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HEADER BIOSYNTHETIC PROTEIN 13-JUN-22 8DAJ
TITLE STRUCTURE AND BIOCHEMISTRY OF A PROMISCUOUS THERMOPHILIC
TITLE 2 POLYHYDROXYBUTYRATE DEPOLYMERASE FROM LIHUAXUELLA THERMOPHILIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE, PHB DEPOLYMERASE FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLYHYDROXYBUTYRATE DEPOLYMERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LIHUAXUELLA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 1173111;
SOURCE 4 GENE: SAMN05444955_11823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOPLASTIC, THERMOPHILE, ENZYME, POLYHYDROXYALKANOATES, BIOSYNTHETIC
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.THOMAS,S.QUIRK,D.J.E.HUARD,R.L.LIEBERMAN
REVDAT 1 15-FEB-23 8DAJ 0
JRNL AUTH G.M.THOMAS,S.QUIRK,D.J.E.HUARD,R.L.LIEBERMAN
JRNL TITL BIOPLASTIC DEGRADATION BY A POLYHYDROXYBUTYRATE DEPOLYMERASE
JRNL TITL 2 FROM A THERMOPHILIC SOIL BACTERIUM.
JRNL REF PROTEIN SCI. V. 31 E4470 2022
JRNL REFN ESSN 1469-896X
JRNL PMID 36222314
JRNL DOI 10.1002/PRO.4470
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.THOMAS,S.QUIRK,D.J.E.HUARD,R.L.LIEBERMAN
REMARK 1 TITL STRUCTURE AND BIOCHEMISTRY OF A PROMISCUOUS THERMOPHILIC
REMARK 1 TITL 2 POLYHYDROXYBUTYRATE DEPOLYMERASE FROM LIHUAXUELLA
REMARK 1 TITL 3 THERMOPHILIA
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 148631
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) : 0.163
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.560
REMARK 3 FREE R VALUE TEST SET COUNT : 3802
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 36.9300 - 3.6000 1.00 5528 151 0.1408 0.1627
REMARK 3 2 3.6000 - 2.8600 1.00 5484 152 0.1481 0.1433
REMARK 3 3 2.8600 - 2.5000 1.00 5564 158 0.1597 0.1756
REMARK 3 4 2.5000 - 2.2700 1.00 5457 141 0.1549 0.1902
REMARK 3 5 2.2700 - 2.1100 1.00 5575 150 0.1479 0.1456
REMARK 3 6 2.1100 - 1.9800 1.00 5440 144 0.1534 0.1592
REMARK 3 7 1.9800 - 1.8800 1.00 5570 142 0.1575 0.1796
REMARK 3 8 1.8800 - 1.8000 1.00 5529 150 0.1680 0.1935
REMARK 3 9 1.8000 - 1.7300 1.00 5587 142 0.1553 0.1426
REMARK 3 10 1.7300 - 1.6700 1.00 5480 150 0.1588 0.1509
REMARK 3 11 1.6700 - 1.6200 1.00 5509 152 0.1658 0.1714
REMARK 3 12 1.6200 - 1.5700 1.00 5497 146 0.1672 0.1684
REMARK 3 13 1.5700 - 1.5300 1.00 5593 146 0.1660 0.2243
REMARK 3 14 1.5300 - 1.4900 1.00 5483 150 0.1778 0.2002
REMARK 3 15 1.4900 - 1.4600 1.00 5526 146 0.1799 0.2556
REMARK 3 16 1.4600 - 1.4300 1.00 5475 138 0.1814 0.2085
REMARK 3 17 1.4300 - 1.4000 1.00 5537 147 0.1820 0.1990
REMARK 3 18 1.4000 - 1.3700 1.00 5553 140 0.1856 0.2158
REMARK 3 19 1.3700 - 1.3500 1.00 5556 142 0.1903 0.2303
REMARK 3 20 1.3500 - 1.3300 1.00 5527 136 0.1870 0.2039
REMARK 3 21 1.3300 - 1.3000 1.00 5477 134 0.1943 0.2017
