS THR PRO
SEQRES 7 A 563 LYS SER THR ILE THR ASP VAL GLU ILE CYS ARG VAL ALA
SEQRES 8 A 563 MET PHE VAL THR THR GLY PRO LYS SER ASN LEU THR LEU
SEQRES 9 A 563 GLU ALA TRP LEU PRO SER ASN TRP THR GLY ARG PHE LEU
SEQRES 10 A 563 SER THR GLY ASN SER GLY MET ALA GLY CYS ILE GLN TYR
SEQRES 11 A 563 ASP ASP VAL ALA TYR GLY ALA GLY PHE GLY PHE ALA THR
SEQRES 12 A 563 VAL GLY ALA ASN ASN GLY HIS ASN GLY THR SER ALA VAL
SEQRES 13 A 563 SER MET TYR LYS ASN SER GLY VAL VAL GLU ASP TYR VAL
SEQRES 14 A 563 TYR ARG SER VAL HIS THR GLY THR VAL LEU GLY LYS GLU
SEQRES 15 A 563 LEU THR LYS LYS PHE TYR GLY LYS LYS HIS THR LYS SER
SEQRES 16 A 563 TYR TYR LEU GLY CYS SER THR GLY GLY ARG GLN GLY TRP
SEQRES 17 A 563 LYS GLU ALA GLN SER PHE PRO ASP ASP PHE ASP GLY ILE
SEQRES 18 A 563 VAL ALA GLY ALA PRO ALA MET ARG PHE ASN GLY LEU GLN
SEQRES 19 A 563 SER ARG SER GLY SER PHE TRP GLY ILE THR GLY PRO PRO
SEQRES 20 A 563 GLY ALA PRO THR HIS LEU SER PRO GLU GLU TRP ALA MET
SEQRES 21 A 563 VAL GLN LYS ASN VAL LEU VAL GLN CYS ASP GLU PRO LEU
SEQRES 22 A 563 ASP GLY VAL ALA ASP GLY ILE LEU GLU ASP PRO ASN LEU
SEQRES 23 A 563 CYS GLN TYR ARG PRO GLU ALA LEU VAL CYS SER LYS GLY
SEQRES 24 A 563 GLN THR LYS ASN CYS LEU THR GLY PRO GLN ILE GLU THR
SEQRES 25 A 563 VAL ARG LYS VAL PHE GLY PRO LEU TYR GLY ASN ASN GLY
SEQRES 26 A 563 THR TYR ILE TYR PRO ARG ILE PRO PRO GLY ALA ASP GLN
SEQRES 27 A 563 GLY PHE GLY PHE ALA ILE GLY GLU GLN PRO PHE PRO TYR
SEQRES 28 A 563 SER THR GLU TRP PHE GLN TYR VAL ILE TRP ASN ASP THR
SEQRES 29 A 563 LYS TRP ASP PRO ASN THR ILE GLY PRO ASN ASP TYR GLN
SEQRES 30 A 563 LYS ALA SER GLU VAL ASN PRO PHE ASN VAL GLU THR TRP
SEQRES 31 A 563 GLU GLY ASP LEU SER LYS PHE ARG LYS ARG GLY SER LYS
SEQRES 32 A 563 ILE ILE HIS TRP HIS GLY LEU GLU ASP GLY LEU ILE SER
SEQRES 33 A 563 SER ASP ASN SER MET GLU TYR TYR ASN HIS VAL SER ALA
SEQRES 34 A 563 THR MET GLY LEU SER ASN THR GLU LEU ASP GLU PHE TYR
SEQRES 35 A 563 ARG TYR PHE ARG VAL SER GLY CYS GLY HIS CYS SER GLY
SEQRES 36 A 563 GLY ILE GLY ALA ASN ARG ILE GLY ASN ASN ARG ALA ASN
SEQRES 37 A 563 LEU GLY GLY LYS GLU ALA LYS ASN ASN VAL LEU LEU ALA
SEQRES 38 A 563 LEU VAL LYS TRP VAL GLU GLU GLY GLN ALA PRO GLU THR
SEQRES 39 A 563 ILE THR GLY VAL ARG TYR VAL ASN GLY ALA THR THR GLY
SEQRES 40 A 563 LYS VAL GLU VAL GLU ARG ARG HIS CYS ARG TYR PRO TYR
SEQRES 41 A 563 ARG ASN VAL TRP ASP ARG LYS GLY ASN TYR LYS ASN PRO
