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HEADER HYDROLASE 05-NOV-21 7VVE
TITLE COMPLEX STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT IN COMPLEX
TITLE 2 WITH MONO(2-HYDROXYETHYL) TEREPHTHALIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LC-CUTINASE,LCC,PET-DIGESTING ENZYME,POLY(ETHYLENE
COMPND 5 TEREPHTHALATE) HYDROLASE,PET HYDROLASE,PETASE;
COMPND 6 EC: 3.1.1.74,3.1.1.101;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNKNOWN PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS PLASTIC DEGRADATION, HYDROLASE, ACTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NIU,W.ZENG,J.W.HUANG,C.C.CHEN,W.D.LIU,R.T.GUO
REVDAT 1 09-MAR-22 7VVE 0
JRNL AUTH W.ZENG,X.LI,Y.YANG,J.MIN,J.-W.HUANG,W.LIU,D.NIU,X.YANG,
JRNL AUTH 2 X.HAN,L.ZHANG,L.DAI,C.-C.CHEN,R.-T.GUO
JRNL TITL SUBSTRATE-BINDING MODE OF A THERMOPHILIC PET HYDROLASE AND
JRNL TITL 2 ENGINEERING THE ENZYME TO ENHANCE THE HYDROLYTIC EFFICACY.
JRNL REF ACS CATALYSIS V. 12 3033 2022
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.1C05800
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 35218
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1835
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2272
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.1520
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3908
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.776
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4101 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3665 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5603 ; 1.720 ; 1.655
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8477 ; 1.482 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 7.112 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 203 ;27.473 ;20.640
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 576 ;12.295 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;21.153 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 543 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4694 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 901 ; 0.001 ; 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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7VVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1300025351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : LIQUID ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER METALJET
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.34138
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37584
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
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 (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.07300
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
REMARK 200 STARTING MODEL: 7DS7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE 0.1 M SODIUM
REMARK 280 CACODYLATE PH 6.5 16-20% W/V PEG 8000, VAPOR DIFFUSION, SITTING
REMARK 280 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 21.13850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.87300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.87300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.13850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.54500
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
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: 80 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 80 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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 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 34
REMARK 465 MET A 35
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 THR A 96 -12.87 78.77
REMARK 500 ALA A 165 -118.37 65.03
REMARK 500 THR A 188 57.72 36.32
REMARK 500 HIS A 218 -85.51 -126.42
REMARK 500 THR B 96 -3.62 69.83
REMARK 500 ALA B 165 -118.14 67.29
REMARK 500 THR B 188 58.23 33.34
REMARK 500 HIS B 218 -87.15 -125.23
REMARK 500 ASN B 248 126.04 -39.37
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 821 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 822 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B 848 DISTANCE = 6.01 ANGSTROMS
