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HEADER HYDROLASE 23-DEC-24 9HUN
TITLE CRYSTAL STRUCTURE OF FERULOYL ESTERASE FROM FUSARIUM OXYSPORUM G122S
TITLE 2 VARIANT IN COMPLEX WITH BENZOIC ACID
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_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 9HUN 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. 1.71 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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 142930
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) : 0.161
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.996
REMARK 3 FREE R VALUE TEST SET COUNT : 7141
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) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10072
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 533
REMARK 3 BIN FREE R VALUE : 0.3140
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 : 673
REMARK 3 SOLVENT ATOMS : 814
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82600
REMARK 3 B22 (A**2) : -4.15500
REMARK 3 B33 (A**2) : 2.55500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.32400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.914
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8994 ; 0.013 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 8009 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12251 ; 1.990 ; 1.828
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18622 ; 0.688 ; 1.743
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1056 ; 6.924 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ; 7.878 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1290 ;14.265 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1407 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10268 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2036 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1819 ; 0.255 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 46 ; 0.245 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4457 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 634 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.153 ; 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): 4161 ; 2.591 ; 2.839
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4161 ; 2.591 ; 2.839
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5229 ; 3.252 ; 5.093
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5230 ; 3.252 ; 5.094
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4833 ; 3.962 ; 3.305
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4834 ; 3.961 ; 3.306
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7019 ; 5.573 ; 5.850
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7020 ; 5.572 ; 5.850
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 588
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1456 -10.3505 -13.6547
REMARK 3 T TENSOR
REMARK 3 T11: 0.1498 T22: 0.1048
REMARK 3 T33: 0.0878 T12: 0.0283
REMARK 3 T13: 0.0158 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 1.2435 L22: 0.8727
REMARK 3 L33: 0.8066 L12: 0.3215
REMARK 3 L13: -0.3582 L23: -0.1435
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.1799 S13: -0.1280
REMARK 3 S21: 0.2143 S22: 0.0321 S23: 0.1670
REMARK 3 S31: 0.0514 S32: -0.0445 S33: -0.0400
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): 7.1080 13.2928 -41.0737
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.0308
REMARK 3 T33: 0.0426 T12: 0.0109
REMARK 3 T13: -0.0306 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.9626 L22: 0.9503
