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HEADER HYDROLASE 03-OCT-20 7D79
TITLE THE STRUCTURE OF DCSB COMPLEX WITH ITS SUBSTRATE ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DLTD DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: D, A, B, C;
COMPND 4 SYNONYM: THIOESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BEAUVERIA BASSIANA (STRAIN ARSEF 2860);
SOURCE 3 ORGANISM_COMMON: WHITE MUSCARDINE DISEASE FUNGUS;
SOURCE 4 ORGANISM_TAXID: 655819;
SOURCE 5 STRAIN: ARSEF 2860;
SOURCE 6 GENE: BBA_03809;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS THIOESTERASE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TANG,J.H.ZHOU,G.Q.WANG
REVDAT 1 27-JAN-21 7D79 0
JRNL AUTH D.W.GAO,C.S.JAMIESON,G.WANG,Y.YAN,J.ZHOU,K.N.HOUK,Y.TANG
JRNL TITL A POLYKETIDE CYCLASE THAT FORMS MEDIUM-RING LACTONES.
JRNL REF J.AM.CHEM.SOC. V. 143 80 2021
JRNL REFN ESSN 1520-5126
JRNL PMID 33351624
JRNL DOI 10.1021/JACS.0C11226
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.973
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 3 NUMBER OF REFLECTIONS : 59724
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) : 0.182
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.988
REMARK 3 FREE R VALUE TEST SET COUNT : 2979
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 5.7990 - 5.7990 0.91 2853 165 0.1537 0.1861
REMARK 3 2 5.7990 - 4.6052 0.93 2915 163 0.1531 0.1939
REMARK 3 3 4.6052 - 4.0238 0.91 2887 136 0.1452 0.1685
REMARK 3 4 4.0238 - 3.6562 0.95 2933 167 0.1571 0.2092
REMARK 3 5 3.6562 - 3.3943 0.96 3044 158 0.1746 0.1855
REMARK 3 6 3.3943 - 3.1942 0.91 2862 160 0.1899 0.2200
REMARK 3 7 3.1942 - 3.0343 0.89 2813 124 0.1946 0.2564
REMARK 3 8 3.0343 - 2.9023 0.93 2940 144 0.2025 0.2631
REMARK 3 9 2.9023 - 2.7906 0.94 2927 151 0.1988 0.2397
REMARK 3 10 2.7906 - 2.6943 0.94 2988 166 0.2037 0.2577
REMARK 3 11 2.6943 - 2.6101 0.95 2932 181 0.1994 0.2436
REMARK 3 12 2.6101 - 2.5355 0.95 2998 156 0.2007 0.2864
REMARK 3 13 2.5355 - 2.4688 0.89 2770 132 0.2040 0.2491
REMARK 3 14 2.4688 - 2.4085 0.86 2752 154 0.2065 0.2700
REMARK 3 15 2.4085 - 2.3538 0.87 2708 127 0.2077 0.2546
REMARK 3 16 2.3538 - 2.3037 0.85 2715 123 0.2079 0.3170
REMARK 3 17 2.3037 - 2.2576 0.80 2474 135 0.2172 0.3009
REMARK 3 18 2.2576 - 2.2150 0.74 2371 116 0.2469 0.3330
REMARK 3 19 2.2150 - 2.1755 0.70 2190 119 0.2265 0.2687
REMARK 3 20 2.1755 - 2.1386 0.64 2000 113 0.2165 0.2533
REMARK 3 21 2.1386 - 2.1100 0.54 1673 89 0.2426 0.3213
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) : 0.265
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.10
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 : 0.002 9261
REMARK 3 ANGLE : 0.489 12509
REMARK 3 CHIRALITY : 0.044 1379
REMARK 3 PLANARITY : 0.004 1634
REMARK 3 DIHEDRAL : 3.013 7272
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 7D79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1300018887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
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 : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64129
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MMT, 25% PEG 1500, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.2K
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, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 47.26300
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PRO D 3
REMARK 465 LEU D 4
REMARK 465 SER D 5
REMARK 465 ALA D 301
REMARK 465 GLY D 302
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 VAL A 202
REMARK 465 ILE A 203
REMARK 465 ASP A 204
REMARK 465 ARG A 205
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PRO B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 VAL B 202
REMARK 465 ILE B 203
REMARK 465 ASP B 204
REMARK 465 ARG B 205
REMARK 465 GLY B 206
REMARK 465 ALA B 301
REMARK 465 GLY B 302
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PRO C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 ALA C 201
REMARK 465 VAL C 202
REMARK 465 ILE C 203
REMARK 465 ASP C 204
REMARK 465 ARG C 205
REMARK 465 GLY C 206
REMARK 465 GLU C 283
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 D 47 -45.08 67.06
