| content |
HEADER HYDROLASE 04-DEC-24 9HL5
TITLE CRYSTAL STRUCTURE OF HALO-TOLERANT PETASE FROM MARINE METAGENOME
TITLE 2 (HALOPETASE1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: FIRST (1, S) AND LAST (270, A) AMINO ACIDS ARE FROM
COMPND 6 FX-CLONING.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: BXT89_15940;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, HALO-TOLERANT, HYDROLASE, HALOPETASE, HALOPETASE1,
KEYWDS 2 POLYESTERASE, MARINE, METAGENOME
EXPDTA X-RAY DIFFRACTION
AUTHOR O.TURAK,M.KRIEGEL,B.HOCKER
REVDAT 1 01-OCT-25 9HL5 0
JRNL AUTH O.TURAK,A.GAGSTEIGER,A.UPADHYAY,M.KRIEGEL,P.SALEIN,
JRNL AUTH 2 S.BOHNKE-BRANDT,S.AGARWAL,E.BORCHERT,B.HOCKER
JRNL TITL A THIRD TYPE OF PETASE FROM THE MARINE HALOPSEUDOMONAS
JRNL TITL 2 LINEAGE.
JRNL REF PROTEIN SCI. V. 34 70305 2025
JRNL REFN ESSN 1469-896X
JRNL PMID 40960396
JRNL DOI 10.1002/PRO.70305
REMARK 2
REMARK 2 RESOLUTION. 1.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.1-5286
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) : 1.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 93271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.110
REMARK 3 R VALUE (WORKING SET) : 0.110
REMARK 3 FREE R VALUE : 0.129
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.240
REMARK 3 FREE R VALUE TEST SET COUNT : 2092
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 35.2700 - 2.8600 1.00 6412 147 0.1512 0.1664
REMARK 3 2 2.8600 - 2.2700 1.00 6177 142 0.1099 0.1162
REMARK 3 3 2.2700 - 1.9800 1.00 6138 141 0.0873 0.1017
REMARK 3 4 1.9800 - 1.8000 1.00 6087 140 0.0831 0.1099
REMARK 3 5 1.8000 - 1.6700 1.00 6093 140 0.0825 0.1077
REMARK 3 6 1.6700 - 1.5700 1.00 6072 139 0.0789 0.1011
REMARK 3 7 1.5700 - 1.5000 1.00 6047 139 0.0777 0.1041
REMARK 3 8 1.5000 - 1.4300 1.00 6076 140 0.0823 0.1085
REMARK 3 9 1.4300 - 1.3800 1.00 6007 137 0.0915 0.1238
REMARK 3 10 1.3800 - 1.3300 1.00 6040 138 0.0961 0.1090
REMARK 3 11 1.3300 - 1.2900 1.00 6034 139 0.1092 0.1374
REMARK 3 12 1.2900 - 1.2500 1.00 5984 136 0.1193 0.1608
REMARK 3 13 1.2500 - 1.2200 1.00 6003 138 0.1257 0.1490
REMARK 3 14 1.2200 - 1.1900 1.00 6015 139 0.1368 0.1571
REMARK 3 15 1.1900 - 1.1600 1.00 5994 137 0.1447 0.1510
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) : 0.069
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 10.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.38
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 : 0.007 2256
REMARK 3 ANGLE : 1.059 3020
REMARK 3 CHIRALITY : 0.089 309
REMARK 3 PLANARITY : 0.011 388
REMARK 3 DIHEDRAL : 14.576 832
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 9HL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-DEC-24.