REMARK 3 L33: 0.6987 L12: 0.3816
REMARK 3 L13: -0.3481 L23: -0.3912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: -0.0169 S13: 0.1271
REMARK 3 S21: 0.0448 S22: -0.0275 S23: -0.0420
REMARK 3 S31: -0.0981 S32: 0.0278 S33: -0.0037
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 9HUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-24.
REMARK 100 THE DEPOSITION ID IS D_1292144124.
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 : 143024
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 89.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.53700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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 (%): 57.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, TRIS-HCL PH 8.5, VAPOR
REMARK 280 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 44.96700
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
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, E, F
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 HD22 ASN B 101 C1 NAG B 605 1.52
REMARK 500 HD22 ASN A 362 C1 NAG D 1 1.53
REMARK 500 HD21 ASN B 151 C1 NAG E 1 1.57
REMARK 500 HD22 ASN B 66 C1 NAG B 604 1.59
REMARK 500 HD22 ASN A 151 C1 NAG C 1 1.60
REMARK 500 HD22 ASN B 362 C1 NAG F 1 1.60
REMARK 500 ND2 ASN B 151 C1 NAG E 1 1.60
REMARK 500 ND2 ASN B 362 C1 NAG F 1 1.65
REMARK 500 ND2 ASN A 151 C1 NAG C 1 1.67
REMARK 500 ND2 ASN A 101 C1 NAG A 601 1.76
REMARK 500 ND2 ASN B 66 C1 NAG B 604 1.78
REMARK 500 OD1 ASN B 111 C1 NAG B 606 1.81
REMARK 500 OD1 ASN A 66 C1 NAG A 606 1.88
REMARK 500 OD1 ASN A 111 C1 NAG A 607 2.09
REMARK 500 OD1 ASN A 324 O HOH A 701 2.14
REMARK 500 O6 MAN E 9 O HOH B 913 2.15
REMARK 500 NZ LYS B 194 O HOH B 701 2.18
REMARK 500 O4 NAG C 1 O5 NAG C 2 2.19
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 115 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 MET A 124 CG - SD - CE ANGL. DEV. = -18.2 DEGREES
REMARK 500 CYS A 200 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 314 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 MET B 124 CG - SD - CE ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG B 205 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 398 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 443 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 446 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 446 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 499 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 517 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 517 NE - CZ - NH2 ANGL. DEV. = -3.2 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 TYR A 170 -31.85 -149.20
REMARK 500 SER A 201 -114.87 80.81
REMARK 500 SER A 201 -131.16 85.52
REMARK 500 ALA A 227 39.23 -74.34
REMARK 500 ASP A 270 -103.47 -79.05
REMARK 500 LYS A 298 116.43 -8.30
REMARK 500 ASN A 383 68.14 38.99
REMARK 500 LEU A 394 30.75 -95.71
REMARK 500 PHE A 441 -12.41 -143.52
REMARK 500 CYS A 453 -24.94 73.94
REMARK 500 TYR B 170 -32.11 -149.34
REMARK 500 SER B 201 -113.08 78.64
REMARK 500 SER B 201 -125.94 80.78
REMARK 500 ALA B 227 42.88 -81.61
REMARK 500 ASP B 270 -99.86 -79.00
REMARK 500 ASN B 303 37.76 73.46
REMARK 500 PHE B 441 -11.35 -145.44
REMARK 500 CYS B 453 -20.47 67.78
REMARK 500 LYS B 527 -60.33 -128.33
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 ARG A 331 ILE A 332 149.50
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 290 0.08 SIDE CHAIN
REMARK 500 ARG A 499 0.09 SIDE CHAIN
REMARK 500 ARG B 526 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 A1042 DISTANCE = 5.82 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 E 1
