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HEADER HYDROLASE 27-JUL-17 5Y2Y
TITLE CRYSTAL STRUCTURE OF HALOTAG (M175C) COMPLEXED WITH DANSYL-PEG2-
TITLE 2 HALOTAG LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HALOTAG, HALOALKANE DEHALOGENASE, DANSYL LIGAND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LEE,M.KANG,H.RHEE,C.LEE
REVDAT 1 06-SEP-17 5Y2Y 0
JRNL AUTH M.G.KANG,H.LEE,B.H.KIM,Y.DUNBAYEV,J.K.SEO,C.LEE,H.W.RHEE
JRNL TITL STRUCTURE-GUIDED SYNTHESIS OF A PROTEIN-BASED FLUORESCENT
JRNL TITL 2 SENSOR FOR ALKYL HALIDES
JRNL REF CHEM. COMMUN. (CAMB.) V. 53 9226 2017
JRNL REFN ESSN 1364-548X
JRNL PMID 28766590
JRNL DOI 10.1039/C7CC03714G
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 26291
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1315
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 2.3653 - 2.2742 0.00 0 0 0.1400 0.2170
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 5Y2Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004581.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-15
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26399
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 56.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.07300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 38.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.10.1-2155
REMARK 200 STARTING MODEL: 4KAF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 0.1M CITRIC
REMARK 280 ACID PH5.5., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.19650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.47100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.17750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.47100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.19650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.17750
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 SER A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 GLY A 297
REMARK 465 SER B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 SER B 296
REMARK 465 GLY B 297
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 OE2 GLU A 224 O HOH A 401 1.99
REMARK 500 O HOH A 516 O HOH A 552 2.12
REMARK 500 O HOH A 501 O HOH A 545 2.13
REMARK 500 O HOH B 505 O HOH B 543 2.14
REMARK 500 O HOH B 481 O HOH B 535 2.14
REMARK 500 OD2 ASP A 156 O HOH A 402 2.16
REMARK 500 O HOH A 525 O HOH A 543 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 516 O HOH B 534 4555 2.13
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 PRO A 9 45.96 -88.89
REMARK 500 PRO A 42 46.57 -106.79
REMARK 500 THR A 43 -161.16 -100.97
REMARK 500 GLU A 98 -88.95 -107.79
REMARK 500 ASP A 106 -129.12 55.60
REMARK 500 ARG A 153 48.08 -87.69
REMARK 500 ASP A 156 -78.76 -104.71
REMARK 500 VAL A 245 -70.87 -133.18
REMARK 500 LEU A 271 -95.39 -117.31
REMARK 500 PRO B 9 47.83 -89.26
REMARK 500 PRO B 42 46.86 -106.57
REMARK 500 THR B 43 -161.29 -101.37
REMARK 500 GLU B 98 -86.92 -108.09
REMARK 500 ASP B 106 -125.70 55.67
REMARK 500 ARG B 153 49.14 -88.02
REMARK 500 ASP B 156 -70.97 -107.34
REMARK 500 VAL B 245 -68.68 -129.25
REMARK 500 LEU B 271 -95.80 -118.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8LL A 300
REMARK 610 8LL B 300
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8LL A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 8LL B 300 and ASP B
REMARK 800 106
DBREF 5Y2Y A 2 293 UNP P0A3G3 DHAA_RHOSO 2 293
DBREF 5Y2Y B 2 293 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 5Y2Y SER A -1 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y GLY A 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y SER A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y ALA A 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 5Y2Y VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 5Y2Y THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 5Y2Y GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 5Y2Y PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 5Y2Y MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 5Y2Y PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 5Y2Y THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 5Y2Y LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 5Y2Y VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 5Y2Y THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 5Y2Y CYS A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 5Y2Y GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 5Y2Y ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 5Y2Y GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 5Y2Y ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 5Y2Y LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 5Y2Y ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 5Y2Y ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 5Y2Y LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 5Y2Y SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 5Y2Y THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 5Y2Y GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y SER B -1 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y GLY B 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y SER B 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y ALA B 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 5Y2Y VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 5Y2Y THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 5Y2Y GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 5Y2Y PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 5Y2Y MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 5Y2Y PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 5Y2Y THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 5Y2Y LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 5Y2Y VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 5Y2Y THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 5Y2Y CYS B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 5Y2Y GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 5Y2Y ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 5Y2Y GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 5Y2Y ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 5Y2Y LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 5Y2Y ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 5Y2Y ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 5Y2Y LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 5Y2Y SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 5Y2Y THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 5Y2Y GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y SER B 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 5Y2Y GLY B 297 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 299 SER GLY SER ALA GLU ILE GLY THR GLY PHE PRO PHE ASP
