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HEADER HYDROLASE 05-JUN-23 8JMP
TITLE STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE, ICCG IN COMPLEX WITH 1,4-
TITLE 2 BUTANEDIOL TEREPHTHALATE
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
KEYWDS PETASE, CUTINASE, ENZYME ENGINEERING, PBAT DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YANG,T.XUE,Y.ZHENG,S.CHENG,R.-T.GUO,C.-C.CHEN
REVDAT 1 29-NOV-23 8JMP 0
JRNL AUTH Y.YANG,S.CHENG,Y.ZHENG,T.XUE,J.W.HUANG,L.ZHANG,Y.YANG,
JRNL AUTH 2 R.T.GUO,C.C.CHEN
JRNL TITL REMODELING THE POLYMER-BINDING CAVITY TO IMPROVE THE
JRNL TITL 2 EFFICACY OF PBAT-DEGRADING ENZYME.
JRNL REF J HAZARD MATER V. 464 32965 2023
JRNL REFN ESSN 1873-3336
JRNL PMID 37979420
JRNL DOI 10.1016/J.JHAZMAT.2023.132965
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.17.1_3660: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 78612
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3772
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 31.6200 - 5.6900 0.92 2553 132 0.1724 0.1610
REMARK 3 2 5.6900 - 4.5200 0.98 2708 134 0.1352 0.1501
REMARK 3 3 4.5200 - 3.9500 0.98 2728 141 0.1201 0.1319
REMARK 3 4 3.9500 - 3.5900 0.99 2757 143 0.1335 0.1731
REMARK 3 5 3.5900 - 3.3300 1.00 2800 140 0.1478 0.1673
REMARK 3 6 3.3300 - 3.1400 1.00 2741 139 0.1459 0.2259
REMARK 3 7 3.1400 - 2.9800 1.00 2818 143 0.1535 0.1991
REMARK 3 8 2.9800 - 2.8500 1.00 2781 136 0.1550 0.1928
REMARK 3 9 2.8500 - 2.7400 1.00 2768 138 0.1528 0.1969
REMARK 3 10 2.7400 - 2.6500 1.00 2815 145 0.1596 0.1822
REMARK 3 11 2.6500 - 2.5600 1.00 2756 140 0.1673 0.2191
REMARK 3 12 2.5600 - 2.4900 1.00 2823 139 0.1614 0.2030
REMARK 3 13 2.4900 - 2.4200 1.00 2708 133 0.1582 0.2431
REMARK 3 14 2.4200 - 2.3600 1.00 2844 146 0.1605 0.1876
REMARK 3 15 2.3600 - 2.3100 1.00 2771 141 0.1527 0.1857
REMARK 3 16 2.3100 - 2.2600 1.00 2799 137 0.1464 0.1971
REMARK 3 17 2.2600 - 2.2200 1.00 2797 143 0.1549 0.2044
REMARK 3 18 2.2200 - 2.1800 1.00 2757 142 0.1591 0.2177
REMARK 3 19 2.1700 - 2.1400 1.00 2806 140 0.1643 0.2351
REMARK 3 20 2.1400 - 2.1000 1.00 2794 137 0.1672 0.2086
REMARK 3 21 2.1000 - 2.0700 1.00 2749 135 0.1680 0.2186
REMARK 3 22 2.0700 - 2.0300 1.00 2831 147 0.1611 0.2461
REMARK 3 23 2.0300 - 2.0000 1.00 2790 137 0.1679 0.2346
REMARK 3 24 2.0000 - 1.9800 1.00 2753 139 0.1833 0.2901
REMARK 3 25 1.9800 - 1.9500 1.00 2789 141 0.1881 0.3270
REMARK 3 26 1.9500 - 1.9200 1.00 2790 142 0.1885 0.2362
REMARK 3 27 1.9200 - 1.9000 1.00 2814 142 0.1725 0.2171
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) : 19.600
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 4054
REMARK 3 ANGLE : 0.790 5555
REMARK 3 CHIRALITY : 0.051 625
REMARK 3 PLANARITY : 0.006 732
REMARK 3 DIHEDRAL : 17.769 587
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 8JMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 15-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1300038219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78612
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 36.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.230
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.14390
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.260
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 (%): 49.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% V/V PEG 8000 AND 0.1 M SODIUM
REMARK 280 CACODYLATE, PH 6.5, EVAPORATION, 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 20.59500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.98950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.46400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.98950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.59500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.46400
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: 9880 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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 465 GLY B 34
REMARK 465 GLN B 293
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 NH2 ARG B 124 O HOH B 301 1.95
REMARK 500 OE1 GLN A 224 O HOH A 501 1.96
REMARK 500 O HOH B 514 O HOH B 530 2.02
