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HEADER HYDROLASE 12-JUN-18 6GRY
TITLE GLUCURONOYL ESTERASE FROM SOLIBACTER USITATUS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDATUS SOLIBACTER USITATUS;
SOURCE 3 ORGANISM_TAXID: 332163;
SOURCE 4 GENE: ACID_4275;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CARBOHYDRATE ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LO LEGGIO,J.LARSBRINK,R.MELAND KNUDSEN,S.MAZURKEWICH,J.C.NAVARRO
AUTHOR 2 POULSEN
REVDAT 1 15-AUG-18 6GRY 0
JRNL AUTH J.ARNLING BAATH,S.MAZURKEWICH,R.M.KNUDSEN,J.N.POULSEN,
JRNL AUTH 2 L.OLSSON,L.LO LEGGIO,J.LARSBRINK
JRNL TITL BIOCHEMICAL AND STRUCTURAL FEATURES OF DIVERSE BACTERIAL
JRNL TITL 2 GLUCURONOYL ESTERASES FACILITATING RECALCITRANT BIOMASS
JRNL TITL 3 CONVERSION.
JRNL REF BIOTECHNOL BIOFUELS V. 11 213 2018
JRNL REFN ESSN 1754-6834
JRNL PMID 30083226
JRNL DOI 10.1186/S13068-018-1213-X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.368
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 29890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.235
REMARK 3 FREE R VALUE TEST SET COUNT : 967
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 47.3013 - 3.8259 0.99 4494 150 0.1597 0.2141
REMARK 3 2 3.8259 - 3.0369 1.00 4226 142 0.1708 0.2133
REMARK 3 3 3.0369 - 2.6531 1.00 4182 139 0.1932 0.2394
REMARK 3 4 2.6531 - 2.4105 1.00 4148 137 0.2117 0.2535
REMARK 3 5 2.4105 - 2.2377 1.00 4130 138 0.2271 0.3086
REMARK 3 6 2.2377 - 2.1058 1.00 4060 136 0.2451 0.3289
REMARK 3 7 2.1058 - 2.0003 0.90 3683 125 0.2752 0.3047
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.258
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.416
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.64
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 : 0.013 3296
REMARK 3 ANGLE : 1.206 4413
REMARK 3 CHIRALITY : 0.059 438
REMARK 3 PLANARITY : 0.008 569
REMARK 3 DIHEDRAL : 15.398 1944
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 6GRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.899
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS BUILT=20180126
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29889
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.11570
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 90.87000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.13_2998
REMARK 200 STARTING MODEL: UNDEPOSITED MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 0.3 M
REMARK 280 DIETHYLENE GLYCOL, 0.3 M TRIETHYLENE GLYCOL, 0.3 M TETRAETHYLENE
REMARK 280 GLYCOL, AND 0.3 M PENTAETHYLENE GLYCOL, 0.05 M TRIS, 0.05 M
REMARK 280 BICINE, 20% V/V PEG500MME, 10% W/V PEG20000, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 142.05600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.28950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.28950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 213.08400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.28950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.28950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.02800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.28950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.28950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 213.08400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.28950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.28950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 71.02800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 142.05600
