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HEADER HYDROLASE 17-DEC-21 7QJT
TITLE CRYSTAL STRUCTURE OF A CUTINASE ENZYME FROM THERMOBIFIDA
TITLE 2 CELLULOSILYTICA TB100 (711)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE (711);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA CELLULOSILYTICA TB100;
SOURCE 3 ORGANISM_TAXID: 665004;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,T.J.SHAKESPEARE,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJT 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. 1.78 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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 65.0
REMARK 3 NUMBER OF REFLECTIONS : 17057
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) : 0.182
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.001
REMARK 3 FREE R VALUE TEST SET COUNT : 853
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) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 1
REMARK 3 BIN FREE R VALUE : 0.4650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35900
REMARK 3 B22 (A**2) : 0.35900
REMARK 3 B33 (A**2) : -0.71700
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): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.471
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2115 ; 0.012 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1912 ; 0.001 ; 0.014
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2884 ; 1.777 ; 1.651
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4408 ; 1.430 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 7.906 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;27.158 ;20.625
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 305 ;13.385 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;11.744 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2418 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 494 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 462 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 43 ; 0.257 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1017 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 199 ; 0.181 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.136 ; 0.200
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): 2 ; 0.082 ; 0.200
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): 1067 ; 1.276 ; 1.589
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1066 ; 1.268 ; 1.588
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1332 ; 2.218 ; 2.378
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1333 ; 2.218 ; 2.380
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1047 ; 1.494 ; 1.791
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1048 ; 1.494 ; 1.793
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1552 ; 2.538 ; 2.615
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1553 ; 2.537 ; 2.616
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 267
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8901 26.5490 -5.7805
REMARK 3 T TENSOR
REMARK 3 T11: 0.0011 T22: 0.0023
REMARK 3 T33: 0.0269 T12: -0.0009
REMARK 3 T13: -0.0021 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.2824 L22: 0.3098
REMARK 3 L33: 0.2621 L12: -0.0059
REMARK 3 L13: -0.0888 L23: -0.0747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.0060 S13: -0.0152
REMARK 3 S21: 0.0055 S22: 0.0078 S23: 0.0007
REMARK 3 S31: -0.0050 S32: -0.0080 S33: -0.0064
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 7QJT 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_1292118620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-20
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) : 0.9763
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 : 17061
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.777
REMARK 200 RESOLUTION RANGE LOW (A) : 77.285
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1
REMARK 200 DATA REDUNDANCY : 26.20
REMARK 200 R MERGE (I) : 0.63900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.3
REMARK 200 DATA REDUNDANCY IN SHELL : 22.00
REMARK 200 R MERGE FOR SHELL (I) : 3.12700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
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: 5ZOA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M TRIS PH 8.5, 20 % (W/V) PEG 8000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 22.09200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.64850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.64850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.13800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.64850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.64850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.04600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.64850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.64850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.13800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.64850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.64850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 11.04600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 22.09200
