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HEADER HYDROLASE 14-JAN-25 9LJ7
TITLE CRYSTAL STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE VARIANT, ICCG-
TITLE 2 H218S/F222I
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 OTHER_DETAILS: H218S, F222I
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 LEAF-BRANCH COMPOST CUTINASE, PET HYDROLASE, PETASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.X.TU,Y.YANG,J.S.TONG
REVDAT 1 21-JAN-26 9LJ7 0
JRNL AUTH J.K.WANG,Y.X.TU,Y.YANG,X.WANG,J.S.TONG,J.Z.YAO
JRNL TITL COMPUTATIONAL DISCOVERY, BIOCHEMICAL CHARACTERIZATION,
JRNL TITL 2 CRYSTAL STRUCTURE, AND CATALYTIC MECHANISM OF A HIGHLY
JRNL TITL 3 EFFICIENT POLY (ETHYLENE TEREPHTHALATE) HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 66399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.1700 - 3.8922 1.00 4924 148 0.1519 0.1581
REMARK 3 2 3.8922 - 3.0896 1.00 4707 149 0.1563 0.1607
REMARK 3 3 3.0896 - 2.6991 1.00 4665 143 0.1745 0.2170
REMARK 3 4 2.6991 - 2.4523 1.00 4617 144 0.1819 0.2299
REMARK 3 5 2.4523 - 2.2766 1.00 4618 138 0.1791 0.2125
REMARK 3 6 2.2766 - 2.1424 1.00 4577 149 0.1735 0.2251
REMARK 3 7 2.1424 - 2.0351 1.00 4577 136 0.1797 0.2195
REMARK 3 8 2.0351 - 1.9465 1.00 4569 143 0.1851 0.2090
REMARK 3 9 1.9465 - 1.8715 1.00 4565 146 0.1934 0.2438
REMARK 3 10 1.8715 - 1.8070 1.00 4545 142 0.1886 0.2459
REMARK 3 11 1.8070 - 1.7505 1.00 4552 135 0.1914 0.2294
REMARK 3 12 1.7505 - 1.7004 1.00 4550 149 0.1948 0.2075
REMARK 3 13 1.7004 - 1.6557 1.00 4555 139 0.1954 0.2155
REMARK 3 14 1.6557 - 1.6153 0.98 4382 135 0.2026 0.2395
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 4044
REMARK 3 ANGLE : 0.857 5548
REMARK 3 CHIRALITY : 0.054 633
REMARK 3 PLANARITY : 0.006 731
REMARK 3 DIHEDRAL : 9.052 2419
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9LJ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 26-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1300055758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPX
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66503
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.615
REMARK 200 RESOLUTION RANGE LOW (A) : 49.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 25.88
REMARK 200 R MERGE (I) : 0.07930
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 52.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.7 M SODIUM ACETATE PH 7.0, 5% PEG
REMARK 280 3350, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 49.25400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.82900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.82900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.88100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.82900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.82900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.62700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.82900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.82900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.88100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.82900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.82900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 24.62700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.25400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -50.82900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -50.82900
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 73.88100
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: 9840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 3
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: 10010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 MET A 35
REMARK 465 LEU A 294
REMARK 465 GLU A 295
REMARK 465 LEU A 296
REMARK 465 VAL A 297
REMARK 465 PRO A 298
REMARK 465 ARG A 299
REMARK 465 MET B 35
REMARK 465 LEU B 294
REMARK 465 GLU B 295
REMARK 465 LEU B 296
REMARK 465 VAL B 297
REMARK 465 PRO B 298
REMARK 465 ARG B 299
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER B 69 O HOH B 401 2.09
REMARK 500 O HOH A 545 O HOH A 634 2.16
REMARK 500 O HOH B 561 O HOH B 659 2.17
REMARK 500 OG SER B 165 NE1 TRP B 190 2.17
REMARK 500 O HOH B 613 O HOH B 625 2.18
REMARK 500 O HOH A 618 O HOH A 661 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 A 577 O HOH B 430 7555 2.19
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 SER A 165 -115.85 54.93
REMARK 500 THR A 188 63.58 34.05
REMARK 500 SER A 218 -74.19 -120.39
REMARK 500 SER B 165 -118.90 61.73
REMARK 500 THR B 188 63.46 32.54
REMARK 500 ASP B 193 -128.84 25.72
REMARK 500 LYS B 194 143.91 75.94
REMARK 500 SER B 218 -80.99 -128.52
REMARK 500 SER B 218 -82.46 -127.48
REMARK 500 CYS B 292 -98.79 -105.27
REMARK 500
REMARK 500 REMARK: NULL
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 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 65 O
REMARK 620 2 VAL A 68 O 95.8
REMARK 620 3 PHE A 71 O 106.0 95.6
REMARK 620 4 HOH A 477 O 97.1 166.9 82.7
REMARK 620 5 HOH A 579 O 170.8 90.2 80.2 76.7
REMARK 620 6 HOH A 632 O 100.9 87.0 152.6 88.7 72.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 65 O
REMARK 620 2 VAL B 68 O 89.0
REMARK 620 3 PHE B 71 O 106.7 90.4
REMARK 620 4 HOH B 433 O 103.9 167.1 86.2
REMARK 620 5 HOH B 502 O 169.4 90.3 83.9 76.9
REMARK 620 N 1 2 3 4
DBREF 9LJ7 A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 9LJ7 B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 9LJ7 MET A 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 9LJ7 GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 9LJ7 SER A 218 UNP G9BY57 HIS 218 ENGINEERED MUTATION
SEQADV 9LJ7 ILE A 222 UNP G9BY57 PHE 222 ENGINEERED MUTATION
