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HEADER HYDROLASE 24-FEB-15 5AJH
TITLE CRYSTAL STRUCTURE OF FUSARIUM OXYSPORUM CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 17-230;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM F. SP. RAPHANI;
SOURCE 3 ORGANISM_TAXID: 1089458;
SOURCE 4 STRAIN: PHW815;
SOURCE 5 ATCC: NRRL 54005;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HYDROLASE, ALPHA/BETA HYDROLASE FOLD, ESTERASE, PET MODIFICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DIMAROGONA,E.NIKOLAIVITS,M.KANELLI,P.CHRISTAKOPOULOS,M.SANDGREN,
AUTHOR 2 E.TOPAKAS
REVDAT 1 02-SEP-15 5AJH 0
JRNL AUTH M.DIMAROGONA,E.NIKOLAIVITS,M.KANELLI,P.CHRISTAKOPOULOS,
JRNL AUTH 2 M.SANDGREN,E.TOPAKAS
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF A FUSARIUM OXYSPORUM
JRNL TITL 2 CUTINASE WITH POLYETHYLENE TEREPHTHALATE MODIFICATION
JRNL TITL 3 POTENTIAL.
JRNL REF BIOCHIM.BIOPHYS.ACTA 2015
JRNL REFN ESSN 0006-3002
JRNL PMID 26291558
JRNL DOI 10.1016/J.BBAGEN.2015.08.009
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 120.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.70
REMARK 3 NUMBER OF REFLECTIONS : 40392
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) : 0.18355
REMARK 3 R VALUE (WORKING SET) : 0.18143
REMARK 3 FREE R VALUE : 0.22373
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2067
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) : 1.900
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.949
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2913
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.284
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.312
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 468
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.117
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09
REMARK 3 B22 (A**2) : -0.73
REMARK 3 B33 (A**2) : 0.81
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4368 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4168 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5937 ; 1.212 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9558 ; 0.774 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 603 ; 4.982 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;40.111 ;24.295
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 641 ;13.595 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;17.787 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 674 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5133 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 957 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2403 ; 0.875 ; 1.817
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2402 ; 0.874 ; 1.817
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3006 ; 1.445 ; 2.720
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1965 ; 1.029 ; 1.915
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 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
REMARK 3 RIDING POSITIONS.
REMARK 3 SIDE CHAINS OF RESIDUES 79, 97, 108, 157, 165 IN CHAIN A,
REMARK 3 79 AND 97 IN CHAIN B, AND 31, 66, 67, 82, 159, 165, 206
REMARK 3 IN CHAIN C, HAVE BEEN TRIMMED DUE TO INSUFFICIENT
REMARK 3 ELECTRON DENSITY
REMARK 4
REMARK 4 5AJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-63056.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MARMOSAIC 225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 120.90
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.6
REMARK 200 R MERGE (I) : 0.23
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.5
REMARK 200 R MERGE FOR SHELL (I) : 1.27
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.50
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: PDB ENTRY 1CEX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12M MONOSACCHARIDES, PH 8.5
REMARK 280 12.5% MPD, 12.5% PEG1000, 12.5% PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 17.95300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 120.98250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.07050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 120.98250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.95300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.07050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 MET A 0