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: 870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 593 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 609 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 632 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 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 HE2 HIS A 267 MG MG A 303 0.98
REMARK 500 HE2 HIS A 265 MG MG A 303 1.13
REMARK 500 HH21 ARG A 120 HO1 GOL A 301 1.15
REMARK 500 H2 ALA A 1 MG MG A 303 1.18
REMARK 500 HD1 HIS A 155 H ASN A 157 1.25
REMARK 500 OG SER A 31 HD3 PRO A 32 1.47
REMARK 500 HH11 ARG A 196 O HOH A 407 1.57
REMARK 500 O HOH A 600 O HOH A 629 2.14
REMARK 500 O HOH A 560 O HOH A 626 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 HE2 HIS A 264 MG MG A 303 4455 1.11
REMARK 500 HE2 HIS A 266 MG MG A 303 4455 1.21
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 30 154.12 -33.24
REMARK 500 SER A 31 -75.45 -60.25
REMARK 500 THR A 60 6.69 59.69
REMARK 500 SER A 129 -116.26 68.46
REMARK 500 HIS A 183 -79.98 -130.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 302
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 305 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 173 OE1
REMARK 620 2 GLU A 173 OE2 46.1
REMARK 620 3 ASN A 203 OD1 75.0 120.9
REMARK 620 4 GLU A 252 OE1 100.7 92.8 93.5
REMARK 620 5 HOH A 497 O 72.4 85.9 80.1 171.5
REMARK 620 6 HOH A 526 O 162.1 151.1 87.2 78.1 106.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 185 OE2
REMARK 620 2 GLU A 201 OE1 87.4
REMARK 620 3 GLU A 253 OE2 83.8 95.3
REMARK 620 4 HOH A 414 O 154.9 106.4 74.4
REMARK 620 5 HOH A 444 O 77.7 165.1 83.4 87.5
REMARK 620 6 HOH A 475 O 100.9 90.8 172.4 99.7 91.8
REMARK 620 N 1 2 3 4 5
DBREF 7QJT A 1 268 PDB 7QJT 7QJT 1 268
SEQRES 1 A 268 ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLN ALA
SEQRES 2 A 268 SER LEU GLU ALA SER ARG GLY PRO PHE PRO VAL SER GLU
SEQRES 3 A 268 GLU ARG VAL SER SER PRO VAL SER GLY PHE GLY GLY GLY
SEQRES 4 A 268 THR ILE TYR TYR PRO GLN GLU ASN ASN THR TYR GLY ALA
SEQRES 5 A 268 VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER SER
SEQRES 6 A 268 VAL ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY PHE
SEQRES 7 A 268 VAL VAL ILE THR ILE ASP THR ASN THR THR LEU ASP GLN
SEQRES 8 A 268 PRO ASP SER ARG ALA ASP GLN LEU GLU ALA ALA LEU ASP
SEQRES 9 A 268 HIS MET VAL ASP GLY ALA SER SER THR VAL ARG SER ARG
SEQRES 10 A 268 ILE ASP ARG ASN ARG LEU ALA VAL MET GLY HIS SER MET
SEQRES 11 A 268 GLY GLY GLY GLY THR LEU ARG LEU ALA SER ARG ARG PRO
SEQRES 12 A 268 ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS LEU
SEQRES 13 A 268 ASN LYS SER TRP SER ASN VAL GLN VAL PRO THR LEU ILE
SEQRES 14 A 268 ILE GLY ALA GLU ASN ASP THR VAL ALA PRO VAL ALA LEU
SEQRES 15 A 268 HIS ALA GLU PRO SER TYR THR SER ILE PRO THR SER THR
SEQRES 16 A 268 ARG LYS ALA TYR LEU GLU LEU ASN GLY ALA SER HIS PHE
SEQRES 17 A 268 ALA PRO SER VAL ALA ASN ALA THR ILE GLY MET TYR GLY
SEQRES 18 A 268 VAL ALA TRP LEU LYS ARG PHE VAL ASP GLU ASP THR ARG
SEQRES 19 A 268 TYR THR ARG PHE LEU CYS PRO GLY PRO ARG THR GLY LEU
SEQRES 20 A 268 PHE SER ASP VAL GLU GLU TYR ARG SER THR CYS PRO PHE
SEQRES 21 A 268 LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL A 301 14
HET PG4 A 302 23
HET MG A 303 1
HET MG A 304 1
HET MG A 305 1
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 MG 3(MG 2+)
FORMUL 7 HOH *241(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 THR A 62 SER A 65 5 4
HELIX 3 AA3 VAL A 66 SER A 75 1 10
HELIX 4 AA4 GLN A 91 GLY A 109 1 19
HELIX 5 AA5 SER A 111 SER A 116 1 6
HELIX 6 AA6 SER A 129 ARG A 142 1 14
HELIX 7 AA7 HIS A 183 ILE A 191 1 9
HELIX 8 AA8 PHE A 208 VAL A 212 5 5
HELIX 9 AA9 ASN A 214 ASP A 230 1 17
HELIX 10 AB1 TYR A 235 CYS A 240 1 6
SHEET 1 AA1 6 VAL A 24 ARG A 28 0
SHEET 2 AA1 6 GLY A 38 PRO A 44 -1 O ILE A 41 N GLU A 27
SHEET 3 AA1 6 VAL A 79 ASP A 84 -1 O VAL A 80 N TYR A 42
SHEET 4 AA1 6 TYR A 50 SER A 56 1 N VAL A 53 O ILE A 81
SHEET 5 AA1 6 ILE A 118 HIS A 128 1 O ALA A 124 N ALA A 52
SHEET 6 AA1 6 ALA A 147 LEU A 151 1 O LEU A 151 N GLY A 127
SHEET 1 AA2 3 THR A 167 ALA A 172 0
SHEET 2 AA2 3 LYS A 197 LEU A 202 1 O LEU A 202 N GLY A 171
SHEET 3 AA2 3 VAL A 251 SER A 256 -1 O GLU A 253 N GLU A 201
SSBOND 1 CYS A 240 CYS A 258 1555 1555 2.07
LINK O ALA A 1 MG MG A 303 1555 1555 1.92
LINK OE1 GLU A 173 MG MG A 305 1555 1555 2.63
LINK OE2 GLU A 173 MG MG A 305 1555 1555 2.97
LINK OE2 GLU A 185 MG MG A 304 1555 1555 2.09
LINK OE1 GLU A 201 MG MG A 304 1555 1555 2.01
LINK OD1 ASN A 203 MG MG A 305 1555 1555 1.95
LINK OE1 GLU A 252 MG MG A 305 1555 1555 2.04
LINK OE2 GLU A 253 MG MG A 304 1555 1555 2.12
LINK MG MG A 304 O HOH A 414 1555 1555 2.05
LINK MG MG A 304 O HOH A 444 1555 1555 2.12
LINK MG MG A 304 O HOH A 475 1555 1555 1.90
LINK MG MG A 305 O HOH A 497 1555 1555 2.38
LINK MG MG A 305 O HOH A 526 1555 1555 2.54
CISPEP 1 CYS A 240 PRO A 241 0 -0.30
CISPEP 2 CYS A 258 PRO A 259 0 4.78
CRYST1 109.297 109.297 44.184 90.00 90.00 90.00 P 43 21 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 0.009149 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022633 0.00000
TER 4018 HIS A 267
MASTER 386 0 5 10 9 0 0 6 2304 1 57 21
END |