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HEADER HYDROLASE 26-NOV-21 7W45
TITLE COMPLEX STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT LCC
TITLE 2 ICCG_KIP
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;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, MUTANT, CATALYSIS, HYDROLASE
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 7W45 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. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 35644
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1919
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) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2395
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3914
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.01000
REMARK 3 B22 (A**2) : -0.84000
REMARK 3 B33 (A**2) : -0.17000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.499
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4071 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3656 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5584 ; 1.585 ; 1.648
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8473 ; 1.398 ; 1.565
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 530 ; 6.952 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;29.207 ;20.388
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 591 ;12.855 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;18.791 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 549 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4675 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 902 ; 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 7W45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1300025941.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-21
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 : 37746
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 35.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
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 (%): 44.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 % PEG 8000, 0.2 M CALCIUM ACETATE
REMARK 280 HYDRATE, 0.1 M SODIUM CACODYLATE TRIHYDATE, PH 6.5, 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 20.18500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.75600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.38500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.75600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.18500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.38500
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: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 465 ALA B 31
REMARK 465 GLY B 32
REMARK 465 ALA B 33
REMARK 465 GLY B 34
REMARK 465 MET B 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 SER A 145 19.85 -147.09
REMARK 500 SER A 165 -116.51 61.93
REMARK 500 THR A 188 59.20 37.02
REMARK 500 HIS A 218 -86.27 -123.11
REMARK 500 THR B 96 -2.23 69.42
REMARK 500 SER B 165 -119.55 57.13
REMARK 500 THR B 188 55.39 33.91
REMARK 500 HIS B 218 -86.16 -125.20
REMARK 500 ASN B 239 19.26 55.85
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 662 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 7.85 ANGSTROMS
REMARK 525 HOH B 637 DISTANCE = 5.99 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 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 65 O
REMARK 620 2 VAL A 68 O 73.9
REMARK 620 3 PHE A 71 O 114.4 92.9
REMARK 620 4 HOH A 550 O 164.8 95.5 76.3
REMARK 620 5 HOH A 553 O 109.8 176.2 86.4 80.7
REMARK 620 6 HOH A 598 O 88.4 78.6 152.6 78.7 100.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 193 OD1
REMARK 620 2 ASP A 193 OD2 51.8
REMARK 620 3 THR A 195 O 84.1 92.6
REMARK 620 4 THR A 195 OG1 71.8 122.6 70.2
REMARK 620 5 HOH A 482 O 93.6 122.0 133.4 65.1
REMARK 620 6 HOH A 578 O 125.4 77.6 78.7 142.9 134.4
REMARK 620 7 HOH A 592 O 107.5 76.5 152.0 137.3 72.5 73.8
REMARK 620 8 HOH B 501 O 150.7 157.1 87.9 79.0 71.8 80.1 92.5
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 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 65 O
REMARK 620 2 VAL B 68 O 77.6
REMARK 620 3 PHE B 71 O 110.4 95.5
REMARK 620 4 HOH B 557 O 104.1 178.2 83.2
REMARK 620 5 HOH B 574 O 168.2 100.1 81.2 78.5
REMARK 620 6 HOH B 593 O 93.2 87.9 156.3 92.8 75.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 193 OD1
REMARK 620 2 ASP B 193 OD2 53.1
REMARK 620 3 THR B 195 O 80.4 97.2
REMARK 620 4 THR B 195 OG1 72.0 125.0 69.6
REMARK 620 5 HOH B 439 O 129.1 83.2 81.0 140.6
REMARK 620 6 HOH B 532 O 76.0 94.0 139.8 72.4 138.8
REMARK 620 7 HOH B 535 O 143.3 161.5 95.2 72.4 85.2 85.3
