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HEADER HYDROLASE 11-MAY-23 8JCT
TITLE CRYSTAL STRUCTURE OF FUNGAL CUTINASE FROM ASPERGILLUS FUMIGATIAFFINIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.74;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATIAFFINIS;
SOURCE 3 ORGANISM_TAXID: 340414;
SOURCE 4 GENE: CNMCM6457_007885, CNMCM6805_005550;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE ; ASPERGILLUS FUMIGATIAFFINIS; FUNGAL CUTINASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KIM,S.H.LEE,K.-J.KIM
REVDAT 1 15-MAY-24 8JCT 0
JRNL AUTH S.H.LEE,M.KIM,K.J.KIM
JRNL TITL CHARACTERIZATION AND ENGINEERING OF NOVEL FUNGAL PET
JRNL TITL 2 DEGRADING ENZYME FROM ASPERGILLUS FUMIGATIAFFINIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0405
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 3985
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 199
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 294
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 13
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1375
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.62000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : 2.03000
REMARK 3 B12 (A**2) : -0.31000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.469
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.384
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.510
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1403 ; 0.004 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1345 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1909 ; 1.175 ; 1.643
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3102 ; 0.373 ; 1.563
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 188 ; 6.732 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 7 ; 8.808 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 218 ;18.034 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 222 ; 0.048 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1659 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 301 ; 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): 755 ; 3.094 ; 4.751
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 755 ; 3.092 ; 4.752
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 942 ; 4.911 ; 8.530
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 943 ; 4.911 ; 8.532
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 648 ; 3.590 ; 5.250
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 647 ; 3.586 ; 5.245
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 968 ; 6.078 ; 9.514
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1570 ; 8.428 ;44.600
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1569 ; 8.426 ;44.540
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 8JCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1300037640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-22
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4184
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
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: REFMAC
REMARK 200 STARTING MODEL: 4OHY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1 M HEPES PH7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 31.52650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 18.20183
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 71.77200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 31.52650
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 18.20183
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 71.77200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 31.52650
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 18.20183
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 71.77200
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 31.52650
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 18.20183
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 71.77200
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 31.52650
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 18.20183
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 71.77200
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 31.52650
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 18.20183
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 71.77200
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 36.40367
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 143.54400
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 36.40367
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 143.54400
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 36.40367
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 143.54400
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 36.40367
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 143.54400
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 36.40367
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 143.54400
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 36.40367
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 143.54400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 217 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 219 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ARG A 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 HIS A 194
REMARK 465 HIS A 195
REMARK 465 HIS A 196
REMARK 465 HIS A 197
REMARK 465 HIS A 198
REMARK 465 HIS A 199
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 36 -90.09 -94.58
REMARK 500 SER A 105 -127.16 52.33
REMARK 500 CYS A 163 1.62 -68.28
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 25 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 217 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 218 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 219 DISTANCE = 6.82 ANGSTROMS
DBREF1 8JCT A 2 191 UNP A0A8H4MGN0_9EURO
DBREF2 8JCT A A0A8H4MGN0 22 211
SEQADV 8JCT MET A 1 UNP A0A8H4MGN INITIATING METHIONINE
SEQADV 8JCT LEU A 192 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT GLU A 193 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 194 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 195 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 196 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 197 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 198 UNP A0A8H4MGN EXPRESSION TAG
SEQADV 8JCT HIS A 199 UNP A0A8H4MGN EXPRESSION TAG
SEQRES 1 A 199 MET ARG GLN THR ALA ILE THR GLY ASP GLU LEU ARG THR
SEQRES 2 A 199 GLY PRO CYS GLU PRO ILE THR PHE ILE PHE ALA ARG GLY
SEQRES 3 A 199 SER THR GLU PRO GLY LEU LEU GLY ILE THR THR GLY PRO
SEQRES 4 A 199 GLY VAL CYS ASN ALA LEU LYS LEU SER ARG PRO GLY GLN
SEQRES 5 A 199 VAL ALA CYS GLN GLY VAL GLY PRO ALA TYR THR ALA ASP
SEQRES 6 A 199 LEU ALA SER ASN PHE LEU PRO GLN GLY THR SER GLN ILE
SEQRES 7 A 199 ALA ILE ASP GLU ALA ALA GLY LEU PHE LYS LEU ALA ALA
SEQRES 8 A 199 SER LYS CYS PRO ASP THR LYS ILE VAL ALA GLY GLY TYR
SEQRES 9 A 199 SER GLN GLY ALA ALA VAL MET HIS GLY ALA ILE ARG ASN
SEQRES 10 A 199 LEU PRO SER ASN VAL GLN ASN MET ILE LYS GLY VAL VAL
SEQRES 11 A 199 LEU PHE GLY ASP THR ARG ASN LYS GLN ASP GLY GLY ARG
SEQRES 12 A 199 ILE PRO ASN PHE PRO THR ASP ARG THR LYS ILE TYR CYS
SEQRES 13 A 199 ALA PHE GLY ASP LEU VAL CYS ASP GLY THR LEU ILE ILE
SEQRES 14 A 199 THR ALA ALA HIS LEU SER TYR GLY ASP ASP VAL PRO ASN
SEQRES 15 A 199 ALA THR SER PHE LEU LEU SER LYS VAL LEU GLU HIS HIS
SEQRES 16 A 199 HIS HIS HIS HIS
FORMUL 2 HOH *19(H2 O)
HELIX 1 AA1 THR A 36 ARG A 49 1 14
HELIX 2 AA2 ASP A 65 LEU A 71 5 7
HELIX 3 AA3 SER A 76 CYS A 94 1 19
HELIX 4 AA4 SER A 105 ARG A 116 1 12
HELIX 5 AA5 PRO A 119 ASN A 124 1 6
HELIX 6 AA6 PRO A 148 ASP A 150 5 3
HELIX 7 AA7 ASP A 160 GLY A 165 5 6
HELIX 8 AA8 SER A 175 ASP A 178 5 4
HELIX 9 AA9 ASP A 179 VAL A 191 1 13
SHEET 1 AA1 5 VAL A 53 GLY A 57 0
SHEET 2 AA1 5 ILE A 19 ALA A 24 1 N PHE A 21 O GLN A 56
SHEET 3 AA1 5 LYS A 98 TYR A 104 1 O VAL A 100 N ILE A 22
SHEET 4 AA1 5 ILE A 126 PHE A 132 1 O PHE A 132 N GLY A 103
SHEET 5 AA1 5 THR A 152 TYR A 155 1 O TYR A 155 N LEU A 131
SSBOND 1 CYS A 16 CYS A 94 1555 1555 2.06
SSBOND 2 CYS A 42 CYS A 55 1555 1555 2.05
SSBOND 3 CYS A 156 CYS A 163 1555 1555 2.07
CISPEP 1 GLY A 59 PRO A 60 0 2.09
CRYST1 63.053 63.053 215.316 90.00 90.00 120.00 H 3 2 18
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 0.015860 0.009157 0.000000 0.00000
SCALE2 0.000000 0.018313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004644 0.00000
TER 1376 GLU A 193
MASTER 367 0 0 9 5 0 0 6 1394 1 6 16
END |