REMARK 500 SER D 114 -129.93 59.19
REMARK 500 CYS D 137 55.74 33.82
REMARK 500 PHE D 142 -37.37 -141.49
REMARK 500 ASN D 212 47.03 -82.80
REMARK 500 LYS D 236 -35.50 -131.51
REMARK 500 LEU D 246 42.02 -107.63
REMARK 500 LEU A 47 -49.88 65.48
REMARK 500 SER A 114 -125.09 60.48
REMARK 500 CYS A 137 56.08 39.38
REMARK 500 PHE A 142 -32.18 -140.42
REMARK 500 LYS A 236 -33.56 -134.42
REMARK 500 LEU A 246 55.09 -117.74
REMARK 500 PHE B 40 109.33 -57.27
REMARK 500 LEU B 47 -46.92 67.73
REMARK 500 SER B 114 -124.31 60.03
REMARK 500 CYS B 137 59.24 33.50
REMARK 500 PHE B 142 -39.62 -141.06
REMARK 500 GLN B 226 71.52 -118.76
REMARK 500 LEU B 246 50.86 -107.12
REMARK 500 PHE C 40 108.26 -59.96
REMARK 500 LEU C 47 -35.45 72.82
REMARK 500 SER C 114 -123.96 60.68
REMARK 500 CYS C 137 58.81 38.27
REMARK 500 PHE C 142 -43.23 -143.58
REMARK 500 LEU C 246 55.09 -112.49
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 C 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 158 OD1
REMARK 620 2 SER C 161 OG 134.8
REMARK 620 3 GLU C 167 O 109.3 113.3
REMARK 620 N 1 2
DBREF 7D79 D 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
DBREF 7D79 A 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
DBREF 7D79 B 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
DBREF 7D79 C 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
SEQADV 7D79 MET D -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D79 GLY D -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER D -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER D -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER D -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER D -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY D -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 LEU D -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 VAL D -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 PRO D -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 ARG D -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY D -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER D -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS D 0 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 MET A -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D79 GLY A -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER A -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER A -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER A -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER A -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY A -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 LEU A -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 VAL A -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 PRO A -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 ARG A -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY A -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER A -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS A 0 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 MET B -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D79 GLY B -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER B -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER B -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER B -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER B -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY B -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 LEU B -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 VAL B -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 PRO B -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 ARG B -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY B -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER B -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS B 0 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 MET C -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D79 GLY C -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER C -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER C -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER C -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER C -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY C -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 LEU C -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 VAL C -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 PRO C -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 ARG C -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 GLY C -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 SER C -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D79 HIS C 0 UNP J4WAT9 EXPRESSION TAG
