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HEADER HYDROLASE 31-OCT-22 8BHH
TITLE THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM OXYSPORUM
TITLE 2 IN COMPLEX WITH P-COUMARIC 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 FERULIC ACID ESTERASE, COUMMARIC ACID, TANNASE-LIKE, FERULOYL
KEYWDS 2 ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DIMAROGONA,E.TOPAKAS,C.KOSINAS,C.FEROUSI,E.NIKOLAIVITS
REVDAT 1 05-JUL-23 8BHH 0
JRNL AUTH C.KOSINAS,A.ZERVA,E.TOPAKAS,M.DIMAROGONA
JRNL TITL STRUCTURE-FUNCTION STUDIES OF A NOVEL LACCASE-LIKE
JRNL TITL 2 MULTICOPPER OXIDASE FROM THERMOTHELOMYCES THERMOPHILA
JRNL TITL 3 PROVIDE INSIGHTS INTO ITS BIOLOGICAL ROLE.
JRNL REF ACTA CRYSTALLOGR D STRUCT 2023
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 37326583
JRNL DOI 10.1107/S2059798323004175
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 69.5
REMARK 3 NUMBER OF REFLECTIONS : 99895
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5158
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) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 637
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 581
REMARK 3 SOLVENT ATOMS : 891
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : -0.31000
REMARK 3 B33 (A**2) : 0.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.26000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8807 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 7819 ; 0.002 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11907 ; 1.831 ; 1.728
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18132 ; 1.417 ; 1.649
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1029 ; 7.094 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 426 ;33.374 ;22.606
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1270 ;14.849 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;19.907 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1178 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9683 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2004 ; 0.002 ; 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): 4090 ; 2.558 ; 2.806
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4088 ; 2.558 ; 2.806
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5120 ; 3.257 ; 4.196
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5121 ; 3.257 ; 4.197
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4717 ; 3.416 ; 3.135
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4717 ; 3.416 ; 3.135
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6786 ; 4.808 ; 4.572
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10439 ; 6.049 ;34.609
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10439 ; 6.050 ;34.609
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 8BHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1292126207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-20
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) : 0.97624
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 : AUTOPROCESS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105053
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 113.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.5
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
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: 6FAT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, 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 44.81850
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, 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, G, I
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 ASP A 36
REMARK 465 PHE A 37
REMARK 465 ALA A 38
REMARK 465 ALA A 39
REMARK 465 LYS A 40
REMARK 465 SER B 297
REMARK 465 LYS B 298
REMARK 465 GLY B 299
REMARK 465 GLN B 300