SEQRES 42 A 563 ASP SER TRP LYS CYS GLU LEU PRO LEU GLU GLN LYS LEU
SEQRES 43 A 563 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 44 A 563 HIS HIS HIS HIS
SEQRES 1 B 563 SER MET ASP THR SER THR ASP ILE CYS LEU PRO GLN ASP
SEQRES 2 B 563 ASN MET ARG PRO THR PHE LEU LEU PHE SER GLY LEU GLY
SEQRES 3 B 563 ALA CYS ALA ALA ALA GLY LYS GLY ASP ASP PHE ALA ALA
SEQRES 4 B 563 LYS CYS ALA GLY PHE LYS THR SER LEU LYS LEU PRO ASN
SEQRES 5 B 563 THR LYS VAL TRP PHE THR GLU HIS VAL PRO ALA GLY LYS
SEQRES 6 B 563 ASN ILE THR PHE PRO ASP ASN HIS PRO THR CYS THR PRO
SEQRES 7 B 563 LYS SER THR ILE THR ASP VAL GLU ILE CYS ARG VAL ALA
SEQRES 8 B 563 MET PHE VAL THR THR GLY PRO LYS SER ASN LEU THR LEU
SEQRES 9 B 563 GLU ALA TRP LEU PRO SER ASN TRP THR GLY ARG PHE LEU
SEQRES 10 B 563 SER THR GLY ASN SER GLY MET ALA GLY CYS ILE GLN TYR
SEQRES 11 B 563 ASP ASP VAL ALA TYR GLY ALA GLY PHE GLY PHE ALA THR
SEQRES 12 B 563 VAL GLY ALA ASN ASN GLY HIS ASN GLY THR SER ALA VAL
SEQRES 13 B 563 SER MET TYR LYS ASN SER GLY VAL VAL GLU ASP TYR VAL
SEQRES 14 B 563 TYR ARG SER VAL HIS THR GLY THR VAL LEU GLY LYS GLU
SEQRES 15 B 563 LEU THR LYS LYS PHE TYR GLY LYS LYS HIS THR LYS SER
SEQRES 16 B 563 TYR TYR LEU GLY CYS SER THR GLY GLY ARG GLN GLY TRP
SEQRES 17 B 563 LYS GLU ALA GLN SER PHE PRO ASP ASP PHE ASP GLY ILE
SEQRES 18 B 563 VAL ALA GLY ALA PRO ALA MET ARG PHE ASN GLY LEU GLN
SEQRES 19 B 563 SER ARG SER GLY SER PHE TRP GLY ILE THR GLY PRO PRO
SEQRES 20 B 563 GLY ALA PRO THR HIS LEU SER PRO GLU GLU TRP ALA MET
SEQRES 21 B 563 VAL GLN LYS ASN VAL LEU VAL GLN CYS ASP GLU PRO LEU
SEQRES 22 B 563 ASP GLY VAL ALA ASP GLY ILE LEU GLU ASP PRO ASN LEU
SEQRES 23 B 563 CYS GLN TYR ARG PRO GLU ALA LEU VAL CYS SER LYS GLY
SEQRES 24 B 563 GLN THR LYS ASN CYS LEU THR GLY PRO GLN ILE GLU THR
SEQRES 25 B 563 VAL ARG LYS VAL PHE GLY PRO LEU TYR GLY ASN ASN GLY
SEQRES 26 B 563 THR TYR ILE TYR PRO ARG ILE PRO PRO GLY ALA ASP GLN
SEQRES 27 B 563 GLY PHE GLY PHE ALA ILE GLY GLU GLN PRO PHE PRO TYR
SEQRES 28 B 563 SER THR GLU TRP PHE GLN TYR VAL ILE TRP ASN ASP THR
SEQRES 29 B 563 LYS TRP ASP PRO ASN THR ILE GLY PRO ASN ASP TYR GLN
SEQRES 30 B 563 LYS ALA SER GLU VAL ASN PRO PHE ASN VAL GLU THR TRP
SEQRES 31 B 563 GLU GLY ASP LEU SER LYS PHE ARG LYS ARG GLY SER LYS
SEQRES 32 B 563 ILE ILE HIS TRP HIS GLY LEU GLU ASP GLY LEU ILE SER
SEQRES 33 B 563 SER ASP ASN SER MET GLU TYR TYR ASN HIS VAL SER ALA