REMARK 3 22 1.3000 - 1.2800 0.99 5530 141 0.2045 0.1934
REMARK 3 23 1.2800 - 1.2700 0.97 5267 134 0.2184 0.2085
REMARK 3 24 1.2700 - 1.2500 0.95 5332 136 0.2266 0.2478
REMARK 3 25 1.2500 - 1.2300 0.93 5044 136 0.2299 0.2192
REMARK 3 26 1.2300 - 1.2200 0.90 5062 124 0.2625 0.3109
REMARK 3 27 1.2200 - 1.2000 0.48 2647 74 0.3165 0.3645
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.123
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.57
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 : 0.005 2506
REMARK 3 ANGLE : 0.961 3410
REMARK 3 CHIRALITY : 0.109 348
REMARK 3 PLANARITY : 0.008 464
REMARK 3 DIHEDRAL : 6.371 370
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 8DAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1000266161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-21
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 36.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 16.70
REMARK 200 R MERGE (I) : 0.13390
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47280
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.510
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
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 (%): 36.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRATE PH 5.6, 18% PROPANOL, AND
REMARK 280 20% PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 70.42000
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 140.84000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 140.84000
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 70.42000
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 C1 IPA A 406 LIES ON A SPECIAL POSITION.
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 O2 EDO A 407 O HOH A 501 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 236 CB - CA - C ANGL. DEV. = 14.7 DEGREES
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 41 -11.32 72.13
REMARK 500 ASN A 61 63.22 66.40
REMARK 500 SER A 121 -120.27 65.22
REMARK 500 ASP A 168 111.71 -32.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8DAJ A 3 302 UNP A0A1H8IKU3_9BACL
DBREF2 8DAJ A A0A1H8IKU3 34 333
SEQADV 8DAJ GLY A 1 UNP A0A1H8IKU EXPRESSION TAG
SEQADV 8DAJ PRO A 2 UNP A0A1H8IKU EXPRESSION TAG
SEQRES 1 A 302 GLY PRO ALA GLY GLN PHE ILE ARG ASP THR ALA PRO ASP
SEQRES 2 A 302 GLY ARG VAL TYR LYS LEU TYR ILE PRO SER GLY TYR ASN
SEQRES 3 A 302 GLY SER THR PRO LEU PRO LEU VAL VAL MET LEU HIS GLY
SEQRES 4 A 302 CYS THR GLN ASN PRO ASP ASP PHE ALA ALA GLY THR GLU
SEQRES 5 A 302 MET ASN VAL TYR ALA GLU GLN ASN ASN PHE LEU VAL ALA
SEQRES 6 A 302 TYR PRO GLU GLN PRO SER SER ALA ASN LEU ASN LYS CYS
SEQRES 7 A 302 TRP ASN TRP PHE ASP SER ASN HIS GLN SER ARG GLY ARG
SEQRES 8 A 302 GLY GLU PRO ALA SER ILE ALA GLY VAL VAL GLU ASP VAL
SEQRES 9 A 302 LYS ARG ASN TYR SER VAL ASP SER ARG ARG VAL TYR ALA
