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HEADER HYDROLASE 27-JUL-22 8AIR
TITLE CRYSTAL STRUCTURE OF CUTINASE RGCUTII FROM RHIZOBACTER GUMMIPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RGCUTII;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBACTER GUMMIPHILUS;
SOURCE 3 ORGANISM_TAXID: 946333;
SOURCE 4 GENE: A4W93_03190;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PET, CUTINASE, ESTER BOND, CLEAVAGE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,M.D.ALLEN,A.R.PICKFORD,J.E.MCGEEHAN
REVDAT 1 08-MAR-23 8AIR 0
JRNL AUTH L.AVILAN,M.ZAHN
JRNL TITL AUTOINHIBITION ON POLY(ETHYLENE TEREPHTHALATE), A PROPERTY
JRNL TITL 2 OF ISPETASE AND ITS MESOPHILIC HOMOLOGUES, CAN BE ELIMINATED
JRNL TITL 3 BY ENZYME ENGINEERING
JRNL REF TO BE PUBLISHED 2023
JRNL REFN
JRNL DOI 10.1002/CSSC.202202277
REMARK 2
REMARK 2 RESOLUTION. 1.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 104451
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.041
REMARK 3 FREE R VALUE TEST SET COUNT : 5265
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) : 1.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6904
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.4140
REMARK 3 BIN FREE R VALUE SET COUNT : 366
REMARK 3 BIN FREE R VALUE : 0.4140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46600
REMARK 3 B22 (A**2) : 0.46600
REMARK 3 B33 (A**2) : -1.51100
REMARK 3 B12 (A**2) : 0.23300
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): 0.036
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2019 ; 0.011 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 1786 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2764 ; 1.841 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4177 ; 0.638 ; 1.544
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 271 ; 6.252 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 13 ;10.686 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 300 ;13.146 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 306 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2354 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 418 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 393 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 62 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1021 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 236 ; 0.207 ; 0.200
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): 1041 ; 0.842 ; 0.741
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1039 ; 0.836 ; 0.739
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1301 ; 1.321 ; 1.108
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1302 ; 1.322 ; 1.112
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 978 ; 1.376 ; 0.896
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 979 ; 1.376 ; 0.897
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1455 ; 2.046 ; 1.290
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1456 ; 2.046 ; 1.291
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 25 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5331 -15.6011 1.0352
REMARK 3 T TENSOR
REMARK 3 T11: 0.0143 T22: 0.0042
REMARK 3 T33: 0.0616 T12: 0.0054
REMARK 3 T13: -0.0069 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.8408 L22: 0.8759
REMARK 3 L33: 1.0906 L12: 0.1578
REMARK 3 L13: 0.0635 L23: 0.3490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: -0.0317 S13: -0.0196
REMARK 3 S21: 0.0436 S22: 0.0081 S23: -0.0081
REMARK 3 S31: 0.0389 S32: 0.0348 S33: -0.0195
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8AIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1292124336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-18
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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112681
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 49.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.77400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
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: 4CG1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 1 M SODIUM
REMARK 280 ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 74.24867
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 148.49733
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 111.37300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 185.62167
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 37.12433
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.24867
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 148.49733
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 185.62167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 111.37300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.12433
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 645 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 658 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 LYS A 2
REMARK 465 LEU A 3
REMARK 465 ASN A 4
REMARK 465 ARG A 5
REMARK 465 LEU A 6
REMARK 465 PHE A 7