SEQRES 2 A 299 PRO HIS TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR
SEQRES 3 A 299 VAL ASP VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE
SEQRES 4 A 299 LEU HIS GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN
SEQRES 5 A 299 ILE ILE PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA
SEQRES 6 A 299 PRO ASP LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP
SEQRES 7 A 299 LEU GLY TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP
SEQRES 8 A 299 ALA PHE ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU
SEQRES 9 A 299 VAL ILE HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP
SEQRES 10 A 299 ALA LYS ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE
SEQRES 11 A 299 MET GLU PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP
SEQRES 12 A 299 PRO GLU PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR
SEQRES 13 A 299 THR ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL
SEQRES 14 A 299 PHE ILE GLU GLY THR LEU PRO CYS GLY VAL VAL ARG PRO
SEQRES 15 A 299 LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE
SEQRES 16 A 299 LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO
SEQRES 17 A 299 ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL
SEQRES 18 A 299 ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER
SEQRES 19 A 299 PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL
SEQRES 20 A 299 LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER
SEQRES 21 A 299 LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU
SEQRES 22 A 299 ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER
SEQRES 23 A 299 GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY
SEQRES 1 B 299 SER GLY SER ALA GLU ILE GLY THR GLY PHE PRO PHE ASP
SEQRES 2 B 299 PRO HIS TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR
SEQRES 3 B 299 VAL ASP VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE
SEQRES 4 B 299 LEU HIS GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN
SEQRES 5 B 299 ILE ILE PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA
SEQRES 6 B 299 PRO ASP LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP
SEQRES 7 B 299 LEU GLY TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP
SEQRES 8 B 299 ALA PHE ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU
SEQRES 9 B 299 VAL ILE HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP
SEQRES 10 B 299 ALA LYS ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE
SEQRES 11 B 299 MET GLU PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP
SEQRES 12 B 299 PRO GLU PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR
SEQRES 13 B 299 THR ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL
SEQRES 14 B 299 PHE ILE GLU GLY THR LEU PRO CYS GLY VAL VAL ARG PRO
SEQRES 15 B 299 LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE
SEQRES 16 B 299 LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO
SEQRES 17 B 299 ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL
SEQRES 18 B 299 ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER
SEQRES 19 B 299 PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL
SEQRES 20 B 299 LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER
SEQRES 21 B 299 LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU
SEQRES 22 B 299 ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER
SEQRES 23 B 299 GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY
HET 8LL A 300 25
HET CL A 301 1
HET 8LL B 300 25
HET CL B 301 1
HETNAM 8LL 5-(DIMETHYLAMINO)-~{N}-[2-(2-HEXOXYETHOXY)
HETNAM 2 8LL ETHYL]NAPHTHALENE-1-SULFONAMIDE
HETNAM CL CHLORIDE ION
FORMUL 3 8LL 2(C22 H34 N2 O4 S)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *318(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 GLY A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 SER A 291 1 14
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 PHE B 80 LEU B 95 1 16
HELIX 21 AC3 TRP B 107 ASN B 119 1 13
HELIX 22 AC4 THR B 137 TRP B 141 5 5
HELIX 23 AC5 PRO B 142 ARG B 153 1 12
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 THR B 172 VAL B 177 5 6
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 ASN B 195 ASP B 198 5 4
HELIX 30 AD3 ARG B 199 LEU B 209 1 11
HELIX 31 AD4 PRO B 215 SER B 232 1 18
HELIX 32 AD5 PRO B 248 LEU B 259 1 12
HELIX 33 AD6 LEU B 273 ASN B 278 1 6
HELIX 34 AD7 ASN B 278 SER B 291 1 14
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O VAL A 265 N LEU A 238
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 ASP B 106 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 PHE B 131 1 O ALA B 127 N ILE B 104
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O PHE B 239 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O ILE B 267 N TRP B 240
LINK OD1 ASP A 106 C26 8LL A 300 1555 1555 1.39
LINK OD1 ASP B 106 C26 8LL B 300 1555 1555 1.40
CISPEP 1 ASN A 41 PRO A 42 0 0.71
CISPEP 2 GLU A 214 PRO A 215 0 -2.69
CISPEP 3 THR A 242 PRO A 243 0 3.32
CISPEP 4 ASN B 41 PRO B 42 0 -0.72
CISPEP 5 GLU B 214 PRO B 215 0 -4.53
CISPEP 6 THR B 242 PRO B 243 0 1.36
SITE 1 AC1 13 ASP A 106 PRO A 142 PHE A 144 ALA A 145
SITE 2 AC1 13 PHE A 149 THR A 172 CYS A 175 GLY A 176
SITE 3 AC1 13 GLY A 244 VAL A 245 ASN A 272 LEU A 273
SITE 4 AC1 13 PHE B 144
SITE 1 AC2 3 ASN A 41 TRP A 107 PRO A 206
SITE 1 AC3 4 ASN B 41 TRP B 107 PRO B 206 8LL B 300
SITE 1 AC4 22 VAL A 178 GLY B 40 ASN B 41 HIS B 105
SITE 2 AC4 22 TRP B 107 GLY B 108 SER B 109 ALA B 110
SITE 3 AC4 22 GLU B 130 ILE B 132 TRP B 141 PRO B 142
SITE 4 AC4 22 ALA B 145 PHE B 149 THR B 172 CYS B 175
SITE 5 AC4 22 GLY B 176 PRO B 243 GLY B 244 LEU B 271
SITE 6 AC4 22 ASN B 272 CL B 301
CRYST1 44.393 72.355 174.942 90.00 90.00 90.00 P 21 21 21 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 0.022526 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005716 0.00000
TER 2336 LEU A 293
TER 4680 ILE B 295
MASTER 322 0 4 34 16 0 12 6 5048 2 52 46
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