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 PEG A 405
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 193 OD1
REMARK 620 2 ASP A 193 OD2 50.8
REMARK 620 3 THR A 195 O 85.6 97.9
REMARK 620 4 THR A 195 OG1 73.1 123.9 75.5
REMARK 620 5 HOH A 593 O 124.7 80.3 76.2 144.8
REMARK 620 6 HOH A 648 O 86.6 107.1 139.9 64.6 137.8
REMARK 620 7 HOH A 718 O 108.5 74.6 151.5 131.7 75.5 67.3
REMARK 620 8 HOH B 523 O 150.0 158.7 90.3 77.1 82.6 77.6 88.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 193 OD1
REMARK 620 2 ASP B 193 OD2 51.7
REMARK 620 3 THR B 195 O 81.6 95.8
REMARK 620 4 THR B 195 OG1 76.1 127.8 74.4
REMARK 620 5 HOH B 542 O 123.7 79.1 77.6 142.5
REMARK 620 6 HOH B 702 O 81.9 97.0 145.8 72.7 136.0
REMARK 620 7 HOH B 720 O 156.2 150.9 97.7 80.8 78.7 86.0
REMARK 620 8 HOH B 721 O 115.2 72.0 138.8 144.0 61.7 75.3 80.9
REMARK 620 N 1 2 3 4 5 6 7
DBREF 7VVE A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 7VVE B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 7VVE GLY A 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVE MET A 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVE GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7VVE ALA A 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 7VVE CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7VVE ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7VVE CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 7VVE GLY B 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVE MET B 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVE GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7VVE ALA B 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 7VVE CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7VVE ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7VVE CYS B 283 UNP G9BY57 SER 283 CONFLICT
SEQRES 1 A 260 GLY MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR
SEQRES 2 A 260 ARG SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA
SEQRES 3 A 260 THR TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY
SEQRES 4 A 260 GLY GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR
SEQRES 5 A 260 PHE GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP
SEQRES 6 A 260 ALA SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER
SEQRES 7 A 260 HIS GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG
SEQRES 8 A 260 PHE ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA
SEQRES 9 A 260 ALA LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL
SEQRES 10 A 260 ARG ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY
SEQRES 11 A 260 HIS ALA MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU
SEQRES 12 A 260 GLN ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO
SEQRES 13 A 260 TRP HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL
SEQRES 14 A 260 LEU ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL
SEQRES 15 A 260 SER GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER
SEQRES 16 A 260 THR THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER
SEQRES 17 A 260 HIS ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL
SEQRES 18 A 260 TYR THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP
SEQRES 19 A 260 THR ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO
SEQRES 20 A 260 ALA LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
SEQRES 1 B 260 GLY MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR
SEQRES 2 B 260 ARG SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA
SEQRES 3 B 260 THR TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY
SEQRES 4 B 260 GLY GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR
SEQRES 5 B 260 PHE GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP
SEQRES 6 B 260 ALA SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER
SEQRES 7 B 260 HIS GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG
SEQRES 8 B 260 PHE ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA
SEQRES 9 B 260 ALA LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL
SEQRES 10 B 260 ARG ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY
SEQRES 11 B 260 HIS ALA MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU
SEQRES 12 B 260 GLN ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO
SEQRES 13 B 260 TRP HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL
SEQRES 14 B 260 LEU ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL
SEQRES 15 B 260 SER GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER
SEQRES 16 B 260 THR THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER
SEQRES 17 B 260 HIS ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL
SEQRES 18 B 260 TYR THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP
SEQRES 19 B 260 THR ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO
SEQRES 20 B 260 ALA LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
HET CA A 401 1
HET C9C A 402 15
HET PEG A 403 7
HET PEG A 404 7
HET PEG A 405 5
HET PG0 A 406 8
HET CA B 401 1
HET C9C B 402 15
HETNAM CA CALCIUM ION
HETNAM C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETSYN C9C MONOHYDROXYETHYL TEREPHTHALATE
HETSYN PG0 PEG 6000
FORMUL 3 CA 2(CA 2+)
FORMUL 4 C9C 2(C10 H10 O5)
FORMUL 5 PEG 3(C4 H10 O3)
FORMUL 8 PG0 C5 H12 O3
FORMUL 11 HOH *670(H2 O)
HELIX 1 AA1 ARG A 47 ALA A 52 5 6
HELIX 2 AA2 SER A 64 VAL A 68 5 5
HELIX 3 AA3 ASP A 98 SER A 101 5 4
HELIX 4 AA4 LEU A 102 HIS A 112 1 11
HELIX 5 AA5 GLY A 127 SER A 145 1 19
HELIX 6 AA6 PRO A 147 ALA A 152 1 6
HELIX 7 AA7 ALA A 165 ASN A 178 1 14
HELIX 8 AA8 HIS A 218 LEU A 226 1 9
HELIX 9 AA9 ILE A 243 SER A 247 5 5
HELIX 10 AB1 ASN A 249 ASP A 265 1 17
HELIX 11 AB2 ASP A 267 ARG A 269 5 3
HELIX 12 AB3 TYR A 270 CYS A 275 1 6
HELIX 13 AB4 SER B 48 ALA B 52 5 5
HELIX 14 AB5 ASP B 98 SER B 101 5 4
HELIX 15 AB6 LEU B 102 HIS B 112 1 11
HELIX 16 AB7 GLY B 127 SER B 145 1 19
HELIX 17 AB8 PRO B 147 ALA B 152 1 6
HELIX 18 AB9 ALA B 165 ASN B 178 1 14
HELIX 19 AC1 HIS B 218 LEU B 226 1 9
HELIX 20 AC2 ILE B 243 SER B 247 5 5
HELIX 21 AC3 ASN B 249 ASP B 265 1 17
HELIX 22 AC4 ASP B 267 ARG B 269 5 3
HELIX 23 AC5 TYR B 270 CYS B 275 1 6
SHEET 1 AA1 6 SER A 57 VAL A 63 0
SHEET 2 AA1 6 GLY A 74 THR A 80 -1 O ILE A 76 N TYR A 61
SHEET 3 AA1 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 AA1 6 PHE A 86 SER A 92 1 N MET A 91 O LEU A 117
SHEET 5 AA1 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 AA1 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 AA2 3 VAL A 202 ALA A 207 0
SHEET 2 AA2 3 LYS A 232 LEU A 237 1 O VAL A 235 N GLY A 206
SHEET 3 AA2 3 LEU A 282 THR A 287 -1 O ARG A 286 N TYR A 234
SHEET 1 AA3 6 SER B 57 VAL B 63 0
SHEET 2 AA3 6 GLY B 74 THR B 80 -1 O GLY B 74 N VAL B 63
SHEET 3 AA3 6 VAL B 115 ILE B 119 -1 O VAL B 116 N TYR B 77
SHEET 4 AA3 6 PHE B 86 SER B 92 1 N ILE B 89 O LEU B 117
SHEET 5 AA3 6 LEU B 154 HIS B 164 1 O ASP B 155 N PHE B 86
SHEET 6 AA3 6 ALA B 184 LEU B 187 1 O LEU B 187 N GLY B 163
SHEET 1 AA4 3 VAL B 202 ALA B 207 0
SHEET 2 AA4 3 LYS B 232 LEU B 237 1 O VAL B 235 N GLY B 206
SHEET 3 AA4 3 LEU B 282 THR B 287 -1 O CYS B 283 N GLU B 236
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.03
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.03
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.05
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.04
LINK OD1 ASP A 193 CA CA A 401 1555 1555 2.55
LINK OD2 ASP A 193 CA CA A 401 1555 1555 2.60
LINK O THR A 195 CA CA A 401 1555 1555 2.43
LINK OG1 THR A 195 CA CA A 401 1555 1555 2.66
LINK CA CA A 401 O HOH A 593 1555 1555 2.65
LINK CA CA A 401 O HOH A 648 1555 1555 2.64
LINK CA CA A 401 O HOH A 718 1555 1555 2.57
LINK CA CA A 401 O HOH B 523 1555 4455 2.59
LINK OD1 ASP B 193 CA CA B 401 1555 1555 2.47
LINK OD2 ASP B 193 CA CA B 401 1555 1555 2.66
LINK O THR B 195 CA CA B 401 1555 1555 2.42
LINK OG1 THR B 195 CA CA B 401 1555 1555 2.43
LINK CA CA B 401 O HOH B 542 1555 1555 2.56
LINK CA CA B 401 O HOH B 702 1555 1555 2.62
LINK CA CA B 401 O HOH B 720 1555 1555 2.33
LINK CA CA B 401 O HOH B 721 1555 1555 2.60
CRYST1 42.277 85.090 147.746 90.00 90.00 90.00 P 21 21 21 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 0.023654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006768 0.00000
TER 1958 GLN A 293
TER 3927 GLN B 293
MASTER 339 0 8 23 18 0 0 6 4637 2 84 40
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