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HEADER HYDROLASE 05-NOV-21 7VVC
TITLE CRYSTAL STRUCTURE OF INACTIVE MUTANT OF LEAF-BRANCH COMPOST CUTINASE
TITLE 2 VARIANT
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 7VVC 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. 1.82 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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 44723
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2390
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3125
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 717
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.02000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.718
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4140 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3691 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5679 ; 1.637 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8545 ; 1.507 ; 1.564
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 6.983 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;28.701 ;20.583
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 583 ;11.472 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;17.511 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 555 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4813 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 917 ; 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 7VVC 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_1300025352.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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 : 45015
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
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 : 4.800
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
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 (%): 45.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE,SODIUM ACETATE
REMARK 280 TRIHYDRATE,POLYETHYLENE GLYCOL 4000, GLYCEROL, PH 4.6, VAPOR
REMARK 280 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 20.71450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.69500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.35100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.69500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.71450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.35100
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: 9680 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: 10080 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 24
REMARK 465 ALA A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 27
REMARK 465 GLY A 28
REMARK 465 ALA A 29
REMARK 465 GLY A 30
REMARK 465 ALA A 31
REMARK 465 GLY A 32
REMARK 465 ALA A 33
REMARK 465 GLY A 34
REMARK 465 MET A 35
REMARK 465 GLY B 24
REMARK 465 ALA B 25
REMARK 465 GLY B 26
REMARK 465 ALA B 27
REMARK 465 GLY B 28
REMARK 465 ALA B 29
REMARK 465 GLY B 30
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 ALA A 165 -119.38 61.12
REMARK 500 THR A 188 56.40 37.38
REMARK 500 HIS A 218 -85.40 -120.06
REMARK 500 ALA B 165 -118.28 63.47
REMARK 500 THR B 188 61.08 33.10
REMARK 500 HIS B 218 -89.85 -130.52
REMARK 500 ASN B 239 16.69 58.68
REMARK 500 ASN B 289 60.89 37.77
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 872 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 873 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH A 874 DISTANCE = 7.58 ANGSTROMS
REMARK 525 HOH B 842 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 843 DISTANCE = 6.12 ANGSTROMS
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 52.7
REMARK 620 3 THR A 195 O 83.2 88.5
REMARK 620 4 THR A 195 OG1 73.8 124.8 70.9
REMARK 620 5 HOH A 547 O 130.9 81.7 78.0 137.3
REMARK 620 6 HOH A 744 O 104.4 76.9 153.3 135.8 77.9
REMARK 620 7 HOH B 515 O 150.6 155.2 87.9 76.8 73.5 96.1
REMARK 620 8 HOH B 654 O 96.1 122.6 140.1 70.7 126.7 65.6 73.4
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 51.6
REMARK 620 3 THR B 195 O 80.1 97.7
REMARK 620 4 THR B 195 OG1 74.0 125.6 70.4
REMARK 620 5 HOH B 570 O 128.2 84.9 79.6 138.9
REMARK 620 6 HOH B 711 O 146.3 161.7 91.6 72.4 81.3
REMARK 620 7 HOH B 720 O 83.3 95.6 145.1 75.7 133.8 85.5
REMARK 620 8 HOH B 741 O 124.3 83.2 144.6 136.5 65.1 80.1 69.0
REMARK 620 N 1 2 3 4 5 6 7
DBREF 7VVC A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 7VVC B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 7VVC GLY A 24 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA A 25 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 26 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA A 27 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 28 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA A 29 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 30 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA A 31 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 32 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA A 33 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC MET A 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7VVC ALA A 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 7VVC CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7VVC ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7VVC CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 7VVC GLY B 24 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA B 25 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 26 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA B 27 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 28 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA B 29 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 30 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA B 31 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 32 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC ALA B 33 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC MET B 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7VVC GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7VVC ALA B 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 7VVC CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7VVC ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7VVC CYS B 283 UNP G9BY57 SER 283 CONFLICT
