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HEADER HYDROLASE 10-DEC-20 7B7H
TITLE THE GLUCURONOYL ESTERASE OTCE15A R268A VARIANT FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH, AND COVALENTLY LINKED TO, D-GLUCURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE (STRAIN DSM 11246 / JCM 15787 /
SOURCE 3 PB90-1);
SOURCE 4 ORGANISM_TAXID: 452637;
SOURCE 5 STRAIN: DSM 11246 / JCM 15787 / PB90-1;
SOURCE 6 GENE: OTER_0116;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CE15, GLUCURONOYL ESTERASE, GLUCURONATE, GLUCURONIC ACID, HYDROLASE,
KEYWDS 2 BIOMASS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 12-JAN-22 7B7H 0
JRNL AUTH Z.ZONG,S.MAZURKEWICH,J.LARSBRINK,L.LO LEGGIO
JRNL TITL PROBING THE CATALYTIC MECHANISM AND BIOMASS ASSOCIATION OF
JRNL TITL 2 GLUCURONOYL ESTERASE OTCE15A, AN ENZYME FACILITATING
JRNL TITL 3 RECALCITRANT LIGNOCELLULOSE CONVERSION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 32152
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1988
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 43.1500 - 4.3300 0.98 2176 145 0.1764 0.1909
REMARK 3 2 4.3300 - 3.4400 0.97 2177 142 0.1552 0.2017
REMARK 3 3 3.4400 - 3.0000 0.98 2176 139 0.1533 0.1995
REMARK 3 4 3.0000 - 2.7300 0.98 2194 153 0.1586 0.2059
REMARK 3 5 2.7300 - 2.5300 0.98 2168 146 0.1695 0.2389
REMARK 3 6 2.5300 - 2.3800 0.97 2167 137 0.1713 0.2352
REMARK 3 7 2.3800 - 2.2600 0.97 2147 142 0.1628 0.2175
REMARK 3 8 2.2600 - 2.1600 0.97 2184 139 0.1862 0.2461
REMARK 3 9 2.1600 - 2.0800 0.97 2161 146 0.1988 0.2388
REMARK 3 10 2.0800 - 2.0100 0.96 2132 138 0.2193 0.2669
REMARK 3 11 2.0100 - 1.9500 0.97 2159 148 0.2586 0.2594
REMARK 3 12 1.9500 - 1.8900 0.96 2125 135 0.2765 0.2994
REMARK 3 13 1.8900 - 1.8400 0.95 2127 143 0.3231 0.3358
REMARK 3 14 1.8400 - 1.8000 0.92 2071 135 0.3706 0.3838
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) : 0.246
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.594
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.54
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 3068
REMARK 3 ANGLE : 0.897 4146
REMARK 3 CHIRALITY : 0.054 431
REMARK 3 PLANARITY : 0.008 545
REMARK 3 DIHEDRAL : 14.378 1079
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 7B7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.008
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 : 32171
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.796
REMARK 200 RESOLUTION RANGE LOW (A) : 43.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.12020
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 1.25600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.950
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: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS SCREEN CONSISTING OF 0.1 M
REMARK 280 BUFFER SYSTEM 1 (IMIDAZOLE AND MES), 30% PRECIPITANT MIX 2
REMARK 280 (ETHYLENE GLYCOL AND PEG 8000) AND AMINO ACID ADDITIVES (L-
REMARK 280 GLUTAMATE, ALANINE (RACEMIC); GLYCINE; LYSINE HCL (RACEMIC);
REMARK 280 SERINE (RACEMIC)). SOAKING WAS CARRIED OUT IN A SATURATED
REMARK 280 SOLUTION OF BNZ-GLCA IN 10% DMSO AND 90% MOTHER LIQUOR FOR 30
REMARK 280 SECONDS BEFORE BEING FLASH FROZEN., PH 6.5, VAPOR DIFFUSION,
REMARK 280 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: 5470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 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 LEU A 155
REMARK 465 SER A 156
REMARK 465 ALA A 157
REMARK 465 ARG A 158
REMARK 465 TRP A 159
REMARK 465 ILE A 160
REMARK 465 PRO A 161
REMARK 465 ALA A 162
REMARK 465 GLU A 163
REMARK 465 ALA A 164
REMARK 465 PRO A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 ALA A 168
REMARK 465 ASN A 169
REMARK 465 HIS A 170
REMARK 465 ARG A 171
REMARK 465 ALA A 172
REMARK 465 THR A 173
REMARK 465 GLU A 174
REMARK 465 ALA A 175
REMARK 465 GLY A 385
REMARK 465 GLU A 386
REMARK 465 ASP A 387
REMARK 465 VAL A 388
REMARK 465 SER A 428
