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HEADER HYDROLASE 14-AUG-23 8Q6S
TITLE A CARBOHYDRATE ESTERASE FAMILY 15 (CE15) GLUCURONOYL ESTERASE FROM
TITLE 2 PHOCAEICOLA VULGATUS ATCC 8482
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOCAEICOLA VULGATUS ATCC 8482;
SOURCE 3 ORGANISM_TAXID: 435590;
SOURCE 4 GENE: BVU_0175;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS ESTERASE, CE15, GLUCURONOYL ESTERASE, BACTEROIDOTA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,A.SEVESO,S.BANERJEE,L.LO LEGGIO,J.LARSBRINK
REVDAT 1 13-DEC-23 8Q6S 0
JRNL AUTH A.SEVESO,S.MAZURKEWICH,S.BANERJEE,L.LO LEGGIO,J.LARSBRINK
JRNL TITL POLYSACCHARIDE UTILIZATION LOCI FROM BACTEROIDOTA ENCODE
JRNL TITL 2 CE15 ENZYMES WITH POSSIBLE ROLE IN CLEAVING PECTIN-LIGNIN
JRNL TITL 3 BONDS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 50735
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3551
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 48.6400 - 5.8100 1.00 2106 159 0.1495 0.1913
REMARK 3 2 5.8100 - 4.6100 1.00 2049 154 0.1362 0.1971
REMARK 3 3 4.6100 - 4.0300 1.00 2018 151 0.1369 0.2152
REMARK 3 4 4.0300 - 3.6600 1.00 2024 152 0.1576 0.2234
REMARK 3 5 3.6600 - 3.4000 1.00 2013 151 0.1787 0.2207
REMARK 3 6 3.4000 - 3.2000 1.00 2007 151 0.1913 0.2573
REMARK 3 7 3.2000 - 3.0400 1.00 2010 152 0.2055 0.2767
REMARK 3 8 3.0400 - 2.9000 0.99 1989 149 0.2167 0.2736
REMARK 3 9 2.9000 - 2.7900 0.98 1958 148 0.2104 0.2803
REMARK 3 10 2.7900 - 2.7000 0.97 1934 146 0.2137 0.3197
REMARK 3 11 2.7000 - 2.6100 0.96 1937 146 0.2176 0.3155
REMARK 3 12 2.6100 - 2.5400 0.95 1915 143 0.2090 0.2873
REMARK 3 13 2.5400 - 2.4700 0.95 1882 142 0.2228 0.3012
REMARK 3 14 2.4700 - 2.4100 0.94 1886 143 0.2426 0.3278
REMARK 3 15 2.4100 - 2.3600 0.93 1844 138 0.2427 0.3402
REMARK 3 16 2.3600 - 2.3100 0.92 1851 139 0.2531 0.3225
REMARK 3 17 2.3100 - 2.2600 0.92 1822 138 0.2678 0.3133
REMARK 3 18 2.2600 - 2.2200 0.91 1832 136 0.2776 0.3252
REMARK 3 19 2.2200 - 2.1800 0.90 1797 135 0.2935 0.3580
REMARK 3 20 2.1800 - 2.1400 0.89 1780 134 0.3155 0.3492
REMARK 3 21 2.1400 - 2.1100 0.90 1796 135 0.3302 0.3318
REMARK 3 22 2.1100 - 2.0700 0.88 1765 133 0.3521 0.4276
REMARK 3 23 2.0700 - 2.0400 0.87 1732 129 0.3761 0.4102
REMARK 3 24 2.0400 - 2.0100 0.85 1704 130 0.4150 0.4490
REMARK 3 25 2.0100 - 1.9900 0.78 1533 117 0.4483 0.4766
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) : 0.351
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.985
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.29
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 : 0.010 6617
REMARK 3 ANGLE : 1.121 8978
REMARK 3 CHIRALITY : 0.063 899
REMARK 3 PLANARITY : 0.009 1181
REMARK 3 DIHEDRAL : 15.903 2457
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 8Q6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292131356.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-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 : 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) : 0.976254
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 : 50852
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 48.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.640
