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HEADER HYDROLASE 17-DEC-21 7QJN
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA-HYDROLASE ENZYME FROM CANDIDATUS
TITLE 2 KRYPTOBACTER TENGCHONGENSIS (306)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA/BETA-HYDROLASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: ALPHA/BETA-HYDROLASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDATUS KRYPTOBACTER TENGCHONGENSIS;
SOURCE 3 ORGANISM_TAXID: 1643429;
SOURCE 4 GENE: JGI24_00892;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,R.S.GILL,E.ERICKSON,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJN 0
JRNL AUTH E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,
JRNL AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,
JRNL AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,
JRNL AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)
JRNL TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY
JRNL REF NAT COMMUN V. 13 7850 2022
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-022-35237-X
REMARK 2
REMARK 2 RESOLUTION. 1.89 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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 46.5
REMARK 3 NUMBER OF REFLECTIONS : 14489
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 663
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.44
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) : 0.2943
REMARK 3 BIN FREE R VALUE : 0.3943
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 18
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 : 2216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.82280
REMARK 3 B22 (A**2) : 5.82280
REMARK 3 B33 (A**2) : -11.64570
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) : 0.330
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.347
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.244
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.336
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.244
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 : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2276 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3074 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 792 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 380 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2276 ; 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 : 297 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
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 : 1918 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.97
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.54
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9748 -32.1109 -11.6147
REMARK 3 T TENSOR
REMARK 3 T11: -0.0145 T22: 0.0201
REMARK 3 T33: -0.2231 T12: 0.0619
REMARK 3 T13: 0.0532 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 1.3011 L22: 1.3716
REMARK 3 L33: 3.758 L12: -0.1688
REMARK 3 L13: 0.8619 L23: 0.7122
REMARK 3 S TENSOR
REMARK 3 S11: 0.1443 S12: -0.132 S13: 0.2076
REMARK 3 S21: -0.132 S22: -0.2163 S23: 0.3402
REMARK 3 S31: 0.2076 S32: 0.3402 S33: 0.072
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7QJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1292118049.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-21
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14490
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 64.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 17.70
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.84100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: ALPHAFOLD MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE / POTASSIUM PHOSPHATE DIBASIC PH 5.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 77.67667
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 38.83833
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 38.83833
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 77.67667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 HOH A 466 LIES ON A SPECIAL POSITION.
