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HEADER SUGAR BINDING PROTEIN 23-OCT-22 8BF3
TITLE CRYSTAL STRUCTURE OF FERULOYL ESTERASE WTSFAE1B IN COMPLEX WITH
TITLE 2 XYLOBIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULOYL ESTERASE, COMPLEX, (ALPHA/BETA/ALPHA)-SANDWICH, SUGAR
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WILKENS
REVDAT 1 30-NOV-22 8BF3 0
JRNL AUTH C.WILKENS
JRNL TITL CRYSTAL STRUCTURE OF FERULOYL ESTERASE WTSFAE1B IN COMPLEX
JRNL TITL 2 WITH XYLOBIOSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 272728
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.117
REMARK 3 R VALUE (WORKING SET) : 0.117
REMARK 3 FREE R VALUE : 0.138
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.050
REMARK 3 FREE R VALUE TEST SET COUNT : 5520
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 40.4700 - 3.7000 1.00 17709 183 0.1268 0.1357
REMARK 3 2 3.7000 - 2.9300 1.00 17751 185 0.1106 0.1324
REMARK 3 3 2.9300 - 2.5600 1.00 17754 192 0.1071 0.1199
REMARK 3 4 2.5600 - 2.3300 1.00 17737 190 0.0984 0.1389
REMARK 3 5 2.3300 - 2.1600 1.00 17729 182 0.0933 0.1101
REMARK 3 6 2.1600 - 2.0300 1.00 17778 182 0.0932 0.1075
REMARK 3 7 2.0300 - 1.9300 1.00 17738 187 0.0875 0.1283
REMARK 3 8 1.9300 - 1.8500 1.00 17754 190 0.0914 0.1193
REMARK 3 9 1.8500 - 1.7800 1.00 17742 184 0.0896 0.1161
REMARK 3 10 1.7800 - 1.7200 1.00 17753 190 0.0840 0.1108
REMARK 3 11 1.7200 - 1.6600 1.00 17745 193 0.0863 0.1033
REMARK 3 12 1.6600 - 1.6200 1.00 17800 187 0.0867 0.1111
REMARK 3 13 1.6200 - 1.5700 1.00 17744 189 0.0883 0.1110
REMARK 3 14 1.5700 - 1.5300 1.00 17741 187 0.0959 0.1324
REMARK 3 15 1.5300 - 1.5000 1.00 17717 188 0.1073 0.1324
REMARK 3 16 1.5000 - 1.4700 1.00 17734 189 0.1156 0.1330
REMARK 3 17 1.4700 - 1.4400 1.00 17751 192 0.1252 0.1468
REMARK 3 18 1.4400 - 1.4100 1.00 17803 189 0.1349 0.1484
REMARK 3 19 1.4100 - 1.3900 1.00 17700 185 0.1416 0.1560
REMARK 3 20 1.3900 - 1.3600 1.00 17731 189 0.1574 0.1668
REMARK 3 21 1.3600 - 1.3400 1.00 17734 186 0.1673 0.1779
REMARK 3 22 1.3400 - 1.3200 1.00 17819 189 0.1826 0.1945
REMARK 3 23 1.3200 - 1.3000 1.00 17737 189 0.2011 0.2397
REMARK 3 24 1.3000 - 1.2800 1.00 17654 183 0.2241 0.2269
REMARK 3 25 1.2800 - 1.2600 0.98 17316 185 0.2419 0.2747
REMARK 3 26 1.2600 - 1.2500 0.95 16989 180 0.2504 0.2791
REMARK 3 27 1.2500 - 1.2300 0.95 16869 175 0.2568 0.2781
REMARK 3 28 1.2300 - 1.2200 0.90 15883 167 0.2706 0.3373
REMARK 3 29 1.2200 - 1.2000 0.86 15237 162 0.2785 0.2442
REMARK 3 30 1.2000 - 1.1900 0.82 14519 151 0.2906 0.3329
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) : 0.115
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.32
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 : 0.006 5939
REMARK 3 ANGLE : 0.884 8065
REMARK 3 CHIRALITY : 0.075 847
REMARK 3 PLANARITY : 0.008 1056
REMARK 3 DIHEDRAL : 11.953 2193
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 8BF3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292126237.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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) : 0.976
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 : 272728
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.190
REMARK 200 RESOLUTION RANGE LOW (A) : 40.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 12.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23
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: 8BBP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000; 0.1M HEPES PH 7; 0.2M
