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HEADER HYDROLASE 25-APR-18 5ZRR
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S
TITLE 2 MUTANT IN MONOETHYL SUCCINATE 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 5ZRR 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. 1.34 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) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.381
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 52198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.008
REMARK 3 FREE R VALUE TEST SET COUNT : 2614
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 41.6282 - 3.5713 0.99 2853 149 0.1648 0.1733
REMARK 3 2 3.5713 - 2.8348 1.00 2740 144 0.1480 0.1399
REMARK 3 3 2.8348 - 2.4765 1.00 2709 142 0.1480 0.1992
REMARK 3 4 2.4765 - 2.2501 1.00 2684 141 0.1466 0.1786
REMARK 3 5 2.2501 - 2.0888 1.00 2692 149 0.1436 0.1680
REMARK 3 6 2.0888 - 1.9657 1.00 2663 136 0.1377 0.1724
REMARK 3 7 1.9657 - 1.8672 1.00 2671 146 0.1438 0.1648
REMARK 3 8 1.8672 - 1.7860 1.00 2660 135 0.1411 0.1974
REMARK 3 9 1.7860 - 1.7172 1.00 2658 137 0.1455 0.1440
REMARK 3 10 1.7172 - 1.6579 1.00 2646 145 0.1549 0.1866
REMARK 3 11 1.6579 - 1.6061 1.00 2640 138 0.1482 0.1807
REMARK 3 12 1.6061 - 1.5602 1.00 2659 142 0.1523 0.1705
REMARK 3 13 1.5602 - 1.5191 1.00 2644 138 0.1542 0.1795
REMARK 3 14 1.5191 - 1.4821 1.00 2630 135 0.1559 0.1916
REMARK 3 15 1.4821 - 1.4484 1.00 2604 132 0.1763 0.2058
REMARK 3 16 1.4484 - 1.4175 0.99 2634 140 0.2222 0.2618
REMARK 3 17 1.4175 - 1.3892 0.99 2627 143 0.2999 0.3205
REMARK 3 18 1.3892 - 1.3630 0.95 2489 130 0.3460 0.3232
REMARK 3 19 1.3630 - 1.3386 0.65 1681 92 0.3463 0.4099
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.42
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 2131
REMARK 3 ANGLE : 1.167 2903
REMARK 3 CHIRALITY : 0.082 309
REMARK 3 PLANARITY : 0.006 385
REMARK 3 DIHEDRAL : 11.323 790
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 5ZRR 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_1300007543.
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 : 52202
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40100
REMARK 200 FOR SHELL : 2.500
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: 4WFI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M ZNSO4, 0.1 M MES PH 6.5, 25%
REMARK 280 V/V 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 24.75350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.39150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.69850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.39150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.75350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.69850
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 677 O HOH A 731 2.12
REMARK 500 O HOH A 617 O HOH A 634 2.13
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 512 O HOH A 606 3454 2.14
REMARK 500 O HOH A 751 O HOH A 763 4455 2.15
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 ARG A 156 17.77 -158.06
REMARK 500 ALA A 176 -121.95 63.18
REMARK 500 THR A 199 58.42 32.45
REMARK 500 HIS A 230 -86.64 -116.71
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 ZN A 405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 43 N
REMARK 620 2 GLY A 43 O 75.9
REMARK 620 3 ASP A 46 OD1 136.4 81.3
REMARK 620 4 GLU A 50 OE2 119.3 97.5 100.1
REMARK 620 5 HOH A 710 O 86.4 162.0 110.5 93.7
REMARK 620 N 1 2 3 4
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 GLU A 57 OE2
REMARK 620 2 HOH A 603 O 114.0
REMARK 620 3 GLU A 155 OE2 83.6 35.6
REMARK 620 4 HOH A 547 O 100.8 98.7 87.0
REMARK 620 N 1 2 3
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 ASP A 204 OD1
REMARK 620 2 THR A 206 O 89.4
REMARK 620 3 THR A 206 OG1 82.5 79.6
REMARK 620 4 HOH A 574 O 104.3 75.3 153.8
REMARK 620 5 HOH A 550 O 85.5 152.0 72.5 132.6
REMARK 620 6 HOH A 672 O 164.4 84.9 82.2 88.3 92.8
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 96.1 151.4
REMARK 620 4 GLU A 296 OE1 97.1 83.5 100.2