REMARK 610 NAG F 1
REMARK 610 NAG A 601
REMARK 610 NAG A 606
REMARK 610 NAG A 607
REMARK 610 NAG B 604
REMARK 610 NAG B 606
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 107.8
REMARK 620 3 ASP A 274 OD2 97.4 53.6
REMARK 620 4 VAL A 276 O 78.9 76.7 126.8
REMARK 620 5 ASP A 278 OD1 89.2 144.3 157.0 76.1
REMARK 620 6 ILE A 280 O 80.3 129.7 76.3 150.7 83.2
REMARK 620 7 HOH A 788 O 163.2 87.9 87.1 111.2 80.8 85.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 270 OD1
REMARK 620 2 ASP B 274 OD1 104.4
REMARK 620 3 ASP B 274 OD2 100.7 51.4
REMARK 620 4 VAL B 276 O 76.4 75.3 124.6
REMARK 620 5 ASP B 278 OD1 92.7 139.7 159.3 73.7
REMARK 620 6 ILE B 280 O 78.8 131.0 79.7 148.0 87.6
REMARK 620 7 HOH B 819 O 163.9 91.5 87.3 110.7 76.1 88.9
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 9HUN A 1 563 UNP A0A1D3S5H0_FUSOX
DBREF2 9HUN A A0A1D3S5H0 1 563
DBREF1 9HUN B 1 563 UNP A0A1D3S5H0_FUSOX
DBREF2 9HUN B A0A1D3S5H0 1 563
SEQADV 9HUN SER A 122 UNP A0A1D3S5H GLY 122 ENGINEERED MUTATION
SEQADV 9HUN 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 MAN C 4 21
HET MAN C 5 21
HET MAN C 6 21
HET MAN C 7 21
HET MAN C 8 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 MAN D 7 21
HET MAN D 8 21
HET MAN D 9 21
HET MAN D 10 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 MAN E 10 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 A 601 28
HET PEG A 602 17
HET EDO A 603 10
HET EDO A 604 10
HET EDO A 605 10
HET NAG A 606 28
HET NAG A 607 28
HET EDO A 608 10
HET BEZ A 609 14
HET PEG A 610 17
HET EDO A 611 10
HET PEG A 612 17
HET CA A 613 1
HET PEG B 601 17
HET PEG B 602 17
HET EDO B 603 10
HET NAG B 604 28
HET NAG B 605 28
HET NAG B 606 28
HET PEG B 607 17
HET PEG B 608 17
HET EDO B 609 10
HET EDO B 610 10
HET EDO B 611 10
HET PEG B 612 17
HET PEG B 613 17
HET EDO B 614 10
HET EDO B 615 10
HET EDO B 616 10
HET BEZ B 617 14
HET EDO B 618 10
HET EDO B 619 10
HET EDO B 620 10
HET CA B 621 1
HET EDO B 622 10
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 BEZ BENZOIC ACID
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 14(C8 H15 N O6)
FORMUL 3 BMA 4(C6 H12 O6)
FORMUL 3 MAN 26(C6 H12 O6)
FORMUL 8 PEG 9(C4 H10 O3)
FORMUL 9 EDO 16(C2 H6 O2)
FORMUL 15 BEZ 2(C7 H6 O2)
FORMUL 19 CA 2(CA 2+)
FORMUL 42 HOH *814(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 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 ASN A 477 GLY A 489 1 13
HELIX 22 AC4 ASN A 502 ALA A 504 5 3
HELIX 23 AC5 ASN A 532 ASP A 534 5 3
HELIX 24 AC6 PHE B 37 LEU B 48 1 12
HELIX 25 AC7 GLN B 129 PHE B 139 1 11
HELIX 26 AC8 ALA B 155 TYR B 159 5 5
HELIX 27 AC9 ASN B 161 TYR B 170 1 10
HELIX 28 AD1 TYR B 170 GLY B 189 1 20
HELIX 29 AD2 SER B 201 PHE B 214 1 14
HELIX 30 AD3 ARG B 229 GLY B 245 1 17
HELIX 31 AD4 SER B 254 ASP B 270 1 17
HELIX 32 AD5 ASP B 270 GLY B 275 1 6
HELIX 33 AD6 ASP B 283 CYS B 287 5 5
HELIX 34 AD7 ARG B 290 VAL B 295 5 6
HELIX 35 AD8 THR B 306 PHE B 317 1 12
HELIX 36 AD9 ASN B 323 GLY B 325 5 3
HELIX 37 AE1 PHE B 349 VAL B 359 1 11
HELIX 38 AE2 ASP B 367 ILE B 371 5 5
HELIX 39 AE3 GLY B 372 ASN B 383 1 12
HELIX 40 AE4 PRO B 384 VAL B 387 5 4
HELIX 41 AE5 LEU B 394 GLY B 401 1 8
HELIX 42 AE6 SER B 416 GLY B 432 1 17
HELIX 43 AE7 SER B 434 ASP B 439 1 6
HELIX 44 AE8 GLU B 473 ASN B 476 5 4
HELIX 45 AE9 ASN B 477 GLY B 489 1 13
HELIX 46 AF1 ASN B 502 ALA B 504 5 3
HELIX 47 AF2 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 PHE A 93 N LYS A 54
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 SER A 118 1 N LEU A 117 O ALA A 142
