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HEADER HYDROLASE 25-DEC-24 9L75
TITLE A NOVEL PE HYDROLASE AND ITS STRUCTURAL BASIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VREELANDELLA VENUSTA;
SOURCE 3 ORGANISM_TAXID: 44935;
SOURCE 4 GENE: JDS37_04195;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYETHYLENE, PE-DEGRADING ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.S.WANG,D.Y.SUN,H.H.JIA,Y.Z.SUN,L.N.QIU
REVDAT 1 31-DEC-25 9L75 0
JRNL AUTH Y.S.WANG,D.Y.SUN,H.H.JIA,Y.Z.SUN,L.N.QIU
JRNL TITL A NOVEL PE HYDROLASE AND ITS STRUCTURAL BASIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 1.20.1_4487
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 : FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.360
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24571
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1180
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 (A) : 2.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.84
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.54
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2933
REMARK 3 BIN R VALUE (WORKING SET) : 0.2961
REMARK 3 BIN FREE R VALUE : 0.3779
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 105
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 : 4270
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.04
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9L75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 27-DEC-24.
REMARK 100 THE DEPOSITION ID IS D_1300055014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-24
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 : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER D8 QUEST
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
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 : APEX 2
REMARK 200 DATA SCALING SOFTWARE : APEX 2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24571
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.720
REMARK 200 RESOLUTION RANGE LOW (A) : 42.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.43
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 42% PEG 200 0.1 M HEPES PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.66000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.33000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.49500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 9.16500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.82500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 84.71000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -146.72202
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -27.49500
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 VAL B 2
REMARK 465 PRO B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 VAL B 6
REMARK 465 ASP B 7
REMARK 465 PHE B 8
REMARK 465 ASP B 9
REMARK 465 THR B 10
REMARK 465 LEU B 11
REMARK 465 CYS B 12
REMARK 465 THR B 274
REMARK 465 PRO B 275
REMARK 465 GLY B 276
REMARK 465 THR B 277
REMARK 465 PRO B 278
REMARK 465 GLY B 279
REMARK 465 ALA B 280
REMARK 465 PRO B 281
REMARK 465 ALA B 282
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 OE1 GLU A 268 NH1 ARG A 272 2.17
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 59 -130.05 53.75
REMARK 500 THR A 102 -112.50 -103.78
REMARK 500 SER A 122 -128.84 47.06
REMARK 500 TYR A 135 54.99 -109.45
REMARK 500 ARG A 272 5.55 -60.93
REMARK 500 PRO A 281 170.32 -59.34
REMARK 500 GLU B 14 144.40 -36.39
