| content |
HEADER HYDROLASE 11-APR-17 5XG0
TITLE CRYSTAL STRUCTURE OF A NOVEL PET HYDROLASE FROM IDEONELLA SAKAIENSIS
TITLE 2 201-F6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 30-290;
COMPND 5 SYNONYM: PETASE;
COMPND 6 EC: 3.1.1.101;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS METAL-BINDING, SUBSTRATE BINDING, ACIDOCALCISOMAL PYROPHOSPHATASE,
KEYWDS 2 INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
REVDAT 1 20-DEC-17 5XG0 0
JRNL AUTH X.HAN,W.D.LIU,J.W.HUANG,J.MA,Y.Y.ZHENG,T.P.KO,L.XU,
JRNL AUTH 2 Y.S.CHANG,C.C.CHEN,R.T.GUO
JRNL TITL STRUCTURAL INSIGHT INTO CATALYTIC MECHANISM OF PET HYDROLASE
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-02255-Z
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 88161
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4552
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.1330
REMARK 3 BIN FREE R VALUE SET COUNT : 337
REMARK 3 BIN FREE R VALUE : 0.1870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.39000
REMARK 3 B33 (A**2) : -0.58000
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): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.085
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5954 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5237 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8113 ; 1.507 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12185 ; 0.834 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 790 ; 6.846 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 231 ;34.816 ;23.506
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 867 ;11.270 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;18.202 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 889 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6835 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1228 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5XG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92787
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 32.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.07600
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: PHASER, PHASER
REMARK 200 STARTING MODEL: 4WFI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 6000, GLYCEROL,
REMARK 280 MES, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 31.74000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.52050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.60800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.52050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.74000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.60800
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 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 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 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 GLY A -6
REMARK 465 ALA A -5
REMARK 465 GLY A -4
REMARK 465 ALA A -3
REMARK 465 GLY A -2
REMARK 465 GLY B -6
REMARK 465 ALA B -5
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 GLY B -2
REMARK 465 ALA B -1
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 B 512 O HOH C 353 2554 1.79
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 SER B 96 CB SER B 96 OG -0.081