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 OG1 THR B 370 O HOH B 701 2.03
REMARK 500 O4 NAG G 2 O5 BMA G 3 2.04
REMARK 500 O2 MAN C 8 C2 MAN C 9 2.09
REMARK 500 O4 NAG E 1 O5 NAG E 2 2.13
REMARK 500 O4 NAG C 1 O5 NAG C 2 2.16
REMARK 500 O HOH B 1101 O HOH B 1197 2.18
REMARK 500 NE2 GLN B 490 O HOH B 702 2.19
REMARK 500 O SER A 297 O HOH A 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O6 MAN I 10 O HOH B 1078 2544 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 422 CD GLU B 422 OE1 -0.077
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 - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 314 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 526 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = -4.8 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 GLU A 59 113.40 -167.53
REMARK 500 TYR A 170 -33.42 -149.27
REMARK 500 SER A 201 -111.90 72.25
REMARK 500 ALA A 225 49.35 37.90
REMARK 500 ALA A 227 34.17 -78.49
REMARK 500 ASP A 270 -96.17 -86.28
REMARK 500 LYS A 298 109.67 -49.78
REMARK 500 TYR A 329 147.91 -170.59
REMARK 500 ASN A 383 66.19 38.34
REMARK 500 CYS A 453 -21.03 74.28
REMARK 500 TYR B 170 -31.68 -150.16
REMARK 500 SER B 201 -114.08 72.84
REMARK 500 SER B 201 -124.40 69.08
REMARK 500 ALA B 227 36.90 -78.00
REMARK 500 ASP B 270 -93.04 -86.28
REMARK 500 PHE B 441 -14.14 -144.66
REMARK 500 CYS B 453 -19.49 73.20
REMARK 500 LYS B 527 -53.99 -125.92
REMARK 500
REMARK 500 REMARK: NULL
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 607 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 97.5 54.6
REMARK 620 4 VAL A 276 O 82.5 72.9 126.0
REMARK 620 5 ASP A 278 OD1 94.1 140.4 157.0 75.1
REMARK 620 6 ILE A 280 O 79.7 131.7 77.1 152.7 85.6
REMARK 620 7 HOH A 824 O 163.3 91.1 85.9 108.6 77.5 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 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 270 OD1
REMARK 620 2 ASP B 274 OD1 103.7
REMARK 620 3 ASP B 274 OD2 98.4 55.8
REMARK 620 4 VAL B 276 O 78.0 78.5 132.2
REMARK 620 5 ASP B 278 OD1 94.2 141.6 154.3 72.4
REMARK 620 6 ILE B 280 O 78.4 132.5 76.8 144.9 83.9
REMARK 620 7 HOH B 826 O 162.6 92.9 86.3 111.2 75.5 86.5
REMARK 620 N 1 2 3 4 5 6
DBREF1 8BHH A 36 543 UNP A0A1D3S5H0_FUSOX
DBREF2 8BHH A A0A1D3S5H0 36 543
DBREF1 8BHH B 36 543 UNP A0A1D3S5H0_FUSOX
DBREF2 8BHH B A0A1D3S5H0 36 543
SEQRES 1 A 508 ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU
SEQRES 2 A 508 LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL
SEQRES 3 A 508 PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO
SEQRES 4 A 508 THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE
SEQRES 5 A 508 CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER
SEQRES 6 A 508 ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR
SEQRES 7 A 508 GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY
SEQRES 8 A 508 CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE
SEQRES 9 A 508 GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY
SEQRES 10 A 508 THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL
SEQRES 11 A 508 GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL
SEQRES 12 A 508 LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS
SEQRES 13 A 508 HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY
SEQRES 14 A 508 ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP
SEQRES 15 A 508 PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE
SEQRES 16 A 508 ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE
SEQRES 17 A 508 THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU
SEQRES 18 A 508 GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS
SEQRES 19 A 508 ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU
SEQRES 20 A 508 ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL
SEQRES 21 A 508 CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO
SEQRES 22 A 508 GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR
SEQRES 23 A 508 GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO
SEQRES 24 A 508 GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN
SEQRES 25 A 508 PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE
SEQRES 26 A 508 TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO
SEQRES 27 A 508 ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN
SEQRES 28 A 508 VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS
SEQRES 29 A 508 ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP
SEQRES 30 A 508 GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN
SEQRES 31 A 508 HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU
SEQRES 32 A 508 ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY
SEQRES 33 A 508 HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN
SEQRES 34 A 508 ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN
SEQRES 35 A 508 VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN
SEQRES 36 A 508 ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY
SEQRES 37 A 508 ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS
SEQRES 38 A 508 ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN
SEQRES 39 A 508 TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU
SEQRES 40 A 508 GLU
SEQRES 1 B 508 ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU
SEQRES 2 B 508 LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL
SEQRES 3 B 508 PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO
SEQRES 4 B 508 THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE
SEQRES 5 B 508 CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER
SEQRES 6 B 508 ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR
SEQRES 7 B 508 GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY
SEQRES 8 B 508 CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE
SEQRES 9 B 508 GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY
SEQRES 10 B 508 THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL
SEQRES 11 B 508 GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL
SEQRES 12 B 508 LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS
SEQRES 13 B 508 HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY
SEQRES 14 B 508 ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP
SEQRES 15 B 508 PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE
SEQRES 16 B 508 ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE
SEQRES 17 B 508 THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU
SEQRES 18 B 508 GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS
SEQRES 19 B 508 ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU
SEQRES 20 B 508 ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL
SEQRES 21 B 508 CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO
SEQRES 22 B 508 GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR
SEQRES 23 B 508 GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO
SEQRES 24 B 508 GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN
SEQRES 25 B 508 PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE
SEQRES 26 B 508 TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO
SEQRES 27 B 508 ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN
SEQRES 28 B 508 VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS
SEQRES 29 B 508 ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP
SEQRES 30 B 508 GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN
SEQRES 31 B 508 HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU
SEQRES 32 B 508 ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY
SEQRES 33 B 508 HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN
SEQRES 34 B 508 ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN
SEQRES 35 B 508 VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN
SEQRES 36 B 508 ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY
SEQRES 37 B 508 ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS
SEQRES 38 B 508 ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN
SEQRES 39 B 508 TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU
SEQRES 40 B 508 GLU
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET MAN C 7 11
HET MAN C 8 11
HET MAN C 9 11
HET MAN C 10 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET MAN G 6 11
HET MAN G 7 11
HET MAN G 8 11
HET MAN G 9 11
HET MAN G 10 11
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET MAN I 5 11
HET MAN I 6 11
HET MAN I 7 11
HET MAN I 8 11
HET MAN I 9 11
HET MAN I 10 11
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET MAN E 6 11
HET HC4 A 601 12
HET NAG A 602 14
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET CA A 607 1
HET PG4 B 601 13
HET P6G B 602 19
HET NAG B 603 14
HET HC4 B 604 12
HET EDO B 605 4
HET EDO B 606 4
HET EDO B 607 4
HET EDO B 608 4
HET PEG B 609 7
HET EDO B 610 4
HET NAG B 611 14
HET NAG B 612 14
HET EDO B 613 4
HET CA B 614 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM HC4 4'-HYDROXYCINNAMIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
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 HC4 PARA-COUMARIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 NAG 12(C8 H15 N O6)
FORMUL 3 BMA 4(C6 H12 O6)
FORMUL 3 MAN 24(C6 H12 O6)
FORMUL 7 HC4 2(C9 H8 O3)
FORMUL 9 EDO 10(C2 H6 O2)
FORMUL 13 CA 2(CA 2+)
FORMUL 14 PG4 C8 H18 O5
FORMUL 15 P6G C12 H26 O7
FORMUL 22 PEG C4 H10 O3
FORMUL 28 HOH *891(H2 O)
HELIX 1 AA1 GLY A 43 LEU A 48 1 6
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 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 ARG B 229 GLY B 245 1 17
HELIX 32 AD5 SER B 254 ASP B 270 1 17
HELIX 33 AD6 ASP B 270 GLY B 275 1 6
HELIX 34 AD7 ASP B 283 CYS B 287 5 5
HELIX 35 AD8 ARG B 290 VAL B 295 5 6
HELIX 36 AD9 THR B 306 PHE B 317 1 12
HELIX 37 AE1 ASN B 323 GLY B 325 5 3
HELIX 38 AE2 PHE B 349 VAL B 359 1 11
HELIX 39 AE3 ASP B 367 ILE B 371 5 5
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 ASN B 465 LEU B 469 5 5
HELIX 46 AF1 GLU B 473 ASN B 476 5 4
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 3 THR A 53 PHE A 57 0
SHEET 2 AA1 3 ILE A 87 GLY A 97 -1 O PHE A 93 N LYS A 54
SHEET 3 AA1 3 HIS A 60 VAL A 61 -1 N VAL A 61 O ILE A 87
SHEET 1 AA2 9 THR A 53 PHE A 57 0
SHEET 2 AA2 9 ILE A 87 GLY A 97 -1 O PHE A 93 N LYS A 54
SHEET 3 AA2 9 SER A 100 PRO A 109 -1 O ALA A 106 N VAL A 90
SHEET 4 AA2 9 ALA A 142 ALA A 146 -1 O THR A 143 N TRP A 107
SHEET 5 AA2 9 PHE A 116 SER A 118 1 N LEU A 117 O VAL A 144
SHEET 6 AA2 9 SER A 195 CYS A 200 1 O TYR A 196 N SER A 118
SHEET 7 AA2 9 GLY A 220 GLY A 224 1 O GLY A 224 N GLY A 199
SHEET 8 AA2 9 LYS A 403 GLY A 409 1 O ILE A 405 N ILE A 221
SHEET 9 AA2 9 TYR A 442 VAL A 447 1 O ARG A 443 N HIS A 406
SHEET 1 AA3 2 ASN A 66 THR A 68 0
SHEET 2 AA3 2 SER A 80 ILE A 82 -1 O THR A 81 N ILE A 67
SHEET 1 AA4 2 LEU A 320 TYR A 321 0
SHEET 2 AA4 2 TYR A 327 TYR A 329 -1 O TYR A 329 N LEU A 320
SHEET 1 AA5 2 THR A 494 TYR A 500 0
SHEET 2 AA5 2 VAL A 509 CYS A 516 -1 O GLU A 510 N ARG A 499
SHEET 1 AA6 2 ARG A 521 TRP A 524 0
SHEET 2 AA6 2 TRP A 536 GLU A 539 -1 O GLU A 539 N ARG A 521
SHEET 1 AA7 9 THR B 53 VAL B 61 0
SHEET 2 AA7 9 ILE B 87 GLY B 97 -1 O ARG B 89 N GLU B 59
SHEET 3 AA7 9 SER B 100 PRO B 109 -1 O ALA B 106 N VAL B 90
SHEET 4 AA7 9 ALA B 142 ALA B 146 -1 O THR B 143 N TRP B 107
SHEET 5 AA7 9 PHE B 116 SER B 118 1 N LEU B 117 O VAL B 144
SHEET 6 AA7 9 SER B 195 CYS B 200 1 O TYR B 196 N PHE B 116
SHEET 7 AA7 9 GLY B 220 GLY B 224 1 O VAL B 222 N TYR B 197
SHEET 8 AA7 9 LYS B 403 GLY B 409 1 O ILE B 405 N ILE B 221