REMARK 500 O HOH B 427 O HOH B 560 2.10
REMARK 500 O HOH A 596 O HOH A 626 2.11
REMARK 500 O HOH A 795 O HOH B 404 2.13
REMARK 500 O HOH B 420 O HOH B 430 2.13
REMARK 500 O HOH A 747 O HOH A 761 2.14
REMARK 500 O HOH B 369 O HOH B 480 2.15
REMARK 500 O HOH A 636 O HOH B 585 2.15
REMARK 500 O HOH B 450 O HOH B 585 2.15
REMARK 500 O HOH B 544 O HOH B 563 2.16
REMARK 500 O HOH B 585 O HOH B 596 2.16
REMARK 500 O HOH A 763 O HOH A 767 2.16
REMARK 500 NH1 ARG A 107 O HOH A 502 2.17
REMARK 500 O HOH A 721 O HOH A 751 2.17
REMARK 500 O HOH B 421 O HOH B 477 2.18
REMARK 500 O HOH B 550 O HOH B 556 2.19
REMARK 500 O HOH B 442 O HOH B 545 2.19
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 B 517 O HOH B 539 4455 2.01
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 THR A 96 -8.04 73.68
REMARK 500 ALA A 165 -120.50 65.20
REMARK 500 THR A 188 59.99 31.52
REMARK 500 HIS A 218 -82.11 -125.17
REMARK 500 THR B 96 -0.19 67.16
REMARK 500 ALA B 165 -119.21 64.34
REMARK 500 THR B 188 63.62 28.67
REMARK 500 HIS B 218 -83.57 -127.47
REMARK 500 ASN B 239 18.66 55.98
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 193 OD1
REMARK 620 2 ASP A 193 OD2 52.6
REMARK 620 3 THR A 195 O 84.9 94.1
REMARK 620 4 THR A 195 OG1 71.8 123.8 71.3
REMARK 620 5 HOH A 634 O 129.2 81.0 78.2 141.2
REMARK 620 6 HOH A 681 O 107.2 75.5 152.4 135.7 74.9
REMARK 620 7 HOH B 357 O 149.9 157.2 87.0 78.1 76.9 93.1
REMARK 620 8 HOH B 407 O 92.0 116.5 138.5 68.5 131.1 67.3 75.3
REMARK 620 N 1 2 3 4 5 6 7
DBREF 8JMP A 36 293 UNP G9BY57 PETH_UNKP 36 293
DBREF 8JMP B 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 8JMP GLY A 34 UNP G9BY57 EXPRESSION TAG
SEQADV 8JMP MET A 35 UNP G9BY57 EXPRESSION TAG
SEQADV 8JMP GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 8JMP ALA A 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 8JMP CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 8JMP ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 8JMP CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 8JMP GLY B 34 UNP G9BY57 EXPRESSION TAG
SEQADV 8JMP MET B 35 UNP G9BY57 EXPRESSION TAG
SEQADV 8JMP GLY B 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 8JMP ALA B 165 UNP G9BY57 SER 165 CONFLICT
SEQADV 8JMP CYS B 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 8JMP ILE B 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 8JMP 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 EMX A 402 28
HETNAM CA CALCIUM ION
HETNAM EMX 4-[4-(4-CARBOXYPHENYL)CARBONYLOXYBUTOXYCARBONYL]BENZOIC
HETNAM 2 EMX ACID
HETSYN EMX 4,4'-((BUTANE-1,4-DIYLBIS(OXY))BIS(CARBONYL))DIBENZOIC
HETSYN 2 EMX ACID
FORMUL 3 CA CA 2+
FORMUL 4 EMX C20 H18 O8
FORMUL 5 HOH *667(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 ASP B 98 SER B 101 5 4
HELIX 14 AB5 LEU B 102 HIS B 112 1 11
HELIX 15 AB6 GLY B 127 SER B 145 1 19
HELIX 16 AB7 PRO B 147 ARG B 153 1 7
HELIX 17 AB8 ALA B 165 ASN B 178 1 14
HELIX 18 AB9 HIS B 218 LEU B 226 1 9
HELIX 19 AC1 ILE B 243 SER B 247 5 5
HELIX 20 AC2 ASN B 249 ASP B 265 1 17
HELIX 21 AC3 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 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 CYS A 283 N GLU A 236
SHEET 1 AA3 6 SER B 57 VAL 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 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 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 2.06
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.02
SSBOND 3 CYS B 238 CYS B 283 1555 1555 2.04
SSBOND 4 CYS B 275 CYS B 292 1555 1555 2.02
LINK OD1 ASP A 193 CA CA A 401 1555 1555 2.47
LINK OD2 ASP A 193 CA CA A 401 1555 1555 2.46
LINK O THR A 195 CA CA A 401 1555 1555 2.32
LINK OG1 THR A 195 CA CA A 401 1555 1555 2.55
LINK CA CA A 401 O HOH A 634 1555 1555 2.47
LINK CA CA A 401 O HOH A 681 1555 1555 2.39
LINK CA CA A 401 O HOH B 357 1555 4455 2.48
LINK CA CA A 401 O HOH B 407 1555 4455 2.50
CRYST1 41.190 84.928 147.979 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 0.024278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006758 0.00000
TER 1964 GLN A 293
TER 3922 CYS B 292
MASTER 331 0 2 21 18 0 0 6 4590 2 44 40
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