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HEADER HYDROLASE 26-MAR-24 8YTU
TITLE MIPA-PETASE FROM MICROMONOSPORA PATTALOONGENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: RECOMBINANT MIPA-PETASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA PATTALOONGENSIS;
SOURCE 3 ORGANISM_TAXID: 405436;
SOURCE 4 GENE: SAMN05444365_106119;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: -T1R
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HONG,H.SEO,J.PARK,K.-J.KIM
REVDAT 1 15-JAN-25 8YTU 0
JRNL AUTH H.SEO,H.HONG,J.PARK,S.H.LEE,D.KI,A.RYU,H.Y.SAGONG,K.J.KIM
JRNL TITL LANDSCAPE PROFILING OF PET DEPOLYMERASES USING A NATURAL
JRNL TITL 2 SEQUENCE CLUSTER FRAMEWORK.
JRNL REF SCIENCE V. 387 P5637 2025
JRNL REFN ESSN 1095-9203
JRNL PMID 39745946
JRNL DOI 10.1126/SCIENCE.ADP5637
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0411
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) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 136706
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 7442
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) : 1.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6109
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.4920
REMARK 3 BIN FREE R VALUE SET COUNT : 356
REMARK 3 BIN FREE R VALUE : 0.4780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5675
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 483
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.92000
REMARK 3 B22 (A**2) : 0.87000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.00000
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): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.868
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5922 ; 0.007 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 5322 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8100 ; 1.446 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12205 ; 0.514 ; 1.564
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 780 ; 6.743 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ; 7.590 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 790 ;12.038 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 868 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7304 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1500 ; 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): 3099 ; 1.963 ; 2.301
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3099 ; 1.961 ; 2.301
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3886 ; 2.743 ; 4.125
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3887 ; 2.743 ; 4.127
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2823 ; 2.664 ; 2.575
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2824 ; 2.663 ; 2.578
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4215 ; 4.065 ; 4.595
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6697 ; 5.870 ;24.670
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6589 ; 5.739 ;23.310
