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HEADER HYDROLASE 19-DEC-23 8VEK
TITLE ISPETASE - ACC MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PISCINIBACTER SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, PROTEIN ENGINEERING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.JOHO,S.ROYAN,S.NEWTON,A.T.CAPUTO,A.ARDEVOL GRAU,C.JACKSON
REVDAT 1 19-JUN-24 8VEK 0
JRNL AUTH Y.JOHO,S.ROYAN,A.T.CAPUTO,S.NEWTON,T.S.PEAT,J.NEWMAN,
JRNL AUTH 2 C.JACKSON,A.ARDEVOL
JRNL TITL ENHANCING PET DEGRADING ENZYMES: A COMBINATORY APPROACH.
JRNL REF CHEMBIOCHEM V. 25 00084 2024
JRNL REFN ESSN 1439-7633
JRNL PMID 38584134
JRNL DOI 10.1002/CBIC.202400084
REMARK 2
REMARK 2 RESOLUTION. 1.14 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) : 1.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.6
REMARK 3 NUMBER OF REFLECTIONS : 78462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 3857
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 31.2500 - 3.4500 0.99 3684 196 0.1308 0.1481
REMARK 3 2 3.4500 - 2.7400 1.00 3574 178 0.1348 0.1571
REMARK 3 3 2.7400 - 2.3900 1.00 3532 182 0.1302 0.1575
REMARK 3 4 2.3900 - 2.1700 0.99 3507 181 0.1190 0.1324
REMARK 3 5 2.1700 - 2.0200 0.99 3490 158 0.1167 0.1424
REMARK 3 6 2.0200 - 1.9000 0.99 3454 178 0.1172 0.1498
REMARK 3 7 1.9000 - 1.8000 0.99 3475 169 0.1203 0.1481
REMARK 3 8 1.8000 - 1.7200 0.99 3442 200 0.1169 0.1293
REMARK 3 9 1.7200 - 1.6600 0.99 3433 177 0.1082 0.1195
REMARK 3 10 1.6600 - 1.6000 0.99 3426 171 0.1021 0.1415
REMARK 3 11 1.6000 - 1.5500 0.98 3384 178 0.0985 0.1422
REMARK 3 12 1.5500 - 1.5100 0.98 3384 214 0.1045 0.1290
REMARK 3 13 1.5100 - 1.4700 0.98 3399 172 0.1123 0.1410
REMARK 3 14 1.4700 - 1.4300 0.98 3383 166 0.1174 0.1646
REMARK 3 15 1.4300 - 1.4000 0.98 3374 179 0.1275 0.1552
REMARK 3 16 1.4000 - 1.3700 0.98 3361 189 0.1306 0.1771
REMARK 3 17 1.3700 - 1.3400 0.97 3346 168 0.1443 0.1647
REMARK 3 18 1.3400 - 1.3200 0.97 3363 172 0.1498 0.1844
REMARK 3 19 1.3200 - 1.2900 0.94 3239 157 0.1652 0.1958
REMARK 3 20 1.2900 - 1.2700 0.82 2837 135 0.1705 0.2388
REMARK 3 21 1.2700 - 1.2500 0.64 2193 118 0.1707 0.2200
REMARK 3 22 1.2500 - 1.2300 0.44 1504 79 0.1751 0.2206
REMARK 3 23 1.2300 - 1.2100 0.30 1041 49 0.1744 0.2252
REMARK 3 24 1.2100 - 1.2000 0.21 720 34 0.1958 0.1683
REMARK 3 25 1.2000 - 1.1800 0.14 492 24 0.2007 0.1917
REMARK 3 26 1.1800 - 1.1600 0.10 336 21 0.2065 0.1548
REMARK 3 27 1.1600 - 1.1500 0.05 173 11 0.2200 0.3319
REMARK 3 28 1.1500 - 1.1400 0.02 59 1 0.2329 0.1496
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.081
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.683
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.41
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 : 0.016 2150
REMARK 3 ANGLE : 1.439 2964
REMARK 3 CHIRALITY : 0.111 328
REMARK 3 PLANARITY : 0.016 393
REMARK 3 DIHEDRAL : 13.311 793
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 8VEK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1000280040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-19
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89827
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.140
REMARK 200 RESOLUTION RANGE LOW (A) : 51.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 1.70300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.208 M AMMONIUM SULFATE, 23.2 W/V
REMARK 280 POLYETHYLENE GLYCOL 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 25.38200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.64900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.64900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.38200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.20500
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 27
REMARK 465 GLY A 28
REMARK 465 ALA A 291
REMARK 465 SER A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
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 HG SER A 188 O HOH A 401 1.53
REMARK 500 O PRO A 210 HG SER A 214 1.59
REMARK 500 OG SER A 188 O HOH A 401 2.12
REMARK 500 O HOH A 404 O HOH A 637 2.19
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 ASN A 73 46.59 -144.08
REMARK 500 THR A 88 -9.28 74.63
REMARK 500 SER A 160 -116.66 62.90
REMARK 500 SER A 214 -81.41 -127.08
REMARK 500 SER A 214 -83.22 -126.07
REMARK 500 SER A 214 -83.84 -125.50
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 123 0.12 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 727 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 728 DISTANCE = 6.53 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8VE9 RELATED DB: PDB
REMARK 900 DIFFERENT POINT MUTANTS OF SAME ENZYME
DBREF1 8VEK A 30 290 UNP PETH_IDESA
DBREF2 8VEK A A0A0K8P6T7 30 290
SEQADV 8VEK MET A 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8VEK GLY A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK SER A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK ALA A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8VEK CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8VEK CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 8VEK ALA A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK SER A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEK HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLY SER ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ALA SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL CYS ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER ALA SER HIS HIS HIS HIS HIS HIS
HET GOL A 301 14
HET GOL A 302 14
HET SO4 A 303 5
HET SO4 A 304 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 HOH *328(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 PHE A 106 1 11
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N GLY A 79 O VAL A 107
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.07
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.06
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.07
CRYST1 50.764 68.410 79.298 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 0.019699 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012611 0.00000
TER 4077 SER A 290
MASTER 302 0 4 9 9 0 0 6 2269 1 44 21
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