SEQRES 1 A 270 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA GLY MET SER
SEQRES 2 A 270 ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG SER ALA
SEQRES 3 A 270 LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR TYR THR
SEQRES 4 A 270 VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY GLY VAL
SEQRES 5 A 270 ILE TYR TYR PRO THR GLY THR SER LEU THR PHE GLY GLY
SEQRES 6 A 270 ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA SER SER
SEQRES 7 A 270 LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS GLY PHE
SEQRES 8 A 270 VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE ASP GLY
SEQRES 9 A 270 PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA LEU ASN
SEQRES 10 A 270 TYR LEU ARG THR SER SER PRO SER ALA VAL ARG ALA ARG
SEQRES 11 A 270 LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS ALA MET
SEQRES 12 A 270 GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN ASN PRO
SEQRES 13 A 270 SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP HIS THR
SEQRES 14 A 270 ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU ILE VAL
SEQRES 15 A 270 GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER GLN HIS
SEQRES 16 A 270 ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR THR PRO
SEQRES 17 A 270 LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS ILE ALA
SEQRES 18 A 270 PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR THR ILE
SEQRES 19 A 270 SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR ARG TYR
SEQRES 20 A 270 ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA LEU CYS
SEQRES 21 A 270 ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
SEQRES 1 B 270 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA GLY MET SER
SEQRES 2 B 270 ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG SER ALA
SEQRES 3 B 270 LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR TYR THR
SEQRES 4 B 270 VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY GLY VAL
SEQRES 5 B 270 ILE TYR TYR PRO THR GLY THR SER LEU THR PHE GLY GLY
SEQRES 6 B 270 ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA SER SER
SEQRES 7 B 270 LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS GLY PHE
SEQRES 8 B 270 VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE ASP GLY
SEQRES 9 B 270 PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA LEU ASN
SEQRES 10 B 270 TYR LEU ARG THR SER SER PRO SER ALA VAL ARG ALA ARG
SEQRES 11 B 270 LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS ALA MET
SEQRES 12 B 270 GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN ASN PRO
SEQRES 13 B 270 SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP HIS THR
SEQRES 14 B 270 ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU ILE VAL
SEQRES 15 B 270 GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER GLN HIS
SEQRES 16 B 270 ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR THR PRO
SEQRES 17 B 270 LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS ILE ALA
SEQRES 18 B 270 PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR THR ILE
SEQRES 19 B 270 SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR ARG TYR
SEQRES 20 B 270 ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA LEU CYS
SEQRES 21 B 270 ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
HET CA A 401 1
HET ACY A 402 4
HET GOL A 403 6
HET CA B 401 1
HET ACY B 402 4
HET ACT B 403 4
HET GOL B 404 6
HETNAM CA CALCIUM ION
HETNAM ACY ACETIC ACID
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 ACY 2(C2 H4 O2)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 8 ACT C2 H3 O2 1-
FORMUL 10 HOH *717(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 LEU A 274 5 8
HELIX 12 AB3 ARG B 47 ALA B 52 5 6
HELIX 13 AB4 SER B 64 VAL B 68 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 LEU B 274 5 8
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 MET B 91 O ILE B 119
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 ARG B 286 N TYR B 234
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.08
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.06
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.02
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.03
LINK OD1 ASP A 193 CA CA A 401 1555 1555 2.46
LINK OD2 ASP A 193 CA CA A 401 1555 1555 2.59
LINK O THR A 195 CA CA A 401 1555 1555 2.47
LINK OG1 THR A 195 CA CA A 401 1555 1555 2.56
LINK CA CA A 401 O HOH A 547 1555 1555 2.65
LINK CA CA A 401 O HOH A 744 1555 1555 2.46
LINK CA CA A 401 O HOH B 515 1555 4455 2.63
LINK CA CA A 401 O HOH B 654 1555 4455 2.45
LINK OD1 ASP B 193 CA CA B 401 1555 1555 2.49
LINK OD2 ASP B 193 CA CA B 401 1555 1555 2.54
LINK O THR B 195 CA CA B 401 1555 1555 2.49
LINK OG1 THR B 195 CA CA B 401 1555 1555 2.55
LINK CA CA B 401 O HOH B 570 1555 1555 2.62
LINK CA CA B 401 O HOH B 711 1555 1555 2.57
LINK CA CA B 401 O HOH B 720 1555 1555 2.52
LINK CA CA B 401 O HOH B 741 1555 1555 2.45
CRYST1 41.429 84.702 147.390 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 0.024138 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011806 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006785 0.00000
TER 1992 GLN A 293
TER 3989 GLN B 293
MASTER 350 0 7 22 18 0 0 6 4665 2 50 42
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