| content |
HEADER HYDROLASE 07-DEC-20 7B5V
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
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 7B5V 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 94391
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 7079
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 42.0800 - 5.2700 0.99 3004 244 0.1367 0.2040
REMARK 3 2 5.2700 - 4.1800 1.00 2967 241 0.1048 0.1611
REMARK 3 3 4.1800 - 3.6500 1.00 2918 236 0.1286 0.1416
REMARK 3 4 3.6500 - 3.3200 1.00 2968 241 0.1510 0.2112
REMARK 3 5 3.3200 - 3.0800 1.00 2938 238 0.1678 0.2020
REMARK 3 6 3.0800 - 2.9000 1.00 2922 238 0.1810 0.2208
REMARK 3 7 2.9000 - 2.7500 1.00 2916 235 0.1833 0.2336
REMARK 3 8 2.7500 - 2.6300 1.00 2908 236 0.1847 0.2200
REMARK 3 9 2.6300 - 2.5300 1.00 2956 240 0.1893 0.2195
REMARK 3 10 2.5300 - 2.4500 1.00 2901 236 0.1839 0.2104
REMARK 3 11 2.4500 - 2.3700 1.00 2918 236 0.1790 0.2155
REMARK 3 12 2.3700 - 2.3000 1.00 2973 242 0.1758 0.2304
REMARK 3 13 2.3000 - 2.2400 1.00 2884 233 0.1805 0.2094
REMARK 3 14 2.2400 - 2.1900 1.00 2922 237 0.1793 0.2228
REMARK 3 15 2.1900 - 2.1400 1.00 2918 238 0.1747 0.2209
REMARK 3 16 2.1400 - 2.0900 1.00 2932 237 0.1787 0.2327
REMARK 3 17 2.0900 - 2.0500 1.00 2900 235 0.1784 0.2101
REMARK 3 18 2.0500 - 2.0100 1.00 2931 237 0.1845 0.2322
REMARK 3 19 2.0100 - 1.9700 1.00 2918 237 0.1968 0.2298
REMARK 3 20 1.9700 - 1.9400 1.00 2874 234 0.2156 0.2458
REMARK 3 21 1.9400 - 1.9100 1.00 2959 239 0.2405 0.2867
REMARK 3 22 1.9100 - 1.8800 1.00 2863 232 0.2338 0.2943
REMARK 3 23 1.8800 - 1.8500 1.00 2939 238 0.2374 0.2656
REMARK 3 24 1.8500 - 1.8300 1.00 2887 234 0.2481 0.2670
REMARK 3 25 1.8300 - 1.8000 1.00 2930 238 0.2609 0.2953
REMARK 3 26 1.8000 - 1.7800 1.00 2917 236 0.2819 0.2998
REMARK 3 27 1.7800 - 1.7600 1.00 2919 237 0.2938 0.3335
REMARK 3 28 1.7600 - 1.7400 1.00 2858 232 0.3128 0.2982
REMARK 3 29 1.7400 - 1.7200 1.00 2944 239 0.3259 0.3703
REMARK 3 30 1.7200 - 1.7000 0.87 2528 203 0.4008 0.4179
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) : 0.224
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.64
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 5777
REMARK 3 ANGLE : 0.875 7827
REMARK 3 CHIRALITY : 0.061 814
REMARK 3 PLANARITY : 0.005 1030
REMARK 3 DIHEDRAL : 20.040 2118
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 7B5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112713.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
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 : 94462
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.697
REMARK 200 RESOLUTION RANGE LOW (A) : 42.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW, MORDA
REMARK 200 STARTING MODEL: 6NE9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG - B9 - 0.1 M CITRATE PH 5, 20%
REMARK 280 PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 51.98100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.48300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.98100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.48300
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 809 LIES ON A SPECIAL POSITION.