SHEET 9 AA7 9 TYR B 442 VAL B 447 1 O PHE B 445 N HIS B 406
SHEET 1 AA8 2 ASN B 66 THR B 68 0
SHEET 2 AA8 2 SER B 80 ILE B 82 -1 O THR B 81 N ILE B 67
SHEET 1 AA9 2 LEU B 320 TYR B 321 0
SHEET 2 AA9 2 TYR B 327 TYR B 329 -1 O TYR B 329 N LEU B 320
SHEET 1 AB1 2 THR B 494 TYR B 500 0
SHEET 2 AB1 2 VAL B 509 CYS B 516 -1 O GLU B 510 N ARG B 499
SHEET 1 AB2 2 ARG B 521 TRP B 524 0
SHEET 2 AB2 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 2.11
SSBOND 2 CYS A 76 CYS A 127 1555 1555 2.11
SSBOND 3 CYS A 200 CYS A 453 1555 1555 2.07
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 2.09
SSBOND 7 CYS B 41 CYS B 88 1555 1555 2.19
SSBOND 8 CYS B 76 CYS B 127 1555 1555 2.15
SSBOND 9 CYS B 200 CYS B 453 1555 1555 2.17
SSBOND 10 CYS B 269 CYS B 287 1555 1555 2.11
SSBOND 11 CYS B 296 CYS B 304 1555 1555 2.11
SSBOND 12 CYS B 516 CYS B 538 1555 1555 2.04
LINK ND2 ASN A 101 C1 NAG A 602 1555 1555 1.43
LINK ND2 ASN A 151 C1 NAG E 1 1555 1555 1.43
LINK ND2 ASN A 362 C1 NAG C 1 1555 1555 1.41
LINK ND2 ASN B 66 C1 NAG B 611 1555 1555 1.45
LINK ND2 ASN B 101 C1 NAG B 603 1555 1555 1.43
LINK ND2 ASN B 111 C1 NAG B 612 1555 1555 1.45
LINK ND2 ASN B 151 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN B 362 C1 NAG I 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.46
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.37
LINK O6 BMA C 3 C1 MAN C 7 1555 1555 1.53
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.46
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.45
LINK O6 MAN C 7 C1 MAN C 8 1555 1555 1.43
LINK O3 MAN C 7 C1 MAN C 10 1555 1555 1.45
LINK O2 MAN C 8 C1 MAN C 9 1555 1555 1.46
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.51
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.36
LINK O6 BMA G 3 C1 MAN G 7 1555 1555 1.40
LINK O2 MAN G 4 C1 MAN G 5 1555 1555 1.38
LINK O2 MAN G 5 C1 MAN G 6 1555 1555 1.46
LINK O6 MAN G 7 C1 MAN G 8 1555 1555 1.44
LINK O3 MAN G 7 C1 MAN G 10 1555 1555 1.41
LINK O2 MAN G 8 C1 MAN G 9 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.41
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.49
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.43
LINK O6 BMA I 3 C1 MAN I 7 1555 1555 1.45
LINK O2 MAN I 4 C1 MAN I 5 1555 1555 1.45
LINK O2 MAN I 5 C1 MAN I 6 1555 1555 1.41
LINK O6 MAN I 7 C1 MAN I 8 1555 1555 1.38
LINK O3 MAN I 7 C1 MAN I 10 1555 1555 1.43
LINK O2 MAN I 8 C1 MAN I 9 1555 1555 1.42
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.51
LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.34
LINK O6 MAN E 4 C1 MAN E 5 1555 1555 1.35
LINK O2 MAN E 5 C1 MAN E 6 1555 1555 1.47
LINK OD1 ASP A 270 CA CA A 607 1555 1555 2.29
LINK OD1 ASP A 274 CA CA A 607 1555 1555 2.39
LINK OD2 ASP A 274 CA CA A 607 1555 1555 2.48
LINK O VAL A 276 CA CA A 607 1555 1555 2.38
LINK OD1 ASP A 278 CA CA A 607 1555 1555 2.33
LINK O ILE A 280 CA CA A 607 1555 1555 2.31
LINK CA CA A 607 O HOH A 824 1555 1555 2.39
LINK OD1 ASP B 270 CA CA B 614 1555 1555 2.25
LINK OD1 ASP B 274 CA CA B 614 1555 1555 2.36
LINK OD2 ASP B 274 CA CA B 614 1555 1555 2.46
LINK O VAL B 276 CA CA B 614 1555 1555 2.41
LINK OD1 ASP B 278 CA CA B 614 1555 1555 2.34
LINK O ILE B 280 CA CA B 614 1555 1555 2.33
LINK CA CA B 614 O HOH B 826 1555 1555 2.41
CISPEP 1 THR A 77 PRO A 78 0 -5.31
CISPEP 2 ALA A 125 GLY A 126 0 -9.06
CISPEP 3 TYR A 518 PRO A 519 0 1.26
CISPEP 4 THR B 77 PRO B 78 0 -3.35
CISPEP 5 ALA B 125 GLY B 126 0 -6.94
CISPEP 6 TYR B 518 PRO B 519 0 3.19
CRYST1 67.704 89.637 116.978 90.00 103.99 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 0.014770 0.000000 0.003679 0.00000
SCALE2 0.000000 0.011156 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008810 0.00000
TER 3969 GLU A 543
TER 7940 GLU B 543
MASTER 390 0 57 49 37 0 0 6 9316 2 629 80
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