HEADER ISOMERASE 13-AUG-13 3WGX
TITLE CRYSTAL STRUCTURE OF ERP46 TRX2 IN A COMPLEX WITH PRX4 C-TERM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRX2 DOMAIN, UNP RESIDUES 190-298;
COMPND 5 SYNONYM: ERP46, ENDOPLASMIC RETICULUM RESIDENT PROTEIN 46, ER PROTEIN
COMPND 6 46, THIOREDOXIN-LIKE PROTEIN P46;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PEROXIREDOXIN-4;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: C-TERM DOMAIN, UNP RESIDUES 244-263;
COMPND 13 SYNONYM: PRX4;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TLP46;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3)RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: POPTG;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 14 ORGANISM_COMMON: MOUSE;
SOURCE 15 ORGANISM_TAXID: 10090;
SOURCE 16 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS PDI FAMILY MEMBER, THIOREDOXIN DOMAIN, PROTEIN DISULFIDE ISOMERASE,
KEYWDS 2 ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.INABA,M.SUZUKI,R.KOJIMA
REVDAT 1 25-JUN-14 3WGX 0
JRNL AUTH R.KOJIMA,M.OKUMURA,S.MASUI,S.KANEMURA,M.INOUE,M.SAIKI,
JRNL AUTH 2 H.YAMAGUCHI,T.HIKIMA,M.SUZUKI,S.AKIYAMA,K.INABA
JRNL TITL RADICALLY DIFFERENT THIOREDOXIN DOMAIN ARRANGEMENT OF ERP46,
JRNL TITL 2 AN EFFICIENT DISULFIDE BOND INTRODUCER OF THE MAMMALIAN PDI
JRNL TITL 3 FAMILY
JRNL REF STRUCTURE V. 22 431 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24462249
JRNL DOI 10.1016/J.STR.2013.12.013
REMARK 2
REMARK 2 RESOLUTION. 0.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1386)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 126561
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6367
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 26.7962 - 2.8587 0.98 4265 207 0.1506 0.1736
REMARK 3 2 2.8587 - 2.2694 0.98 4245 228 0.1665 0.1872
REMARK 3 3 2.2694 - 1.9827 0.98 4279 239 0.1452 0.1523
REMARK 3 4 1.9827 - 1.8014 0.97 4204 237 0.1487 0.1640
REMARK 3 5 1.8014 - 1.6723 0.97 4161 212 0.1420 0.1520
REMARK 3 6 1.6723 - 1.5737 0.96 4236 186 0.1389 0.1555
REMARK 3 7 1.5737 - 1.4949 0.96 4150 229 0.1355 0.1659
REMARK 3 8 1.4949 - 1.4299 0.95 4094 252 0.1375 0.1656
REMARK 3 9 1.4299 - 1.3748 0.95 4108 231 0.1354 0.1421
REMARK 3 10 1.3748 - 1.3274 0.94 4129 194 0.1355 0.1654
REMARK 3 11 1.3274 - 1.2859 0.94 4045 214 0.1240 0.1440
REMARK 3 12 1.2859 - 1.2491 0.93 4049 196 0.1163 0.1278
REMARK 3 13 1.2491 - 1.2162 0.93 4008 227 0.1093 0.1182
REMARK 3 14 1.2162 - 1.1866 0.93 4109 186 0.1047 0.1382
REMARK 3 15 1.1866 - 1.1596 0.93 3996 232 0.1022 0.1170
REMARK 3 16 1.1596 - 1.1349 0.92 4004 194 0.0995 0.1246
REMARK 3 17 1.1349 - 1.1122 0.92 4005 226 0.1015 0.1174
REMARK 3 18 1.1122 - 1.0912 0.92 3950 219 0.1050 0.1282
REMARK 3 19 1.0912 - 1.0717 0.91 3915 209 0.1044 0.1246
REMARK 3 20 1.0717 - 1.0536 0.91 3990 213 0.1081 0.1309
REMARK 3 21 1.0536 - 1.0366 0.90 3915 200 0.1158 0.1388
REMARK 3 22 1.0366 - 1.0206 0.90 3923 201 0.1230 0.1462
REMARK 3 23 1.0206 - 1.0056 0.90 3858 230 0.1327 0.1540
REMARK 3 24 1.0056 - 0.9915 0.90 3866 220 0.1409 0.1642
REMARK 3 25 0.9915 - 0.9781 0.89 3892 189 0.1505 0.1676
REMARK 3 26 0.9781 - 0.9653 0.89 3863 214 0.1613 0.1734
REMARK 3 27 0.9653 - 0.9533 0.89 3829 194 0.1643 0.1866
REMARK 3 28 0.9533 - 0.9418 0.88 3847 203 0.1766 0.2088
REMARK 3 29 0.9418 - 0.9308 0.88 3814 190 0.1911 0.1944
REMARK 3 30 0.9308 - 0.9204 0.80 3445 195 0.2306 0.2587