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 8YTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300046368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
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 : DCM SI (111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136706
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
REMARK 200 RESOLUTION RANGE LOW (A) : 36.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 0.3640
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CAPS, PH 10.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 24.53350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.93750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.70550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.93750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.53350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.70550
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 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 38
REMARK 465 ALA A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 ALA A 42
REMARK 465 SER A 43
REMARK 465 ALA A 44
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 38
REMARK 465 ALA B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 ALA B 42
REMARK 465 SER B 43
REMARK 465 ALA B 44
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 MET C 38
REMARK 465 ALA C 39
REMARK 465 PRO C 40
REMARK 465 PRO C 41
REMARK 465 ALA C 42
REMARK 465 SER C 43
REMARK 465 HIS C 301
REMARK 465 HIS C 302
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 O HOH C 408 O HOH C 429 1.75
REMARK 500 O HOH A 669 O HOH A 683 1.83
REMARK 500 O HOH A 527 O HOH B 645 1.88
REMARK 500 O HOH B 529 O HOH B 645 1.91
REMARK 500 ND1 HIS C 297 O HOH C 401 2.01
REMARK 500 O HOH A 610 O HOH A 658 2.08
REMARK 500 O HOH A 503 O HOH A 642 2.13
REMARK 500 SG CYS C 292 O HOH C 401 2.14
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 O HOH A 623 O HOH C 450 4545 2.16
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 SER A 147 -64.49 -133.55
REMARK 500 SER A 168 -120.24 60.74
REMARK 500 HIS A 222 -82.11 -127.00
REMARK 500 SER B 168 -119.06 59.61
REMARK 500 HIS B 222 -80.39 -131.10
REMARK 500 ASN B 246 30.95 -98.16
REMARK 500 LEU C 49 127.21 -36.48
REMARK 500 ALA C 85 149.34 177.90
REMARK 500 SER C 147 -60.27 -136.68
REMARK 500 SER C 168 -116.26 62.94
REMARK 500 HIS C 222 -81.37 -126.76
REMARK 500 HIS C 222 -81.37 -125.32
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 47 0.10 SIDE CHAIN
REMARK 500 ARG A 101 0.26 SIDE CHAIN
REMARK 500 ARG A 110 0.26 SIDE CHAIN
REMARK 500 ARG A 134 0.09 SIDE CHAIN
REMARK 500 ARG A 185 0.28 SIDE CHAIN
REMARK 500 ARG A 201 0.22 SIDE CHAIN
REMARK 500 ARG B 47 0.08 SIDE CHAIN
REMARK 500 ARG B 101 0.29 SIDE CHAIN
REMARK 500 ARG B 110 0.23 SIDE CHAIN
REMARK 500 ARG B 134 0.12 SIDE CHAIN
REMARK 500 ARG B 140 0.26 SIDE CHAIN
REMARK 500 ARG B 161 0.11 SIDE CHAIN
REMARK 500 ARG B 201 0.28 SIDE CHAIN
REMARK 500 ARG B 257 0.26 SIDE CHAIN
REMARK 500 ARG C 111 0.07 SIDE CHAIN
REMARK 500 ARG C 134 0.08 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 B 676 DISTANCE = 5.83 ANGSTROMS