REMARK 280 LICL, 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 32.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.47000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.47000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.67500
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLN A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 PRO A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 ARG A 13
REMARK 465 PRO A 14
REMARK 465 GLY A 15
REMARK 465 PHE A 16
REMARK 465 ARG A 17
REMARK 465 ALA A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 224
REMARK 465 THR A 225
REMARK 465 GLN A 226
REMARK 465 GLY A 227
REMARK 465 GLN A 228
REMARK 465 GLN A 229
REMARK 465 GLY A 230
REMARK 465 ILE A 231
REMARK 465 PRO A 232
REMARK 465 SER A 233
REMARK 465 GLY A 234
REMARK 465 SER A 235
REMARK 465 GLY A 236
REMARK 465 ALA A 301
REMARK 465 GLY A 302
REMARK 465 ARG A 303
REMARK 465 GLN A 304
REMARK 465 GLN A 305
REMARK 465 GLY A 306
REMARK 465 ALA A 307
REMARK 465 ASP A 308
REMARK 465 ALA A 309
REMARK 465 GLU A 310
REMARK 465 LYS A 311
REMARK 465 ILE A 312
REMARK 465 LEU A 387
REMARK 465 LEU A 388
REMARK 465 GLN B 1
REMARK 465 VAL B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 PRO B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 ARG B 13
REMARK 465 PRO B 14
REMARK 465 GLY B 15
REMARK 465 PHE B 16
REMARK 465 ARG B 17
REMARK 465 ALA B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 224
REMARK 465 THR B 225
REMARK 465 GLN B 226
REMARK 465 GLY B 227
REMARK 465 GLN B 228
REMARK 465 GLN B 229
REMARK 465 GLY B 230
REMARK 465 ILE B 231
REMARK 465 PRO B 232
REMARK 465 SER B 233
REMARK 465 GLY B 234
REMARK 465 SER B 235
REMARK 465 GLY B 236
REMARK 465 MET B 237
REMARK 465 ARG B 303
REMARK 465 GLN B 304
REMARK 465 GLN B 305
REMARK 465 GLY B 306
REMARK 465 LEU B 387
REMARK 465 LEU B 388
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 ALA B 307 CB
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 HZ2 LYS A 197 O HOH A 507 1.41
REMARK 500 HG1 THR A 261 O HOH A 509 1.55
REMARK 500 HH TYR A 163 O HOH A 503 1.57
REMARK 500 O HOH B 503 O HOH B 823 1.68
REMARK 500 O HOH A 813 O HOH A 863 1.76
REMARK 500 O HOH B 769 O HOH B 854 1.80
REMARK 500 O HOH B 854 O HOH B 907 1.82
REMARK 500 O2 XYP B 403 O HOH B 501 1.82
REMARK 500 O HOH A 511 O HOH A 759 1.83
REMARK 500 O HOH B 807 O HOH B 820 1.86
REMARK 500 O HOH B 807 O HOH B 937 1.86
REMARK 500 OG SER A 43 O HOH A 501 1.88
REMARK 500 OH TYR B 163 O HOH B 502 1.89
REMARK 500 O HOH B 501 O HOH B 556 1.89
REMARK 500 O HOH A 813 O HOH A 948 1.90
REMARK 500 O HOH A 863 O HOH A 948 1.91
REMARK 500 O HOH A 800 O HOH A 948 1.91
REMARK 500 O ASP A 41 O HOH A 502 1.93
REMARK 500 O HOH A 947 O HOH A 960 1.93
REMARK 500 OE1 GLN B 108 O HOH B 503 1.95
REMARK 500 O VAL B 222 O HOH B 504 1.98
REMARK 500 O HOH B 515 O HOH B 788 1.98
REMARK 500 O HOH A 570 O HOH A 849 1.99
REMARK 500 O HOH A 699 O HOH A 834 1.99
REMARK 500 OH TYR A 163 O HOH A 503 2.00
REMARK 500 O HOH A 545 O HOH A 887 2.00
REMARK 500 O HOH A 853 O HOH A 893 2.01
REMARK 500 O HOH B 877 O HOH B 906 2.01
REMARK 500 O HOH A 960 O HOH B 863 2.02
REMARK 500 O HOH A 882 O HOH A 977 2.03
REMARK 500 O HOH A 898 O HOH A 969 2.03
REMARK 500 O HOH A 842 O HOH A 864 2.03
REMARK 500 O HOH A 525 O HOH A 762 2.05
REMARK 500 O HOH A 771 O HOH A 947 2.05
REMARK 500 O HOH B 624 O HOH B 813 2.07
REMARK 500 O HOH A 824 O HOH A 879 2.07
REMARK 500 O HOH B 531 O HOH B 887 2.08
REMARK 500 O HOH A 737 O HOH A 998 2.08
REMARK 500 O HOH A 878 O HOH A 899 2.09
REMARK 500 OE1 GLN A 161 O HOH A 504 2.09
REMARK 500 O HOH B 734 O HOH B 935 2.09