REMARK 100 THE DEPOSITION ID IS D_1292143594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-24
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) : 0.9763
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93276
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.160
REMARK 200 RESOLUTION RANGE LOW (A) : 35.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06117
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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 : 4.170
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 (%): 48.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 40 % (V/V) PEG400,
REMARK 280 VAPOR DIFFUSION, SITTING 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 26.17000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.26500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 56.0 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 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 HOH A 401 O HOH A 548 1.94
REMARK 500 O HOH A 418 O HOH A 559 1.95
REMARK 500 O HOH A 408 O HOH A 558 1.96
REMARK 500 O HOH A 563 O HOH A 564 2.01
REMARK 500 O HOH A 450 O HOH A 469 2.03
REMARK 500 O HOH A 466 O HOH A 557 2.04
REMARK 500 O HOH A 576 O HOH A 583 2.04
REMARK 500 O3 GOL A 303 O HOH A 401 2.05
REMARK 500 O HOH A 530 O HOH A 574 2.06
REMARK 500 O HOH A 536 O HOH A 571 2.08
REMARK 500 OG SER A 239 O HOH A 402 2.09
REMARK 500 O HOH A 416 O HOH A 561 2.11
REMARK 500 O HOH A 534 O HOH A 573 2.12
REMARK 500 O HOH A 555 O HOH A 569 2.15
REMARK 500 O HOH A 482 O HOH A 581 2.16
REMARK 500 O HOH A 540 O HOH A 541 2.16
REMARK 500 O HOH A 547 O HOH A 572 2.17
REMARK 500 OD2 ASP A 277 O HOH A 403 2.17
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 442 O HOH A 481 2554 1.88
REMARK 500 O HOH A 432 O HOH A 489 4445 1.91
REMARK 500 O HOH A 412 O HOH A 502 2555 1.92
REMARK 500 O HOH A 409 O HOH A 559 2555 2.03
REMARK 500 O3 GOL A 320 O HOH A 436 4545 2.15
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 LEU A 59 -45.49 70.39
REMARK 500 THR A 86 -7.40 74.94
REMARK 500 SER A 153 -131.11 67.86
REMARK 500 ALA A 206 70.76 -113.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9HL5 A 20 287 PDB 9HL5 9HL5 20 287
SEQRES 1 A 268 SER THR ASN PRO GLY GLY GLY GLY GLY GLY SER ASN PRO
SEQRES 2 A 268 ASP THR GLY THR GLY PHE PRO GLY VAL SER SER PHE SER
SEQRES 3 A 268 ALA ASP GLY SER PHE ALA THR THR SER GLY SER ALA GLY
SEQRES 4 A 268 LEU SER CYS THR VAL PHE ARG PRO SER THR LEU GLY ALA
SEQRES 5 A 268 ASN GLY LEU LYS HIS PRO ILE ILE VAL TRP GLY ASN GLY
SEQRES 6 A 268 THR THR ALA SER PRO SER THR TYR SER GLY ILE LEU GLU
SEQRES 7 A 268 HIS TRP ALA SER HIS GLY PHE VAL VAL ILE ALA ALA ASN
SEQRES 8 A 268 THR SER ASN ALA GLY THR GLY GLN ASP MET LEU ASN CYS
SEQRES 9 A 268 VAL ASP TYR LEU THR THR GLN ASN ASN ARG SER THR GLY