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 20 MM NACL, AND 20
REMARK 280 -24% (W/V) PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 29.34850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 GLU A 14
REMARK 465 ASN A 15
REMARK 465 LEU A 16
REMARK 465 TYR A 17
REMARK 465 PHE A 18
REMARK 465 GLN A 19
REMARK 465 GLY A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 SER A 24
REMARK 465 PRO A 25
REMARK 465 LYS A 427
REMARK 465 MET B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 GLU B 14
REMARK 465 ASN B 15
REMARK 465 LEU B 16
REMARK 465 TYR B 17
REMARK 465 PHE B 18
REMARK 465 GLN B 19
REMARK 465 GLY B 20
REMARK 465 HIS B 21
REMARK 465 SER B 22
REMARK 465 LYS B 23
REMARK 465 SER B 24
REMARK 465 PRO B 25
REMARK 465 ARG B 26
REMARK 465 GLU B 162
REMARK 465 ILE B 163
REMARK 465 THR B 164
REMARK 465 ASP B 165
REMARK 465 GLU B 166
REMARK 465 LYS B 167
REMARK 465 MET B 168
REMARK 465 LYS B 169
REMARK 465 LYS B 170
REMARK 465 ASN B 426
REMARK 465 LYS B 427
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 LYS A 27 155.18 -46.64
REMARK 500 ASP A 28 -78.06 -71.72
REMARK 500 TYR A 29 -46.30 93.77
REMARK 500 LYS A 66 -51.45 -123.28
REMARK 500 MET A 79 -41.75 -138.72
REMARK 500 LEU A 158 37.53 -97.09
REMARK 500 SER A 172 -143.17 -116.45
REMARK 500 SER A 264 -127.74 64.27
REMARK 500 CYS A 291 15.96 57.63
REMARK 500 ASP A 357 78.40 55.35
REMARK 500 MET A 393 17.30 -148.53
REMARK 500 HIS A 406 106.73 -53.41
REMARK 500 LYS B 66 -57.27 -127.07
REMARK 500 MET B 79 -61.24 -125.84
REMARK 500 ARG B 96 130.23 -176.03
REMARK 500 SER B 172 79.82 -107.96
REMARK 500 LYS B 257 59.43 -140.48
REMARK 500 SER B 264 -116.77 58.41
REMARK 500 ARG B 325 42.34 -142.11
REMARK 500 ASP B 357 78.22 63.32
REMARK 500 MET B 385 121.40 -36.46
REMARK 500 MET B 393 23.82 -148.18
REMARK 500 ALA B 407 167.70 174.68
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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 300 O
REMARK 620 2 GLU A 302 O 86.9
REMARK 620 3 HOH A 686 O 87.6 146.3
REMARK 620 4 HOH A 712 O 89.0 93.0 120.0
REMARK 620 5 HOH A 730 O 169.1 87.3 92.2 100.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 300 O
REMARK 620 2 GLU B 302 O 88.4
REMARK 620 3 HOH B 666 O 95.1 148.0
REMARK 620 4 HOH B 712 O 164.0 80.3 88.7
REMARK 620 5 HOH B 714 O 100.3 88.9 121.5 90.9
REMARK 620 N 1 2 3 4
DBREF 8Q6S A 23 427 UNP A6KWT9 A6KWT9_PHOV8 23 427
DBREF 8Q6S B 23 427 UNP A6KWT9 A6KWT9_PHOV8 23 427
SEQADV 8Q6S MET A 2 UNP A6KWT9 INITIATING METHIONINE
SEQADV 8Q6S GLY A 3 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER A 4 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER A 5 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 6 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 7 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 8 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 9 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 10 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 11 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER A 12 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER A 13 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLU A 14 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S ASN A 15 