| 7b6b-pdb | HEADER HYDROLASE 07-DEC-20 7B6B
TITLE THE CARBOHYDRATE BINDING MODULE FAMILY 48 (CBM48) AND CARBOXY-TERMINAL
TITLE 2 CARBOHYDRATE ESTERASE FAMILY 1 (CE1) DOMAINS OF THE MULTIDOMAIN
TITLE 3 ESTERASE DMCE1B FROM DYSGONOMONAS MOSSII IN COMPLEX WITH METHYL
TITLE 4 FERULATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 1 PROTEIN WITH AN N-TERMINAL
COMPND 3 CARBOHYDRATE BINDING MODULE FAMILY 48;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DYSGONOMONAS MOSSII DSM 22836;
SOURCE 3 ORGANISM_TAXID: 742767;
SOURCE 4 GENE: HMPREF9456_02279;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CARBOHYDRATE ESTERASE, CE1, CBM48, CARBOHYDRATE BINDING MODULE, CBM,
KEYWDS 2 CE, PUL, LIGNIN, XYLAN, FERULATE, FEROUYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,C.KMEZIK,G.BRANDEN,J.LARSBRINK
REVDAT 1 10-MAR-21 7B6B 0
JRNL AUTH C.KMEZIK,S.MAZURKEWICH,T.MEENTS,L.S.MCKEE,A.IDSTROM,
JRNL AUTH 2 M.ARMENI,O.SAVOLAINEN,G.BRANDEN,J.LARSBRINK
JRNL TITL A POLYSACCHARIDE UTILIZATION LOCUS FROM THE GUT BACTERIUM
JRNL TITL 2 DYSGONOMONAS MOSSII ENCODES FUNCTIONALLY DISTINCT
JRNL TITL 3 CARBOHYDRATE ESTERASES
JRNL REF J.BIOL.CHEM. 2021
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1016/J.JBC.2021.100500
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 123368
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 9253
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 43.9000 - 4.3700 1.00 4042 328 0.1462 0.1609
REMARK 3 2 4.3700 - 3.4700 1.00 3924 318 0.1284 0.1392
REMARK 3 3 3.4700 - 3.0300 1.00 3917 318 0.1494 0.1620
REMARK 3 4 3.0300 - 2.7600 1.00 3891 316 0.1623 0.1800
REMARK 3 5 2.7600 - 2.5600 1.00 3880 314 0.1660 0.1731
REMARK 3 6 2.5600 - 2.4100 1.00 3885 315 0.1729 0.1852
REMARK 3 7 2.4100 - 2.2900 1.00 3857 313 0.1680 0.1834
REMARK 3 8 2.2900 - 2.1900 1.00 3897 316 0.1641 0.1868
REMARK 3 9 2.1900 - 2.1000 1.00 3853 312 0.1618 0.1839
REMARK 3 10 2.1000 - 2.0300 1.00 3879 315 0.1610 0.1759
REMARK 3 11 2.0300 - 1.9700 1.00 3901 315 0.1633 0.1848
REMARK 3 12 1.9700 - 1.9100 1.00 3849 313 0.1636 0.1887
REMARK 3 13 1.9100 - 1.8600 1.00 3856 312 0.1727 0.2093
REMARK 3 14 1.8600 - 1.8200 1.00 3865 314 0.1699 0.1901
REMARK 3 15 1.8200 - 1.7700 1.00 3886 315 0.1673 0.1940
REMARK 3 16 1.7700 - 1.7400 1.00 3819 310 0.1669 0.1916
REMARK 3 17 1.7400 - 1.7000 1.00 3876 314 0.1636 0.1812
REMARK 3 18 1.7000 - 1.6700 1.00 3853 313 0.1627 0.1788
REMARK 3 19 1.6700 - 1.6400 1.00 3860 313 0.1669 0.2079
REMARK 3 20 1.6400 - 1.6100 1.00 3852 312 0.1709 0.2084
REMARK 3 21 1.6100 - 1.5900 1.00 3857 312 0.1746 0.2054
REMARK 3 22 1.5900 - 1.5600 1.00 3834 311 0.1795 0.1862
REMARK 3 23 1.5600 - 1.5400 1.00 3835 312 0.1781 0.2041
REMARK 3 24 1.5400 - 1.5200 1.00 3919 317 0.1865 0.2232
REMARK 3 25 1.5200 - 1.5000 1.00 3830 310 0.1941 0.2454
REMARK 3 26 1.5000 - 1.4800 1.00 3833 311 0.2102 0.2340