SEQRES 1 D 322 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 322 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER
SEQRES 3 D 322 PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE
SEQRES 4 D 322 ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO
SEQRES 5 D 322 ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU
SEQRES 6 D 322 MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN
SEQRES 7 D 322 GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY
SEQRES 8 D 322 ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU
SEQRES 9 D 322 GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE
SEQRES 10 D 322 SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU
SEQRES 11 D 322 TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA
SEQRES 12 D 322 ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL
SEQRES 13 D 322 CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP
SEQRES 14 D 322 LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN
SEQRES 15 D 322 LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN
SEQRES 16 D 322 SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY
SEQRES 17 D 322 GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA
SEQRES 18 D 322 VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE
SEQRES 19 D 322 ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO
SEQRES 20 D 322 LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU
SEQRES 21 D 322 MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU
SEQRES 22 D 322 GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS
SEQRES 23 D 322 LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL
SEQRES 24 D 322 LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET
SEQRES 25 D 322 THR GLU PHE ILE ARG GLU ASN VAL ALA GLY
SEQRES 1 A 322 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 322 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER
SEQRES 3 A 322 PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE
SEQRES 4 A 322 ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO
SEQRES 5 A 322 ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU
SEQRES 6 A 322 MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN
SEQRES 7 A 322 GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY
SEQRES 8 A 322 ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU
SEQRES 9 A 322 GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE
SEQRES 10 A 322 SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU
SEQRES 11 A 322 TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA
SEQRES 12 A 322 ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL
SEQRES 13 A 322 CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP
SEQRES 14 A 322 LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN
SEQRES 15 A 322 LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN
SEQRES 16 A 322 SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY
SEQRES 17 A 322 GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA
SEQRES 18 A 322 VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE
SEQRES 19 A 322 ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO
SEQRES 20 A 322 LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU
SEQRES 21 A 322 MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU
SEQRES 22 A 322 GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS
SEQRES 23 A 322 LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL
SEQRES 24 A 322 LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET
SEQRES 25 A 322 THR GLU PHE ILE ARG GLU ASN VAL ALA GLY
SEQRES 1 B 322 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 322 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER
SEQRES 3 B 322 PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE
SEQRES 4 B 322 ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO
SEQRES 5 B 322 ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU
SEQRES 6 B 322 MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN
SEQRES 7 B 322 GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY
SEQRES 8 B 322 ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU
SEQRES 9 B 322 GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE
SEQRES 10 B 322 SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU
SEQRES 11 B 322 TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA
SEQRES 12 B 322 ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL
SEQRES 13 B 322 CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP
SEQRES 14 B 322 LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN
SEQRES 15 B 322 LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN
SEQRES 16 B 322 SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY
SEQRES 17 B 322 GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA
SEQRES 18 B 322 VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE
SEQRES 19 B 322 ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO
SEQRES 20 B 322 LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU
SEQRES 21 B 322 MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU
SEQRES 22 B 322 GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS
SEQRES 23 B 322 LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL
SEQRES 24 B 322 LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET
SEQRES 25 B 322 THR GLU PHE ILE ARG GLU ASN VAL ALA GLY
SEQRES 1 C 322 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 322 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU SER SER
SEQRES 3 C 322 PHE GLN VAL VAL GLU CYS LYS THR ILE ASP GLY ILE ILE
SEQRES 4 C 322 ILE ARG GLY ARG PHE TYR ALA VAL ASP GLY LYS GLY PRO
SEQRES 5 C 322 ALA ILE ILE MET THR PRO GLY PHE ASN CYS VAL LYS GLU
SEQRES 6 C 322 MET LEU LEU PRO ASP ILE ALA GLU THR PHE GLN SER GLN
SEQRES 7 C 322 GLY PHE ASN THR TYR ILE TYR ASP PRO ARG SER ILE GLY
SEQRES 8 C 322 ASP SER ASP GLY SER PRO LYS ASN LEU ILE ASP PRO LEU
SEQRES 9 C 322 GLN GLN ALA GLU ASP LEU ALA ASP ILE VAL THR HIS ILE
SEQRES 10 C 322 SER SER LEU PRO SER VAL ASP SER SER LYS ILE THR LEU
SEQRES 11 C 322 TRP GLY MET SER PHE GLY GLY THR VAL SER ALA CYS ALA
SEQRES 12 C 322 ALA ALA VAL ASP ARG ARG VAL LYS ALA LEU VAL MET VAL
SEQRES 13 C 322 CYS PRO ILE LEU SER PHE TYR GLN ALA GLU LYS ARG ASP
SEQRES 14 C 322 LYS ALA PHE LEU GLN LEU ILE ARG ASP ARG GLN SER GLN
SEQRES 15 C 322 LEU ARG GLY ASN GLU PRO PHE MET LEU PRO PRO PHE ASN
SEQRES 16 C 322 SER LYS GLY GLU ASN PRO ILE GLY MET ALA GLY SER GLY
SEQRES 17 C 322 GLY PRO GLY GLY ILE GLU ALA TYR GLY PHE MET GLY ALA
SEQRES 18 C 322 VAL ILE ASP ARG GLY ALA PRO ASN PHE ARG ASN LYS ILE
SEQRES 19 C 322 ALA LEU GLN THR TYR GLN LYS LEU ALA TRP TRP GLN PRO
SEQRES 20 C 322 LYS GLU ILE LEU LYS LEU VAL ASP LYS THR PRO VAL LEU
SEQRES 21 C 322 MET VAL THR PRO GLU LEU ASP THR MET SER PRO PRO GLU
SEQRES 22 C 322 GLU GLN LYS ALA ALA PHE GLU LEU PHE PRO GLN THR LYS
SEQRES 23 C 322 LYS PHE LEU GLU ALA LYS GLY LYS GLY HIS LEU THR VAL
SEQRES 24 C 322 LEU SER GLY GLU GLY SER VAL GLU VAL VAL ASP ALA MET
SEQRES 25 C 322 THR GLU PHE ILE ARG GLU ASN VAL ALA GLY
HET CL D 401 1
HET EDO D 402 4
HET EDO D 403 4
HET EDO D 404 4
HET GY0 D 405 20
HET CL A 401 1
HET CL A 402 1
HET GOL A 403 6
HET EDO A 404 4
HET EDO A 405 4
HET EDO B 401 4
HET GYF B 402 7
HET CL C 401 1
HET GOL C 402 6
HET NA C 403 1
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GY0 METHYL 3-[(E,3R,9R)-3,9-BIS(OXIDANYL)DEC-4-
HETNAM 2 GY0 ENOYL]SULFANYLPROPANOATE
HETNAM GOL GLYCEROL
HETNAM GYF METHYL 3-SULFANYLPROPANOATE
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 CL 4(CL 1-)
FORMUL 6 EDO 6(C2 H6 O2)
FORMUL 9 GY0 C14 H24 O5 S
FORMUL 12 GOL 2(C3 H8 O3)
FORMUL 16 GYF C4 H8 O2 S
FORMUL 19 NA NA 1+
FORMUL 20 HOH *573(H2 O)
HELIX 1 AA1 LEU D 47 GLN D 58 1 12
HELIX 2 AA2 ASP D 82 SER D 99 1 18
HELIX 3 AA3 SER D 114 ASP D 127 1 14