REMARK 465 GLN A 8
REMARK 465 VAL A 9
REMARK 465 ALA A 10
REMARK 465 CYS A 11
REMARK 465 LEU A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 THR A 15
REMARK 465 LEU A 16
REMARK 465 VAL A 17
REMARK 465 THR A 18
REMARK 465 ALA A 19
REMARK 465 THR A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 ALA A 24
REMARK 465 GLU A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
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 OG SER A 259 O HOH A 401 1.77
REMARK 500 O HOH A 402 O HOH A 602 1.92
REMARK 500 OXT ACT A 302 O HOH A 402 2.05
REMARK 500 O HOH A 626 O HOH A 691 2.07
REMARK 500 O HOH A 700 O HOH A 726 2.13
REMARK 500 O HOH A 413 O HOH A 601 2.13
REMARK 500 O HOH A 409 O HOH A 651 2.14
REMARK 500 O HOH A 460 O HOH A 586 2.15
REMARK 500 O HOH A 413 O HOH A 649 2.16
REMARK 500 O HOH A 578 O HOH A 644 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 O HOH A 408 O HOH A 568 6555 2.02
REMARK 500 O HOH A 410 O HOH A 419 8555 2.05
REMARK 500 O HOH A 403 O HOH A 618 6555 2.19
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 40 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 145 CG - CD - NE ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 224 NE - CZ - NH2 ANGL. DEV. = -6.0 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 ASN A 53 87.03 -151.39
REMARK 500 ASN A 65 36.75 -140.22
REMARK 500 SER A 152 -125.71 68.39
REMARK 500 HIS A 206 -87.37 -122.36
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 115 0.12 SIDE CHAIN
REMARK 500 ARG A 145 0.12 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 734 DISTANCE = 6.30 ANGSTROMS
DBREF1 8AIR A 1 279 UNP A0A1W6L438_9BURK
DBREF2 8AIR A A0A1W6L438 1 279
SEQADV 8AIR LEU A 280 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR GLU A 281 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 282 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 283 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 284 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 285 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 286 UNP A0A1W6L43 EXPRESSION TAG
SEQADV 8AIR HIS A 287 UNP A0A1W6L43 EXPRESSION TAG
SEQRES 1 A 287 MET LYS LEU ASN ARG LEU PHE GLN VAL ALA CYS LEU ALA
SEQRES 2 A 287 ALA THR LEU VAL THR ALA THR ALA ALA SER ALA VAL GLN
SEQRES 3 A 287 ILE GLY PRO ALA PRO THR LYS ALA SER LEU GLU ALA SER
SEQRES 4 A 287 ARG GLY PRO PHE THR VAL ALA THR THR ARG LEU SER ALA
SEQRES 5 A 287 ASN GLY HIS GLY GLY GLY THR ILE TYR TYR PRO THR ASN
SEQRES 6 A 287 ALA GLY ALA LYS VAL GLY VAL ILE ALA ILE VAL PRO GLY
SEQRES 7 A 287 TYR LEU SER TYR GLN SER SER ILE GLU TRP TRP GLY PRO
SEQRES 8 A 287 ARG LEU ALA SER HIS GLY PHE ALA VAL VAL THR ILE ASP
SEQRES 9 A 287 THR LEU THR ILE TYR ASP GLN PRO SER SER ARG SER SER
SEQRES 10 A 287 GLN GLN LEU ARG ALA LEU ASP GLN VAL VAL ALA LEU GLY
SEQRES 11 A 287 SER LYS SER THR SER PRO LEU TYR ASN LYS VAL ASP GLY
SEQRES 12 A 287 SER ARG THR GLY VAL MET GLY TRP SER MET GLY GLY GLY
SEQRES 13 A 287 GLY SER LEU ILE SER ALA GLN ASN ARG PRO SER ILE LYS
SEQRES 14 A 287 ALA ALA ALA PRO GLN ALA PRO TRP ASN THR THR SER ASN
SEQRES 15 A 287 PHE SER SER LEU THR VAL PRO THR LEU ILE PHE ALA CYS
SEQRES 16 A 287 GLN ALA ASP VAL VAL ALA PRO ILE LEU SER HIS ALA VAL
SEQRES 17 A 287 PRO PHE TYR ASN SER MET SER ARG ASN PRO LYS GLN TYR
SEQRES 18 A 287 LEU GLU ARG THR ALA GLY ASP HIS PHE CYS PHE ASN ASN
SEQRES 19 A 287 ALA ASN PRO THR VAL GLY LEU LYS GLY VAL ALA TRP MET
SEQRES 20 A 287 LYS ARG PHE ILE ASP GLY ASP THR ARG TYR THR SER PHE
SEQRES 21 A 287 ALA CYS SER ASN PRO ASN ALA LEU GLY PHE SER SER PHE
SEQRES 22 A 287 ARG THR GLU ARG CYS SER LEU GLU HIS HIS HIS HIS HIS
SEQRES 23 A 287 HIS
HET ACT A 301 4
HET ACT A 302 4
HETNAM ACT ACETATE ION
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 HOH *334(H2 O)
HELIX 1 AA1 THR A 32 ALA A 38 1 7
HELIX 2 AA2 TYR A 82 GLU A 87 5 6
HELIX 3 AA3 TRP A 88 SER A 95 1 8
HELIX 4 AA4 GLN A 111 GLY A 130 1 20
HELIX 5 AA5 SER A 152 ARG A 165 1 14
HELIX 6 AA6 HIS A 206 MET A 214 1 9
HELIX 7 AA7 ASN A 236 ASP A 252 1 17
HELIX 8 AA8 ASP A 254 ARG A 256 5 3
HELIX 9 AA9 TYR A 257 SER A 263 1 7
SHEET 1 AA1 6 VAL A 45 LEU A 50 0
SHEET 2 AA1 6 GLY A 58 PRO A 63 -1 O ILE A 60 N THR A 48
SHEET 3 AA1 6 PHE A 98 ILE A 103 -1 O VAL A 100 N TYR A 61
SHEET 4 AA1 6 VAL A 70 VAL A 76 1 N ILE A 75 O VAL A 101
SHEET 5 AA1 6 VAL A 141 GLY A 150 1 O ASP A 142 N VAL A 70
SHEET 6 AA1 6 ALA A 170 ALA A 171 1 O ALA A 170 N VAL A 148
SHEET 1 AA2 3 THR A 190 CYS A 195 0
SHEET 2 AA2 3 LYS A 219 ARG A 224 1 O GLN A 220 N ILE A 192
SHEET 3 AA2 3 PHE A 270 GLU A 276 -1 O ARG A 274 N TYR A 221
SSBOND 1 CYS A 195 CYS A 231 1555 1555 2.11
SSBOND 2 CYS A 262 CYS A 278 1555 1555 2.08
CRYST1 63.127 63.127 222.746 90.00 90.00 120.00 P 61 2 2 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 0.015841 0.009146 0.000000 0.00000
SCALE2 0.000000 0.018292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004489 0.00000
TER 1953 LEU A 280
MASTER 443 0 2 9 9 0 0 6 2262 1 12 23
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