REMARK 3 27 1.4800 - 1.4600 0.94 3634 295 0.2106 0.2429
REMARK 3 28 1.4600 - 1.4400 0.88 3393 275 0.2214 0.2340
REMARK 3 29 1.4400 - 1.4200 0.85 3292 267 0.2357 0.2672
REMARK 3 30 1.4200 - 1.4100 0.80 3046 247 0.2374 0.2611
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) : 0.125
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.986
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.96
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 : 0.009 5882
REMARK 3 ANGLE : 1.026 7987
REMARK 3 CHIRALITY : 0.090 828
REMARK 3 PLANARITY : 0.007 1055
REMARK 3 DIHEDRAL : 19.525 2157
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 7B6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123374
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.408
REMARK 200 RESOLUTION RANGE LOW (A) : 43.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.350
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: 7B5V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8, 25% PEG 6000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.25550
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 271
REMARK 465 GLY A 272
REMARK 465 SER A 273
REMARK 465 SER A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 SER A 281
REMARK 465 SER A 282
REMARK 465 GLU A 283
REMARK 465 ASN A 284
REMARK 465 LEU A 285
REMARK 465 TYR A 286
REMARK 465 PHE A 287
REMARK 465 GLN A 288
REMARK 465 GLY A 289
REMARK 465 HIS A 290
REMARK 465 SER A 291
REMARK 465 GLU A 292
REMARK 465 GLU A 293
REMARK 465 ALA A 294
REMARK 465 SER A 495
REMARK 465 ALA A 496
REMARK 465 ASN A 497
REMARK 465 SER A 498
REMARK 465 PRO A 499
REMARK 465 GLN A 500
REMARK 465 GLY A 501
REMARK 465 LEU A 502
REMARK 465 ARG A 503
REMARK 465 GLY A 504
REMARK 465 LEU A 505
REMARK 465 ILE A 571
REMARK 465 GLU A 572
REMARK 465 GLN A 573
REMARK 465 GLY A 574
REMARK 465 GLY A 575
REMARK 465 MET B 271
REMARK 465 GLY B 272
REMARK 465 SER B 273
REMARK 465 SER B 274
REMARK 465 HIS B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 SER B 281
REMARK 465 SER B 282
REMARK 465 GLU B 283
REMARK 465 ASN B 284
REMARK 465 LEU B 285
REMARK 465 TYR B 286
REMARK 465 PHE B 287
REMARK 465 GLN B 288
REMARK 465 GLY B 289
REMARK 465 HIS B 290
REMARK 465 SER B 291
REMARK 465 GLU B 292
REMARK 465 GLU B 293
REMARK 465 ALA B 294
REMARK 465 SER B 494
REMARK 465 SER B 495
REMARK 465 ALA B 496
REMARK 465 ASN B 497
REMARK 465 SER B 498
REMARK 465 PRO B 499
REMARK 465 GLN B 500
REMARK 465 GLY B 501
REMARK 465 LEU B 502
REMARK 465 ARG B 503
REMARK 465 GLY B 504
REMARK 465 LEU B 505
REMARK 465 PHE B 506
REMARK 465 GLN B 507
REMARK 465 GLU B 572
REMARK 465 GLN B 573
REMARK 465 GLY B 574
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 ALA A 324 68.58 -155.31
REMARK 500 ASP A 397 11.41 -140.44
REMARK 500 ASN A 436 73.19 -111.67
REMARK 500 ASN A 459 -85.56 -101.69
REMARK 500 ASP A 484 -164.70 -118.96
REMARK 500 GLU A 518 -59.00 -124.13