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 103 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = 3.4 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 44 40.44 -140.61
REMARK 500 THR A 59 -7.66 74.97
REMARK 500 SER A 131 -123.04 66.40
REMARK 500 SER A 185 -84.15 -136.60
REMARK 500 ASN B 44 40.03 -140.46
REMARK 500 THR B 59 -9.99 72.91
REMARK 500 SER B 131 -121.19 64.08
REMARK 500 SER B 185 -82.78 -128.42
REMARK 500 ASN C 44 47.87 -142.64
REMARK 500 THR C 59 -8.60 71.51
REMARK 500 SER C 131 -117.98 66.13
REMARK 500 SER C 185 -84.28 -126.13
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 662 DISTANCE = 6.27 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XFX RELATED DB: PDB
REMARK 900 RELATED ID: 5XFZ RELATED DB: PDB
REMARK 900 RELATED ID: 5XFY RELATED DB: PDB
DBREF1 5XG0 A 1 261 UNP PETH_IDESA
DBREF2 5XG0 A A0A0K8P6T7 30 290
DBREF1 5XG0 B 1 261 UNP PETH_IDESA
DBREF2 5XG0 B A0A0K8P6T7 30 290
DBREF1 5XG0 C 1 261 UNP PETH_IDESA
DBREF2 5XG0 C A0A0K8P6T7 30 290
SEQADV 5XG0 GLY A -6 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA A -5 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY A -4 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA A -3 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY A -2 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA A -1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 MET A 0 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY B -6 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA B -5 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY B -4 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA B -3 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY B -2 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA B -1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 MET B 0 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY C -6 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA C -5 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY C -4 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA C -3 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 GLY C -2 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 ALA C -1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XG0 MET C 0 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 268 GLY ALA GLY ALA GLY ALA MET ASN PRO TYR ALA ARG GLY
SEQRES 2 A 268 PRO ASN PRO THR ALA ALA SER LEU GLU ALA SER ALA GLY
SEQRES 3 A 268 PRO PHE THR VAL ARG SER PHE THR VAL SER ARG PRO SER
SEQRES 4 A 268 GLY TYR GLY ALA GLY THR VAL TYR TYR PRO THR ASN ALA
SEQRES 5 A 268 GLY GLY THR VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR
SEQRES 6 A 268 THR ALA ARG GLN SER SER ILE LYS TRP TRP GLY PRO ARG
SEQRES 7 A 268 LEU ALA SER HIS GLY PHE VAL VAL ILE THR ILE ASP THR
SEQRES 8 A 268 ASN SER THR LEU ASP GLN PRO SER SER ARG SER SER GLN
SEQRES 9 A 268 GLN MET ALA ALA LEU ARG GLN VAL ALA SER LEU ASN GLY
SEQRES 10 A 268 THR SER SER SER PRO ILE TYR GLY LYS VAL ASP THR ALA
SEQRES 11 A 268 ARG MET GLY VAL MET GLY TRP SER MET GLY GLY GLY GLY
SEQRES 12 A 268 SER LEU ILE SER ALA ALA ASN ASN PRO SER LEU LYS ALA
SEQRES 13 A 268 ALA ALA PRO GLN ALA PRO TRP ASP SER SER THR ASN PHE