REMARK 500 O HOH B 789 O HOH B 919 2.10
REMARK 500 NZ LYS B 197 O HOH B 505 2.11
REMARK 500 O HOH B 706 O HOH B 903 2.12
REMARK 500 N GLU A 313 O HOH A 505 2.13
REMARK 500 O HOH A 832 O HOH A 886 2.13
REMARK 500 O HOH A 518 O HOH A 847 2.13
REMARK 500 O HOH A 854 O HOH B 879 2.13
REMARK 500 O HOH B 932 O HOH B 953 2.14
REMARK 500 O HOH B 844 O HOH B 852 2.14
REMARK 500
REMARK 500 THIS ENTRY HAS 57 CLOSE CONTACTS
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 HH12 ARG B 162 OD2 ASP B 317 4545 1.59
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 SER A 39 122.98 -172.09
REMARK 500 GLU A 79 168.69 177.25
REMARK 500 ASP A 175 -179.53 -170.09
REMARK 500 SER A 272 -122.31 53.33
REMARK 500 SER B 39 120.86 -171.64
REMARK 500 GLU B 79 167.73 175.33
REMARK 500 ASP B 175 -179.68 -170.41
REMARK 500 SER B 272 -118.51 51.21
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 A1031 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1032 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A1033 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1034 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A1035 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1036 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A1037 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A1038 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A1039 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH B 997 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 998 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 999 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B1002 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B1003 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B1004 DISTANCE = 6.50 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8BBP RELATED DB: PDB
REMARK 900 APO STRUCTURE
REMARK 900 RELATED ID: 6RZN RELATED DB: PDB
REMARK 900 APO STRUCTURE
DBREF1 8BF3 A 1 386 UNP A0A5S8WFA0_9BACT
DBREF2 8BF3 A A0A5S8WFA0 1 386
DBREF1 8BF3 B 1 386 UNP A0A5S8WFA0_9BACT
DBREF2 8BF3 B A0A5S8WFA0 1 386
SEQADV 8BF3 LEU A 387 UNP A0A5S8WFA EXPRESSION TAG
SEQADV 8BF3 LEU A 388 UNP A0A5S8WFA EXPRESSION TAG
SEQADV 8BF3 LEU B 387 UNP A0A5S8WFA EXPRESSION TAG
SEQADV 8BF3 LEU B 388 UNP A0A5S8WFA EXPRESSION TAG
SEQRES 1 A 388 GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG
SEQRES 2 A 388 PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU
SEQRES 3 A 388 ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER
SEQRES 4 A 388 LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN
SEQRES 5 A 388 THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP
SEQRES 6 A 388 THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO
SEQRES 7 A 388 GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS
SEQRES 8 A 388 ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY
SEQRES 9 A 388 THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU
SEQRES 10 A 388 SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY
SEQRES 11 A 388 THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY
SEQRES 12 A 388 PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR
SEQRES 13 A 388 GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU
SEQRES 14 A 388 HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET
SEQRES 15 A 388 GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN
SEQRES 16 A 388 GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY
SEQRES 17 A 388 ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO
SEQRES 18 A 388 VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY
