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HEADER HYDROLASE 26-MAR-24 8YTY
TITLE THE M12+P185V VARIANT OF KUBU-PETASE FROM KUTZNERIA BURIRAMENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RECOMBINANT KUBU-P-M12+P185V VARIANT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KUTZNERIA BURIRAMENSIS;
SOURCE 3 ORGANISM_TAXID: 1045776;
SOURCE 4 GENE: BCF44_11928;
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 J.PARK,H.SEO,H.HONG,K.-J.KIM
REVDAT 1 15-JAN-25 8YTY 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. 1.15 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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 74333
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3990
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4853
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1826
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 367
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : 0.08000
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): 0.035
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.022
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.446
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): 1967 ; 0.014 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 1777 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2711 ; 1.838 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4091 ; 0.647 ; 1.559
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 6.672 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 10 ; 9.767 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 248 ;11.722 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 299 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2400 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 476 ; 0.004 ; 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): 1052 ; 0.998 ; 0.837
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1052 ; 0.988 ; 0.837
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1324 ; 1.422 ; 1.510
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1325 ; 1.423 ; 1.512
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 915 ; 1.769 ; 0.967
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 914 ; 1.757 ; 0.962
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1386 ; 2.495 ; 1.714
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2354 ; 5.094 ;12.690
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2229 ; 4.357 ; 9.270
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 8YTY 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_1300046372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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 : 74333
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 32.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
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 (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM ACETATE TRIBASIC PH
REMARK 280 4.6, TACSIMATE PH 4.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 32.48150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.82250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.86500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.48150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.82250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.86500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.48150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.82250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 41.86500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.48150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.82250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 41.86500
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 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 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 546 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 548 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 641 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 37
REMARK 465 ALA A 38
REMARK 465 ASP A 39
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
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 GLN A 217 O HOH A 301 1.95
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 313 O HOH A 313 2555 1.38
REMARK 500 O HOH A 317 O HOH A 505 8544 1.90
REMARK 500 O ASN A 65 CD2 LEU A 289 6445 2.12
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 PRO A 215 CA - N - CD ANGL. DEV. = -10.4 DEGREES
REMARK 500 PRO A 215 CA - N - CD ANGL. DEV. = -10.1 DEGREES