REMARK 620 8 HOH B 569 O 120.6 78.8 145.1 140.4 64.1 75.0 83.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF 7W45 A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 7W45 B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 7W45 GLY A 24 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA A 25 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY A 26 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA A 27 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY A 28 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA A 29 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY A 30 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA A 31 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY A 32 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA A 33 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY A 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 MET A 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 LYS A 59 UNP G9BY57 ALA 59 ENGINEERED MUTATION
SEQADV 7W45 ILE A 63 UNP G9BY57 VAL 63 ENGINEERED MUTATION
SEQADV 7W45 GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7W45 CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7W45 ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7W45 PRO A 248 UNP G9BY57 ASN 248 ENGINEERED MUTATION
SEQADV 7W45 CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 7W45 GLY B 24 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA B 25 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY B 26 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA B 27 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY B 28 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA B 29 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY B 30 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA B 31 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY B 32 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 ALA B 33 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 GLY B 34 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 MET B 35 UNP G9BY57 EXPRESSION TAG
SEQADV 7W45 LYS B 59 UNP G9BY57 ALA 59 ENGINEERED MUTATION
SEQADV 7W45 ILE B 63 UNP G9BY57 VAL 63 ENGINEERED MUTATION
SEQADV 7W45 GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7W45 CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7W45 ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7W45 PRO B 248 UNP G9BY57 ASN 248 ENGINEERED MUTATION
SEQADV 7W45 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 LYS THR TYR THR
SEQRES 4 A 270 ILE 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 SER 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 PRO 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 LYS THR TYR THR
SEQRES 4 B 270 ILE 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 SER 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 PRO 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 NA A 301 1
HET CA A 302 1
HET CA A 303 1
HET CA B 301 1
HET CA B 302 1
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
FORMUL 3 NA NA 1+
FORMUL 4 CA 4(CA 2+)
FORMUL 8 HOH *500(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 SER 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 SER B 48 ALA B 52 5 5
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 ARG B 153 1 7
HELIX 18 AB9 SER 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 ILE 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 ILE A 89 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 ILE B 63 0
SHEET 2 AA3 6 GLY B 74 THR B 80 -1 O GLY B 74 N ILE B 63
SHEET 3 AA3 6 VAL B 115 ILE B 119 -1 O VAL B 118 N VAL B 75
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 233 N ILE B 204
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 2.01
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.04
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.05
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.05
LINK O ARG A 65 CA CA A 303 1555 1555 2.71
LINK O VAL A 68 CA CA A 303 1555 1555 2.57
LINK O PHE A 71 CA CA A 303 1555 1555 2.49
LINK OG SER A 136 NA NA A 301 1555 1555 3.01
LINK OD1 ASP A 193 CA CA A 302 1555 1555 2.35
LINK OD2 ASP A 193 CA CA A 302 1555 1555 2.54
LINK O THR A 195 CA CA A 302 1555 1555 2.30
LINK OG1 THR A 195 CA CA A 302 1555 1555 2.55
LINK CA CA A 302 O HOH A 482 1555 1555 2.51
LINK CA CA A 302 O HOH A 578 1555 1555 2.39
LINK CA CA A 302 O HOH A 592 1555 1555 2.39
LINK CA CA A 302 O HOH B 501 1555 4455 2.49
LINK CA CA A 303 O HOH A 550 1555 1555 2.95
LINK CA CA A 303 O HOH A 553 1555 1555 2.56
LINK CA CA A 303 O HOH A 598 1555 1555 2.35
LINK O ARG B 65 CA CA B 302 1555 1555 2.54
LINK O VAL B 68 CA CA B 302 1555 1555 2.52
LINK O PHE B 71 CA CA B 302 1555 1555 2.51
LINK OD1 ASP B 193 CA CA B 301 1555 1555 2.42
LINK OD2 ASP B 193 CA CA B 301 1555 1555 2.41
LINK O THR B 195 CA CA B 301 1555 1555 2.41
LINK OG1 THR B 195 CA CA B 301 1555 1555 2.39
LINK CA CA B 301 O HOH B 439 1555 1555 2.47
LINK CA CA B 301 O HOH B 532 1555 1555 2.51
LINK CA CA B 301 O HOH B 535 1555 1555 2.52
LINK CA CA B 301 O HOH B 569 1555 1555 2.45
LINK CA CA B 302 O HOH B 557 1555 1555 2.46
LINK CA CA B 302 O HOH B 574 1555 1555 2.59
LINK CA CA B 302 O HOH B 593 1555 1555 2.42
CRYST1 40.370 84.770 147.512 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 0.024771 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011797 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006779 0.00000
TER 1973 GLN A 293
TER 3959 GLN B 293
MASTER 375 0 5 22 18 0 0 6 4419 2 45 42
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