SEQADV 9LJ7 CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 9LJ7 ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 9LJ7 CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 9LJ7 LEU A 294 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 GLU A 295 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 LEU A 296 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 VAL A 297 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 PRO A 298 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 ARG A 299 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 MET B 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 9LJ7 GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 9LJ7 SER B 218 UNP G9BY57 HIS 218 ENGINEERED MUTATION
SEQADV 9LJ7 ILE B 222 UNP G9BY57 PHE 222 ENGINEERED MUTATION
SEQADV 9LJ7 CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 9LJ7 ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 9LJ7 CYS B 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 9LJ7 LEU B 294 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 GLU B 295 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 LEU B 296 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 VAL B 297 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 PRO B 298 UNP G9BY57 EXPRESSION TAG
SEQADV 9LJ7 ARG B 299 UNP G9BY57 EXPRESSION TAG
SEQRES 1 A 265 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 A 265 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR
SEQRES 3 A 265 TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 A 265 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 A 265 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 A 265 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 A 265 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 A 265 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 A 265 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 A 265 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 A 265 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 A 265 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 A 265 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 A 265 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 A 265 GLN SER ALA ILE PRO ILE TYR GLN ASN LEU PRO SER THR
SEQRES 16 A 265 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 A 265 ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR
SEQRES 18 A 265 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 A 265 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 A 265 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN LEU
SEQRES 21 A 265 GLU LEU VAL PRO ARG
SEQRES 1 B 265 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 B 265 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR
SEQRES 3 B 265 TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 B 265 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 B 265 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 B 265 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 B 265 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 B 265 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 B 265 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 B 265 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 B 265 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 B 265 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 B 265 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 B 265 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 B 265 GLN SER ALA ILE PRO ILE TYR GLN ASN LEU PRO SER THR
SEQRES 16 B 265 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 B 265 ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR
SEQRES 18 B 265 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 B 265 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 B 265 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN LEU
SEQRES 21 B 265 GLU LEU VAL PRO ARG
HET ACT A 301 4
HET CA A 302 1
HET ACT A 303 4
HET ACT B 301 4
HET ACT B 302 4
HET ACT B 303 4
HET CA B 304 1
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
FORMUL 3 ACT 5(C2 H3 O2 1-)
FORMUL 4 CA 2(CA 2+)
FORMUL 10 HOH *625(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 SER 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 ALA B 152 1 6
HELIX 18 AB9 SER B 165 ASN B 178 1 14
HELIX 19 AC1 SER 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 TYR A 78 N ALA A 59
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 VAL B 63 0
SHEET 2 AA3 6 GLY B 74 THR B 80 -1 O TYR B 78 N ALA B 59
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 VAL B 115
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 183 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 2.04
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.03
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.03
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.03
LINK O ARG A 65 CA CA A 302 1555 1555 2.41
LINK O VAL A 68 CA CA A 302 1555 1555 2.32
LINK O PHE A 71 CA CA A 302 1555 1555 2.37
LINK CA CA A 302 O HOH A 477 1555 1555 2.38
LINK CA CA A 302 O HOH A 579 1555 1555 2.81
LINK CA CA A 302 O HOH A 632 1555 1555 2.37
LINK O ARG B 65 CA CA B 304 1555 1555 2.38
LINK O VAL B 68 CA CA B 304 1555 1555 2.29
LINK O PHE B 71 CA CA B 304 1555 1555 2.41
LINK CA CA B 304 O HOH B 433 1555 1555 2.55
LINK CA CA B 304 O HOH B 502 1555 1555 2.73
CRYST1 101.658 101.658 98.508 90.00 90.00 90.00 P 43 21 2 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 0.009837 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010151 0.00000
TER 1958 GLN A 293
TER 3922 GLN B 293
MASTER 356 0 7 22 18 0 0 6 4529 2 43 42
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