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HEADER HYDROLASE 26-NOV-21 7W44
TITLE COMPLEX STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT LCC
TITLE 2 ICCG_RIP
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: UNIDENTIFIED 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: PET46EK /LIC
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 7W44 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. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 47432
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 : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2483
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3417
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 174
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 615
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : -1.06000
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): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4025 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3705 ; 0.001 ; 0.014
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5512 ; 1.645 ; 1.647
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8499 ; 1.495 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 520 ; 7.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 201 ;28.608 ;20.348
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 572 ;10.607 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;19.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 542 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4667 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 989 ; 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 7W44 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_1300025940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-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 : 49376
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 24.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
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 (%): 52.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 12% W/V PEG 20,000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.11800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.11800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.28350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.63500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.28350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.63500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.11800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.28350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.63500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.11800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.28350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.63500
REMARK 290 SMTRY3 8 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 625 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 633 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 35
REMARK 465 GLN A 293
REMARK 465 ALA A 294
REMARK 465 GLY A 295
REMARK 465 ALA A 296
REMARK 465 GLY A 297
REMARK 465 ALA A 298
REMARK 465 GLY A 299
REMARK 465 ALA A 300
REMARK 465 GLY A 301
REMARK 465 ALA A 302
REMARK 465 GLY A 303
REMARK 465 MET B 35
REMARK 465 GLN B 293
REMARK 465 ALA B 294
REMARK 465 GLY B 295
REMARK 465 ALA B 296
REMARK 465 GLY B 297
REMARK 465 ALA B 298
REMARK 465 GLY B 299
REMARK 465 ALA B 300
REMARK 465 GLY B 301
REMARK 465 ALA B 302
REMARK 465 GLY B 303
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 -4.45 72.87
REMARK 500 SER A 145 18.20 -146.70
REMARK 500 SER A 165 -122.64 66.39
REMARK 500 THR A 188 55.71 37.62
REMARK 500 HIS A 218 -84.29 -123.02
REMARK 500 SER B 165 -122.88 66.88
REMARK 500 THR B 188 61.51 32.21
REMARK 500 HIS B 218 -87.59 -126.21
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 838 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 11.59 ANGSTROMS
DBREF 7W44 A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 7W44 B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 7W44 MET A 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 7W44 ARG A 59 UNP G9BY57 ALA 59 CONFLICT
SEQADV 7W44 ILE A 63 UNP G9BY57 VAL 63 CONFLICT
SEQADV 7W44 GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7W44 CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7W44 ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7W44 PRO A 248 UNP G9BY57 ASN 248 CONFLICT
SEQADV 7W44 CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 7W44 ALA A 294 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY A 295 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA A 296 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY A 297 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA A 298 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY A 299 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA A 300 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY A 301 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA A 302 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY A 303 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 MET B 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 7W44 ARG B 59 UNP G9BY57 ALA 59 CONFLICT
SEQADV 7W44 ILE B 63 UNP G9BY57 VAL 63 CONFLICT
SEQADV 7W44 GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 7W44 CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 7W44 ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 7W44 PRO B 248 UNP G9BY57 ASN 248 CONFLICT
SEQADV 7W44 CYS B 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 7W44 ALA B 294 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY B 295 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA B 296 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY B 297 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA B 298 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY B 299 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA B 300 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY B 301 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 ALA B 302 UNP G9BY57 EXPRESSION TAG
SEQADV 7W44 GLY B 303 UNP G9BY57 EXPRESSION TAG
SEQRES 1 A 269 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 A 269 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ARG THR
SEQRES 3 A 269 TYR THR ILE SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 A 269 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 A 269 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 A 269 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 A 269 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 A 269 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 A 269 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 A 269 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 A 269 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 A 269 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 A 269 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 A 269 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 A 269 GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR
SEQRES 16 A 269 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 A 269 ILE ALA PRO ASN SER PRO ASN ALA ALA ILE SER VAL TYR
SEQRES 18 A 269 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 A 269 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 A 269 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN ALA
SEQRES 21 A 269 GLY ALA GLY ALA GLY ALA GLY ALA GLY
SEQRES 1 B 269 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 B 269 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ARG THR
SEQRES 3 B 269 TYR THR ILE SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 B 269 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 B 269 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 B 269 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 B 269 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 B 269 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 B 269 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 B 269 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 B 269 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 B 269 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 B 269 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 B 269 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 B 269 GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR
SEQRES 16 B 269 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 B 269 ILE ALA PRO ASN SER PRO ASN ALA ALA ILE SER VAL TYR
SEQRES 18 B 269 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 B 269 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 B 269 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN ALA
SEQRES 21 B 269 GLY ALA GLY ALA GLY ALA GLY ALA GLY
HET EDO A 401 4
HET IMD B 401 5
HET EDO B 402 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IMD IMIDAZOLE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 4 IMD C3 H5 N2 1+
FORMUL 6 HOH *615(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 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 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 VAL A 58 ILE A 63 0
SHEET 2 AA1 6 GLY A 74 PRO A 79 -1 O GLY A 74 N ILE A 63
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 VAL A 115
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 ILE B 76 N TYR B 61
SHEET 3 AA3 6 PHE B 114 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 2.08
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.04
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.10
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.12
CRYST1 64.567 153.270 118.236 90.00 90.00 90.00 C 2 2 21 16
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 0.015488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006524 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008458 0.00000
TER 1952 CYS A 292
TER 3906 CYS B 292
MASTER 337 0 3 22 18 0 0 6 4518 2 21 42
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