REMARK 500 ARG B 59 -126.38 45.22
REMARK 500 THR B 102 -112.79 -108.10
REMARK 500 SER B 122 -127.56 59.84
REMARK 500 HIS B 201 37.85 -91.55
REMARK 500 ARG B 272 11.60 -69.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9L75 A 2 275 UNP A0AAQ0CHA8_9GAMM
DBREF2 9L75 A A0AAQ0CHA8 2 275
DBREF1 9L75 B 2 275 UNP A0AAQ0CHA8_9GAMM
DBREF2 9L75 B A0AAQ0CHA8 2 275
SEQADV 9L75 PHE A 8 UNP A0AAQ0CHA SER 8 CONFLICT
SEQADV 9L75 ASN A 181 UNP A0AAQ0CHA LYS 181 CONFLICT
SEQADV 9L75 GLY A 233 UNP A0AAQ0CHA ARG 233 CONFLICT
SEQADV 9L75 GLY A 276 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 THR A 277 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 PRO A 278 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 GLY A 279 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 ALA A 280 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 PRO A 281 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 ALA A 282 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 PHE B 8 UNP A0AAQ0CHA SER 8 CONFLICT
SEQADV 9L75 ASN B 181 UNP A0AAQ0CHA LYS 181 CONFLICT
SEQADV 9L75 GLY B 233 UNP A0AAQ0CHA ARG 233 CONFLICT
SEQADV 9L75 GLY B 276 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 THR B 277 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 PRO B 278 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 GLY B 279 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 ALA B 280 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 PRO B 281 UNP A0AAQ0CHA EXPRESSION TAG
SEQADV 9L75 ALA B 282 UNP A0AAQ0CHA EXPRESSION TAG
SEQRES 1 A 281 VAL PRO THR THR VAL ASP PHE ASP THR LEU CYS PRO GLU
SEQRES 2 A 281 PRO ILE PHE GLN ASP ARG TRP VAL ALA THR PRO ARG GLY
SEQRES 3 A 281 ARG VAL PHE THR ARG THR TRP GLU THR SER HIS LEU ARG
SEQRES 4 A 281 SER ASP VAL PRO ILE VAL LEU LEU HIS ASP SER LEU GLY
SEQRES 5 A 281 CYS VAL ASP LEU TRP ARG SER PHE PRO ALA ALA LEU CYS
SEQRES 6 A 281 ALA ALA THR GLN ARG ARG VAL ILE ALA TYR ASP ARG LEU
SEQRES 7 A 281 GLY PHE GLY ARG SER ASP ALA CYS LEU THR PRO PRO LEU
SEQRES 8 A 281 LEU SER PHE ILE ASP ASP GLU PRO SER THR SER PHE ALA
SEQRES 9 A 281 ALA LEU GLN SER ALA PHE GLN LEU THR HIS PHE ILE ALA
SEQRES 10 A 281 LEU GLY HIS SER VAL GLY GLY CYS MET ALA VAL HIS CYS
SEQRES 11 A 281 ALA GLY GLN TYR VAL GLU GLN CYS GLN GLY LEU ILE THR
SEQRES 12 A 281 ILE ALA ALA GLN ALA VAL ASN GLU PRO ARG THR GLN GLN
SEQRES 13 A 281 GLY ILE GLU GLU ALA ARG ALA ALA PHE GLN MET PRO GLU
SEQRES 14 A 281 GLN PHE ALA LYS LEU GLU LYS TYR HIS GLY ASN LYS ALA
SEQRES 15 A 281 ARG TRP VAL LEU ASN GLY TRP ILE ASP THR TRP LEU HIS
SEQRES 16 A 281 PRO ALA PHE GLU HIS TRP SER LEU THR PRO ALA LEU GLN
SEQRES 17 A 281 HIS VAL HIS CYS PRO THR LEU VAL LEU HIS GLY GLU ASN
SEQRES 18 A 281 ASP GLU TYR GLY SER HIS ARG GLN PRO GLU GLY ILE ALA
SEQRES 19 A 281 ARG HIS THR ARG GLY PRO ALA HIS THR GLU ILE LEU PRO
SEQRES 20 A 281 GLY VAL GLY HIS VAL PRO HIS ARG GLU VAL GLU ALA VAL
SEQRES 21 A 281 VAL VAL HIS TYR VAL SER GLU PHE ILE GLU ARG LEU THR
SEQRES 22 A 281 PRO GLY THR PRO GLY ALA PRO ALA
SEQRES 1 B 281 VAL PRO THR THR VAL ASP PHE ASP THR LEU CYS PRO GLU
SEQRES 2 B 281 PRO ILE PHE GLN ASP ARG TRP VAL ALA THR PRO ARG GLY
SEQRES 3 B 281 ARG VAL PHE THR ARG THR TRP GLU THR SER HIS LEU ARG
SEQRES 4 B 281 SER ASP VAL PRO ILE VAL LEU LEU HIS ASP SER LEU GLY
SEQRES 5 B 281 CYS VAL ASP LEU TRP ARG SER PHE PRO ALA ALA LEU CYS
SEQRES 6 B 281 ALA ALA THR GLN ARG ARG VAL ILE ALA TYR ASP ARG LEU
SEQRES 7 B 281 GLY PHE GLY ARG SER ASP ALA CYS LEU THR PRO PRO LEU
