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HEADER HYDROLASE 25-APR-18 5ZRS
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S
TITLE 2 MUTANT IN MONOETHYL ADIPATE BOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD, PROTEIN ENGINEERING,
KEYWDS 2 THERMOSTABILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,S.UCHIYAMA,
AUTHOR 2 F.KAWAI,N.ITO,M.ODA
REVDAT 1 12-SEP-18 5ZRS 0
JRNL AUTH N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,
JRNL AUTH 2 S.UCHIYAMA,F.KAWAI,N.ITO,M.ODA
JRNL TITL STRUCTURAL DYNAMICS OF THE PET-DEGRADING CUTINASE-LIKE
JRNL TITL 2 ENZYME FROM SACCHAROMONOSPORA VIRIDIS AHK190 IN
JRNL TITL 3 SUBSTRATE-BOUND STATES ELUCIDATES THE CA2+-DRIVEN CATALYTIC
JRNL TITL 4 CYCLE.
JRNL REF BIOCHEMISTRY 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 30110540
JRNL DOI 10.1021/ACS.BIOCHEM.8B00624
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.349
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 50518
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.004
REMARK 3 FREE R VALUE TEST SET COUNT : 2528
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 49.6389 - 3.6743 1.00 2861 150 0.1451 0.1696
REMARK 3 2 3.6743 - 2.9165 1.00 2725 143 0.1380 0.1639
REMARK 3 3 2.9165 - 2.5478 1.00 2712 142 0.1470 0.1700
REMARK 3 4 2.5478 - 2.3149 1.00 2705 145 0.1421 0.1643
REMARK 3 5 2.3149 - 2.1490 1.00 2685 139 0.1379 0.1801
REMARK 3 6 2.1490 - 2.0223 1.00 2647 139 0.1409 0.1799
REMARK 3 7 2.0223 - 1.9210 1.00 2665 140 0.1407 0.1712
REMARK 3 8 1.9210 - 1.8374 1.00 2656 143 0.1465 0.2022
REMARK 3 9 1.8374 - 1.7666 1.00 2660 139 0.1528 0.1750
REMARK 3 10 1.7666 - 1.7057 1.00 2651 138 0.1670 0.2043
REMARK 3 11 1.7057 - 1.6523 1.00 2666 142 0.1696 0.2311
REMARK 3 12 1.6523 - 1.6051 1.00 2635 141 0.1805 0.2118
REMARK 3 13 1.6051 - 1.5628 1.00 2618 135 0.1951 0.2100
REMARK 3 14 1.5628 - 1.5247 1.00 2647 137 0.2072 0.2281
REMARK 3 15 1.5247 - 1.4900 1.00 2610 137 0.2349 0.2585
REMARK 3 16 1.4900 - 1.4583 1.00 2655 143 0.2512 0.2803
REMARK 3 17 1.4583 - 1.4291 1.00 2633 138 0.2709 0.3152
REMARK 3 18 1.4291 - 1.4022 0.99 2559 137 0.2997 0.2994
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.121
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.674
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.78
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 : 0.009 2127
REMARK 3 ANGLE : 1.342 2893
REMARK 3 CHIRALITY : 0.086 308
REMARK 3 PLANARITY : 0.007 383
REMARK 3 DIHEDRAL : 11.424 789
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 5ZRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1300007545.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : CRYO-COOLED CHANNEL-CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50522
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11900
REMARK 200 FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.80400
REMARK 200 FOR SHELL : 2.100
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: 4WFJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M ZNSO4 0.1 M MES PH 6.5 25% V/V
REMARK 280 PEG MME 550, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 25.22850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.39250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.92800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.39250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.22850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.92800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 LEU A 306
REMARK 465 ASN A 307
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 HOH A 501 O HOH A 573 2.04
REMARK 500 O HOH A 739 O HOH A 775 2.07
REMARK 500 O3 GOL A 407 O HOH A 501 2.10
REMARK 500 O HOH A 504 O HOH A 606 2.13
REMARK 500 O HOH A 509 O HOH A 742 2.14
REMARK 500 O HOH A 638 O HOH A 750 2.15
REMARK 500 OAI 9J6 A 401 O HOH A 502 2.17
REMARK 500 O HOH A 782 O HOH A 879 2.17
REMARK 500 O HOH A 730 O HOH A 806 2.18
REMARK 500 O HOH A 579 O HOH A 685 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 ASN A 47 109.63 -162.94
REMARK 500 THR A 107 -3.74 70.73
REMARK 500 ALA A 176 -119.66 66.30
REMARK 500 THR A 199 57.86 32.44
REMARK 500 HIS A 230 -88.42 -117.16
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 890 DISTANCE = 6.56 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 ZN A 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 43 N
REMARK 620 2 GLY A 43 O 77.6
REMARK 620 3 ASP A 46 OD1 143.0 84.7
REMARK 620 4 ASP A 46 OD2 91.5 84.5 54.2
REMARK 620 5 GLU A 50 OE2 119.9 103.1 95.5 148.5
REMARK 620 6 HOH A 653 O 91.9 168.7 101.8 91.9 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 100.4
REMARK 620 3 PHE A 81 O 100.7 82.8
REMARK 620 4 HOH A 617 O 165.8 93.5 83.8
REMARK 620 5 HOH A 660 O 88.6 166.5 85.6 78.3
REMARK 620 6 HOH A 772 O 96.6 93.0 162.7 79.7 96.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD1
REMARK 620 2 THR A 206 O 93.1
REMARK 620 3 THR A 206 OG1 85.2 80.2
REMARK 620 4 HOH A 663 O 87.9 156.5 76.5
REMARK 620 5 HOH A 662 O 164.2 78.3 80.3 94.8
REMARK 620 6 HOH A 652 O 106.4 81.4 158.7 120.8 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 220 OE1
REMARK 620 2 GLU A 220 OE2 55.4
REMARK 620 3 ASP A 250 OD1 100.7 155.9