SEQRES 19 A 388 SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS
SEQRES 20 A 388 ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU
SEQRES 21 A 388 THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET
SEQRES 22 A 388 GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO
SEQRES 23 A 388 GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE
SEQRES 24 A 388 MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE
SEQRES 25 A 388 GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS
SEQRES 26 A 388 SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP
SEQRES 27 A 388 ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR
SEQRES 28 A 388 LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER
SEQRES 29 A 388 THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU
SEQRES 30 A 388 SER GLU PHE ALA PRO MET LEU PHE LYS LEU LEU
SEQRES 1 B 388 GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG
SEQRES 2 B 388 PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU
SEQRES 3 B 388 ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER
SEQRES 4 B 388 LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN
SEQRES 5 B 388 THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP
SEQRES 6 B 388 THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO
SEQRES 7 B 388 GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS
SEQRES 8 B 388 ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY
SEQRES 9 B 388 THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU
SEQRES 10 B 388 SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY
SEQRES 11 B 388 THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY
SEQRES 12 B 388 PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR
SEQRES 13 B 388 GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU
SEQRES 14 B 388 HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET
SEQRES 15 B 388 GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN
SEQRES 16 B 388 GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY
SEQRES 17 B 388 ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO
SEQRES 18 B 388 VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY
SEQRES 19 B 388 SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS
SEQRES 20 B 388 ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU
SEQRES 21 B 388 THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET
SEQRES 22 B 388 GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO
SEQRES 23 B 388 GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE
SEQRES 24 B 388 MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE
SEQRES 25 B 388 GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS
SEQRES 26 B 388 SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP
SEQRES 27 B 388 ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR
SEQRES 28 B 388 LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER
SEQRES 29 B 388 THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU
SEQRES 30 B 388 SER GLU PHE ALA PRO MET LEU PHE LYS LEU LEU
HET XYP C 1 19
HET XYP C 2 18
HET EDO A 401 10
HET EDO A 402 10
HET EDO A 403 10
HET EDO A 404 10
HET EDO A 405 10
HET EDO A 406 10
HET EDO B 401 10
HET EDO B 402 10
HET XYP B 403 20
HET EDO B 404 10
HET EDO B 405 10
HET EDO B 406 10
HET EDO B 407 10
HET EDO B 408 10
HET EDO B 409 10
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 XYP 3(C5 H10 O5)
FORMUL 4 EDO 14(C2 H6 O2)
FORMUL 19 HOH *1043(H2 O)
HELIX 1 AA1 GLY A 54 VAL A 58 5 5
HELIX 2 AA2 GLY A 115 PHE A 122 5 8
HELIX 3 AA3 ASP A 177 MET A 182 1 6
HELIX 4 AA4 ARG A 184 GLN A 195 1 12
