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HEADER HYDROLASE 19-MAY-26 30ZT
TITLE PURH INHIBITED BY PMSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIENELACTONE HYDROLASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROMICROBIUM;
SOURCE 3 ORGANISM_TAXID: 2040;
SOURCE 4 STRAIN: LTX1;
SOURCE 5 GENE: BJ975_002808, IDH50_06695;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: T7 EXPRESS LYSY/IQ;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET DERIVED
KEYWDS INHIBITOR, ALPHA BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BLOCH,S.PANNEERSELVAM
REVDAT 1 16-SEP-26 30ZT 0
JRNL AUTH Y.BLOCH,S.PANNEERSELVAM
JRNL TITL OBSERVATION OF SULFONYLATION ELIMINATION PRODUCTS BY
JRNL TITL 2 CRYSTALLOGRAPHY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.ZHANG,K.CAO,H.LIU,Y.WANG,B.ZHANG,H.HAN,Z.CUI,H.CAO
REMARK 1 TITL DISCOVERY OF A POLYESTER POLYURETHANE-DEGRADING BACTERIUM
REMARK 1 TITL 2 FROM A COASTAL MUDFLAT AND IDENTIFICATION OF ITS DEGRADING
REMARK 1 TITL 3 ENZYME.
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 PMID 39612876
REMARK 1 DOI 10.1016/J.JHAZMAT.2024.136659
REMARK 2
REMARK 2 RESOLUTION. 1.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 86359
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1922
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.78
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3166
REMARK 3 BIN FREE R VALUE : 0.3226
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2013
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59520
REMARK 3 B22 (A**2) : -0.54580
REMARK 3 B33 (A**2) : 1.14100
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.110
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.032
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.034
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.032
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.032
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.978
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4360 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7868 ; 6.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1327 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 741 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4331 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 316 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 18 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4620 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 5.91
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 13.79
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 30ZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-26.
REMARK 100 THE DEPOSITION ID IS D_1292156937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-25
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05965
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS 3.23.0-G7AFF524E7-RELEASE
REMARK 200 DATA SCALING SOFTWARE : DIALS 3.23.0-G7AFF524E7-RELEASE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86578
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.125
REMARK 200 RESOLUTION RANGE LOW (A) : 55.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 23.40
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 55.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.00
REMARK 200 R MERGE FOR SHELL (I) : 0.04200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 73.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (W/V) PEG 3350, 100 MM GLYCINE PH
REMARK 280 9, 7 MM PMSF, 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 18.10650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.09350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.02700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.09350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.10650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.02700
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 MET A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 21 CG CD OE1 OE2
REMARK 470 ASN A 22 CG OD1 ND2
REMARK 470 GLN A 26 CG CD OE1 NE2
REMARK 470 GLU A 29 CG CD OE1 OE2
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 LYS A 169 HE ARG A 172 1.52
REMARK 500 HH12 ARG A 172 O HOH A 410 1.56
REMARK 500 CG2 THR A 141 O HOH A 640 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 452 O HOH A 562 4455 2.12
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 91 -1.56 71.14
REMARK 500 SER A 158 -121.93 61.64
REMARK 500 THR A 181 56.29 39.49
REMARK 500 HIS A 212 -85.12 -126.08
REMARK 500 HIS A 212 -85.12 -132.70
REMARK 500 LEU A 220 48.48 -84.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 126 0.09 SIDE CHAIN