SEQRES 34 B 563 THR MET GLY LEU SER ASN THR GLU LEU ASP GLU PHE TYR
SEQRES 35 B 563 ARG TYR PHE ARG VAL SER GLY CYS GLY HIS CYS SER GLY
SEQRES 36 B 563 GLY ILE GLY ALA ASN ARG ILE GLY ASN ASN ARG ALA ASN
SEQRES 37 B 563 LEU GLY GLY LYS GLU ALA LYS ASN ASN VAL LEU LEU ALA
SEQRES 38 B 563 LEU VAL LYS TRP VAL GLU GLU GLY GLN ALA PRO GLU THR
SEQRES 39 B 563 ILE THR GLY VAL ARG TYR VAL ASN GLY ALA THR THR GLY
SEQRES 40 B 563 LYS VAL GLU VAL GLU ARG ARG HIS CYS ARG TYR PRO TYR
SEQRES 41 B 563 ARG ASN VAL TRP ASP ARG LYS GLY ASN TYR LYS ASN PRO
SEQRES 42 B 563 ASP SER TRP LYS CYS GLU LEU PRO LEU GLU GLN LYS LEU
SEQRES 43 B 563 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 44 B 563 HIS HIS HIS HIS
HET NAG C 1 28
HET NAG C 2 27
HET BMA C 3 21
HET NAG D 1 28
HET NAG D 2 27
HET BMA D 3 21
HET MAN D 4 21
HET MAN D 5 21
HET MAN D 6 21
HET NAG E 1 28
HET NAG E 2 27
HET BMA E 3 21
HET MAN E 4 21
HET MAN E 5 21
HET MAN E 6 21
HET MAN E 7 21
HET MAN E 8 21
HET MAN E 9 21
HET NAG F 1 28
HET NAG F 2 27
HET BMA F 3 21
HET MAN F 4 21
HET MAN F 5 21
HET MAN F 6 21
HET MAN F 7 21
HET MAN F 8 21
HET MAN F 9 21
HET MAN F 10 21
HET NAG G 1 28
HET NAG G 2 27
HET BMA G 3 21
HET MAN G 4 21
HET MAN G 5 21
HET MAN G 6 21
HET MAN G 7 21
HET MAN G 8 21
HET MAN G 9 21
HET MAN G 10 21
HET NAG A 601 28
HET PEG A 602 17
HET PEG A 603 17
HET EDO A 604 10
HET PEG A 605 17
HET EDO A 606 10
HET PGE A 607 24
HET NAG A 608 28
HET CA A 609 1
HET PEG A 610 17
HET NAG B 601 28
HET PEG B 602 17
HET EDO B 603 10
HET EDO B 604 10
HET EDO B 605 10
HET EDO B 606 10
HET EDO B 607 10
HET NAG B 608 28
HET NAG B 609 28
HET CA B 610 1
HET PEG B 611 17
HET PEG B 612 17
HET PEG B 613 17
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 15(C8 H15 N O6)
FORMUL 3 BMA 5(C6 H12 O6)
FORMUL 4 MAN 23(C6 H12 O6)
FORMUL 9 PEG 8(C4 H10 O3)
FORMUL 11 EDO 7(C2 H6 O2)
FORMUL 14 PGE C6 H14 O4
FORMUL 16 CA 2(CA 2+)
FORMUL 31 HOH *606(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 ASP A 283 CYS A 287 5 5
HELIX 11 AB2 ARG A 290 VAL A 295 5 6
HELIX 12 AB3 THR A 306 PHE A 317 1 12
HELIX 13 AB4 ASN A 323 GLY A 325 5 3
HELIX 14 AB5 GLY A 339 ALA A 343 5 5
HELIX 15 AB6 PHE A 349 VAL A 359 1 11
HELIX 16 AB7 ASP A 367 ILE A 371 5 5
HELIX 17 AB8 GLY A 372 ASN A 383 1 12
HELIX 18 AB9 PRO A 384 VAL A 387 5 4
HELIX 19 AC1 LEU A 394 ARG A 400 1 7
HELIX 20 AC2 SER A 416 GLY A 432 1 17
HELIX 21 AC3 SER A 434 ASP A 439 1 6