REMARK 620 5 GLU A 118 OE1 64.3 108.4 49.2 68.8
REMARK 620 6 GLU A 118 OE2 60.8 106.4 50.0 71.6 3.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9J3 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 ZN 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 SO4 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: 5ZRS RELATED DB: PDB
DBREF 5ZRR A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 5ZRR GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRR PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRR ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 5ZRR PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 5ZRR SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 5ZRR LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRR LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRR 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 5ZRR MHO A 188 MET MODIFIED RESIDUE
HET MHO A 188 9
HET 9J3 A 401 10
HET ZN A 402 1
HET ZN A 403 1
HET ZN A 404 1
HET ZN A 405 1
HET GOL A 406 6
HET SO4 A 407 5
HETNAM MHO S-OXYMETHIONINE
HETNAM 9J3 4-ETHOXY-4-OXOBUTANOIC ACID
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MHO C5 H11 N O3 S
FORMUL 2 9J3 C6 H10 O4
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 SO4 O4 S 2-
FORMUL 9 HOH *276(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 TRP A 115 SER A 122 1 8
HELIX 3 AA3 GLN A 138 SER A 157 1 20
HELIX 4 AA4 ASP A 158 GLU A 163 1 6
HELIX 5 AA5 ALA A 176 ARG A 189 1 14
HELIX 6 AA6 HIS A 230 LEU A 238 1 9
HELIX 7 AA7 PHE A 255 ILE A 259 5 5
HELIX 8 AA8 ASN A 261 ASP A 277 1 17
HELIX 9 AA9 ASP A 279 ARG A 281 5 3
HELIX 10 AB1 TYR A 282 CYS A 287 1 6
SHEET 1 AA1 6 VAL A 69 ALA A 78 0
SHEET 2 AA1 6 GLY A 82 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 ILE A 130
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 ALA A 245 N ILE A 216
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O GLU A 296 N GLU A 248
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.04
LINK N GLY A 43 ZN ZN A 405 1555 1555 2.20
LINK O GLY A 43 ZN ZN A 405 1555 1555 2.25
LINK OD1 ASP A 46 ZN ZN A 405 1555 1555 1.98
LINK OE2 GLU A 50 ZN ZN A 405 1555 1555 1.99
LINK OE2 GLU A 57 ZN ZN A 403 1555 1555 1.99
LINK C VAL A 187 N MHO A 188 1555 1555 1.33
LINK C MHO A 188 N ARG A 189 1555 1555 1.34
LINK OD1 ASP A 204 ZN ZN A 404 1555 1555 2.27
LINK O THR A 206 ZN ZN A 404 1555 1555 2.22
LINK OG1 THR A 206 ZN ZN A 404 1555 1555 2.28
LINK OE1 GLU A 220 ZN ZN A 402 1555 1555 2.03
LINK OE2 GLU A 220 ZN ZN A 402 1555 1555 2.59
LINK OD1 ASP A 250 ZN ZN A 402 1555 1555 1.95
LINK OE1 GLU A 296 ZN ZN A 402 1555 1555 1.89
LINK ZN ZN A 403 O HOH A 603 1555 1555 1.97
LINK ZN ZN A 404 O HOH A 574 1555 1555 2.33
LINK ZN ZN A 404 O HOH A 550 1555 1555 2.29
LINK ZN ZN A 404 O HOH A 672 1555 1555 2.20
LINK ZN ZN A 405 O HOH A 710 1555 1555 2.32
LINK OE1 GLU A 118 ZN ZN A 402 1555 3444 1.97
LINK OE2 GLU A 118 ZN ZN A 402 1555 3444 2.57
LINK OE2 GLU A 155 ZN ZN A 403 1555 2455 1.94
LINK ZN ZN A 403 O HOH A 547 1555 2454 1.95
CISPEP 1 CYS A 287 PRO A 288 0 -0.83
CISPEP 2 CYS A 302 PRO A 303 0 -2.06
SITE 1 AC1 10 GLY A 105 PHE A 106 THR A 107 ALA A 176
SITE 2 AC1 10 MET A 177 TRP A 201 ILE A 224 HIS A 254
SITE 3 AC1 10 HOH A 540 HOH A 645
SITE 1 AC2 4 GLU A 118 GLU A 220 ASP A 250 GLU A 296
SITE 1 AC3 4 GLU A 57 GLU A 155 HOH A 547 HOH A 603
SITE 1 AC4 6 ASP A 204 THR A 206 HOH A 550 HOH A 574
SITE 2 AC4 6 HOH A 672 HOH A 729
SITE 1 AC5 4 GLY A 43 ASP A 46 GLU A 50 HOH A 710
SITE 1 AC6 10 PHE A 77 ASP A 151 TYR A 152 GLU A 155
SITE 2 AC6 10 ARG A 156 GLN A 284 HOH A 503 HOH A 506
SITE 3 AC6 10 HOH A 523 HOH A 547
SITE 1 AC7 6 SER A 79 GLY A 80 GLU A 91 THR A 92
SITE 2 AC7 6 ASP A 93 HOH A 562
CRYST1 49.507 61.397 76.783 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 0.020199 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016287 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013024 0.00000
TER 2055 LYS A 305
MASTER 345 0 8 10 9 0 13 6 2343 1 57 21
END |