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HEADER HYDROLASE 01-OCT-19 6SZ4
TITLE THE GLUCURONOYL ESTERASE OTCE15A H408A VARIANT FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH, AND COVALENTLY LINKED TO, D-GLUCURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE PB90-1;
SOURCE 3 ORGANISM_TAXID: 452637;
SOURCE 4 GENE: OTER_0116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, COMPLEX, BIOMASS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 27-NOV-19 6SZ4 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE GLUCURONOYL ESTERASE OTCE15A H408A VARIANT FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH, AND COVALENTLY LINKED TO,
JRNL TITL 3 D-GLUCURONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 30624
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.460
REMARK 3 FREE R VALUE TEST SET COUNT : 2286
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 45.5600 - 4.4100 0.98 1813 146 0.1551 0.2121
REMARK 3 2 4.4100 - 3.5000 0.97 1822 147 0.1588 0.2327
REMARK 3 3 3.5000 - 3.0600 0.97 1793 149 0.1950 0.2611
REMARK 3 4 3.0600 - 2.7800 0.97 1795 144 0.2000 0.2650
REMARK 3 5 2.7800 - 2.5800 0.97 1818 146 0.2017 0.2445
REMARK 3 6 2.5800 - 2.4200 0.96 1774 142 0.2080 0.3089
REMARK 3 7 2.4200 - 2.3000 0.97 1787 145 0.2178 0.3205
REMARK 3 8 2.3000 - 2.2000 0.96 1799 148 0.2420 0.3071
REMARK 3 9 2.2000 - 2.1200 0.96 1781 146 0.2484 0.3305
REMARK 3 10 2.1200 - 2.0500 0.96 1777 140 0.2634 0.3493
REMARK 3 11 2.0500 - 1.9800 0.95 1764 145 0.2896 0.3337
REMARK 3 12 1.9800 - 1.9200 0.95 1760 138 0.3061 0.3975
REMARK 3 13 1.9200 - 1.8700 0.95 1740 145 0.3406 0.3669
REMARK 3 14 1.8700 - 1.8300 0.95 1792 142 0.3650 0.4638
REMARK 3 15 1.8300 - 1.7900 0.94 1756 141 0.4049 0.4955
REMARK 3 16 1.7900 - 1.7500 0.84 1567 122 0.4333 0.5221
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) : 38.923
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.37
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 : 0.012 3198
REMARK 3 ANGLE : 1.181 4373
REMARK 3 CHIRALITY : 0.060 465
REMARK 3 PLANARITY : 0.009 583
REMARK 3 DIHEDRAL : 21.536 1145
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 6SZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30662
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.749
REMARK 200 RESOLUTION RANGE LOW (A) : 45.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.09829
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.82850
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472
REMARK 200 STARTING MODEL: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION OF 0.2 M AMMONIUM FORMATE NONE 20 % W/V PEG 3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 MET A 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLU A 24
REMARK 465 ASN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 PHE A 28
REMARK 465 GLN A 29
REMARK 465 GLY A 30
REMARK 465 HIS A 31
REMARK 465 SER A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 432
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 ARG A 51 NE - CZ - NH1 ANGL. DEV. = -3.5 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 THR A 35 140.83 -176.01
REMARK 500 VAL A 70 -72.96 -120.11
REMARK 500 ASP A 150 104.12 -30.10
REMARK 500 ASN A 169 40.80 72.40
REMARK 500 ALA A 222 72.10 45.38
REMARK 500 ALA A 223 44.75 -69.14
REMARK 500 ASP A 226 -63.63 -123.02
REMARK 500 SER A 267 -121.65 52.80
REMARK 500 HIS A 328 39.90 -142.51
REMARK 500 ASP A 360 70.58 53.72
REMARK 500 LYS A 427 137.85 -11.47
REMARK 500 ALA A 429 30.73 -83.03
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 FMT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BDP A 501 bound
REMARK 800 to SER A 267
DBREF 6SZ4 A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6SZ4 MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6SZ4 GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SZ4 ALA A 408 UNP B1ZMF4 HIS 408 ENGINEERED MUTATION