SEQRES 14 A 268 SER SER VAL THR VAL PRO THR LEU ILE PHE ALA CYS GLU
SEQRES 15 A 268 ASN ASP SER ILE ALA PRO VAL ASN SER SER ALA LEU PRO
SEQRES 16 A 268 ILE TYR ASP SER MET SER ARG ASN ALA LYS GLN PHE LEU
SEQRES 17 A 268 GLU ILE ASN GLY GLY SER HIS SER CYS ALA ASN SER GLY
SEQRES 18 A 268 ASN SER ASN GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA
SEQRES 19 A 268 TRP MET LYS ARG PHE MET ASP ASN ASP THR ARG TYR SER
SEQRES 20 A 268 THR PHE ALA CYS GLU ASN PRO ASN SER THR ARG VAL SER
SEQRES 21 A 268 ASP PHE ARG THR ALA ASN CYS SER
SEQRES 1 B 268 GLY ALA GLY ALA GLY ALA MET ASN PRO TYR ALA ARG GLY
SEQRES 2 B 268 PRO ASN PRO THR ALA ALA SER LEU GLU ALA SER ALA GLY
SEQRES 3 B 268 PRO PHE THR VAL ARG SER PHE THR VAL SER ARG PRO SER
SEQRES 4 B 268 GLY TYR GLY ALA GLY THR VAL TYR TYR PRO THR ASN ALA
SEQRES 5 B 268 GLY GLY THR VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR
SEQRES 6 B 268 THR ALA ARG GLN SER SER ILE LYS TRP TRP GLY PRO ARG
SEQRES 7 B 268 LEU ALA SER HIS GLY PHE VAL VAL ILE THR ILE ASP THR
SEQRES 8 B 268 ASN SER THR LEU ASP GLN PRO SER SER ARG SER SER GLN
SEQRES 9 B 268 GLN MET ALA ALA LEU ARG GLN VAL ALA SER LEU ASN GLY
SEQRES 10 B 268 THR SER SER SER PRO ILE TYR GLY LYS VAL ASP THR ALA
SEQRES 11 B 268 ARG MET GLY VAL MET GLY TRP SER MET GLY GLY GLY GLY
SEQRES 12 B 268 SER LEU ILE SER ALA ALA ASN ASN PRO SER LEU LYS ALA
SEQRES 13 B 268 ALA ALA PRO GLN ALA PRO TRP ASP SER SER THR ASN PHE
SEQRES 14 B 268 SER SER VAL THR VAL PRO THR LEU ILE PHE ALA CYS GLU
SEQRES 15 B 268 ASN ASP SER ILE ALA PRO VAL ASN SER SER ALA LEU PRO
SEQRES 16 B 268 ILE TYR ASP SER MET SER ARG ASN ALA LYS GLN PHE LEU
SEQRES 17 B 268 GLU ILE ASN GLY GLY SER HIS SER CYS ALA ASN SER GLY
SEQRES 18 B 268 ASN SER ASN GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA
SEQRES 19 B 268 TRP MET LYS ARG PHE MET ASP ASN ASP THR ARG TYR SER
SEQRES 20 B 268 THR PHE ALA CYS GLU ASN PRO ASN SER THR ARG VAL SER
SEQRES 21 B 268 ASP PHE ARG THR ALA ASN CYS SER
SEQRES 1 C 268 GLY ALA GLY ALA GLY ALA MET ASN PRO TYR ALA ARG GLY
SEQRES 2 C 268 PRO ASN PRO THR ALA ALA SER LEU GLU ALA SER ALA GLY
SEQRES 3 C 268 PRO PHE THR VAL ARG SER PHE THR VAL SER ARG PRO SER
SEQRES 4 C 268 GLY TYR GLY ALA GLY THR VAL TYR TYR PRO THR ASN ALA
SEQRES 5 C 268 GLY GLY THR VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR
SEQRES 6 C 268 THR ALA ARG GLN SER SER ILE LYS TRP TRP GLY PRO ARG
SEQRES 7 C 268 LEU ALA SER HIS GLY PHE VAL VAL ILE THR ILE ASP THR
SEQRES 8 C 268 ASN SER THR LEU ASP GLN PRO SER SER ARG SER SER GLN
SEQRES 9 C 268 GLN MET ALA ALA LEU ARG GLN VAL ALA SER LEU ASN GLY
SEQRES 10 C 268 THR SER SER SER PRO ILE TYR GLY LYS VAL ASP THR ALA
SEQRES 11 C 268 ARG MET GLY VAL MET GLY TRP SER MET GLY GLY GLY GLY
SEQRES 12 C 268 SER LEU ILE SER ALA ALA ASN ASN PRO SER LEU LYS ALA
SEQRES 13 C 268 ALA ALA PRO GLN ALA PRO TRP ASP SER SER THR ASN PHE
SEQRES 14 C 268 SER SER VAL THR VAL PRO THR LEU ILE PHE ALA CYS GLU
SEQRES 15 C 268 ASN ASP SER ILE ALA PRO VAL ASN SER SER ALA LEU PRO
SEQRES 16 C 268 ILE TYR ASP SER MET SER ARG ASN ALA LYS GLN PHE LEU
SEQRES 17 C 268 GLU ILE ASN GLY GLY SER HIS SER CYS ALA ASN SER GLY
SEQRES 18 C 268 ASN SER ASN GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA
SEQRES 19 C 268 TRP MET LYS ARG PHE MET ASP ASN ASP THR ARG TYR SER
SEQRES 20 C 268 THR PHE ALA CYS GLU ASN PRO ASN SER THR ARG VAL SER
SEQRES 21 C 268 ASP PHE ARG THR ALA ASN CYS SER
FORMUL 4 HOH *1124(H2 O)
HELIX 1 AA1 THR A 10 ALA A 16 1 7
HELIX 2 AA2 ARG A 61 LYS A 66 5 6
HELIX 3 AA3 TRP A 67 PHE A 77 1 11
HELIX 4 AA4 GLN A 90 GLY A 110 1 21
HELIX 5 AA5 SER A 131 ASN A 144 1 14
HELIX 6 AA6 SER A 185 SER A 192 1 8
HELIX 7 AA7 ASN A 217 ASP A 234 1 18
HELIX 8 AA8 ASP A 236 ARG A 238 5 3
HELIX 9 AA9 TYR A 239 GLU A 245 1 7
HELIX 10 AB1 THR B 10 ALA B 16 1 7
HELIX 11 AB2 ARG B 61 LYS B 66 1 6
HELIX 12 AB3 TRP B 67 PHE B 77 1 11
HELIX 13 AB4 GLN B 90 GLY B 110 1 21
HELIX 14 AB5 SER B 131 ASN B 144 1 14
HELIX 15 AB6 SER B 185 MET B 193 1 9
HELIX 16 AB7 ASN B 217 ASP B 234 1 18
HELIX 17 AB8 ASP B 236 ARG B 238 5 3
HELIX 18 AB9 TYR B 239 GLU B 245 1 7
HELIX 19 AC1 THR C 10 ALA C 16 1 7
HELIX 20 AC2 ARG C 61 LYS C 66 5 6
HELIX 21 AC3 TRP C 67 PHE C 77 1 11
HELIX 22 AC4 GLN C 90 GLY C 110 1 21
HELIX 23 AC5 SER C 131 ASN C 144 1 14
HELIX 24 AC6 SER C 185 MET C 193 1 9
HELIX 25 AC7 ASN C 217 ASP C 234 1 18
HELIX 26 AC8 ASP C 236 ARG C 238 5 3
HELIX 27 AC9 TYR C 239 GLU C 245 1 7
SHEET 1 AA1 6 VAL A 23 THR A 27 0
SHEET 2 AA1 6 ALA A 36 PRO A 42 -1 O VAL A 39 N PHE A 26
SHEET 3 AA1 6 VAL A 78 ASP A 83 -1 O VAL A 79 N TYR A 40
SHEET 4 AA1 6 VAL A 49 VAL A 55 1 N ILE A 52 O ILE A 80
SHEET 5 AA1 6 VAL A 120 GLY A 129 1 O ASP A 121 N VAL A 49
SHEET 6 AA1 6 ALA A 149 ALA A 150 1 O ALA A 149 N VAL A 127
SHEET 1 AA2 3 THR A 169 CYS A 174 0
SHEET 2 AA2 3 LYS A 198 ILE A 203 1 O GLN A 199 N ILE A 171
SHEET 3 AA2 3 VAL A 252 ALA A 258 -1 O ASP A 254 N GLU A 202
SHEET 1 AA3 6 VAL B 23 THR B 27 0
SHEET 2 AA3 6 ALA B 36 PRO B 42 -1 O VAL B 39 N PHE B 26
SHEET 3 AA3 6 VAL B 78 ASP B 83 -1 O VAL B 79 N TYR B 40
SHEET 4 AA3 6 VAL B 49 VAL B 55 1 N ILE B 52 O ILE B 80
SHEET 5 AA3 6 VAL B 120 GLY B 129 1 O ASP B 121 N VAL B 49
SHEET 6 AA3 6 ALA B 149 ALA B 150 1 O ALA B 149 N VAL B 127
SHEET 1 AA4 3 THR B 169 CYS B 174 0
SHEET 2 AA4 3 LYS B 198 ILE B 203 1 O GLN B 199 N ILE B 171
SHEET 3 AA4 3 VAL B 252 ALA B 258 -1 O ASP B 254 N GLU B 202
SHEET 1 AA5 6 VAL C 23 THR C 27 0
SHEET 2 AA5 6 ALA C 36 PRO C 42 -1 O VAL C 39 N PHE C 26
SHEET 3 AA5 6 VAL C 78 ASP C 83 -1 O VAL C 79 N TYR C 40
SHEET 4 AA5 6 VAL C 49 VAL C 55 1 N ILE C 52 O ILE C 80
SHEET 5 AA5 6 VAL C 120 GLY C 129 1 O ASP C 121 N VAL C 49
SHEET 6 AA5 6 ALA C 149 ALA C 150 1 O ALA C 149 N VAL C 127
SHEET 1 AA6 3 THR C 169 CYS C 174 0
SHEET 2 AA6 3 LYS C 198 ILE C 203 1 O LEU C 201 N ALA C 173
SHEET 3 AA6 3 VAL C 252 ALA C 258 -1 O ARG C 256 N PHE C 200
SSBOND 1 CYS A 174 CYS A 210 1555 1555 2.04
SSBOND 2 CYS A 244 CYS A 260 1555 1555 2.05
SSBOND 3 CYS B 174 CYS B 210 1555 1555 2.05
SSBOND 4 CYS B 244 CYS B 260 1555 1555 2.06
SSBOND 5 CYS C 174 CYS C 210 1555 1555 2.06
SSBOND 6 CYS C 244 CYS C 260 1555 1555 2.05
CRYST1 63.480 69.216 153.041 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 0.015753 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014448 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006534 0.00000
TER 1933 SER A 261
TER 3861 SER B 261
TER 5816 SER C 261
MASTER 370 0 0 27 27 0 0 6 6937 3 12 63
END |