DBREF1 8YTU A 39 294 UNP A0A1H3QT72_9ACTN
DBREF2 8YTU A A0A1H3QT72 39 294
DBREF1 8YTU B 39 294 UNP A0A1H3QT72_9ACTN
DBREF2 8YTU B A0A1H3QT72 39 294
DBREF1 8YTU C 39 294 UNP A0A1H3QT72_9ACTN
DBREF2 8YTU C A0A1H3QT72 39 294
SEQADV 8YTU MET A 38 UNP A0A1H3QT7 INITIATING METHIONINE
SEQADV 8YTU LEU A 295 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU GLU A 296 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 297 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 298 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 299 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 300 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 301 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS A 302 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU MET B 38 UNP A0A1H3QT7 INITIATING METHIONINE
SEQADV 8YTU LEU B 295 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU GLU B 296 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 297 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 298 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 299 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 300 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 301 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS B 302 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU MET C 38 UNP A0A1H3QT7 INITIATING METHIONINE
SEQADV 8YTU LEU C 295 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU GLU C 296 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 297 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 298 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 299 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 300 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 301 UNP A0A1H3QT7 EXPRESSION TAG
SEQADV 8YTU HIS C 302 UNP A0A1H3QT7 EXPRESSION TAG
SEQRES 1 A 265 MET ALA PRO PRO ALA SER ALA THR GLU ARG GLY LEU ALA
SEQRES 2 A 265 PRO THR ALA ALA ASN ILE THR GLY ASP GLY SER TYR GLY
SEQRES 3 A 265 VAL VAL SER ALA THR ILE THR GLY ALA SER GLY PHE GLY
SEQRES 4 A 265 GLY GLY VAL VAL TYR TYR PRO ASN ALA THR GLU ARG PHE
SEQRES 5 A 265 PRO VAL VAL ALA ILE SER PRO GLY TYR THR GLU ARG TRP
SEQRES 6 A 265 SER SER PHE ALA TRP LEU GLY ARG ARG LEU ALA SER TRP
SEQRES 7 A 265 GLY PHE VAL VAL VAL GLY ILE GLU THR ASN SER LEU PHE
SEQRES 8 A 265 ASP GLN PRO ASN SER ARG GLY THR GLN LEU LEU ARG ALA
SEQRES 9 A 265 LEU ASP TRP ALA SER SER SER ALA PRO ALA ALA VAL ARG
SEQRES 10 A 265 ASP ARG VAL ASP ALA THR ARG GLN GLY VAL SER GLY HIS
SEQRES 11 A 265 SER MET GLY GLY GLY GLY THR LEU SER ALA MET ASP GLN
SEQRES 12 A 265 ARG PRO SER VAL ARG ALA GLY VAL PRO LEU ALA PRO TRP
SEQRES 13 A 265 HIS THR THR THR SER TRP PRO ARG VAL THR ASN PRO VAL
SEQRES 14 A 265 MET ILE LEU GLY GLY GLN ASN ASP GLY ILE ALA PRO VAL
SEQRES 15 A 265 SER SER HIS ALA ILE PRO MET TYR THR GLY VAL ALA SER
SEQRES 16 A 265 GLY GLU LYS ALA TYR VAL GLU LEU ALA GLY ALA GLY HIS
SEQRES 17 A 265 ASN PHE PRO ASN SER ALA ASN PRO ILE VAL SER ARG ALA
SEQRES 18 A 265 ALA VAL SER TRP PHE LYS ARG PHE LEU ASP ASP ASP THR