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S LEU A 16 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S TYR A 17 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S PHE A 18 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLN A 19 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLY A 20 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS A 21 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER A 22 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S MET B 2 UNP A6KWT9 INITIATING METHIONINE
SEQADV 8Q6S GLY B 3 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER B 4 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER B 5 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 6 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 7 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 8 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 9 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 10 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 11 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER B 12 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER B 13 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLU B 14 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S ASN B 15 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S LEU B 16 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S TYR B 17 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S PHE B 18 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLN B 19 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S GLY B 20 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S HIS B 21 UNP A6KWT9 EXPRESSION TAG
SEQADV 8Q6S SER B 22 UNP A6KWT9 EXPRESSION TAG
SEQRES 1 A 426 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 426 ASN LEU TYR PHE GLN GLY HIS SER LYS SER PRO ARG LYS
SEQRES 3 A 426 ASP TYR ALA LYS LEU ALA ASN TYR ASP GLU SER LYS VAL
SEQRES 4 A 426 PRO GLN TYR THR LEU PRO SER VAL LEU MET CYS HIS ASP
SEQRES 5 A 426 GLY GLU MET VAL GLN THR LYS GLU GLN TRP GLU GLN LYS
SEQRES 6 A 426 ARG ARG PRO GLU ILE LEU ASN LEU PHE THR THR TYR MET
SEQRES 7 A 426 PHE GLY LYS ALA PRO VAL LEU LYS HIS LYS LEU PRO CYS
SEQRES 8 A 426 THR VAL SER ARG ILE ASN GLU LYS ALA LEU ASN GLY ARG
SEQRES 9 A 426 ALA THR ARG LYS GLU ILE THR ILE GLN LEU THR ASP ASP
SEQRES 10 A 426 PRO GLN GLY PRO HIS ILE ASP LEU GLN LEU TYR LEU PRO
SEQRES 11 A 426 ASN HIS VAL SER GLY LYS ILE PRO VAL PHE LEU GLY ILE
SEQRES 12 A 426 SER PHE MET PRO ASN TYR THR ILE TYR ASP ASP PRO ASP
SEQRES 13 A 426 LEU SER VAL PRO GLU ILE THR ASP GLU LYS MET LYS LYS
SEQRES 14 A 426 ARG SER PHE ARG GLY SER MET ASP LYS SER TRP GLN LEU
SEQRES 15 A 426 ASP LYS ILE LEU GLU HIS GLY TYR GLY LEU ALA THR PHE
SEQRES 16 A 426 CYS TYR ASN ASP VAL ASP PRO ASP PHE ASP ASP ASP PHE
SEQRES 17 A 426 GLN ASN GLY VAL HIS PRO TYR TYR TYR GLU LYS GLY GLN
SEQRES 18 A 426 ASN PHE PRO ASP PRO ASP GLN TRP GLY SER ILE ALA ALA
SEQRES 19 A 426 TRP ALA TRP GLY MET SER ARG ALA MET ASP TYR LEU GLU
SEQRES 20 A 426 THR ASP LYS LYS VAL ASP ALA LYS LYS VAL ALA VAL ILE
SEQRES 21 A 426 GLY HIS SER ARG LEU GLY LYS THR ALA VAL TRP ALA GLY
SEQRES 22 A 426 ALA SER ASP PRO ARG PHE ALA LEU VAL ILE SER GLY ASN
SEQRES 23 A 426 SER GLY CYS CYS GLY VAL ALA ILE SER ARG ARG CYS PHE
