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HEADER HYDROLASE 07-MAR-25 9QDV
TITLE CRYSTAL STRUCTURE OF THE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) MUT3
TITLE 2 VARIANT EXPRESSED IN E. COLI (E_PHL7MUT3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7), CATALYSIS-DEFICIENT
COMPND 3 S131A MUTANT;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMPOST METAGENOME;
SOURCE 3 ORGANISM_TAXID: 702656;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS E. COLI, LCC, K. PHAFFII, PETASE, P. PASTORIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.USEINI,N.STRATER,G.STRIEDNER,C.SONNENDECKER
REVDAT 1 10-SEP-25 9QDV 0
JRNL AUTH L.FOHLER,F.FASCHINGEDER,L.LEIBETSEDER,Z.ZHAO,A.USEINI,
JRNL AUTH 2 N.STRATER,C.SONNENDECKER,T.A.EWING,A.P.H.A.MOERS,
JRNL AUTH 3 M.W.T.WERTEN,D.M.VAN VLIET,M.K.JULSING,W.ZIMMERMANN,
JRNL AUTH 4 G.STRIEDNER
JRNL TITL TRADE-OFFS BETWEEN STABILITY AND ACTIVITY OF GLYCOSYLATED
JRNL TITL 2 AND NON-GLYCOSYLATED POLYESTER HYDROLASES PHL7 AND PHL7MUT3
JRNL REF ACS ES T ENG 2025
JRNL DOI 10.1021/ACSESTENGG.5C00272
REMARK 2
REMARK 2 RESOLUTION. 0.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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) : 0.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.2
REMARK 3 NUMBER OF REFLECTIONS : 292736
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.119
REMARK 3 R VALUE (WORKING SET) : 0.119
REMARK 3 FREE R VALUE : 0.131
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.980
REMARK 3 FREE R VALUE TEST SET COUNT : 5774
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 32.9300 - 2.7800 1.00 24163 178 0.1203 0.1281
REMARK 3 2 2.7800 - 2.2000 0.99 23841 288 0.1130 0.1294
REMARK 3 3 2.2000 - 1.9300 0.99 24169 201 0.1081 0.1009
REMARK 3 4 1.9300 - 1.7500 1.00 24071 253 0.1044 0.1060
REMARK 3 5 1.7500 - 1.6200 1.00 24165 224 0.0988 0.1197
REMARK 3 6 1.6200 - 1.5300 1.00 24231 215 0.0931 0.0908
REMARK 3 7 1.5300 - 1.4500 1.00 24088 276 0.0919 0.1077
REMARK 3 8 1.4500 - 1.3900 1.00 24272 218 0.0945 0.1087
REMARK 3 9 1.3900 - 1.3400 1.00 24150 245 0.0980 0.1137
REMARK 3 10 1.3400 - 1.2900 0.98 23748 216 0.1007 0.1392
REMARK 3 11 1.2900 - 1.2500 0.98 23780 216 0.1071 0.1305
REMARK 3 12 1.2500 - 1.2100 0.99 24049 186 0.1096 0.1305
REMARK 3 13 1.2100 - 1.1800 0.99 24007 222 0.1114 0.1474
REMARK 3 14 1.1800 - 1.1500 0.99 23947 249 0.1173 0.1258
REMARK 3 15 1.1500 - 1.1300 1.00 24087 292 0.1247 0.1446
REMARK 3 16 1.1300 - 1.1000 1.00 24102 244 0.1349 0.1554
REMARK 3 17 1.1000 - 1.0800 1.00 24150 255 0.1482 0.1643
REMARK 3 18 1.0800 - 1.0600 0.99 23926 245 0.1646 0.1915
REMARK 3 19 1.0600 - 1.0400 0.95 23006 221 0.1808 0.1727
REMARK 3 20 1.0400 - 1.0200 0.90 21732 259 0.1876 0.2226
REMARK 3 21 1.0200 - 1.0100 0.83 19962 237 0.1987 0.2234
REMARK 3 22 1.0100 - 0.9900 0.76 18246 178 0.2145 0.2252
REMARK 3 23 0.9900 - 0.9800 0.67 16316 168 0.2350 0.2429
REMARK 3 24 0.9800 - 0.9600 0.60 14577 125 0.2483 0.2926
REMARK 3 25 0.9600 - 0.9500 0.51 12187 110 0.2505 0.2489
REMARK 3 26 0.9500 - 0.9400 0.39 9489 99 0.2583 0.2528
REMARK 3 27 0.9400 - 0.9300 0.26 6345 90 0.2635 0.2782
REMARK 3 28 0.9300 - 0.9100 0.16 3856 30 0.2580 0.2718
REMARK 3 29 0.9100 - 0.9000 0.09 2215 14 0.2633 0.3284
REMARK 3 30 0.9000 - 0.8900 0.05 1099 20 0.2608 0.2593
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) : 0.071
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.681
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.45
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 : 0.010 4327
REMARK 3 ANGLE : 1.205 5944
REMARK 3 CHIRALITY : 0.089 653
REMARK 3 PLANARITY : 0.015 804
REMARK 3 DIHEDRAL : 12.593 1594
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 9QDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1292145512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-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) : 0.7300
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 292736
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.890
REMARK 200 RESOLUTION RANGE LOW (A) : 75.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.96
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 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 (%): 42.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M HEPES, PH 7.5, 25%
REMARK 280 W/V PEG 3350, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 75.22050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.95100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.22050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.95100
REMARK 290 SMTRY3 4 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 1
REMARK 465 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 MET B 1
REMARK 465 GLU B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
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 64 -2.43 63.33
REMARK 500 THR A 64 -2.43 74.13
REMARK 500 SER A 131 -127.85 63.72
REMARK 500 HIS A 185 -101.87 -116.49
REMARK 500 PRO A 243 -172.69 -68.66
REMARK 500 THR B 64 -6.01 74.17
REMARK 500 SER B 131 -127.24 63.31
REMARK 500 LEU B 176 51.70 -111.74
REMARK 500 HIS B 185 -101.07 -116.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 87 ASP A 88 148.44
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 99 0.09 SIDE CHAIN
