| content |
HEADER HYDROLASE 17-DEC-21 7QJP
TITLE CRYSTAL STRUCTURE OF A CUTINASE ENZYME FROM SACCHAROPOLYSPORA FLAVA
TITLE 2 (611)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA FLAVA;
SOURCE 3 ORGANISM_TAXID: 95161;
SOURCE 4 GENE: SAMN05660874_00127;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,L.AVILAN,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJP 0
JRNL AUTH E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,
JRNL AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,
JRNL AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,
JRNL AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)
JRNL TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY
JRNL REF NAT COMMUN V. 13 7850 2022
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-022-35237-X
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 3 NUMBER OF REFLECTIONS : 40562
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) : 0.141
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.884
REMARK 3 FREE R VALUE TEST SET COUNT : 1981
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) : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 509
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 15.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 34
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1949
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 314
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01300
REMARK 3 B22 (A**2) : 0.01300
REMARK 3 B33 (A**2) : -0.04300
REMARK 3 B12 (A**2) : 0.00700
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.911
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2039 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1826 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2795 ; 2.013 ; 1.653
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4253 ; 1.617 ; 1.577
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 6.804 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;34.092 ;23.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 297 ;11.036 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ; 8.956 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 279 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2344 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 432 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 391 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 23 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1020 ; 0.175 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 233 ; 0.237 ; 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): 1037 ; 1.170 ; 1.470
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1036 ; 1.118 ; 1.468
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1297 ; 1.761 ; 2.200
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1298 ; 1.768 ; 2.201
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1002 ; 1.886 ; 1.652
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1003 ; 1.885 ; 1.656
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1493 ; 2.738 ; 2.411
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1494 ; 2.737 ; 2.413
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 6 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8150 38.3597 -18.4699
REMARK 3 T TENSOR
REMARK 3 T11: 0.0146 T22: 0.0096
REMARK 3 T33: 0.0038 T12: 0.0088
REMARK 3 T13: 0.0029 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.4783 L22: 1.2670
REMARK 3 L33: 1.1105 L12: -0.2585
REMARK 3 L13: -0.3487 L23: 0.1200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.0076 S13: -0.0521
REMARK 3 S21: -0.0524 S22: -0.0019 S23: -0.0278
REMARK 3 S31: 0.0895 S32: 0.0315 S33: 0.0298
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 7QJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1292118059.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-21
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 : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8153
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40562
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.561
REMARK 200 RESOLUTION RANGE LOW (A) : 77.367
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 17.40
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.15300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: 1JFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.2 M SODIUM FLUORIDE,
REMARK 280 0.1 M BIS-TRIS PROPANE PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
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
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
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 TOTAL BURIED SURFACE AREA: 470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 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 649 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 0