SEQRES 24 A 426 GLY GLU THR VAL GLU ALA MET ASN VAL ARG PHE PRO HIS
SEQRES 25 A 426 TRP PHE CYS GLY ASN TYR LYS GLN PHE ASN ASP ARG GLU
SEQRES 26 A 426 LYS TYR LEU PRO PHE ASP GLN HIS GLU LEU VAL ALA LEU
SEQRES 27 A 426 ILE ALA PRO ARG PRO ILE TYR ILE ALA SER ALA GLU GLU
SEQRES 28 A 426 ASP ASN TRP SER ASP GLN LYS GLY GLU PHE LEU GLY GLY
SEQRES 29 A 426 LYS GLY ALA GLU PRO VAL TYR ALA LEU TYR GLY LEU GLY
SEQRES 30 A 426 GLY ILE GLY CYS GLU GLU MET PRO PRO VAL ASP THR PRO
SEQRES 31 A 426 TYR MET ASN GLY PRO ILE ALA TYR HIS ASN ARG LYS GLY
SEQRES 32 A 426 PRO HIS ALA VAL LEU PRO TYR ASP TRP GLU GLN PHE LEU
SEQRES 33 A 426 ARG PHE ALA ASP LYS TYR PHE LYS ASN LYS
SEQRES 1 B 426 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 426 ASN LEU TYR PHE GLN GLY HIS SER LYS SER PRO ARG LYS
SEQRES 3 B 426 ASP TYR ALA LYS LEU ALA ASN TYR ASP GLU SER LYS VAL
SEQRES 4 B 426 PRO GLN TYR THR LEU PRO SER VAL LEU MET CYS HIS ASP
SEQRES 5 B 426 GLY GLU MET VAL GLN THR LYS GLU GLN TRP GLU GLN LYS
SEQRES 6 B 426 ARG ARG PRO GLU ILE LEU ASN LEU PHE THR THR TYR MET
SEQRES 7 B 426 PHE GLY LYS ALA PRO VAL LEU LYS HIS LYS LEU PRO CYS
SEQRES 8 B 426 THR VAL SER ARG ILE ASN GLU LYS ALA LEU ASN GLY ARG
SEQRES 9 B 426 ALA THR ARG LYS GLU ILE THR ILE GLN LEU THR ASP ASP
SEQRES 10 B 426 PRO GLN GLY PRO HIS ILE ASP LEU GLN LEU TYR LEU PRO
SEQRES 11 B 426 ASN HIS VAL SER GLY LYS ILE PRO VAL PHE LEU GLY ILE
SEQRES 12 B 426 SER PHE MET PRO ASN TYR THR ILE TYR ASP ASP PRO ASP
SEQRES 13 B 426 LEU SER VAL PRO GLU ILE THR ASP GLU LYS MET LYS LYS
SEQRES 14 B 426 ARG SER PHE ARG GLY SER MET ASP LYS SER TRP GLN LEU
SEQRES 15 B 426 ASP LYS ILE LEU GLU HIS GLY TYR GLY LEU ALA THR PHE
SEQRES 16 B 426 CYS TYR ASN ASP VAL ASP PRO ASP PHE ASP ASP ASP PHE
SEQRES 17 B 426 GLN ASN GLY VAL HIS PRO TYR TYR TYR GLU LYS GLY GLN
SEQRES 18 B 426 ASN PHE PRO ASP PRO ASP GLN TRP GLY SER ILE ALA ALA
SEQRES 19 B 426 TRP ALA TRP GLY MET SER ARG ALA MET ASP TYR LEU GLU
SEQRES 20 B 426 THR ASP LYS LYS VAL ASP ALA LYS LYS VAL ALA VAL ILE
SEQRES 21 B 426 GLY HIS SER ARG LEU GLY LYS THR ALA VAL TRP ALA GLY
SEQRES 22 B 426 ALA SER ASP PRO ARG PHE ALA LEU VAL ILE SER GLY ASN
SEQRES 23 B 426 SER GLY CYS CYS GLY VAL ALA ILE SER ARG ARG CYS PHE
SEQRES 24 B 426 GLY GLU THR VAL GLU ALA MET ASN VAL ARG PHE PRO HIS
SEQRES 25 B 426 TRP PHE CYS GLY ASN TYR LYS GLN PHE ASN ASP ARG GLU
SEQRES 26 B 426 LYS TYR LEU PRO PHE ASP GLN HIS GLU LEU VAL ALA LEU
SEQRES 27 B 426 ILE ALA PRO ARG PRO ILE TYR ILE ALA SER ALA GLU GLU
SEQRES 28 B 426 ASP ASN TRP SER ASP GLN LYS GLY GLU PHE LEU GLY GLY
SEQRES 29 B 426 LYS GLY ALA GLU PRO VAL TYR ALA LEU TYR GLY LEU GLY
SEQRES 30 B 426 GLY ILE GLY CYS GLU GLU MET PRO PRO VAL ASP THR PRO
SEQRES 31 B 426 TYR MET ASN GLY PRO ILE ALA TYR HIS ASN ARG LYS GLY
SEQRES 32 B 426 PRO HIS ALA VAL LEU PRO TYR ASP TRP GLU GLN PHE LEU
SEQRES 33 B 426 ARG PHE ALA ASP LYS TYR PHE LYS ASN LYS
HET PEG A 501 7
HET NA A 502 1
HET NA B 501 1
HET MES B 502 12
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 PEG C4 H10 O3
FORMUL 4 NA 2(NA 1+)
FORMUL 6 MES C6 H13 N O4 S
FORMUL 7 HOH *281(H2 O)
HELIX 1 AA1 ASP A 36 VAL A 40 5 5
HELIX 2 AA2 THR A 59 LYS A 66 1 8
HELIX 3 AA3 LYS A 66 MET A 79 1 14