REMARK 500 ALA A 278 N - CA - CB ANGL. DEV. = -8.7 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 SER A 162 -123.73 63.86
REMARK 500 HIS A 218 -83.68 -126.03
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 128 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 65 -22.24
REMARK 500 SER A 264 -17.48
REMARK 500 GLY A 274 14.30
REMARK 500 GLY A 274 -12.37
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 666 DISTANCE = 7.58 ANGSTROMS
REMARK 525 HOH A 667 DISTANCE = 9.91 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8YTU RELATED DB: PDB
REMARK 900 RELATED ID: 8YTV RELATED DB: PDB
REMARK 900 RELATED ID: 8YTW RELATED DB: PDB
DBREF1 8YTY A 38 288 UNP A0A3E0H050_9PSEU
DBREF2 8YTY A A0A3E0H050 38 288
SEQADV 8YTY MET A 37 UNP A0A3E0H05 INITIATING METHIONINE
SEQADV 8YTY ARG A 95 UNP A0A3E0H05 THR 95 VARIANT
SEQADV 8YTY ASN A 119 UNP A0A3E0H05 THR 119 VARIANT
SEQADV 8YTY SER A 127 UNP A0A3E0H05 GLN 127 VARIANT
SEQADV 8YTY GLN A 131 UNP A0A3E0H05 GLU 131 VARIANT
SEQADV 8YTY CYS A 173 UNP A0A3E0H05 ALA 173 VARIANT
SEQADV 8YTY ILE A 184 UNP A0A3E0H05 VAL 184 VARIANT
SEQADV 8YTY VAL A 185 UNP A0A3E0H05 PRO 185 VARIANT
SEQADV 8YTY HIS A 190 UNP A0A3E0H05 ASP 190 VARIANT
SEQADV 8YTY CYS A 197 UNP A0A3E0H05 LYS 197 VARIANT
SEQADV 8YTY CYS A 236 UNP A0A3E0H05 ALA 236 VARIANT
SEQADV 8YTY SER A 239 UNP A0A3E0H05 ASP 239 VARIANT
SEQADV 8YTY SER A 279 UNP A0A3E0H05 ALA 279 VARIANT
SEQADV 8YTY CYS A 281 UNP A0A3E0H05 SER 281 VARIANT
SEQADV 8YTY LEU A 289 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY GLU A 290 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 291 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 292 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 293 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 294 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 295 UNP A0A3E0H05 EXPRESSION TAG
SEQADV 8YTY HIS A 296 UNP A0A3E0H05 EXPRESSION TAG
SEQRES 1 A 260 MET ALA ASP GLN VAL GLY GLN ALA PRO THR ALA ALA ASN
SEQRES 2 A 260 ILE THR GLY ASP GLY SER PHE ALA THR ALA SER ALA PRO
SEQRES 3 A 260 ILE THR ASN GLN THR GLY PHE GLY GLY GLY THR VAL TYR
SEQRES 4 A 260 TYR PRO THR ALA ALA GLY THR TYR PRO VAL VAL ALA VAL
SEQRES 5 A 260 VAL PRO GLY PHE VAL SER ARG TRP SER GLN ILE SER TRP
SEQRES 6 A 260 LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL VAL VAL
SEQRES 7 A 260 GLY ALA ASP THR ASN SER GLY PHE ASP SER PRO SER SER
SEQRES 8 A 260 ARG ALA ASP GLN LEU LEU ALA ALA LEU ASN TRP ALA VAL
SEQRES 9 A 260 ASN SER ALA PRO ALA ALA VAL ARG GLY LYS VAL ASP GLY
SEQRES 10 A 260 THR ARG ARG GLY VAL ALA GLY TRP SER MET GLY GLY GLY
SEQRES 11 A 260 GLY THR LEU GLU ALA LEU CYS LYS ASP THR THR GLY THR
SEQRES 12 A 260 VAL LYS ALA GLY ILE VAL LEU ALA PRO TRP HIS ILE GLY
SEQRES 13 A 260 GLN ASP PHE SER CYS VAL THR LYS PRO VAL PHE ILE VAL
SEQRES 14 A 260 GLY ALA GLN ASN ASP THR ILE ALA PRO PRO ALA GLN HIS
SEQRES 15 A 260 ALA VAL PRO PHE TYR ASN ALA ALA ALA GLY PRO LYS SER
SEQRES 16 A 260 TYR LEU GLU LEU CYS GLY ALA SER HIS PHE PHE PRO THR
SEQRES 17 A 260 THR ALA ASN PRO THR VAL SER ARG ALA MET VAL SER TRP
SEQRES 18 A 260 LEU LYS ARG PHE VAL SER SER ASP ASP ARG PHE THR PRO
SEQRES 19 A 260 PHE THR CYS GLY PHE ALA GLY ALA SER VAL CYS ALA PHE
SEQRES 20 A 260 ARG SER THR ALA CYS LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *367(H2 O)
HELIX 1 AA1 ARG A 95 SER A 100 5 6
HELIX 2 AA2 TRP A 101 SER A 108 1 8
HELIX 3 AA3 SER A 124 SER A 142 1 19
HELIX 4 AA4 PRO A 144 GLY A 149 1 6
HELIX 5 AA5 SER A 162 ASP A 175 1 14
HELIX 6 AA6 HIS A 218 ALA A 226 1 9
HELIX 7 AA7 PHE A 241 THR A 245 5 5
HELIX 8 AA8 ASN A 247 VAL A 262 1 16
HELIX 9 AA9 ASP A 265 CYS A 273 5 9
SHEET 1 AA1 9 THR A 58 PRO A 62 0
SHEET 2 AA1 9 GLY A 72 PRO A 77 -1 O VAL A 74 N ALA A 61
SHEET 3 AA1 9 VAL A 112 ALA A 116 -1 O GLY A 115 N THR A 73
SHEET 4 AA1 9 TYR A 83 VAL A 89 1 N VAL A 86 O VAL A 114
SHEET 5 AA1 9 VAL A 151 TRP A 161 1 O ASP A 152 N TYR A 83
SHEET 6 AA1 9 VAL A 180 LEU A 186 1 O LYS A 181 N ARG A 156
SHEET 7 AA1 9 VAL A 202 ALA A 207 1 O VAL A 205 N VAL A 185
SHEET 8 AA1 9 LYS A 230 LEU A 235 1 O LEU A 235 N GLY A 206
SHEET 9 AA1 9 VAL A 280 SER A 285 -1 O CYS A 281 N GLU A 234
SSBOND 1 CYS A 173 CYS A 197 1555 1555 2.02
SSBOND 2 CYS A 236 CYS A 281 1555 1555 2.02
SSBOND 3 CYS A 273 CYS A 288 1555 1555 2.03
CRYST1 64.963 81.645 83.730 90.00 90.00 90.00 I 2 2 2 8
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 0.015393 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012248 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011943 0.00000
TER 1956 GLU A 290
MASTER 402 0 0 9 9 0 0 6 2193 1 6 20
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