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 66.0 KCAL/MOL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 21
REMARK 465 HIS A 22
REMARK 465 ILE A 23
REMARK 465 THR A 24
REMARK 465 ASP A 346
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 OE2 GLU A 354 O HOH A 601 2.07
REMARK 500 OE1 GLN A 269 O HOH A 602 2.15
REMARK 500 OE2 GLU A 87 O HOH A 603 2.17
REMARK 500 OD2 ASP A 380 O HOH A 604 2.18
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 O1 EDO A 504 HO1 EDO A 504 7556 1.51
REMARK 500 O1 EDO A 504 O1 EDO A 504 7556 1.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 309 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
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 LEU A 38 37.74 -99.76
REMARK 500 LYS A 55 -58.74 -122.87
REMARK 500 VAL A 68 -73.79 -126.20
REMARK 500 SER A 105 132.89 178.55
REMARK 500 SER A 257 -132.31 64.20
REMARK 500 PRO A 323 41.91 -81.20
REMARK 500 TRP A 348 32.68 -95.40
REMARK 500 ASP A 387 -82.08 -117.15
REMARK 500 HIS A 398 109.27 -52.25
REMARK 500 ASP A 399 -179.18 -172.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 522
DBREF 6GRY A 23 417 UNP Q01YM8 Q01YM8_SOLUE 23 417
SEQADV 6GRY GLY A 21 UNP Q01YM8 EXPRESSION TAG
SEQADV 6GRY HIS A 22 UNP Q01YM8 EXPRESSION TAG
SEQRES 1 A 397 GLY HIS ILE THR ASP GLU ALA LYS VAL PRO ALA TYR THR
SEQRES 2 A 397 LEU PRO ALA VAL LEU ALA LEU LYS SER GLY GLN PRO VAL
SEQRES 3 A 397 THR ASP ALA LYS SER TRP THR THR LYS ARG ARG PRO GLU
SEQRES 4 A 397 ILE LEU ALA ILE TYR GLU ALA GLU VAL TYR GLY LYS SER
SEQRES 5 A 397 PRO ALA ARG PRO PRO LYS LEU ASN TYR GLU VAL LYS SER
SEQRES 6 A 397 VAL GLU LYS GLN ALA LEU GLY GLY LYS ALA THR ARG LYS
SEQRES 7 A 397 ILE VAL THR ILE PHE PHE SER ASP LYS PRO ASP ALA PRO
SEQRES 8 A 397 LYS MET ASP LEU LEU LEU TYR LEU PRO ALA ALA ALA ALA
SEQRES 9 A 397 LYS PRO ALA PRO VAL ILE LEU GLY LEU SER PHE GLY GLY
SEQRES 10 A 397 ILE HIS THR VAL ALA ASN ASP PRO GLY VAL PRO LEU ALA
SEQRES 11 A 397 GLU GLN TRP THR ARG ASP ASN ARG LYS GLN PRO SER ALA
SEQRES 12 A 397 GLU LYS SER ARG GLY GLY GLU ALA SER ARG TRP GLN VAL
SEQRES 13 A 397 GLU LYS ILE LEU ALA ALA GLY TYR GLY LEU ALA THR VAL
SEQRES 14 A 397 TYR TYR GLU GLN ILE GLU PRO ASP PHE ALA GLY GLY MET
SEQRES 15 A 397 LYS TYR GLY ILE ARG PRO LEU PHE PHE LYS PRO GLY GLN
SEQRES 16 A 397 THR GLU PRO GLU PRO GLY ASP TRP GLY ALA VAL ALA ALA
SEQRES 17 A 397 TRP ALA TRP GLY ALA SER ARG ALA MET ASP TYR LEU GLU
SEQRES 18 A 397 LYS ASP LYS ASP VAL ASP ALA ARG ARG VAL GLY LEU ILE
SEQRES 19 A 397 GLY HIS SER ARG LEU GLY LYS ALA ALA ILE TRP ALA GLY
SEQRES 20 A 397 ALA GLN ASP ALA ARG PHE THR PHE ILE ILE SER ASN GLU
SEQRES 21 A 397 SER GLY GLU GLY GLY ALA ALA ILE SER ARG ARG ASP TYR
SEQRES 22 A 397 GLY GLU ARG THR THR ALA LEU ASN THR ARG PHE PRO HIS
SEQRES 23 A 397 TRP PHE ASP GLY ASN TYR LYS LYS TYR ASN ASP ARG GLU
SEQRES 24 A 397 ASN GLU MET PRO PHE ASP SER HIS MET ALA LEU ALA LEU
SEQRES 25 A 397 MET ALA PRO ARG GLY LEU TYR VAL ALA SER ALA GLU GLY
SEQRES 26 A 397 ASP GLN TRP SER ASP PRO LYS GLY GLU PHE LEU GLY ALA
SEQRES 27 A 397 ALA ASN ALA SER PRO VAL TRP GLU LEU PHE GLY LYS LYS
SEQRES 28 A 397 GLY ILE GLY THR MET THR MET PRO ASP LEU HIS GLU PRO
SEQRES 29 A 397 VAL GLY ASP SER VAL ARG TYR HIS ILE ARG ALA GLY LYS
SEQRES 30 A 397 HIS ASP VAL THR GLU TYR ASP TRP GLU GLN TYR LEU LYS
