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HEADER HYDROLASE 01-OCT-19 6SYU
TITLE THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH XYLOBIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE;
SOURCE 3 ORGANISM_TAXID: 107709;
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 6SYU 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH XYLOBIOSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.33 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) : 1.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.9
REMARK 3 NUMBER OF REFLECTIONS : 57992
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.145
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.480
REMARK 3 FREE R VALUE TEST SET COUNT : 4338
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 41.5800 - 4.1400 0.99 2299 189 0.1279 0.1477
REMARK 3 2 4.1400 - 3.2900 0.98 2296 180 0.1044 0.1254
REMARK 3 3 3.2900 - 2.8700 0.98 2281 189 0.1125 0.1281
REMARK 3 4 2.8700 - 2.6100 0.97 2259 186 0.1149 0.1377
REMARK 3 5 2.6100 - 2.4200 0.98 2260 176 0.1127 0.1553
REMARK 3 6 2.4200 - 2.2800 0.97 2266 190 0.1105 0.1346
REMARK 3 7 2.2800 - 2.1700 0.97 2250 183 0.1116 0.1232
REMARK 3 8 2.1700 - 2.0700 0.97 2262 180 0.1109 0.1395
REMARK 3 9 2.0700 - 1.9900 0.97 2252 183 0.1120 0.1372
REMARK 3 10 1.9900 - 1.9200 0.97 2239 184 0.1155 0.1569
REMARK 3 11 1.9200 - 1.8600 0.96 2273 187 0.1234 0.1495
REMARK 3 12 1.8600 - 1.8100 0.96 2220 177 0.1254 0.1489
REMARK 3 13 1.8100 - 1.7600 0.96 2236 173 0.1327 0.1458
REMARK 3 14 1.7600 - 1.7200 0.96 2267 176 0.1286 0.1542
REMARK 3 15 1.7200 - 1.6800 0.96 2197 191 0.1261 0.1555
REMARK 3 16 1.6800 - 1.6400 0.96 2215 175 0.1275 0.1599
REMARK 3 17 1.6400 - 1.6100 0.95 2240 183 0.1280 0.1583
REMARK 3 18 1.6100 - 1.5800 0.95 2220 167 0.1301 0.1657
REMARK 3 19 1.5800 - 1.5500 0.87 2013 165 0.1376 0.1726
REMARK 3 20 1.5500 - 1.5300 0.73 1696 137 0.1345 0.1668
REMARK 3 21 1.5300 - 1.5000 0.65 1500 133 0.1375 0.1543
REMARK 3 22 1.5000 - 1.4800 0.59 1368 104 0.1396 0.1642
REMARK 3 23 1.4800 - 1.4600 0.54 1246 102 0.1459 0.1766
REMARK 3 24 1.4600 - 1.4400 0.47 1092 88 0.1446 0.1837
REMARK 3 25 1.4400 - 1.4200 0.43 996 80 0.1514 0.1850
REMARK 3 26 1.4200 - 1.4000 0.38 902 73 0.1487 0.1856
REMARK 3 27 1.4000 - 1.3800 0.34 780 63 0.1546 0.1993
REMARK 3 28 1.3800 - 1.3600 0.30 698 56 0.1600 0.1689
REMARK 3 29 1.3600 - 1.3500 0.25 581 48 0.1722 0.2483
REMARK 3 30 1.3500 - 1.3300 0.11 250 20 0.1823 0.2343
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) : 0.078
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.94
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 : 0.008 3419
REMARK 3 ANGLE : 1.021 4669
REMARK 3 CHIRALITY : 0.076 489
REMARK 3 PLANARITY : 0.008 626
REMARK 3 DIHEDRAL : 19.237 1260
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 6SYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104585.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.91837
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 : 57996
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 41.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04829
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 22.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.16640
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
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 (%): 33.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION C12: 0.09 M NPS
REMARK 280 (0.3M SODIUM NITRATE, 0.3 SODIUM PHOSPHATE DIBASIC, 0.3M
REMARK 280 AMMONIUM SULFATE), 0.1 M BUFFER SYSTEM 3 PH 8.5 (TRIS; BICINE),
REMARK 280 50 % V/V PRECIPITANT MIX 4 (25% V/V MPD; 25% PEG 1000; 25% W/V