REMARK 465 LEU A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 GLY A 4
REMARK 465 GLN A 5
REMARK 465 ASP A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 LEU A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 ARG A 13
REMARK 465 GLN A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 GLU A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 MET B 0
REMARK 465 LEU B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 3
REMARK 465 GLY B 4
REMARK 465 GLN B 5
REMARK 465 ASP B 6
REMARK 465 ALA B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 LEU B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 ARG B 13
REMARK 465 GLN B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 ALA B 217
REMARK 465 LEU B 218
REMARK 465 GLU B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
REMARK 465 MET C 0
REMARK 465 LEU C 1
REMARK 465 PRO C 2
REMARK 465 ALA C 3
REMARK 465 GLY C 4
REMARK 465 GLN C 5
REMARK 465 ASP C 6
REMARK 465 ALA C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 LEU C 10
REMARK 465 GLU C 11
REMARK 465 ALA C 12
REMARK 465 ARG C 13
REMARK 465 GLN C 14
REMARK 465 LEU C 15
REMARK 465 GLY C 16
REMARK 465 GLY C 17
REMARK 465 ALA C 214
REMARK 465 ALA C 215
REMARK 465 ALA C 216
REMARK 465 ALA C 217
REMARK 465 LEU C 218
REMARK 465 GLU C 219
REMARK 465 HIS C 220
REMARK 465 HIS C 221
REMARK 465 HIS C 222
REMARK 465 HIS C 223
REMARK 465 HIS C 224
REMARK 465 HIS C 225
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 79 CZ NH1 NH2
REMARK 470 ARG A 97 CZ NH1 NH2
REMARK 470 GLN A 108 CD OE1 NE2
REMARK 470 ARG A 157 NE CZ NH1 NH2
REMARK 470 GLU A 165 CD OE1 OE2
REMARK 470 LEU A 218 CG CD1 CD2
REMARK 470 ARG B 79 NH1 NH2
REMARK 470 ARG B 97 CZ NH1 NH2
REMARK 470 SER C 31 CB OG
REMARK 470 LYS C 66 CD CE NZ
REMARK 470 ASN C 67 OD1 ND2
REMARK 470 LEU C 82 CD1 CD2
REMARK 470 LYS C 159 CD CE NZ
REMARK 470 GLU C 165 CD OE1 OE2
REMARK 470 GLN C 206 CD OE1 NE2
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 THR A 44 -9.92 74.73
REMARK 500 SER A 121 -119.91 68.22
REMARK 500 LEU A 183 63.00 -104.94
REMARK 500 THR B 44 -9.98 77.37
REMARK 500 SER B 121 -119.72 62.61
REMARK 500 ALA B 191 56.92 -119.87
REMARK 500 SER C 29 1.03 -68.29
REMARK 500 SER C 121 -120.81 62.98
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 C2044 DISTANCE = 5.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B1219
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 145 IN ALL CHAINS OF THE DEPOSITED STRUCTURE IS AN
REMARK 999 ALANINE INSTEAD OF VALINE
DBREF 5AJH A 1 214 UNP X0BTD8 X0BTD8_FUSOX 17 230
DBREF 5AJH B 1 214 UNP X0BTD8 X0BTD8_FUSOX 17 230
DBREF 5AJH C 1 214 UNP X0BTD8 X0BTD8_FUSOX 17 230
SEQADV 5AJH MET A 0 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA A 215 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA A 216 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA A 217 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH LEU A 218 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH GLU A 219 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 220 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 221 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 222 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 223 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 224 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS A 225 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA A 145 UNP X0BTD8 VAL 161 CLONING ARTEFACT
SEQADV 5AJH MET B 0 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA B 215 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA B 216 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA B 217 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH LEU B 218 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH GLU B 219 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 220 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 221 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 222 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 223 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 224 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS B 225 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA B 145 UNP X0BTD8 VAL 161 CLONING ARTEFACT