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) : 0.070
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.11
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 : 0.013 2158
REMARK 3 ANGLE : 1.500 2945
REMARK 3 CHIRALITY : 0.101 299
REMARK 3 PLANARITY : 0.010 388
REMARK 3 DIHEDRAL : 13.217 824
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 3WGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB096320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : DIP-6040 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126561
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.920
REMARK 200 RESOLUTION RANGE LOW (A) : 26.785
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.3
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 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 27.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 20% PEG3350 , PH 6.8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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
REMARK 350 BIOMOLECULE: 2
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: 880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A 186
REMARK 465 ARG A 296
REMARK 465 THR A 297
REMARK 465 GLU A 298
REMARK 465 GLY B 186
REMARK 465 GLY C 301
REMARK 465 TRP C 302
REMARK 465 LYS C 303
REMARK 465 PRO C 304
REMARK 465 GLY C 305
REMARK 465 SER C 306
REMARK 465 GLU C 307
REMARK 465 THR C 308
REMARK 465 ILE C 309
REMARK 465 ILE C 310
REMARK 465 PRO C 311
REMARK 465 ASP C 312
REMARK 465 PRO C 313
REMARK 465 HIS D 294
REMARK 465 GLY D 301
REMARK 465 TRP D 302
REMARK 465 LYS D 303
REMARK 465 PRO D 304
REMARK 465 GLY D 305
REMARK 465 SER D 306
REMARK 465 GLU D 307
REMARK 465 THR D 308
REMARK 465 ILE D 309
REMARK 465 ILE D 310
REMARK 465 PRO D 311
REMARK 465 ASP D 312
REMARK 465 PRO D 313
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 205 CG CD OE1 NE2
REMARK 470 LYS A 272 CD CE NZ
REMARK 470 GLN A 295 CD OE1 NE2
REMARK 470 ARG B 296 CZ NH1 NH2
REMARK 470 GLU D 296 CD OE1 OE2
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 OG SER A 187 O HOH A 393 1.94
REMARK 500 O HOH A 372 O HOH A 436 2.04
REMARK 500 O HOH A 450 O HOH A 458 2.07
REMARK 500 O HOH B 468 O HOH B 591 2.09
REMARK 500 OE1 GLU A 228 O HOH A 397 2.11
REMARK 500 O HOH B 563 O HOH B 587 2.13
REMARK 500 O HOH B 568 O HOH B 590 2.16
REMARK 500 O HOH A 432 O HOH A 440 2.17
REMARK 500 O HOH B 537 O HOH B 546 2.18
REMARK 500 O HOH B 505 O HOH B 568 2.18
REMARK 500 O HOH B 479 O HOH B 600 2.19
REMARK 500 O HOH B 553 O HOH B 556 2.19
REMARK 500 O HOH B 575 O HOH D 402 2.19
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 436 O HOH A 437 1455 2.08
REMARK 500 O HOH B 570 O HOH B 571 1565 2.08
REMARK 500 O HOH A 414 O HOH A 436 1655 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
DBREF 3WGX A 190 298 UNP Q8NBS9 TXND5_HUMAN 190 298
DBREF 3WGX B 190 298 UNP Q8NBS9 TXND5_HUMAN 190 298
DBREF 3WGX C 294 313 UNP O08807 PRDX4_MOUSE 244 263
DBREF 3WGX D 294 313 UNP O08807 PRDX4_MOUSE 244 263
SEQADV 3WGX GLY A 186 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX SER A 187 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX HIS A 188 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX MET A 189 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX ALA A 220 UNP Q8NBS9 CYS 220 ENGINEERED MUTATION