REMARK 500 SER A 542 -122.62 48.14
REMARK 500 SER A 542 -117.87 45.87
REMARK 500 SER A 637 -153.68 -112.56
REMARK 500 ALA B 324 65.45 -155.80
REMARK 500 ALA B 324 65.45 -158.33
REMARK 500 GLU B 343 -146.15 -121.66
REMARK 500 ASN B 436 66.32 -105.76
REMARK 500 ASN B 459 -81.58 -101.66
REMARK 500 ASP B 484 -169.64 -117.63
REMARK 500 GLU B 518 -55.38 -125.65
REMARK 500 SER B 542 -122.61 50.53
REMARK 500 SER B 637 -153.26 -114.27
REMARK 500 SER B 637 -148.14 -114.62
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7B6B A 292 656 UNP F8X1N1 F8X1N1_9BACT 292 656
DBREF 7B6B B 292 656 UNP F8X1N1 F8X1N1_9BACT 292 656
SEQADV 7B6B MET A 271 UNP F8X1N1 INITIATING METHIONINE
SEQADV 7B6B GLY A 272 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER A 273 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER A 274 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 275 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 276 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 277 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 278 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 279 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 280 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER A 281 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER A 282 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLU A 283 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B ASN A 284 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B LEU A 285 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B TYR A 286 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B PHE A 287 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLN A 288 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLY A 289 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS A 290 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER A 291 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B MET B 271 UNP F8X1N1 INITIATING METHIONINE
SEQADV 7B6B GLY B 272 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER B 273 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER B 274 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 275 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 276 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 277 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 278 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 279 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 280 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER B 281 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER B 282 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLU B 283 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B ASN B 284 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B LEU B 285 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B TYR B 286 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B PHE B 287 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLN B 288 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B GLY B 289 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B HIS B 290 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B6B SER B 291 UNP F8X1N1 EXPRESSION TAG