SEQRES 19 A 265 ARG PHE ALA PRO PHE ALA CYS ASP PHE GLY GLY ALA SER
SEQRES 20 A 265 ILE SER GLN PHE ARG SER THR CYS PRO VAL LEU GLU HIS
SEQRES 21 A 265 HIS HIS HIS HIS HIS
SEQRES 1 B 265 MET ALA PRO PRO ALA SER ALA THR GLU ARG GLY LEU ALA
SEQRES 2 B 265 PRO THR ALA ALA ASN ILE THR GLY ASP GLY SER TYR GLY
SEQRES 3 B 265 VAL VAL SER ALA THR ILE THR GLY ALA SER GLY PHE GLY
SEQRES 4 B 265 GLY GLY VAL VAL TYR TYR PRO ASN ALA THR GLU ARG PHE
SEQRES 5 B 265 PRO VAL VAL ALA ILE SER PRO GLY TYR THR GLU ARG TRP
SEQRES 6 B 265 SER SER PHE ALA TRP LEU GLY ARG ARG LEU ALA SER TRP
SEQRES 7 B 265 GLY PHE VAL VAL VAL GLY ILE GLU THR ASN SER LEU PHE
SEQRES 8 B 265 ASP GLN PRO ASN SER ARG GLY THR GLN LEU LEU ARG ALA
SEQRES 9 B 265 LEU ASP TRP ALA SER SER SER ALA PRO ALA ALA VAL ARG
SEQRES 10 B 265 ASP ARG VAL ASP ALA THR ARG GLN GLY VAL SER GLY HIS
SEQRES 11 B 265 SER MET GLY GLY GLY GLY THR LEU SER ALA MET ASP GLN
SEQRES 12 B 265 ARG PRO SER VAL ARG ALA GLY VAL PRO LEU ALA PRO TRP
SEQRES 13 B 265 HIS THR THR THR SER TRP PRO ARG VAL THR ASN PRO VAL
SEQRES 14 B 265 MET ILE LEU GLY GLY GLN ASN ASP GLY ILE ALA PRO VAL
SEQRES 15 B 265 SER SER HIS ALA ILE PRO MET TYR THR GLY VAL ALA SER
SEQRES 16 B 265 GLY GLU LYS ALA TYR VAL GLU LEU ALA GLY ALA GLY HIS
SEQRES 17 B 265 ASN PHE PRO ASN SER ALA ASN PRO ILE VAL SER ARG ALA
SEQRES 18 B 265 ALA VAL SER TRP PHE LYS ARG PHE LEU ASP ASP ASP THR
SEQRES 19 B 265 ARG PHE ALA PRO PHE ALA CYS ASP PHE GLY GLY ALA SER
SEQRES 20 B 265 ILE SER GLN PHE ARG SER THR CYS PRO VAL LEU GLU HIS
SEQRES 21 B 265 HIS HIS HIS HIS HIS
SEQRES 1 C 265 MET ALA PRO PRO ALA SER ALA THR GLU ARG GLY LEU ALA
SEQRES 2 C 265 PRO THR ALA ALA ASN ILE THR GLY ASP GLY SER TYR GLY
SEQRES 3 C 265 VAL VAL SER ALA THR ILE THR GLY ALA SER GLY PHE GLY
SEQRES 4 C 265 GLY GLY VAL VAL TYR TYR PRO ASN ALA THR GLU ARG PHE
SEQRES 5 C 265 PRO VAL VAL ALA ILE SER PRO GLY TYR THR GLU ARG TRP
SEQRES 6 C 265 SER SER PHE ALA TRP LEU GLY ARG ARG LEU ALA SER TRP
SEQRES 7 C 265 GLY PHE VAL VAL VAL GLY ILE GLU THR ASN SER LEU PHE
SEQRES 8 C 265 ASP GLN PRO ASN SER ARG GLY THR GLN LEU LEU ARG ALA
SEQRES 9 C 265 LEU ASP TRP ALA SER SER SER ALA PRO ALA ALA VAL ARG
SEQRES 10 C 265 ASP ARG VAL ASP ALA THR ARG GLN GLY VAL SER GLY HIS
SEQRES 11 C 265 SER MET GLY GLY GLY GLY THR LEU SER ALA MET ASP GLN
SEQRES 12 C 265 ARG PRO SER VAL ARG ALA GLY VAL PRO LEU ALA PRO TRP
SEQRES 13 C 265 HIS THR THR THR SER TRP PRO ARG VAL THR ASN PRO VAL
SEQRES 14 C 265 MET ILE LEU GLY GLY GLN ASN ASP GLY ILE ALA PRO VAL
SEQRES 15 C 265 SER SER HIS ALA ILE PRO MET TYR THR GLY VAL ALA SER
SEQRES 16 C 265 GLY GLU LYS ALA TYR VAL GLU LEU ALA GLY ALA GLY HIS
SEQRES 17 C 265 ASN PHE PRO ASN SER ALA ASN PRO ILE VAL SER ARG ALA
SEQRES 18 C 265 ALA VAL SER TRP PHE LYS ARG PHE LEU ASP ASP ASP THR
SEQRES 19 C 265 ARG PHE ALA PRO PHE ALA CYS ASP PHE GLY GLY ALA SER
SEQRES 20 C 265 ILE SER GLN PHE ARG SER THR CYS PRO VAL LEU GLU HIS
SEQRES 21 C 265 HIS HIS HIS HIS HIS
HET EDO A 401 4
HET GOL B 401 6
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 EDO C2 H6 O2