HELIX 5 AA5 GLY A 239 ASP A 248 1 10
HELIX 6 AA6 ASP A 248 PHE A 257 1 10
HELIX 7 AA7 GLY A 262 ASP A 264 5 3
HELIX 8 AA8 SER A 272 ASN A 285 1 14
HELIX 9 AA9 LYS A 314 LYS A 325 1 12
HELIX 10 AB1 VAL A 341 HIS A 355 1 15
HELIX 11 AB2 THR A 369 ALA A 381 1 13
HELIX 12 AB3 PRO A 382 LEU A 384 5 3
HELIX 13 AB4 GLY B 54 VAL B 58 5 5
HELIX 14 AB5 GLY B 115 PHE B 122 5 8
HELIX 15 AB6 ASP B 177 MET B 182 1 6
HELIX 16 AB7 ARG B 184 GLN B 195 1 12
HELIX 17 AB8 GLY B 239 ASP B 248 1 10
HELIX 18 AB9 ASP B 248 PHE B 257 1 10
HELIX 19 AC1 GLY B 262 ASP B 264 5 3
HELIX 20 AC2 SER B 272 ASN B 285 1 14
HELIX 21 AC3 ASP B 308 LYS B 325 1 18
HELIX 22 AC4 VAL B 341 HIS B 355 1 15
HELIX 23 AC5 THR B 369 ALA B 381 1 13
HELIX 24 AC6 PRO B 382 LEU B 384 5 3
SHEET 1 AA1 4 GLU A 26 ILE A 27 0
SHEET 2 AA1 4 VAL A 33 TYR A 38 -1 O THR A 34 N GLU A 26
SHEET 3 AA1 4 MET A 68 VAL A 73 -1 O PHE A 69 N VAL A 37
SHEET 4 AA1 4 VAL A 62 LYS A 63 -1 N VAL A 62 O SER A 70
SHEET 1 AA2 4 GLU A 59 GLU A 60 0
SHEET 2 AA2 4 VAL A 45 GLY A 49 -1 N ILE A 47 O GLU A 59
SHEET 3 AA2 4 GLU A 79 VAL A 87 -1 O ASN A 84 N THR A 48
SHEET 4 AA2 4 VAL A 90 ALA A 92 -1 O VAL A 90 N VAL A 87
SHEET 1 AA3 5 GLU A 59 GLU A 60 0
SHEET 2 AA3 5 VAL A 45 GLY A 49 -1 N ILE A 47 O GLU A 59
SHEET 3 AA3 5 GLU A 79 VAL A 87 -1 O ASN A 84 N THR A 48
SHEET 4 AA3 5 ASN A 106 ILE A 113 -1 O PHE A 111 N TYR A 81
SHEET 5 AA3 5 VAL A 100 ASP A 103 -1 N ARG A 101 O GLN A 108
SHEET 1 AA416 VAL A 360 SER A 364 0
SHEET 2 AA416 LEU A 330 GLY A 336 1 N ILE A 333 O ARG A 362
SHEET 3 AA416 TYR A 291 PHE A 295 1 N ILE A 292 O TRP A 332
SHEET 4 AA416 ARG A 266 LEU A 271 1 N GLY A 270 O PHE A 295
SHEET 5 AA416 VAL A 165 LEU A 169 1 N TYR A 167 O ALA A 267
SHEET 6 AA416 ILE A 202 MET A 205 1 O VAL A 204 N LEU A 168
SHEET 7 AA416 ARG A 146 THR A 152 -1 N TYR A 149 O MET A 205
SHEET 8 AA416 THR A 131 TYR A 137 -1 N THR A 133 O VAL A 150
SHEET 9 AA416 THR B 131 TYR B 137 -1 O LYS B 134 N VAL A 132
SHEET 10 AA416 ARG B 146 THR B 152 -1 O VAL B 150 N THR B 133
SHEET 11 AA416 ILE B 202 MET B 205 -1 O MET B 205 N TYR B 149
SHEET 12 AA416 VAL B 165 LEU B 169 1 N LEU B 168 O VAL B 204
SHEET 13 AA416 ARG B 266 LEU B 271 1 O ALA B 267 N TYR B 167
SHEET 14 AA416 TYR B 291 PHE B 295 1 O PHE B 295 N GLY B 270
SHEET 15 AA416 LEU B 330 GLY B 336 1 O TRP B 332 N ILE B 292
SHEET 16 AA416 VAL B 360 SER B 364 1 O ARG B 362 N ILE B 333
SHEET 1 AA5 4 GLU B 26 ILE B 27 0
SHEET 2 AA5 4 VAL B 33 TYR B 38 -1 O THR B 34 N GLU B 26
SHEET 3 AA5 4 MET B 68 VAL B 73 -1 O PHE B 69 N VAL B 37
SHEET 4 AA5 4 VAL B 62 LYS B 63 -1 N VAL B 62 O SER B 70
SHEET 1 AA6 4 GLU B 59 GLU B 60 0
SHEET 2 AA6 4 VAL B 45 GLY B 49 -1 N ILE B 47 O GLU B 59
SHEET 3 AA6 4 GLU B 79 VAL B 87 -1 O ASN B 84 N THR B 48
SHEET 4 AA6 4 VAL B 90 ALA B 92 -1 O VAL B 90 N VAL B 87
SHEET 1 AA7 5 GLU B 59 GLU B 60 0
SHEET 2 AA7 5 VAL B 45 GLY B 49 -1 N ILE B 47 O GLU B 59
SHEET 3 AA7 5 GLU B 79 VAL B 87 -1 O ASN B 84 N THR B 48
SHEET 4 AA7 5 ASN B 106 ILE B 113 -1 O PHE B 111 N TYR B 81
SHEET 5 AA7 5 VAL B 100 ASP B 103 -1 N ARG B 101 O GLN B 108
LINK O4 XYP C 1 C1 XYP C 2 1555 1555 1.37
CISPEP 1 SER A 24 PRO A 25 0 -7.82
CISPEP 2 GLY A 74 PRO A 75 0 7.08
CISPEP 3 SER B 24 PRO B 25 0 -7.88
CISPEP 4 GLY B 74 PRO B 75 0 6.73
CRYST1 65.580 99.350 132.940 90.00 90.00 90.00 P 21 21 21 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 0.015249 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007522 0.00000
TER 5612 LYS A 386
TER 11132 LYS B 386
MASTER 457 0 17 24 42 0 0 6 6570 2 197 60
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