SEQRES 1 A 386 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 386 ASN LEU TYR PHE GLN GLY HIS SER GLU GLU ALA GLU VAL
SEQRES 3 A 386 GLY ILE SER ALA SER THR ASN ILE PRO GLY ALA GLN TYR
SEQRES 4 A 386 PRO GLN ILE LEU SER GLY ASN ARG VAL LEU PHE ARG ILE
SEQRES 5 A 386 LYS ALA PRO ASP ALA LYS ARG VAL GLN VAL ASP LEU GLY
SEQRES 6 A 386 LYS LYS TYR ASP MET VAL ARG GLU GLU GLU GLY SER TRP
SEQRES 7 A 386 ALA ILE THR THR ASP PRO ILE VAL GLU GLY PHE HIS TYR
SEQRES 8 A 386 TYR SER ILE LEU ILE ASP GLY VAL ALA VAL CYS ASP PRO
SEQRES 9 A 386 ALA SER ARG THR PHE TYR GLY MET SER ARG MET ALA SER
SEQRES 10 A 386 GLY ILE GLU ILE PRO GLU GLU GLY VAL ASP TYR TYR ASN
SEQRES 11 A 386 LEU LYS ASN VAL PRO HIS GLY GLN ILE ARG GLN ILE ARG
SEQRES 12 A 386 TYR PHE SER ASP VAL THR LYS ALA TRP ARG ARG ALA PHE
SEQRES 13 A 386 VAL TYR THR PRO ALA GLY TYR ASP ALA ASN THR SER GLN
SEQRES 14 A 386 ARG TYR PRO VAL LEU TYR LEU GLN HIS GLY GLY GLY GLU
SEQRES 15 A 386 ASP GLU THR GLY TRP PRO ASN GLN GLY LYS MET ASP ALA
SEQRES 16 A 386 ILE ILE ASP ASN LEU ILE ALA GLU GLY LYS ALA LYS PRO
SEQRES 17 A 386 MET ILE VAL VAL MET ASP ASN GLY TYR ALA VAL ASP PRO
SEQRES 18 A 386 SER ALA SER SER ALA ASN SER PRO GLN GLY LEU ARG GLY
SEQRES 19 A 386 LEU PHE GLN ASN SER ALA LEU GLU LYS VAL PHE ILE ASN
SEQRES 20 A 386 GLU ILE ILE PRO LEU VAL ASP LYS GLU PHE ARG THR ILE
SEQRES 21 A 386 ALA ASP ARG ASP HIS ARG ALA MET ALA GLY LEU SER MET
SEQRES 22 A 386 GLY GLY PHE GLN ALA PHE GLN ILE ALA MET THR ASN LEU
SEQRES 23 A 386 ASP LYS PHE ALA TYR VAL GLY GLY PHE SER GLY GLY GLY
SEQRES 24 A 386 ILE ILE GLU GLN GLY GLY ASP PHE SER LYS MET TYR ASN
SEQRES 25 A 386 ASN VAL TRP SER ASP VAL ASP THR PHE ASN LYS ARG VAL
SEQRES 26 A 386 LYS LEU ILE TYR LEU SER ILE GLY THR ALA GLU PRO THR
SEQRES 27 A 386 ASN MET TYR GLN THR VAL ASN ASN PHE HIS LYS GLU PHE
SEQRES 28 A 386 GLU LYS ALA GLY ILE LYS HIS VAL TYR TYR GLU SER PRO
SEQRES 29 A 386 GLY THR SER HIS GLU TRP LEU THR TRP ARG ARG SER LEU
SEQRES 30 A 386 ASN GLN PHE ALA GLU LEU LEU PHE LYS
SEQRES 1 B 386 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 386 ASN LEU TYR PHE GLN GLY HIS SER GLU GLU ALA GLU VAL
SEQRES 3 B 386 GLY ILE SER ALA SER THR ASN ILE PRO GLY ALA GLN TYR
SEQRES 4 B 386 PRO GLN ILE LEU SER GLY ASN ARG VAL LEU PHE ARG ILE
SEQRES 5 B 386 LYS ALA PRO ASP ALA LYS ARG VAL GLN VAL ASP LEU GLY
SEQRES 6 B 386 LYS LYS TYR ASP MET VAL ARG GLU GLU GLU GLY SER TRP
SEQRES 7 B 386 ALA ILE THR THR ASP PRO ILE VAL GLU GLY PHE HIS TYR
SEQRES 8 B 386 TYR SER ILE LEU ILE ASP GLY VAL ALA VAL CYS ASP PRO