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *483(H2 O)
HELIX 1 AA1 ARG A 101 SER A 104 5 4
HELIX 2 AA2 PHE A 105 SER A 114 1 10
HELIX 3 AA3 GLN A 130 SER A 147 1 18
HELIX 4 AA4 PRO A 150 ASP A 155 1 6
HELIX 5 AA5 SER A 168 ARG A 181 1 14
HELIX 6 AA6 HIS A 222 VAL A 230 1 9
HELIX 7 AA7 ASN A 246 SER A 250 5 5
HELIX 8 AA8 ASN A 252 ASP A 268 1 17
HELIX 9 AA9 ASP A 270 ARG A 272 5 3
HELIX 10 AB1 PHE A 273 CYS A 278 1 6
HELIX 11 AB2 ARG B 101 SER B 104 5 4
HELIX 12 AB3 PHE B 105 SER B 114 1 10
HELIX 13 AB4 GLN B 130 SER B 148 1 19
HELIX 14 AB5 PRO B 150 ASP B 155 1 6
HELIX 15 AB6 SER B 168 ARG B 181 1 14
HELIX 16 AB7 HIS B 222 VAL B 230 1 9
HELIX 17 AB8 ASN B 246 SER B 250 5 5
HELIX 18 AB9 ASN B 252 ASP B 268 1 17
HELIX 19 AC1 ASP B 270 ARG B 272 5 3
HELIX 20 AC2 PHE B 273 CYS B 278 1 6
HELIX 21 AC3 VAL B 294 HIS B 298 5 5
HELIX 22 AC4 ARG C 101 SER C 104 5 4
HELIX 23 AC5 PHE C 105 SER C 114 1 10
HELIX 24 AC6 GLN C 130 SER C 146 1 17
HELIX 25 AC7 PRO C 150 ASP C 155 1 6
HELIX 26 AC8 SER C 168 ARG C 181 1 14
HELIX 27 AC9 HIS C 222 VAL C 230 1 9
HELIX 28 AD1 ASN C 246 SER C 250 5 5
HELIX 29 AD2 ASN C 252 ASP C 268 1 17
HELIX 30 AD3 ASP C 270 ASP C 279 5 10
HELIX 31 AD4 VAL C 294 HIS C 298 5 5
SHEET 1 AA1 6 VAL A 64 THR A 68 0
SHEET 2 AA1 6 GLY A 78 PRO A 83 -1 O TYR A 82 N VAL A 65
SHEET 3 AA1 6 VAL A 118 ILE A 122 -1 O VAL A 119 N TYR A 81
SHEET 4 AA1 6 PHE A 89 SER A 95 1 N VAL A 92 O VAL A 120
SHEET 5 AA1 6 VAL A 157 HIS A 167 1 O ASP A 158 N PHE A 89
SHEET 6 AA1 6 ALA A 186 LEU A 190 1 O LEU A 190 N GLY A 166
SHEET 1 AA2 3 VAL A 206 GLY A 211 0
SHEET 2 AA2 3 LYS A 235 LEU A 240 1 O LEU A 240 N GLY A 210
SHEET 3 AA2 3 ILE A 285 SER A 290 -1 O ARG A 289 N TYR A 237
SHEET 1 AA3 6 VAL B 64 THR B 68 0
SHEET 2 AA3 6 GLY B 78 PRO B 83 -1 O TYR B 82 N VAL B 65
SHEET 3 AA3 6 VAL B 118 ILE B 122 -1 O GLY B 121 N VAL B 79
SHEET 4 AA3 6 PHE B 89 SER B 95 1 N VAL B 92 O VAL B 120
SHEET 5 AA3 6 VAL B 157 HIS B 167 1 O ASP B 158 N PHE B 89
SHEET 6 AA3 6 ALA B 186 LEU B 190 1 O LEU B 190 N GLY B 166
SHEET 1 AA4 3 VAL B 206 GLY B 211 0
SHEET 2 AA4 3 LYS B 235 LEU B 240 1 O LEU B 240 N GLY B 210
SHEET 3 AA4 3 ILE B 285 SER B 290 -1 O ARG B 289 N TYR B 237
SHEET 1 AA5 6 VAL C 64 THR C 68 0
SHEET 2 AA5 6 GLY C 77 PRO C 83 -1 O VAL C 80 N ALA C 67
SHEET 3 AA5 6 VAL C 118 GLU C 123 -1 O VAL C 119 N TYR C 81
SHEET 4 AA5 6 PHE C 89 SER C 95 1 N VAL C 92 O VAL C 120
SHEET 5 AA5 6 VAL C 157 HIS C 167 1 O ASP C 158 N PHE C 89
SHEET 6 AA5 6 ALA C 186 LEU C 190 1 O LEU C 190 N GLY C 166
SHEET 1 AA6 3 VAL C 206 GLY C 211 0
SHEET 2 AA6 3 LYS C 235 LEU C 240 1 O ALA C 236 N ILE C 208
SHEET 3 AA6 3 ILE C 285 SER C 290 -1 O ARG C 289 N TYR C 237
SSBOND 1 CYS A 278 CYS A 292 1555 1555 2.06
CRYST1 49.067 103.411 131.875 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 0.020380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007583 0.00000
TER 1859 VAL A 294
TER 3781 HIS B 300
TER 5714 HIS C 300
MASTER 411 0 2 31 27 0 0 6 6168 3 12 63
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