REMARK 280 PEG 3350), VAPOR 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: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 320 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 320 NE - CZ - NH2 ANGL. DEV. = -4.2 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 ARG A 57 -54.16 -123.25
REMARK 500 VAL A 70 -71.86 -122.32
REMARK 500 ASP A 150 107.66 -25.69
REMARK 500 ASP A 226 -179.25 72.41
REMARK 500 SER A 267 -127.20 60.35
REMARK 500 HIS A 328 41.33 -146.84
REMARK 500 ASP A 360 70.70 61.46
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 92.4
REMARK 620 3 HOH A 980 O 97.6 93.6
REMARK 620 4 HOH A 649 O 85.8 85.6 176.5
REMARK 620 5 HOH A1047 O 166.2 88.7 96.1 80.6
REMARK 620 6 HOH A 748 O 89.1 158.4 107.5 73.0 84.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYP A
REMARK 800 501 through XYP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYP A
REMARK 800 503 through XYP A 504
DBREF 6SYU A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6SYU MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6SYU GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYU SER A 32 UNP B1ZMF4 EXPRESSION TAG
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 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 XYP A 501 19
HET XYP A 502 18
HET XYP A 503 18
HET XYP A 504 19
HET MG A 505 1
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 PG4 A 511 31
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 XYP 4(C5 H10 O5)
FORMUL 4 MG MG 2+
FORMUL 5 EDO 5(C2 H6 O2)
FORMUL 10 PG4 C8 H18 O5
FORMUL 11 HOH *626(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 GLU A 174 ARG A 177 5 4
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 GLY A 202 LEU A 204 5 3
HELIX 10 AB1 ASP A 210 TRP A 219 5 10
HELIX 11 AB2 GLY A 234 GLU A 251 1 18
HELIX 12 AB3 SER A 267 ASP A 280 1 14
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 LEU A 426 1 16
SHEET 1 AA1 9 MET A 82 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 PHE A 107 -1 O THR A 104 N LYS A 85
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 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 VAL A 350
SHEET 1 AA2 2 GLY A 167 ALA A 168 0
SHEET 2 AA2 2 ARG A 171 ALA A 172 -1 O ARG A 171 N ALA A 168
LINK O HIS A 303 MG MG A 505 1555 1555 2.35
LINK O GLU A 305 MG MG A 505 1555 1555 2.29
LINK O4A XYP A 501 C4B XYP A 502 1555 1555 1.38
LINK C1B XYP A 503 O4B XYP A 504 1555 1555 1.38
LINK MG MG A 505 O HOH A 980 1555 1555 2.42
LINK MG MG A 505 O HOH A 649 1555 1555 2.56
LINK MG MG A 505 O HOH A1047 1555 1555 2.39
LINK MG MG A 505 O HOH A 748 1555 1555 2.27
CISPEP 1 ALA A 344 PRO A 345 0 5.49
SITE 1 AC1 6 HIS A 303 GLU A 305 HOH A 649 HOH A 748
SITE 2 AC1 6 HOH A 980 HOH A1047
SITE 1 AC2 6 ALA A 125 ARG A 129 PRO A 209 HOH A 603
SITE 2 AC2 6 HOH A 607 HOH A 708
SITE 1 AC3 4 PRO A 394 GLY A 396 HOH A 672 HOH A 911
SITE 1 AC4 4 ARG A 323 ARG A 324 ASP A 326 HIS A 328
SITE 1 AC5 5 ARG A 68 ASP A 231 HOH A 638 HOH A 640
SITE 2 AC5 5 HOH A 895
SITE 1 AC6 7 SER A 259 ARG A 282 LYS A 427 HOH A 604
SITE 2 AC6 7 HOH A 866 HOH A 891 HOH A 926
SITE 1 AC7 9 HIS A 91 GLY A 96 ASN A 124 ALA A 125
SITE 2 AC7 9 HOH A 619 HOH A 732 HOH A1037 HOH A1039
SITE 3 AC7 9 HOH A1099
SITE 1 AC8 13 ARG A 51 SER A 267 ARG A 268 LYS A 271
SITE 2 AC8 13 GLU A 305 PHE A 314 TRP A 317 TRP A 358
SITE 3 AC8 13 HOH A 739 HOH A 766 HOH A 844 HOH A 969
SITE 4 AC8 13 HOH A 981
SITE 1 AC9 16 ASN A 213 ALA A 217 SER A 218 ALA A 222
SITE 2 AC9 16 ALA A 223 ALA A 224 GLY A 225 HOH A 601
SITE 3 AC9 16 HOH A 644 HOH A 735 HOH A 738 HOH A 764
SITE 4 AC9 16 HOH A 767 HOH A 899 HOH A 946 HOH A1015
CRYST1 43.686 44.340 50.979 77.24 67.27 70.58 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 0.022891 -0.008071 -0.008783 0.00000
SCALE2 0.000000 0.023914 -0.002556 0.00000
SCALE3 0.000000 0.000000 0.021389 0.00000
TER 6333 ALA A 432
MASTER 337 0 11 19 11 0 21 6 3804 1 163 33
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