SEQRES 9 B 386 ALA SER ARG THR PHE TYR GLY MET SER ARG MET ALA SER
SEQRES 10 B 386 GLY ILE GLU ILE PRO GLU GLU GLY VAL ASP TYR TYR ASN
SEQRES 11 B 386 LEU LYS ASN VAL PRO HIS GLY GLN ILE ARG GLN ILE ARG
SEQRES 12 B 386 TYR PHE SER ASP VAL THR LYS ALA TRP ARG ARG ALA PHE
SEQRES 13 B 386 VAL TYR THR PRO ALA GLY TYR ASP ALA ASN THR SER GLN
SEQRES 14 B 386 ARG TYR PRO VAL LEU TYR LEU GLN HIS GLY GLY GLY GLU
SEQRES 15 B 386 ASP GLU THR GLY TRP PRO ASN GLN GLY LYS MET ASP ALA
SEQRES 16 B 386 ILE ILE ASP ASN LEU ILE ALA GLU GLY LYS ALA LYS PRO
SEQRES 17 B 386 MET ILE VAL VAL MET ASP ASN GLY TYR ALA VAL ASP PRO
SEQRES 18 B 386 SER ALA SER SER ALA ASN SER PRO GLN GLY LEU ARG GLY
SEQRES 19 B 386 LEU PHE GLN ASN SER ALA LEU GLU LYS VAL PHE ILE ASN
SEQRES 20 B 386 GLU ILE ILE PRO LEU VAL ASP LYS GLU PHE ARG THR ILE
SEQRES 21 B 386 ALA ASP ARG ASP HIS ARG ALA MET ALA GLY LEU SER MET
SEQRES 22 B 386 GLY GLY PHE GLN ALA PHE GLN ILE ALA MET THR ASN LEU
SEQRES 23 B 386 ASP LYS PHE ALA TYR VAL GLY GLY PHE SER GLY GLY GLY
SEQRES 24 B 386 ILE ILE GLU GLN GLY GLY ASP PHE SER LYS MET TYR ASN
SEQRES 25 B 386 ASN VAL TRP SER ASP VAL ASP THR PHE ASN LYS ARG VAL
SEQRES 26 B 386 LYS LEU ILE TYR LEU SER ILE GLY THR ALA GLU PRO THR
SEQRES 27 B 386 ASN MET TYR GLN THR VAL ASN ASN PHE HIS LYS GLU PHE
SEQRES 28 B 386 GLU LYS ALA GLY ILE LYS HIS VAL TYR TYR GLU SER PRO
SEQRES 29 B 386 GLY THR SER HIS GLU TRP LEU THR TRP ARG ARG SER LEU
SEQRES 30 B 386 ASN GLN PHE ALA GLU LEU LEU PHE LYS
HET SZQ A 701 15
HET SZQ A 702 15
HET CL A 703 1
HET EDO A 704 4
HET EDO B 701 4
HET EDO B 702 4
HETNAM SZQ TRANS-METHYLFERULATE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN SZQ METHYL (~{E})-3-(3-METHOXY-4-OXIDANYL-PHENYL)PROP-2-
HETSYN 2 SZQ ENOATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SZQ 2(C11 H12 O4)
FORMUL 5 CL CL 1-
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 9 HOH *723(H2 O)
HELIX 1 AA1 SER A 314 ASN A 316 5 3
HELIX 2 AA2 LYS A 462 GLU A 473 1 12
HELIX 3 AA3 ASN A 508 GLU A 518 1 11
HELIX 4 AA4 GLU A 518 PHE A 527 1 10
HELIX 5 AA5 ASP A 532 ASP A 534 5 3
HELIX 6 AA6 SER A 542 THR A 554 1 13
HELIX 7 AA7 ASN A 555 PHE A 559 5 5
HELIX 8 AA8 ASP A 576 SER A 578 5 3
HELIX 9 AA9 LYS A 579 VAL A 584 1 6
HELIX 10 AB1 ASP A 587 VAL A 595 1 9
HELIX 11 AB2 PRO A 607 GLY A 625 1 19
HELIX 12 AB3 GLU A 639 LEU A 654 1 16
HELIX 13 AB4 SER B 314 ASN B 316 5 3
HELIX 14 AB5 LYS B 462 GLU B 473 1 12
HELIX 15 AB6 SER B 509 GLU B 518 1 10
HELIX 16 AB7 GLU B 518 PHE B 527 1 10
HELIX 17 AB8 ASP B 532 ASP B 534 5 3
HELIX 18 AB9 SER B 542 THR B 554 1 13
HELIX 19 AC1 ASP B 576 SER B 578 5 3
HELIX 20 AC2 LYS B 579 VAL B 584 1 6
HELIX 21 AC3 ASP B 587 VAL B 595 1 9
HELIX 22 AC4 PRO B 607 GLY B 625 1 19
HELIX 23 AC5 GLU B 639 LEU B 654 1 16
SHEET 1 AA1 5 ILE A 298 SER A 299 0
SHEET 2 AA1 5 GLN A 311 ILE A 312 -1 O ILE A 312 N ILE A 298
SHEET 3 AA1 5 VAL A 318 LYS A 323 -1 O LEU A 319 N GLN A 311