HELIX 4 AA4 GLN D 144 GLU D 146 5 3
HELIX 5 AA5 LYS D 147 ARG D 164 1 18
HELIX 6 AA6 GLY D 189 GLY D 200 1 12
HELIX 7 AA7 GLN D 217 TRP D 225 1 9
HELIX 8 AA8 GLN D 226 LYS D 232 1 7
HELIX 9 AA9 PRO D 251 PHE D 262 1 12
HELIX 10 AB1 GLY D 284 VAL D 300 1 17
HELIX 11 AB2 LEU A 47 GLN A 58 1 12
HELIX 12 AB3 ASP A 82 SER A 99 1 18
HELIX 13 AB4 SER A 114 ASP A 127 1 14
HELIX 14 AB5 GLN A 144 GLU A 146 5 3
HELIX 15 AB6 LYS A 147 ARG A 164 1 18
HELIX 16 AB7 GLY A 189 ALA A 201 1 13
HELIX 17 AB8 GLN A 217 TRP A 225 1 9
HELIX 18 AB9 GLN A 226 LYS A 232 1 7
HELIX 19 AC1 PRO A 251 LEU A 261 1 11
HELIX 20 AC2 GLY A 284 VAL A 300 1 17
HELIX 21 AC3 LEU B 47 GLN B 58 1 12
HELIX 22 AC4 ASP B 82 SER B 99 1 18
HELIX 23 AC5 SER B 114 ASP B 127 1 14
HELIX 24 AC6 GLN B 144 GLU B 146 5 3
HELIX 25 AC7 LYS B 147 ARG B 164 1 18
HELIX 26 AC8 GLY B 189 ALA B 201 1 13
HELIX 27 AC9 GLN B 217 TRP B 225 1 9
HELIX 28 AD1 GLN B 226 LEU B 231 1 6
HELIX 29 AD2 PRO B 251 PHE B 262 1 12
HELIX 30 AD3 GLY B 284 VAL B 300 1 17
HELIX 31 AD4 LEU C 47 GLN C 58 1 12
HELIX 32 AD5 ASP C 82 SER C 99 1 18
HELIX 33 AD6 SER C 114 ALA C 125 1 12
HELIX 34 AD7 GLN C 144 GLU C 146 5 3
HELIX 35 AD8 LYS C 147 ARG C 164 1 18
HELIX 36 AD9 GLY C 189 GLY C 200 1 12
HELIX 37 AE1 GLN C 217 TRP C 225 1 9
HELIX 38 AE2 GLN C 226 LYS C 232 1 7
HELIX 39 AE3 PRO C 251 LEU C 261 1 11
HELIX 40 AE4 SER C 285 VAL C 300 1 16
SHEET 1 AA1 8 GLN D 8 LYS D 13 0
SHEET 2 AA1 8 ILE D 19 TYR D 25 -1 O ILE D 20 N CYS D 12
SHEET 3 AA1 8 ASN D 61 TYR D 65 -1 O THR D 62 N TYR D 25
SHEET 4 AA1 8 GLY D 31 THR D 37 1 N ILE D 34 O ASN D 61
SHEET 5 AA1 8 VAL D 103 MET D 113 1 O TRP D 111 N ILE D 35
SHEET 6 AA1 8 VAL D 130 VAL D 136 1 O VAL D 136 N GLY D 112
SHEET 7 AA1 8 VAL D 239 PRO D 244 1 O LEU D 240 N MET D 135
SHEET 8 AA1 8 LYS D 266 ALA D 271 1 O LEU D 269 N THR D 243
SHEET 1 AA2 2 MET D 170 LEU D 171 0
SHEET 2 AA2 2 ILE D 214 ALA D 215 -1 O ILE D 214 N LEU D 171
SHEET 1 AA3 8 GLN A 8 LYS A 13 0
SHEET 2 AA3 8 ILE A 19 TYR A 25 -1 O ILE A 20 N CYS A 12
SHEET 3 AA3 8 ASN A 61 TYR A 65 -1 O THR A 62 N TYR A 25
SHEET 4 AA3 8 GLY A 31 THR A 37 1 N ILE A 34 O ASN A 61
SHEET 5 AA3 8 VAL A 103 MET A 113 1 O TRP A 111 N ILE A 35
SHEET 6 AA3 8 VAL A 130 VAL A 136 1 O LYS A 131 N ILE A 108
SHEET 7 AA3 8 VAL A 239 PRO A 244 1 O LEU A 240 N LEU A 133
SHEET 8 AA3 8 LYS A 266 ALA A 271 1 O LEU A 269 N THR A 243
SHEET 1 AA4 2 MET A 170 LEU A 171 0
SHEET 2 AA4 2 ILE A 214 ALA A 215 -1 O ILE A 214 N LEU A 171
SHEET 1 AA5 8 GLN B 8 LYS B 13 0
SHEET 2 AA5 8 ILE B 19 TYR B 25 -1 O ILE B 20 N CYS B 12
SHEET 3 AA5 8 ASN B 61 TYR B 65 -1 O THR B 62 N TYR B 25
SHEET 4 AA5 8 GLY B 31 THR B 37 1 N ILE B 34 O ASN B 61
SHEET 5 AA5 8 VAL B 103 MET B 113 1 O TRP B 111 N ILE B 35
SHEET 6 AA5 8 VAL B 130 VAL B 136 1 O VAL B 136 N GLY B 112
SHEET 7 AA5 8 VAL B 239 PRO B 244 1 O LEU B 240 N MET B 135
SHEET 8 AA5 8 LYS B 266 ALA B 271 1 O LEU B 269 N THR B 243
SHEET 1 AA6 2 MET B 170 LEU B 171 0
SHEET 2 AA6 2 ILE B 214 ALA B 215 -1 O ILE B 214 N LEU B 171
SHEET 1 AA7 8 GLN C 8 LYS C 13 0
SHEET 2 AA7 8 ILE C 19 TYR C 25 -1 O ILE C 20 N CYS C 12
SHEET 3 AA7 8 ASN C 61 TYR C 65 -1 O THR C 62 N TYR C 25
SHEET 4 AA7 8 GLY C 31 THR C 37 1 N ILE C 34 O ASN C 61
SHEET 5 AA7 8 VAL C 103 MET C 113 1 O TRP C 111 N ILE C 35
SHEET 6 AA7 8 VAL C 130 VAL C 136 1 O LYS C 131 N ILE C 108
SHEET 7 AA7 8 VAL C 239 PRO C 244 1 O LEU C 240 N LEU C 133
SHEET 8 AA7 8 LYS C 266 ALA C 271 1 O LEU C 269 N MET C 241
SHEET 1 AA8 2 MET C 170 LEU C 171 0
SHEET 2 AA8 2 ILE C 214 ALA C 215 -1 O ILE C 214 N LEU C 171
LINK OD1 ASP C 158 NA NA C 403 1555 1555 2.61
LINK OG SER C 161 NA NA C 403 1555 1555 2.92
LINK O GLU C 167 NA NA C 403 1555 1555 3.16
CISPEP 1 SER D 76 PRO D 77 0 -0.46
CISPEP 2 SER A 76 PRO A 77 0 -1.43
CISPEP 3 SER B 76 PRO B 77 0 -0.02
CISPEP 4 SER C 76 PRO C 77 0 -2.75
CRYST1 47.263 59.011 113.990 84.85 78.55 84.01 P 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 0.021158 -0.002221 -0.004138 0.00000
SCALE2 0.000000 0.017039 -0.001211 0.00000
SCALE3 0.000000 0.000000 0.008973 0.00000
TER 2291 VAL D 300
TER 4538 GLY A 302
TER 6780 VAL B 300
TER 9009 GLY C 302
MASTER 398 0 15 40 40 0 0 6 9619 4 67 100
END |