REMARK 620 4 GLU A 296 OE1 104.9 86.6 98.1
REMARK 620 5 GLU A 118 OE2 61.7 108.8 49.6 80.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9J6 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ZNO RELATED DB: PDB
REMARK 900 RELATED ID: 5ZRQ RELATED DB: PDB
REMARK 900 RELATED ID: 5ZRR RELATED DB: PDB
DBREF 5ZRS A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 5ZRS GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRS PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRS ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 5ZRS PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 5ZRS SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 5ZRS LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRS LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRS ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 265 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 A 265 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 A 265 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 A 265 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 A 265 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 A 265 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 A 265 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 A 265 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 A 265 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 A 265 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 A 265 MET GLY HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 A 265 THR VAL MHO ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 A 265 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 A 265 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 265 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 A 265 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 A 265 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 A 265 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 A 265 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 A 265 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 265 PRO TYR LYS LEU ASN
MODRES 5ZRS MHO A 188 MET MODIFIED RESIDUE
HET MHO A 188 9
HET 9J6 A 401 12
HET ZN A 402 1
HET ZN A 403 1
HET ZN A 404 1
HET CA A 405 1
HET GOL A 406 6
HET GOL A 407 6
HETNAM MHO S-OXYMETHIONINE
HETNAM 9J6 6-ETHOXY-6-OXOHEXANOIC ACID
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN 9J6 ADIPIC ACID MONOETHYL ESTER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MHO C5 H11 N O3 S
FORMUL 2 9J6 C8 H14 O4
FORMUL 3 ZN 3(ZN 2+)
FORMUL 6 CA CA 2+
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *390(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 SER A 109 MET A 113 5 5
HELIX 3 AA3 SER A 114 SER A 122 1 9
HELIX 4 AA4 GLN A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O ILE A 86 N GLU A 72
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O ASP A 166 N PHE A 97
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O LEU A 249 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O GLU A 297 N GLU A 248
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.04
LINK N GLY A 43 ZN ZN A 404 1555 1555 2.16
LINK O GLY A 43 ZN ZN A 404 1555 1555 2.21
LINK OD1 ASP A 46 ZN ZN A 404 1555 1555 1.96
LINK OD2 ASP A 46 ZN ZN A 404 1555 1555 2.66
LINK OE2 GLU A 50 ZN ZN A 404 1555 1555 2.04
LINK O SER A 76 CA CA A 405 1555 1555 2.29
LINK O ALA A 78 CA CA A 405 1555 1555 2.31
LINK O PHE A 81 CA CA A 405 1555 1555 2.34
LINK C VAL A 187 N MHO A 188 1555 1555 1.33
LINK C MHO A 188 N ARG A 189 1555 1555 1.33
LINK OD1 ASP A 204 ZN ZN A 403 1555 1555 2.25
LINK O THR A 206 ZN ZN A 403 1555 1555 2.15
LINK OG1 THR A 206 ZN ZN A 403 1555 1555 2.33
LINK OE1 GLU A 220 ZN ZN A 402 1555 1555 2.00
LINK OE2 GLU A 220 ZN ZN A 402 1555 1555 2.58
LINK OD1 ASP A 250 ZN ZN A 402 1555 1555 1.96
LINK OE1 GLU A 296 ZN ZN A 402 1555 1555 1.93
LINK ZN ZN A 403 O HOH A 663 1555 1555 2.34
LINK ZN ZN A 403 O HOH A 662 1555 1555 2.42
LINK ZN ZN A 403 O HOH A 652 1555 1555 2.24
LINK ZN ZN A 404 O HOH A 653 1555 1555 2.18
LINK CA CA A 405 O HOH A 617 1555 1555 2.60
LINK CA CA A 405 O HOH A 660 1555 1555 2.40
LINK CA CA A 405 O HOH A 772 1555 1555 2.36
LINK OE2 GLU A 118 ZN ZN A 402 1555 3455 1.94
CISPEP 1 CYS A 287 PRO A 288 0 -1.69
CISPEP 2 CYS A 302 PRO A 303 0 -2.98
SITE 1 AC1 13 GLY A 105 PHE A 106 ALA A 176 MET A 177
SITE 2 AC1 13 TRP A 201 GLY A 208 ILE A 224 SER A 237
SITE 3 AC1 13 HIS A 254 HOH A 502 HOH A 546 HOH A 664
SITE 4 AC1 13 HOH A 703
SITE 1 AC2 4 GLU A 118 GLU A 220 ASP A 250 GLU A 296
SITE 1 AC3 5 ASP A 204 THR A 206 HOH A 652 HOH A 662
SITE 2 AC3 5 HOH A 663
SITE 1 AC4 4 GLY A 43 ASP A 46 GLU A 50 HOH A 653
SITE 1 AC5 6 SER A 76 ALA A 78 PHE A 81 HOH A 617
SITE 2 AC5 6 HOH A 660 HOH A 772
SITE 1 AC6 7 ARG A 64 LYS A 232 GLU A 248 GLU A 296
SITE 2 AC6 7 GLU A 297 HOH A 557 HOH A 578
SITE 1 AC7 7 GLY A 52 PRO A 53 GLU A 91 ASP A 93
SITE 2 AC7 7 GLU A 94 HOH A 501 HOH A 608
CRYST1 50.457 63.856 78.785 90.00 90.00 90.00 P 21 21 21 4
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 0.019819 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012693 0.00000
TER 2049 LYS A 305
MASTER 348 0 8 11 9 0 14 6 2460 1 66 21
END |