HELIX 4 AA4 PRO A 148 ILE A 152 5 5
HELIX 5 AA5 MET A 177 GLN A 182 1 6
HELIX 6 AA6 GLN A 182 HIS A 189 1 8
HELIX 7 AA7 ASN A 199 VAL A 201 5 3
HELIX 8 AA8 VAL A 213 TYR A 218 5 6
HELIX 9 AA9 GLY A 231 GLU A 248 1 18
HELIX 10 AB1 SER A 264 ASP A 277 1 14
HELIX 11 AB2 ILE A 295 CYS A 299 5 5
HELIX 12 AB3 THR A 303 PHE A 311 1 9
HELIX 13 AB4 CYS A 316 ASN A 323 5 8
HELIX 14 AB5 ARG A 325 LEU A 329 5 5
HELIX 15 AB6 ASP A 332 LEU A 339 1 8
HELIX 16 AB7 ASP A 353 SER A 356 5 4
HELIX 17 AB8 ASP A 357 ALA A 368 1 12
HELIX 18 AB9 ALA A 368 ALA A 373 1 6
HELIX 19 AC1 LEU A 374 GLY A 376 5 3
HELIX 20 AC2 LEU A 409 LYS A 425 1 17
HELIX 21 AC3 ASP B 36 VAL B 40 5 5
HELIX 22 AC4 THR B 59 LYS B 66 1 8
HELIX 23 AC5 LYS B 66 MET B 79 1 14
HELIX 24 AC6 PRO B 148 ILE B 152 5 5
HELIX 25 AC7 MET B 177 GLN B 182 1 6
HELIX 26 AC8 GLN B 182 HIS B 189 1 8
HELIX 27 AC9 ASN B 199 VAL B 201 5 3
HELIX 28 AD1 VAL B 213 TYR B 218 5 6
HELIX 29 AD2 GLY B 231 GLU B 248 1 18
HELIX 30 AD3 SER B 264 ASP B 277 1 14
HELIX 31 AD4 ILE B 295 CYS B 299 5 5
HELIX 32 AD5 THR B 303 PHE B 311 1 9
HELIX 33 AD6 CYS B 316 ASN B 323 5 8
HELIX 34 AD7 ARG B 325 LEU B 329 5 5
HELIX 35 AD8 ASP B 332 LEU B 339 1 8
HELIX 36 AD9 ASP B 353 SER B 356 5 4
HELIX 37 AE1 ASP B 357 GLY B 367 1 11
HELIX 38 AE2 ALA B 368 LEU B 374 1 7
HELIX 39 AE3 LEU B 409 LYS B 425 1 17
SHEET 1 AA1 9 CYS A 92 ALA A 101 0
SHEET 2 AA1 9 ALA A 106 GLN A 114 -1 O ALA A 106 N ALA A 101
SHEET 3 AA1 9 HIS A 123 PRO A 131 -1 O LEU A 128 N LYS A 109
SHEET 4 AA1 9 GLY A 192 CYS A 197 -1 O LEU A 193 N TYR A 129
SHEET 5 AA1 9 ILE A 138 SER A 145 1 N GLY A 143 O ALA A 194
SHEET 6 AA1 9 VAL A 253 HIS A 263 1 O ALA A 259 N LEU A 142
SHEET 7 AA1 9 LEU A 282 GLY A 286 1 O ILE A 284 N VAL A 260
SHEET 8 AA1 9 ILE A 345 ALA A 350 1 O TYR A 346 N SER A 285
SHEET 9 AA1 9 ILE A 397 ARG A 402 1 O HIS A 400 N SER A 349
SHEET 1 AA2 9 CYS B 92 ALA B 101 0
SHEET 2 AA2 9 ALA B 106 GLN B 114 -1 O THR B 112 N THR B 93
SHEET 3 AA2 9 HIS B 123 PRO B 131 -1 O ILE B 124 N ILE B 113
SHEET 4 AA2 9 GLY B 192 CYS B 197 -1 O LEU B 193 N TYR B 129
SHEET 5 AA2 9 ILE B 138 SER B 145 1 N GLY B 143 O ALA B 194
SHEET 6 AA2 9 VAL B 253 HIS B 263 1 O ASP B 254 N ILE B 138
SHEET 7 AA2 9 LEU B 282 GLY B 286 1 O LEU B 282 N VAL B 260
SHEET 8 AA2 9 ILE B 345 ALA B 350 1 O TYR B 346 N SER B 285
SHEET 9 AA2 9 ILE B 397 ARG B 402 1 O HIS B 400 N SER B 349
LINK O PHE A 300 NA NA A 502 1555 1555 2.43
LINK O GLU A 302 NA NA A 502 1555 1555 2.31
LINK NA NA A 502 O HOH A 686 1555 1555 2.40
LINK NA NA A 502 O HOH A 712 1555 1555 2.48
LINK NA NA A 502 O HOH A 730 1555 1555 2.40
LINK O PHE B 300 NA NA B 501 1555 1555 2.30
LINK O GLU B 302 NA NA B 501 1555 1555 2.26
LINK NA NA B 501 O HOH B 666 1555 1555 2.32
LINK NA NA B 501 O HOH B 712 1555 1555 2.45
LINK NA NA B 501 O HOH B 714 1555 1555 2.38
CISPEP 1 ALA A 341 PRO A 342 0 3.54
CISPEP 2 ALA B 341 PRO B 342 0 1.21
CRYST1 77.382 58.697 89.539 90.00 103.95 90.00 P 1 21 1 4
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 0.012923 0.000000 0.003209 0.00000
SCALE2 0.000000 0.017037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011508 0.00000
TER 3260 ASN A 426
TER 6403 LYS B 425
MASTER 343 0 4 39 18 0 0 6 6663 2 33 66
END |