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 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 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 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 ASN B 508
REMARK 465 GLU B 572
REMARK 465 GLN B 573
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 292 CB
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 GLU A 295 -41.06 -142.52
REMARK 500 ALA A 324 64.52 -159.92
REMARK 500 GLU A 343 -152.27 -122.63
REMARK 500 ASP A 397 21.24 -144.04
REMARK 500 ASN A 459 -81.99 -103.77
REMARK 500 ASP A 484 -169.76 -111.58
REMARK 500 GLU A 518 -54.48 -124.08
REMARK 500 SER A 542 -119.83 47.32
REMARK 500 ASN A 555 48.02 -142.81
REMARK 500 SER A 637 -150.63 -115.99
REMARK 500 ALA B 324 64.64 -157.88
REMARK 500 GLU B 345 30.03 -91.83
REMARK 500 ASP B 397 20.66 -146.76
REMARK 500 ASN B 459 -83.98 -103.79
REMARK 500 ASP B 484 -167.67 -116.60
REMARK 500 GLU B 518 -59.87 -123.60
REMARK 500 SER B 542 -122.15 49.25
REMARK 500 SER B 637 -151.53 -119.47
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 B1134 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B1135 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH B1136 DISTANCE = 6.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 701
DBREF 7B5V A 292 656 UNP F8X1N1 F8X1N1_9BACT 292 656
DBREF 7B5V B 292 656 UNP F8X1N1 F8X1N1_9BACT 292 656
SEQADV 7B5V MET A 271 UNP F8X1N1 INITIATING METHIONINE
SEQADV 7B5V GLY A 272 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER A 273 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER A 274 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 275 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 276 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 277 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 278 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 279 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 280 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER A 281 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER A 282 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLU A 283 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V ASN A 284 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V LEU A 285 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V TYR A 286 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V PHE A 287 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLN A 288 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLY A 289 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS A 290 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER A 291 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V MET B 271 UNP F8X1N1 INITIATING METHIONINE
SEQADV 7B5V GLY B 272 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER B 273 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER B 274 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 275 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 276 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 277 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 278 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 279 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 280 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER B 281 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V SER B 282 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLU B 283 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V ASN B 284 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V LEU B 285 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V TYR B 286 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V PHE B 287 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLN B 288 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V GLY B 289 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V HIS B 290 UNP F8X1N1 EXPRESSION TAG
SEQADV 7B5V 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 CL A 701 1
HET PEG A 702 7
HET EDO B 701 4
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL CL 1-
FORMUL 4 PEG C4 H10 O3
FORMUL 5 EDO C2 H6 O2
FORMUL 6 HOH *648(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 ASP A 576 SER A 578 5 3
HELIX 8 AA8 LYS A 579 VAL A 584 1 6
HELIX 9 AA9 ASP A 587 VAL A 595 1 9
HELIX 10 AB1 PRO A 607 GLY A 625 1 19
HELIX 11 AB2 GLU A 639 LEU A 654 1 16
HELIX 12 AB3 LYS B 462 GLU B 473 1 12
HELIX 13 AB4 ALA B 510 GLU B 518 1 9
HELIX 14 AB5 GLU B 518 PHE B 527 1 10
HELIX 15 AB6 ASP B 532 ASP B 534 5 3
HELIX 16 AB7 SER B 542 THR B 554 1 13
HELIX 17 AB8 ASP B 576 SER B 578 5 3
HELIX 18 AB9 LYS B 579 VAL B 584 1 6
HELIX 19 AC1 ASP B 587 VAL B 595 1 9
HELIX 20 AC2 PRO B 607 GLY B 625 1 19
HELIX 21 AC3 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 598 O VAL A 629
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 539
SHEET 6 AA416 ILE A 480 MET A 483 1 O VAL A 482 N LEU A 446
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 PHE B 415 -1 O GLN B 411 N ILE A 409
SHEET 10 AA416 TRP B 422 THR B 429 -1 O ARG B 423 N TYR B 414
SHEET 11 AA416 ILE B 480 MET B 483 -1 O MET B 483 N PHE B 426
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 539 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 SER B 633 N ILE B 602
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 ARG B 317 LYS B 323 -1 O LEU B 319 N GLN B 311
SHEET 4 AA5 5 SER B 347 PRO B 354 -1 O TRP B 348 N ILE B 322
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
CISPEP 1 TYR A 309 PRO A 310 0 4.36
CISPEP 2 TYR B 309 PRO B 310 0 5.33
SITE 1 AC1 4 GLY A 450 SER A 542 MET A 543 HOH A 997
SITE 1 AC2 7 GLY A 306 ALA A 307 GLN A 308 TYR A 309
SITE 2 AC2 7 ALA A 375 HOH A 811 HOH A 913
SITE 1 AC3 4 ASP A 326 ARG B 329 ASP B 367 GLY B 368
CRYST1 103.962 80.966 107.350 90.00 105.67 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 0.009619 0.000000 0.002698 0.00000
SCALE2 0.000000 0.012351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009675 0.00000
TER 2816 LYS A 656
TER 5624 LYS B 656
MASTER 381 0 3 21 44 0 4 6 6191 2 11 60
END |