SEQRES 8 B 281 LEU SER PHE ILE ASP ASP GLU PRO SER THR SER PHE ALA
SEQRES 9 B 281 ALA LEU GLN SER ALA PHE GLN LEU THR HIS PHE ILE ALA
SEQRES 10 B 281 LEU GLY HIS SER VAL GLY GLY CYS MET ALA VAL HIS CYS
SEQRES 11 B 281 ALA GLY GLN TYR VAL GLU GLN CYS GLN GLY LEU ILE THR
SEQRES 12 B 281 ILE ALA ALA GLN ALA VAL ASN GLU PRO ARG THR GLN GLN
SEQRES 13 B 281 GLY ILE GLU GLU ALA ARG ALA ALA PHE GLN MET PRO GLU
SEQRES 14 B 281 GLN PHE ALA LYS LEU GLU LYS TYR HIS GLY ASN LYS ALA
SEQRES 15 B 281 ARG TRP VAL LEU ASN GLY TRP ILE ASP THR TRP LEU HIS
SEQRES 16 B 281 PRO ALA PHE GLU HIS TRP SER LEU THR PRO ALA LEU GLN
SEQRES 17 B 281 HIS VAL HIS CYS PRO THR LEU VAL LEU HIS GLY GLU ASN
SEQRES 18 B 281 ASP GLU TYR GLY SER HIS ARG GLN PRO GLU GLY ILE ALA
SEQRES 19 B 281 ARG HIS THR ARG GLY PRO ALA HIS THR GLU ILE LEU PRO
SEQRES 20 B 281 GLY VAL GLY HIS VAL PRO HIS ARG GLU VAL GLU ALA VAL
SEQRES 21 B 281 VAL VAL HIS TYR VAL SER GLU PHE ILE GLU ARG LEU THR
SEQRES 22 B 281 PRO GLY THR PRO GLY ALA PRO ALA
HET PEG A 301 7
HET PEG A 302 7
HET PEG A 303 7
HET PEG B 301 7
HET PEG B 302 7
HET PEG B 303 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 PEG 6(C4 H10 O3)
FORMUL 9 HOH *50(H2 O)
HELIX 1 AA1 THR A 4 ASP A 9 5 6
HELIX 2 AA2 CYS A 54 ARG A 59 5 6
HELIX 3 AA3 SER A 60 GLN A 70 1 11
HELIX 4 AA4 SER A 94 GLU A 99 1 6
HELIX 5 AA5 THR A 102 PHE A 111 1 10
HELIX 6 AA6 SER A 122 TYR A 135 1 14
HELIX 7 AA7 GLU A 152 PHE A 166 1 15
HELIX 8 AA8 MET A 168 GLY A 180 1 13
HELIX 9 AA9 LYS A 182 LEU A 195 1 14
HELIX 10 AB1 HIS A 196 GLU A 200 5 5
HELIX 11 AB2 LEU A 204 GLN A 209 1 6
HELIX 12 AB3 HIS A 228 THR A 238 1 11
HELIX 13 AB4 VAL A 253 VAL A 258 1 6
HELIX 14 AB5 VAL A 258 ARG A 272 1 15
HELIX 15 AB6 CYS B 54 ARG B 59 5 6
HELIX 16 AB7 SER B 60 GLN B 70 1 11
HELIX 17 AB8 SER B 94 GLU B 99 1 6
HELIX 18 AB9 THR B 102 PHE B 111 1 10
HELIX 19 AC1 SER B 122 TYR B 135 1 14
HELIX 20 AC2 GLU B 152 GLN B 167 1 16
HELIX 21 AC3 MET B 168 GLY B 180 1 13
HELIX 22 AC4 LYS B 182 LEU B 195 1 14
HELIX 23 AC5 HIS B 196 GLU B 200 5 5
HELIX 24 AC6 LEU B 204 GLN B 209 1 6
HELIX 25 AC7 HIS B 228 THR B 238 1 11
HELIX 26 AC8 VAL B 253 VAL B 258 1 6
HELIX 27 AC9 VAL B 258 ARG B 272 1 15
SHEET 1 AA1 8 ILE A 16 THR A 24 0
SHEET 2 AA1 8 GLY A 27 GLU A 35 -1 O VAL A 29 N VAL A 22
SHEET 3 AA1 8 VAL A 73 TYR A 76 -1 O VAL A 73 N TRP A 34
SHEET 4 AA1 8 ILE A 45 LEU A 48 1 N LEU A 47 O ILE A 74
SHEET 5 AA1 8 PHE A 116 HIS A 121 1 O ILE A 117 N VAL A 46
SHEET 6 AA1 8 CYS A 139 ILE A 145 1 O GLN A 140 N PHE A 116
SHEET 7 AA1 8 THR A 215 GLY A 220 1 O LEU A 218 N THR A 144
SHEET 8 AA1 8 ALA A 242 LEU A 247 1 O LEU A 247 N HIS A 219
SHEET 1 AA2 8 ILE B 16 VAL B 22 0
SHEET 2 AA2 8 VAL B 29 GLU B 35 -1 O VAL B 29 N VAL B 22
SHEET 3 AA2 8 VAL B 73 TYR B 76 -1 O ALA B 75 N ARG B 32
SHEET 4 AA2 8 ILE B 45 LEU B 48 1 N ILE B 45 O ILE B 74
SHEET 5 AA2 8 PHE B 116 HIS B 121 1 O LEU B 119 N LEU B 48
SHEET 6 AA2 8 CYS B 139 ILE B 145 1 O GLN B 140 N PHE B 116
SHEET 7 AA2 8 THR B 215 GLY B 220 1 O LEU B 218 N THR B 144
SHEET 8 AA2 8 ALA B 242 LEU B 247 1 O HIS B 243 N VAL B 217
CISPEP 1 GLU A 14 PRO A 15 0 -5.21
CRYST1 169.420 169.420 54.990 90.00 90.00 120.00 P 65 12
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 0.005902 0.003408 0.000000 0.00000
SCALE2 0.000000 0.006816 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018185 0.00000
TER 2204 ALA A 282
TER 4272 LEU B 273
MASTER 283 0 6 27 16 0 0 6 4362 2 42 44
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