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 708 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH A 709 DISTANCE = 7.26 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 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 175 OE1
REMARK 620 2 TYR A 257 O 101.4
REMARK 620 3 ASP A 260 OD1 163.5 93.5
REMARK 620 4 HOH A 402 O 85.4 109.9 96.1
REMARK 620 5 HOH A 591 O 91.2 87.5 82.5 162.7
REMARK 620 6 HOH A 638 O 84.7 168.1 79.4 80.6 82.2
REMARK 620 N 1 2 3 4 5
DBREF1 30ZT A 28 286 UNP A0A8I0FTC2_9ACTN
DBREF2 30ZT A A0A8I0FTC2 28 286
SEQADV 30ZT MET A 13 UNP A0A8I0FTC INITIATING METHIONINE
SEQADV 30ZT HIS A 14 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT HIS A 15 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT HIS A 16 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT HIS A 17 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT HIS A 18 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT HIS A 19 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT GLY A 20 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT GLU A 21 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT ASN A 22 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT LEU A 23 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT TYR A 24 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT PHE A 25 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT GLN A 26 UNP A0A8I0FTC EXPRESSION TAG
SEQADV 30ZT SER A 27 UNP A0A8I0FTC EXPRESSION TAG
SEQRES 1 A 274 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 A 274 GLN SER ALA GLU ASN PRO TYR GLU ARG GLY PRO ALA PRO
SEQRES 3 A 274 THR ASN SER SER ILE GLU ALA THR ARG GLY PRO TYR ALA
SEQRES 4 A 274 VAL SER THR LYS THR ILE SER SER LEU SER ALA ARG GLY
SEQRES 5 A 274 PHE GLY GLY GLY THR ILE TYR TYR PRO THR SER THR ALA
SEQRES 6 A 274 ASP GLY THR PHE GLY VAL VAL ALA ILE SER PRO GLY TYR
SEQRES 7 A 274 THR ALA ALA GLN SER THR ILE GLN TRP LEU GLY PRO ARG
SEQRES 8 A 274 ILE ALA SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR
SEQRES 9 A 274 ASN THR ARG LEU ASP GLN PRO GLY SER ARG GLY THR GLN
SEQRES 10 A 274 LEU LEU ALA ALA LEU ASP GLN THR ILE ALA ASP THR THR
SEQRES 11 A 274 VAL ARG SER ARG ILE ASP ALA SER ARG GLN ALA VAL VAL
SEQRES 12 A 274 GLY HIS SER MET GLY GLY GLY GLY THR LEU GLU ALA ALA
SEQRES 13 A 274 LYS SER ARG ARG SER ILE GLU ALA THR VAL GLY LEU THR
SEQRES 14 A 274 PRO TRP ASN LEU ASP LYS THR TRP PRO GLU VAL GLU ALA
SEQRES 15 A 274 ALA SER LEU GLU ILE GLY ALA GLN ASN ASP THR VAL ALA
SEQRES 16 A 274 PRO PRO GLY SER HIS ALA ILE PRO PHE TYR ASN SER LEU
SEQRES 17 A 274 THR ASN ALA GLU ARG ARG ALA TYR LEU GLU LEU ARG GLY
SEQRES 18 A 274 ALA SER HIS PHE ALA PRO ASN THR SER ASN THR THR ILE
SEQRES 19 A 274 ALA LYS TYR THR ILE ALA TRP LEU LYS ARG TYR VAL ASP
SEQRES 20 A 274 ASP ASP THR ARG TYR GLU GLN PHE ILE SER PRO GLY PRO
SEQRES 21 A 274 SER PRO SER LEU THR ASN GLY ILE SER ASP TYR ARG ILE
SEQRES 22 A 274 GLN
HET PMS A 301 17
HET NA A 302 1
HETNAM PMS PHENYLMETHANESULFONIC ACID
HETNAM NA SODIUM ION
FORMUL 2 PMS C7 H8 O3 S
FORMUL 3 NA NA 1+
FORMUL 4 HOH *309(H2 O)
HELIX 1 AA1 HIS A 19 ALA A 28 1 10
HELIX 2 AA2 THR A 39 ALA A 45 1 7
HELIX 3 AA3 ALA A 93 GLN A 98 5 6
HELIX 4 AA4 TRP A 99 SER A 106 1 8
HELIX 5 AA5 GLN A 122 ASP A 140 1 19
HELIX 6 AA6 VAL A 143 SER A 145 5 3
HELIX 7 AA7 SER A 158 ARG A 171 1 14
HELIX 8 AA8 HIS A 212 LEU A 220 1 9
HELIX 9 AA9 PHE A 237 THR A 241 5 5
HELIX 10 AB1 ASN A 243 ASP A 259 1 17
HELIX 11 AB2 ASP A 261 ARG A 263 5 3
HELIX 12 AB3 TYR A 264 SER A 269 1 6
SHEET 1 AA1 9 VAL A 52 ILE A 57 0
SHEET 2 AA1 9 GLY A 68 PRO A 73 -1 O ILE A 70 N LYS A 55
SHEET 3 AA1 9 VAL A 110 ILE A 114 -1 O VAL A 111 N TYR A 71
SHEET 4 AA1 9 PHE A 81 SER A 87 1 N VAL A 84 O ILE A 112
SHEET 5 AA1 9 ILE A 147 HIS A 157 1 O ASP A 148 N PHE A 81
SHEET 6 AA1 9 ALA A 176 LEU A 180 1 O LEU A 180 N GLY A 156
SHEET 7 AA1 9 ALA A 195 ALA A 201 1 O ILE A 199 N GLY A 179
SHEET 8 AA1 9 ARG A 226 LEU A 231 1 O LEU A 231 N GLY A 200
SHEET 9 AA1 9 ILE A 280 GLN A 286 -1 O ASP A 282 N GLU A 230
LINK OG SER A 158 S PMS A 301 1555 1555 1.57
LINK OE1 GLU A 175 NA NA A 302 1555 1555 2.38
LINK O TYR A 257 NA NA A 302 1555 1555 2.28
LINK OD1AASP A 260 NA NA A 302 1555 1555 2.40
LINK NA NA A 302 O HOH A 402 1555 1555 2.37
LINK NA NA A 302 O HOH A 591 1555 1555 2.55
LINK NA NA A 302 O HOH A 638 1555 1555 2.51
CISPEP 1 SER A 269 PRO A 270 0 3.73
CRYST1 36.213 76.054 82.187 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 0.027614 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012167 0.00000
TER 4261 GLN A 286
MASTER 343 0 2 12 9 0 0 6 2333 1 26 22
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