SEQRES 1 A 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 A 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 A 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 A 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 A 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 A 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 A 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 A 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 A 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 A 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 A 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 A 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 A 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 A 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 A 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 A 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 A 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 A 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 A 421 SER ARG VAL ALA VAL HIS GLY HIS SER ARG LEU GLY LYS
SEQRES 21 A 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 A 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 A 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 A 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 A 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 A 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 A 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 A 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 A 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 A 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 A 421 HIS ILE ARG PRO GLY PRO ALA GLY MET THR ALA GLN ASP
SEQRES 32 A 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 A 421 SER ALA LEU PRO ALA
HET BDP A 501 21
HET FMT A 502 5
HETNAM BDP BETA-D-GLUCOPYRANURONIC ACID
HETNAM FMT FORMIC ACID
HETSYN BDP D-GLUCURONIC ACID
FORMUL 2 BDP C6 H10 O7
FORMUL 3 FMT C H2 O2
FORMUL 4 HOH *109(H2 O)
HELIX 1 AA1 ASP A 50 ARG A 57 1 8
HELIX 2 AA2 ARG A 57 VAL A 70 1 14
HELIX 3 AA3 LEU A 94 GLY A 96 5 3
HELIX 4 AA4 ASN A 124 ARG A 129 1 6
HELIX 5 AA5 GLY A 143 VAL A 147 5 5
HELIX 6 AA6 THR A 173 ARG A 177 5 5
HELIX 7 AA7 ASP A 180 TRP A 184 5 5
HELIX 8 AA8 PRO A 185 ARG A 192 1 8
HELIX 9 AA9 CYS A 201 CYS A 205 1 5
HELIX 10 AB1 ASP A 210 ALA A 214 5 5
HELIX 11 AB2 SER A 215 ASP A 221 1 7
HELIX 12 AB3 GLY A 234 GLU A 251 1 18
HELIX 13 AB4 SER A 267 ASP A 280 1 14
HELIX 14 AB5 THR A 306 PHE A 314 1 9
HELIX 15 AB6 ALA A 319 ASP A 326 5 8
HELIX 16 AB7 HIS A 328 LEU A 332 5 5
HELIX 17 AB8 ASP A 335 LEU A 342 1 8
HELIX 18 AB9 ASP A 356 ALA A 359 5 4
HELIX 19 AC1 ASP A 360 PHE A 378 1 19
HELIX 20 AC2 THR A 411 LEU A 426 1 16
SHEET 1 AA1 9 VAL A 83 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 ARG A 106 -1 O ARG A 100 N GLU A 90
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O LEU A 118 N VAL A 103
SHEET 4 AA1 9 ALA A 195 TYR A 200 -1 O THR A 198 N LEU A 119
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PRO A 134 O ALA A 195
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N LEU A 137
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O LEU A 285 N VAL A 263
SHEET 8 AA1 9 LEU A 348 ALA A 353 1 O TYR A 349 N SER A 288
SHEET 9 AA1 9 LEU A 399 ARG A 404 1 O ARG A 400 N VAL A 350
LINK OG SER A 267 C6 BDP A 501 1555 1555 1.37
CISPEP 1 ALA A 344 PRO A 345 0 -0.48
SITE 1 AC1 3 PRO A 407 ALA A 408 HOH A 610
SITE 1 AC2 9 SER A 267 ARG A 268 LYS A 271 SER A 291
SITE 2 AC2 9 GLU A 305 ILE A 310 PHE A 314 TRP A 358
SITE 3 AC2 9 HOH A 602
CRYST1 43.104 44.150 50.179 76.10 66.23 70.85 P 1 1
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 0.023200 -0.008054 -0.009283 0.00000
SCALE2 0.000000 0.023976 -0.003022 0.00000
SCALE3 0.000000 0.000000 0.021948 0.00000
TER 6022 PRO A 431
MASTER 284 0 2 20 9 0 4 6 3199 1 27 33
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