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 ASN A 78
REMARK 465 LYS A 79
REMARK 465 VAL A 173
REMARK 465 PRO A 174
REMARK 465 ASP A 175
REMARK 465 SER A 176
REMARK 465 VAL A 177
REMARK 465 LEU A 284
REMARK 465 GLU A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
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 SER A 124 -117.47 54.37
REMARK 500 GLU A 138 0.10 -69.95
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7QJN A 1 283 UNP A0A656D8B6_9BACT
DBREF2 7QJN A A0A656D8B6 1 283
SEQADV 7QJN LEU A 284 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN GLU A 285 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 286 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 287 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 288 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 289 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 290 UNP A0A656D8B EXPRESSION TAG
SEQADV 7QJN HIS A 291 UNP A0A656D8B EXPRESSION TAG
SEQRES 1 A 291 MET LYS VAL LYS SER LYS PRO LEU THR LEU TYR ASN VAL
SEQRES 2 A 291 SER GLY ASP ARG ILE THR ALA ASP VAL HIS PHE VAL GLU
SEQRES 3 A 291 SER PHE LEU PRO ALA PRO VAL VAL ILE TYR SER HIS GLY
SEQRES 4 A 291 PHE LEU GLY PHE LYS ASP TRP GLY PHE ILE PRO TYR VAL
SEQRES 5 A 291 ALA GLU ARG PHE ALA GLU ASN GLY PHE VAL PHE VAL ARG
SEQRES 6 A 291 PHE ASN PHE SER HIS ASN GLY ILE GLY GLU ASN PRO ASN
SEQRES 7 A 291 LYS ILE THR GLU PHE ASP LYS LEU ALA LYS ASN THR ILE
SEQRES 8 A 291 SER LYS GLN ILE GLU ASP LEU THR ALA VAL ILE GLU TYR
SEQRES 9 A 291 VAL PHE SER ASP GLU PHE GLY VAL LEU ASN ASP GLY GLN
SEQRES 10 A 291 LEU PHE LEU LEU GLY HIS SER GLY GLY GLY GLY ILE SER
SEQRES 11 A 291 ILE ILE LYS ALA VAL GLU ASP GLU ARG VAL ARG ALA LEU
SEQRES 12 A 291 ALA LEU TRP ALA SER ILE SER THR PHE ARG ARG TYR SER
SEQRES 13 A 291 LYS HIS GLN ILE GLU GLU LEU GLU LYS ASN GLY TYR ILE
SEQRES 14 A 291 PHE VAL ARG VAL PRO ASP SER VAL ILE GLN VAL LYS ILE
SEQRES 15 A 291 GLU LYS ILE VAL TYR ASP ASP PHE VAL GLU ASN SER GLU
SEQRES 16 A 291 ARG TYR ASP ILE ILE LYS ALA ILE SER LYS LEU LYS ILE
SEQRES 17 A 291 PRO ILE LEU ILE VAL HIS GLY THR ALA ASP ALA ILE VAL
SEQRES 18 A 291 PRO LEU ALA GLU ALA GLU LYS LEU ARG ASN SER ASN PRO
SEQRES 19 A 291 GLU TYR THR LYS LEU VAL LEU ILE SER GLY ALA ASN HIS
SEQRES 20 A 291 LEU PHE ASN VAL LYS HIS PRO MET GLU HIS SER THR ASP
SEQRES 21 A 291 GLN LEU ASP LYS ALA ILE ASP GLU THR VAL LEU PHE PHE
SEQRES 22 A 291 LYS LYS ILE ILE GLU ASN LYS LYS ALA ASP LEU GLU HIS
SEQRES 23 A 291 HIS HIS HIS HIS HIS
HET PO4 A 301 5
HET PO4 A 302 5
HET PO4 A 303 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 3(O4 P 3-)
FORMUL 5 HOH *108(H2 O)
HELIX 1 AA1 VAL A 25 LEU A 29 5 5
HELIX 2 AA2 PHE A 48 ASN A 59 1 12
HELIX 3 AA3 GLU A 82 ALA A 87 1 6
HELIX 4 AA4 THR A 90 PHE A 106 1 17
HELIX 5 AA5 GLY A 125 ASP A 137 1 13
HELIX 6 AA6 SER A 156 GLY A 167 1 12
HELIX 7 AA7 LYS A 184 GLU A 192 1 9
HELIX 8 AA8 ASP A 198 LEU A 206 1 9
HELIX 9 AA9 PRO A 222 ASN A 233 1 12
HELIX 10 AB1 THR A 259 ASP A 283 1 25
SHEET 1 AA1 8 LYS A 4 TYR A 11 0
SHEET 2 AA1 8 ARG A 17 PHE A 24 -1 O ILE A 18 N LEU A 10
SHEET 3 AA1 8 VAL A 62 PHE A 66 -1 O PHE A 63 N HIS A 23
SHEET 4 AA1 8 ALA A 31 SER A 37 1 N TYR A 36 O VAL A 64
SHEET 5 AA1 8 ASN A 114 HIS A 123 1 O GLN A 117 N VAL A 33
SHEET 6 AA1 8 VAL A 140 TRP A 146 1 O TRP A 146 N GLY A 122
SHEET 7 AA1 8 ILE A 210 GLY A 215 1 O VAL A 213 N LEU A 145
SHEET 8 AA1 8 THR A 237 ILE A 242 1 O LYS A 238 N ILE A 212
SHEET 1 AA2 2 TYR A 168 VAL A 171 0
SHEET 2 AA2 2 VAL A 180 GLU A 183 -1 O ILE A 182 N ILE A 169
CISPEP 1 LEU A 29 PRO A 30 0 1.15
CISPEP 2 HIS A 253 PRO A 254 0 5.80
CRYST1 74.920 74.920 116.515 90.00 90.00 120.00 P 32 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 0.013348 0.007706 0.000000 0.00000
SCALE2 0.000000 0.015412 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008583 0.00000
TER 2217 ASP A 283
MASTER 290 0 3 10 10 0 0 6 2339 1 15 23
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