SHEET 4 AA1 5 SER A 347 THR A 351 -1 O TRP A 348 N ILE A 322
SHEET 5 AA1 5 VAL A 341 ARG A 342 -1 N VAL A 341 O ALA A 349
SHEET 1 AA2 4 LYS A 337 ASP A 339 0
SHEET 2 AA2 4 VAL A 330 ASP A 333 -1 N VAL A 332 O TYR A 338
SHEET 3 AA2 4 GLY A 358 ILE A 366 -1 O SER A 363 N ASP A 333
SHEET 4 AA2 4 VAL A 369 VAL A 371 -1 O VAL A 371 N ILE A 364
SHEET 1 AA3 5 LYS A 337 ASP A 339 0
SHEET 2 AA3 5 VAL A 330 ASP A 333 -1 N VAL A 332 O TYR A 338
SHEET 3 AA3 5 GLY A 358 ILE A 366 -1 O SER A 363 N ASP A 333
SHEET 4 AA3 5 ARG A 384 ILE A 391 -1 O ILE A 391 N GLY A 358
SHEET 5 AA3 5 THR A 378 GLY A 381 -1 N PHE A 379 O ALA A 386
SHEET 1 AA416 VAL A 629 SER A 633 0
SHEET 2 AA416 LEU A 597 GLY A 603 1 N ILE A 602 O SER A 633
SHEET 3 AA416 TYR A 561 PHE A 565 1 N GLY A 564 O TYR A 599
SHEET 4 AA416 ARG A 536 LEU A 541 1 N GLY A 540 O PHE A 565
SHEET 5 AA416 VAL A 443 GLN A 447 1 N TYR A 445 O ALA A 537
SHEET 6 AA416 ILE A 480 MET A 483 1 O VAL A 482 N LEU A 444
SHEET 7 AA416 ALA A 421 THR A 429 -1 N PHE A 426 O MET A 483
SHEET 8 AA416 GLN A 408 SER A 416 -1 N TYR A 414 O ARG A 423
SHEET 9 AA416 GLN B 408 SER B 416 -1 O GLN B 411 N ILE A 409
SHEET 10 AA416 ALA B 421 THR B 429 -1 O ARG B 423 N TYR B 414
SHEET 11 AA416 ILE B 480 MET B 483 -1 O VAL B 481 N TYR B 428
SHEET 12 AA416 VAL B 443 GLN B 447 1 N LEU B 446 O VAL B 482
SHEET 13 AA416 ARG B 536 LEU B 541 1 O ALA B 537 N TYR B 445
SHEET 14 AA416 TYR B 561 PHE B 565 1 O PHE B 565 N GLY B 540
SHEET 15 AA416 LEU B 597 GLY B 603 1 O TYR B 599 N GLY B 564
SHEET 16 AA416 VAL B 629 SER B 633 1 O VAL B 629 N ILE B 598
SHEET 1 AA5 5 ILE B 298 SER B 299 0
SHEET 2 AA5 5 GLN B 311 ILE B 312 -1 O ILE B 312 N ILE B 298
SHEET 3 AA5 5 VAL B 318 LYS B 323 -1 O LEU B 319 N GLN B 311
SHEET 4 AA5 5 SER B 347 THR B 351 -1 O ILE B 350 N PHE B 320
SHEET 5 AA5 5 VAL B 341 ARG B 342 -1 N VAL B 341 O ALA B 349
SHEET 1 AA6 4 LYS B 337 ASP B 339 0
SHEET 2 AA6 4 VAL B 330 ASP B 333 -1 N VAL B 332 O TYR B 338
SHEET 3 AA6 4 GLY B 358 ILE B 366 -1 O LEU B 365 N GLN B 331
SHEET 4 AA6 4 VAL B 369 VAL B 371 -1 O VAL B 371 N ILE B 364
SHEET 1 AA7 5 LYS B 337 ASP B 339 0
SHEET 2 AA7 5 VAL B 330 ASP B 333 -1 N VAL B 332 O TYR B 338
SHEET 3 AA7 5 GLY B 358 ILE B 366 -1 O LEU B 365 N GLN B 331
SHEET 4 AA7 5 ARG B 384 ILE B 391 -1 O ILE B 391 N GLY B 358
SHEET 5 AA7 5 THR B 378 GLY B 381 -1 N PHE B 379 O ALA B 386
SSBOND 1 CYS A 372 CYS B 372 1555 1555 2.02
CISPEP 1 TYR A 309 PRO A 310 0 1.61
CISPEP 2 TYR B 309 PRO B 310 0 6.03
CRYST1 73.258 50.511 90.148 90.00 100.14 90.00 P 1 21 1 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 0.013650 0.000000 0.002441 0.00000
SCALE2 0.000000 0.019798 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011269 0.00000
TER 2814 LYS A 656
TER 5685 LYS B 656
MASTER 337 0 6 23 44 0 0 6 6256 2 44 60
END
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