REMARK 465 ALA A 429
REMARK 465 LEU A 430
REMARK 465 PRO A 431
REMARK 465 ALA A 432
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 OG SER A 267 C6 GCU A 501 1.37
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 ARG A 57 -51.56 -124.11
REMARK 500 VAL A 70 -71.67 -123.34
REMARK 500 ASP A 150 102.71 -32.46
REMARK 500 SER A 267 -124.90 58.79
REMARK 500 ILE A 302 50.84 39.95
REMARK 500 ASP A 360 73.95 57.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GCU A 501
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 513 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 250 O
REMARK 620 2 ASP A 253 O 92.3
REMARK 620 3 VAL A 256 O 109.5 87.9
REMARK 620 4 EDO A 524 O1 98.6 168.4 84.6
REMARK 620 5 GLY A 530 OXT 133.0 82.7 117.0 92.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 514 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 97.1
REMARK 620 3 HOH A 630 O 90.4 150.7
REMARK 620 4 HOH A 679 O 98.5 92.3 114.7
REMARK 620 5 HOH A 691 O 156.3 84.3 77.9 105.2
REMARK 620 N 1 2 3 4
DBREF 7B7H A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 7B7H MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 7B7H GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 7B7H ALA A 268 UNP B1ZMF4 ARG 268 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 ALA 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 HIS 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 GCU A 501 12
HET DMS A 502 4
HET DMS A 503 4
HET DMS A 504 4
HET DMS A 505 4
HET DMS A 506 4
HET DMS A 507 4
HET DMS A 508 4
HET DMS A 509 4
HET DMS A 510 4
HET DMS A 511 4
HET DMS A 512 4
HET NA A 513 1
HET NA A 514 1
HET EDO A 515 4
HET EDO A 516 4
HET EDO A 517 4
HET EDO A 518 4
HET EDO A 519 4
HET EDO A 520 4
HET EDO A 521 4
HET EDO A 522 4
HET EDO A 523 4
HET EDO A 524 4
HET EDO A 525 4
HET EDO A 526 4
HET GLY A 527 5
HET GLY A 528 5
HET GLY A 529 5
HET GLY A 530 5
HETNAM GCU ALPHA-D-GLUCOPYRANURONIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GLY GLYCINE
HETSYN GCU ALPHA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC
HETSYN 2 GCU ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 GCU C6 H10 O7
FORMUL 3 DMS 11(C2 H6 O S)
FORMUL 14 NA 2(NA 1+)
FORMUL 16 EDO 12(C2 H6 O2)
FORMUL 28 GLY 4(C2 H5 N O2)
FORMUL 32 HOH *111(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 ASP A 180 TRP A 184 5 5
HELIX 7 AA7 PRO A 185 ARG A 192 1 8
HELIX 8 AA8 GLY A 202 LEU A 204 5 3
HELIX 9 AA9 ALA A 214 ALA A 224 1 11
HELIX 10 AB1 GLY A 234 ASP A 253 1 20
HELIX 11 AB2 SER A 267 ASP A 280 1 14
HELIX 12 AB3 LEU A 298 ILE A 302 5 5
HELIX 13 AB4 THR A 306 PHE A 314 1 9
HELIX 14 AB5 ALA A 319 ASP A 326 5 8
HELIX 15 AB6 HIS A 328 LEU A 332 5 5
HELIX 16 AB7 ASP A 335 LEU A 342 1 8
HELIX 17 AB8 ASP A 356 ALA A 359 5 4
HELIX 18 AB9 ASP A 360 PHE A 378 1 19
HELIX 19 AC1 THR A 411 LYS A 427 1 17
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 106 N VAL A 83
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 VAL A 196 N TYR A 121
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 VAL A 135
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O ASN A 289 N GLY A 265
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 LEU A 348
LINK O LEU A 250 NA NA A 513 1555 1555 2.47
LINK O ASP A 253 NA NA A 513 1555 1555 2.36
LINK O VAL A 256 NA NA A 513 1555 1555 2.40
LINK O HIS A 303 NA NA A 514 1555 1555 2.26
LINK O GLU A 305 NA NA A 514 1555 1555 2.30
LINK NA NA A 513 O1 EDO A 524 1555 1555 2.36
LINK NA NA A 513 OXT GLY A 530 1555 1555 2.27
LINK NA NA A 514 O HOH A 630 1555 1555 2.43
LINK NA NA A 514 O HOH A 679 1555 1555 2.32
LINK NA NA A 514 O HOH A 691 1555 1555 2.33
CISPEP 1 ALA A 344 PRO A 345 0 3.93
CRYST1 47.333 47.298 51.112 61.95 67.92 88.27 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 0.021127 -0.000637 -0.009503 0.00000
SCALE2 0.000000 0.021152 -0.012066 0.00000
SCALE3 0.000000 0.000000 0.024307 0.00000
TER 2887 LYS A 427
MASTER 321 0 30 19 9 0 0 6 3105 1 117 33
END |