SEQRES 10 A 302 ALA GLY LEU SER ALA GLY GLY ALA MET SER VAL ILE MET
SEQRES 11 A 302 GLY ALA THR TYR PRO ASP VAL PHE ALA ALA ILE GLY VAL
SEQRES 12 A 302 GLY SER GLY LEU GLU TYR LYS ALA ALA THR SER MET THR
SEQRES 13 A 302 SER ALA TYR MET ALA MET ILE ASN GLY GLY PRO ASP PRO
SEQRES 14 A 302 VAL GLN GLN GLY ASN LEU ALA TYR GLN ALA MET GLY SER
SEQRES 15 A 302 HIS ALA ARG VAL VAL PRO VAL ILE VAL PHE HIS GLY THR
SEQRES 16 A 302 SER ASP TYR THR VAL TYR PRO VAL ASN GLY HIS GLN VAL
SEQRES 17 A 302 ILE SER GLN TRP ALA GLN THR ASN ASP ARG ALA GLY ASP
SEQRES 18 A 302 GLY VAL ASP ASN ASN HIS ILE ASP ASP GLN ALA ASP VAL
SEQRES 19 A 302 THR MET ASN GLY SER VAL PRO ASN GLY ARG THR TYR THR
SEQRES 20 A 302 ARG TYR LEU TYR LYS ASP GLN ASN GLY ASN VAL VAL MET
SEQRES 21 A 302 GLU LYS ILE MET VAL ASN GLY MET GLY HIS ALA TRP SER
SEQRES 22 A 302 GLY GLY SER THR ALA GLY THR TYR THR ASP PRO ALA GLY
SEQRES 23 A 302 PRO GLU ALA SER SER MET MET TRP SER PHE PHE VAL ASN
SEQRES 24 A 302 HIS PRO LYS
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET IPA A 405 4
HET IPA A 406 4
HET EDO A 407 4
HET IPA A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET IPA A 412 4
HET EDO A 413 4
HET EDO A 414 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN IPA 2-PROPANOL
FORMUL 2 EDO 10(C2 H6 O2)
FORMUL 6 IPA 4(C3 H8 O)
FORMUL 16 HOH *334(H2 O)
HELIX 1 AA1 ASN A 43 GLU A 52 1 10
HELIX 2 AA2 GLU A 52 ASN A 61 1 10
HELIX 3 AA3 ASP A 83 GLN A 87 5 5
HELIX 4 AA4 ARG A 91 TYR A 108 1 18
HELIX 5 AA5 SER A 121 TYR A 134 1 14
HELIX 6 AA6 SER A 154 GLY A 165 1 12
HELIX 7 AA7 ASP A 168 GLY A 181 1 14
HELIX 8 AA8 SER A 182 ALA A 184 5 3
HELIX 9 AA9 PRO A 202 GLY A 220 1 19
HELIX 10 AB1 GLU A 288 ASN A 299 1 12
SHEET 1 AA110 GLN A 5 THR A 10 0
SHEET 2 AA110 VAL A 16 ILE A 21 -1 O ILE A 21 N GLN A 5
SHEET 3 AA110 LEU A 63 PRO A 67 -1 O VAL A 64 N TYR A 20
SHEET 4 AA110 LEU A 31 LEU A 37 1 N MET A 36 O ALA A 65
SHEET 5 AA110 VAL A 110 LEU A 120 1 O TYR A 116 N VAL A 35
SHEET 6 AA110 ALA A 140 GLY A 144 1 O GLY A 144 N GLY A 119
SHEET 7 AA110 VAL A 189 GLY A 194 1 O ILE A 190 N VAL A 143
SHEET 8 AA110 VAL A 258 VAL A 265 1 O ILE A 263 N VAL A 191
SHEET 9 AA110 THR A 245 LYS A 252 -1 N TYR A 249 O LYS A 262
SHEET 10 AA110 VAL A 234 SER A 239 -1 N MET A 236 O ARG A 248
SHEET 1 AA2 2 TRP A 272 SER A 273 0
SHEET 2 AA2 2 THR A 282 ASP A 283 1 O ASP A 283 N TRP A 272
SSBOND 1 CYS A 40 CYS A 78 1555 1555 2.04
CRYST1 45.510 45.510 211.260 90.00 90.00 120.00 P 31 2 1 6
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 0.021973 0.012686 0.000000 0.00000
SCALE2 0.000000 0.025372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004734 0.00000
TER 2390 LYS A 302
MASTER 287 0 14 10 12 0 0 6 2668 1 58 24
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