SEQADV 3WGX GLY B 186 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX SER B 187 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX HIS B 188 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX MET B 189 UNP Q8NBS9 EXPRESSION TAG
SEQADV 3WGX ALA B 220 UNP Q8NBS9 CYS 220 ENGINEERED MUTATION
SEQRES 1 A 113 GLY SER HIS MET GLY LEU TYR GLU LEU SER ALA SER ASN
SEQRES 2 A 113 PHE GLU LEU HIS VAL ALA GLN GLY ASP HIS PHE ILE LYS
SEQRES 3 A 113 PHE PHE ALA PRO TRP CYS GLY HIS ALA LYS ALA LEU ALA
SEQRES 4 A 113 PRO THR TRP GLU GLN LEU ALA LEU GLY LEU GLU HIS SER
SEQRES 5 A 113 GLU THR VAL LYS ILE GLY LYS VAL ASP CYS THR GLN HIS
SEQRES 6 A 113 TYR GLU LEU CYS SER GLY ASN GLN VAL ARG GLY TYR PRO
SEQRES 7 A 113 THR LEU LEU TRP PHE ARG ASP GLY LYS LYS VAL ASP GLN
SEQRES 8 A 113 TYR LYS GLY LYS ARG ASP LEU GLU SER LEU ARG GLU TYR
SEQRES 9 A 113 VAL GLU SER GLN LEU GLN ARG THR GLU
SEQRES 1 B 113 GLY SER HIS MET GLY LEU TYR GLU LEU SER ALA SER ASN
SEQRES 2 B 113 PHE GLU LEU HIS VAL ALA GLN GLY ASP HIS PHE ILE LYS
SEQRES 3 B 113 PHE PHE ALA PRO TRP CYS GLY HIS ALA LYS ALA LEU ALA
SEQRES 4 B 113 PRO THR TRP GLU GLN LEU ALA LEU GLY LEU GLU HIS SER
SEQRES 5 B 113 GLU THR VAL LYS ILE GLY LYS VAL ASP CYS THR GLN HIS
SEQRES 6 B 113 TYR GLU LEU CYS SER GLY ASN GLN VAL ARG GLY TYR PRO
SEQRES 7 B 113 THR LEU LEU TRP PHE ARG ASP GLY LYS LYS VAL ASP GLN
SEQRES 8 B 113 TYR LYS GLY LYS ARG ASP LEU GLU SER LEU ARG GLU TYR
SEQRES 9 B 113 VAL GLU SER GLN LEU GLN ARG THR GLU
SEQRES 1 C 20 HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER
SEQRES 2 C 20 GLU THR ILE ILE PRO ASP PRO
SEQRES 1 D 20 HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER
SEQRES 2 D 20 GLU THR ILE ILE PRO ASP PRO
HET GOL B 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *388(H2 O)
HELIX 1 1 ASN A 198 ALA A 204 1 7
HELIX 2 2 CYS A 217 LEU A 234 1 18
HELIX 3 3 HIS A 250 ASN A 257 1 8
HELIX 4 4 ASP A 282 GLN A 295 1 14
HELIX 5 5 ASN B 198 ALA B 204 1 7
HELIX 6 6 CYS B 217 LEU B 234 1 18
HELIX 7 7 HIS B 250 GLY B 256 1 7
HELIX 8 8 ASP B 282 GLN B 295 1 14
SHEET 1 A 5 LEU A 191 LEU A 194 0
SHEET 2 A 5 VAL A 240 ASP A 246 1 O LYS A 244 N LEU A 194
SHEET 3 A 5 ASP A 207 PHE A 213 1 N LYS A 211 O VAL A 245
SHEET 4 A 5 THR A 264 ARG A 269 -1 O THR A 264 N PHE A 212
SHEET 5 A 5 LYS A 272 GLN A 276 -1 O VAL A 274 N TRP A 267
SHEET 1 B 2 GLY A 261 TYR A 262 0
SHEET 2 B 2 CYS C 298 PRO C 299 -1 O CYS C 298 N TYR A 262
SHEET 1 C 5 LEU B 191 LEU B 194 0
SHEET 2 C 5 VAL B 240 ASP B 246 1 O LYS B 244 N LEU B 194
SHEET 3 C 5 ASP B 207 PHE B 213 1 N LYS B 211 O VAL B 245
SHEET 4 C 5 THR B 264 ARG B 269 -1 O THR B 264 N PHE B 212
SHEET 5 C 5 LYS B 272 GLN B 276 -1 O VAL B 274 N TRP B 267
SHEET 1 D 2 GLY B 261 TYR B 262 0
SHEET 2 D 2 CYS D 298 PRO D 299 -1 O CYS D 298 N TYR B 262
SSBOND 1 CYS A 217 CYS C 298 1555 1555 2.12
SSBOND 2 CYS A 247 CYS A 254 1555 1555 2.05
SSBOND 3 CYS B 217 CYS D 298 1555 1555 2.11
SSBOND 4 CYS B 247 CYS B 254 1555 1555 2.03
CISPEP 1 TYR A 262 PRO A 263 0 -8.04
CISPEP 2 TYR B 262 PRO B 263 0 -7.98
SITE 1 AC1 9 LYS A 280 ASP B 207 ARG B 269 ASP B 270
SITE 2 AC1 9 THR B 297 GLU B 298 HOH B 523 HOH B 592
SITE 3 AC1 9 HIS C 294
CRYST1 35.098 36.406 40.594 81.17 87.47 85.40 P 1 2
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 0.028492 -0.002292 -0.000924 0.00000
SCALE2 0.000000 0.027557 -0.004198 0.00000
SCALE3 0.000000 0.000000 0.024943 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