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
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 H ASN A 247 O HOH A 401 1.06
REMARK 500 N ASN A 247 O HOH A 401 1.96
REMARK 500 O HOH A 585 O HOH A 629 1.96
REMARK 500 O HOH A 585 O HOH A 639 1.98
REMARK 500 OD1 ASP A 215 O HOH A 402 2.00
REMARK 500 O HOH A 502 O HOH A 641 2.00
REMARK 500 O HOH A 414 O HOH A 651 2.01
REMARK 500 O HOH A 412 O HOH A 639 2.06
REMARK 500 O HOH A 472 O HOH A 607 2.08
REMARK 500 O HOH A 408 O HOH A 621 2.09
REMARK 500 OE2 GLU A 13 O HOH A 403 2.11
REMARK 500 O ASP A 5 O HOH A 404 2.12
REMARK 500 O HOH A 425 O HOH A 544 2.12
REMARK 500 OE1 GLU A 13 O HOH A 405 2.18
REMARK 500 O HOH A 408 O HOH A 478 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 463 O HOH A 463 4555 2.04
REMARK 500 O HOH A 415 O HOH A 634 4554 2.08
REMARK 500 O HOH A 523 O HOH A 613 3565 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 13 CD GLU A 13 OE2 -0.092
REMARK 500 GLU A 14 CD GLU A 14 OE1 0.108
REMARK 500 GLU A 14 CD GLU A 14 OE2 0.080
REMARK 500 GLU A 68 CD GLU A 68 OE2 0.070
REMARK 500 ASP A 215 CG ASP A 215 OD2 0.212
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 20 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 215 CB - CG - OD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP A 215 CB - CG - OD2 ANGL. DEV. = 7.5 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 131 -120.18 63.47
REMARK 500 THR A 154 59.01 38.67
REMARK 500 HIS A 185 -85.89 -124.35
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 714 DISTANCE = 5.95 ANGSTROMS
DBREF1 7QJP A 1 260 UNP A0A1I6NU60_9PSEU
DBREF2 7QJP A A0A1I6NU60 34 293
SEQADV 7QJP MET A 0 UNP A0A1I6NU6 INITIATING METHIONINE
SEQADV 7QJP LEU A 261 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP GLU A 262 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 263 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 264 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 265 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 266 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 267 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 7QJP HIS A 268 UNP A0A1I6NU6 EXPRESSION TAG
SEQRES 1 A 269 MET ALA GLU PRO ALA ASP VAL HIS GLY PRO ASP PRO THR
SEQRES 2 A 269 GLU GLU SER ILE THR ALA PRO ARG GLY PRO PHE GLU VAL
SEQRES 3 A 269 ASP GLU GLU SER VAL SER ARG LEU SER VAL SER GLY PHE
SEQRES 4 A 269 GLY GLY GLY THR ILE TYR TYR PRO THR ASP THR THR ASP
SEQRES 5 A 269 GLY LEU PHE SER ALA VAL SER ILE SER PRO GLY PHE THR
SEQRES 6 A 269 GLY THR GLN GLU THR MET ALA TRP TYR GLY PRO ARG LEU
SEQRES 7 A 269 ALA SER GLN GLY PHE VAL VAL PHE THR ILE ASP THR ILE
SEQRES 8 A 269 THR THR THR ASP GLN PRO ASP SER ARG ALA ARG GLN LEU
SEQRES 9 A 269 GLN ALA SER LEU ASP TYR LEU VAL ASN ASP SER ASP VAL
SEQRES 10 A 269 LYS ASP ILE ILE ASP PRO ALA ARG LEU GLY VAL MET GLY
SEQRES 11 A 269 HIS SER MET GLY GLY GLY GLY SER LEU LYS ALA ALA LEU
SEQRES 12 A 269 ASP ASN PRO ALA LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 A 269 TRP HIS THR THR LYS ASP PHE SER GLY VAL GLN THR PRO
SEQRES 14 A 269 THR LEU ILE ILE GLY ALA GLN ASN ASP THR VAL ALA PRO
SEQRES 15 A 269 VAL SER GLN HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 A 269 ASP ASP PRO GLY LYS ALA TYR LEU GLU LEU ALA GLY ALA
SEQRES 17 A 269 SER HIS LEU ALA PRO ASN THR ASP ASN THR THR ILE ALA
SEQRES 18 A 269 LYS PHE SER ILE ALA TRP LEU LYS ARG PHE LEU ASP ASP
SEQRES 19 A 269 ASP THR ARG TYR ASP GLN PHE LEU CYS PRO PRO PRO GLU
SEQRES 20 A 269 ASN ASP ASP SER ILE SER ASP TYR GLN SER THR CYS PRO
SEQRES 21 A 269 TYR LEU GLU HIS HIS HIS HIS HIS HIS
HET PG4 A 301 31
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 2 PG4 C8 H18 O5
FORMUL 3 HOH *314(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 SER A 31 VAL A 35 5 5
HELIX 3 AA3 THR A 66 ALA A 71 5 6
HELIX 4 AA4 TRP A 72 SER A 79 1 8
HELIX 5 AA5 GLN A 95 ASP A 113 1 19
HELIX 6 AA6 VAL A 116 ASP A 118 5 3
HELIX 7 AA7 SER A 131 ASN A 144 1 14
HELIX 8 AA8 HIS A 185 LEU A 193 1 9
HELIX 9 AA9 LEU A 210 THR A 214 5 5
HELIX 10 AB1 ASN A 216 ASP A 232 1 17
HELIX 11 AB2 ASP A 234 ARG A 236 5 3
HELIX 12 AB3 TYR A 237 CYS A 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O PHE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N PHE A 54
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O LEU A 204 N GLY A 173
SHEET 3 AA2 3 ILE A 251 SER A 256 -1 O ASP A 253 N GLU A 203
SSBOND 1 CYS A 242 CYS A 258 1555 1555 2.03
CISPEP 1 ASP A 196 PRO A 197 0 1.22
CISPEP 2 CYS A 242 PRO A 243 0 -9.86
CISPEP 3 CYS A 258 PRO A 259 0 -8.42
CRYST1 89.336 89.336 74.324 90.00 90.00 120.00 P 3 2 1 6
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 0.011194 0.006463 0.000000 0.00000
SCALE2 0.000000 0.012925 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013455 0.00000
TER 3846 LEU A 261
MASTER 416 0 1 12 9 0 0 6 2276 1 33 21
END |