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HEADER HYDROLASE 03-OCT-20 7D78
TITLE THE STRUCTURE OF THIOESTERASE DCSB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DLTD DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: D, A;
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, POLYKETIDES, LACTONES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TANG,J.H.ZHOU,G.Q.WANG
REVDAT 1 27-JAN-21 7D78 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. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.363
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 42956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.026
REMARK 3 FREE R VALUE TEST SET COUNT : 2159
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 4.8442 - 4.8442 0.98 2799 168 0.1358 0.1677
REMARK 3 2 4.8442 - 3.8461 1.00 2781 141 0.1234 0.1350
REMARK 3 3 3.8461 - 3.3603 1.00 2754 146 0.1388 0.1716
REMARK 3 4 3.3603 - 3.0532 1.00 2738 150 0.1533 0.1985
REMARK 3 5 3.0532 - 2.8344 1.00 2744 157 0.1616 0.1945
REMARK 3 6 2.8344 - 2.6673 1.00 2717 126 0.1573 0.1825
REMARK 3 7 2.6673 - 2.5338 1.00 2748 120 0.1592 0.2302
REMARK 3 8 2.5338 - 2.4235 1.00 2724 147 0.1567 0.1899
REMARK 3 9 2.4235 - 2.3302 1.00 2695 161 0.1531 0.2224
REMARK 3 10 2.3302 - 2.2498 1.00 2708 124 0.1501 0.1982
REMARK 3 11 2.2498 - 2.1795 0.99 2707 163 0.1482 0.2135
REMARK 3 12 2.1795 - 2.1172 1.00 2741 126 0.1493 0.1880
REMARK 3 13 2.1172 - 2.0614 0.99 2662 154 0.1475 0.2162
REMARK 3 14 2.0614 - 2.0111 0.99 2708 138 0.1566 0.1863
REMARK 3 15 2.0111 - 1.9700 0.96 2571 138 0.1657 0.2421
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) : 0.172
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.08
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 4702
REMARK 3 ANGLE : 0.812 6360
REMARK 3 CHIRALITY : 0.056 701
REMARK 3 PLANARITY : 0.006 832
REMARK 3 DIHEDRAL : 4.805 3972
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 7D78 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_1300018870.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-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 : BL18U1
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 PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43010
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
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 (%): 43.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MIB, 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: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 89.35350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.78450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.35350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.78450
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL D 404 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 552 LIES ON A SPECIAL POSITION.
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 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 ALA A 301
REMARK 465 GLY A 302
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 O HOH D 563 O HOH D 598 2.06
REMARK 500 O HOH D 529 O HOH D 598 2.06
REMARK 500 O HOH D 715 O HOH D 735 2.07
REMARK 500 O HOH A 542 O HOH A 735 2.10
REMARK 500 OE1 GLU D 11 O HOH D 501 2.15
REMARK 500 O HOH D 504 O HOH A 593 2.17
REMARK 500 O HOH D 501 O HOH D 726 2.19
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 LEU D 47 -44.53 69.48
REMARK 500 SER D 114 -133.58 62.60
REMARK 500 CYS D 137 55.02 39.02
REMARK 500 PHE D 142 -37.93 -140.63
REMARK 500 VAL D 202 33.22 -80.57
REMARK 500 LEU D 246 41.33 -106.28
REMARK 500 VAL D 300 75.22 -113.32
REMARK 500 LEU A 47 -48.07 67.09
REMARK 500 SER A 114 -136.84 59.52
REMARK 500 CYS A 137 56.58 36.42
REMARK 500 PHE A 142 -44.34 -142.31
REMARK 500 ASN A 209 8.13 -67.57
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 D 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 146 O
REMARK 620 2 HOH D 624 O 68.8
REMARK 620 3 HOH D 728 O 122.2 98.3
REMARK 620 N 1 2
DBREF 7D78 D 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
DBREF 7D78 A 1 302 UNP J4WAT9 J4WAT9_BEAB2 17 318
SEQADV 7D78 MET D -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D78 GLY D -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER D -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER D -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER D -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER D -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 GLY D -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 LEU D -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 VAL D -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 PRO D -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 ARG D -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 GLY D -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER D -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS D 0 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 MET A -19 UNP J4WAT9 INITIATING METHIONINE
SEQADV 7D78 GLY A -18 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER A -17 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER A -16 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -15 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -14 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -13 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -12 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -11 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A -10 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER A -9 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER A -8 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 GLY A -7 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 LEU A -6 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 VAL A -5 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 PRO A -4 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 ARG A -3 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 GLY A -2 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 SER A -1 UNP J4WAT9 EXPRESSION TAG
SEQADV 7D78 HIS A 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
HET NA D 401 1
HET GOL D 402 6
HET CL D 403 1
HET CL D 404 1
HET GOL A 401 6
HET GOL A 402 6
HET EDO A 403 4
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NA NA 1+
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 CL 2(CL 1-)
FORMUL 9 EDO C2 H6 O2
FORMUL 10 HOH *524(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 ALA D 201 1 13
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 LEU A 100 1 19
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 VAL A 202 GLY A 206 5 5
HELIX 18 AB9 GLN A 217 TRP A 225 1 9
HELIX 19 AC1 GLN A 226 LYS A 232 1 7
HELIX 20 AC2 PRO A 251 PHE A 262 1 12
HELIX 21 AC3 GLY A 284 VAL A 300 1 17
SHEET 1 AA1 8 GLN D 8 LYS D 13 0
SHEET 2 AA1 8 ILE D 19 TYR D 25 -1 O PHE D 24 N GLN D 8
SHEET 3 AA1 8 ASN D 61 ASP D 66 -1 O THR D 62 N TYR D 25
SHEET 4 AA1 8 GLY D 31 THR D 37 1 N MET D 36 O TYR D 63
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 LYS D 131 N ILE D 108
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 PHE A 24 N GLN A 8
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 MET A 36 O TYR A 63
SHEET 5 AA3 8 VAL A 103 MET A 113 1 O ASP A 104 N GLY A 31
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 MET A 135
SHEET 8 AA3 8 LYS A 266 ALA A 271 1 O LEU A 269 N MET A 241
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
LINK O GLU D 146 NA NA D 401 1555 1555 2.82
LINK NA NA D 401 O HOH D 624 1555 1555 3.14
LINK NA NA D 401 O HOH D 728 1555 1555 3.00
CISPEP 1 SER D 76 PRO D 77 0 -0.05
CISPEP 2 SER A 76 PRO A 77 0 0.02
CRYST1 178.707 47.569 71.695 90.00 93.19 90.00 C 1 2 1 8
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 0.005596 0.000000 0.000312 0.00000
SCALE2 0.000000 0.021022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013970 0.00000
TER 2306 GLY D 302
TER 4584 VAL A 300
MASTER 331 0 7 21 20 0 0 6 5100 2 26 50
END |