SEQADV 5AJH MET C 0 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA C 215 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA C 216 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA C 217 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH LEU C 218 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH GLU C 219 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 220 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 221 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 222 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 223 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 224 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH HIS C 225 UNP X0BTD8 EXPRESSION TAG
SEQADV 5AJH ALA C 145 UNP X0BTD8 VAL 161 CLONING ARTEFACT
SEQRES 1 A 226 MET LEU PRO ALA GLY GLN ASP ALA ALA ALA LEU GLU ALA
SEQRES 2 A 226 ARG GLN LEU GLY GLY SER ILE THR ARG ASN ASP LEU ALA
SEQRES 3 A 226 ASN GLY ASN SER GLY SER CYS PRO GLY VAL ILE PHE ILE
SEQRES 4 A 226 TYR ALA ARG GLY SER THR GLU SER GLY ASN LEU GLY THR
SEQRES 5 A 226 LEU GLY PRO ARG VAL ALA SER LYS LEU GLU ALA LYS TYR
SEQRES 6 A 226 GLY LYS ASN GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA
SEQRES 7 A 226 TYR ARG ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY
SEQRES 8 A 226 THR SER SER ALA ALA ILE ARG GLU MET LEU GLY HIS PHE
SEQRES 9 A 226 SER ASP ALA ASN GLN LYS CYS PRO ASP ALA VAL LEU ILE
SEQRES 10 A 226 ALA GLY GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA
SEQRES 11 A 226 SER VAL THR ASP VAL ASP ALA GLY ILE ARG GLU LYS ILE
SEQRES 12 A 226 ALA GLY ALA VAL LEU PHE GLY TYR THR LYS ASN LEU GLN
SEQRES 13 A 226 ASN ARG GLY LYS ILE PRO SER TYR PRO GLU ASP ARG THR
SEQRES 14 A 226 LYS VAL PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY
SEQRES 15 A 226 SER LEU ILE VAL ALA ALA PRO HIS LEU ALA TYR GLN SER
SEQRES 16 A 226 ALA ALA SER GLY ALA ALA PRO GLU PHE LEU ILE GLN LYS
SEQRES 17 A 226 ALA ASP ALA ALA GLY ALA ALA ALA ALA ALA LEU GLU HIS
SEQRES 18 A 226 HIS HIS HIS HIS HIS
SEQRES 1 B 226 MET LEU PRO ALA GLY GLN ASP ALA ALA ALA LEU GLU ALA
SEQRES 2 B 226 ARG GLN LEU GLY GLY SER ILE THR ARG ASN ASP LEU ALA
SEQRES 3 B 226 ASN GLY ASN SER GLY SER CYS PRO GLY VAL ILE PHE ILE
SEQRES 4 B 226 TYR ALA ARG GLY SER THR GLU SER GLY ASN LEU GLY THR
SEQRES 5 B 226 LEU GLY PRO ARG VAL ALA SER LYS LEU GLU ALA LYS TYR
SEQRES 6 B 226 GLY LYS ASN GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA
SEQRES 7 B 226 TYR ARG ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY
SEQRES 8 B 226 THR SER SER ALA ALA ILE ARG GLU MET LEU GLY HIS PHE
SEQRES 9 B 226 SER ASP ALA ASN GLN LYS CYS PRO ASP ALA VAL LEU ILE
SEQRES 10 B 226 ALA GLY GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA
SEQRES 11 B 226 SER VAL THR ASP VAL ASP ALA GLY ILE ARG GLU LYS ILE
SEQRES 12 B 226 ALA GLY ALA VAL LEU PHE GLY TYR THR LYS ASN LEU GLN
SEQRES 13 B 226 ASN ARG GLY LYS ILE PRO SER TYR PRO GLU ASP ARG THR
SEQRES 14 B 226 LYS VAL PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY
SEQRES 15 B 226 SER LEU ILE VAL ALA ALA PRO HIS LEU ALA TYR GLN SER
SEQRES 16 B 226 ALA ALA SER GLY ALA ALA PRO GLU PHE LEU ILE GLN LYS
SEQRES 17 B 226 ALA ASP ALA ALA GLY ALA ALA ALA ALA ALA LEU GLU HIS
SEQRES 18 B 226 HIS HIS HIS HIS HIS
SEQRES 1 C 226 MET LEU PRO ALA GLY GLN ASP ALA ALA ALA LEU GLU ALA
SEQRES 2 C 226 ARG GLN LEU GLY GLY SER ILE THR ARG ASN ASP LEU ALA
SEQRES 3 C 226 ASN GLY ASN SER GLY SER CYS PRO GLY VAL ILE PHE ILE
SEQRES 4 C 226 TYR ALA ARG GLY SER THR GLU SER GLY ASN LEU GLY THR
SEQRES 5 C 226 LEU GLY PRO ARG VAL ALA SER LYS LEU GLU ALA LYS TYR
SEQRES 6 C 226 GLY LYS ASN GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA
SEQRES 7 C 226 TYR ARG ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY
SEQRES 8 C 226 THR SER SER ALA ALA ILE ARG GLU MET LEU GLY HIS PHE
SEQRES 9 C 226 SER ASP ALA ASN GLN LYS CYS PRO ASP ALA VAL LEU ILE
SEQRES 10 C 226 ALA GLY GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA
SEQRES 11 C 226 SER VAL THR ASP VAL ASP ALA GLY ILE ARG GLU LYS ILE
SEQRES 12 C 226 ALA GLY ALA VAL LEU PHE GLY TYR THR LYS ASN LEU GLN
SEQRES 13 C 226 ASN ARG GLY LYS ILE PRO SER TYR PRO GLU ASP ARG THR
SEQRES 14 C 226 LYS VAL PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY
SEQRES 15 C 226 SER LEU ILE VAL ALA ALA PRO HIS LEU ALA TYR GLN SER
SEQRES 16 C 226 ALA ALA SER GLY ALA ALA PRO GLU PHE LEU ILE GLN LYS
SEQRES 17 C 226 ALA ASP ALA ALA GLY ALA ALA ALA ALA ALA LEU GLU HIS
SEQRES 18 C 226 HIS HIS HIS HIS HIS
HET MPD A1219 8
HET MPD A1220 8
HET MPD A1221 8
HET MPD B1217 8
HET MPD B1218 8
HET MPD B1219 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 4 MPD 6(C6 H14 O2)
FORMUL 5 HOH *468(H2 O)
HELIX 1 1 ASN A 28 CYS A 32 5 5
HELIX 2 2 LEU A 52 GLY A 65 1 14
HELIX 3 3 THR A 81 LEU A 87 5 7
HELIX 4 4 SER A 92 CYS A 110 1 19
HELIX 5 5 SER A 121 VAL A 134 1 14
HELIX 6 6 ASP A 135 LYS A 141 1 7
HELIX 7 7 PRO A 164 ASP A 166 5 3
HELIX 8 8 ASP A 176 GLY A 181 5 6
HELIX 9 9 ALA A 186 ALA A 191 5 6
HELIX 10 10 TYR A 192 GLY A 198 1 7
HELIX 11 11 GLY A 198 LEU A 218 1 21
HELIX 12 12 LEU B 52 GLY B 65 1 14
HELIX 13 13 THR B 81 LEU B 87 5 7
HELIX 14 14 SER B 92 CYS B 110 1 19
HELIX 15 15 SER B 121 VAL B 134 1 14
HELIX 16 16 ASP B 135 GLU B 140 1 6
HELIX 17 17 PRO B 164 ASP B 166 5 3
HELIX 18 18 ASP B 176 GLY B 181 5 6
HELIX 19 19 PRO B 188 ALA B 191 5 4
HELIX 20 20 TYR B 192 GLY B 198 1 7
HELIX 21 21 GLY B 198 ALA B 211 1 14
HELIX 22 22 ASN C 22 GLY C 27 1 6
HELIX 23 23 LEU C 52 GLY C 68 1 17
HELIX 24 24 THR C 81 LEU C 87 5 7
HELIX 25 25 SER C 92 CYS C 110 1 19
HELIX 26 26 SER C 121 VAL C 134 1 14
HELIX 27 27 ASP C 135 LYS C 141 1 7
HELIX 28 28 PRO C 164 ASP C 166 5 3
HELIX 29 29 ASP C 176 GLY C 181 5 6
HELIX 30 30 ALA C 186 ALA C 191 5 6
HELIX 31 31 TYR C 192 GLY C 198 1 7
HELIX 32 32 GLY C 198 ALA C 211 1 14
SHEET 1 AA 5 VAL A 69 GLY A 73 0
SHEET 2 AA 5 VAL A 35 ALA A 40 1 O VAL A 35 N TRP A 70
SHEET 3 AA 5 VAL A 114 TYR A 120 1 O VAL A 114 N ILE A 36
SHEET 4 AA 5 ILE A 142 PHE A 148 1 N ALA A 143 O LEU A 115
SHEET 5 AA 5 THR A 168 PHE A 171 1 O LYS A 169 N LEU A 147
SHEET 1 AB 2 ILE A 184 VAL A 185 0
SHEET 2 AB 2 VAL B 185 ALA B 186 -1 O VAL B 185 N VAL A 185
SHEET 1 BA 5 VAL B 69 GLY B 73 0
SHEET 2 BA 5 VAL B 35 ALA B 40 1 O VAL B 35 N TRP B 70
SHEET 3 BA 5 VAL B 114 TYR B 120 1 O VAL B 114 N ILE B 36
SHEET 4 BA 5 ILE B 142 PHE B 148 1 N ALA B 143 O LEU B 115
SHEET 5 BA 5 THR B 168 PHE B 171 1 O LYS B 169 N LEU B 147
SHEET 1 CA 5 VAL C 69 GLY C 73 0
SHEET 2 CA 5 VAL C 35 ALA C 40 1 O VAL C 35 N TRP C 70
SHEET 3 CA 5 VAL C 114 TYR C 120 1 O VAL C 114 N ILE C 36
SHEET 4 CA 5 ILE C 142 PHE C 148 1 N ALA C 143 O LEU C 115
SHEET 5 CA 5 THR C 168 PHE C 171 1 O LYS C 169 N LEU C 147
SSBOND 1 CYS A 32 CYS A 110 1555 1555 2.04
SSBOND 2 CYS A 172 CYS A 179 1555 1555 2.04
SSBOND 3 CYS B 32 CYS B 110 1555 1555 2.04
SSBOND 4 CYS B 172 CYS B 179 1555 1555 2.06
SSBOND 5 CYS C 32 CYS C 110 1555 1555 2.03
SSBOND 6 CYS C 172 CYS C 179 1555 1555 2.05
SITE 1 AC1 7 ASN A 22 ASN A 26 ARG A 139 PRO A 164
SITE 2 AC1 7 ARG A 167 HOH A2010 HOH A2212
SITE 1 AC2 6 ASN A 85 SER A 121 LEU A 183 VAL A 185
SITE 2 AC2 6 HOH A2092 LEU B 190
SITE 1 AC3 6 GLY A 42 SER A 43 TYR A 120 SER A 121
SITE 2 AC3 6 HIS A 189 HOH A2048
SITE 1 AC4 6 ASN B 85 SER B 121 VAL B 178 VAL B 185
SITE 2 AC4 6 MPD B1218 HOH B2036
SITE 1 AC5 6 GLY B 42 SER B 43 TYR B 120 HIS B 189
SITE 2 AC5 6 MPD B1217 HOH B2036
SITE 1 AC6 4 LEU B 154 ARG B 157 GLY B 158 HOH B2155
CRYST1 35.906 60.141 241.965 90.00 90.00 90.00 P 21 21 21 12
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 0.027850 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004133 0.00000
TER 1421 LEU A 218
TER 2852 ALA B 216
TER 4249 ALA C 213
MASTER 430 0 6 32 17 0 11 6 4762 3 60 54
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