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 ARG A 443 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 ILE A 328 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 SER B 118 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 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 VAL B 447 N HIS B 408
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 LYS B 537 N VAL B 523
SSBOND 1 CYS A 41 CYS A 88 1555 1555 2.23
SSBOND 2 CYS A 76 CYS A 127 1555 1555 2.25
SSBOND 3 CYS A 200 CYS A 453 1555 1555 2.13
SSBOND 4 CYS A 269 CYS A 287 1555 1555 2.14
SSBOND 5 CYS A 296 CYS A 304 1555 1555 2.16
SSBOND 6 CYS A 516 CYS A 538 1555 1555 2.16
SSBOND 7 CYS B 41 CYS B 88 1555 1555 2.31
SSBOND 8 CYS B 76 CYS B 127 1555 1555 2.08
SSBOND 9 CYS B 200 CYS B 453 1555 1555 2.21
SSBOND 10 CYS B 269 CYS B 287 1555 1555 2.10
SSBOND 11 CYS B 296 CYS B 304 1555 1555 2.06
SSBOND 12 CYS B 516 CYS B 538 1555 1555 2.13
LINK ND2 ASN A 362 C1 NAG D 1 1555 1555 1.57
LINK ND2 ASN B 101 C1 NAG B 605 1555 1555 1.52
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.38
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.39
LINK O6 BMA C 3 C1 MAN C 4 1555 1555 1.40
LINK O3 BMA C 3 C1 MAN C 8 1555 1555 1.40
LINK O6 MAN C 4 C1 MAN C 5 1555 1555 1.41
LINK O3 MAN C 4 C1 MAN C 7 1555 1555 1.40
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.40
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.40
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.39
LINK O6 BMA D 3 C1 MAN D 7 1555 1555 1.40
LINK O2 MAN D 4 C1 MAN D 5 1555 1555 1.39
LINK O2 MAN D 5 C1 MAN D 6 1555 1555 1.39
LINK O6 MAN D 7 C1 MAN D 8 1555 1555 1.42
LINK O3 MAN D 7 C1 MAN D 10 1555 1555 1.40
LINK O2 MAN D 8 C1 MAN D 9 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 1.41
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.38
LINK O6 BMA E 3 C1 MAN E 7 1555 1555 1.41
LINK O2 MAN E 4 C1 MAN E 5 1555 1555 1.41
LINK O2 MAN E 5 C1 MAN E 6 1555 1555 1.41
LINK O6 MAN E 7 C1 MAN E 8 1555 1555 1.41
LINK O3 MAN E 7 C1 MAN E 10 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 1.41
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.39
LINK O6 BMA F 3 C1 MAN F 7 1555 1555 1.40
LINK O2 MAN F 4 C1 MAN F 5 1555 1555 1.39
LINK O2 MAN F 5 C1 MAN F 6 1555 1555 1.38
LINK O6 MAN F 7 C1 MAN F 8 1555 1555 1.41
LINK O3 MAN F 7 C1 MAN F 10 1555 1555 1.39
LINK O2 MAN F 8 C1 MAN F 9 1555 1555 1.40
LINK OD1 ASP A 270 CA CA A 613 1555 1555 2.20
LINK OD1 ASP A 274 CA CA A 613 1555 1555 2.36
LINK OD2 ASP A 274 CA CA A 613 1555 1555 2.54
LINK O VAL A 276 CA CA A 613 1555 1555 2.45
LINK OD1 ASP A 278 CA CA A 613 1555 1555 2.49
LINK O ILE A 280 CA CA A 613 1555 1555 2.48
LINK CA CA A 613 O HOH A 788 1555 1555 2.39
LINK OD1 ASP B 270 CA CA B 621 1555 1555 2.17
LINK OD1 ASP B 274 CA CA B 621 1555 1555 2.59
LINK OD2 ASP B 274 CA CA B 621 1555 1555 2.43
LINK O VAL B 276 CA CA B 621 1555 1555 2.55
LINK OD1 ASP B 278 CA CA B 621 1555 1555 2.46
LINK O ILE B 280 CA CA B 621 1555 1555 2.38
LINK CA CA B 621 O HOH B 819 1555 1555 2.27
CISPEP 1 THR A 77 PRO A 78 0 -11.71
CISPEP 2 ALA A 125 GLY A 126 0 -15.34
CISPEP 3 TYR A 518 PRO A 519 0 3.67
CISPEP 4 THR B 77 PRO B 78 0 -0.33
CISPEP 5 ALA B 125 GLY B 126 0 -13.08
CISPEP 6 TYR B 518 PRO B 519 0 0.78
CRYST1 68.004 89.934 115.148 90.00 103.77 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 0.014705 0.000000 0.003603 0.00000
SCALE2 0.000000 0.011119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008941 0.00000
TER 7924 GLU A 543
TER 15746 GLU B 543
MASTER 571 0 73 47 34 0 0 6 9401 2 1403 88
END |