SEQRES 10 A 268 THR TYR ALA ASN LYS LEU ASP LEU ASN ARG ILE GLY ALA
SEQRES 11 A 268 ALA GLY HIS SER GLN GLY GLY GLY GLY THR ILE MET ALA
SEQRES 12 A 268 GLY GLN ASP TYR ARG ILE LYS VAL THR ALA PRO PHE GLN
SEQRES 13 A 268 PRO TYR THR ILE GLY LEU GLY HIS ASN SER SER SER GLN
SEQRES 14 A 268 SER ASN GLN ASN GLY PRO MET PHE LEU MET THR GLY SER
SEQRES 15 A 268 ALA ASP THR ILE ALA SER PRO THR LEU ASN ALA LEU PRO
SEQRES 16 A 268 VAL TYR ASN ARG ALA ASN VAL PRO VAL PHE TRP GLY GLU
SEQRES 17 A 268 LEU SER GLY ALA SER HIS PHE GLU PRO VAL GLY SER ALA
SEQRES 18 A 268 GLY ASP PHE ARG GLY PRO SER THR ALA TRP PHE ARG TYR
SEQRES 19 A 268 HIS LEU MET ASP ASP ALA SER ALA GLU ASP THR PHE TYR
SEQRES 20 A 268 GLY SER ASN CYS ASP LEU CYS THR ASP ASN ASP TRP GLU
SEQRES 21 A 268 VAL ARG ARG LYS GLY ILE ASN ALA
HET GOL A 301 14
HET GOL A 302 14
HET GOL A 303 14
HET GOL A 304 14
HET GOL A 305 14
HET PGE A 306 24
HET PG4 A 307 31
HET PEG A 308 17
HET PEG A 309 17
HET PEG A 310 17
HET GOL A 311 14
HET EDO A 312 10
HET EDO A 313 10
HET GOL A 314 14
HET PGE A 315 24
HET EDO A 316 10
HET EDO A 317 10
HET GOL A 318 14
HET GOL A 319 14
HET GOL A 320 14
HET EDO A 321 10
HET GOL A 322 14
HET PGE A 323 24
HET EDO A 324 10
HET PGE A 325 24
HET EDO A 326 10
HET GOL A 327 14
HET GOL A 328 14
HET GOL A 329 14
HET PGE A 330 24
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 GOL 14(C3 H8 O3)
FORMUL 7 PGE 5(C6 H14 O4)
FORMUL 8 PG4 C8 H18 O5
FORMUL 9 PEG 3(C4 H10 O3)
FORMUL 13 EDO 7(C2 H6 O2)
FORMUL 32 HOH *185(H2 O)
HELIX 1 AA1 GLY A 70 LEU A 74 5 5
HELIX 2 AA2 SER A 88 THR A 91 5 4
HELIX 3 AA3 TYR A 92 HIS A 102 1 11
HELIX 4 AA4 GLY A 117 ASN A 132 1 16
HELIX 5 AA5 SER A 153 GLY A 163 1 11
HELIX 6 AA6 ASN A 184 GLN A 191 5 8
HELIX 7 AA7 SER A 207 ALA A 212 1 6
HELIX 8 AA8 ALA A 212 ALA A 219 1 8
HELIX 9 AA9 ALA A 240 ASP A 242 5 3
HELIX 10 AB1 PHE A 243 ASP A 257 1 15
HELIX 11 AB2 ASP A 258 SER A 260 5 3
HELIX 12 AB3 ALA A 261 TYR A 266 1 6
HELIX 13 AB4 ASP A 271 ASP A 275 5 5
SHEET 1 AA1 6 THR A 52 ALA A 57 0
SHEET 2 AA1 6 CYS A 61 PRO A 66 -1 O VAL A 63 N GLY A 55
SHEET 3 AA1 6 VAL A 105 ALA A 109 -1 O ALA A 108 N THR A 62
SHEET 4 AA1 6 HIS A 76 GLY A 82 1 N PRO A 77 O VAL A 105
SHEET 5 AA1 6 LEU A 142 HIS A 152 1 O ASP A 143 N HIS A 76
SHEET 6 AA1 6 VAL A 170 PHE A 174 1 O PHE A 174 N GLY A 151
SHEET 1 AA2 3 MET A 195 GLY A 200 0
SHEET 2 AA2 3 VAL A 223 LEU A 228 1 O PHE A 224 N MET A 195
SHEET 3 AA2 3 TRP A 278 LYS A 283 -1 O ARG A 281 N TRP A 225
SSBOND 1 CYS A 61 CYS A 123 1555 1555 2.06
SSBOND 2 CYS A 270 CYS A 273 1555 1555 2.06
CRYST1 52.340 70.530 72.460 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 0.019106 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014178 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013801 0.00000
TER 3924 ALA A 287
MASTER 277 0 30 13 9 0 0 6 2335 1 472 21
END |