SEQRES 31 A 397 PHE ALA LYS ALA GLN TRP GLY
HET PG4 A 501 31
HET PG4 A 502 31
HET EDO A 503 10
HET EDO A 504 10
HET EDO A 505 10
HET EDO A 506 10
HET EDO A 507 10
HET EDO A 508 10
HET EDO A 509 10
HET EDO A 510 10
HET EDO A 511 10
HET EDO A 512 10
HET EDO A 513 10
HET EDO A 514 10
HET EDO A 515 10
HET PEG A 516 17
HET PEG A 517 17
HET PEG A 518 17
HET PEG A 519 17
HET PEG A 520 17
HET PEG A 521 17
HET PGE A 522 24
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 PG4 2(C8 H18 O5)
FORMUL 4 EDO 13(C2 H6 O2)
FORMUL 17 PEG 6(C4 H10 O3)
FORMUL 23 PGE C6 H14 O4
FORMUL 24 HOH *222(H2 O)
HELIX 1 AA1 ASP A 25 VAL A 29 5 5
HELIX 2 AA2 ASP A 48 LYS A 55 1 8
HELIX 3 AA3 LYS A 55 VAL A 68 1 14
HELIX 4 AA4 ALA A 163 ARG A 167 5 5
HELIX 5 AA5 GLU A 170 GLN A 175 1 6
HELIX 6 AA6 GLN A 175 ALA A 182 1 8
HELIX 7 AA7 GLU A 192 ILE A 194 5 3
HELIX 8 AA8 GLY A 200 GLY A 205 5 6
HELIX 9 AA9 ILE A 206 PHE A 211 5 6
HELIX 10 AB1 GLY A 224 GLU A 241 1 18
HELIX 11 AB2 SER A 257 ASP A 270 1 14
HELIX 12 AB3 ILE A 288 ASP A 292 5 5
HELIX 13 AB4 GLY A 294 PHE A 304 1 11
HELIX 14 AB5 GLY A 310 GLU A 319 5 10
HELIX 15 AB6 ASP A 325 LEU A 332 1 8
HELIX 16 AB7 ASP A 350 SER A 362 1 13
HELIX 17 AB8 SER A 362 LEU A 367 1 6
HELIX 18 AB9 THR A 401 GLY A 417 1 17
SHEET 1 AA110 ASN A 80 ALA A 90 0
SHEET 2 AA110 ALA A 95 PHE A 103 -1 O THR A 101 N GLU A 82
SHEET 3 AA110 LYS A 112 PRO A 120 -1 O LEU A 119 N THR A 96
SHEET 4 AA110 GLY A 185 TYR A 190 -1 O THR A 188 N LEU A 116
SHEET 5 AA110 ALA A 127 SER A 134 1 N SER A 134 O VAL A 189
SHEET 6 AA110 VAL A 246 HIS A 256 1 O GLY A 252 N LEU A 131
SHEET 7 AA110 PHE A 275 ASN A 279 1 O ASN A 279 N GLY A 255
SHEET 8 AA110 GLY A 337 ALA A 343 1 O TYR A 339 N SER A 278
SHEET 9 AA110 VAL A 389 ARG A 394 1 O ARG A 390 N LEU A 338
SHEET 10 AA110 VAL A 385 GLY A 386 -1 N VAL A 385 O TYR A 391
SHEET 1 AA2 2 GLU A 151 TRP A 153 0
SHEET 2 AA2 2 LYS A 159 PRO A 161 -1 O GLN A 160 N GLN A 152
CISPEP 1 ALA A 334 PRO A 335 0 3.08
SITE 1 AC1 7 ARG A 57 ARG A 235 ALA A 268 GLN A 269
SITE 2 AC1 7 ASP A 270 ALA A 271 ARG A 272
SITE 1 AC2 4 LYS A 71 PRO A 73 PHE A 210 ASP A 222
SITE 1 AC3 2 GLY A 369 LYS A 370
SITE 1 AC4 6 GLU A 383 GLU A 406 LYS A 410 HOH A 623
SITE 2 AC4 6 HOH A 626 HOH A 796
SITE 1 AC5 2 VAL A 83 LYS A 88
SITE 1 AC6 2 ARG A 207 HOH A 646
SITE 1 AC7 6 ARG A 75 PRO A 77 ASP A 238 GLU A 241
SITE 2 AC7 6 LYS A 242 HOH A 649
SITE 1 AC8 1 HOH A 673
SITE 1 AC9 3 ARG A 390 LYS A 410 HOH A 635
SITE 1 AD1 3 GLN A 415 HOH A 634 HOH A 738
SITE 1 AD2 2 THR A 53 HOH A 648
SITE 1 AD3 4 LYS A 125 LYS A 165 GLY A 417 HOH A 611
SITE 1 AD4 7 THR A 274 ARG A 336 GLN A 415 PEG A 519
SITE 2 AD4 7 HOH A 607 HOH A 694 HOH A 738
SITE 1 AD5 2 ASN A 80 ASP A 106
SITE 1 AD6 3 SER A 257 PGE A 522 HOH A 651
SITE 1 AD7 7 LYS A 261 GLY A 282 GLU A 283 ARG A 296
SITE 2 AD7 7 TRP A 348 HOH A 633 HOH A 723
SITE 1 AD8 2 ASP A 350 HOH A 700
SITE 1 AD9 6 PRO A 335 LYS A 370 SER A 388 GLN A 415
SITE 2 AD9 6 EDO A 514 HOH A 751
SITE 1 AE1 4 LYS A 112 ASP A 114 PRO A 148 HOH A 791
SITE 1 AE2 1 ASP A 317
SITE 1 AE3 5 TYR A 191 GLU A 192 ASP A 197 PEG A 516
SITE 2 AE3 5 HOH A 678
CRYST1 54.579 54.579 284.112 90.00 90.00 90.00 P 43 21 2 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 0.018322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003520 0.00000
TER 6112 GLY A 417
MASTER 393 0 22 18 12 0 28 6 3413 1 318 31
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