REMARK 500 ARG B 99 0.09 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 756 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 757 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 758 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 759 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 760 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 761 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH B 675 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 676 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 677 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 678 DISTANCE = 6.49 ANGSTROMS
DBREF1 9QDV A 1 259 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QDV A A0AA82WPD4 1 259
DBREF1 9QDV B 1 259 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QDV B A0AA82WPD4 1 259
SEQADV 9QDV SER A 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QDV GLU A 175 UNP A0AA82WPD GLN 175 ENGINEERED MUTATION
SEQADV 9QDV THR A 210 UNP A0AA82WPD LEU 210 ENGINEERED MUTATION
SEQADV 9QDV LYS A 233 UNP A0AA82WPD ASP 233 ENGINEERED MUTATION
SEQADV 9QDV LEU A 260 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV GLU A 261 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 262 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS A 267 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV SER B 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QDV GLU B 175 UNP A0AA82WPD GLN 175 ENGINEERED MUTATION
SEQADV 9QDV THR B 210 UNP A0AA82WPD LEU 210 ENGINEERED MUTATION
SEQADV 9QDV LYS B 233 UNP A0AA82WPD ASP 233 ENGINEERED MUTATION
SEQADV 9QDV LEU B 260 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV GLU B 261 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 262 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDV HIS B 267 UNP A0AA82WPD EXPRESSION TAG
SEQRES 1 A 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 A 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 A 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 A 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 A 267 LEU VAL VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 267 HIS THR VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 A 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP LYS ASP
SEQRES 19 A 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 B 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 B 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 B 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 B 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 B 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 B 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 B 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 B 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 B 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 B 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 B 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 B 267 LEU VAL VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 B 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 B 267 HIS THR VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 B 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP LYS ASP
SEQRES 19 B 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 B 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *840(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 GLN A 95 ARG A 111 1 17
HELIX 5 AA5 VAL A 116 ASN A 118 5 3
HELIX 6 AA6 SER A 131 ASN A 144 1 14
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 SER A 208 THR A 214 5 7
HELIX 9 AA9 ASP A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 ARG A 236 5 3
HELIX 11 AB2 TYR A 237 CYS A 242 1 6
HELIX 12 AB3 THR B 12 ALA B 18 1 7
HELIX 13 AB4 GLY B 66 ALA B 71 5 6
HELIX 14 AB5 TRP B 72 SER B 79 1 8
HELIX 15 AB6 GLN B 95 ARG B 111 1 17
HELIX 16 AB7 SER B 131 ASN B 144 1 14
HELIX 17 AB8 HIS B 185 LEU B 193 1 9
HELIX 18 AB9 SER B 208 THR B 214 5 7
HELIX 19 AC1 ASP B 216 ASP B 232 1 17
HELIX 20 AC2 ASP B 234 ARG B 236 5 3
HELIX 21 AC3 TYR B 237 CYS B 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O ILE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O MET A 128 N ALA A 58
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N VAL A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O GLU A 252 N GLU A 203
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O ILE B 43 N THR B 28
SHEET 3 AA3 6 VAL B 83 ILE B 87 -1 O VAL B 84 N TYR B 44
SHEET 4 AA3 6 PHE B 54 SER B 60 1 N VAL B 57 O ILE B 85
SHEET 5 AA3 6 ILE B 120 HIS B 130 1 O MET B 128 N ALA B 58
SHEET 6 AA3 6 ALA B 149 LEU B 153 1 O LEU B 153 N GLY B 129
SHEET 1 AA4 3 THR B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O ALA B 200 N VAL B 171
SHEET 3 AA4 3 ILE B 250 SER B 255 -1 O ARG B 254 N TYR B 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.05
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.04
CISPEP 1 CYS A 242 PRO A 243 0 -8.45
CISPEP 2 CYS A 257 PRO A 258 0 -3.14
CISPEP 3 CYS B 242 PRO B 243 0 -5.72
CISPEP 4 CYS B 257 PRO B 258 0 -4.16
CRYST1 150.441 43.902 100.123 90.00 130.87 90.00 C 1 2 1 8
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 0.006647 0.000000 0.005751 0.00000
SCALE2 0.000000 0.022778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013207 0.00000
TER 4105 LEU A 260
TER 8298 LEU B 260
MASTER 324 0 0 21 18 0 0 6 4778 2 4 42
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