HELIX 22 AC4 GLU A 473 ASN A 476 5 4
HELIX 23 AC5 ASN A 477 GLY A 489 1 13
HELIX 24 AC6 ASN A 502 ALA A 504 5 3
HELIX 25 AC7 ASN A 532 ASP A 534 5 3
HELIX 26 AC8 PHE B 37 LEU B 48 1 12
HELIX 27 AC9 GLN B 129 PHE B 139 1 11
HELIX 28 AD1 ALA B 155 TYR B 159 5 5
HELIX 29 AD2 ASN B 161 TYR B 170 1 10
HELIX 30 AD3 TYR B 170 GLY B 189 1 20
HELIX 31 AD4 SER B 201 PHE B 214 1 14
HELIX 32 AD5 PRO B 215 PHE B 218 5 4
HELIX 33 AD6 ARG B 229 GLY B 245 1 17
HELIX 34 AD7 SER B 254 ASP B 270 1 17
HELIX 35 AD8 ASP B 270 GLY B 275 1 6
HELIX 36 AD9 ASP B 283 CYS B 287 5 5
HELIX 37 AE1 ARG B 290 VAL B 295 5 6
HELIX 38 AE2 THR B 306 PHE B 317 1 12
HELIX 39 AE3 ASN B 323 GLY B 325 5 3
HELIX 40 AE4 PHE B 349 VAL B 359 1 11
HELIX 41 AE5 ASP B 367 ILE B 371 5 5
HELIX 42 AE6 GLY B 372 ASN B 383 1 12
HELIX 43 AE7 PRO B 384 VAL B 387 5 4
HELIX 44 AE8 LEU B 394 ARG B 400 1 7
HELIX 45 AE9 SER B 416 GLY B 432 1 17
HELIX 46 AF1 SER B 434 ASP B 439 1 6
HELIX 47 AF2 ASN B 477 GLY B 489 1 13
HELIX 48 AF3 ASN B 502 ALA B 504 5 3
HELIX 49 AF4 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 108 N CYS A 88
SHEET 4 AA1 9 ALA A 142 ALA A 146 -1 O THR A 143 N TRP A 107
SHEET 5 AA1 9 PHE A 116 THR A 119 1 N LEU A 117 O ALA A 142
SHEET 6 AA1 9 SER A 195 CYS A 200 1 O TYR A 196 N PHE A 116
SHEET 7 AA1 9 GLY A 220 GLY A 224 1 O VAL A 222 N TYR A 197
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 GLU A 510 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 GLU A 539 N ARG A 521
SHEET 1 AA6 9 THR B 53 VAL B 61 0
SHEET 2 AA6 9 ILE B 87 GLY B 97 -1 O PHE B 93 N LYS B 54
SHEET 3 AA6 9 SER B 100 PRO B 109 -1 O ALA B 106 N VAL B 90
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 SER B 118
SHEET 7 AA6 9 GLY B 220 GLY B 224 1 O VAL B 222 N TYR B 197
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 ARG B 443 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 2.18
SSBOND 2 CYS A 76 CYS A 127 1555 1555 2.08
SSBOND 3 CYS A 200 CYS A 453 1555 1555 2.09
SSBOND 4 CYS A 269 CYS A 287 1555 1555 2.10
SSBOND 5 CYS A 296 CYS A 304 1555 1555 2.10
SSBOND 6 CYS A 516 CYS A 538 1555 1555 2.14
SSBOND 7 CYS B 41 CYS B 88 1555 1555 2.15
SSBOND 8 CYS B 76 CYS B 127 1555 1555 2.07
SSBOND 9 CYS B 200 CYS B 453 1555 1555 2.11
SSBOND 10 CYS B 269 CYS B 287 1555 1555 2.12
SSBOND 11 CYS B 296 CYS B 304 1555 1555 2.08
SSBOND 12 CYS B 516 CYS B 538 1555 1555 2.11
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.39
LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.40
LINK O6 MAN D 4 C1 MAN D 5 1555 1555 1.41
LINK O2 MAN D 5 C1 MAN D 6 1555 1555 1.39
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.39
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.39
LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.41
LINK O3 BMA E 3 C1 MAN E 8 1555 1555 1.39
LINK O6 MAN E 4 C1 MAN E 5 1555 1555 1.39
LINK O3 MAN E 4 C1 MAN E 7 1555 1555 1.39
LINK O2 MAN E 5 C1 MAN E 6 1555 1555 1.40
LINK O2 MAN E 8 C1 MAN E 9 1555 1555 1.40
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.38
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.38
LINK O6 BMA F 3 C1 MAN F 7 1555 1555 1.40
LINK O2 MAN F 4 C1 MAN F 5 1555 1555 1.40
LINK O2 MAN F 5 C1 MAN F 6 1555 1555 1.40
LINK O6 MAN F 7 C1 MAN F 8 1555 1555 1.40
LINK O3 MAN F 7 C1 MAN F 10 1555 1555 1.40
LINK O2 MAN F 8 C1 MAN F 9 1555 1555 1.40
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.39
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.40
LINK O6 BMA G 3 C1 MAN G 7 1555 1555 1.40
LINK O2 MAN G 4 C1 MAN G 5 1555 1555 1.40
LINK O2 MAN G 5 C1 MAN G 6 1555 1555 1.39
LINK O6 MAN G 7 C1 MAN G 8 1555 1555 1.40
LINK O3 MAN G 7 C1 MAN G 10 1555 1555 1.39
LINK O2 MAN G 8 C1 MAN G 9 1555 1555 1.39
LINK OD1 ASP A 270 CA CA A 609 1555 1555 2.36
LINK OD1 ASP A 274 CA CA A 609 1555 1555 2.45
LINK OD2 ASP A 274 CA CA A 609 1555 1555 2.52
LINK O VAL A 276 CA CA A 609 1555 1555 2.45
LINK OD1 ASP A 278 CA CA A 609 1555 1555 2.44
LINK O ILE A 280 CA CA A 609 1555 1555 2.27
LINK CA CA A 609 O HOH A 845 1555 1555 2.33
LINK OD1 ASP B 270 CA CA B 610 1555 1555 2.16
LINK OD1 ASP B 274 CA CA B 610 1555 1555 2.55
LINK OD2 ASP B 274 CA CA B 610 1555 1555 2.55
LINK O VAL B 276 CA CA B 610 1555 1555 2.44
LINK OD1 ASP B 278 CA CA B 610 1555 1555 2.45
LINK O ILE B 280 CA CA B 610 1555 1555 2.40
LINK CA CA B 610 O HOH B 765 1555 1555 2.42
CISPEP 1 THR A 77 PRO A 78 0 -11.36
CISPEP 2 TYR A 518 PRO A 519 0 -0.89
CISPEP 3 THR B 77 PRO B 78 0 -4.40
CISPEP 4 ALA B 125 GLY B 126 0 -13.67
CISPEP 5 TYR B 518 PRO B 519 0 0.88
CRYST1 68.561 89.261 116.484 90.00 101.73 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 0.014586 0.000000 0.003027 0.00000
SCALE2 0.000000 0.011203 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008768 0.00000
TER 7807 GLU A 543
TER 15600 GLU B 543
MASTER 565 0 61 49 34 0 0 6 9134 2 1275 88
END |